NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1371546596|ref|XP_002809102|]
View 

pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 [Plasmodium falciparum 3D7]

Protein Classification

ATP-dependent RNA helicase( domain architecture ID 13388279)

DEAD/DEAH box containing ATP-dependent RNA helicase catalyzes the unwinding of RNA, similar to DEAH box protein 34 (DHX34) that is required for nonsense-mediated decay (NMD) degradation of mRNA transcripts containing premature stop codons

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
477-1045 1.30e-145

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: 458.78  E-value: 1.30e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  477 ESLPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLV 556
Cdd:COG1643      8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGETV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  557 GYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNIC-LKRNDLKLIVTSATID 635
Cdd:COG1643     88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMSATLD 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  636 AKKFSAFFGNAPIYNIQGRTFKVHIEYL--RTPCNDYIEC---AVQKAIQIHvsdnnydnnFGDILIFMTGQEDINATCY 710
Cdd:COG1643    168 AERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDAvadAVREALAEE---------PGDILVFLPGEREIRRTAE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  711 LLSERFYevyesykesknnkKDTInkiknilnednnnnnndsnikkkvdgdnntndhmiypfyIFPIYSQLSSEQQSKIF 790
Cdd:COG1643    239 ALRGRLP-------------PDTE---------------------------------------ILPLYGRLSAAEQDRAF 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  791 KKYD--LRKIIVSTNIAETSLTLDGIKYVIDTGYCKLKVYNQTIGMDVLQVTPISQANANQRSGRAGRTGAGICYRLYTE 868
Cdd:COG1643    267 APAPhgRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSE 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  869 NTFLcDLYQNNIPEIQRSNLSNVVLLLKSLHVQNLFEFDFIDVPSKESI---INSLHElwvLGAINNEGNLTDIGRKMVQ 945
Cdd:COG1643    347 EDFA-RRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIadaRALLQE---LGALDADGRLTPLGRALAR 422
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  946 FPLDPPLSKIVIYSQNFQCTKEILIIVSMLSSPSIFLESkennesieskkekftvPESDHLTLLNIYLQWRSHNysyswc 1025
Cdd:COG1643    423 LPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGA----------------AGSDLLARLNLWRRLREQQ------ 480
                          570       580
                   ....*....|....*....|
gi 1371546596 1026 tKNFIQYKALNKAKEVYSQL 1045
Cdd:COG1643    481 -REFLSYLRLREWRDLARQL 499
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1066-1143 6.02e-20

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: 85.00  E-value: 6.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596 1066 IRKTICSGYFHNAAKLK-SFSEYINLRTNVSCHVHPNSSLYNI-GYTPDYVIYQEIVFTTKEYMRNVTTVDPEWLCELGP 1143
Cdd:pfam07717    1 LRAALAAGLYPNVARRDpKGKGYTTLSDNQRVFIHPSSVLFNEkTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
477-1045 1.30e-145

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 458.78  E-value: 1.30e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  477 ESLPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLV 556
Cdd:COG1643      8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGETV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  557 GYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNIC-LKRNDLKLIVTSATID 635
Cdd:COG1643     88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMSATLD 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  636 AKKFSAFFGNAPIYNIQGRTFKVHIEYL--RTPCNDYIEC---AVQKAIQIHvsdnnydnnFGDILIFMTGQEDINATCY 710
Cdd:COG1643    168 AERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDAvadAVREALAEE---------PGDILVFLPGEREIRRTAE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  711 LLSERFYevyesykesknnkKDTInkiknilnednnnnnndsnikkkvdgdnntndhmiypfyIFPIYSQLSSEQQSKIF 790
Cdd:COG1643    239 ALRGRLP-------------PDTE---------------------------------------ILPLYGRLSAAEQDRAF 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  791 KKYD--LRKIIVSTNIAETSLTLDGIKYVIDTGYCKLKVYNQTIGMDVLQVTPISQANANQRSGRAGRTGAGICYRLYTE 868
Cdd:COG1643    267 APAPhgRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSE 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  869 NTFLcDLYQNNIPEIQRSNLSNVVLLLKSLHVQNLFEFDFIDVPSKESI---INSLHElwvLGAINNEGNLTDIGRKMVQ 945
Cdd:COG1643    347 EDFA-RRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIadaRALLQE---LGALDADGRLTPLGRALAR 422
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  946 FPLDPPLSKIVIYSQNFQCTKEILIIVSMLSSPSIFLESkennesieskkekftvPESDHLTLLNIYLQWRSHNysyswc 1025
Cdd:COG1643    423 LPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGA----------------AGSDLLARLNLWRRLREQQ------ 480
                          570       580
                   ....*....|....*....|
gi 1371546596 1026 tKNFIQYKALNKAKEVYSQL 1045
Cdd:COG1643    481 -REFLSYLRLREWRDLARQL 499
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
477-1143 7.61e-143

