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Conserved domains on  [gi|2038246692|ref|XP_041424338|]
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ATP-dependent RNA helicase DDX25 isoform X1 [Xenopus laevis]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030634)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
65-293 0e+00

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


:

Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 507.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  65 HNVEVLQRDPTSPLFSVKSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 144
Cdd:cd18048     1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 145 RVDANKKYPQCICLSPTFELALQTGKVVEEMGKFCAGIEVIYALRGNRPGKGSRLEAQIVIGTPGTVLDWCFKLRLITVE 224
Cdd:cd18048    81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038246692 225 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 293
Cdd:cd18048   161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
297-433 5.63e-49

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 163.83  E-value: 5.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 297 IQQFYDQCENKEQKYSALCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKV 376
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038246692 377 LVTTNVCARGIDVEQVSIVVNFDLPVNVdgsvdfETYLHRIGRTGRFGKKGIAVSLI 433
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
65-293 0e+00

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 507.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  65 HNVEVLQRDPTSPLFSVKSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 144
Cdd:cd18048     1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 145 RVDANKKYPQCICLSPTFELALQTGKVVEEMGKFCAGIEVIYALRGNRPGKGSRLEAQIVIGTPGTVLDWCFKLRLITVE 224
Cdd:cd18048    81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038246692 225 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 293
Cdd:cd18048   161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
83-456 6.22e-113

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 339.05  E-value: 6.22e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  83 SFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAN-KKYPQCICLSPT 161
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 162 FELALQTGKVVEEMGKFCaGIEV--IY----------ALRGNrpgkgsrleAQIVIGTPGTVLDWcFKLRLITVENISVF 229
Cdd:COG0513    81 RELALQVAEELRKLAKYL-GLRVatVYggvsigrqirALKRG---------VDIVVATPGRLLDL-IERGALDLSGVETL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 230 VLDEADVMINvQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELTLKNIQQFYDQCeNKEQ 309
Cdd:COG0513   150 VLDEADRMLD-MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLV-DKRD 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 310 KYSALCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDV 389
Cdd:COG0513   228 KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDI 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038246692 390 EQVSIVVNFDLPvnvdgsVDFETYLHRIGRTGRFGKKGIAVSLIENFFVYMLKEIEDHFNTKITKLN 456
Cdd:COG0513   308 DDVSHVINYDLP------EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEE 368
PTZ00424 PTZ00424
helicase 45; Provisional
81-461 6.09e-98

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 300.20  E-value: 6.09e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  81 VKSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSP 160
Cdd:PTZ00424   27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 161 TFELALQTGKVVEEMGKFC--------AGIEVIYALRGNRPGkgsrleAQIVIGTPGTVLDWCFKlRLITVENISVFVLD 232
Cdd:PTZ00424  105 TRELAQQIQKVVLALGDYLkvrchacvGGTVVRDDINKLKAG------VHMVVGTPGRVYDMIDK-RHLRVDDLKLFILD 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 233 EADVMINvQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELTLKNIQQFYDQCENKEQKYS 312
Cdd:PTZ00424  178 EADEMLS-RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFD 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 313 ALCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRaDMIQR-FREGREKVLVTTNVCARGIDVEQ 391
Cdd:PTZ00424  257 TLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDR-DLIMReFRSGSTRVLITTDLLARGIDVQQ 335
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 392 VSIVVNFDLPVNVdgsvdfETYLHRIGRTGRFGKKGIAVSLIENFFVYMLKEIEDHFNTKItklNSMDMD 461
Cdd:PTZ00424  336 VSLVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQI---EEMPME 396
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
297-433 5.63e-49

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 163.83  E-value: 5.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 297 IQQFYDQCENKEQKYSALCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKV 376
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038246692 377 LVTTNVCARGIDVEQVSIVVNFDLPVNVdgsvdfETYLHRIGRTGRFGKKGIAVSLI 433
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
106-271 3.73e-37

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: 133.91  E-value: 3.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 106 SKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTFELALQTGKVVEEMGKFCaGIEVI 185
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 186 YALRGNRPGKGSRL--EAQIVIGTPGTVLDWCFKLRLItvENISVFVLDEADVMInVQGHSDHSVRVKRSMPKSCQMLLF 263
Cdd:pfam00270  78 SLLGGDSRKEQLEKlkGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154

                  ....*...
gi 2038246692 264 SATFEDSV 271
Cdd:pfam00270 155 SATLPRNL 162
DEXDc smart00487
DEAD-like helicases superfamily;
97-300 3.40e-35

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 129.92  E-value: 3.40e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692   97 IYAMGFNRPSKIQENALPMMLADPpQNLIAQSQSGTGKTAAFVLAMLSRVDaNKKYPQCICLSPTFELALQTGKVVEEMG 176
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  177 KFCAGIEVIYaLRGNRPGKGSRL----EAQIVIGTPGTVLDwCFKLRLITVENISVFVLDEADVMINvQGHSDHSVRVKR 252
Cdd:smart00487  79 PSLGLKVVGL-YGGDSKREQLRKlesgKTDILVTTPGRLLD-LLENDKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLK 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2038246692  253 SMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLkkEELTLKNIQQF 300
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
309-424 1.12e-27

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: 106.14  E-value: 1.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 309 QKYSALCNLYGVITIAQAIVFCQTRKIASwLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGID 388
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2038246692 389 VEQVSIVVNFDLPVNVdgsvdfETYLHRIGRTGRFG 424
Cdd:pfam00271  80 LPDVDLVINYDLPWNP------ASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
338-424 1.25e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.20  E-value: 1.25e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  338 WLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVVNFDLPVNVdgsvdfETYLHRI 417
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75

                   ....*..
gi 2038246692  418 GRTGRFG 424
Cdd:smart00490  76 GRAGRAG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
314-430 9.17e-09

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 57.82  E-value: 9.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 314 LCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYD--------RADMIQRFREGREKVLVTTNVCAR 385
Cdd:COG1111   344 LKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQASKEGdkgltqkeQIEILERFRAGEFNVLVATSVAEE 423
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2038246692 386 GIDVEQVSIVVNFDlpvNVDGSVDFEtylHRIGRTGRFGKKGIAV 430
Cdd:COG1111   424 GLDIPEVDLVIFYE---PVPSEIRSI---QRKGRTGRKREGRVVV 462
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
327-458 5.40e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 48.94  E-value: 5.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 327 IVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVVNFDLPVNVdg 406
Cdd:PRK11057  240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI-- 317
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038246692 407 svdfETYLHRIGRTGRFGKKGIAVSL------------IENFFVYMLKEIEDHfntkitKLNSM 458
Cdd:PRK11057  318 ----ESYYQETGRAGRDGLPAEAMLFydpadmawlrrcLEEKPAGQQQDIERH------KLNAM 371
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
65-293 0e+00

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 507.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  65 HNVEVLQRDPTSPLFSVKSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 144
Cdd:cd18048     1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 145 RVDANKKYPQCICLSPTFELALQTGKVVEEMGKFCAGIEVIYALRGNRPGKGSRLEAQIVIGTPGTVLDWCFKLRLITVE 224
Cdd:cd18048    81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038246692 225 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 293
Cdd:cd18048   161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
89-286 6.39e-122

DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 353.42  E-value: 6.39e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  89 LKNELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTFELALQT 168
Cdd:cd17963     1 LKPELLKGLYAMGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 169 GKVVEEMGKFCaGIEVIYALRGNRPGKGSRLEAQIVIGTPGTVLDWCFKlRLITVENISVFVLDEADVMINVQGHSDHSV 248
Cdd:cd17963    81 GEVVEKMGKFT-GVKVALAVPGNDVPRGKKITAQIVIGTPGTVLDWLKK-RQLDLKKIKILVLDEADVMLDTQGHGDQSI 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2038246692 249 RVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIK 286
Cdd:cd17963   159 RIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
82-286 9.54e-114

DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 333.23  E-value: 9.54e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  82 KSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPT 161
Cdd:cd18047     1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 162 FELALQTGKVVEEMGKFCAGIEVIYALRGNRPGKGSRLEAQIVIGTPGTVLDWCFKLRLITVENISVFVLDEADVMINVQ 241
Cdd:cd18047    81 YELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQ 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2038246692 242 GHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIK 286
Cdd:cd18047   161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
83-456 6.22e-113

