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Conserved domains on  [gi|1063680967|ref|NP_001321998|]
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nuclear DEIH-boxhelicase [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
217-820 6.51e-114

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: 380.58  E-value: 6.51e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKeacKIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:COG1643     10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGG---RIGMLEPRRLAARAAAERMAEELGEPVGET 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILLRVLIG----KGVnssvpDIthIIVDEIHERDSYSDFMLMILRDLLPSN-PHLRL 371
Cdd:COG1643     87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRdpelEGV-----DT--VIFDEFHERSLNADLLLALLLDLQPALrPDLKL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  372 ILMSATLDAERFSEYFGGCPVVRVPGFTYPVRTFFLDDalsvlnsdknshllsavkrdfkDEDKVSLDEAIdlawtndef 451
Cdd:COG1643    160 LVMSATLDAERFARLLGDAPVIESSGRTYPVEVRYRPL----------------------PADERDLEDAV--------- 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  452 dclVDLVssegsheaynyqnsttgltplmvfagkgrvsdvckllsvgadctlkskegitalelaekenqfetAQIIREHA 531
Cdd:COG1643    209 ---ADAV-----------------------------------------------------------------REALAEEP 220
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  532 GNIqsnsqqaqdlldkymatikpeevdvglivklmkkicsdskdgaiLVFLPGWEEISKTKEkLLDDRFFAHsakFIILC 611
Cdd:COG1643    221 GDI--------------------------------------------LVFLPGEREIRRTAE-ALRGRLPPD---TEILP 252
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  612 LHSRVPAEEQKKVFNRPPRGCRKIVLATNIAESAVTIDDVVYVIDSGRMKEKSYDPYNDVSTLQSSWVSKANAKQRAGRA 691
Cdd:COG1643    253 LYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRA 332
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  692 GRCQAGICYHLYSKLRAASLPEYRVPEVMRmpVD--ELCLQVKML---DPncnvNDFlqKLMDPPVAQSIENALIILKDI 766
Cdd:COG1643    333 GRLAPGICYRLWSEEDFARRPAFTDPEILR--ADlaSLILELAAWglgDP----EDL--PFLDPPPARAIADARALLQEL 404
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1063680967  767 GALTPEEELTELGQKFGQLPVHPRISKMIYFAILVNCLDPALILACAADEKDPF 820
Cdd:COG1643    405 GALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR 458
R3H_DEXH_helicase cd06007
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may ...
18-76 5.13e-26

R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may function as ATP-dependent DNA or RNA helicases. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


:

Pssm-ID: 100077  Cd Length: 59  Bit Score: 102.01  E-value: 5.13e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063680967   18 GAWATKVLEDFRASGNDSYVFEQQLTNSERGIIHQMCRTMGLRSKSNGSGEERRLSLFK 76
Cdd:cd06007      1 RIAINKALEDFRASDNEEYEFPSSLTNHERAVIHRLCRKLGLKSKSKGKGSNRRLSVYK 59
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
919-1007 3.07e-10

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: 58.03  E-value: 3.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  919 LRAVIAVGLYPMLGRMCPLSKNRTRSVIetiaGAKVRVPSLSNNVdmSSTKFDEALIVFDEITRGDWgVVIRSCTVLPTI 998
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGKGYTTLSD----NQRVFIHPSSVLF--NEKTFPPEWVVYQELVETTK-VYIRTVTAISPE 73

                   ....*....
gi 1063680967  999 PVLLFSREI 1007
Cdd:pfam07717   74 WLLLFAPHI 82
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
468-575 2.24e-06

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.11  E-value: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  468 NYQNSTtGLTPLMVFAGKGRVSDVCKLLSVGADCTLKSKEGITALELAEKENQFETAQIIREHAGNIQSNSQQAQDLLDK 547
Cdd:COG0666    180 NARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
                           90       100
                   ....*....|....*....|....*...
gi 1063680967  548 YMATIKPEEVDVGLIVKLMKKICSDSKD 575
Cdd:COG0666    259 AAAAGAALIVKLLLLALLLLAAALLDLL 286
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
217-820 6.51e-114

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 380.58  E-value: 6.51e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKeacKIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:COG1643     10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGG---RIGMLEPRRLAARAAAERMAEELGEPVGET 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILLRVLIG----KGVnssvpDIthIIVDEIHERDSYSDFMLMILRDLLPSN-PHLRL 371
Cdd:COG1643     87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRdpelEGV-----DT--VIFDEFHERSLNADLLLALLLDLQPALrPDLKL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  372 ILMSATLDAERFSEYFGGCPVVRVPGFTYPVRTFFLDDalsvlnsdknshllsavkrdfkDEDKVSLDEAIdlawtndef 451
Cdd:COG1643    160 LVMSATLDAERFARLLGDAPVIESSGRTYPVEVRYRPL----------------------PADERDLEDAV--------- 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  452 dclVDLVssegsheaynyqnsttgltplmvfagkgrvsdvckllsvgadctlkskegitalelaekenqfetAQIIREHA 531
Cdd:COG1643    209 ---ADAV-----------------------------------------------------------------REALAEEP 220
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  532 GNIqsnsqqaqdlldkymatikpeevdvglivklmkkicsdskdgaiLVFLPGWEEISKTKEkLLDDRFFAHsakFIILC 611
Cdd:COG1643    221 GDI--------------------------------------------LVFLPGEREIRRTAE-ALRGRLPPD---TEILP 252
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  612 LHSRVPAEEQKKVFNRPPRGCRKIVLATNIAESAVTIDDVVYVIDSGRMKEKSYDPYNDVSTLQSSWVSKANAKQRAGRA 691
Cdd:COG1643    253 LYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRA 332
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  692 GRCQAGICYHLYSKLRAASLPEYRVPEVMRmpVD--ELCLQVKML---DPncnvNDFlqKLMDPPVAQSIENALIILKDI 766
Cdd:COG1643    333 GRLAPGICYRLWSEEDFARRPAFTDPEILR--ADlaSLILELAAWglgDP----EDL--PFLDPPPARAIADARALLQEL 404
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1063680967  767 GALTPEEELTELGQKFGQLPVHPRISKMIYFAILVNCLDPALILACAADEKDPF 820
Cdd:COG1643    405 GALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR 458
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
233-395 4.72e-83

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: 268.94  E-value: 4.72e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  233 NQVVLIAGETGCGKTTQVPQYLLDHMWHsKKEACKIICTQPRRISAISVSDRISWERGETIGRTVGYKVRLQSEGGRESS 312
Cdd:cd17917      1 NQVVVIVGETGSGKTTQVPQFLLEDGLA-KGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  313 VVFCTNGILLRVLIGkgvNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLRLILMSATLDAERFSEYFGGCPV 392
Cdd:cd17917     80 IKFCTDGILLRELLS---DPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPV 156

