|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
119-487 |
1.65e-167 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 483.50 E-value: 1.65e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 119 ADLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIikfnaKHGRGKNPQCLVLAP 198
Cdd:COG0513 5 ADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-----DPSRPRAPQALILAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 199 TRELARQVEKEFRE--SAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQ 276
Cdd:COG0513 80 TRELALQVAEELRKlaKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 277 VGFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTIDLvgDSDQKLADGITMYSIAADSYGRASIIGPLVK 356
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEV--APENATAETIEQRYYLVDKRDKLELLRRLLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 357 EHGkGGKCIVFTQTKRDADRLAFGLAKS-YKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLVIHY 435
Cdd:COG0513 238 DED-PERAIVFCNTKRGADRLAEKLQKRgISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15228722 436 ELPNNTETFVHRTGRTGRAGKKGSAILIHGQDQTRAVKMIEKEVGSRFNELP 487
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEE 368
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
117-488 |
2.64e-102 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 317.90 E-value: 2.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 117 AIADLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIikfNAKHGRgknPQCLVL 196
Cdd:PRK11776 5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL---DVKRFR---VQALVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 197 APTRELARQVEKEFRESAPSLD-----TIClyGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEA 271
Cdd:PRK11776 79 CPTRELADQVAKEIRRLARFIPnikvlTLC--GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 272 DQMLQVGFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTIDLVGDSDqklADGITMYSIAADSYGRASII 351
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHD---LPAIEQRFYEVSPDERLPAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 352 GPLVKEHgKGGKCIVFTQTKRDADRLAFGL-AKSYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVD 430
Cdd:PRK11776 234 QRLLLHH-QPESCVVFCNTKKECQEVADALnAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 431 LVIHYELPNNTETFVHRTGRTGRAGKKGSAILIHGQDQTRAVKMIEKEVGSRFN--ELPS 488
Cdd:PRK11776 313 AVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNwePLPS 372
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
127-322 |
4.30e-98 |
|
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: 297.43 E-value: 4.30e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRGknPQCLVLAPTRELARQV 206
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRG--PQALVLAPTRELAMQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 207 EKEFRE--SAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVE 284
Cdd:cd00268 79 AEVARKlgKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 15228722 285 IILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTID 322
Cdd:cd00268 159 KILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
119-477 |
2.57e-90 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 292.14 E-value: 2.57e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 119 ADLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIikfnakHGRGKNPQCLVLAP 198
Cdd:PRK11634 9 ADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL------DPELKAPQILVLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 199 TRELARQVEK---EFRESAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQML 275
Cdd:PRK11634 83 TRELAVQVAEamtDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 276 QVGFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTIdlvgdsdqKLADGITMYSIAADSYGraSIIG--- 352
Cdd:PRK11634 163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEV--------RIQSSVTTRPDISQSYW--TVWGmrk 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 353 --PLVK--EHGKGGKCIVFTQTKRDADRLAFGLAKS-YKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVP 427
Cdd:PRK11634 233 neALVRflEAEDFDAAIIFVRTKNATLEVAEALERNgYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVE 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15228722 428 NVDLVIHYELPNNTETFVHRTGRTGRAGKKGSAILIHGQDQTRAVKMIEK 477
Cdd:PRK11634 313 RISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIER 362
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
121-492 |
1.69e-86 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 276.69 E-value: 1.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 121 LGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKfNAKHGRGKNP-QCLVLAPT 199
Cdd:PRK10590 6 LGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLIT-RQPHAKGRRPvRALILTPT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 200 RELARQVEKEFRESAPSLD--TICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQV 277
Cdd:PRK10590 85 RELAAQIGENVRDYSKYLNirSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 278 GFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTIDLV---GDSDQkladgITMYSIAADSYGRASIIGPL 354
Cdd:PRK10590 165 GFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVArrnTASEQ-----VTQHVHFVDKKRKRELLSQM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 355 VKEhGKGGKCIVFTQTKRDADRLAFGLAKS-YKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLVI 433
