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Conserved domains on  [gi|1911174477|ref|XP_036204026|]
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ATP-dependent DNA/RNA helicase DHX36 isoform X1 [Myotis myotis]

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 ...
209-388 3.58e-126

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: 380.34  E-value: 3.58e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVAAERAETCGN 288
Cdd:cd17981      1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 GNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILMS 368
Cdd:cd17981     81 GNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160
                          170       180
                   ....*....|....*....|
gi 1911174477  369 ATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17981    161 ATLNAEKFSDYFNNCPMIHI 180
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
217-778 6.22e-120

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


The actual alignment was detected with superfamily member COG1643:

Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 387.13  E-value: 6.22e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  217 ELVNMIDNHQVTVISGETGCGKTTQVTQFILDnyieRGKGSACRIVCTQPRRISAISVAERVAAERAETCGNgnSTGYQI 296
Cdd:COG1643     18 ELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE--TVGYRV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  297 RLQSRLpRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLL-NYRPDLKVILMSATLNAEK 375
Cdd:COG1643     92 RFEDKV-SAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMSATLDAER 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  376 FSEYFGNCPMIHIPGFTFPVveyllediiEkIRYVPEQKEHRsqfkrgfmqghvnrqekeekeatykeRWPDyvrelrkr 455
Cdd:COG1643    171 FARLLGDAPVIESSGRTYPV---------E-VRYRPLPADER--------------------------DLED-------- 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  456 ysastvdviemmdddkvdlnLIAALIRyIVLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDRFLIIPLHSLMPTVNQ 535
Cdd:COG1643    207 --------------------AVADAVR-EALAEEPGDILVFLPGEREIRRTAEALRGRL---PPDTEILPLYGRLSAAEQ 262
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  536 TQVFKRTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYH 615
Cdd:COG1643    263 DRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYR 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  616 LYNSLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAHFlsRLMDPPS----NEAVSLsikhLMELNALDKQEELTPL 691
Cdd:COG1643    343 LWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPParaiADARAL----LQELGALDADGRLTPL 416
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  692 GVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPfviplgkekvadaRRkelaKDSKSDHLTVVNAFEGWEEA 771
Cdd:COG1643    417 GRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDP-------------RR----GAAGSDLLARLNLWRRLREQ 479

                   ....*..
gi 1911174477  772 RRRGFRY 778
Cdd:COG1643    480 QREFLSY 486
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
833-919 1.39e-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: 81.14  E-value: 1.39e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  833 IKAVICAGLYPKVAKiRLNLGKKRKMVKvytkTDGLVSIHPKSVNVEQTEFHYNWLIYHLKMRTSSIYLYDCTEVSPYCL 912
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYTTLS----DNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWL 75

                   ....*..
gi 1911174477  913 LFFGGDI 919
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 ...
209-388 3.58e-126

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: 380.34  E-value: 3.58e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVAAERAETCGN 288
Cdd:cd17981      1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 GNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILMS 368
Cdd:cd17981     81 GNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160
                          170       180
                   ....*....|....*....|
gi 1911174477  369 ATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17981    161 ATLNAEKFSDYFNNCPMIHI 180
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
217-778 6.22e-120

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 387.13  E-value: 6.22e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  217 ELVNMIDNHQVTVISGETGCGKTTQVTQFILDnyieRGKGSACRIVCTQPRRISAISVAERVAAERAETCGNgnSTGYQI 296
Cdd:COG1643     18 ELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE--TVGYRV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  297 RLQSRLpRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLL-NYRPDLKVILMSATLNAEK 375
Cdd:COG1643     92 RFEDKV-SAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMSATLDAER 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  376 FSEYFGNCPMIHIPGFTFPVveyllediiEkIRYVPEQKEHRsqfkrgfmqghvnrqekeekeatykeRWPDyvrelrkr 455
Cdd:COG1643    171 FARLLGDAPVIESSGRTYPV---------E-VRYRPLPADER--------------------------DLED-------- 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  456 ysastvdviemmdddkvdlnLIAALIRyIVLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDRFLIIPLHSLMPTVNQ 535
Cdd:COG1643    207 --------------------AVADAVR-EALAEEPGDILVFLPGEREIRRTAEALRGRL---PPDTEILPLYGRLSAAEQ 262
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  536 TQVFKRTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYH 615
Cdd:COG1643    263 DRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYR 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  616 LYNSLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAHFlsRLMDPPS----NEAVSLsikhLMELNALDKQEELTPL 691
Cdd:COG1643    343 LWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPParaiADARAL----LQELGALDADGRLTPL 416
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  692 GVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPfviplgkekvadaRRkelaKDSKSDHLTVVNAFEGWEEA 771
Cdd:COG1643    417 GRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDP-------------RR----GAAGSDLLARLNLWRRLREQ 479

                   ....*..
gi 1911174477  772 RRRGFRY 778
Cdd:COG1643    480 QREFLSY 486
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
207-773 5.70e-92

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


Pssm-ID: 273900 [Multi-domain]  Cd Length: 1283  Bit Score: 319.79  E-value: 5.70e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  207 EKLPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILdnyiERGKGSACRIVCTQPRRISAISVAERVAAERAEtc 286
Cdd:TIGR01967   64 DNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICL----ELGRGSHGLIGHTQPRRLAARTVAQRIAEELGT-- 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  287 GNGNSTGYQIRLQSRLpRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVIL 366
Cdd:TIGR01967  138 PLGEKVGYKVRFHDQV-SSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIII 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  367 MSATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYVPEQkehrsqfkrgfmqghvnrQEKEEkeatykerwp 446
Cdd:TIGR01967  217 TSATIDPERFSRHFNNAPIIEVSGRTYPV----------EVRYRPLV------------------EEQED---------- 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  447 dyvrelrkrysastvdviemmDDDKVDLNLIAALIRyiVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKSDrflIIPL 526
Cdd:TIGR01967  259 ---------------------DDLDQLEAILDAVDE--LFAEGPGDILIFLPGEREIRDAAEILRKRNLRHTE---ILPL 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  527 HSLMPTVNQTQVFKrtPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAG 606
Cdd:TIGR01967  313 YARLSNKEQQRVFQ--PHSGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCG 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  607 RVQPGHCYHLYNSLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAHFlsRLMDPPSNEAVSLSIKHLMELNALDKQE 686
Cdd:TIGR01967  391 RVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLALRLGDIAAF--PFIEAPDPRAIRDGFRLLEELGALDDDE 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  687 ---ELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKEKVADARRKELaKDSKSDHLTVVN 763
Cdd:TIGR01967  469 aepQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARF-KDPRSDFLSRVN 547
                          570
                   ....*....|
gi 1911174477  764 AFEGWEEARR 773
Cdd:TIGR01967  548 LWRHIEEQRQ 557
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
204-763 1.27e-85