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: 463.47  E-value: 7.61e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  477 ESLPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLV 556
Cdd:TIGR01967   64 DNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKV 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  557 GYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATIDA 636
Cdd:TIGR01967  144 GYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDP 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  637 KKFSAFFGNAPIYNIQGRTFKVHIEYlR--TPCNDYIECAVQKAIQIHVsDNNYDNNFGDILIFMTGQEDINATCYLLSE 714
Cdd:TIGR01967  224 ERFSRHFNNAPIIEVSGRTYPVEVRY-RplVEEQEDDDLDQLEAILDAV-DELFAEGPGDILIFLPGEREIRDAAEILRK 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  715 RFYEVYEsykesknnkkdtinkiknilnednnnnnndsnikkkvdgdnntndhmiypfyIFPIYSQLSSEQQSKIFKKYD 794
Cdd:TIGR01967  302 RNLRHTE----------------------------------------------------ILPLYARLSNKEQQRVFQPHS 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  795 LRKIIVSTNIAETSLTLDGIKYVIDTGYCKLKVYNQTIGMDVLQVTPISQANANQRSGRAGRTGAGICYRLYTENTFLC- 873
Cdd:TIGR01967  330 GRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSr 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  874 DLYQNniPEIQRSNLSNVVLLLKSLHVQNLFEFDFIDVPSKESI---INSLHELWVLGAINNEGNLTDIGRKMVQFPLDP 950
Cdd:TIGR01967  410 PEFTD--PEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIrdgFRLLEELGALDDDEAEPQLTPIGRQLAQLPVDP 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  951 PLSKIVIYSQNFQCTKEILIIVSMLSSPSIFLESKENNESIESKKEKFTVPESDHLTLLNIY------LQWRSHNYSYSW 1024
Cdd:TIGR01967  488 RLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWrhieeqRQALSANQFRNA 567
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596 1025 CTKNFIQYKALNKAKEVYSQLIDIIKTLNIKNVSCDNKWELIRKTICSGYFHNAAKLKSFSEYINLRtNVSCHVHPNSSL 1104
Cdd:TIGR01967  568 CRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKALLSGLLSQIGMKDEKHEYDGAR-GRKFHIFPGSPL 646
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1371546596 1105 YniGYTPDYVIYQEIVFTTKEYMRNVTTVDPEWLCELGP 1143
Cdd:TIGR01967  647 F--KKPPKWVMAAELVETSKLYARLVAKIEPEWVEPVAG 683
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
477-1138 1.29e-141

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 460.68  E-value: 1.29e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  477 ESLPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLV 556
Cdd:PRK11131    71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCV 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  557 GYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATIDA 636
Cdd:PRK11131   151 GYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDP 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  637 KKFSAFFGNAPIYNIQGRTFKVHIEYlrTPCNDYIECAVQKAIQ--IHVSDNNYDNNFGDILIFMTGQEDINATCYLLSe 714
Cdd:PRK11131   231 ERFSRHFNNAPIIEVSGRTYPVEVRY--RPIVEEADDTERDQLQaiFDAVDELGREGPGDILIFMSGEREIRDTADALN- 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  715 rfyevyesykesKNNKKDTinkiknilnednnnnnndsnikkkvdgdnntndhmiypfYIFPIYSQLSSEQQSKIFKKYD 794
Cdd:PRK11131   308 ------------KLNLRHT---------------------------------------EILPLYARLSNSEQNRVFQSHS 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  795 LRKIIVSTNIAETSLTLDGIKYVIDTGYCKLKVYNQTIGMDVLQVTPISQANANQRSGRAGRTGAGICYRLYTENTFL-- 872
Cdd:PRK11131   337 GRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLsr 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  873 ---CDlyqnniPEIQRSNLSNVVLLLKSLHVQNLFEFDFIDVPSKESIINSLHELWVLGAINNEGN-----LTDIGRKMV 944
Cdd:PRK11131   417 pefTD------PEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLA 490
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  945 QFPLDPPLSKIVIYSQNFQCTKEILIIVSMLSSPSIFLESKENNESIESKKEKFTVPESDHLTLLNI--YLQWR----SH 1018
Cdd:PRK11131   491 QLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLwnYLQEQqkalSS 570
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596 1019 NYSYSWCTKNFIQYKALNKAKEVYSQLIDIIKTLNIKNVSCDNKWELIRKTICSGYF-HNAAKLKSFSEYINLRtNVSCH 1097
Cdd:PRK11131   571 NQFRRLCRTDYLNYLRVREWQDIYTQLRQVVKELGIPVNSEPAEYREIHTALLTGLLsHIGMKDAEKQEYTGAR-NARFS 649
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1371546596 1098 VHPNSSLYNigYTPDYVIYQEIVFTTKEYMRNVTTVDPEWL 1138
Cdd:PRK11131   650 IFPGSGLFK--KPPKWVMVAELVETSRLWGRIAARIEPEWI 688
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
479-651 6.54e-93

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: 294.37  E-value: 6.54e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLVGY 558
Cdd:cd17983      1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  559 TIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATIDAKK 638
Cdd:cd17983     81 AIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDADK 160
                          170
                   ....*....|...
gi 1371546596  639 FSAFFGNAPIYNI 651
Cdd:cd17983    161 FADFFGNVPIFTI 173
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
920-1008 2.57e-26

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: 104.24  E-value: 2.57e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  920 SLHELWVLGAINNEGNLTDIGRKMVQFPLDPPLSKIVIYSQNFQCTKEILIIVSMLSSPSIFLES--------------- 984
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprsaakaarrr 80
                           90       100
                   ....*....|....*....|....
gi 1371546596  985 KENNESIESKKEKFTVPESDHLTL 1008
Cdd:pfam04408   81 RRAADEKARAKFARLDLEGDHLTL 104
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
927-1009 2.68e-26

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 103.12  E-value: 2.68e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596   927 LGAINNEGNLTDIGRKMVQFPLDPPLSKIVIYSQNFQCTKEILIIVSMLSSPSIFleSKENNESIESKKEKFTVPESDHL 1006
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESDHL 79

                    ...
gi 1371546596  1007 TLL 1009
Cdd:smart00847   80 TLL 82
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1066-1143 6.02e-20