                   ...
gi 1063680967  393 VRV 395
Cdd:cd17917    157 IHI 159
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
217-878 1.53e-71

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 263.84  E-value: 1.53e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDhMWHSKKEAckIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:PRK11131    73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE-LGRGVKGL--IGHTQPRRLAARTVANRIAEELETELGGC 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILL------RVLIgkgvnssvpDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLR 370
Cdd:PRK11131   150 VGYKVRFNDQVSDNTMVKLMTDGILLaeiqqdRLLM---------QYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLK 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  371 LILMSATLDAERFSEYFGGCPVVRVPGFTYPVRTFF---LDDAlsvlnsdknshllsavkrDFKDEDKVsldEAIdlawt 447
Cdd:PRK11131   221 VIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYrpiVEEA------------------DDTERDQL---QAI----- 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  448 ndeFDClVDLVSSEGSheaynyqnsttgltplmvfagkgrvsdvckllsvgadctlkskegitalelaekenqfetaqii 527
Cdd:PRK11131   275 ---FDA-VDELGREGP---------------------------------------------------------------- 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  528 rehagniqsnsqqaqdlldkymatikpeevdvglivklmkkicsdskdGAILVFLPGWEEISKTKEKlLDDRFFAHSAkf 607
Cdd:PRK11131   287 ------------------------------------------------GDILIFMSGEREIRDTADA-LNKLNLRHTE-- 315
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  608 iILCLHSRVPAEEQKKVFNrpPRGCRKIVLATNIAESAVTIDDVVYVIDSGRMKEKSYDPYNDVSTLQSSWVSKANAKQR 687
Cdd:PRK11131   316 -ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQR 392
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  688 AGRAGRCQAGICYHLYSKLRAASLPEYRVPEVMRMPVDELCLQVKMLDPNcNVNDFlqKLMDPPVAQSIENALIILKDIG 767
Cdd:PRK11131   393 KGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLG-DIAAF--PFVEAPDKRNIQDGVRLLEELG 469
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  768 ALTPEE-----ELTELGQKFGQLPVHPRISKMIYFAILVNCLDPALILACAADEKDPFTMPLspgDRKKAAAAKHElaSL 842
Cdd:PRK11131   470 AITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPM---DKQQASDEKHR--RF 544
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1063680967  843 YGDHSDHLATVAAF---QCWKNAKASGQAKEFCSKYFIS 878
Cdd:PRK11131   545 ADKESDFLAFVNLWnylQEQQKALSSNQFRRLCRTDYLN 583
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
217-813 4.58e-65

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: 238.13  E-value: 4.58e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVE-SNQVVLIAgETGCGKTTQVPQYLLDHmwhsKKEACKIICTQPRRISAISVSDRISWERGETIGR 295
Cdd:TIGR01970    1 LPIHAVLPALRDALAaHPQVVLEA-PPGAGKSTAVPLALLDA----PGIGGKIIMLEPRRLAARSAAQRLASQLGEAVGQ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  296 TVGYKVRLQSEGGRESSVVFCTNGILLRVLIGkgvNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPS-NPHLRLILM 374
Cdd:TIGR01970   76 TVGYRVRGENKVSRRTRLEVVTEGILTRMIQD---DPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAM 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  375 SATLDAERFSEYFGGCPVVRVPGFTYPVRTFFLddalsvlnsdknshllsAVKRDFKDEDKVSldeaidlawtndefDCL 454
Cdd:TIGR01970  153 SATLDGERLSSLLPDAPVVESEGRSFPVEIRYL-----------------PLRGDQRLEDAVS--------------RAV 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  455 VDLVSSEGsheaynyqnsttgltplmvfagkgrvsdvckllsvgadctlkskegitalelaekenqfetaqiirehagni 534
Cdd:TIGR01970  202 EHALASET------------------------------------------------------------------------ 209
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  535 qsnsqqaqdlldkymatikpeevdvglivklmkkicsdskdGAILVFLPGWEEISKTKEKLLDdrffAHSAKFIILCLHS 614
Cdd:TIGR01970  210 -----------------------------------------GSILVFLPGQAEIRRVQEQLAE----RLDSDVLICPLYG 244
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  615 RVPAEEQKKVFNRPPRGCRKIVLATNIAESAVTIDDVVYVIDSGRMKEKSYDPYNDVSTLQSSWVSKANAKQRAGRAGRC 694
Cdd:TIGR01970  245 ELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRL 324
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  695 QAGICYHLYSKLRAASLPEYRVPEVMRMPVDELCLQVKMLdpncNVNDFLQ-KLMDPPVAQSIENALIILKDIGALTPEE 773
Cdd:TIGR01970  325 EPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALELAQW----GAKDPSDlRWLDAPPSVALAAARQLLQRLGALDAQG 400
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 1063680967  774 ELTELGQKFGQLPVHPRISKMiyfaiLVNCLDPALI-LACA 813
Cdd:TIGR01970  401 RLTAHGKAMAALGCHPRLAAM-----LLSAHSTGLAaLACD 436
R3H_DEXH_helicase cd06007
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may ...
18-76 5.13e-26

R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may function as ATP-dependent DNA or RNA helicases. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100077  Cd Length: 59  Bit Score: 102.01  E-value: 5.13e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063680967   18 GAWATKVLEDFRASGNDSYVFEQQLTNSERGIIHQMCRTMGLRSKSNGSGEERRLSLFK 76
Cdd:cd06007      1 RIAINKALEDFRASDNEEYEFPSSLTNHERAVIHRLCRKLGLKSKSKGKGSNRRLSVYK 59
DEXDc smart00487
DEAD-like helicases superfamily;
223-401 5.39e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 107.19  E-value: 5.39e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967   223 RDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMwhSKKEACKIICTQPRRISAISVSDRISWERGETIGRTVGY--- 299
Cdd:smart00487   14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAL--KRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLygg 91
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967   300 ---KVRLQSEGGRESSVVFCTNGILLRVLIGKGVNSSvpDITHIIVDEIHERD--SYSDFMLMILRDLlpsNPHLRLILM 374
Cdd:smart00487   92 dskREQLRKLESGKTDILVTTPGRLLDLLENDKLSLS--NVDLVILDEAHRLLdgGFGDQLEKLLKLL---PKNVQLLLL 166
                           170       180
                    ....*....|....*....|....*....
gi 1063680967   375 SATL--DAERFSEYFGGCPVVRVPGFTYP 401
Cdd:smart00487  167 SATPpeEIENLLELFLNDPVFIDVGFTPL 195
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
759-851 4.54e-24

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: 98.08  E-value: 4.54e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  759 ALIILKDIGALTPEEELTELGQKFGQLPVHPRISKMIYFAILVNCLDPALILACAADEKDPFTMPLSPGDRKKAAAAK-- 836
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAARrr 80
                           90       100
                   ....*....|....*....|...
gi 1063680967  837 --------HELASLYGDHSDHLA 851
Cdd:pfam04408   81 rraadekaRAKFARLDLEGDHLT 103
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
919-1007 3.07e-10