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 339.05  E-value: 6.22e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  83 SFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAN-KKYPQCICLSPT 161
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 162 FELALQTGKVVEEMGKFCaGIEV--IY----------ALRGNrpgkgsrleAQIVIGTPGTVLDWcFKLRLITVENISVF 229
Cdd:COG0513    81 RELALQVAEELRKLAKYL-GLRVatVYggvsigrqirALKRG---------VDIVVATPGRLLDL-IERGALDLSGVETL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 230 VLDEADVMINvQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELTLKNIQQFYDQCeNKEQ 309
Cdd:COG0513   150 VLDEADRMLD-MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLV-DKRD 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 310 KYSALCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDV 389
Cdd:COG0513   228 KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDI 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038246692 390 EQVSIVVNFDLPvnvdgsVDFETYLHRIGRTGRFGKKGIAVSLIENFFVYMLKEIEDHFNTKITKLN 456
Cdd:COG0513   308 DDVSHVINYDLP------EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEE 368
PTZ00424 PTZ00424
helicase 45; Provisional
81-461 6.09e-98

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 300.20  E-value: 6.09e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  81 VKSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSP 160
Cdd:PTZ00424   27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 161 TFELALQTGKVVEEMGKFC--------AGIEVIYALRGNRPGkgsrleAQIVIGTPGTVLDWCFKlRLITVENISVFVLD 232
Cdd:PTZ00424  105 TRELAQQIQKVVLALGDYLkvrchacvGGTVVRDDINKLKAG------VHMVVGTPGRVYDMIDK-RHLRVDDLKLFILD 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 233 EADVMINvQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELTLKNIQQFYDQCENKEQKYS 312
Cdd:PTZ00424  178 EADEMLS-RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFD 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 313 ALCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRaDMIQR-FREGREKVLVTTNVCARGIDVEQ 391
Cdd:PTZ00424  257 TLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDR-DLIMReFRSGSTRVLITTDLLARGIDVQQ 335
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 392 VSIVVNFDLPVNVdgsvdfETYLHRIGRTGRFGKKGIAVSLIENFFVYMLKEIEDHFNTKItklNSMDMD 461
Cdd:PTZ00424  336 VSLVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQI---EEMPME 396
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
80-459 1.27e-75

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 244.33  E-value: 1.27e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  80 SVKSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLS 159
Cdd:PRK11776    2 SMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAG--KDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 160 PTFELALQTGKVVEEMGKFCAGIEVIyALRGN---RPGKGSrLE--AQIVIGTPGTVLDWCFKLRLiTVENISVFVLDEA 234
Cdd:PRK11776   80 PTRELADQVAKEIRRLARFIPNIKVL-TLCGGvpmGPQIDS-LEhgAHIIVGTPGRILDHLRKGTL-DLDALNTLVLDEA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 235 DVMINVqGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELTLKNIQQFYdQCENkEQKYSAL 314
Cdd:PRK11776  157 DRMLDM-GFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFY-EVSP-DERLPAL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 315 CNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSI 394
Cdd:PRK11776  234 QRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEA 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038246692 395 VVNFDLPvnvdgsVDFETYLHRIGRTGRFGKKGIAVSLIENFFVYMLKEIEDHFNTKIT--KLNSMD 459
Cdd:PRK11776  314 VINYELA------RDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNwePLPSLS 374
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
84-445 1.11e-74

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 241.00  E-value: 1.11e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  84 FEELHLKNELLRGIYAMGFNRPSKIQENALPmmLADPPQNLIAQSQSGTGKTAAFVLAMLSR-VDANKKY---PQCICLS 159
Cdd:PRK11192    3 FSELELDESLLEALQDKGYTRPTAIQAEAIP--PALDGRDVLGSAPTGTGKTAAFLLPALQHlLDFPRRKsgpPRILILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 160 PTFELALQTGKVVEEMGKF----CAGIE--VIY-----ALRGNRpgkgsrleaQIVIGTPGTVLDWcfklrlITVEN--- 225
Cdd:PRK11192   81 PTRELAMQVADQARELAKHthldIATITggVAYmnhaeVFSENQ---------DIVVATPGRLLQY------IKEENfdc 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 226 --ISVFVLDEADVMINVQGHSDhsvrVKRsMPKSC----QMLLFSATFE-DSVWAFAERIVPDPNIIKLKKEELTLKNIQ 298
Cdd:PRK11192  146 raVETLILDEADRMLDMGFAQD----IET-IAAETrwrkQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIH 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 299 QFYDQCENKEQKYSALCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLV 378
Cdd:PRK11192  221 QWYYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLV 300
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038246692 379 TTNVCARGIDVEQVSIVVNFDLPVNVDgsvdfeTYLHRIGRTGRFGKKGIAVSLIENFFVYMLKEIE 445
Cdd:PRK11192  301 ATDVAARGIDIDDVSHVINFDMPRSAD------TYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIE 361
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
83-445 1.13e-61

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 211.63  E-value: 1.13e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  83 SFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTF 162
Cdd:PRK11634    7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNG--RDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 163 ELALQTGKVVEEMGKFCAGIEVIYALRGNRPG---KGSRLEAQIVIGTPGTVLDWcFKLRLITVENISVFVLDEADVMIN 239
Cdd:PRK11634   85 ELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDvqlRALRQGPQIVVGTPGRLLDH-LKRGTLDLSKLSGLVLDEADEMLR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 240 VqGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELTLKNIQQFYDQCENKeQKYSALCNLYG 319
Cdd:PRK11634  164 M-GFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGM-RKNEALVRFLE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 320 VITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVVNFD 399
Cdd:PRK11634  242 AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYD 321
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2038246692 400 LPvnvdgsVDFETYLHRIGRTGRFGKKGIAVSLIENFFVYMLKEIE 445
Cdd:PRK11634  322 IP------MDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIE 361
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
84-453 3.54e-60

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 204.38  E-value: 3.54e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  84 FEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAN----KKY---PQCI 156
Cdd:PRK01297   89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAG--HDAIGRAQTGTGKTAAFLISIINQLLQTpppkERYmgePRAL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 157 CLSPTFELALQTGKVVEEMGKFcAGIEVIYALRGNRPGKGSR-LEAQ---IVIGTPGTVLDwcFKLR-LITVENISVFVL 231
Cdd:PRK01297  167 IIAPTRELVVQIAKDAAALTKY-TGLNVMTFVGGMDFDKQLKqLEARfcdILVATPGRLLD--FNQRgEVHLDMVEVMVL 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 232 DEADVMINVqGHSDHSVRVKRSMPKSC--QMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELTLKNIQQfYDQCENKEQ 309
Cdd:PRK01297  244 DEADRMLDM-GFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQ-HVYAVAGSD 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 310 KYSALCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDV 389
Cdd:PRK01297  322 KYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHI 401
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038246692 390 EQVSIVVNFDLPVNVDgsvdfeTYLHRIGRTGRFGKKGIAVSLIENFFVYMLKEIEDHFNTKIT 453
Cdd:PRK01297  402 DGISHVINFTLPEDPD------DYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIS 459
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
83-433 8.80e-56

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 191.95  E-value: 8.80e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  83 SFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQ------CI 156
Cdd:PRK10590    2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEG--RDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 157 CLSPTFELALQTGKVVEEMGKFC--------AGIEV---IYALRGNrpgkgsrleAQIVIGTPGTVLDWCFKlRLITVEN 225
Cdd:PRK10590   80 ILTPTRELAAQIGENVRDYSKYLnirslvvfGGVSInpqMMKLRGG---------VDVLVATPGRLLDLEHQ-NAVKLDQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 226 ISVFVLDEADVMINVqGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELTLKNIQQ---FYD 302
Cdd:PRK10590  150 VEILVLDEADRMLDM-GFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQhvhFVD 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 303 qcenKEQKYSALCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNV 382
Cdd:PRK10590  229 ----KKRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDI 304
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2038246692 383 CARGIDVEQVSIVVNFDLPvNVDgsvdfETYLHRIGRTGRFGKKGIAVSLI 433
Cdd:PRK10590  305 AARGLDIEELPHVVNYELP-NVP-----EDYVHRIGRTGRAAATGEALSLV 349
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
82-457 3.98e-54