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: 85.00  E-value: 6.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596 1066 IRKTICSGYFHNAAKLK-SFSEYINLRTNVSCHVHPNSSLYNI-GYTPDYVIYQEIVFTTKEYMRNVTTVDPEWLCELGP 1143
Cdd:pfam07717    1 LRAALAAGLYPNVARRDpKGKGYTTLSDNQRVFIHPSSVLFNEkTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
477-1045 1.30e-145

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 458.78  E-value: 1.30e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  477 ESLPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLV 556
Cdd:COG1643      8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGETV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  557 GYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNIC-LKRNDLKLIVTSATID 635
Cdd:COG1643     88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMSATLD 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  636 AKKFSAFFGNAPIYNIQGRTFKVHIEYL--RTPCNDYIEC---AVQKAIQIHvsdnnydnnFGDILIFMTGQEDINATCY 710
Cdd:COG1643    168 AERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDAvadAVREALAEE---------PGDILVFLPGEREIRRTAE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  711 LLSERFYevyesykesknnkKDTInkiknilnednnnnnndsnikkkvdgdnntndhmiypfyIFPIYSQLSSEQQSKIF 790
Cdd:COG1643    239 ALRGRLP-------------PDTE---------------------------------------ILPLYGRLSAAEQDRAF 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  791 KKYD--LRKIIVSTNIAETSLTLDGIKYVIDTGYCKLKVYNQTIGMDVLQVTPISQANANQRSGRAGRTGAGICYRLYTE 868
Cdd:COG1643    267 APAPhgRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSE 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  869 NTFLcDLYQNNIPEIQRSNLSNVVLLLKSLHVQNLFEFDFIDVPSKESI---INSLHElwvLGAINNEGNLTDIGRKMVQ 945
Cdd:COG1643    347 EDFA-RRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIadaRALLQE---LGALDADGRLTPLGRALAR 422
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  946 FPLDPPLSKIVIYSQNFQCTKEILIIVSMLSSPSIFLESkennesieskkekftvPESDHLTLLNIYLQWRSHNysyswc 1025
Cdd:COG1643    423 LPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGA----------------AGSDLLARLNLWRRLREQQ------ 480
                          570       580
                   ....*....|....*....|
gi 1371546596 1026 tKNFIQYKALNKAKEVYSQL 1045
Cdd:COG1643    481 -REFLSYLRLREWRDLARQL 499
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
477-1143 7.61e-143

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: 463.47  E-value: 7.61e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  477 ESLPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLV 556
Cdd:TIGR01967   64 DNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKV 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  557 GYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATIDA 636
Cdd:TIGR01967  144 GYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDP 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  637 KKFSAFFGNAPIYNIQGRTFKVHIEYlR--TPCNDYIECAVQKAIQIHVsDNNYDNNFGDILIFMTGQEDINATCYLLSE 714
Cdd:TIGR01967  224 ERFSRHFNNAPIIEVSGRTYPVEVRY-RplVEEQEDDDLDQLEAILDAV-DELFAEGPGDILIFLPGEREIRDAAEILRK 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  715 RFYEVYEsykesknnkkdtinkiknilnednnnnnndsnikkkvdgdnntndhmiypfyIFPIYSQLSSEQQSKIFKKYD 794
Cdd:TIGR01967  302 RNLRHTE----------------------------------------------------ILPLYARLSNKEQQRVFQPHS 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  795 LRKIIVSTNIAETSLTLDGIKYVIDTGYCKLKVYNQTIGMDVLQVTPISQANANQRSGRAGRTGAGICYRLYTENTFLC- 873
Cdd:TIGR01967  330 GRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSr 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  874 DLYQNniPEIQRSNLSNVVLLLKSLHVQNLFEFDFIDVPSKESI---INSLHELWVLGAINNEGNLTDIGRKMVQFPLDP 950
Cdd:TIGR01967  410 PEFTD--PEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIrdgFRLLEELGALDDDEAEPQLTPIGRQLAQLPVDP 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  951 PLSKIVIYSQNFQCTKEILIIVSMLSSPSIFLESKENNESIESKKEKFTVPESDHLTLLNIY------LQWRSHNYSYSW 1024
Cdd:TIGR01967  488 RLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWrhieeqRQALSANQFRNA 567
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596 1025 CTKNFIQYKALNKAKEVYSQLIDIIKTLNIKNVSCDNKWELIRKTICSGYFHNAAKLKSFSEYINLRtNVSCHVHPNSSL 1104
Cdd:TIGR01967  568 CRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKALLSGLLSQIGMKDEKHEYDGAR-GRKFHIFPGSPL 646
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1371546596 1105 YniGYTPDYVIYQEIVFTTKEYMRNVTTVDPEWLCELGP 1143
Cdd:TIGR01967  647 F--KKPPKWVMAAELVETSKLYARLVAKIEPEWVEPVAG 683
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
477-1138 1.29e-141