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: 58.03  E-value: 3.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  919 LRAVIAVGLYPMLGRMCPLSKNRTRSVIetiaGAKVRVPSLSNNVdmSSTKFDEALIVFDEITRGDWgVVIRSCTVLPTI 998
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGKGYTTLSD----NQRVFIHPSSVLF--NEKTFPPEWVVYQELVETTK-VYIRTVTAISPE 73

                   ....*....
gi 1063680967  999 PVLLFSREI 1007
Cdd:pfam07717   74 WLLLFAPHI 82
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
25-76 2.24e-08

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 52.69  E-value: 2.24e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1063680967    25 LEDFRASGNDSYVFEQqLTNSERGIIHQMCRTMGLRSKSNGSGEERRLSLFK 76
Cdd:smart00393   28 IARFVKSTKESVELPP-MNSYERKIVHELAEKYGLESESFGEGPKRRVVISK 78
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
23-76 2.32e-07

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 49.03  E-value: 2.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1063680967   23 KVLEDFRASGNDSYVFEQqLTNSERGIIHQMCRTMGLRSKSNGSGEERRLSLFK 76
Cdd:pfam01424    8 EKLAEFVKDTGKSLELPP-MSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
468-575 2.24e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.11  E-value: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  468 NYQNSTtGLTPLMVFAGKGRVSDVCKLLSVGADCTLKSKEGITALELAEKENQFETAQIIREHAGNIQSNSQQAQDLLDK 547
Cdd:COG0666    180 NARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
                           90       100
                   ....*....|....*....|....*...
gi 1063680967  548 YMATIKPEEVDVGLIVKLMKKICSDSKD 575
Cdd:COG0666    259 AAAAGAALIVKLLLLALLLLAAALLDLL 286
Ank_5 pfam13857
Ankyrin repeats (many copies);
475-515 1.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.59e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1063680967  475 GLTPLMVFAGKGRVSDVCKLLSVGADCTLKSKEGITALELA 515
Cdd:pfam13857   16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
475-530 3.59e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 3.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063680967  475 GLTPLMVFAGKGRVSDVCKLLSVGADCTLKSKEGITALELAEKENQFETAQIIREH 530
Cdd:PTZ00322   115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
217-820 6.51e-114

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 380.58  E-value: 6.51e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKeacKIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:COG1643     10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGG---RIGMLEPRRLAARAAAERMAEELGEPVGET 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILLRVLIG----KGVnssvpDIthIIVDEIHERDSYSDFMLMILRDLLPSN-PHLRL 371
Cdd:COG1643     87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRdpelEGV-----DT--VIFDEFHERSLNADLLLALLLDLQPALrPDLKL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  372 ILMSATLDAERFSEYFGGCPVVRVPGFTYPVRTFFLDDalsvlnsdknshllsavkrdfkDEDKVSLDEAIdlawtndef 451
Cdd:COG1643    160 LVMSATLDAERFARLLGDAPVIESSGRTYPVEVRYRPL----------------------PADERDLEDAV--------- 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  452 dclVDLVssegsheaynyqnsttgltplmvfagkgrvsdvckllsvgadctlkskegitalelaekenqfetAQIIREHA 531
Cdd:COG1643    209 ---ADAV-----------------------------------------------------------------REALAEEP 220
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  532 GNIqsnsqqaqdlldkymatikpeevdvglivklmkkicsdskdgaiLVFLPGWEEISKTKEkLLDDRFFAHsakFIILC 611
Cdd:COG1643    221 GDI--------------------------------------------LVFLPGEREIRRTAE-ALRGRLPPD---TEILP 252
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  612 LHSRVPAEEQKKVFNRPPRGCRKIVLATNIAESAVTIDDVVYVIDSGRMKEKSYDPYNDVSTLQSSWVSKANAKQRAGRA 691
Cdd:COG1643    253 LYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRA 332
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  692 GRCQAGICYHLYSKLRAASLPEYRVPEVMRmpVD--ELCLQVKML---DPncnvNDFlqKLMDPPVAQSIENALIILKDI 766
Cdd:COG1643    333 GRLAPGICYRLWSEEDFARRPAFTDPEILR--ADlaSLILELAAWglgDP----EDL--PFLDPPPARAIADARALLQEL 404
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1063680967  767 GALTPEEELTELGQKFGQLPVHPRISKMIYFAILVNCLDPALILACAADEKDPF 820
Cdd:COG1643    405 GALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR 458
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
233-395 4.72e-83

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: 268.94  E-value: 4.72e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  233 NQVVLIAGETGCGKTTQVPQYLLDHMWHsKKEACKIICTQPRRISAISVSDRISWERGETIGRTVGYKVRLQSEGGRESS 312
Cdd:cd17917      1 NQVVVIVGETGSGKTTQVPQFLLEDGLA-KGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  313 VVFCTNGILLRVLIGkgvNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLRLILMSATLDAERFSEYFGGCPV 392
Cdd:cd17917     80 IKFCTDGILLRELLS---DPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPV 156

                   ...
gi 1063680967  393 VRV 395
Cdd:cd17917    157 IHI 159
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
549-703 8.23e-77

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: 251.68  E-value: 8.23e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  549 MATIKPEEVDVGLIVKLMKKICSDSKDGAILVFLPGWEEISKTKEKLLDDRFFAHSAKFIILCLHSRVPAEEQKKVFNRP 628
Cdd:cd18791     17 ISSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDLGKLLVLPLHSSLPPEEQQRVFEPP 96
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063680967  629 PRGCRKIVLATNIAESAVTIDDVVYVIDSGRMKEKSYDPYNDVSTLQSSWVSKANAKQRAGRAGRCQAGICYHLY 703
Cdd:cd18791     97 PPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
217-878 1.53e-71