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 186.72  E-value: 3.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  82 KSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLA----MLSRVDANKKY---PQ 154
Cdd:PRK04837    8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAG--RDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKvnqPR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 155 CICLSPTFELALQTGKVVEEMGKFCaGIEVIYALRGNRPGKGSR-LEAQ--IVIGTPGTVLDWcFKLRLITVENISVFVL 231
Cdd:PRK04837   86 ALIMAPTRELAVQIHADAEPLAQAT-GLKLGLAYGGDGYDKQLKvLESGvdILIGTTGRLIDY-AKQNHINLGAIQVVVL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 232 DEADVMINVQGHSDhsVR-VKRSMPKSCQML--LFSATFEDSVWAFAERIVPDPNIIKLKKEELTLKNIQQ--FYdqcEN 306
Cdd:PRK04837  164 DEADRMFDLGFIKD--IRwLFRRMPPANQRLnmLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFY---PS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 307 KEQKYSALCNLYGVITIAQAIVFCQTR----KIASWLSQklsdDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNV 382
Cdd:PRK04837  239 NEEKMRLLQTLIEEEWPDRAIIFANTKhrceEIWGHLAA----DGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDV 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038246692 383 CARGIDVEQVSIVVNFDLPvnvDgsvDFETYLHRIGRTGRFGKKGIAVSLIENFFVYMLKEIEDHFNTKI--TKLNS 457
Cdd:PRK04837  315 AARGLHIPAVTHVFNYDLP---D---DCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIpvSKYDS 385
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
77-452 9.02e-54

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 189.39  E-value: 9.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  77 PLFSVkSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLadPPQNLIAQSQSGTGKTAAFVLAMLSR-------VDAN 149
Cdd:PRK04537    5 PLTDL-TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVAL--PGGDVAGQAQTGTGKTLAFLVAVMNRllsrpalADRK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 150 KKYPQCICLSPTFELALQTGKvveEMGKFCAGIEVIYAL--RGNRPGKGSRLEAQ---IVIGTPGTVLDWCFKLRLITVE 224
Cdd:PRK04537   82 PEDPRALILAPTRELAIQIHK---DAVKFGADLGLRFALvyGGVDYDKQRELLQQgvdVIIATPGRLIDYVKQHKVVSLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 225 NISVFVLDEADVMINVQGHSDhsVR-VKRSMPKSC--QMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELTLKNIQQ-F 300
Cdd:PRK04537  159 ACEICVLDEADRMFDLGFIKD--IRfLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQrI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 301 YDQCEnkEQKYSALCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTT 380
Cdd:PRK04537  237 YFPAD--EEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVAT 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038246692 381 NVCARGIDVEQVSIVVNFDLPvnvdgsVDFETYLHRIGRTGRFGKKGIAVSLIENFFVYMLKEIEDHFNTKI 452
Cdd:PRK04537  315 DVAARGLHIDGVKYVYNYDLP------FDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKI 380
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
297-433 5.63e-49

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 163.83  E-value: 5.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 297 IQQFYDQCENKEQKYSALCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKV 376
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038246692 377 LVTTNVCARGIDVEQVSIVVNFDLPVNVdgsvdfETYLHRIGRTGRFGKKGIAVSLI 433
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
93-286 1.12e-48

DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 165.31  E-value: 1.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANK----KYPQCICLSPTFELALQT 168
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSG--RDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 169 GKVVEEMGKFCaGIEVIyALRGNRPGK--GSRLE--AQIVIGTPGTVLDwCFKLRLITVENISVFVLDEADVMINvQGHS 244
Cdd:cd00268    79 AEVARKLGKGT-GLKVA-AIYGGAPIKkqIEALKkgPDIVVGTPGRLLD-LIERGKLDLSNVKYLVLDEADRMLD-MGFE 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2038246692 245 DHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIK 286
Cdd:cd00268   155 EDVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
84-282 6.54e-48

DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 163.62  E-value: 6.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  84 FEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTFE 163
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSG--RDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 164 LALQTGKVVEEMGKFCaGIEVIyALRGNRPGKGS--RLEA--QIVIGTPGTVLDwCFKLRLITVENISVFVLDEADVMIN 239
Cdd:cd17940    79 LALQTSQVCKELGKHM-GVKVM-VTTGGTSLRDDimRLYQtvHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLS 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2038246692 240 vQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDP 282
Cdd:cd17940   156 -QDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
86-285 1.32e-44

DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 154.79  E-value: 1.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  86 ELHLKNELLRGIYAMGFNRPSKIQENA-LPMMLAdppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTFEL 164
Cdd:cd17939     1 DMGLSEDLLRGIYAYGFEKPSAIQQRAiVPIIKG---RDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTREL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 165 ALQTGKVVEEMGKFcAGIEVIYALRGNRPG---KGSRLEAQIVIGTPGTVLDwCFKLRLITVENISVFVLDEADVMINvQ 241
Cdd:cd17939    78 AQQIQKVVKALGDY-MGVKVHACIGGTSVRedrRKLQYGPHIVVGTPGRVFD-MLQRRSLRTDKIKMFVLDEADEMLS-R 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2038246692 242 GHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNII 285
Cdd:cd17939   155 GFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
84-282 1.26e-42

DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 149.52  E-value: 1.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  84 FEELHLKNELLRGIYAMGFNRPSKIQENA-LPMMLAdppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTF 162
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAiMPCIKG---YDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 163 ELALQTGKVVEEMGKFCaGIEVIYALRGNR---PGKGSRLEAQIVIGTPGTVLDWCFKlRLITVENISVFVLDEADVMIN 239
Cdd:cd18046    78 ELAQQIQKVVMALGDYM-GIKCHACIGGTSvrdDAQKLQAGPHIVVGTPGRVFDMINR-RYLRTDYIKMFVLDEADEMLS 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2038246692 240 vQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDP 282
Cdd:cd18046   156 -RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
40-435 5.06e-42

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 156.10  E-value: 5.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  40 KGKSEDLANHSLLnkLLRRTLvdsphNVEVLQRDPTSPLFSvksFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLAD 119
Cdd:PLN00206   89 PGSTSGLSSSQAE--LLRRKL-----EIHVKGEAVPPPILS---FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSG 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 120 ppQNLIAQSQSGTGKTAAFVLAMLSRV-------DANKKYPQCICLSPTFELALQtgkvVEEMGKFCA-GIEVIYAL--R 189
Cdd:PLN00206  159 --RSLLVSADTGSGKTASFLVPIISRCctirsghPSEQRNPLAMVLTPTRELCVQ----VEDQAKVLGkGLPFKTALvvG 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 190 GN-RPGKGSRLE--AQIVIGTPGTVLDWCFKlRLITVENISVFVLDEADVMINvQGHSDHSVRVKRSMPKScQMLLFSAT 266
Cdd:PLN00206  233 GDaMPQQLYRIQqgVELIVGTPGRLIDLLSK-HDIELDNVSVLVLDEVDCMLE-RGFRDQVMQIFQALSQP-QVLLFSAT 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 267 FEDSVWAFAERIVPDPNIIKLKKEELTLKNIQQ--FYDQCENKEQKysalcnLYGVITIAQ-----AIVFCQTRKIASWL 339
Cdd:PLN00206  310 VSPEVEKFASSLAKDIILISIGNPNRPNKAVKQlaIWVETKQKKQK------LFDILKSKQhfkppAVVFVSSRLGADLL 383
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 340 SQKLS-DDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVVNFDLPVNVdgsvdfETYLHRIG 418
Cdd:PLN00206  384 ANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTI------KEYIHQIG 457
                         410
                  ....*....|....*..
gi 2038246692 419 RTGRFGKKGIAVSLIEN 435
Cdd:PLN00206  458 RASRMGEKGTAIVFVNE 474
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
84-285 6.49e-41

DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 144.92  E-value: 6.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  84 FEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTFE 163
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKG--RDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 164 LALQTGKVVEEMGKFcAGIEVIYALRGNRPGKG-SRLE--AQIVIGTPGTVLDwCFKLRLITVENISVFVLDEADVMINv 240
Cdd:cd18045    79 LAVQIQKVLLALGDY-MNVQCHACIGGTSVGDDiRKLDygQHIVSGTPGRVFD-MIRRRSLRTRHIKMLVLDEADEMLN- 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2038246692 241 QGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNII 285
Cdd:cd18045   156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
PTZ00110 PTZ00110
helicase; Provisional
13-467 2.24e-38