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 460.68  E-value: 1.29e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  477 ESLPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLV 556
Cdd:PRK11131    71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCV 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  557 GYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATIDA 636
Cdd:PRK11131   151 GYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDP 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  637 KKFSAFFGNAPIYNIQGRTFKVHIEYlrTPCNDYIECAVQKAIQ--IHVSDNNYDNNFGDILIFMTGQEDINATCYLLSe 714
Cdd:PRK11131   231 ERFSRHFNNAPIIEVSGRTYPVEVRY--RPIVEEADDTERDQLQaiFDAVDELGREGPGDILIFMSGEREIRDTADALN- 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  715 rfyevyesykesKNNKKDTinkiknilnednnnnnndsnikkkvdgdnntndhmiypfYIFPIYSQLSSEQQSKIFKKYD 794
Cdd:PRK11131   308 ------------KLNLRHT---------------------------------------EILPLYARLSNSEQNRVFQSHS 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  795 LRKIIVSTNIAETSLTLDGIKYVIDTGYCKLKVYNQTIGMDVLQVTPISQANANQRSGRAGRTGAGICYRLYTENTFL-- 872
Cdd:PRK11131   337 GRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLsr 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  873 ---CDlyqnniPEIQRSNLSNVVLLLKSLHVQNLFEFDFIDVPSKESIINSLHELWVLGAINNEGN-----LTDIGRKMV 944
Cdd:PRK11131   417 pefTD------PEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLA 490
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  945 QFPLDPPLSKIVIYSQNFQCTKEILIIVSMLSSPSIFLESKENNESIESKKEKFTVPESDHLTLLNI--YLQWR----SH 1018
Cdd:PRK11131   491 QLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLwnYLQEQqkalSS 570
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596 1019 NYSYSWCTKNFIQYKALNKAKEVYSQLIDIIKTLNIKNVSCDNKWELIRKTICSGYF-HNAAKLKSFSEYINLRtNVSCH 1097
Cdd:PRK11131   571 NQFRRLCRTDYLNYLRVREWQDIYTQLRQVVKELGIPVNSEPAEYREIHTALLTGLLsHIGMKDAEKQEYTGAR-NARFS 649
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1371546596 1098 VHPNSSLYNigYTPDYVIYQEIVFTTKEYMRNVTTVDPEWL 1138
Cdd:PRK11131   650 IFPGSGLFK--KPPKWVMVAELVETSRLWGRIAARIEPEWI 688
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
479-651 6.54e-93

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: 294.37  E-value: 6.54e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLVGY 558
Cdd:cd17983      1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  559 TIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATIDAKK 638
Cdd:cd17983     81 AIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDADK 160
                          170
                   ....*....|...
gi 1371546596  639 FSAFFGNAPIYNI 651
Cdd:cd17983    161 FADFFGNVPIFTI 173
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
495-651 6.61e-87

DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 277.42  E-value: 6.61e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  495 NNIIIIVGETGSGKTTQIVQYLYEEGY--HRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLVGYTIRFEDNTTKDTKI 572
Cdd:cd17917      1 NQVVVIVGETGSGKTTQVPQFLLEDGLakGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371546596  573 RYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATIDAKKFSAFFGNAPIYNI 651
Cdd:cd17917     81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
479-651 1.75e-84

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: 271.92  E-value: 1.75e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLVGY 558
Cdd:cd17978      1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGMIGITQPRRVAAVSVAKRVAEEMGVELGQLVGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  559 TIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKR-----NDLKLIVTSAT 633
Cdd:cd17978     81 SVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVIIMSAT 160
                          170
                   ....*....|....*...
gi 1371546596  634 IDAKKFSAFFGNAPIYNI 651
Cdd:cd17978    161 LDADLFSEYFNGAPVLYI 178
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
476-651 5.90e-83

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: 267.43  E-value: 5.90e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  476 KESLPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSL 555
Cdd:cd17971      3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLGQE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  556 VGYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATID 635
Cdd:cd17971     83 VGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSATLD 162
                          170
                   ....*....|....*.
gi 1371546596  636 AKKFSAFFGNAPIYNI 651
Cdd:cd17971    163 AVKFSQYFYEAPIFTI 178
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
479-980 2.39e-75

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


Pssm-ID: 273901 [Multi-domain]  Cd Length: 819  Bit Score: 267.02  E-value: 2.39e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQI-VQYLYEEGYHRNgiICCTQPRRVAAVSVAYRVSYEMNVDIGSLVG 557
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVpLALLDAPGIGGK--IIMLEPRRLAARSAAQRLASQLGEAVGQTVG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  558 YTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNI-CLKRNDLKLIVTSATIDA 636
Cdd:TIGR01970   79 YRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVqSSLREDLKILAMSATLDG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  637 KKFSAFFGNAPIYNIQGRTFKVHIEYLRTPCNDYIECAVQKAIQIHVSDNNydnnfGDILIFMTGQEDINATCYLLSERF 716
Cdd:TIGR01970  159 ERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDAVSRAVEHALASET-----GSILVFLPGQAEIRRVQEQLAERL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  717 yevyesykesknnkkdtinkiknilnednnnnnndsniKKKVDgdnntndhmiypfyIFPIYSQLSSEQQSKIFK--KYD 794
Cdd:TIGR01970  234 --------------------------------------DSDVL--------------ICPLYGELSLAAQDRAIKpdPQG 261
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  795 LRKIIVSTNIAETSLTLDGIKYVIDTGYCKLKVYNQTIGMDVLQVTPISQANANQRSGRAGRTGAGICYRLYTENTFLCD 874
Cdd:TIGR01970  262 RRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQRL 341
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  875 LYQNNiPEIQRSNLSNVVLLLKSLHVQNLFEFDFIDVPSKESIINSLHELWVLGAINNEGNLTDIGRKMVQFPLDPPLSK 954
Cdd:TIGR01970  342 PAQDE-PEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAA 420
                          490       500
                   ....*....|....*....|....*.
gi 1371546596  955 IVIYSQNFQCTKEILIIVSMLSSPSI 980
Cdd:TIGR01970  421 MLLSAHSTGLAALACDLAALLEERGL 446
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
471-651 3.06e-75