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 263.84  E-value: 1.53e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDhMWHSKKEAckIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:PRK11131    73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE-LGRGVKGL--IGHTQPRRLAARTVANRIAEELETELGGC 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILL------RVLIgkgvnssvpDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLR 370
Cdd:PRK11131   150 VGYKVRFNDQVSDNTMVKLMTDGILLaeiqqdRLLM---------QYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLK 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  371 LILMSATLDAERFSEYFGGCPVVRVPGFTYPVRTFF---LDDAlsvlnsdknshllsavkrDFKDEDKVsldEAIdlawt 447
Cdd:PRK11131   221 VIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYrpiVEEA------------------DDTERDQL---QAI----- 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  448 ndeFDClVDLVSSEGSheaynyqnsttgltplmvfagkgrvsdvckllsvgadctlkskegitalelaekenqfetaqii 527
Cdd:PRK11131   275 ---FDA-VDELGREGP---------------------------------------------------------------- 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  528 rehagniqsnsqqaqdlldkymatikpeevdvglivklmkkicsdskdGAILVFLPGWEEISKTKEKlLDDRFFAHSAkf 607
Cdd:PRK11131   287 ------------------------------------------------GDILIFMSGEREIRDTADA-LNKLNLRHTE-- 315
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  608 iILCLHSRVPAEEQKKVFNrpPRGCRKIVLATNIAESAVTIDDVVYVIDSGRMKEKSYDPYNDVSTLQSSWVSKANAKQR 687
Cdd:PRK11131   316 -ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQR 392
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  688 AGRAGRCQAGICYHLYSKLRAASLPEYRVPEVMRMPVDELCLQVKMLDPNcNVNDFlqKLMDPPVAQSIENALIILKDIG 767
Cdd:PRK11131   393 KGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLG-DIAAF--PFVEAPDKRNIQDGVRLLEELG 469
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  768 ALTPEE-----ELTELGQKFGQLPVHPRISKMIYFAILVNCLDPALILACAADEKDPFTMPLspgDRKKAAAAKHElaSL 842
Cdd:PRK11131   470 AITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPM---DKQQASDEKHR--RF 544
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1063680967  843 YGDHSDHLATVAAF---QCWKNAKASGQAKEFCSKYFIS 878
Cdd:PRK11131   545 ADKESDFLAFVNLWnylQEQQKALSSNQFRRLCRTDYLN 583
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
180-395 1.83e-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: 236.27  E-value: 1.83e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  180 FKKPHMTKHDIENnvvSLSSRLKKERHFREIFEARSKLPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMW 259
Cdd:cd17972     25 FATPEQISMDLKN---ELMYQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFI 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  260 HSKKEA-CKIICTQPRRISAISVSDRISWERGETIGRTVGYKVRLQSEGGR-ESSVVFCTNGILLRVLigkgvNSSVPDI 337
Cdd:cd17972    102 QNDRAAeCNIVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRpHASILFCTVGVLLRKL-----EAGIRGI 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063680967  338 THIIVDEIHERDSYSDFMLMILRDLLPSNPHLRLILMSATLDAERFSEYFGGCPVVRV 395
Cdd:cd17972    177 SHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
217-395 2.35e-68

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


Pssm-ID: 350745 [Multi-domain]  Cd Length: 176  Bit Score: 227.79  E-value: 2.35e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMwHSKKEACKIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:cd17987      1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDC-YANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILLRVLIGKgvNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLRLILMSA 376
Cdd:cd17987     80 VGYQIRLESRVSPKTLLTFCTNGVLLRTLMAG--DSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSA 157
                          170
                   ....*....|....*....
gi 1063680967  377 TLDAERFSEYFGGCPVVRV 395
Cdd:cd17987    158 ALDVNLFIRYFGSCPVIYI 176
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
217-395 9.09e-68

DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an important role in the assembly of the mitochondrial large ribosomal subunit. DHX30 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350734 [Multi-domain]  Cd Length: 178  Bit Score: 226.21  E-value: 9.09e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKEA-CKIICTQPRRISAISVSDRISWERGETIGR 295
Cdd:cd17976      1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGArCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  296 TVGYKVRLQSE-GGRESSVVFCTNGILLRVLIGkgvNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLRLILM 374
Cdd:cd17976     81 NVGYQVRLESRpPPRGGALLFCTVGVLLKKLQS---NPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLM 157
                          170       180
                   ....*....|....*....|.
gi 1063680967  375 SATLDAERFSEYFGGCPVVRV 395
Cdd:cd17976    158 SATGDNQRLSRYFGGCPVVRV 178
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
217-395 6.51e-66

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: 220.87  E-value: 6.51e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLD-HMWHSKKEACKIICTQPRRISAISVSDRISWERGET--I 293
Cdd:cd17981      1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDdAIERGKGSSCRIVCTQPRRISAISVAERVAAERAEScgL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  294 GRTVGYKVRLQSEGGRE-SSVVFCTNGILLRVLIGkgvNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLRLI 372
Cdd:cd17981     81 GNSTGYQIRLESRKPRKqGSILYCTTGIVLQWLQS---DPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVI 157
                          170       180
                   ....*....|....*....|...
gi 1063680967  373 LMSATLDAERFSEYFGGCPVVRV 395
Cdd:cd17981    158 LMSATLNAEKFSDYFNNCPMIHI 180
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
217-813 4.58e-65

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: 238.13  E-value: 4.58e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVE-SNQVVLIAgETGCGKTTQVPQYLLDHmwhsKKEACKIICTQPRRISAISVSDRISWERGETIGR 295
Cdd:TIGR01970    1 LPIHAVLPALRDALAaHPQVVLEA-PPGAGKSTAVPLALLDA----PGIGGKIIMLEPRRLAARSAAQRLASQLGEAVGQ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  296 TVGYKVRLQSEGGRESSVVFCTNGILLRVLIGkgvNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPS-NPHLRLILM 374
Cdd:TIGR01970   76 TVGYRVRGENKVSRRTRLEVVTEGILTRMIQD---DPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAM 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  375 SATLDAERFSEYFGGCPVVRVPGFTYPVRTFFLddalsvlnsdknshllsAVKRDFKDEDKVSldeaidlawtndefDCL 454
Cdd:TIGR01970  153 SATLDGERLSSLLPDAPVVESEGRSFPVEIRYL-----------------PLRGDQRLEDAVS--------------RAV 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  455 VDLVSSEGsheaynyqnsttgltplmvfagkgrvsdvckllsvgadctlkskegitalelaekenqfetaqiirehagni 534
Cdd:TIGR01970  202 EHALASET------------------------------------------------------------------------ 209
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  535 qsnsqqaqdlldkymatikpeevdvglivklmkkicsdskdGAILVFLPGWEEISKTKEKLLDdrffAHSAKFIILCLHS 614
Cdd:TIGR01970  210 -----------------------------------------GSILVFLPGQAEIRRVQEQLAE----RLDSDVLICPLYG 244
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  615 RVPAEEQKKVFNRPPRGCRKIVLATNIAESAVTIDDVVYVIDSGRMKEKSYDPYNDVSTLQSSWVSKANAKQRAGRAGRC 694
Cdd:TIGR01970  245 ELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRL 324
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  695 QAGICYHLYSKLRAASLPEYRVPEVMRMPVDELCLQVKMLdpncNVNDFLQ-KLMDPPVAQSIENALIILKDIGALTPEE 773
Cdd:TIGR01970  325 EPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALELAQW----GAKDPSDlRWLDAPPSVALAAARQLLQRLGALDAQG 400
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 1063680967  774 ELTELGQKFGQLPVHPRISKMiyfaiLVNCLDPALI-LACA 813
Cdd:TIGR01970  401 RLTAHGKAMAALGCHPRLAAM-----LLSAHSTGLAaLACD 436
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
217-395 7.91e-63