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 301.59  E-value: 1.27e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  204 HFREKLPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILdnyiERGKGSACRIVCTQPRRISAISVAERVAAERA 283
Cdd:PRK11131    68 TYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICL----ELGRGVKGLIGHTQPRRLAARTVANRIAEELE 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  284 etCGNGNSTGYQIRLQSRLpRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLK 363
Cdd:PRK11131   144 --TELGGCVGYKVRFNDQV-SDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLK 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  364 VILMSATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYVPeqkehrsqfkrgfMQGHVNRQEKEEKEATYke 443
Cdd:PRK11131   221 VIITSATIDPERFSRHFNNAPIIEVSGRTYPV----------EVRYRP-------------IVEEADDTERDQLQAIF-- 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  444 rwpDYVRELRkrysastvdviemmdddkvdlnliaaliryivlEEEDGAILVFLPGWDNISTLHDLLMSQVMFKSDrflI 523
Cdd:PRK11131   276 ---DAVDELG---------------------------------REGPGDILIFMSGEREIRDTADALNKLNLRHTE---I 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  524 IPLHSLMPTVNQTQVFKrtPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKG 603
Cdd:PRK11131   317 LPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKG 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  604 RAGRVQPGHCYHLY-----NSlRASLLDdyqlPEILRTPLEELCLQIKILRLGGIAHFlsRLMDPPSNEAVSLSIKHLME 678
Cdd:PRK11131   395 RCGRVSEGICIRLYseddfLS-RPEFTD----PEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEE 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  679 LNALDKQE-----ELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKEKVADARRKELAkD 753
Cdd:PRK11131   468 LGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFA-D 546
                          570
                   ....*....|
gi 1911174477  754 SKSDHLTVVN 763
Cdd:PRK11131   547 KESDFLAFVN 556
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
463-617 1.17e-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: 248.60  E-value: 1.17e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  463 VIEMMDDDKVDLNLIAALIRYIVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKS-DRFLIIPLHSLMPTVNQTQVFKR 541
Cdd:cd18791     16 GISSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDlGKLLVLPLHSSLPPEEQQRVFEP 95
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1911174477  542 TPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYHLY 617
Cdd:cd18791     96 PPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
672-761 4.47e-28

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: 108.86  E-value: 4.47e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  672 SIKHLMELNALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLG------------- 738
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80
                           90       100
                   ....*....|....*....|....
gi 1911174477  739 -KEKVADARRKELAKDSKSDHLTV 761
Cdd:pfam04408   81 rRAADEKARAKFARLDLEGDHLTL 104
DEXDc smart00487
DEAD-like helicases superfamily;
212-394 4.45e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.81  E-value: 4.45e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477   212 FGMQKELVN-MIDNHQVTVISGETGCGKTTQVTQFILDNYIergKGSACRIVCTQPRRISAISVAERVAAERAETCGN-- 288
Cdd:smart00487   10 RPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALK---RGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKvv 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477   289 GNSTGYQIRLQ-SRLPRKQGSILYCTTGIILQWLQSDP-HLSSVSHIVLDEIHER--NLQSDVLMTVIKDLlnyRPDLKV 364
Cdd:smart00487   87 GLYGGDSKREQlRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKLLKLL---PKNVQL 163
                           170       180       190
                    ....*....|....*....|....*....|..
gi 1911174477   365 ILMSATL--NAEKFSEYFGNCPMIHIPGFTFP 394
Cdd:smart00487  164 LLLSATPpeEIENLLELFLNDPVFIDVGFTPL 195
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
678-762 1.04e-24

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: 98.49  E-value: 1.04e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477   678 ELNALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFviPLGKEKVADARRKELAkDSKSD 757
Cdd:smart00847    1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFA-DPESD 77

                    ....*
gi 1911174477   758 HLTVV 762
Cdd:smart00847   78 HLTLL 82
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
833-919 1.39e-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: 81.14  E-value: 1.39e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  833 IKAVICAGLYPKVAKiRLNLGKKRKMVKvytkTDGLVSIHPKSVNVEQTEFHYNWLIYHLKMRTSSIYLYDCTEVSPYCL 912
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYTTLS----DNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWL 75

                   ....*..
gi 1911174477  913 LFFGGDI 919
Cdd:pfam07717   76 LLFAPHI 82
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
215-374 7.78e-12

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 64.57  E-value: 7.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  215 QKELVNMIDNHQVTVISGETGCGKTTqVTQF-ILDNYIERGKGSacRIVCTQPRRISAISVAERvAAERAETCG------ 287
Cdd:pfam00270    4 QAEAIPAILEGRDVLVQAPTGSGKTL-AFLLpALEALDKLDNGP--QALVLAPTRELAEQIYEE-LKKLGKGLGlkvasl 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  288 -NGNSTGYQIRLQSRLPrkqgsILYCTTGIILQWLQSDPHLSSVSHIVLDEIHE--RNLQSDVLMTVIKDLlnyRPDLKV 364
Cdd:pfam00270   80 lGGDSRKEQLEKLKGPD-----ILVGTPGRLLDLLQERKLLKNLKLLVLDEAHRllDMGFGPDLEEILRRL---PKKRQI 151
                          170
                   ....*....|
gi 1911174477  365 ILMSATLNAE 374
Cdd:pfam00270  152 LLLSATLPRN 161
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
59-366 5.75e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 40.56  E-value: 5.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477   59 HLKGRDIGLWYAKKQGQKSKEAERQERAVVHMDEHREEQIVQLLHSVQAKSDKDSEAQISWFAPEDHGYGSEAPAENKPN 138
Cdd:COG5635     26 AIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLLLLLAEALL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  139 SEKKLEDREKKLINQEKKTFRMRDKYIDRDSEYLLQENEPDVNLDQQLLEDLQkkkTDLRYIEMQHFREKLPSFGmqkel 218
Cdd:COG5635    106 ALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLY---VPLNLLERIESLKRLELLE----- 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  219 vnmiDNHQVTVISGETGCGKTTqVTQFILDNYIERGKGSACRIvctqPRRISAISVAERVAAERAetcgngnstgyqirL 298
Cdd:COG5635    178 ----AKKKRLLILGEPGSGKTT-LLRYLALELAERYLDAEDPI----PILIELRDLAEEASLEDL--------------L 234
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911174477  299 QSRLPRKQGSilycTTGIILQWLQSDphlssvsHIV-----LDEIHERNLQSDVLmTVIKDLLNYRPDLKVIL 366
Cdd:COG5635    235 AEALEKRGGE----PEDALERLLRNG-------RLLllldgLDEVPDEADRDEVL-NQLRRFLERYPKARVII 295
 