Cdd:PRK10590 240 IGK-GNWQQVLVFTRTKHGANHLAEQLNKDgIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15228722 434 HYELPNNTETFVHRTGRTGRAGKKGSAILIHGQDQTRAVKMIEKEVGsrfNELPSIAVE 492
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK---KEIPRIAIP 374
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
119-461 |
8.28e-82 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 263.37 E-value: 8.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 119 ADLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRGKN-PQCLVLA 197
Cdd:PRK04837 11 SDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRKVNqPRALIMA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 198 PTRELARQVEKEFRESAPS--LDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQML 275
Cdd:PRK04837 91 PTRELAVQIHADAEPLAQAtgLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 276 QVGFAEDVEIILQKLPA--KRQSMMFSATMPSWIRSLTKKYLNNPLTIDLvgDSDQKLADGIT---MYSIAADsygRASI 350
Cdd:PRK04837 171 DLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEV--EPEQKTGHRIKeelFYPSNEE---KMRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 351 IGPLVKEHGKgGKCIVFTQTKrdadrlafglaksYKCEALH--------------GDISQAQRERTLAGFRDGNFSILVA 416
Cdd:PRK04837 246 LQTLIEEEWP-DRAIIFANTK-------------HRCEEIWghlaadghrvglltGDVAQKKRLRILEEFTRGDLDILVA 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15228722 417 TDVAARGLDVPNVDLVIHYELPNNTETFVHRTGRTGRAGKKGSAI 461
Cdd:PRK04837 312 TDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSI 356
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
127-498 |
2.18e-78 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 258.16 E-value: 2.18e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPiidKIIKFNAKH--GRGKNPQCLVLAPTRELAR 204
Cdd:PTZ00110 141 ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLP---AIVHINAQPllRYGDGPIVLVLAPTRELAE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 205 QVEKEFRESAPS--LDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAED 282
Cdd:PTZ00110 218 QIREQCNKFGASskIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 283 VEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNN-PLTIDlVGDSDQKLADGITMYSIAADSYGRASIIGPLVKEHGK- 360
Cdd:PTZ00110 298 IRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVN-VGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRd 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 361 GGKCIVFTQTKRDADRLAFGL-AKSYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLVIHYELPN 439
Cdd:PTZ00110 377 GDKILIFVETKKGADFLTKELrLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPN 456
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228722 440 NTETFVHRTGRTGRAGKKGSAILIHGQDQTRA----VKMIEKEVGSRFNELPSIAVERGSASM 498
Cdd:PTZ00110 457 QIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLardlVKVLREAKQPVPPELEKLSNERSNGTE 519
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
119-477 |
4.53e-78 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 254.10 E-value: 4.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 119 ADLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKH-GRgknPQCLVLA 197
Cdd:PRK11192 4 SELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKsGP---PRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 198 PTRELARQVEKEFRESAP--SLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQML 275
Cdd:PRK11192 81 PTRELAMQVADQARELAKhtHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 276 QVGFAEDVEIILQKLPAKRQSMMFSATMP-SWIRSLTKKYLNNPLTIDlvGDSDQKLADGITMYSIAADSY--GRASIIG 352
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVE--AEPSRRERKKIHQWYYRADDLehKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 353 PLVKEHGKggKCIVFTQTKRDADRLAFGLAKS-YKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDL 431
Cdd:PRK11192 239 LLKQPEVT--RSIVFVRTRERVHELAGWLRKAgINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSH 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15228722 432 VIHYELPNNTETFVHRTGRTGRAGKKGSAI-LIHGQDQtravKMIEK 477
Cdd:PRK11192 317 VINFDMPRSADTYLHRIGRTGRAGRKGTAIsLVEAHDH----LLLGK 359
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
120-487 |
9.20e-76 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 249.44 E-value: 9.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 120 DLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRGK-NPQCLVLAP 198
Cdd:PRK01297 91 DFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERYMgEPRALIIAP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 199 TRELARQVEKEFRE--SAPSLDTICLYGGTPIGQQMRELNYG-IDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQML 275
Cdd:PRK01297 171 TRELVVQIAKDAAAltKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRML 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 276 QVGFAEDVEIILQKLPAK--RQSMMFSATMPSWIRSLTKKYLNNPLTIDLvgDSDQKLADGIT--MYSIA-ADSYgraSI 350
Cdd:PRK01297 251 DMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEI--EPENVASDTVEqhVYAVAgSDKY---KL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 351 IGPLVKEHGkGGKCIVFTQTKRDADRLAFGLAKS-YKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNV 429
Cdd:PRK01297 326 LYNLVTQNP-WERVMVFANRKDEVRRIEERLVKDgINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15228722 430 DLVIHYELPNNTETFVHRTGRTGRAGKKGSAILIHGQDQTRAVKMIEKEVGSRFN-ELP 487