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: 246.56  E-value: 3.06e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  471 ELLKLKESLPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNG--IICCTQPRRVAAVSVAYRVSYEM 548
Cdd:cd17973      5 EILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPkkLVACTQPRRVAAMSVAQRVAEEM 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  549 NVDIGSLVGYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLI 628
Cdd:cd17973     85 DVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLI 164
                          170       180
                   ....*....|....*....|...
gi 1371546596  629 VTSATIDAKKFSAFFGNAPIYNI 651
Cdd:cd17973    165 VMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
479-651 3.48e-75

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: 245.88  E-value: 3.48e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHR-NGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLVG 557
Cdd:cd17974      1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKgGGKIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  558 YTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATIDAK 637
Cdd:cd17974     81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160
                          170
                   ....*....|....
gi 1371546596  638 KFSAFFGNAPIYNI 651
Cdd:cd17974    161 KFSAFFDDAPIFRI 174
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
479-651 1.20e-68

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: 227.82  E-value: 1.20e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLVGY 558
Cdd:cd17984      1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGSKVGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  559 TIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRN-----DLKLIVTSAT 633
Cdd:cd17984     81 QVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVVMSAT 160
                          170
                   ....*....|....*...
gi 1371546596  634 IDAKKFSAFFGNAPIYNI 651
Cdd:cd17984    161 LELAKLSAFFGNCPVFDI 178
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
479-643 2.04e-68

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: 227.35  E-value: 2.04e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNG-IICCTQPRRVAAVSVAYRVSYEMNVDIGSLVG 557
Cdd:cd17980      1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGrVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  558 YTIRFEDNTTKD-TKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATIDA 636
Cdd:cd17980     81 YCIRFDDCTDPQaTRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160

                   ....*..
gi 1371546596  637 KKFSAFF 643
Cdd:cd17980    161 EKFRDFF 167
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
479-648 2.29e-64

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: 215.40  E-value: 2.29e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLVGY 558
Cdd:cd17989      1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAVGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  559 TIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATIDAKK 638
Cdd:cd17989     81 KVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAER 160
                          170
                   ....*....|
gi 1371546596  639 FSAFFGNAPI 648
Cdd:cd17989    161 FSRHFNNAPI 170
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
478-962 5.29e-64

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 233.66  E-value: 5.29e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  478 SLPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQI-VQYLYEEGyhRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLV 556
Cdd:PRK11664     3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLpLQLLQHGG--INGKIIMLEPRRLAARNVAQRLAEQLGEKPGETV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  557 GYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNI--CLkRNDLKLIVTSATI 634
Cdd:PRK11664    81 GYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVqqGL-RDDLKLLIMSATL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  635 DAKKFSAFFGNAPIYNIQGRTFKVHIEYLRTPCNDYIECAVQKAIQihvsdNNYDNNFGDILIFMTGQEDINATCYLLSE 714
Cdd:PRK11664   160 DNDRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQRFDEAVARATA-----ELLRQESGSLLLFLPGVGEIQRVQEQLAS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  715 RFYEvyesykesknnkkDTInkiknilnednnnnnndsnikkkvdgdnntndhmiypfyIFPIYSQLS-SEQQSKIF-KK 792
Cdd:PRK11664   235 RVAS-------------DVL---------------------------------------LCPLYGALSlAEQQKAILpAP 262
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  793 YDLRKIIVSTNIAETSLTLDGIKYVIDTGYCKLKVYNQTIGMDVLQVTPISQANANQRSGRAGRTGAGICYRLYTENTFL 872
Cdd:PRK11664   263 AGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAE 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  873 CDLYQNNiPEIQRSNLSNVVLLLKSLHVQNLFEFDFIDVPSKESIINSLHELWVLGAINNEGNLTDIGRKMVQFPLDPPL 952
Cdd:PRK11664   343 RAAAQSE-PEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRL 421
                          490
                   ....*....|
gi 1371546596  953 SKIVIYSQNF 962
Cdd:PRK11664   422 AAMLVAAKED 431
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
479-647 6.42e-63

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: 212.21  E-value: 6.42e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGY-----HRNGIICCTQPRRVAAVSVAYRVSYEMNVdIG 553
Cdd:cd17982      1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFgspesDNPGMIGITQPRRVAAVSMAKRVAEELNV-FG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  554 SLVGYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRND--------- 624
Cdd:cd17982     80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159
                          170       180
                   ....*....|....*....|....*..
gi 1371546596  625 -LKLIVTSATIDAKKFSA---FFGNAP 647
Cdd:cd17982    160 pLKLVIMSATLRVEDFTEnklLFPRPP 186
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
656-866 4.28e-58

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: 197.37  E-value: 4.28e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  656 FKVHIEYLRTP-----------CNDYIECAVQKAIQIHVSDNNydnnfGDILIFMTGQEDINATCYLLserfyevyESYK 724
Cdd:cd18791      1 FPVEVYYLEDIlellgissekeDPDYVDAAVRLILQIHRTEEP-----GDILVFLPGQEEIERLCELL--------REEL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  725 ESKNNKKdtinkiknilnednnnnnndsnikkkvdgdnntndhmiypFYIFPIYSQLSSEQQSKIFKKYDL--RKIIVST 802
Cdd:cd18791     68 LSPDLGK----------------------------------------LLVLPLHSSLPPEEQQRVFEPPPPgvRKVVLAT 107
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371546596  803 NIAETSLTLDGIKYVIDTGYCKLKVYNQTIGMDVLQVTPISQANANQRSGRAGRTGAGICYRLY 866
Cdd:cd18791    108 NIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
479-648 6.37e-57