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 146.46  E-value: 2.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  13 GSQAELLDFQNNNVVA-EGKLDFEHGTLKGKSEDLANHsllnklLRRTlvdspHNVEVLQ-RDPTSPlfsVKSFEELHLK 90
Cdd:PTZ00110   73 GKRLQPIDWKSINLVPfEKNFYKEHPEVSALSSKEVDE------IRKE-----KEITIIAgENVPKP---VVSFEYTSFP 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  91 NELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDA--NKKY---PQCICLSPTFELA 165
Cdd:PTZ00110  139 DYILKSLKNAGFTEPTPIQVQGWPIALSG--RDMIGIAETGSGKTLAFLLPAIVHINAqpLLRYgdgPIVLVLAPTRELA 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 166 LQtgkVVEEMGKFCAGIE----VIYalrGNRPGKGSRLE----AQIVIGTPGTVLDW----CFKLRLITVenisvFVLDE 233
Cdd:PTZ00110  217 EQ---IREQCNKFGASSKirntVAY---GGVPKRGQIYAlrrgVEILIACPGRLIDFlesnVTNLRRVTY-----LVLDE 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 234 ADVMINVQGHSDHSVRVKRSMPKScQMLLFSATFEDSVWAFAErivpdpniiKLKKEE--------LTLK---NIQQFYD 302
Cdd:PTZ00110  286 ADRMLDMGFEPQIRKIVSQIRPDR-QTLMWSATWPKEVQSLAR---------DLCKEEpvhvnvgsLDLTachNIKQEVF 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 303 QCENKEQKySALCNLYGVITI--AQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTT 380
Cdd:PTZ00110  356 VVEEHEKR-GKLKMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIAT 434
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 381 NVCARGIDVEQVSIVVNFDLPVNVdgsvdfETYLHRIGRTGRFGKKGIAVSL-------IENFFVYMLKEIEDHFNTKIT 453
Cdd:PTZ00110  435 DVASRGLDVKDVKYVINFDFPNQI------EDYVHRIGRTGRAGAKGASYTFltpdkyrLARDLVKVLREAKQPVPPELE 508
                         490
                  ....*....|....*
gi 2038246692 454 KL-NSMDMDEMGKIW 467
Cdd:PTZ00110  509 KLsNERSNGTERRRW 523
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
106-271 3.73e-37

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: 133.91  E-value: 3.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 106 SKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTFELALQTGKVVEEMGKFCaGIEVI 185
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 186 YALRGNRPGKGSRL--EAQIVIGTPGTVLDWCFKLRLItvENISVFVLDEADVMInVQGHSDHSVRVKRSMPKSCQMLLF 263
Cdd:pfam00270  78 SLLGGDSRKEQLEKlkGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154

                  ....*...
gi 2038246692 264 SATFEDSV 271
Cdd:pfam00270 155 SATLPRNL 162
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
83-286 2.27e-36

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 133.20  E-value: 2.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  83 SFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLAdpPQNLIAQSQSGTGKTAAFVLAMLSRVDAN--KKYPQCICLSP 160
Cdd:cd17959     2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILD--GRDVVAMARTGSGKTAAFLIPMIEKLKAHspTVGARALILSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 161 TFELALQTGKVVEEMGKFcAGIEVIyALRGnrpgkGSRLEAQ---------IVIGTPGTVLDWC--FKLRLITVENIsvf 229
Cdd:cd17959    80 TRELALQTLKVTKELGKF-TDLRTA-LLVG-----GDSLEEQfealasnpdIIIATPGRLLHLLveMNLKLSSVEYV--- 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038246692 230 VLDEADVMINVqGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIK 286
Cdd:cd17959   150 VFDEADRLFEM-GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
93-286 2.98e-36

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 132.39  E-value: 2.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTFELALQTGKVV 172
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAG--HDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 173 EEMGKFCAGIEVIYaLRGNRPGKGSRLEA---QIVIGTPGTVLDwCFKLRLITVENISVFVLDEADVMinVQGHSDHSVR 249
Cdd:cd17943    79 KKIGKKLEGLKCEV-FIGGTPVKEDKKKLkgcHIAVGTPGRIKQ-LIELGALNVSHVRLFVLDEADKL--MEGSFQKDVN 154
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2038246692 250 V-KRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIK 286
Cdd:cd17943   155 WiFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEXDc smart00487
DEAD-like helicases superfamily;
97-300 3.40e-35

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 129.92  E-value: 3.40e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692   97 IYAMGFNRPSKIQENALPMMLADPpQNLIAQSQSGTGKTAAFVLAMLSRVDaNKKYPQCICLSPTFELALQTGKVVEEMG 176
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  177 KFCAGIEVIYaLRGNRPGKGSRL----EAQIVIGTPGTVLDwCFKLRLITVENISVFVLDEADVMINvQGHSDHSVRVKR 252
Cdd:smart00487  79 PSLGLKVVGL-YGGDSKREQLRKlesgKTDILVTTPGRLLD-LLENDKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLK 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2038246692  253 SMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLkkEELTLKNIQQF 300
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
93-271 1.38e-32

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 122.36  E-value: 1.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV---DANKKYPQCICLSPTFELALQTG 169
Cdd:cd17947     1 LLRALSSLGFTKPTPIQAAAIPLALLG--KDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 170 KVVEEMGKFCaGIEVIYALrgnrpgKGSRLEAQ---------IVIGTPGTVLDWCFKLRLITVENISVFVLDEADVMINV 240
Cdd:cd17947    79 SVLQQLAQFT-DITFALAV------GGLSLKAQeaalrarpdIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEE 151
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2038246692 241 qGHSDHSVRVKRSMPKSCQMLLFSATFEDSV 271
Cdd:cd17947   152 -GFADELKEILRLCPRTRQTMLFSATMTDEV 181
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
89-287 2.59e-31

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 119.23  E-value: 2.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  89 LKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV------DANKKYPQCICLSPTF 162
Cdd:cd17961     1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEG--KDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 163 ELALQTGKVVEEMGKFC------------AGIEVIYALRGNRPgkgsrleaQIVIGTPGTVLDWCFKLRLITVENISVFV 230
Cdd:cd17961    79 ELAQQVSKVLEQLTAYCrkdvrvvnlsasSSDSVQRALLAEKP--------DIVVSTPARLLSHLESGSLLLLSTLKYLV 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038246692 231 LDEADVMINVqGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKL 287
Cdd:cd17961   151 IDEADLVLSY-GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
83-267 2.19e-29

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 114.51  E-value: 2.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  83 SFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV----------DANKKY 152
Cdd:cd17967     1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPIISKLledgppsvgrGRRKAY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 153 PQCICLSPTFELALQtgkVVEEMGKFCAG----IEVIYalrGNRPGKGSRLEAQ----IVIGTPGTVLDWCFKLRlITVE 224
Cdd:cd17967    79 PSALILAPTRELAIQ---IYEEARKFSYRsgvrSVVVY---GGADVVHQQLQLLrgcdILVATPGRLVDFIERGR-ISLS 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2038246692 225 NISVFVLDEADVMIN----------VQgHSDhsvrvkrsMPK--SCQMLLFSATF 267
Cdd:cd17967   152 SIKFLVLDEADRMLDmgfepqirkiVE-HPD--------MPPkgERQTLMFSATF 197
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
67-271 3.78e-29

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 115.06  E-value: 3.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  67 VEVLQRDPTSPlfsVKSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR- 145
Cdd:cd18052    31 VEVTGRNPPPA---ILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPVLTGm 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 146 ----VDA----NKKYPQCICLSPTFELALQTGKvveEMGKFC-----------AGIEVIYALRGNRPGkgsrleAQIVIG 206
Cdd:cd18052   106 mkegLTAssfsEVQEPQALIVAPTRELANQIFL---EARKFSygtcirpvvvyGGVSVGHQIRQIEKG------CHILVA 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038246692 207 TPGTVLDWcFKLRLITVENISVFVLDEADVMINVQGHSD-HSVRVKRSMP--KSCQMLLFSATFEDSV 271
Cdd:cd18052   177 TPGRLLDF-IGRGKISLSKLKYLILDEADRMLDMGFGPEiRKLVSEPGMPskEDRQTLMFSATFPEEI 243
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
83-282 6.42e-29

DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 112.82  E-value: 6.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  83 SFEELHLKNELLRGIYAMGFNRPSKIQENALP--MMLADppqnLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSP 160
Cdd:cd17950     3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPqaILGMD----VLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 161 TFELALQTGKVVEEMGKFCAGI--EVIYalrGNRPGKGSR--LEA---QIVIGTPGTVLDwCFKLRLITVENISVFVLDE 233
Cdd:cd17950    79 TRELAFQISNEYERFSKYMPNVktAVFF---GGVPIKKDIevLKNkcpHIVVGTPGRILA-LVREKKLKLSHVKHFVLDE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2038246692 234 ADVMI-------NVQghsdhsvRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDP 282
Cdd:cd17950   155 CDKMLeqldmrrDVQ-------EIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDP 203
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
309-424 1.12e-27