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 ...
209-388 3.58e-126

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: 380.34  E-value: 3.58e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVAAERAETCGN 288
Cdd:cd17981      1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 GNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILMS 368
Cdd:cd17981     81 GNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160
                          170       180
                   ....*....|....*....|
gi 1911174477  369 ATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17981    161 ATLNAEKFSDYFNNCPMIHI 180
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
217-778 6.22e-120

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 387.13  E-value: 6.22e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  217 ELVNMIDNHQVTVISGETGCGKTTQVTQFILDnyieRGKGSACRIVCTQPRRISAISVAERVAAERAETCGNgnSTGYQI 296
Cdd:COG1643     18 ELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE--TVGYRV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  297 RLQSRLpRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLL-NYRPDLKVILMSATLNAEK 375
Cdd:COG1643     92 RFEDKV-SAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMSATLDAER 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  376 FSEYFGNCPMIHIPGFTFPVveyllediiEkIRYVPEQKEHRsqfkrgfmqghvnrqekeekeatykeRWPDyvrelrkr 455
Cdd:COG1643    171 FARLLGDAPVIESSGRTYPV---------E-VRYRPLPADER--------------------------DLED-------- 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  456 ysastvdviemmdddkvdlnLIAALIRyIVLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDRFLIIPLHSLMPTVNQ 535
Cdd:COG1643    207 --------------------AVADAVR-EALAEEPGDILVFLPGEREIRRTAEALRGRL---PPDTEILPLYGRLSAAEQ 262
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  536 TQVFKRTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYH 615
Cdd:COG1643    263 DRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYR 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  616 LYNSLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAHFlsRLMDPPS----NEAVSLsikhLMELNALDKQEELTPL 691
Cdd:COG1643    343 LWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPParaiADARAL----LQELGALDADGRLTPL 416
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  692 GVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPfviplgkekvadaRRkelaKDSKSDHLTVVNAFEGWEEA 771
Cdd:COG1643    417 GRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDP-------------RR----GAAGSDLLARLNLWRRLREQ 479

                   ....*..
gi 1911174477  772 RRRGFRY 778
Cdd:COG1643    480 QREFLSY 486
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
207-773 5.70e-92

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


Pssm-ID: 273900 [Multi-domain]  Cd Length: 1283  Bit Score: 319.79  E-value: 5.70e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  207 EKLPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILdnyiERGKGSACRIVCTQPRRISAISVAERVAAERAEtc 286
Cdd:TIGR01967   64 DNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICL----ELGRGSHGLIGHTQPRRLAARTVAQRIAEELGT-- 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  287 GNGNSTGYQIRLQSRLpRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVIL 366
Cdd:TIGR01967  138 PLGEKVGYKVRFHDQV-SSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIII 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  367 MSATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYVPEQkehrsqfkrgfmqghvnrQEKEEkeatykerwp 446
Cdd:TIGR01967  217 TSATIDPERFSRHFNNAPIIEVSGRTYPV----------EVRYRPLV------------------EEQED---------- 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  447 dyvrelrkrysastvdviemmDDDKVDLNLIAALIRyiVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKSDrflIIPL 526
Cdd:TIGR01967  259 ---------------------DDLDQLEAILDAVDE--LFAEGPGDILIFLPGEREIRDAAEILRKRNLRHTE---ILPL 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  527 HSLMPTVNQTQVFKrtPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAG 606
Cdd:TIGR01967  313 YARLSNKEQQRVFQ--PHSGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCG 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  607 RVQPGHCYHLYNSLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAHFlsRLMDPPSNEAVSLSIKHLMELNALDKQE 686
Cdd:TIGR01967  391 RVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLALRLGDIAAF--PFIEAPDPRAIRDGFRLLEELGALDDDE 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  687 ---ELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKEKVADARRKELaKDSKSDHLTVVN 763
Cdd:TIGR01967  469 aepQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARF-KDPRSDFLSRVN 547
                          570
                   ....*....|
gi 1911174477  764 AFEGWEEARR 773
Cdd:TIGR01967  548 LWRHIEEQRQ 557
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
225-388 4.23e-88

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: 278.96  E-value: 4.23e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  225 HQVTVISGETGCGKTTQVTQFILDNYIERGKGsaCRIVCTQPRRISAISVAERVAAERAETCGNgnSTGYQIRLQSRLPR 304
Cdd:cd17917      1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGK--GRIVCTQPRRIAAISVAERVAEERGEKLGE--EVGYQIRFESKTSS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  305 KqGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILMSATLNAEKFSEYFGNCP 384
Cdd:cd17917     77 K-TRIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAP 155

                   ....
gi 1911174477  385 MIHI 388
Cdd:cd17917    156 VIHI 159
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
204-763 1.27e-85