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: 212.01  E-value: 7.91e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKEA-CKIICTQPRRISAISVSDRISWERGETIGR 295
Cdd:cd17985      1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPvANIICTQPRRISAISVAERVAQERAERVGQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  296 TVGYKVRLQSEGGRESSVVFCTNGILLRVLIGkgvNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLRLILMS 375
Cdd:cd17985     81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEG---DPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMS 157
                          170       180
                   ....*....|....*....|
gi 1063680967  376 ATLDAERFSEYFGGCPVVRV 395
Cdd:cd17985    158 ATLNAELFSDYFNSCPVIHI 177
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
217-399 9.66e-58

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: 197.34  E-value: 9.66e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKEaCKIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:cd17988      1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKY-CNIVVTQPRRIAAISIARRVSQEREWTLGSL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILLRVLIGkgvNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNP-HLRLILMS 375
Cdd:cd17988     80 VGYQVGLERPASEETRLIYCTTGVLLQKLIN---NKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSrHVKIILMS 156
                          170       180
                   ....*....|....*....|....
gi 1063680967  376 ATLDAERFSEYFgGCPVVRVPGFT 399
Cdd:cd17988    157 ATISCKEFADYF-TTPNNPAYVFE 179
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
217-395 2.13e-55

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: 190.35  E-value: 2.13e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSkkeackIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:cd17979      1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH------IACTQPRRIACISLAKRVAFESLNQYGSK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILLRVLigkGVNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLRLILMSA 376
Cdd:cd17979     75 VAYQIRFERTRTLATKLLFLTEGLLLRQI---QRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSA 151
                          170
                   ....*....|....*....
gi 1063680967  377 TLDAERFSEYFGGCPVVRV 395
Cdd:cd17979    152 TINIELFSGYFEGAPVVQV 170
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
217-395 7.70e-55

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: 189.36  E-value: 7.70e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKEA--CKIICTQPRRISAISVSDRISWERGETIG 294
Cdd:cd17975      1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLLNGGTAqkCNIVCTQPRRISAMSLATRVCEELGCESG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  295 -----RTVGYKVRLQSEGGRESSVVFCTNGILLRVLIGKGVNSSvpdITHIIVDEIHERDSYSDFMLMILRDLLPSNPHL 369
Cdd:cd17975     81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSS---ISHIIVDEVHERSVQSDFLLIILKEILHKRSDL 157
                          170       180
                   ....*....|....*....|....*.
gi 1063680967  370 RLILMSATLDAERFSEYFGGCPVVRV 395
Cdd:cd17975    158 HLILMSATVDCEKFSSYFTHCPILRI 183
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
215-798 6.43e-51

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 194.76  E-value: 6.43e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  215 SKLPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLdhmwHSKKEACKIICTQPRRISAISVSDRISWERGETIG 294
Cdd:PRK11664     2 SSLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLL----QHGGINGKIIMLEPRRLAARNVAQRLAEQLGEKPG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  295 RTVGYKVRLQSEGGRESSVVFCTNGILLRVLigkgvnSSVPDITHI---IVDEIHERDSYSDFMLMI-------LRDllp 364
Cdd:PRK11664    78 ETVGYRMRAESKVGPNTRLEVVTEGILTRMI------QRDPELSGVglvILDEFHERSLQADLALALlldvqqgLRD--- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  365 snpHLRLILMSATLDAERFSEYFGGCPVVRVPGFTYPVrtfflddalsvlnsdknshllsavkrdfkdedkvsldeaidl 444
Cdd:PRK11664   149 ---DLKLLIMSATLDNDRLQQLLPDAPVIVSEGRSFPV------------------------------------------ 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  445 awtndefdclvdlvssegsheAYNYQnsttgltPLmvfagkgrvsdvckllsvgadctlkskegitalelaekenqfeta 524
Cdd:PRK11664   184 ---------------------ERRYQ-------PL--------------------------------------------- 190
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  525 qiirehagniqsnsqQAQDLLDKYMATikpeevdvgLIVKLMKKicsdsKDGAILVFLPGWEEISKTKEkLLDDRFfahs 604
Cdd:PRK11664   191 ---------------PAHQRFDEAVAR---------ATAELLRQ-----ESGSLLLFLPGVGEIQRVQE-QLASRV---- 236
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  605 AKFIILC-LHSRVPAEEQKKVFNRPPRGCRKIVLATNIAESAVTIDDVVYVIDSGRMKEKSYDPYNDVSTLQSSWVSKAN 683
Cdd:PRK11664   237 ASDVLLCpLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQAS 316
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  684 AKQRAGRAGRCQAGICYHLYSKLRAASLPEYRVPEVMRmpvDELC-LQVKMLDPNCnvNDFLQ-KLMDPPVAQSIENALI 761
Cdd:PRK11664   317 MTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEPEILH---SDLSgLLLELLQWGC--HDPAQlSWLDQPPAAALAAAKR 391
                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 1063680967  762 ILKDIGALTPEEELTELGQKFGQLPVHPRISKMIYFA 798
Cdd:PRK11664   392 LLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAA 428
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
217-395 1.58e-49

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: 173.69  E-value: 1.58e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKeacKIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:cd17978      1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGG---MIGITQPRRVAAVSVAKRVAEEMGVELGQL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILLRVLIGkgvNSSVPDITHIIVDEIHERDSYSDFMLMILRD-----LLPSNPHLRL 371
Cdd:cd17978     78 VGYSVRFDDVTSEETRIKYMTDGMLLREAIG---DPLLSKYSVIILDEAHERTVHTDVLFGLVKSaqrrrKEQKLSPLKV 154
                          170       180
                   ....*....|....*....|....
gi 1063680967  372 ILMSATLDAERFSEYFGGCPVVRV 395
Cdd:cd17978    155 IIMSATLDADLFSEYFNGAPVLYI 178
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
212-396 2.14e-46

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: 164.96  E-value: 2.14e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  212 EARSKLPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKeacKIICTQPRRISAISVSDRISWERGE 291
Cdd:cd17971      1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRG---KIGCTQPRRVAAMSVAKRVAEEFGC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  292 TIGRTVGYKVRLQSEGGRESSVVFCTNGILLRVLIgkgVNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLRL 371
Cdd:cd17971     78 CLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECL---IDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKL 154
                          170       180
                   ....*....|....*....|....*
gi 1063680967  372 ILMSATLDAERFSEYFGGCPVVRVP 396
Cdd:cd17971    155 IVTSATLDAVKFSQYFYEAPIFTIP 179
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
217-395 2.27e-45