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIScEMP 463
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
120-487 |
9.82e-72 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 236.26 E-value: 9.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 120 DLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKI-IKFNAkhgrgknPQCLVLAP 198
Cdd:PTZ00424 32 ALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIdYDLNA-------CQALILAP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 199 TRELARQVEKEFRESAPSLDTIC--LYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQ 276
Cdd:PTZ00424 105 TRELAQQIQKVVLALGDYLKVRChaCVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 277 VGFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTIdLVgDSDQKLADGITMYSIAADS--YGRASIIGpl 354
Cdd:PTZ00424 185 RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRI-LV-KKDELTLEGIRQFYVAVEKeeWKFDTLCD-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 355 VKEHGKGGKCIVFTQTKRDADRLAFGLA-KSYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLVI 433
Cdd:PTZ00424 261 LYETLTITQAIIYCNTRRKVDYLTKKMHeRDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVI 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15228722 434 HYELPNNTETFVHRTGRTGRAGKKGSAILIHGQDQTRAVKMIEKEVGSRFNELP 487
Cdd:PTZ00424 341 NYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMP 394
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
116-461 |
1.25e-65 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 225.21 E-value: 1.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 116 LAIADLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRG-KNPQCL 194
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKpEDPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 195 VLAPTRELARQVEKEFRESAPSLDT--ICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKR-GALNLSEVQFVVLDEA 271
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLrfALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 272 DQMLQVGFAEDVEIILQKLPAK--RQSMMFSATMPSWIRSLTKKYLNNPltidlvgdsdQKL---ADGITMYSI------ 340
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEP----------EKLvveTETITAARVrqriyf 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 341 AADSYGRASIIGPLVKEhgKGGKCIVFTQTKRDADRLAFGLAKS-YKCEALHGDISQAQRERTLAGFRDGNFSILVATDV 419
Cdd:PRK04537 239 PADEEKQTLLLGLLSRS--EGARTMVFVNTKAFVERVARTLERHgYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDV 316
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15228722 420 AARGLDVPNVDLVIHYELPNNTETFVHRTGRTGRAGKKGSAI 461
Cdd:PRK04537 317 AARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAI 358
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
128-315 |
8.56e-65 |
|
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: 211.24 E-value: 8.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 128 VKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRGKNPQCLVLAPTRELARQVE 207
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 208 KEFRESAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVEIIL 287
Cdd:cd17944 82 KDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIL 161
|
170 180 190
....*....|....*....|....*....|...
gi 15228722 288 QKLPAKR-----QSMMFSATMPSWIRSLTKKYL 315
Cdd:cd17944 162 SVSYKKDsednpQTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
123-316 |
2.41e-60 |
|
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: 199.73 E-value: 2.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 123 ISPEIVKALKGRGIEKLFPIQKAVLEPAME-GRDMIGRARTGTGKTLAFGIPIIDKIIKfNAKHGRGKNPQCLVLAPTRE 201
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLN-TKPAGRRSGVSALIISPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 202 LARQVEKEFRE---SAPSLDTICLYGGTPIGQQMREL-NYGIDVAVGTPGRIIDLMK--RGALNLSEVQFVVLDEADQML 275
Cdd:cd17964 80 LALQIAAEAKKllqGLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15228722 276 QVGFAEDVEIILQKLPAK----RQSMMFSATMPSWIRSLTKKYLN 316
Cdd:cd17964 160 DMGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
127-321 |
2.77e-57 |
|
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: 191.43 E-value: 2.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKfNAKHGRGKNPQCLVLAPTRELARQV 206
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINA-QPPLERGDGPIVLVLAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 207 EKEFRESAPS--LDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVE 284
Cdd:cd17966 80 QQEANKFGGSsrLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 15228722 285 IILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
119-325 |
3.28e-57 |
|
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: 191.93 E-value: 3.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 119 ADLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIK----FNAKHGRGKNPQCL 194
Cdd:cd17967 3 EEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEdgppSVGRGRRKAYPSAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 195 VLAPTRELARQVEKEFRESapSLDTI----CLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDE 270
Cdd:cd17967 83 ILAPTRELAIQIYEEARKF--SYRSGvrsvVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228722 271 ADQMLQVGFAEDVEIILQK--LPAK--RQSMMFSATMPSWIRSLTKKYLNNP--LTIDLVG 325
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdMPPKgeRQTLMFSATFPREIQRLAADFLKNYifLTVGRVG 221