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 301.59  E-value: 1.27e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  204 HFREKLPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILdnyiERGKGSACRIVCTQPRRISAISVAERVAAERA 283
Cdd:PRK11131    68 TYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICL----ELGRGVKGLIGHTQPRRLAARTVANRIAEELE 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  284 etCGNGNSTGYQIRLQSRLpRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLK 363
Cdd:PRK11131   144 --TELGGCVGYKVRFNDQV-SDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLK 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  364 VILMSATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYVPeqkehrsqfkrgfMQGHVNRQEKEEKEATYke 443
Cdd:PRK11131   221 VIITSATIDPERFSRHFNNAPIIEVSGRTYPV----------EVRYRP-------------IVEEADDTERDQLQAIF-- 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  444 rwpDYVRELRkrysastvdviemmdddkvdlnliaaliryivlEEEDGAILVFLPGWDNISTLHDLLMSQVMFKSDrflI 523
Cdd:PRK11131   276 ---DAVDELG---------------------------------REGPGDILIFMSGEREIRDTADALNKLNLRHTE---I 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  524 IPLHSLMPTVNQTQVFKrtPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKG 603
Cdd:PRK11131   317 LPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKG 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  604 RAGRVQPGHCYHLY-----NSlRASLLDdyqlPEILRTPLEELCLQIKILRLGGIAHFlsRLMDPPSNEAVSLSIKHLME 678
Cdd:PRK11131   395 RCGRVSEGICIRLYseddfLS-RPEFTD----PEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEE 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  679 LNALDKQE-----ELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKEKVADARRKELAkD 753
Cdd:PRK11131   468 LGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFA-D 546
                          570
                   ....*....|
gi 1911174477  754 SKSDHLTVVN 763
Cdd:PRK11131   547 KESDFLAFVN 556
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
463-617 1.17e-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: 248.60  E-value: 1.17e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  463 VIEMMDDDKVDLNLIAALIRYIVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKS-DRFLIIPLHSLMPTVNQTQVFKR 541
Cdd:cd18791     16 GISSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDlGKLLVLPLHSSLPPEEQQRVFEP 95
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1911174477  542 TPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYHLY 617
Cdd:cd18791     96 PPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
209-757 2.00e-74

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: 262.39  E-value: 2.00e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKgsacrIVCTQPRRISAISVAERVAAERAETCGN 288
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGGK-----IIMLEPRRLAARSAAQRLASQLGEAVGQ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLN-YRPDLKVILM 367
Cdd:TIGR01970   76 --TVGYRVRGENKVSRRT-RLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSsLREDLKILAM 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  368 SATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYVPEQKEhrsqfkrgfmqghvnrqekeekeatykERWPD 447
Cdd:TIGR01970  153 SATLDGERLSSLLPDAPVVESEGRSFPV----------EIRYLPLRGD---------------------------QRLED 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  448 YVRelrkrysastvDVIEMMdddkvdlnliaaliryivLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDRFLIIPLH 527
Cdd:TIGR01970  196 AVS-----------RAVEHA------------------LASETGSILVFLPGQAEIRRVQEQLAERL---DSDVLICPLY 243
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  528 SLMPTVNQTQVFKRTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGR 607
Cdd:TIGR01970  244 GELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGR 323
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  608 VQPGHCYHLYNSLRASLLDDYQLPEILRTPLEELCLQikILRLGGIAHFLSRLMDPPSNEAVSLSIKHLMELNALDKQEE 687
Cdd:TIGR01970  324 LEPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALE--LAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALDAQGR 401
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  688 LTPLGVHLARLPVEPHIGKMILFG------ALFCCLDPVLT-----------IAASLSFKDPFVIPLGKEkvADARRKEL 750
Cdd:TIGR01970  402 LTAHGKAMAALGCHPRLAAMLLSAhstglaALACDLAALLEerglprqggadLMNRLHRLQQGRQGRGQR--AQQLAKKL 479

                   ....*..
gi 1911174477  751 AKDSKSD 757
Cdd:TIGR01970  480 RRRLRFS 486
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
209-388 2.39e-73

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: 239.74  E-value: 2.39e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVAAERAETCGN 288
Cdd:cd17985      1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 gnSTGYQIRLQSRlpRKQGS-ILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILM 367
Cdd:cd17985     81 --SVGYQIRLESV--KSSATrLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILM 156
                          170       180
                   ....*....|....*....|.
gi 1911174477  368 SATLNAEKFSEYFGNCPMIHI 388
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 ...
182-388 1.63e-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: 234.34  E-value: 1.63e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  182 LDQQLLEDLQ-KKKTDLRYIEMQHFREKLPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACR 260
Cdd:cd17972     31 ISMDLKNELMyQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECN 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  261 IVCTQPRRISAISVAERVAAERAETCgnGNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDphLSSVSHIVLDEIHE 340
Cdd:cd17972    111 IVVTQPRRISAVSVAERVAFERGEEV--GKSCGYSVRFESVLPRPHASILFCTVGVLLRKLEAG--IRGISHVIVDEIHE 186
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1911174477  341 RNLQSDVLMTVIKDLLNYRPDLKVILMSATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17972    187 RDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
209-388 8.07e-69

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: 227.37  E-value: 8.07e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVAAERAETCGN 288
Cdd:cd17976      1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 gnSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILMS 368
Cdd:cd17976     81 --NVGYQVRLESRPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMS 158
                          170       180
                   ....*....|....*....|
gi 1911174477  369 ATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17976    159 ATGDNQRLSRYFGGCPVVRV 178
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
209-388 9.52e-61

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


Pssm-ID: 350745 [Multi-domain]  Cd Length: 176  Bit Score: 204.68  E-value: 9.52e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIErgKGSACRIVCTQPRRISAISVAERVAAERAETCGN 288
Cdd:cd17987      1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYA--NGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQS-DPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILM 367
Cdd:cd17987     79 --TVGYQIRLESRVSPKT-LLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILS 155
                          170       180
                   ....*....|....*....|.
gi 1911174477  368 SATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17987    156 SAALDVNLFIRYFGSCPVIYI 176
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
209-712 1.68e-60