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: 161.90  E-value: 2.27e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWhsKKEACKIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:cd17974      1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGY--TKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGNE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILLRVLIGKgvnssvPDITH---IIVDEIHERDSYSDFMLMILRDLLPSNPHLRLIL 373
Cdd:cd17974     79 VGYSIRFEDCTSEKTVLKYMTDGMLLREFLTE------PDLASysvMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLI 152
                          170       180
                   ....*....|....*....|..
gi 1063680967  374 MSATLDAERFSEYFGGCPVVRV 395
Cdd:cd17974    153 SSATMDAEKFSAFFDDAPIFRI 174
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
217-395 4.31e-45

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: 160.70  E-value: 4.31e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHmwhSKKEACKIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:cd17989      1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLEL---GRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILLRVLigkGVNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLRLILMSA 376
Cdd:cd17989     78 VGYKVRFTDQTSDETCVKLMTDGILLAET---QTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSA 154
                          170
                   ....*....|....*....
gi 1063680967  377 TLDAERFSEYFGGCPVVRV 395
Cdd:cd17989    155 TIDAERFSRHFNNAPIIEV 173
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
204-395 7.01e-45

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: 160.66  E-value: 7.01e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  204 ERHFrEIFEARSKLPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWhSKKEACKIICTQPRRISAISVSD 283
Cdd:cd17973      1 QRYF-EILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDEL-PHQPKKLVACTQPRRVAAMSVAQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  284 RISWERGETIGRTVGYKVRLQSEGGRESSVVFCTNGILLRVLIgkgvnsSVPDITH---IIVDEIHERDSYSDFMLMILR 360
Cdd:cd17973     79 RVAEEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAM------SDPLLSRysvIILDEAHERTLATDILMGLLK 152
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1063680967  361 DLLPSNPHLRLILMSATLDAERFSEYFGGCPVVRV 395
Cdd:cd17973    153 EVVRRRPDLKLIVMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
217-395 2.58e-44

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: 158.65  E-value: 2.58e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVES-NQVVLIAgETGCGKTTQVPQYLLDHMWhskKEACKIICTQPRRISAISVSDRISWERGETIGR 295
Cdd:cd17990      1 LPIAAVLPALRAALDAgGQVVLEA-PPGAGKTTRVPLALLAELW---IAGGKIIVLEPRRVAARAAARRLATLLGEAPGE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  296 TVGYKVRLQSEGGRESSVVFCTNGILLRVLIGkgvNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPS-NPHLRLILM 374
Cdd:cd17990     77 TVGYRVRGESRVGRRTRVEVVTEGVLLRRLQR---DPELSGVGAVILDEFHERSLDADLALALLLEVQQLlRDDLRLLAM 153
                          170       180
                   ....*....|....*....|.
gi 1063680967  375 SATLDAERFSEYFGGCPVVRV 395
Cdd:cd17990    154 SATLDGDGLAALLPEAPVVES 174
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
217-387 5.98e-44

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: 158.02  E-value: 5.98e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKEAckIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:cd17980      1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRV--VGCTQPRRVAAVTVAGRVAEEMGAVLGHE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGR-ESSVVFCTNGILLRVLIgkgvnsSVPDITH---IIVDEIHERDSYSDFMLMILRDLLPSNPHLRLI 372
Cdd:cd17980     79 VGYCIRFDDCTDPqATRIKFLTDGMLVREMM------LDPLLTKysvIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLI 152
                          170
                   ....*....|....*
gi 1063680967  373 LMSATLDAERFSEYF 387
Cdd:cd17980    153 VASATLDAEKFRDFF 167
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
217-392 1.20e-41

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: 151.08  E-value: 1.20e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKeacKIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:cd17983      1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYG---MIGCTQPRRVAAMSVAKRVSEEMGVELGEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILLRVLIGkgvNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLRLILMSA 376
Cdd:cd17983     78 VGYAIRFEDCTSENTVIKYMTDGILLRESLR---DPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSA 154
                          170
                   ....*....|....*.
gi 1063680967  377 TLDAERFSEYFGGCPV 392
Cdd:cd17983    155 TMDADKFADFFGNVPI 170
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
217-395 3.07e-37

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: 138.45  E-value: 3.07e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWhskKEACKIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:cd17984      1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGF---SQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGSK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILLRVLIGKgvnssvPDITH---IIVDEIHERDSYSDFMLMILRDLLPSNP-----H 368
Cdd:cd17984     78 VGYQVRFDDCSSKETAIKYMTDGCLLRHILAD------PNLTKysvIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeH 151
                          170       180
                   ....*....|....*....|....*..
gi 1063680967  369 LRLILMSATLDAERFSEYFGGCPVVRV 395
Cdd:cd17984    152 LKVVVMSATLELAKLSAFFGNCPVFDI 178
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
217-385 1.03e-35

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: 134.79  E-value: 1.03e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKK--EACKIICTQPRRISAISVSDRISWERGeTIG 294
Cdd:cd17982      1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPEsdNPGMIGITQPRRVAAVSMAKRVAEELN-VFG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  295 RTVGYKVRLQSEGGRESSVVFCTNGILLR-----VLIGKgvnSSVpdithIIVDEIHERDSYSDFML------MILRDLL 363
Cdd:cd17982     80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKeiqtdFLLRK---YSV-----IIIDEAHERSVNTDILIgmlsriVPLRAKL 151
                          170       180
                   ....*....|....*....|....*.
gi 1063680967  364 PSNPH----LRLILMSATLDAERFSE 385
Cdd:cd17982    152 YLQDQtvkpLKLVIMSATLRVEDFTE 177
R3H_DEXH_helicase cd06007
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may ...
18-76 5.13e-26

R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may function as ATP-dependent DNA or RNA helicases. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100077  Cd Length: 59  Bit Score: 102.01  E-value: 5.13e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063680967   18 GAWATKVLEDFRASGNDSYVFEQQLTNSERGIIHQMCRTMGLRSKSNGSGEERRLSLFK 76
Cdd:cd06007      1 RIAINKALEDFRASDNEEYEFPSSLTNHERAVIHRLCRKLGLKSKSKGKGSNRRLSVYK 59
DEXDc smart00487
DEAD-like helicases superfamily;
223-401 5.39e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 107.19  E-value: 5.39e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967   223 RDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMwhSKKEACKIICTQPRRISAISVSDRISWERGETIGRTVGY--- 299
Cdd:smart00487   14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAL--KRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLygg 91
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967   300 ---KVRLQSEGGRESSVVFCTNGILLRVLIGKGVNSSvpDITHIIVDEIHERD--SYSDFMLMILRDLlpsNPHLRLILM 374
Cdd:smart00487   92 dskREQLRKLESGKTDILVTTPGRLLDLLENDKLSLS--NVDLVILDEAHRLLdgGFGDQLEKLLKLL---PKNVQLLLL 166
                           170       180
                    ....*....|....*....|....*....
gi 1063680967   375 SATL--DAERFSEYFGGCPVVRVPGFTYP 401
Cdd:smart00487  167 SATPpeEIENLLELFLNDPVFIDVGFTPL 195
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
217-395 1.98e-24