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
127-321 |
2.55e-56 |
|
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: 189.45 E-value: 2.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRGKN--PQCLVLAPTRELAR 204
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKDdgPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 205 QVEKEFRE--SAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAED 282
Cdd:cd17945 81 QIEEETQKfaKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15228722 283 VEIILQKLP--------------------AKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17945 161 VTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
141-310 |
6.15e-56 |
|
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: 186.29 E-value: 6.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 141 PIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIikfnakHGRGKNPQCLVLAPTRELARQVEKEFRESAPSLD-- 218
Cdd:pfam00270 2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL------DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGlk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 219 TICLYGGTPIGQQMRELNyGIDVAVGTPGRIIDLMKRgALNLSEVQFVVLDEADQMLQVGFAEDVEIILQKLPAKRQSMM 298
Cdd:pfam00270 76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 15228722 299 FSATMPSWIRSL 310
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
121-321 |
7.70e-55 |
|
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: 185.66 E-value: 7.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 121 LGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKII-KFNAKHGRGknPQCLVLAPT 199
Cdd:cd17953 17 CGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKdQRPVKPGEG--PIGLIMAPT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 200 RELARQVEKEFRE--SAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGA---LNLSEVQFVVLDEADQM 274
Cdd:cd17953 95 RELALQIYVECKKfsKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNLRRVTYVVLDEADRM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15228722 275 LQVGFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17953 175 FDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
116-462 |
9.24e-55 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 194.24 E-value: 9.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 116 LAIADLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKH-GRGKNPQCL 194
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHpSEQRNPLAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 195 VLAPTRELARQVEKEFRESAPSL--DTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEAD 272
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLpfKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 273 QMLQVGFAEDVEIILQKLPaKRQSMMFSATMPSWIRSLTKKYLNNPLTIDlVGDSDQKlADGITMYSIAADSYGRASIIG 352
Cdd:PLN00206 281 CMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILIS-IGNPNRP-NKAVKQLAIWVETKQKKQKLF 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 353 PLV--KEHGKgGKCIVFTQTKRDADRL--AFGLAKSYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPN 428
Cdd:PLN00206 358 DILksKQHFK-PPAVVFVSSRLGADLLanAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
|
330 340 350
....*....|....*....|....*....|....
gi 15228722 429 VDLVIHYELPNNTETFVHRTGRTGRAGKKGSAIL 462
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIV 470
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
119-321 |
4.40e-54 |
|
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: 182.90 E-value: 4.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 119 ADLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIkfnakhgrgKNPQ---CLV 195
Cdd:cd17954 3 KELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALL---------ENPQrffALV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 196 LAPTRELARQVEKEFRE--SAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKR-GALNLSEVQFVVLDEAD 272
Cdd:cd17954 74 LAPTRELAQQISEQFEAlgSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEAD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15228722 273 QMLQVGFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17954 154 RLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
131-322 |
1.85e-53 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 181.15 E-value: 1.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 131 LKGRGIEKLFPIQKAVLEPAMEG-RDMIGRARTGTGKTLAFGIPIIDKIIkfnakhgRGKNPQCLVLAPTRELARQVEKE 209
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-------RGKGGRVLVLVPTRELAEQWAEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 210 FRESAPSLD--TICLYGGTPIGQQMRELNYG-IDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVEII 286
Cdd:smart00487 74 LKKLGPSLGlkVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 15228722 287 LQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTID 322
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFID 189
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
354-463 |
1.28e-52 |
|
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: 176.54 E-value: 1.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 354 LVKEHGKGGKCIVFTQTKRDADRLAFGLAK-SYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLV 432
Cdd:cd18787 20 LLLEKLKPGKAIIFVNTKKRVDRLAELLEElGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVDHV 99
|
90 100 110
....*....|....*....|....*....|.