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: 106.14  E-value: 1.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 309 QKYSALCNLYGVITIAQAIVFCQTRKIASwLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGID 388
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2038246692 389 VEQVSIVVNFDLPVNVdgsvdfETYLHRIGRTGRFG 424
Cdd:pfam00271  80 LPDVDLVINYDLPWNP------ASYIQRIGRAGRAG 109
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
83-271 3.65e-27

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 107.79  E-value: 3.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  83 SFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTF 162
Cdd:cd17954     1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQG--RDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 163 ELALQTGKVVEEMGkfcAGIEVIYA-LRGnrpgkGSRLEAQ---------IVIGTPGTVLDWC-----FKLRlitveNIS 227
Cdd:cd17954    79 ELAQQISEQFEALG---SSIGLKSAvLVG-----GMDMMAQaialakkphVIVATPGRLVDHLentkgFSLK-----SLK 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2038246692 228 VFVLDEADVMINVqghsDHSVRVKR---SMPKSCQMLLFSATFEDSV 271
Cdd:cd17954   146 FLVMDEADRLLNM----DFEPEIDKilkVIPRERTTYLFSATMTTKV 188
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
93-285 9.42e-26

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 103.78  E-value: 9.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTFELALQTGKVV 172
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLG--RDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 173 EEMGKFCAGIEVIYALRGN-RPGKGSRLE--AQIVIGTPGTVLDwCFKLRLITVENISVFVLDEADVMINvQGHSDHSVR 249
Cdd:cd17962    79 KELMKGLPPMKTALLVGGLpLPPQLYRLQqgVKVIIATPGRLLD-ILKQSSVELDNIKIVVVDEADTMLK-MGFQQQVLD 156
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2038246692 250 VKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNII 285
Cdd:cd17962   157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
84-282 3.54e-25

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 102.30  E-value: 3.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  84 FEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTFE 163
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAG--RDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 164 LALQTGKVVEEMGKfCAGIEVIYALRG-----------NRPgkgsrleaQIVIGTPGTVLD---------WCFKlrlitv 223
Cdd:cd17955    79 LAYQIAEQFRALGA-PLGLRCCVIVGGmdmvkqalelsKRP--------HIVVATPGRLADhlrssddttKVLS------ 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038246692 224 eNISVFVLDEADVMINVQGHSDHSVrVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDP 282
Cdd:cd17955   144 -RVKFLVLDEADRLLTGSFEDDLAT-ILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
84-282 2.30e-24

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 100.09  E-value: 2.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  84 FEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVdankkypQCICLSPTFE 163
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGG--GDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 164 LALQTGKVVEEMGKFCAGIEVIYALR-GNRPGKG--SRLEA--QIVIGTPGTVLDWcFKLRLITVENISVFVLDEADVMI 238
Cdd:cd17938    72 LAEQTYNCIENFKKYLDNPKLRVALLiGGVKAREqlKRLESgvDIVVGTPGRLEDL-IKTGKLDLSSVRFFVLDEADRLL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2038246692 239 NvQGHSDHSVRVKRSMPKSC------QMLLFSATFE-DSVWAFAERIVPDP 282
Cdd:cd17938   151 S-QGNLETINRIYNRIPKITsdgkrlQVIVCSATLHsFEVKKLADKIMHFP 200
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
89-275 8.14e-24

DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 98.81  E-value: 8.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  89 LKNELLRGIYAMGFNRPSKIQENALPMMLAdPPQNLIAQSQSGTGKTAAFVL----AMLSRVDANKKYP-QCICLSPTFE 163
Cdd:cd17964     1 LDPSLLKALTRMGFETMTPVQQKTLKPILS-TGDDVLARAKTGTGKTLAFLLpaiqSLLNTKPAGRRSGvSALIISPTRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 164 LALQTGKVVEEMGKFCAGIEVIYALRGNRPGKG----SRLEAQIVIGTPGTVLDwcfKLR----LITVENISVFVLDEAD 235
Cdd:cd17964    80 LALQIAAEAKKLLQGLRKLRVQSAVGGTSRRAElnrlRRGRPDILVATPGRLID---HLEnpgvAKAFTDLDYLVLDEAD 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2038246692 236 VMINvQGHSDHSVRVKRSMPKSC----QMLLFSATFEDSVWAFA 275
Cdd:cd17964   157 RLLD-MGFRPDLEQILRHLPEKNadprQTLLFSATVPDEVQQIA 199
HELICc smart00490
helicase superfamily c-terminal domain;
338-424 1.25e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.20  E-value: 1.25e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  338 WLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVVNFDLPVNVdgsvdfETYLHRI 417
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75

                   ....*..
gi 2038246692  418 GRTGRFG 424
Cdd:smart00490  76 GRAGRAG 82
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
93-271 6.88e-23

DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 96.11  E-value: 6.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV-----DANKKYPQCICLSPTFELALQ 167
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSN--KDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 168 TGKVVEEMGKF-CAGIEVIYALRGNRPGKG----SRLEAQIVIGTPGTVLD-WCFKLRLITVENISVFVLDEADVMINVq 241
Cdd:cd17960    79 IYEVLQSFLEHhLPKLKCQLLIGGTNVEEDvkkfKRNGPNILVGTPGRLEElLSRKADKVKVKSLEVLVLDEADRLLDL- 157
                         170       180       190
                  ....*....|....*....|....*....|
gi 2038246692 242 GHSDHSVRVKRSMPKSCQMLLFSATFEDSV 271
Cdd:cd17960   158 GFEADLNRILSKLPKQRRTGLFSATQTDAV 187
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
93-285 1.86e-22

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 95.46  E-value: 1.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLAdpPQNLIAQSQSGTGKTAAFVLAMLSRVDANKKY--------PQCICLSPTFEL 164
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQ--NRDIIGIAETGSGKTAAFLIPLLVYISRLPPLdeetkddgPYALILAPTREL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 165 ALQtgkVVEEMGKFCA--GIEVIYALRG-NRPGKGSRLE--AQIVIGTPGTVLDwCFKLRLITVENISVFVLDEADVMIN 239
Cdd:cd17945    79 AQQ---IEEETQKFAKplGIRVVSIVGGhSIEEQAFSLRngCEILIATPGRLLD-CLERRLLVLNQCTYVVLDEADRMID 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038246692 240 vQGHSDHSVRVKRSMPKSC--------------------QMLLFSATFEDSVWAFAERIVPDPNII 285
Cdd:cd17945   155 -MGFEPQVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
93-282 2.12e-22

DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 94.40  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKY-----PQCICLSPTFELALQ 167
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSG--RDMIGIAKTGSGKTAAFIWPMLVHIMDQRELekgegPIAVIVAPTRELAQQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 168 tgkVVEEMGKFCA--GIEVIYALrgnrpGKGSRLE--------AQIVIGTPGTVLDwCFKLRLITVENISVFVLDEADVM 237
Cdd:cd17952    79 ---IYLEAKKFGKayNLRVVAVY-----GGGSKWEqakalqegAEIVVATPGRLID-MVKKKATNLQRVTYLVLDEADRM 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2038246692 238 IN------VQGHSDHsVRVKRsmpkscQMLLFSATFEDSVWAFAERIVPDP 282
Cdd:cd17952   150 FDmgfeyqVRSIVGH-VRPDR------QTLLFSATFKKKIEQLARDILSDP 193
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
94-285 5.86e-22

DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 93.12  E-value: 5.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  94 LRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQ----CICLSPTFELALQTG 169
Cdd:cd17941     2 LKGLKEAGFIKMTEIQRDSIPHALQG--RDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdglgALIISPTRELAMQIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 170 KVVEEMGK---FCAGIeVIyalrGNRPGKGSRLEA---QIVIGTPGTVLDWCFKLRLITVENISVFVLDEADVMINVqGH 243
Cdd:cd17941    80 EVLRKVGKyhsFSAGL-II----GGKDVKEEKERInrmNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDM-GF 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2038246692 244 SDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNII 285
Cdd:cd17941   154 KETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
80-267 9.09e-22

DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350809 [Multi-domain]  Cd Length: 249  Bit Score: 93.95  E-value: 9.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  80 SVKSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAN---------- 149
Cdd:cd18051    19 HIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSK--RDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslpses 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 150 ------KKYPQCICLSPTFELALQtgkVVEEMGKF--CAGIE--VIYAlrGNRPGKGSR-LE--AQIVIGTPGTVLDWCF 216
Cdd:cd18051    97 gyygrrKQYPLALVLAPTRELASQ---IYDEARKFayRSRVRpcVVYG--GADIGQQMRdLErgCHLLVATPGRLVDMLE 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2038246692 217 KLRlITVENISVFVLDEADVMINVqGHSDHSVRV--KRSMPKSC--QMLLFSATF 267
Cdd:cd18051   172 RGK-IGLDYCKYLVLDEADRMLDM-GFEPQIRRIveQDTMPPTGerQTLMFSATF 224
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
93-282 1.96e-21

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 91.88  E-value: 1.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLADPpqNLIAQSQSGTGKTAAFVLAMLSRV--DANKKYPQCICLSPTFELALQTgk 170
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGR--DLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQI-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 171 vVEEMGKFCAGIEVIYAL--RGNRP----GKGSRLEAQIVIGTPGTVLDwCFKLRLITVENISVFVLDEADVMI--NVQG 242
Cdd:cd17957    77 -YRELLKLSKGTGLRIVLlsKSLEAkakdGPKSITKYDILVSTPLRLVF-LLKQGPIDLSSVEYLVLDEADKLFepGFRE 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2038246692 243 HSDHSVRVKRSmpKSCQMLLFSATFEDSVWAFAERIVPDP 282
Cdd:cd17957   155 QTDEILAACTN--PNLQRSLFSATIPSEVEELARSVMKDP 192
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
93-285 2.15e-20

DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 88.68  E-value: 2.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAN------KKYPQCICLSPTFELAL 166
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQG--IDLIGVAQTGTGKTLAYLLPGFIHLDLQpipreqRNGPGVLVLTPTRELAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 167 QtgkVVEEMGKFC-AGIEVI--YAlRGNRPGKGSRLE--AQIVIGTPGTVLDWCFKlRLITVENISVFVLDEADVMINVq 241
Cdd:cd17958    79 Q---IEAECSKYSyKGLKSVcvYG-GGNRNEQIEDLSkgVDIIIATPGRLNDLQMN-NVINLKSITYLVLDEADRMLDM- 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2038246692 242 GHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNII 285
Cdd:cd17958   153 GFEPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
100-286 8.83e-20

DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 87.64  E-value: 8.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 100 MGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKY------PQCICLSPTFELALQTGKVVE 173
Cdd:cd17949     9 MGIEKPTAIQKLAIPVLLQG--RDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdrsdgTLALVLVPTRELALQIYEVLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 174 EMGKFCAGIEVIYALRG-NRPGKGSRLE--AQIVIGTPGTVLDWCFKLRLITVENISVFVLDEADVM------------I 238
Cdd:cd17949    87 KLLKPFHWIVPGYLIGGeKRKSEKARLRkgVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLldmgfekditkiL 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2038246692 239 NVQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIK 286
Cdd:cd17949   167 ELLDDKRSKAGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
93-267 2.04e-19

DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 86.91  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLADPpQNLIAQSQSGTGKTAAF-------VLAMLSRVDANK--KYPQCICLSPTFE 163
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPAAIRDG-KDVIGAAETGSGKTLAFgipilerLLSQKSSNGVGGkqKPLRALILTPTRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 164 LALQTGKVVEEMGKFcAGIEVIYALRGNRPGKGSRL---EAQIVIGTPGTVLDwcfklrLIT--------VENISVFVLD 232
Cdd:cd17946    80 LAVQVKDHLKAIAKY-TNIKIASIVGGLAVQKQERLlkkRPEIVVATPGRLWE------LIQegnehlanLKSLRFLVLD 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2038246692 233 EADVMINvQGHSD--HSV--RVKRSMPKSC---QMLLFSATF 267
Cdd:cd17946   153 EADRMLE-KGHFAelEKIleLLNKDRAGKKrkrQTFVFSATL 193
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
81-282 3.10e-19

DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 86.28  E-value: 3.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  81 VKSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKY-----PQC 155
Cdd:cd17953    11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSG--RDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVkpgegPIG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 156 ICLSPTFELALQtgkVVEEMGKFCA--GIEVIYALRGNR-PGKGSRLE--AQIVIGTPGTVLDWcfkL-----RLITVEN 225
Cdd:cd17953    89 LIMAPTRELALQ---IYVECKKFSKalGLRVVCVYGGSGiSEQIAELKrgAEIVVCTPGRMIDI---LtanngRVTNLRR 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2038246692 226 ISVFVLDEADVMINVqGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDP 282
Cdd:cd17953   163 VTYVVLDEADRMFDM-GFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
94-266 5.41e-18

DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 82.02  E-value: 5.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  94 LRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQ----CICLSPTFELALQTG 169
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEG--RDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRngtgVIIISPTRELALQIY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 170 KVVEEMGKFCAGIEVIYALRGNRPGKGSRLEA--QIVIGTPGTVLDWCFKLRLITVENISVFVLDEADVMINVqGHSDHS 247
Cdd:cd17942    80 GVAKELLKYHSQTFGIVIGGANRKAEAEKLGKgvNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEI-GFEEEM 158
                         170
                  ....*....|....*....
gi 2038246692 248 VRVKRSMPKSCQMLLFSAT 266
Cdd:cd17942   159 RQIIKLLPKRRQTMLFSAT 177
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
93-282 1.04e-17

DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 81.26  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANKKY-----PQCICLSPTFELALQ 167
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSG--RDMVGIAQTGSGKTLAFLLPAIVHINAQPPLergdgPIVLVLAPTRELAQQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 168 tgkVVEEMGKFCAGIEV----IY--ALRGNRPGKGSRlEAQIVIGTPGTVLDW----CFKLRLITvenisVFVLDEADVM 237
Cdd:cd17966    79 ---IQQEANKFGGSSRLrntcVYggAPKGPQIRDLRR-GVEICIATPGRLIDFldqgKTNLRRVT-----YLVLDEADRM 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2038246692 238 INVqGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDP 282
Cdd:cd17966   150 LDM-GFEPQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDY 193
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
93-285 1.82e-15

DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350709 [Multi-domain]  Cd Length: 206  Bit Score: 75.07  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAM-LSRVDANKKYPQC-------ICLSPTFEL 164
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSG--RDMIGIAFTGSGKTLVFTLPLiMFALEQEKKLPFIkgegpygLIVCPSREL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 165 ALQTGKVVEEMGKFCA--------------GIEVIYALRGNRPGkgsrleAQIVIGTPGTVLDWCFKlRLITVENISVFV 230
Cdd:cd17951    79 ARQTHEVIEYYCKALQeggypqlrcllcigGMSVKEQLEVIRKG------VHIVVATPGRLMDMLNK-KKINLDICRYLC 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2038246692 231 LDEADVMINvQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNII 285
Cdd:cd17951   152 LDEADRMID-MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
63-281 1.68e-14

DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 73.51  E-value: 1.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  63 SPHNVEVLQRDPT---------SPLFSvksFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTG 133
Cdd:cd18050    37 TQYDVEELRRKKEitirgvgcpKPVFA---FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSG--RDMVGIAQTGSG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 134 KTAAFVLAMLSRVDaNKKY------PQCICLSPTFELALQTGKVVEEMGKfCAGIEVIYALRGNRPGKGSR-LE--AQIV 204
Cdd:cd18050   112 KTLAYLLPAIVHIN-HQPYlergdgPICLVLAPTRELAQQVQQVADDYGK-SSRLKSTCIYGGAPKGPQIRdLErgVEIC 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038246692 205 IGTPGTVLDWcFKLRLITVENISVFVLDEADVMINVqGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPD 281
Cdd:cd18050   190 IATPGRLIDF-LEAGKTNLRRCTYLVLDEADRMLDM-GFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
81-281 5.85e-14

DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 71.19  E-value: 5.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  81 VKSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVD-----ANKKYPQC 155
Cdd:cd18049    23 VLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSG--LDMVGVAQTGSGKTLSYLLPAIVHINhqpflERGDGPIC 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 156 ICLSPTFELALQTGKVVEEMGKFC-AGIEVIYalrGNRPgKGSRLE-----AQIVIGTPGTVLDW--CFKLRLitvENIS 227
Cdd:cd18049   101 LVLAPTRELAQQVQQVAAEYGRACrLKSTCIY---GGAP-KGPQIRdlergVEICIATPGRLIDFleAGKTNL---RRCT 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2038246692 228 VFVLDEADVMINVqGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPD 281
Cdd:cd18049   174 YLVLDEADRMLDM-GFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
131-396 3.80e-13

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 71.59  E-value: 3.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 131 GTGKT--AAFVLAMLSRVDankkypQCICLSPTFELALQTgkvVEEMGKFCAGIEViyalrgnrPGKGSRLEAQIVIGTP 208
Cdd:COG1061   110 GTGKTvlALALAAELLRGK------RVLVLVPRRELLEQW---AEELRRFLGDPLA--------GGGKKDSDAPITVATY 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 209 GTvLDWCFKLRLItVENISVFVLDEAdvminvqgHsdH----SVRVKRSMPKSCQMLLFSAT------------------ 266
Cdd:COG1061   173 QS-LARRAHLDEL-GDRFGLVIIDEA--------H--HagapSYRRILEAFPAAYRLGLTATpfrsdgreillflfdgiv 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 267 FEDSVW-AFAERIVPDPNII----KLKKEELTLKNIQQFYDQC-----ENKEQKYSALCNLYGviTIAQAIVFCQTRKIA 336
Cdd:COG1061   241 YEYSLKeAIEDGYLAPPEYYgirvDLTDERAEYDALSERLREAlaadaERKDKILRELLREHP--DDRKTLVFCSSVDHA 318
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 337 SWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVV 396
Cdd:COG1061   319 EALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
122-277 5.38e-13

DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 67.57  E-value: 5.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 122 QNLIAQSQSGTGKTAAFVLAMLSRVDANK------KYPQCICLSPTFELALQTGKVVEEMGKFCAgievIYALRGNRPGK 195
Cdd:cd17944    28 KDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTKDFKDITRKLS----VACFYGGTPYQ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 196 GS----RLEAQIVIGTPGTVLDWC--FKLRLITVENIsvfVLDEADVMINVqGHSDH-----SVRVKRSMPKSCQMLLFS 264
Cdd:cd17944   104 QQifaiRNGIDILVGTPGRIKDHLqnGRLDLTKLKHV---VLDEVDQMLDM-GFAEQveeilSVSYKKDSEDNPQTLLFS 179
                         170
                  ....*....|...
gi 2038246692 265 ATFEDSVWAFAER 277
Cdd:cd17944   180 ATCPDWVYNVAKK 192
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
123-266 8.82e-13

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: 65.50  E-value: 8.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 123 NLIAQSQSGTGKTAAFVLAMLSRvdANKKYPQCICLSPTFELALQTGKVVEEMGKFCAGIEVIY-ALRGNRPGKGSRLEA 201
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALLL--LLKKGKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVgGSSAEEREKNKLGDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038246692 202 QIVIGTPGTVLDWCFKLRLITVENISVFVLDEADVM-INVQGHSDHSVRVKRSMPKSCQMLLFSAT 266
Cdd:cd00046    81 DIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALlIDSRGALILDLAVRKAGLKNAQVILLSAT 146
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
93-266 1.19e-12

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 67.27  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLAD-------PPQNLIAQSQSGTGKTAAFVL----AMLSRVDankkyPQ--CICLS 159
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyRPGDLCVSAPTGSGKTLAYVLpivqALSKRVV-----PRlrALIVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 160 PTFELALQtgkVVEEMGKFCAGIEV-IYALRGNR------------PGKGSRLEAQIVIGTPGTVLDWCFKLRLITVENI 226
Cdd:cd17956    76 PTKELVQQ---VYKVFESLCKGTGLkVVSLSGQKsfkkeqklllvdTSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHL 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038246692 227 SVFVLDEADVMIN---------VQGHSDHSVRVKRSM----------PKSCQMLLFSAT 266
Cdd:cd17956   153 RFLVIDEADRLLNqsfqdwletVMKALGRPTAPDLGSfgdanllersVRPLQKLLFSAT 211
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
93-292 3.85e-12

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 65.85  E-value: 3.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  93 LLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDANK-------KYPQCICLSPTFELA 165
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRG--RNTLCAAETGSGKTLTYLLPIIQRLLRYKllaegpfNAPRGLVITPSRELA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 166 LQTGKVVEemgKFCA--GIEVIYALRGNrpGKGSRL-----EAQIVIGTPGTVLdwcfKL---RLITVENISVFVLDEAD 235
Cdd:cd17948    79 EQIGSVAQ---SLTEglGLKVKVITGGR--TKRQIRnphfeEVDILVATPGALS----KLltsRIYSLEQLRHLVLDEAD 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 236 VMIN-------------VQGHSDHSVRVKRSMPKScQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEEL 292
Cdd:cd17948   150 TLLDdsfneklshflrrFPLASRRSENTDGLDPGT-QLVLVSATMPSGVGEVLSKVIDVDSIETVTSDKL 218
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
326-403 3.06e-09

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They 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: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 55.18  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 326 AIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREK--VLVTTNVCARGIDVEQVSIVVNFDLPVN 403
Cdd:cd18793    30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPWWN 109
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
314-430 9.17e-09

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 57.82  E-value: 9.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 314 LCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYD--------RADMIQRFREGREKVLVTTNVCAR 385
Cdd:COG1111   344 LKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQASKEGdkgltqkeQIEILERFRAGEFNVLVATSVAEE 423
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2038246692 386 GIDVEQVSIVVNFDlpvNVDGSVDFEtylHRIGRTGRFGKKGIAV 430
Cdd:COG1111   424 GLDIPEVDLVIFYE---PVPSEIRSI---QRKGRTGRKREGRVVV 462
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
327-458 1.03e-08

Superfamily II DNA helicase RecQ [Replication, recombination and repair];


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 57.46  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 327 IVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNvcA--RGIDVEQVSIVVNFDLPVNV 404
Cdd:COG0514   234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AfgMGIDKPDVRFVIHYDLPKSI 311
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038246692 405 dgsvdfETYLHRIGRTGRFGKKGIAVSL-------IENFFVYMLKEIEDHFNTKITKLNSM 458
Cdd:COG0514   312 ------EAYYQEIGRAGRDGLPAEALLLygpedvaIQRFFIEQSPPDEERKRVERAKLDAM 366
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
326-420 1.21e-08

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 57.54  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 326 AIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREK--VLVTTNVCARGIDVEQVSIVVNFDLPVN 403
Cdd:COG0553   552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWWN 631
                          90       100
                  ....*....|....*....|
gi 2038246692 404 ---VDGSVDfetYLHRIGRT 420
Cdd:COG0553   632 pavEEQAID---RAHRIGQT 648
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
324-404 7.01e-08

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains 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: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 51.44  E-value: 7.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 324 AQAIVFCQTRKIASWLSQKLSDDGHQ-----VALLSGELPVYDRADM----------IQRFREGREKVLVTTNVCARGID 388
Cdd:cd18802    26 FRGIIFVERRATAVVLSRLLKEHPSTlafirCGFLIGRGNSSQRKRSlmtqrkqketLDKFRDGELNLLIATSVLEEGID 105
                          90
                  ....*....|....*.
gi 2038246692 389 VEQVSIVVNFDLPVNV 404
Cdd:cd18802   106 VPACNLVIRFDLPKTL 121
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
324-430 1.12e-07

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases 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: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 51.10  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 324 AQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVY-------DRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVV 396
Cdd:cd18797    36 VKTIVFCRSRKLAELLLRYLKARLVEEGPLASKVASYragylaeDRREIEAELFNGELLGVVATNALELGIDIGGLDAVV 115
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2038246692 397 NFDLPvnvdGSVdfETYLHRIGRTGRFGKKGIAV 430
Cdd:cd18797   116 LAGYP----GSL--ASLWQQAGRAGRRGKDSLVI 143
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
326-425 1.97e-07

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They 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: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 49.90  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 326 AIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVVNFDLPVNVd 405
Cdd:cd18794    33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSM- 111
                          90       100
                  ....*....|....*....|
gi 2038246692 406 gsvdfETYLHRIGRTGRFGK 425
Cdd:cd18794   112 -----ESYYQESGRAGRDGL 126
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
324-430 3.11e-07