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 222.11  E-value: 1.68e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILdnyieRGKGSACRIVCTQPRRISAISVAERVAAERAETCGN 288
Cdd:PRK11664     4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLL-----QHGGINGKIIMLEPRRLAARNVAQRLAEQLGEKPGE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 gnSTGYQIRLQSRL-PRKQGSILycTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDV----LMTVIKDLlnyRPDLK 363
Cdd:PRK11664    79 --TVGYRMRAESKVgPNTRLEVV--TEGILTRMIQRDPELSGVGLVILDEFHERSLQADLalalLLDVQQGL---RDDLK 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  364 VILMSATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYVPeqkehrsqfkrgfmqghVNRQEKEEkEATYKE 443
Cdd:PRK11664   152 LLIMSATLDNDRLQQLLPDAPVIVSEGRSFPV----------ERRYQP-----------------LPAHQRFD-EAVARA 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  444 rwpdyVRELrkrysastvdviemmdddkvdlnliaaliryivLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDRFLI 523
Cdd:PRK11664   204 -----TAEL---------------------------------LRQESGSLLLFLPGVGEIQRVQEQLASRV---ASDVLL 242
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  524 IPLHSLMPTVNQTQVFKRTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKG 603
Cdd:PRK11664   243 CPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAG 322
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  604 RAGRVQPGHCYHLYNSLRASLLDDYQLPEILRTPLEELCLQikILRLGgiAHFLSRLM--DPPSNEAVSLSIKHLMELNA 681
Cdd:PRK11664   323 RAGRLEPGICLHLYSKEQAERAAAQSEPEILHSDLSGLLLE--LLQWG--CHDPAQLSwlDQPPAAALAAAKRLLQQLGA 398
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1911174477  682 LDKQEELTPLGVHLARLPVEPHIGKMILFGA 712
Cdd:PRK11664   399 LDGQGRLTARGRKMAALGNDPRLAAMLVAAK 429
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
209-388 2.72e-60

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: 203.99  E-value: 2.72e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYI-ERGKGSACRIVCTQPRRISAISVAERVAAERAETCG 287
Cdd:cd17975      1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLlNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  288 NG--NS-TGYQIRLQSRlPRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKV 364
Cdd:cd17975     81 PGgkNSlCGYQIRMESR-TGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHL 159
                          170       180
                   ....*....|....*....|....
gi 1911174477  365 ILMSATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17975    160 ILMSATVDCEKFSSYFTHCPILRI 183
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
206-389 8.79e-53

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: 182.30  E-value: 8.79e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  206 REKLPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFIldnyIERGKGSACRIVCTQPRRISAISVAERVAAERAet 285
Cdd:cd17971      3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYL----AEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFG-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  286 CGNGNSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVI 365
Cdd:cd17971     77 CCLGQEVGYTIRFEDCTSPET-VIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLI 155
                          170       180
                   ....*....|....*....|....
gi 1911174477  366 LMSATLNAEKFSEYFGNCPMIHIP 389
Cdd:cd17971    156 VTSATLDAVKFSQYFYEAPIFTIP 179
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
198-388 6.49e-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: 180.30  E-value: 6.49e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  198 RYIEMQHFREKLPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNyiERGKGSACRIVCTQPRRISAISVAER 277
Cdd:cd17973      2 RYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDD--ELPHQPKKLVACTQPRRVAAMSVAQR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  278 VAAERAETCGNgnSTGYQIRLQSRLPRKqgSIL-YCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLL 356
Cdd:cd17973     80 VAEEMDVKLGE--EVGYSIRFEDCSSAK--TILkYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVV 155
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1911174477  357 NYRPDLKVILMSATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17973    156 RRRPDLKLIVMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
209-395 2.26e-51

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: 178.46  E-value: 2.26e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKgsACRIVCTQPRRISAISVAERVAAERAetCGN 288
Cdd:cd17988      1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGK--YCNIVVTQPRRIAAISIARRVSQERE--WTL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 GNSTGYQIRLQsRLPRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLL--NYRpDLKVIL 366
Cdd:cd17988     77 GSLVGYQVGLE-RPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLrtNSR-HVKIIL 154
                          170       180
                   ....*....|....*....|....*....
gi 1911174477  367 MSATLNAEKFSEYFGncpMIHIPGFTFPV 395
Cdd:cd17988    155 MSATISCKEFADYFT---TPNNPAYVFEV 180
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
209-388 8.00e-51

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


Pssm-ID: 350737 [Multi-domain]  Cd Length: 170  Bit Score: 176.48  E-value: 8.00e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIERgkgsacrIVCTQPRRISAISVAERVAAERAETcgN 288
Cdd:cd17979      1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH-------IACTQPRRIACISLAKRVAFESLNQ--Y 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 GNSTGYQIRLQ-SRLPRKQgsILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILM 367
Cdd:cd17979     72 GSKVAYQIRFErTRTLATK--LLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILM 149
                          170       180
                   ....*....|....*....|.
gi 1911174477  368 SATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17979    150 SATINIELFSGYFEGAPVVQV 170
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
209-388 1.98e-48

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: 169.99  E-value: 1.98e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKGsacRIVCTQPRRISAISVAERVAAERAetCGN 288
Cdd:cd17974      1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGG---KIGCTQPRRVAAMSVAARVAEEMG--VKL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 GNSTGYQIRLQSRLPRKqgSIL-YCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILM 367
Cdd:cd17974     76 GNEVGYSIRFEDCTSEK--TVLkYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLIS 153
                          170       180
                   ....*....|....*....|.
gi 1911174477  368 SATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17974    154 SATMDAEKFSAFFDDAPIFRI 174
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
209-388 3.15e-48

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: 169.18  E-value: 3.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFIL-DNYIERGKgsacrIVCTQPRRISAISVAERVAAERAETCG 287
Cdd:cd17983      1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHeDGYTDYGM-----IGCTQPRRVAAMSVAKRVSEEMGVELG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  288 NgnSTGYQIRLQSrLPRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILM 367
Cdd:cd17983     76 E--EVGYAIRFED-CTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVT 152
                          170       180
                   ....*....|....*....|.
gi 1911174477  368 SATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17983    153 SATMDADKFADFFGNVPIFTI 173
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
209-388 3.71e-47