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: 194.20  E-value: 6.37e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRngiICCTQPRRVAAVSVAYRVSYEMNVDIGSLVGY 558
Cdd:cd17979      1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH---IACTQPRRIACISLAKRVAFESLNQYGSKVAY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  559 TIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATIDAKK 638
Cdd:cd17979     78 QIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIEL 157
                          170
                   ....*....|
gi 1371546596  639 FSAFFGNAPI 648
Cdd:cd17979    158 FSGYFEGAPV 167
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
479-651 6.53e-50

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: 174.72  E-value: 6.53e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYE-----EGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIG 553
Cdd:cd17975      1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEdlllnGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  554 -----SLVGYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLI 628
Cdd:cd17975     81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
                          170       180
                   ....*....|....*....|...
gi 1371546596  629 VTSATIDAKKFSAFFGNAPIYNI 651
Cdd:cd17975    161 LMSATVDCEKFSSYFTHCPILRI 183
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
479-651 2.64e-49

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: 172.72  E-value: 2.64e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRN-GIIC---CTQPRRVAAVSVAYRVSYEM--NVDI 552
Cdd:cd17981      1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGkGSSCrivCTQPRRISAISVAERVAAERaeSCGL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  553 GSLVGYTIRFEDNTT-KDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTS 631
Cdd:cd17981     81 GNSTGYQIRLESRKPrKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160
                          170       180
                   ....*....|....*....|
gi 1371546596  632 ATIDAKKFSAFFGNAPIYNI 651
Cdd:cd17981    161 ATLNAEKFSDYFNNCPMIHI 180
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
479-648 1.36e-47

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: 167.70  E-value: 1.36e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYE---EGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSL 555
Cdd:cd17977      1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEyclSAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNIGHE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  556 VGYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATID 635
Cdd:cd17977     81 VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPHL 160
                          170
                   ....*....|...
gi 1371546596  636 AKKFSAFFGNAPI 648
Cdd:cd17977    161 SSKLLSYYGNVPL 173
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
479-651 6.56e-46

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: 163.08  E-value: 6.56e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYhRNGIIC---CTQPRRVAAVSVAYRVSYEMNVDIGSL 555
Cdd:cd17987      1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCY-ANGIPCrifCTQPRRLAAIAVAERVAAERGEKIGQT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  556 VGYTIRFEDNTTKDTKIRYVTDGILLRETLN-DKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATI 634
Cdd:cd17987     80 VGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAAL 159
                          170
                   ....*....|....*..
gi 1371546596  635 DAKKFSAFFGNAPIYNI 651
Cdd:cd17987    160 DVNLFIRYFGSCPVIYI 176
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
454-648 6.02e-45

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: 162.31  E-value: 6.02e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  454 NIENNNKDKKNTLKDKEELLKLKESLPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEgYHRNGI-----IC 528
Cdd:cd17972     34 DLKNELMYQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDD-FIQNDRaaecnIV 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  529 CTQPRRVAAVSVAYRVSYEMNVDIGSLVGYTIRFEDNTTKD-TKIRYVTDGILLRETLNDkeLDKYSVIIMDEAHERSIN 607
Cdd:cd17972    113 VTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRPhASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDIN 190
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1371546596  608 TDVLLGILKNICLKRNDLKLIVTSATIDAKKFSAFFGNAPI 648
Cdd:cd17972    191 TDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPV 231
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
479-651 6.59e-44

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: 157.31  E-value: 6.59e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGI----ICCTQPRRVAAVSVAYRVSYEMNVDIGS 554
Cdd:cd17985      1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLpvanIICTQPRRISAISVAERVAQERAERVGQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  555 LVGYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATI 634
Cdd:cd17985     81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
                          170
                   ....*....|....*..
gi 1371546596  635 DAKKFSAFFGNAPIYNI 651
Cdd:cd17985    161 NAELFSDYFNSCPVIHI 177
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
479-644 1.06e-41

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: 151.12  E-value: 1.06e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGI--ICCTQPRRVAAVSVAYRVSYEMNVDIGSLV 556
Cdd:cd17988      1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYcnIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  557 GYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNIcLKRND--LKLIVTSATI 634
Cdd:cd17988     81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRL-LRTNSrhVKIILMSATI 159
                          170
                   ....*....|
gi 1371546596  635 DAKKFSAFFG 644
Cdd:cd17988    160 SCKEFADYFT 169
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
479-648 6.77e-41

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: 148.63  E-value: 6.77e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYRVSYEMNVDIGSLVGY 558
Cdd:cd17990      1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  559 TIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNI-CLKRNDLKLIVTSATIDAK 637
Cdd:cd17990     81 RVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVqQLLRDDLRLLAMSATLDGD 160
                          170
                   ....*....|.
gi 1371546596  638 KFSAFFGNAPI 648
Cdd:cd17990    161 GLAALLPEAPV 171
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
479-651 9.03e-39

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: 142.73  E-value: 9.03e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYN-NNIIIIVGETGSGKTTQIVQYLYEEGYHRN---GIICCTQPRRVAAVSVAYRVSYEMNVDIGS 554
Cdd:cd17986      1 LPIWAAKFTFLEQLESpSGIVLVSGEPGSGKSTQVPQWCAEFALSRGfqkGQVTVTQPHPLAARSLALRVADEMDLNLGH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  555 LVGYTIRFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTSATI 634
Cdd:cd17986     81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPA 160
                          170
                   ....*....|....*..
gi 1371546596  635 DAKKFSAFFGNAPIYNI 651
Cdd:cd17986    161 LEPKLRAFWGNPPVVHV 177
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
479-648 1.17e-38