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 52.92  E-value: 3.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 324 AQAIVFCQTRK----IASWLSQKL--SDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVVN 397
Cdd:COG1205   289 LRTLVFTRSRRgaelLARYARRALrePDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVL 368
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2038246692 398 FDLPvnvdGSVDfeTYLHRIGRTGRFGKKGIAV 430
Cdd:COG1205   369 AGYP----GTRA--SFWQQAGRAGRRGQDSLVV 395
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
84-285 9.89e-07

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 50.07  E-value: 9.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692  84 FEEL--------HLKNELLRGIYA-MGFNRPSKIQENALPMMLADPPQN---------------LIAqSQSGTGKTAAFV 139
Cdd:cd17965     1 FDQLkllpsvreAIIKEILKGSNKtDEEIKPSPIQTLAIKKLLKTLMRKvtkqtsneepklevfLLA-AETGSGKTLAYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 140 LAMLSRVD-----------------ANKKYPQCICLSPTFELALQTGKVVEEMGKFCA-GIEVIYALRG---NRPGKGSR 198
Cdd:cd17965    80 APLLDYLKrqeqepfeeaeeeyesaKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKlGIKTFSSGFGpsyQRLQLAFK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 199 LEAQIVIGTPGTVLDwCFKLRLITVENISVFVLDEADVMINvQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERI 278
Cdd:cd17965   160 GRIDILVTTPGKLAS-LAKSRPKILSRVTHLVVDEADTLFD-RSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKL 237

                  ....*..
gi 2038246692 279 VPDPNII 285
Cdd:cd17965   238 FPDVVRI 244
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
375-427 3.34e-06

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 45.00  E-value: 3.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2038246692 375 KVLVTTNVCARGIDVEQVSIVVNFDLPVNVdgsvdfETYLHRIGRTGRFGKKG 427
Cdd:cd18785    24 EILVATNVLGEGIDVPSLDTVIFFDPPSSA------ASYIQRVGRAGRGGKDE 70
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
327-458 5.40e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 48.94  E-value: 5.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 327 IVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVVNFDLPVNVdg 406
Cdd:PRK11057  240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI-- 317
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038246692 407 svdfETYLHRIGRTGRFGKKGIAVSL------------IENFFVYMLKEIEDHfntkitKLNSM 458
Cdd:PRK11057  318 ----ESYYQETGRAGRDGLPAEAMLFydpadmawlrrcLEEKPAGQQQDIERH------KLNAM 371
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
325-442 7.79e-05

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase 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: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 43.01  E-value: 7.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 325 QAIVFCQTRKIASWLSQKLsddghQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQ--VSIVVNFdlpv 402
Cdd:cd18789    51 KIIVFTDNVEALYRYAKRL-----LKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEanVAIQISG---- 121
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2038246692 403 nVDGSVdfETYLHRIGRTGRFGKKGIAvslieNFFVYMLK 442
Cdd:cd18789   122 -HGGSR--RQEAQRLGRILRPKKGGGK-----NAFFYSLV 153
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
202-426 1.59e-04

CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 43.57  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 202 QIVIGTPGTVL---DWCFKLRLITVENI--SVFVLDEADVMI-NVQGHSDHSVRVKRSMPKScqMLLFSATFEDSVWAFA 275
Cdd:cd09639    95 PITVCTIDQVLksvFGEFGHYEFTLASIanSLLIFDEVHFYDeYTLALILAVLEVLKDNDVP--ILLMSATLPKFLKEYA 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 276 ERIVPDpniikLKKEELTLKNIQ-QFYDQCENKE-------QKYSALCNLYGvitiaQAIVFCQTRKIASWLSQKLSDDG 347
Cdd:cd09639   173 EKIGYV-----EENEPLDLKPNErAPFIKIESDKvgeisslERLLEFIKKGG-----SVAIIVNTVDRAQEFYQQLKEKG 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 348 HQ--VALLSGELPVYDRAD----MIQRFREGREKVLVTTNVcargidVEqVSIVVNFDLPVNVDGSVDfeTYLHRIGRTG 421
Cdd:cd09639   243 PEeeIMLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQV------IE-ASLDISVDVMITELAPID--SLIQRLGRLH 313

                  ....*
gi 2038246692 422 RFGKK 426
Cdd:cd09639   314 RYGEK 318
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
122-234 2.26e-04

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 42.25  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 122 QNLIAQSQSGTGKT--AAFVLAMLSRVDANKKYPQCIC--LSPTFELALQTGKVVEE-----MGKFCaGIEVIYALRGNR 192
Cdd:cd18034    17 RNTIVVLPTGSGKTliAVMLIKEMGELNRKEKNPKKRAvfLVPTVPLVAQQAEAIRShtdlkVGEYS-GEMGVDKWTKER 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2038246692 193 pGKGSRLEAQIVIGTPGTVLDWcfkLR--LITVENISVFVLDEA 234
Cdd:cd18034    96 -WKEELEKYDVLVMTAQILLDA---LRhgFLSLSDINLLIFDEC 135
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
366-433 4.28e-04

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 40.42  E-value: 4.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038246692 366 IQRFREGREKVLVTTNVCARGIDVEQVSIVVNFdlpvnvDGSVDFETYLHRIGRTGRfGKKGIAVSLI 433
Cdd:cd18801    83 IEQFRKGGYNVLVATSIGEEGLDIGEVDLIICY------DASPSPIRMIQRMGRTGR-KRQGRVVVLL 143
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
327-422 5.58e-04

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases 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: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 40.33  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 327 IVFCQTRKIASWLSQKLSD------DGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVVNFDL 400
Cdd:cd18796    42 LVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
                          90       100
                  ....*....|....*....|..
gi 2038246692 401 PVNVDGsvdfetYLHRIGRTGR 422
Cdd:cd18796   122 PKSVAR------LLQRLGRSGH 137
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
104-207 7.83e-04

DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 40.48  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 104 RPSKIQENALPM----MLADPPQNLIAQSQSGTGKTAAFVLAMLSRVDANKkypQCICLSPTFELALQTgkvVEEMGKFC 179
Cdd:cd17918    15 SLTKDQAQAIKDiekdLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGK---QVAILVPTEILAHQH---YEEARKFL 88
                          90       100
                  ....*....|....*....|....*...
gi 2038246692 180 AGIEVIYALRGNRPGKGSrlEAQIVIGT 207
Cdd:cd17918    89 PFINVELVTGGTKAQILS--GISLLVGT 114
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
333-422 1.50e-03

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 41.01  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 333 RKIASWLSQKLSDDGHQ-------------VALLSGELP------VY----DRADMIQRFREGREKVLVTTNVCARGIDV 389
Cdd:COG4098   306 RKLLKWLKKRLKEGRQLlifvptielleqlVALLQKLFPeeriagVHaedpERKEKVQAFRDGEIPILVTTTILERGVTF 385
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2038246692 390 EQVSIVVnfdlpVNVDGSVDFETYLHRI-GRTGR 422
Cdd:COG4098   386 PNVDVAV-----LGADHPVFTEAALVQIaGRVGR 414
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
325-430 3.16e-03

C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases 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: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 38.30  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 325 QAIVFCQTRKIASWLSQKLSddGhqVALLSGELPVYDRaDMIQR-FREGREKVLVTT-------NVCARGIDVEQVSIVV 396
Cdd:cd18795    45 PVLVFCSSRKECEKTAKDLA--G--IAFHHAGLTREDR-ELVEElFREGLIKVLVATstlaagvNLPARTVIIKGTQRYD 119
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2038246692 397 NF---DLPVNvdgsvdfeTYLHRIGRTGR--FGKKGIAV 430
Cdd:cd18795   120 GKgyrELSPL--------EYLQMIGRAGRpgFDTRGEAI 150
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
332-422 5.95e-03

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase 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: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 37.61  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038246692 332 TRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVVNFDlpVNVDGSVDFE 411
Cdd:cd18790    36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKEGFLRSE 113
                          90
                  ....*....|..
gi 2038246692 412 TYL-HRIGRTGR 422
Cdd:cd18790   114 TSLiQTIGRAAR 125
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
350-422 9.60e-03

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase 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: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 36.94  E-value: 9.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038246692 350 VALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVV-----NFDLpvnvdgsvdfeTYLHRI-GRTGR 422
Cdd:cd18811    64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMViedaeRFGL-----------SQLHQLrGRVGR 131
 
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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