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


Pssm-ID: 350735 [Multi-domain]  Cd Length: 176  Bit Score: 101.83  E-value: 1.98e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKEACKIICTQPRRISAISVSDRISWERGETIGRT 296
Cdd:cd17977      1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNIGHE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGGRESSVVFCTNGILLRVLIgkgvnsSVPDITH---IIVDEIHERDSYSDFMLMILRDLLPSNPHLRLIL 373
Cdd:cd17977     81 VGYVIPFENCCTNETILRYCTDDMLLREMM------SDPLLESygvIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVI 154
                          170       180
                   ....*....|....*....|..
gi 1063680967  374 MSATLDAERFSEYFGGCPVVRV 395
Cdd:cd17977    155 ITCPHLSSKLLSYYGNVPLIEV 176
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
759-851 4.54e-24

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: 98.08  E-value: 4.54e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  759 ALIILKDIGALTPEEELTELGQKFGQLPVHPRISKMIYFAILVNCLDPALILACAADEKDPFTMPLSPGDRKKAAAAK-- 836
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAARrr 80
                           90       100
                   ....*....|....*....|...
gi 1063680967  837 --------HELASLYGDHSDHLA 851
Cdd:pfam04408   81 rraadekaRAKFARLDLEGDHLT 103
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
217-395 3.27e-21

DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 (DQX1) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350744 [Multi-domain]  Cd Length: 177  Bit Score: 92.65  E-value: 3.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  217 LPIASFRDAIISAVESNQ-VVLIAGETGCGKTTQVPQYLLDHMWHSKKEACKIICTQPRRISAISVSDRISWERGETIGR 295
Cdd:cd17986      1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEFALSRGFQKGQVTVTQPHPLAARSLALRVADEMDLNLGH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  296 TVGYKVRLQSEGGRESSVVFCTNGILLRVLigkgvnSSVPDITH---IIVDEIHERDSYSDFMLMILRDLLPSNPHLRLI 372
Cdd:cd17986     81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEM------TSTPLLGAwgvVVLDEAQERSVASDSLLGLLKDVRLQRPELRVV 154
                          170       180
                   ....*....|....*....|...
gi 1063680967  373 LMSATLDAERFSEYFGGCPVVRV 395
Cdd:cd17986    155 VVTSPALEPKLRAFWGNPPVVHV 177
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
766-851 6.79e-19

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: 82.70  E-value: 6.79e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967   766 IGALTPEEELTELGQKFGQLPVHPRISKMIYFAILVNCLDPALILACAADEKDPFtmplspgDRKKAAAAKHELASLYGD 845
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR-------PKEKREDADAARRRFADP 74

                    ....*.
gi 1063680967   846 HSDHLA 851
Cdd:smart00847   75 ESDHLT 80
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
563-693 2.38e-16

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: 76.10  E-value: 2.38e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  563 VKLMKKICSDSKDGAILVFLPGWEEisktkeklLDDRFFAHSAKFIILCLHSRVPAEEQKKVFNRPPRGCRKIVLATNIA 642
Cdd:pfam00271    3 LEALLELLKKERGGKVLIFSQTKKT--------LEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVA 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063680967  643 ESAVTIDDVVYVIDsgrmkeksYDPYNDVSTLqsswvskanaKQRAGRAGR 693
Cdd:pfam00271   75 ERGLDLPDVDLVIN--------YDLPWNPASY----------IQRIGRAGR 107
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
236-377 7.34e-15

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: 73.21  E-value: 7.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  236 VLIAGETGCGKTTQVPQYLLDHMwhsKKEACKIICTQPRRISAISVSDRISWERGETIgrTVGY------KVRLQSEGGR 309
Cdd:cd00046      4 VLITAPTGSGKTLAALLAALLLL---LKKGKKVLVLVPTKALALQTAERLRELFGPGI--RVAVlvggssAEEREKNKLG 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063680967  310 ESSVVFCTNGILLRvLIGKGVNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPH-LRLILMSAT 377
Cdd:cd00046     79 DADIIIATPDMLLN-LLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKnAQVILLSAT 146
HELICc smart00490
helicase superfamily c-terminal domain;
604-693 3.19e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.16  E-value: 3.19e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967   604 SAKFIILCLHSRVPAEEQKKVFNRPPRGCRKIVLATNIAESAVTIDDVVYVIDsgrmkeksYDPyndvstlqssWVSKAN 683
Cdd:smart00490    9 ELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVII--------YDL----------PWSPAS 70
                            90
                    ....*....|
gi 1063680967   684 AKQRAGRAGR 693
Cdd:smart00490   71 YIQRIGRAGR 80
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
215-442 2.19e-13

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 75.01  E-value: 2.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  215 SKLPIASFR----DAIISAVESNQVVLIAGETGCGKTTQVPQYLL---------------DHMWHSKKeackIICTQPRr 275
Cdd:PHA02653   157 SKIPLASLQpdvqLKIFEAWISRKPVVLTGGTGVGKTSQVPKLLLwfnylfggfdnldkiDPNFIERP----IVLSLPR- 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  276 ISAISVSdriswerGETIGRTVGYK------VRLQSEGGRESSV---------VFCTNgillRVLIGKGVNSSVpdithI 340
Cdd:PHA02653   232 VALVRLH-------SITLLKSLGFDeidgspISLKYGSIPDELIntnpkpyglVFSTH----KLTLNKLFDYGT-----V 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  341 IVDEIHERDSYSDFMLMILRDlLPSNPHlRLILMSATL--DAERFSEYFGGCPVVRVPGFT-YPVRTFFLDDALSVLNsd 417
Cdd:PHA02653   296 IIDEVHEHDQIGDIIIAVARK-HIDKIR-SLFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISEVYVKNKYNPKN-- 371
                          250       260
                   ....*....|....*....|....*
gi 1063680967  418 knshllsavKRDFKDEDKVSLDEAI 442
Cdd:PHA02653   372 ---------KRAYIEEEKKNIVTAL 387
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
225-381 5.58e-11

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: 62.65  E-value: 5.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  225 AIISAVESNQVVLIAGETGCGKTT--QVPqyLLDHMWHsKKEACKIICTQPRRISAISVSDRISwERGETIGRTV----- 297
Cdd:pfam00270    6 EAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDK-LDNGPQALVLAPTRELAEQIYEELK-KLGKGLGLKVasllg 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  298 GYKVRLQSEGGRESSVVFCTNGILLRVLIGKGVNSSVpdiTHIIVDEIHE--RDSYSDFMLMILRDLlpsNPHLRLILMS 375
Cdd:pfam00270   82 GDSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNL---KLLVLDEAHRllDMGFGPDLEEILRRL---PKKRQILLLS 155