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: 142.24  E-value: 1.17e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  479 LPIYKSKHELLDAVYNNNIIIIVGETGSGKTTQIVQYLYE------EGYHRNGIIccTQPRRVAAVSVAYRVSYEMNVDI 552
Cdd:cd17976      1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEdyvlrgRGARCNVVI--TQPRRISAVSVAQRVAHELGPNL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  553 GSLVGYTIRFEDN-TTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINTDVLLGILKNICLKRNDLKLIVTS 631
Cdd:cd17976     79 RRNVGYQVRLESRpPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMS 158
                          170
                   ....*....|....*..
gi 1371546596  632 ATIDAKKFSAFFGNAPI 648
Cdd:cd17976    159 ATGDNQRLSRYFGGCPV 175
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
920-1008 2.57e-26

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: 104.24  E-value: 2.57e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  920 SLHELWVLGAINNEGNLTDIGRKMVQFPLDPPLSKIVIYSQNFQCTKEILIIVSMLSSPSIFLES--------------- 984
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprsaakaarrr 80
                           90       100
                   ....*....|....*....|....
gi 1371546596  985 KENNESIESKKEKFTVPESDHLTL 1008
Cdd:pfam04408   81 RRAADEKARAKFARLDLEGDHLTL 104
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
927-1009 2.68e-26

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 103.12  E-value: 2.68e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596   927 LGAINNEGNLTDIGRKMVQFPLDPPLSKIVIYSQNFQCTKEILIIVSMLSSPSIFleSKENNESIESKKEKFTVPESDHL 1006
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESDHL 79

                    ...
gi 1371546596  1007 TLL 1009
Cdd:smart00847   80 TLL 82
DEXDc smart00487
DEAD-like helicases superfamily;
494-662 4.55e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 98.33  E-value: 4.55e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596   494 NNNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIIC-CTQPRRVAAVSVAYRVSYEM----NVDIGSLVGYTIR--FEDNT 566
Cdd:smart00487   23 GLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVlVLVPTRELAEQWAEELKKLGpslgLKVVGLYGGDSKReqLRKLE 102
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596   567 TKDTKIRYVTDGILLRETLNDK-ELDKYSVIIMDEAHERS--INTDVLLGILKnicLKRNDLKLIVTSATI--DAKKFSA 641
Cdd:smart00487  103 SGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLLdgGFGDQLEKLLK---LLPKNVQLLLLSATPpeEIENLLE 179
                           170       180
                    ....*....|....*....|.
gi 1371546596   642 FFGNAPIYNIQGRTFKVHIEY 662
Cdd:smart00487  180 LFLNDPVFIDVGFTPLEPIEQ 200
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1066-1143 6.02e-20

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: 85.00  E-value: 6.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596 1066 IRKTICSGYFHNAAKLK-SFSEYINLRTNVSCHVHPNSSLYNI-GYTPDYVIYQEIVFTTKEYMRNVTTVDPEWLCELGP 1143
Cdd:pfam07717    1 LRAALAAGLYPNVARRDpKGKGYTTLSDNQRVFIHPSSVLFNEkTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80
HELICc smart00490
helicase superfamily c-terminal domain;
772-858 1.50e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 66.85  E-value: 1.50e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596   772 FYIFPIYSQLSSEQQSKIFKKY--DLRKIIVSTNIAETSLTLDGIKYVIDTGYcklkvynqtigmdvlqvtPISQANANQ 849
Cdd:smart00490   12 IKVARLHGGLSQEEREEILDKFnnGKIKVLVATDVAERGLDLPGVDLVIIYDL------------------PWSPASYIQ 73

                    ....*....
gi 1371546596   850 RSGRAGRTG 858
Cdd:smart00490   74 RIGRAGRAG 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
499-633 1.41e-09

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: 57.80  E-value: 1.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  499 IIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVA--YRVSYEMNVDIGSLVGYT---IRFEdNTTKDTKIR 573
Cdd:cd00046      5 LITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAerLRELFGPGIRVAVLVGGSsaeEREK-NKLGDADII 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546596  574 YVTDGILLRETLNDK--ELDKYSVIIMDEAHERSINTDVLLGILKNICLKRN-DLKLIVTSAT 633
Cdd:cd00046     84 IATPDMLLNLLLREDrlFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLkNAQVILLSAT 146
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
774-858 3.10e-09

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: 55.68  E-value: 3.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  774 IFPIYSQLSSEQQSKIFKKY--DLRKIIVSTNIAETSLTLDGIKYVIDTGYCKlkvynqtigmdvlqvtpiSQANANQRS 851
Cdd:pfam00271   41 VARLHGDLSQEEREEILEDFrkGKIDVLVATDVAERGLDLPDVDLVINYDLPW------------------NPASYIQRI 102

                   ....*..
gi 1371546596  852 GRAGRTG 858
Cdd:pfam00271  103 GRAGRAG 109
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
447-867 1.49e-07