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


Pssm-ID: 438710 [Multi-domain]  Cd Length: 178  Bit Score: 166.38  E-value: 3.71e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKgsacRIVCTQPRRISAISVAERVAAERAetCGN 288
Cdd:cd17978      1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGG----MIGITQPRRVAAVSVAKRVAEEMG--VEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 GNSTGYQIRLQSRLPRkQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYR-----PDLK 363
Cdd:cd17978     75 GQLVGYSVRFDDVTSE-ETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLK 153
                          170       180
                   ....*....|....*....|....*
gi 1911174477  364 VILMSATLNAEKFSEYFGNCPMIHI 388
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 ...
209-380 1.17e-45

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: 162.25  E-value: 1.17e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILdnyiERGKGSACR-IVCTQPRRISAISVAERVAAERAETCG 287
Cdd:cd17980      1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLA----EAGWTAGGRvVGCTQPRRVAAVTVAGRVAEEMGAVLG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  288 NgnSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILM 367
Cdd:cd17980     77 H--EVGYCIRFDDCTDPQATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVA 154
                          170
                   ....*....|...
gi 1911174477  368 SATLNAEKFSEYF 380
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 ...
209-388 1.33e-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: 152.99  E-value: 1.33e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILdnyiERGKGSACRIVCTQPRRISAISVAERVAAERAETCGN 288
Cdd:cd17989      1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICL----ELGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILMS 368
Cdd:cd17989     77 --AVGYKVRFTDQTSDET-CVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITS 153
                          170       180
                   ....*....|....*....|
gi 1911174477  369 ATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17989    154 ATIDAERFSRHFNNAPIIEV 173
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
209-388 2.70e-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: 143.84  E-value: 2.70e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILdnyiERGKGSACRIVCTQPRRISAISVAERVAAERAetCGN 288
Cdd:cd17984      1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLY----EAGFSQHGMIGVTQPRRVAAISVAQRVAEEMK--CTL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 GNSTGYQIRLQSrLPRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLL-----NYRPDLK 363
Cdd:cd17984     75 GSKVGYQVRFDD-CSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFqekspNRKEHLK 153
                          170       180
                   ....*....|....*....|....*
gi 1911174477  364 VILMSATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17984    154 VVVMSATLELAKLSAFFGNCPVFDI 178
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
209-378 5.56e-38

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


Pssm-ID: 350740 [Multi-domain]  Cd Length: 191  Bit Score: 140.57  E-value: 5.56e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILD-NYIERGKGSACRIVCTQPRRISAISVAERVAaerAETCG 287
Cdd:cd17982      1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEaGFGSPESDNPGMIGITQPRRVAAVSMAKRVA---EELNV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  288 NGNSTGYQIRLQSRLpRKQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPD------ 361
Cdd:cd17982     78 FGKEVSYQIRYDSTV-SENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdq 156
                          170       180
                   ....*....|....*....|.
gi 1911174477  362 ----LKVILMSATLNAEKFSE 378
Cdd:cd17982    157 tvkpLKLVIMSATLRVEDFTE 177
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
209-386 3.39e-35

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: 132.07  E-value: 3.39e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQFILDNYIERGKgsacRIVCTQPRRISAISVAERVAAERAETCGN 288
Cdd:cd17990      1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGG----KIIVLEPRRVAARAAARRLATLLGEAPGE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLN-YRPDLKVILM 367
Cdd:cd17990     77 --TVGYRVRGESRVGRRT-RVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAM 153
                          170
                   ....*....|....*....
gi 1911174477  368 SATLNAEKFSEYFGNCPMI 386
Cdd:cd17990    154 SATLDGDGLAALLPEAPVV 172
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
672-761 4.47e-28

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: 108.86  E-value: 4.47e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  672 SIKHLMELNALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLG------------- 738
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80
                           90       100
                   ....*....|....*....|....
gi 1911174477  739 -KEKVADARRKELAKDSKSDHLTV 761
Cdd:pfam04408   81 rRAADEKARAKFARLDLEGDHLTL 104
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
209-388 1.40e-26

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: 107.22  E-value: 1.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  209 LPSFGMQKELVNMIDNHQVTVISGETGCGKTTQVTQ----FILDNYIERGKgsacrIVCTQPRRISAISVAERVAAERAE 284
Cdd:cd17977      1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLSAHYQHGV-----VVCTQVHKQTAVWLALRVADEMDV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  285 TCGNgnSTGYQIRLQSRLprKQGSIL-YCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLK 363
Cdd:cd17977     76 NIGH--EVGYVIPFENCC--TNETILrYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELK 151
                          170       180
                   ....*....|....*....|....*
gi 1911174477  364 VILMSATLNAEKFSEYFGNCPMIHI 388
Cdd:cd17977    152 LVIITCPHLSSKLLSYYGNVPLIEV 176
DEXDc smart00487
DEAD-like helicases superfamily;
212-394 4.45e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.81  E-value: 4.45e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477   212 FGMQKELVN-MIDNHQVTVISGETGCGKTTQVTQFILDNYIergKGSACRIVCTQPRRISAISVAERVAAERAETCGN-- 288
Cdd:smart00487   10 RPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALK---RGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKvv 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477   289 GNSTGYQIRLQ-SRLPRKQGSILYCTTGIILQWLQSDP-HLSSVSHIVLDEIHER--NLQSDVLMTVIKDLlnyRPDLKV 364
Cdd:smart00487   87 GLYGGDSKREQlRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKLLKLL---PKNVQL 163
                           170       180       190
                    ....*....|....*....|....*....|..
gi 1911174477   365 ILMSATL--NAEKFSEYFGNCPMIHIPGFTFP 394
Cdd:smart00487  164 LLLSATPpeEIENLLELFLNDPVFIDVGFTPL 195
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
678-762 1.04e-24

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: 98.49  E-value: 1.04e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477   678 ELNALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFviPLGKEKVADARRKELAkDSKSD 757
Cdd:smart00847    1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFA-DPESD 77

                    ....*
gi 1911174477   758 HLTVV 762
Cdd:smart00847   78 HLTLL 82
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
227-388 9.82e-23

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: 96.51  E-value: 9.82e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  227 VTVISGETGCGKTTQVTQFILDNYIERG--KGSacrIVCTQPRRISAISVAERVAAERAETCGNgnSTGYQIRlQSRLPR 304
Cdd:cd17986     20 IVLVSGEPGSGKSTQVPQWCAEFALSRGfqKGQ---VTVTQPHPLAARSLALRVADEMDLNLGH--EVGYSIP-QEDCTG 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  305 KQGSILYCTTGIILQWLQSDPHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNYRPDLKVILMSATLNAEKFSEYFGNCP 384
Cdd:cd17986     94 PNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPALEPKLRAFWGNPP 173

                   ....
gi 1911174477  385 MIHI 388
Cdd:cd17986    174 VVHV 177
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
833-919 1.39e-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: 81.14  E-value: 1.39e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  833 IKAVICAGLYPKVAKiRLNLGKKRKMVKvytkTDGLVSIHPKSVNVEQTEFHYNWLIYHLKMRTSSIYLYDCTEVSPYCL 912
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYTTLS----DNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWL 75

                   ....*..
gi 1911174477  913 LFFGGDI 919
Cdd:pfam07717   76 LLFAPHI 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
228-370 1.02e-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: 72.44  E-value: 1.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  228 TVISGETGCGKTTQVTQFILDNYIERGKgsacRIVCTQPRRISAISVAERVAAERAE--TCGnGNSTGYQIRLQSRLPRK 305
Cdd:cd00046      4 VLITAPTGSGKTLAALLAALLLLLKKGK----KVLVLVPTKALALQTAERLRELFGPgiRVA-VLVGGSSAEEREKNKLG 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1911174477  306 QGSILYCTTGIILQWLQSD--PHLSSVSHIVLDEIHERNLQSDVLMTVIKDLLNY-RPDLKVILMSAT 370
Cdd:cd00046     79 DADIIIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAgLKNAQVILLSAT 146
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
214-611 1.83e-14

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 77.71  E-value: 1.83e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  214 MQKELVNMIDNHQVTVISGETGCGKTTQVTQFIL----------------DNYIERgkgsacRIVCTQPRrisaisvaer 277
Cdd:PHA02653   168 VQLKIFEAWISRKPVVLTGGTGVGKTSQVPKLLLwfnylfggfdnldkidPNFIER------PIVLSLPR---------- 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  278 VAAERAETCGNGNSTGY-QI--------------RLQSRLPRKQGsILYCTTGIILQwlqsdpHLSSVSHIVLDEIHERN 342
Cdd:PHA02653   232 VALVRLHSITLLKSLGFdEIdgspislkygsipdELINTNPKPYG-LVFSTHKLTLN------KLFDYGTVIIDEVHEHD 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  343 LQSDVLMTVI-KDLLNYRpdlKVILMSATL--NAEKFSEYFGNCPMIHIPGFT-FPVVEylledIIEKIRYVPEQKehrs 418
Cdd:PHA02653   305 QIGDIIIAVArKHIDKIR---SLFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISE-----VYVKNKYNPKNK---- 372
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  419 qfkrgfmqghvnRQEKEEkeatykerwpdyvrELRkrysastvdviemmdddkvdlNLIAALIRYIVLEEEDGaiLVFLP 498
Cdd:PHA02653   373 ------------RAYIEE--------------EKK---------------------NIVTALKKYTPPKGSSG--IVFVA 403
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  499 gwdNISTLHDL--LMSQvmfKSDRFLIIPLHSLMPTVNQ--TQVFKRTPPgvrKIVIATNIAETSITIDDVVYVIDGGKI 574
Cdd:PHA02653   404 ---SVSQCEEYkkYLEK---RLPIYDFYIIHGKVPNIDEilEKVYSSKNP---SIIISTPYLESSVTIRNATHVYDTGRV 474
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1911174477  575 KETHFDTQNNIstmsaeWVSKANAKQRKGRAGRVQPG 611
Cdd:PHA02653   475 YVPEPFGGKEM------FISKSMRTQRKGRVGRVSPG 505
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
479-608 2.70e-14

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 69.93  E-value: 2.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  479 ALIRYIVLEEEDGAILVFLPGWDnistlhdLLMSQVMFKSDRFLIIPLHSLMPTVNQTQVFKRTPPGVRKIVIATNIAET 558
Cdd:pfam00271    4 EALLELLKKERGGKVLIFSQTKK-------TLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1911174477  559 SITIDDVVYVIdggkiketHFDTQNNISTMsaewvskanaKQRKGRAGRV 608
Cdd:pfam00271   77 GLDLPDVDLVI--------NYDLPWNPASY----------IQRIGRAGRA 108
HELICc smart00490
helicase superfamily c-terminal domain;
515-607 2.09e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 66.47  E-value: 2.09e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477   515 MFKSDRFLIIPLHSLMPTVNQTQVFKRTPPGVRKIVIATNIAETSITIDDVVYVIdggkiketHFDTqnnistmsaeWVS 594
Cdd:smart00490    6 LLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVI--------IYDL----------PWS 67
                            90
                    ....*....|...
gi 1911174477   595 KANAKQRKGRAGR 607
Cdd:smart00490   68 PASYIQRIGRAGR 80
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
215-374 7.78e-12

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 64.57  E-value: 7.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  215 QKELVNMIDNHQVTVISGETGCGKTTqVTQF-ILDNYIERGKGSacRIVCTQPRRISAISVAERvAAERAETCG------ 287
Cdd:pfam00270    4 QAEAIPAILEGRDVLVQAPTGSGKTL-AFLLpALEALDKLDNGP--QALVLAPTRELAEQIYEE-LKKLGKGLGlkvasl 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  288 -NGNSTGYQIRLQSRLPrkqgsILYCTTGIILQWLQSDPHLSSVSHIVLDEIHE--RNLQSDVLMTVIKDLlnyRPDLKV 364
Cdd:pfam00270   80 lGGDSRKEQLEKLKGPD-----ILVGTPGRLLDLLQERKLLKNLKLLVLDEAHRllDMGFGPDLEEILRRL---PKKRQI 151
                          170
                   ....*....|
gi 1911174477  365 ILMSATLNAE 374
Cdd:pfam00270  152 LLLSATLPRN 161
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
215-389 2.67e-09

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: 57.66  E-value: 2.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  215 QKELVNMIDNHQV-TVISGETGCGKTTQVTQFILDNYIERGKgsacRIVCTQPRRisaiSVAERVAAERAETCGN----- 288
Cdd:cd17921      6 QREALRALYLSGDsVLVSAPTSSGKTLIAELAILRALATSGG----KAVYIAPTR----ALVNQKEADLRERFGPlgknv 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  289 GNSTGYQIRLQSRLPRKQgsILYCTTGIILQWLQSDPH--LSSVSHIVLDEIHERNLQS--DVLMTVIKDLLNYRPDLKV 364
Cdd:cd17921     78 GLLTGDPSVNKLLLAEAD--ILVATPEKLDLLLRNGGErlIQDVRLVVVDEAHLIGDGErgVVLELLLSRLLRINKNARF 155
                          170       180
                   ....*....|....*....|....*.
gi 1911174477  365 ILMSATL-NAEKFSEYFGNCPMIHIP 389
Cdd:cd17921    156 VGLSATLpNAEDLAEWLGVEDLIRFD 181
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
215-255 8.58e-04

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


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 41.00  E-value: 8.58e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1911174477  215 QKELVNMIDNHQVTVISGETGCGKTTqVTQFILDNYIERGK 255
Cdd:cd17933      2 QKAAVRLVLRNRVSVLTGGAGTGKTT-TLKALLAALEAEGK 41
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
188-567 1.61e-03

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


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 42.38  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  188 EDLQKKKTDLRYIEMQHFREKLPSFG--------MQKELVNMI-----DNHQVTVISGETGCGKTTQVTQFILDNyieRG 254
Cdd:COG1203     97 ANFDMARQALDHLLAERLERLLPKKSkprtpinpLQNEALELAleaaeEEPGLFILTAPTGGGKTEAALLFALRL---AA 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  255 KGSACRIVCTQP------------RRISAISVAE---RVAAERAETCGNGNSTGYQIRLQSRL---PrkqgsILYCTtgi 316
Cdd:COG1203    174 KHGGRRIIYALPftsiinqtydrlRDLFGEDVLLhhsLADLDLLEEEEEYESEARWLKLLKELwdaP-----VVVTT--- 245
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  317 ILQWLQSdpHLSSVSH------------IVLDEIH--ERNLQSdVLMTVIKDLLNYrpDLKVILMSATLnaekfseyfgn 382
Cdd:COG1203    246 IDQLFES--LFSNRKGqerrlhnlansvIILDEVQayPPYMLA-LLLRLLEWLKNL--GGSVILMTATL----------- 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  383 cPMIHIPGFtFPVVEYLLEDIIEKIRYVPEQKEHRSQFKRGFMQghvnrqekeekeatykerWPDYVRELRKRYSAS-TV 461
Cdd:COG1203    310 -PPLLREEL-LEAYELIPDEPEELPEYFRAFVRKRVELKEGPLS------------------DEELAELILEALHKGkSV 369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  462 DVIemmdddkvdLNLIAALIR-YIVLEEEDGAILVFLpgwdnistLHdllmSQVMFKsDRFLIIplhslmptvnqTQVFK 540
Cdd:COG1203    370 LVI---------VNTVKDAQElYEALKEKLPDEEVYL--------LH----SRFCPA-DRSEIE-----------KEIKE 416
                          410       420
                   ....*....|....*....|....*...
gi 1911174477  541 RTPPGVRKIVIATNIAETSITID-DVVY 567
Cdd:COG1203    417 RLERGKPCILVSTQVVEAGVDIDfDVVI 444
AAA_22 pfam13401
AAA domain;
223-367 1.78e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.63  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  223 DNHQVTVISGETGCGKTTqVTQFILDNYIERGKGSAcRIVCTQPRriSAISVAERVAAEraetcgngnstgYQIRLQSRL 302
Cdd:pfam13401    3 FGAGILVLTGESGTGKTT-LLRRLLEQLPEVRDSVV-FVDLPSGT--SPKDLLRALLRA------------LGLPLSGRL 66
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1911174477  303 PRKQGsilyctTGIILQWLQsdpHLSSVSHIVLDEIHerNLQSDVLMTvIKDLLNYRP-DLKVILM 367
Cdd:pfam13401   67 SKEEL------LAALQQLLL---ALAVAVVLIIDEAQ--HLSLEALEE-LRDLLNLSSkLLQLILV 120
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
59-366 5.75e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 40.56  E-value: 5.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477   59 HLKGRDIGLWYAKKQGQKSKEAERQERAVVHMDEHREEQIVQLLHSVQAKSDKDSEAQISWFAPEDHGYGSEAPAENKPN 138
Cdd:COG5635     26 AIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLLLLLAEALL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  139 SEKKLEDREKKLINQEKKTFRMRDKYIDRDSEYLLQENEPDVNLDQQLLEDLQkkkTDLRYIEMQHFREKLPSFGmqkel 218
Cdd:COG5635    106 ALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLY---VPLNLLERIESLKRLELLE----- 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  219 vnmiDNHQVTVISGETGCGKTTqVTQFILDNYIERGKGSACRIvctqPRRISAISVAERVAAERAetcgngnstgyqirL 298
Cdd:COG5635    178 ----AKKKRLLILGEPGSGKTT-LLRYLALELAERYLDAEDPI----PILIELRDLAEEASLEDL--------------L 234
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911174477  299 QSRLPRKQGSilycTTGIILQWLQSDphlssvsHIV-----LDEIHERNLQSDVLmTVIKDLLNYRPDLKVIL 366
Cdd:COG5635    235 AEALEKRGGE----PEDALERLLRNG-------RLLllldgLDEVPDEADRDEVL-NQLRRFLERYPKARVII 295
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
306-372 6.19e-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: 39.10  E-value: 6.19e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1911174477  306 QGSILYCTTGIILQWLQSdpHLSSVSHI---VLDE----IHERNLQSDVLMtvIKDLLnyRPDLKVILMSATLN 372
Cdd:cd17963    111 TAQIVIGTPGTVLDWLKK--RQLDLKKIkilVLDEadvmLDTQGHGDQSIR--IKRML--PRNCQILLFSATFP 178
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
548-607 8.20e-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: 8.20e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911174477  548 KIVIATNIAETSITIDDVVYVIdggkiketHFDtqnnistmsaEWVSKANAKQRKGRAGR 607
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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