                   ....*.
gi 1063680967  376 ATLDAE 381
Cdd:pfam00270  156 ATLPRN 161
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
919-1007 3.07e-10

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: 58.03  E-value: 3.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  919 LRAVIAVGLYPMLGRMCPLSKNRTRSVIetiaGAKVRVPSLSNNVdmSSTKFDEALIVFDEITRGDWgVVIRSCTVLPTI 998
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGKGYTTLSD----NQRVFIHPSSVLF--NEKTFPPEWVVYQELVETTK-VYIRTVTAISPE 73

                   ....*....
gi 1063680967  999 PVLLFSREI 1007
Cdd:pfam07717   74 WLLLFAPHI 82
R3H_NRF cd02640
R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB ...
23-76 3.94e-10

R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB proteins that can silence the IFNbeta promoter via binding to a negative regulatory element (NRE). Beside R3H NRF also contains a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100069  Cd Length: 60  Bit Score: 57.02  E-value: 3.94e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1063680967   23 KVLEDFRASGND-SYVFEQQLTNSERGIIHQMCRTMGLRSKSNGSGEERRLSLFK 76
Cdd:cd02640      6 QIIQNYAHSDDIrDMVFSPEFSKEERALIHQIAQKYGLKSRSYGSGNDRYLVISK 60
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
23-76 6.10e-09

R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100064  Cd Length: 59  Bit Score: 53.39  E-value: 6.10e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1063680967   23 KVLEDFRASGN-DSYVFEQqLTNSERGIIHQMCRTMGLRSKSNGSGEERRLSLFK 76
Cdd:cd02325      6 EELEAFAKDAAgKSLELPP-MNSYERKLIHDLAEYYGLKSESEGEGPNRRVVITK 59
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
25-76 2.24e-08

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 52.69  E-value: 2.24e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1063680967    25 LEDFRASGNDSYVFEQqLTNSERGIIHQMCRTMGLRSKSNGSGEERRLSLFK 76
Cdd:smart00393   28 IARFVKSTKESVELPP-MNSYERKIVHELAEKYGLESESFGEGPKRRVVISK 78
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
23-76 2.32e-07

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 49.03  E-value: 2.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1063680967   23 KVLEDFRASGNDSYVFEQqLTNSERGIIHQMCRTMGLRSKSNGSGEERRLSLFK 76
Cdd:pfam01424    8 EKLAEFVKDTGKSLELPP-MSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
223-388 2.57e-07

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 52.26  E-value: 2.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  223 RDAIISAVESNQVVLIAGETGCGKTTqVPQYLLDHMWhsKKEACKIICTQPRRisAIS------VSDRISWERGETIGRT 296
Cdd:cd17921      7 REALRALYLSGDSVLVSAPTSSGKTL-IAELAILRAL--ATSGGKAVYIAPTR--ALVnqkeadLRERFGPLGKNVGLLT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  297 VGYKVRLQSEGgrESSVVFCTNGILlRVLIGKGVNSSVPDITHIIVDEIHERDSYSDFMLM--ILRDLLPSNPHLRLILM 374
Cdd:cd17921     82 GDPSVNKLLLA--EADILVATPEKL-DLLLRNGGERLIQDVRLVVVDEAHLIGDGERGVVLelLLSRLLRINKNARFVGL 158
                          170
                   ....*....|....*
gi 1063680967  375 SATLD-AERFSEYFG 388
Cdd:cd17921    159 SATLPnAEDLAEWLG 173
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
468-575 2.24e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.11  E-value: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  468 NYQNSTtGLTPLMVFAGKGRVSDVCKLLSVGADCTLKSKEGITALELAEKENQFETAQIIREHAGNIQSNSQQAQDLLDK 547
Cdd:COG0666    180 NARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
                           90       100
                   ....*....|....*....|....*...
gi 1063680967  548 YMATIKPEEVDVGLIVKLMKKICSDSKD 575
Cdd:COG0666    259 AAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
407-610 1.26e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 45.72  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  407 LDDALSVLNSDKNSHLLSAVKRDFKDEDKVSLDEAIDLAWTNDEFDCLVDLVSSEGSHEAY----------NYQNSTtGL 476
Cdd:COG0666     76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVkllleagadvNAQDND-GN 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  477 TPLMVFAGKGRVSDVCKLLSVGADCTLKSKEGITALELAEKENQFETAQIIREHAGNIQSNSQQAQDLLDkyMATIKPEE 556
Cdd:COG0666    155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD--LAAENGNL 232
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1063680967  557 VDVGLIVKLMKKICSDSKDGAILVFLPGWEEISKTKEKLLDDRFFAHSAKFIIL 610
Cdd:COG0666    233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
Ank_5 pfam13857
Ankyrin repeats (many copies);
475-515 1.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.59e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1063680967  475 GLTPLMVFAGKGRVSDVCKLLSVGADCTLKSKEGITALELA 515
Cdd:pfam13857   16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
475-530 3.59e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 3.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063680967  475 GLTPLMVFAGKGRVSDVCKLLSVGADCTLKSKEGITALELAEKENQFETAQIIREH 530
Cdd:PTZ00322   115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
R3H_RRM cd02639
R3H domain of mainly fungal proteins which are associated with a RNA recognition motif (RRM) ...
34-76 6.89e-04

R3H domain of mainly fungal proteins which are associated with a RNA recognition motif (RRM) domain. Present in this group is the RNA-binding post-transcriptional regulator Cip2 (Csx1-interacting protein 2) involved in counteracting Csx1 function. Csx1 plays a central role in controlling gene expression during oxidative stress. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100068  Cd Length: 60  Bit Score: 39.20  E-value: 6.89e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1063680967   34 DSYVFEQQLTNSERGIIHQMCRTMGLRSKSNGSGEERRLSLFK 76
Cdd:cd02639     18 DELAFPSSLSPAERRIVHLLASRLGLNHVSDGTGERRQVQITK 60
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
407-534 1.05e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.02  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063680967  407 LDDALSVLNSDKNSHLLSAVKRDFKDEDKVSLDEAIDLAWTNDEFDCLVDLVSSEGSHEAYNYQNSTTGLTPLMVFAGKG 486
Cdd:COG0666     19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1063680967  487 RVSDVCKLLSVGADCTLKSKEGITALELAEKENQFETAQIIREHAGNI 534
Cdd:COG0666     99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146
Ank_2 pfam12796
Ankyrin repeats (3 copies);
470-537 1.14e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.71  E-value: 1.14e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063680967  470 QNSTTGLTPLMVFAGKGRVsDVCKLLSVGADCTLKSkEGITALELAEKENQFETAQIIREHAGNIQSN 537
Cdd:pfam12796   25 LQDKNGRTALHLAAKNGHL-EIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
 
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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