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 55.75  E-value: 1.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  447 KIYSslfNIENNNKDKKNTLKDKEELLKLK-ESLPIyKSKHELLDAVYNNNIIIIVGETGSGKTTQI------VQYLYeE 519
Cdd:PHA02653   134 GIFS---NNVGSKKDTIGILGNPEPFSKIPlASLQP-DVQLKIFEAWISRKPVVLTGGTGVGKTSQVpklllwFNYLF-G 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  520 GYHRNGIICCT-QPR-------RVAAV---SVAYRVSYEMNVDIGSLVgyTIRFEDNTTKDTKIRYVTDGILL---RETL 585
Cdd:PHA02653   209 GFDNLDKIDPNfIERpivlslpRVALVrlhSITLLKSLGFDEIDGSPI--SLKYGSIPDELINTNPKPYGLVFsthKLTL 286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  586 NdkELDKYSVIIMDEAHERSINTDVLLGIL-KNICLKRNdlkLIVTSATI--DAKKFSAFFGNAPIYNIQGRT-FKVHIE 661
Cdd:PHA02653   287 N--KLFDYGTVIIDEVHEHDQIGDIIIAVArKHIDKIRS---LFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISEV 361
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  662 YLRTPCN-----DYIECAVQKAIQIhVSDNNYDNNFGDILIFMTgqediNATCyllserfyEVYESYKESKnnkkdtink 736
Cdd:PHA02653   362 YVKNKYNpknkrAYIEEEKKNIVTA-LKKYTPPKGSSGIVFVAS-----VSQC--------EEYKKYLEKR--------- 418
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  737 iknilnednnnnnndsnikkkvdgdnntndHMIYPFYIfpIYSQLSS--EQQSKIFKKYDLrKIIVSTNIAETSLTLDGI 814
Cdd:PHA02653   419 ------------------------------LPIYDFYI--IHGKVPNidEILEKVYSSKNP-SIIISTPYLESSVTIRNA 465
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  815 KYVIDTGycklKVY-------NQTIgmdvlqvtpISQANANQRSGRAGRTGAGICYRLYT 867
Cdd:PHA02653   466 THVYDTG----RVYvpepfggKEMF---------ISKSMRTQRKGRVGRVSPGTYVYFYD 512
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
489-635 7.35e-07

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: 50.32  E-value: 7.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  489 LDAVYNNNIIIIVGETGSGKTT----QIVQYLYEEGYHRNGIICCtqPRRVAA---VSVAYRVSYEMNVDIGSLV-GYTI 560
Cdd:pfam00270    8 IPAILEGRDVLVQAPTGSGKTLafllPALEALDKLDNGPQALVLA--PTRELAeqiYEELKKLGKGLGLKVASLLgGDSR 85
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371546596  561 RFEDNTTKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAHERSINT--DVLLGILKNIclkRNDLKLIVTSATID 635
Cdd:pfam00270   86 KEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAHRLLDMGfgPDLEEILRRL---PKKRQILLLSATLP 159
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
504-602 3.43e-05

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


Pssm-ID: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 45.23  E-value: 3.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  504 TGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSV-AYRVSYEMNVDIGSLvgytirfEDNTTKDTKIRYVTDGILLR 582
Cdd:cd17931     10 PGAGKTTRVLPQIIREAIKKRLRTLVLAPTRVVAAEMyEALRGLPIRYRTGAV-------KEEHGGNEIVDYMCHGTFTC 82
                           90       100
                   ....*....|....*....|
gi 1371546596  583 ETLNDKELDKYSVIIMDEAH 602
Cdd:cd17931     83 RLLSPKRVPNYNLIIMDEAH 102
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
797-866 1.34e-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: 38.45  E-value: 1.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371546596  797 KIIVSTNIAETSLTLDGIKYVIDTGYcklkvynqtigmdvlqvtPISQANANQRSGRAGRTG--AGICYRLY 866
Cdd:cd18785     24 EILVATNVLGEGIDVPSLDTVIFFDP------------------PSSAASYIQRVGRAGRGGkdEGEVILFV 77
AAA_22 pfam13401
AAA domain;
497-602 2.19e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  497 IIIIVGETGSGKTTQIVQYLYEEGYHRNGIICCTQPRRVAAVSVAYrvsyemnvDIGSLVGYTIRFEDNTTKdtkiryvt 576
Cdd:pfam13401    7 ILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLR--------ALLRALGLPLSGRLSKEE-------- 70
                           90       100
                   ....*....|....*....|....*...
gi 1371546596  577 dgilLRETLND--KELDKYSVIIMDEAH 602
Cdd:pfam13401   71 ----LLAALQQllLALAVAVVLIIDEAQ 94
ResIII pfam04851
Type III restriction enzyme, res subunit;
494-602 2.52e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 39.96  E-value: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596  494 NNNIIIIVGETGSGKT---TQIVQYLYEEGYHRNGIICCtqPRRvAAVSVAY----RVSYEMNVDIGSLVGYTIRFEDNT 566
Cdd:pfam04851   22 GQKRGLIVMATGSGKTltaAKLIARLFKKGPIKKVLFLV--PRK-DLLEQALeefkKFLPNYVEIGEIISGDKKDESVDD 98
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1371546596  567 TKDTKIRYVTDGILLRETLNDKELDKYSVIIMDEAH 602
Cdd:pfam04851   99 NKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
495-631 6.36e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.51  E-value: 6.36e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546596   495 NNIIIIVGETGSGKTTQIVQYLYEEGYHRNGIIcctqprrvaavsvayrvsyemNVDIGSLVGYTIRFEDNTTKDTKIRY 574
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------YIDGEDILEEVLDQLLLIIVGGKKAS 60
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371546596   575 VTDGILLRETLNDKELDKYSVIIMDEAH-------ERSINTDVLLGILKNIcLKRNDLKLIVTS 631
Cdd:smart00382   61 GSGELRLRLALALARKLKPDVLILDEITslldaeqEALLLLLEELRLLLLL-KSEKNLTVILTT 123
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH