|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
37-458 |
8.38e-169 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 481.18 E-value: 8.38e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 37 RFADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRaePGQPLGLVLVPT 116
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR--PRAPQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 117 RELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADM 196
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 197 GFMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVVHSVDPSAGAVTTMEHHVLHVHGADKHAATTEIAARD- 275
Cdd:COG0513 161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 276 -GRVLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVDPPS 354
Cdd:COG0513 241 pERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 355 DHKDYLHRGGRTARAGESGSVVTLVTPNQRRAMTRLMTTAGIVPQTTPVRSGTEalhrVTGAQAPSGIPVVVTAPVAERA 434
Cdd:COG0513 321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEP----VEEKRLERLKPKIKEKLKGKKA 396
|
410 420
....*....|....*....|....
gi 2189654348 435 ERGATSRGRRRPAPATRRGSVRRS 458
Cdd:COG0513 397 GRGGRPGPKGERKARRGKRRRRKR 420
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
38-382 |
5.62e-92 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 286.31 E-value: 5.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRAepgQPLGLVLVPTR 117
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRF---RVQALVLCPTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 118 ELAQQVTDALRPYARS---VKLrLTaVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMA 194
Cdd:PRK11776 83 ELADQVAKEIRRLARFipnIKV-LT-LCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 195 DMGFMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVVHSVDpSAGAVTTMEHHVLHVHGADKHAATTEIAA- 273
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVE-STHDLPAIEQRFYEVSPDERLPALQRLLLh 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 274 -RDGRVLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVDP 352
Cdd:PRK11776 240 hQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
|
330 340 350
....*....|....*....|....*....|
gi 2189654348 353 PSDHKDYLHRGGRTARAGESGSVVTLVTPN 382
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
44-385 |
1.71e-85 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 272.42 E-value: 1.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 44 PAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGL-ALLARTAGRRAEPGQ-PLGLVLVPTRELAQ 121
Cdd:PTZ00110 138 PDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLpAIVHINAQPLLRYGDgPIVLVLAPTRELAE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 122 QVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQ 201
Cdd:PTZ00110 218 QIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 202 VTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVVH----SVDPSAGAVTTMEHHVLHVHgaDKHAATTEIAAR--- 274
Cdd:PTZ00110 298 IRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHvnvgSLDLTACHNIKQEVFVVEEH--EKRGKLKMLLQRimr 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 275 -DGRVLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVDPP 353
Cdd:PTZ00110 376 dGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFP 455
|
330 340 350
....*....|....*....|....*....|..
gi 2189654348 354 SDHKDYLHRGGRTARAGESGSVVTLVTPNQRR 385
Cdd:PTZ00110 456 NQIEDYVHRIGRTGRAGAKGASYTFLTPDKYR 487
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-373 |
1.76e-84 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 267.55 E-value: 1.76e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 3 DRPARTGKARTRALAVQGEFAhpetLTPAlPAAARFADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRT 82
Cdd:PRK01297 59 DKPRRERKPKPASLWKLEDFV----VEPQ-EGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 83 GSGKTLAFGLA----LLARTAGRRAEPGQPLGLVLVPTRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGG- 157
Cdd:PRK01297 134 GTGKTAAFLISiinqLLQTPPPKERYMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARf 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 158 VEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTALLDQVRPEGQR--MLFSATLDRNVDLLVRRYLS 235
Cdd:PRK01297 214 CDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRKEERqtLLFSATFTDDVMNLAKQWTT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 236 DPVVHSVDPSAGAVTTMEHHVLHVHGADKHAATTEIAARDG--RVLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQ 313
Cdd:PRK01297 294 DPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNLVTQNPweRVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHK 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 314 RTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVDPPSDHKDYLHRGGRTARAGESG 373
Cdd:PRK01297 374 RIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASG 433
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
38-379 |
3.61e-83 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 262.96 E-value: 3.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGL-ALLARTAGRRAEPGQPLGLVLVPT 116
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLpALQHLLDFPRRKSGPPRILILTPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 117 RELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRG--DCRlnQVSVTVLDEADQMA 194
Cdd:PRK11192 83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEEnfDCR--AVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 195 DMGFMPQVTALLDQVRPEGQRMLFSATLD-RNVDLLVRRYLSDPVVHSVDPSagavtTMEHHVLH--VHGADKHAATTEI 271
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPS-----RRERKKIHqwYYRADDLEHKTAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 272 AAR------DGRVLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLD 345
Cdd:PRK11192 236 LCHllkqpeVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
|
330 340 350
....*....|....*....|....*....|....
gi 2189654348 346 LVVNVDPPSDHKDYLHRGGRTARAGESGSVVTLV 379
Cdd:PRK11192 316 HVINFDMPRSADTYLHRIGRTGRAGRKGTAISLV 349
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
47-238 |
5.12e-82 |
|
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: 251.59 E-value: 5.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLAR-TAGRRAEPGQPLGLVLVPTRELAQQVTD 125
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKlLPEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 126 ALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTAL 205
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|...
gi 2189654348 206 LDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPV 193
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
38-379 |
3.47e-80 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 255.89 E-value: 3.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRAEPGQ--PL-GLVLV 114
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGrrPVrALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 115 PTRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMA 194
Cdd:PRK10590 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 195 DMGFMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVVHSVdpsAGAVTTMEHHVLHVHGADKHAATTEIAAR 274
Cdd:PRK10590 163 DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEV---ARRNTASEQVTQHVHFVDKKRKRELLSQM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 275 DGR-----VLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVN 349
Cdd:PRK10590 240 IGKgnwqqVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
|
330 340 350
....*....|....*....|....*....|
gi 2189654348 350 VDPPSDHKDYLHRGGRTARAGESGSVVTLV 379
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLV 349
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
37-378 |
4.60e-74 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 239.10 E-value: 4.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 37 RFADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLA----LLARTAGRRAEPGQPLGLV 112
Cdd:PRK04837 9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKVNQPRALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 113 LVPTRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQ 192
Cdd:PRK04837 89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 193 MADMGFMPQVTALLDQVRPEGQR--MLFSATLDRNVDLLVRRYLSDPVVHSVDPSAGAVTTMEHHVLHVHGADKHAATTE 270
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPANQRlnMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 271 IAARD--GRVLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVV 348
Cdd:PRK04837 249 LIEEEwpDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVF 328
|
330 340 350
....*....|....*....|....*....|
gi 2189654348 349 NVDPPSDHKDYLHRGGRTARAGESGSVVTL 378
Cdd:PRK04837 329 NYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
38-385 |
2.41e-73 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 242.83 E-value: 2.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTagrRAEPGQPLGLVLVPTR 117
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL---DPELKAPQILVLAPTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 118 ELAQQVTDALRPYARSVK-LRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADM 196
Cdd:PRK11634 85 ELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 197 GFMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVVHSVDPSAGAVTTMEHHVLHVHGADKHAATTE-IAARD 275
Cdd:PRK11634 165 GFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRfLEAED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 276 -GRVLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVDPPS 354
Cdd:PRK11634 245 fDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM 324
|
330 340 350
....*....|....*....|....*....|.
gi 2189654348 355 DHKDYLHRGGRTARAGESGSVVTLVTPNQRR 385
Cdd:PRK11634 325 DSESYVHRIGRTGRAGRAGRALLFVENRERR 355
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
38-410 |
3.15e-65 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 219.82 E-value: 3.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRA----EPGQPLGLVL 113
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPAladrKPEDPRALIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 114 VPTRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDC-RLNQVSVTVLDEADQ 192
Cdd:PRK04537 91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEADR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 193 MADMGFMPQVTALLDQVRPEGQR--MLFSATLDRNVDLLVRRYLSDPVVHSVDPSAGAVTTMEHHVLHVHGADKHAATTE 270
Cdd:PRK04537 171 MFDLGFIKDIRFLLRRMPERGTRqtLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 271 IAARD--GRVLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVV 348
Cdd:PRK04537 251 LLSRSegARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVY 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2189654348 349 NVDPPSDHKDYLHRGGRTARAGESGSVVTLVTpnQRRAMTrLMTTAGIVPQTTPVRSGTEAL 410
Cdd:PRK04537 331 NYDLPFDAEDYVHRIGRTARLGEEGDAISFAC--ERYAMS-LPDIEAYIEQKIPVEPVTAEL 389
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
43-238 |
3.08e-61 |
|
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: 199.14 E-value: 3.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 43 MPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRA-EPGQ-PLGLVLVPTRELA 120
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPvKPGEgPIGLIMAPTRELA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 121 QQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCR---LNQVSVTVLDEADQMADMG 197
Cdd:cd17953 99 LQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRvtnLRRVTYVVLDEADRMFDMG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2189654348 198 FMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd17953 179 FEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPI 219
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
12-385 |
1.20e-60 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 206.56 E-value: 1.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 12 RTRALAVQGEFAHPETLTpalpaaarFADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFG 91
Cdd:PLN00206 105 RKLEIHVKGEAVPPPILS--------FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 92 LALLARTAGRR----AEPGQPLGLVLVPTRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGR 167
Cdd:PLN00206 177 VPIISRCCTIRsghpSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 168 LKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTALLdQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVVHSVDPSAG 247
Cdd:PLN00206 257 LIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNR 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 248 AVTTMEHHVLHVHGADKHAATTEIAARDGR----VLMFLDTKHAVDRLTDHL-LNSGVRAAALHGGKSQSQRTRTLAQFK 322
Cdd:PLN00206 336 PNKAVKQLAIWVETKQKKQKLFDILKSKQHfkppAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFL 415
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2189654348 323 TGHVTVLVATNVAARGIHVDNLDLVVNVDPPSDHKDYLHRGGRTARAGESGSVVTLVTPNQRR 385
Cdd:PLN00206 416 VGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRN 478
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
47-239 |
1.35e-60 |
|
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: 196.48 E-value: 1.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRA-EPGQ-PLGLVLVPTRELAQQVT 124
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRElEKGEgPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 125 DALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTA 204
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2189654348 205 LLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVV 239
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIR 195
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
47-238 |
5.50e-58 |
|
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: 189.50 E-value: 5.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGL-ALLARTAGRRAEPGQ-PLGLVLVPTRELAQQVT 124
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLpAIVHINAQPPLERGDgPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 125 DALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTA 204
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 2189654348 205 LLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYI 194
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
47-239 |
5.48e-57 |
|
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: 187.91 E-value: 5.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLA---RTAGRRAEPGQ--PLGLVLVPTRELAQ 121
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVyisRLPPLDEETKDdgPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 122 QVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQ 201
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2189654348 202 VTALLDQV-----RPEG---------------QRMLFSATLDRNVDLLVRRYLSDPVV 239
Cdd:cd17945 161 VTKILDAMpvsnkKPDTeeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVV 218
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
61-229 |
9.81e-53 |
|
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: 174.74 E-value: 9.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 61 PIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARtagRRAEPGQPLGLVLVPTRELAQQVTDALRPYARSVKLRLTA 140
Cdd:pfam00270 2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEA---LDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 141 VVGGMSIGRQASALRGgVEVVVATPGRLKDLIDRGDcRLNQVSVTVLDEADQMADMGFMPQVTALLDQVRPEGQRMLFSA 220
Cdd:pfam00270 79 LLGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156
|
....*....
gi 2189654348 221 TLDRNVDLL 229
Cdd:pfam00270 157 TLPRNLEDL 165
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
38-381 |
1.88e-52 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 181.56 E-value: 1.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTagrRAEPGQPLGLVLVPTR 117
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI---DYDLNACQALILAPTR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 118 ELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMG 197
Cdd:PTZ00424 107 ELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 198 FMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVVHSVDPSAGAVTTMEHHVLHVHGADKHAAT--------T 269
Cdd:PTZ00424 187 FKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTlcdlyetlT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 270 EIAArdgrvLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVN 349
Cdd:PTZ00424 267 ITQA-----IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVIN 341
|
330 340 350
....*....|....*....|....*....|..
gi 2189654348 350 VDPPSDHKDYLHRGGRTARAGESGSVVTLVTP 381
Cdd:PTZ00424 342 YDLPASPENYIHRIGRSGRFGRKGVAINFVTP 373
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
38-236 |
1.57e-51 |
|
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: 173.44 E-value: 1.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLAR-------TAGRRAEPGQPLG 110
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKlledgppSVGRGRRKAYPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 111 LVLVPTRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEA 190
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2189654348 191 DQMADMGFMPQVTALLDQ--VRPEGQR--MLFSATLDRNVDLLVRRYLSD 236
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHpdMPPKGERqtLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
38-241 |
4.66e-50 |
|
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: 169.33 E-value: 4.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGrraEPGQPLGLVLVPTR 117
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSE---DPYGIFALVLTPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 118 ELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGD---CRLNQVSVTVLDEADQMA 194
Cdd:cd17955 78 ELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDdttKVLSRVKFLVLDEADRLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2189654348 195 DMGFMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVVHS 241
Cdd:cd17955 158 TGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
37-238 |
8.53e-49 |
|
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: 167.11 E-value: 8.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 37 RFADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRR-AEPGQ-PLGLVLV 114
Cdd:cd18049 25 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPfLERGDgPICLVLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 115 PTRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMA 194
Cdd:cd18049 105 PTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2189654348 195 DMGFMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd18049 185 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYI 228
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
47-238 |
2.09e-48 |
|
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: 164.74 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRAEPGQPLGLVLVPTRELAQQVTDA 126
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 127 LRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRG-DCRLNQVSVTVLDEADQMADMGFMPQVTAL 205
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|...
gi 2189654348 206 LDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPV 193
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
38-238 |
7.48e-48 |
|
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: 163.26 E-value: 7.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRaepgQPL-GLVLVPT 116
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENP----QRFfALVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 117 RELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGD-CRLNQVSVTVLDEADQMAD 195
Cdd:cd17954 78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2189654348 196 MGFMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd17954 158 MDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPV 200
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
253-379 |
8.65e-48 |
|
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: 160.75 E-value: 8.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 253 EHHVLHVHGADKHAATTEI---AARDGRVLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVL 329
Cdd:cd18787 2 KQLYVVVEEEEKKLLLLLLlleKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2189654348 330 VATNVAARGIHVDNLDLVVNVDPPSDHKDYLHRGGRTARAGESGSVVTLV 379
Cdd:cd18787 82 VATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
38-239 |
1.75e-46 |
|
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: 159.78 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRAEPGQPlGLVLVPTR 117
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGAR-ALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 118 ELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMG 197
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2189654348 198 FMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVV 239
Cdd:cd17959 162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVL 203
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
38-238 |
2.95e-46 |
|
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: 161.33 E-value: 2.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGL-ALLARTAGRRAEPGQ-PLGLVLVP 115
Cdd:cd18050 64 FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLpAIVHINHQPYLERGDgPICLVLAP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 116 TRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMAD 195
Cdd:cd18050 144 TRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLD 223
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2189654348 196 MGFMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd18050 224 MGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYV 266
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
47-232 |
2.00e-45 |
|
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: 158.17 E-value: 2.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLA-GRDVLGRGRTGSGKTLAFGLALLARTAGRRAEPGQ------PLGLVLVPTREL 119
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVggkqkpLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 120 AQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGD---CRLNQVSVTVLDEADQMADM 196
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEADRMLEK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2189654348 197 GFMPQVTALLD--QVRPEG-----QRMLFSATLDRNVDLLVRR 232
Cdd:cd17946 161 GHFAELEKILEllNKDRAGkkrkrQTFVFSATLTLDHQLPLKL 203
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
51-246 |
3.63e-45 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 156.11 E-value: 3.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 51 LESQGVTVPFPIQAATLPNSLAG-RDVLGRGRTGSGKTLAFGLALLArtAGRRAEPGQplGLVLVPTRELAQQVTDALRP 129
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALE--ALKRGKGGR--VLVLVPTRELAEQWAEELKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 130 YARSVKLRLTAVVGGMSIGRQASALRGGV-EVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTALLDQ 208
Cdd:smart00487 77 LGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 2189654348 209 VRPEGQRMLFSATLDRNVDLLVRRYLSDPVVHSVDPSA 246
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTP 194
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
38-238 |
6.86e-43 |
|
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: 150.14 E-value: 6.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTagrRAEPGQPLGLVLVPTR 117
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI---DPKKDVIQALILVPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 118 ELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMG 197
Cdd:cd17940 78 ELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2189654348 198 FMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd17940 158 FQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPY 198
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
48-242 |
1.90e-42 |
|
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: 148.98 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 48 LAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRAEPGQPLG-LVLVPTRELAQQVTDA 126
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGaLIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 127 LRPYARSVKLRLTAVVGGMSIGRQASALrGGVEVVVATPGRLKDLIDRG---DCrlNQVSVTVLDEADQMADMGFMPQVT 203
Cdd:cd17941 82 LRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETpgfDT--SNLQMLVLDEADRILDMGFKETLD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2189654348 204 ALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVVHSV 242
Cdd:cd17941 159 AIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
47-239 |
1.93e-42 |
|
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: 148.77 E-value: 1.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLA----LLARTAGRRAEPGqPLGLVLVPTRELAQQ 122
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgfihLDLQPIPREQRNG-PGVLVLTPTRELALQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 123 VTDALRPYARSvKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQV 202
Cdd:cd17958 80 IEAECSKYSYK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 2189654348 203 TALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVV 239
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMI 195
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
47-239 |
2.36e-42 |
|
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: 149.03 E-value: 2.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALL-------ARTAGRRAEpgQPLGLVLVPTREL 119
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqeKKLPFIKGE--GPYGLIVCPSREL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 120 AQQVTDALRPYARSVK------LRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQM 193
Cdd:cd17951 79 ARQTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2189654348 194 ADMGFMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVV 239
Cdd:cd17951 159 IDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVT 204
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
38-236 |
4.14e-42 |
|
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: 149.81 E-value: 4.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLA---------------RTAGRR 102
Cdd:cd18051 23 FSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSqiyeqgpgeslpsesGYYGRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 103 AEpgQPLGLVLVPTRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQV 182
Cdd:cd18051 103 KQ--YPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYC 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2189654348 183 SVTVLDEADQMADMGFMPQVTALLDQ--VRPEGQR--MLFSATLDRNVDLLVRRYLSD 236
Cdd:cd18051 181 KYLVLDEADRMLDMGFEPQIRRIVEQdtMPPTGERqtLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
38-234 |
1.79e-41 |
|
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: 148.58 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLAR------TAGRRAEPGQPLGL 111
Cdd:cd18052 45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGmmkeglTASSFSEVQEPQAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 112 VLVPTRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEAD 191
Cdd:cd18052 125 IVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEAD 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2189654348 192 QMADMGFMPQVTALLDQ--VRPEGQR--MLFSATLDRNVDLLVRRYL 234
Cdd:cd18052 205 RMLDMGFGPEIRKLVSEpgMPSKEDRqtLMFSATFPEEIQRLAAEFL 251
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
47-238 |
7.29e-39 |
|
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: 139.26 E-value: 7.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRAEPGqPLGLVLVPTRELAQQVTDA 126
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKG-LRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 127 LRPYARSVKLRLTAVVGGMS-IGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTAL 205
Cdd:cd17957 80 LLKLSKGTGLRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
|
170 180 190
....*....|....*....|....*....|....
gi 2189654348 206 LDQVR-PEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd17957 160 LAACTnPNLQRSLFSATIPSEVEELARSVMKDPI 193
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
47-238 |
8.96e-39 |
|
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: 139.25 E-value: 8.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRAE--PGQPLGLVLVPTRELAQQVT 124
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANlkKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 125 DALRPYARSVKLRLTA--VVGGMSIGRQ-ASALRGGVEVVVATPGRLKDLIDRGDCRLN--QVSVTVLDEADQMADMGFM 199
Cdd:cd17960 81 EVLQSFLEHHLPKLKCqlLIGGTNVEEDvKKFKRNGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2189654348 200 PQVTALLDQVrPEgQRM--LFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd17960 161 ADLNRILSKL-PK-QRRtgLFSATQTDAVEELIKAGLRNPV 199
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
47-239 |
2.13e-38 |
|
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: 138.49 E-value: 2.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGL----ALLARTAGRRAEPGqPLGLVLVPTRELAQQ 122
Cdd:cd17961 5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALpiiqKILKAKAESGEEQG-TRALILVPTRELAQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 123 VTDALRPYAR--SVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRL-NQVSVTVLDEADQMADMGFM 199
Cdd:cd17961 84 VSKVLEQLTAycRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSYGYE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2189654348 200 PQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVV 239
Cdd:cd17961 164 EDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAI 203
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
47-238 |
6.07e-38 |
|
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: 136.91 E-value: 6.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGrraEPGQPLGLVLVPTRELAQQVTDA 126
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT---EHRNPSALILTPTRELAVQIEDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 127 LRPYARSV-KLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTAL 205
Cdd:cd17962 78 AKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDI 157
|
170 180 190
....*....|....*....|....*....|...
gi 2189654348 206 LDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd17962 158 LENISHDHQTILVSATIPRGIEQLAGQLLQNPV 190
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
61-234 |
7.06e-38 |
|
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: 137.33 E-value: 7.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 61 PIQAATLPNSLA-GRDVLGRGRTGSGKTLAFGLALLARTAgRRAEPGQPLG---LVLVPTRELAQQVTD---ALRPYARS 133
Cdd:cd17964 19 PVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLL-NTKPAGRRSGvsaLIISPTRELALQIAAeakKLLQGLRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 134 VKLRLtaVVGGMSIGRQASAL-RGGVEVVVATPGRLKDLIDrgDCRLNQ----VSVTVLDEADQMADMGFMPQVTALLDQ 208
Cdd:cd17964 98 LRVQS--AVGGTSRRAELNRLrRGRPDILVATPGRLIDHLE--NPGVAKaftdLDYLVLDEADRLLDMGFRPDLEQILRH 173
|
170 180 190
....*....|....*....|....*....|
gi 2189654348 209 VRPEG----QRMLFSATLDRNVDLLVRRYL 234
Cdd:cd17964 174 LPEKNadprQTLLFSATVPDEVQQIARLTL 203
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
51-234 |
9.22e-38 |
|
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: 136.52 E-value: 9.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 51 LESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAG-----RRAEPgqPLGLVLVPTRELAQQVTD 125
Cdd:cd17944 5 LQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEdqqprKRGRA--PKVLVLAPTRELANQVTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 126 ALRPYARsvKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTAL 205
Cdd:cd17944 83 DFKDITR--KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
|
170 180 190
....*....|....*....|....*....|....
gi 2189654348 206 LD---QVRPEG--QRMLFSATLDRNVDLLVRRYL 234
Cdd:cd17944 161 LSvsyKKDSEDnpQTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
40-238 |
7.11e-37 |
|
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: 133.99 E-value: 7.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 40 DLDMPAELLAALESQGVTVPFPI-QAATLPNSLaGRDVLGRGRTGSGKTLAFGLALLARTAGRRAEPGqplGLVLVPTRE 118
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIqQRAIVPIIK-GRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQ---ALVLAPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 119 LAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGF 198
Cdd:cd17939 77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2189654348 199 MPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPV 196
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
38-222 |
7.94e-36 |
|
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: 131.67 E-value: 7.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTagrraepgqpLGLVLVPTR 117
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV----------VALILEPSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 118 ELAQQVTDALRPYAR---SVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMA 194
Cdd:cd17938 71 ELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLL 150
|
170 180 190
....*....|....*....|....*....|....
gi 2189654348 195 DMGFMPQVTAL---LDQVRPEGQR---MLFSATL 222
Cdd:cd17938 151 SQGNLETINRIynrIPKITSDGKRlqvIVCSATL 184
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
47-239 |
1.04e-35 |
|
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: 130.85 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTagrRAEPGQPLGLVLVPTRELAQQVTDA 126
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL---DLERRHPQVLILAPTREIAVQIHDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 127 LRPYARSVK-LRLTAVVGGMSIGRQASALRGgVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTAL 205
Cdd:cd17943 78 FKKIGKKLEgLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWI 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2189654348 206 LDQVrPEGQRML-FSATLDRNVDLLVRRYLSDPVV 239
Cdd:cd17943 157 FSSL-PKNKQVIaFSATYPKNLDNLLARYMRKPVL 190
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
62-238 |
2.97e-33 |
|
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: 125.01 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 62 IQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLA----------RTAGrraepgqPLGLVLVPTRELAQQVTDALRPYA 131
Cdd:cd17949 17 IQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQrllsleprvdRSDG-------TLALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 132 R-SVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDC-RLNQVSVTVLDEADQMADMGFMPQVTALLDQV 209
Cdd:cd17949 90 KpFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADRLLDMGFEKDITKILELL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2189654348 210 R-------------PEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd17949 170 DdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPV 211
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
38-238 |
2.22e-32 |
|
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: 122.17 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTagrRAEPGQPLGLVLVPTR 117
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI---DTSLKATQALVLAPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 118 ELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMG 197
Cdd:cd18046 78 ELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2189654348 198 FMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd18046 158 FKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPI 198
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
44-239 |
3.02e-32 |
|
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: 121.53 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 44 PAELLAALESQGVTVPFPIQAATLPNSLAG--RDVLGRGRTGSGKTLAFGLALLARTAGRRAEPgQplGLVLVPTRELAQ 121
Cdd:cd17963 2 KPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSP-Q--ALCLAPTRELAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 122 QVTDALRPYARSVKLRLTAVVGGMSIGRqasalRGGVE--VVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADM-GF 198
Cdd:cd17963 79 QIGEVVEKMGKFTGVKVALAVPGNDVPR-----GKKITaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2189654348 199 MPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVV 239
Cdd:cd17963 154 GDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANT 194
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
48-231 |
6.96e-31 |
|
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: 117.85 E-value: 6.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 48 LAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRAEPGQPLG-LVLVPTRELAQQVTDA 126
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGvIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 127 LRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKD-LIDRGDCRLNQVSVTVLDEADQMADMGF---MPQV 202
Cdd:cd17942 82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFeeeMRQI 161
|
170 180
....*....|....*....|....*....
gi 2189654348 203 TALLDQVRpegQRMLFSATLDRNVDLLVR 231
Cdd:cd17942 162 IKLLPKRR---QTMLFSATQTRKVEDLAR 187
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
47-259 |
3.61e-30 |
|
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: 117.08 E-value: 3.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRAEPG----QPLGLVLVPTRELAQQ 122
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEgpfnAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 123 VTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQV 202
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2189654348 203 TALL-------------DQVRPEGQRMLFSATLDRNvdllVRRYLSDpvVHSVDPSAGAVTTMEHHVL-HV 259
Cdd:cd17948 161 SHFLrrfplasrrsentDGLDPGTQLVLVSATMPSG----VGEVLSK--VIDVDSIETVTSDKLHRLMpHV 225
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
38-239 |
6.09e-30 |
|
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: 115.64 E-value: 6.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAGRRAEPGqplGLVLVPTR 117
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQ---ALILSPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 118 ELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMG 197
Cdd:cd18045 78 ELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2189654348 198 FMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVV 239
Cdd:cd18045 158 FKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIR 199
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
38-238 |
1.11e-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: 115.13 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTagrRAEPGQPLGLVLVPTR 117
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL---EPVDGQVSVLVICHTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 118 ELAQQVTDA---LRPYARSVKlrlTAVV-GGMSIGRQASALRGGV-EVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQ 192
Cdd:cd17950 81 ELAFQISNEyerFSKYMPNVK---TAVFfGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2189654348 193 M---ADMgfMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPV 238
Cdd:cd17950 158 MleqLDM--RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPL 204
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
273-370 |
1.00e-28 |
|
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: 109.22 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 273 ARDGRVLMFLDTKHAVDrlTDHLLNS-GVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVD 351
Cdd:pfam00271 13 ERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYD 90
|
90
....*....|....*....
gi 2189654348 352 PPSDHKDYLHRGGRTARAG 370
Cdd:pfam00271 91 LPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
47-226 |
4.76e-28 |
|
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: 111.18 E-value: 4.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 47 LLAALESQGVTVPFPIQAATLPNSLAG---------RDVLGRGRTGSGKTLAFGL----ALLARTAGR-RAepgqplgLV 112
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLpivqALSKRVVPRlRA-------LI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 113 LVPTRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRGG--------VEVVVATPGRLKDLIDRGDC-RLNQVS 183
Cdd:cd17956 74 VVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGfTLKHLR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2189654348 184 VTVLDEADQMADMGF---MPQVTALLDQVRPEG-----------------QRMLFSATLDRNV 226
Cdd:cd17956 154 FLVIDEADRLLNQSFqdwLETVMKALGRPTAPDlgsfgdanllersvrplQKLLFSATLTRDP 216
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
289-370 |
8.16e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 97.28 E-value: 8.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 289 DRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVDPPSDHKDYLHRGGRTAR 368
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 2189654348 369 AG 370
Cdd:smart00490 81 AG 82
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
82-239 |
1.65e-20 |
|
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: 90.51 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 82 TGSGKTLAFGLALLarTAGRRAE----------------PGQPLGLVLVPTRELAQQVTDALRPYARSVKLRLTAVVGGM 145
Cdd:cd17965 70 TGSGKTLAYLAPLL--DYLKRQEqepfeeaeeeyesakdTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 146 SIGRQASAL--RGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTALLDQVRPEGQRMLFSATLD 223
Cdd:cd17965 148 GPSYQRLQLafKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227
|
170
....*....|....*.
gi 2189654348 224 RNVDLLVRRYLSDPVV 239
Cdd:cd17965 228 KEFDKTLRKLFPDVVR 243
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
29-239 |
6.55e-18 |
|
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: 82.76 E-value: 6.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 29 TPALPAAARFADLDMPAELLAALESQGVTVPFPIQAATLPNSLAG--RDVLGRGRTGSGKTLAFGLALLARTagrRAEPG 106
Cdd:cd18048 11 TSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV---DALKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 107 QPLGLVLVPTRELAQQVTDALRPYAR-SVKLRLTAVVGGMSIGRqasALRGGVEVVVATPGRLKD------LIDrgdcrL 179
Cdd:cd18048 88 YPQCLCLSPTFELALQTGKVVEEMGKfCVGIQVIYAIRGNRPGK---GTDIEAQIVIGTPGTVLDwcfklrLID-----V 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2189654348 180 NQVSVTVLDEADQMADM-GFMPQVTALLDQVRPEGQRMLFSATLDRNVDLLVRRYLSDPVV 239
Cdd:cd18048 160 TNISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNI 220
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
82-379 |
3.75e-16 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 80.84 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 82 TGSGKTLaFGLALLART-AGRRAepgqplgLVLVPTRELAQQVTDALRPYarsvkLRLTAVVGGmsigrqasALRGGVEV 160
Cdd:COG1061 109 TGTGKTV-LALALAAELlRGKRV-------LVLVPRRELLEQWAEELRRF-----LGDPLAGGG--------KKDSDAPI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 161 VVATPGRLKDLIDRGDCRlNQVSVTVLDEADQMADMGFmpqvTALLDQVRPegQRML-FSATLDRN-------------- 225
Cdd:COG1061 168 TVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPA--AYRLgLTATPFRSdgreillflfdgiv 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 226 -----VDLLVRRYLSDPVVHSVDPSAG-------AVTTMEHHVLHVHGADKHAATTEIA---ARDGRVLMFLDTKHAVDR 290
Cdd:COG1061 241 yeyslKEAIEDGYLAPPEYYGIRVDLTderaeydALSERLREALAADAERKDKILRELLrehPDDRKTLVFCSSVDHAEA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 291 LTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVDPPSDHKDYLHRGGRTARAG 370
Cdd:COG1061 321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPA 400
|
....*....
gi 2189654348 371 ESGSVVTLV 379
Cdd:COG1061 401 PGKEDALVY 409
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
73-221 |
8.09e-16 |
|
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: 74.36 E-value: 8.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 73 GRDVLGRGRTGSGKTLAFGLALL--ARTAGRRAepgqplgLVLVPTRELAQQVTDALRPYARSvKLRLTAVVGGMSIGRQ 150
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALllLLKKGKKV-------LVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEER 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2189654348 151 ASALRGGVEVVVATPGRLKDLIDRGDC-RLNQVSVTVLDEADQMADMGFMPQVTALLDQ--VRPEGQRMLFSAT 221
Cdd:cd00046 73 EKNKLGDADIIIATPDMLLNLLLREDRlFLKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
274-384 |
2.63e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 72.07 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 274 RDGRVLMFL---DTkhaVDRLTDHLLNSGVRAAALHG--------GKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVD 342
Cdd:COG1111 352 PDSRIIVFTqyrDT---AEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIP 428
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2189654348 343 NLDLVVNVDP-PSDHKdYLHRGGRTARAGEsGSVVTLVTPNQR 384
Cdd:COG1111 429 EVDLVIFYEPvPSEIR-SIQRKGRTGRKRE-GRVVVLIAKGTR 469
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
38-237 |
7.83e-13 |
|
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: 67.44 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 38 FADLDMPAELLAALESQGVTVPFPIQAATLPNSLAG--RDVLGRGRTGSGKTLAFGLALLARTagrraEPGQPLG--LVL 113
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-----EPANKYPqcLCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 114 VPTRELAQQVTDALRPYARSV-KLRLTAVVGGMSIGRqasALRGGVEVVVATPGRLKD------LIDRgdcrlNQVSVTV 186
Cdd:cd18047 78 SPTYELALQTGKVIEQMGKFYpELKLAYAVRGNKLER---GQKISEQIVIGTPGTVLDwcsklkFIDP-----KKIKVFV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2189654348 187 LDEADQM-ADMGFMPQvTALLDQVRPEG-QRMLFSATLDRNVDLLVRRYLSDP 237
Cdd:cd18047 150 LDEADVMiATQGHQDQ-SIRIQRMLPRNcQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
61-370 |
2.61e-10 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 62.42 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 61 PIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTAgrraepgqpLGLVLVPTRELAQQVTDALRPYA------RSV 134
Cdd:PRK11057 28 PGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDG---------LTLVVSPLISLMKDQVDQLLANGvaaaclNST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 135 KLR--LTAVVGGMSIGRqasalrggVEVVVATPGRL--KDLIDR-GDCRLNQVSVtvlDEADQMADMG--FMPQVTAL-- 205
Cdd:PRK11057 99 QTReqQLEVMAGCRTGQ--------IKLLYIAPERLmmDNFLEHlAHWNPALLAV---DEAHCISQWGhdFRPEYAALgq 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 206 LDQVRPEGQRMLFSATLD---RNvDLLVRRYLSDPVVH--SVDPSAGAVTTMEHH------VLHVHGAdkhaatteiaaR 274
Cdd:PRK11057 168 LRQRFPTLPFMALTATADdttRQ-DIVRLLGLNDPLIQisSFDRPNIRYTLVEKFkpldqlMRYVQEQ-----------R 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 275 DGRVLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVDPPS 354
Cdd:PRK11057 236 GKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPR 315
|
330
....*....|....*.
gi 2189654348 355 DHKDYLHRGGRTARAG 370
Cdd:PRK11057 316 NIESYYQETGRAGRDG 331
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
275-384 |
3.72e-10 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 62.20 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 275 DGRVLMFLDTKHAVDRLTDHLLNSGVRAAALHG--------GKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDL 346
Cdd:PRK13766 365 DSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaskdgdkGMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDL 444
|
90 100 110
....*....|....*....|....*....|....*....
gi 2189654348 347 VVNVDP-PSDHKdYLHRGGRTARaGESGSVVTLVTPNQR 384
Cdd:PRK13766 445 VIFYEPvPSEIR-SIQRKGRTGR-QEEGRVVVLIAKGTR 481
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
32-379 |
9.87e-10 |
|
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: 61.00 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 32 LPA-AARFADL--DMPAELLAALESQGVTVPFPIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTA---GRRAep 105
Cdd:COG1205 27 IPArEARYAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLedpGATA-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 106 gqplgLVLVPTRELAQ-QVtDALRPYARSVKLRLTAVV--GGMSIGRQASALRGGvEVVVATPgrlkDLIDRG------- 175
Cdd:COG1205 105 -----LYLYPTKALARdQL-RRLRELAEALGLGVRVATydGDTPPEERRWIREHP-DIVLTNP----DMLHYGllphhtr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 176 ------DCRLnqVsvtVLDEADQ-------------------MADMGFMPQVTALldqvrpegqrmlfSATLDrNVDLLV 230
Cdd:COG1205 174 warffrNLRY--V---VIDEAHTyrgvfgshvanvlrrlrriCRHYGSDPQFILA-------------SATIG-NPAEHA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 231 RRYLSDPVVHsVDPSaGAVTTMEHHVL----HVHGADKHAATTEIA-------ARDGRVLMFLD--------TKHAVDRL 291
Cdd:COG1205 235 ERLTGRPVTV-VDED-GSPRGERTFVLwnppLVDDGIRRSALAEAArlladlvREGLRTLVFTRsrrgaellARYARRAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 292 TDHLLnsGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVDPPSDHKDYLHRGGRTARAGe 371
Cdd:COG1205 313 REPDL--ADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRG- 389
|
....*...
gi 2189654348 372 SGSVVTLV 379
Cdd:COG1205 390 QDSLVVLV 397
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
37-386 |
1.47e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 59.91 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 37 RFADLDmPAELLAALESQGVTVPFPIQAATLPNSL-AGRDVLGRGRTGSGKTlafglaLLARTAGRRAEPGQPLGLVLVP 115
Cdd:COG1204 2 KVAELP-LEKVIEFLKERGIEELYPPQAEALEAGLlEGKNLVVSAPTASGKT------LIAELAILKALLNGGKALYIVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 116 TRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASalrGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMAD 195
Cdd:COG1204 75 LRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWL---GRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHLIDD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 196 MGFMPQVTALLDQVR---PEGQRMLFSATLD------------------RNVDLLV------RRYLSDPVVHSVDPSAGA 248
Cdd:COG1204 152 ESRGPTLEVLLARLRrlnPEAQIVALSATIGnaeeiaewldaelvksdwRPVPLNEgvlydgVLRFDDGSRRSKDPTLAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 249 VttmeHHVLHVHG---------------ADKHA----------ATTEIAARDGRVLMFLDTKHAVDRLTDhLLNSGVraA 303
Cdd:COG1204 232 A----LDLLEEGGqvlvfvssrrdaeslAKKLAdelkrrltpeEREELEELAEELLEVSEETHTNEKLAD-CLEKGV--A 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 304 ALHGGKSQSQRTRTLAQFKTGHVTVLVAT-------NVAARGIHVDNLDLVVNVDPPSDhkDYLHRGGRTARAG--ESGS 374
Cdd:COG1204 305 FHHAGLPSELRRLVEDAFREGLIKVLVATptlaagvNLPARRVIIRDTKRGGMVPIPVL--EFKQMAGRAGRPGydPYGE 382
|
410
....*....|..
gi 2189654348 375 VVtLVTPNQRRA 386
Cdd:COG1204 383 AI-LVAKSSDEA 393
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
275-378 |
2.49e-09 |
|
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: 55.44 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 275 DGRVLMFLDTKHAVDRLTDHLLN--SGVRAAALHG--------GKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNL 344
Cdd:cd18801 30 DTRVIIFSEFRDSAEEIVNFLSKirPGIRATRFIGqasgksskGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEV 109
|
90 100 110
....*....|....*....|....*....|....
gi 2189654348 345 DLVVNVDPPSDHKDYLHRGGRTARaGESGSVVTL 378
Cdd:cd18801 110 DLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVL 142
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
277-372 |
3.61e-09 |
|
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: 55.29 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 277 RVLMFLDTKHAVDRLTDHLLN-----SGVRAAALHGGKSQSQRTR----------TLAQFKTGHVTVLVATNVAARGIHV 341
Cdd:cd18802 27 RGIIFVERRATAVVLSRLLKEhpstlAFIRCGFLIGRGNSSQRKRslmtqrkqkeTLDKFRDGELNLLIATSVLEEGIDV 106
|
90 100 110
....*....|....*....|....*....|.
gi 2189654348 342 DNLDLVVNVDPPSDHKDYLHRGGRtARAGES 372
Cdd:cd18802 107 PACNLVIRFDLPKTLRSYIQSRGR-ARAPNS 136
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
327-380 |
5.22e-08 |
|
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: 50.01 E-value: 5.22e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2189654348 327 TVLVATNVAARGIHVDNLDLVVNVDPPSDHKDYLHRGGRTARAGESGSVVTLVT 380
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
82-190 |
9.83e-08 |
|
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: 52.27 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 82 TGSGKTL-AfglALLARTAG---RRAEPGQPLGLVLVPTRELAQQVTDALRPYarsVKLRLTAVVGGMSIGRQASALRGG 157
Cdd:cd18034 25 TGSGKTLiA---VMLIKEMGelnRKEKNPKKRAVFLVPTVPLVAQQAEAIRSH---TDLKVGEYSGEMGVDKWTKERWKE 98
|
90 100 110
....*....|....*....|....*....|....*..
gi 2189654348 158 V----EVVVATPGRLKDLIDRGDCRLNQVSVTVLDEA 190
Cdd:cd18034 99 ElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
82-195 |
2.63e-07 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 50.72 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 82 TGSGKTLAFGLALLA--RTAGRRAepgqplgLVLVPTRELAQQVTDALRPYARSVKLRLTAVVGGMSIGRQASALRggvE 159
Cdd:cd17921 26 TSSGKTLIAELAILRalATSGGKA-------VYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSVNKLLLAEA---D 95
|
90 100 110
....*....|....*....|....*....|....*..
gi 2189654348 160 VVVATPGRLKDLIDRG-DCRLNQVSVTVLDEADQMAD 195
Cdd:cd17921 96 ILVATPEKLDLLLRNGgERLIQDVRLVVVDEAHLIGD 132
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
284-381 |
2.65e-07 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 52.84 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 284 TKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNvaARGIHVD--NLDLVVNVDPPSDHKDYLH 361
Cdd:COG0514 239 SRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AFGMGIDkpDVRFVIHYDLPKSIEAYYQ 316
|
90 100
....*....|....*....|
gi 2189654348 362 RGGRTARAGESGSVVTLVTP 381
Cdd:COG0514 317 EIGRAGRDGLPAEALLLYGP 336
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
244-379 |
3.31e-07 |
|
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: 49.57 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 244 PSAGAVTTMEHHVlhvhGADKHAATTEIAARDGRVLMFLDTKHAVDRLTDHLLN------SGVRAAALHGGKSQSQRTRT 317
Cdd:cd18796 11 PVAPEIFPWAGES----GADAYAEVIFLLERHKSTLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2189654348 318 LAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVDPPSDHKDYLHRGGRTARAGESGSVVTLV 379
Cdd:cd18796 87 EAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLV 148
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
284-371 |
2.41e-06 |
|
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: 46.82 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 284 TKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVDPPSDHKDYLHRG 363
Cdd:cd18794 39 SRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQES 118
|
....*...
gi 2189654348 364 GRTARAGE 371
Cdd:cd18794 119 GRAGRDGL 126
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
82-190 |
1.42e-05 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 44.99 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 82 TGSGKTLaFGLALLARTAGRRAepgqplgLVLVPTRELAQQvtdalrPYARSVKLRLTAVVGGMSIGRQASALrgGVEVV 161
Cdd:cd17926 27 TGSGKTL-TALALIAYLKELRT-------LIVVPTDALLDQ------WKERFEDFLGDSSIGLIGGGKKKDFD--DANVV 90
|
90 100
....*....|....*....|....*....
gi 2189654348 162 VATPGRLKDLIDRGDCRLNQVSVTVLDEA 190
Cdd:cd17926 91 VATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
61-240 |
2.97e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 44.83 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 61 PIQAATLPNSLAGRDVLGRGRTGSGKTLAFGLALLARTagrraepgqPLGLVLVPTRELAQ-QVtDALRpyARSVklRLT 139
Cdd:cd17920 15 PGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLD---------GVTLVVSPLISLMQdQV-DRLQ--QLGI--RAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 140 AVVGGMSIGRQASAL----RGGVEVVVATPGRL-----KDLIDRgDCRLNQVSVTVLDEA--------DQMADMGFMPQV 202
Cdd:cd17920 81 ALNSTLSPEEKREVLlrikNGQYKLLYVTPERLlspdfLELLQR-LPERKRLALIVVDEAhcvsqwghDFRPDYLRLGRL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2189654348 203 TALLDQVrpegQRMLFSATLDRNV--DLLVRRYLSDPVVH 240
Cdd:cd17920 160 RRALPGV----PILALTATATPEVreDILKRLGLRNPVIF 195
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
63-190 |
3.93e-05 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; 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. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 44.11 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 63 QAATLPNSLAGRDVLGRGRTGSGKTLAFGLAL---LARTAGRRAepgqplgLVLVPTRELAQQVTDALRPYARSV--KLR 137
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPIleaLLRDPGSRA-------LYLYPTKALAQDQLRSLRELLEQLglGIR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2189654348 138 LTAVVGGMSIGRQASALRGGVEVVVATPGRLKDLIDRGDCR----LNQVSVTVLDEA 190
Cdd:cd17923 78 VATYDGDTPREERRAIIRNPPRILLTNPDMLHYALLPHHDRwarfLRNLRYVVLDEA 134
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
273-373 |
3.96e-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: 43.78 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 273 ARDGRVLMFLDTKHAVDRLTDHLLnsgvrAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVdp 352
Cdd:cd18789 47 EQGDKIIVFTDNVEALYRYAKRLL-----KPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQI-- 119
|
90 100
....*....|....*....|....*
gi 2189654348 353 pSDH----KDYLHRGGRTARAGESG 373
Cdd:cd18789 120 -SGHggsrRQEAQRLGRILRPKKGG 143
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
60-222 |
4.58e-05 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 43.86 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 60 FPIQAATLPNSLA-GRDVLGRGRTGSGKTLAFGLALLARTA-GRRAepgqplgLVLVPTRELAQQvtdalrPYARSVKLR 137
Cdd:cd18028 3 YPPQAEAVRAGLLkGENLLISIPTASGKTLIAEMAMVNTLLeGGKA-------LYLVPLRALASE------KYEEFKKLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 138 LTAVVGGMSIG--RQASALRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTALLDQVR---PE 212
Cdd:cd18028 70 EIGLKVGISTGdyDEDDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnPN 149
|
170
....*....|
gi 2189654348 213 GQRMLFSATL 222
Cdd:cd18028 150 TQIIGLSATI 159
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
270-353 |
8.50e-05 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 45.22 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 270 EIAARDGRVLMFldTKHA--VDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVT--VLVATNVAARGIhvdNL- 344
Cdd:COG0553 544 ELLAEGEKVLVF--SQFTdtLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGL---NLt 618
|
90
....*....|.
gi 2189654348 345 --DLVVNVDPP 353
Cdd:COG0553 619 aaDHVIHYDLW 629
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
270-353 |
1.58e-04 |
|
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: 41.69 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 270 EIAARDGRVLMF---LDTkhaVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKT--GHVTVLVATNVAARGIhvdNL 344
Cdd:cd18793 22 ELREPGEKVLIFsqfTDT---LDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGVGL---NL 95
|
90
....*....|..
gi 2189654348 345 ---DLVVNVDPP 353
Cdd:cd18793 96 taaNRVILYDPW 107
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
73-341 |
2.62e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 43.33 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 73 GRDVLGRGRTGSGKTLafglalLARTAGRRAEPGQPLGLVLVPTRELAQQVTDALRPYaRSVKLRLTavvggMSIGRQAS 152
Cdd:PRK01172 37 GENVIVSVPTAAGKTL------IAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELSRL-RSLGMRVK-----ISIGDYDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 153 A--LRGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQMADMGFMPQVTALLDQVR---PEGQRMLFSATLDrNVD 227
Cdd:PRK01172 105 PpdFIKRYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSARyvnPDARILALSATVS-NAN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 228 LLVRRYLSDPVVHSVDPSAGAVTTMEHHVLHVHG-----ADKHAATTEIAARDGRVLMFLDTKHAVDRLT---------- 292
Cdd:PRK01172 184 ELAQWLNASLIKSNFRPVPLKLGILYRKRLILDGyersqVDINSLIKETVNDGGQVLVFVSSRKNAEDYAemliqhfpef 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2189654348 293 -------------DHLLNSGVR--AAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHV 341
Cdd:PRK01172 264 ndfkvssennnvyDDSLNEMLPhgVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNL 327
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
277-379 |
4.24e-04 |
|
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: 40.70 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 277 RVLMFLDTKHAVDRLTDHLLNSGVRAAAL-------HGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVN 349
Cdd:cd18797 37 KTIVFCRSRKLAELLLRYLKARLVEEGPLaskvasyRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
|
90 100 110
....*....|....*....|....*....|
gi 2189654348 350 VDPPSDHKDYLHRGGRTARAGEsGSVVTLV 379
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGK-DSLVILV 145
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
39-221 |
4.47e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 42.64 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 39 ADLDMPAELLAALESQGVTVPFPIQAATLPNSLA-GRDVLGRGRTGSGKTLAFGLALLARTA-GRRAepgqplgLVLVPT 116
Cdd:PRK02362 4 AELPLPEGVIEFYEAEGIEELYPPQAEAVEAGLLdGKNLLAAIPTASGKTLIAELAMLKAIArGGKA-------LYIVPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 117 RELAqqvTDALRPYARSVKLRLTAvvgGMSIG---RQASALrGGVEVVVATPGRLKDLIDRGDCRLNQVSVTVLDEADQM 193
Cdd:PRK02362 77 RALA---SEKFEEFERFEELGVRV---GISTGdydSRDEWL-GDNDIIVATSEKVDSLLRNGAPWLDDITCVVVDEVHLI 149
|
170 180 190
....*....|....*....|....*....|.
gi 2189654348 194 --ADMGFMPQVT-ALLDQVRPEGQRMLFSAT 221
Cdd:PRK02362 150 dsANRGPTLEVTlAKLRRLNPDLQVVALSAT 180
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
282-390 |
1.03e-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: 39.63 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 282 LDTKHAVD---RLTDHLLNSgVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVNVDPPSDHKD 358
Cdd:cd18811 42 LDLKAAVAmyeYLKERFRPE-LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLS 120
|
90 100 110
....*....|....*....|....*....|....*
gi 2189654348 359 YLHR-GGRTARaGESGSVVTLV--TPNQRRAMTRL 390
Cdd:cd18811 121 QLHQlRGRVGR-GDHQSYCLLVykDPLTETAKQRL 154
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
74-164 |
1.49e-03 |
|
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: 39.71 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 74 RDVLGRGRTGSGKTLAFGL-ALLARTAGRRAepgqplgLVLVPTRELAQQVTDALRPYARSVKLRLtavvggMSIGRQAS 152
Cdd:cd17918 37 MDRLLSGDVGSGKTLVALGaALLAYKNGKQV-------AILVPTEILAHQHYEEARKFLPFINVEL------VTGGTKAQ 103
|
90
....*....|..
gi 2189654348 153 ALRgGVEVVVAT 164
Cdd:cd17918 104 ILS-GISLLVGT 114
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
270-400 |
1.54e-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: 39.15 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 270 EIAARDGRVLMFLDTKHAVDRLTDHLLNSGVRAAALHGGKSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVVN 349
Cdd:cd18790 22 KRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAI 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2189654348 350 VDP-----PSDHKDYLHRGGRTARaGESGSVV------------TLVTPNQRRAMTRLMTTA-GIVPQT 400
Cdd:cd18790 102 LDAdkegfLRSETSLIQTIGRAAR-NVNGKVIlyadkitdsmqkAIEETERRREIQMEYNEEhGITPKT 169
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
82-190 |
2.41e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.81 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 82 TGSGKTL-AFGLALLARTAG--RRAepgqplgLVLVPTRELAQQVTDALRPYARSvklrlTAVVGGMSIGRQASALRGGV 158
Cdd:pfam04851 32 TGSGKTLtAAKLIARLFKKGpiKKV-------LFLVPRKDLLEQALEEFKKFLPN-----YVEIGEIISGDKKDESVDDN 99
|
90 100 110
....*....|....*....|....*....|....
gi 2189654348 159 EVVVATPGRLKDLIDRGDCRL--NQVSVTVLDEA 190
Cdd:pfam04851 100 KIVVTTIQSLYKALELASLELlpDFFDVIIIDEA 133
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
82-174 |
6.76e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 37.69 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 82 TGSGKTlAFGL--ALLARTAGRRAepgqplgLVLVPTRELAQQVTDALRPYARS--VKLRLTAVVGGMSIGRQASALR-- 155
Cdd:cd17924 41 TGVGKT-TFGLatSLYLASKGKRS-------YLIFPTKSLVKQAYERLSKYAEKagVEVKILVYHSRLKKKEKEELLEki 112
|
90 100
....*....|....*....|.
gi 2189654348 156 --GGVEVVVATPGRLKDLIDR 174
Cdd:cd17924 113 ekGDFDILVTTNQFLSKNFDL 133
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
309-376 |
8.22e-03 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350191 [Multi-domain] Cd Length: 238 Bit Score: 37.99 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 309 KSQSQRTRTLAQFKTGHVTVLVATNVAARGIHVDNLDLVV--NVDPPSDHKDY---------LHR-GGRTARAGESGSVV 376
Cdd:cd18804 128 RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGilNADSGLNSPDFraserafqlLTQvSGRAGRGDKPGKVI 207
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
82-190 |
8.69e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 37.11 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189654348 82 TGSGKTLafgLALLArTAGRRAEPGQPLgLVLVPTRELAQQVTDALRPYARSvKLRLTAVVGGMSIGRQASALRGGvEVV 161
Cdd:cd18035 25 TGLGKTI---IAILV-AADRLTKKGGKV-LILAPSRPLVEQHAENLKRVLNI-PDKITSLTGEVKPEERAERWDAS-KII 97
|
90 100
....*....|....*....|....*....
gi 2189654348 162 VATPGRLKDLIDRGDCRLNQVSVTVLDEA 190
Cdd:cd18035 98 VATPQVIENDLLAGRITLDDVSLLIFDEA 126
|
|
| |