gi 15228722 433 IHYELPNNTETFVHRTGRTGRAGKKGSAILI 463
Cdd:cd18787 100 INYDLPRDAEDYVHRIGRTGRAGRKGTAITF 130
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
120-322 |
1.39e-52 |
|
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: 178.67 E-value: 1.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 120 DLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIdKIIKFNAKhgrgkNPQCLVLAPT 199
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGAL-QRIDTTVR-----ETQALVLAPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 200 RELARQVEKEFRESAPSLD--TICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQV 277
Cdd:cd17939 75 RELAQQIQKVVKALGDYMGvkVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15228722 278 GFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTID 322
Cdd:cd17939 155 GFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
116-325 |
4.78e-52 |
|
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: 179.78 E-value: 4.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 116 LAIADLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKF---NAKHGRGKNPQ 192
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltASSFSEVQEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 193 CLVLAPTRELARQVEKEFRESA--PSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDE 270
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSygTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228722 271 ADQMLQVGFAEDVEIILQKL--PAK--RQSMMFSATMPSWIRSLTKKYLNNP---LTIDLVG 325
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEPgmPSKedRQTLMFSATFPEEIQRLAAEFLKEDylfLTVGRVG 264
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
120-321 |
1.01e-51 |
|
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: 176.72 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 120 DLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIikfNAKHgrgKNPQCLVLAPT 199
Cdd:cd17940 3 DYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI---DPKK---DVIQALILVPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 200 RELARQVEKEFRESAPSLDTICL--YGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQV 277
Cdd:cd17940 77 RELALQTSQVCKELGKHMGVKVMvtTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15228722 278 GFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
127-322 |
8.49e-51 |
|
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: 173.98 E-value: 8.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRGKnpqCLVLAPTRELARQV 206
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATR---VLVLVPTRELAMQC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 207 EKEFRESAPSLD-TICL-YGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRG-ALNLSEVQFVVLDEADQMLQVGFAEDV 283
Cdd:cd17947 78 FSVLQQLAQFTDiTFALaVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADEL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 15228722 284 EIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTID 322
Cdd:cd17947 158 KEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
121-321 |
4.90e-50 |
|
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: 172.10 E-value: 4.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 121 LGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHG-RGknpqcLVLAPT 199
Cdd:cd17959 6 MGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGaRA-----LILSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 200 RELARQVEKEFRESA--PSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQV 277
Cdd:cd17959 81 RELALQTLKVTKELGkfTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15228722 278 GFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
118-319 |
1.32e-48 |
|
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: 168.17 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 118 IADLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIikfnakhgrGKNPQ---CL 194
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL---------SEDPYgifAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 195 VLAPTRELARQVEKEFRE--SAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMK---RGALNLSEVQFVVLD 269
Cdd:cd17955 72 VLTPTRELAYQIAEQFRAlgAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15228722 270 EADQMLQVGFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPL 319
Cdd:cd17955 152 EADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
127-321 |
1.99e-48 |
|
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: 167.59 E-value: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHgRGKNPQCLVLAPTRELARQV 206
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELE-KGEGPIAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 207 EKEFRESAP--SLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVE 284
Cdd:cd17952 80 YLEAKKFGKayNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 15228722 285 IILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
127-303 |
8.00e-48 |
|
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: 167.42 E-value: 8.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAM-EGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRG---KNPQCLVLAPTREL 202
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGgkqKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 203 ARQVEKEFRESA--PSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRG---ALNLSEVQFVVLDEADQMLQV 277
Cdd:cd17946 81 AVQVKDHLKAIAkyTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 15228722 278 GFAEDVEIILQKLPA-------KRQSMMFSATM 303
Cdd:cd17946 161 GHFAELEKILELLNKdragkkrKRQTFVFSATL 193
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
125-323 |
2.19e-47 |
|
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: 165.06 E-value: 2.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 125 PEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRGKNPQCLVLAPTRELAR 204
Cdd:cd17961 3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQGTRALILVPTRELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 205 QVEKEFRE----SAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGAL-NLSEVQFVVLDEADQMLQVGF 279
Cdd:cd17961 83 QVSKVLEQltayCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15228722 280 AEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTIDL 323
Cdd:cd17961 163 EEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
127-322 |
4.16e-47 |
|
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: 164.43 E-value: 4.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPII----DKIIKFNAKHGRGknPQCLVLAPTREL 202
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfalEQEKKLPFIKGEG--PYGLIVCPSREL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 203 ARQ--------VEKEFRESAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQM 274
Cdd:cd17951 79 ARQthevieyyCKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15228722 275 LQVGFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTID 322
Cdd:cd17951 159 IDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
141-317 |
1.23e-46 |
|
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: 164.44 E-value: 1.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 141 PIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKF---------NAKHGRGKN-PQCLVLAPTRELARQVEKEF 210
Cdd:cd18051 46 PVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslpseSGYYGRRKQyPLALVLAPTRELASQIYDEA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 211 RE-SAPSLDTIC-LYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVEIILQ 288
Cdd:cd18051 126 RKfAYRSRVRPCvVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVE 205
|
170 180 190
....*....|....*....|....*....|...
gi 15228722 289 K--LPAK--RQSMMFSATMPSWIRSLTKKYLNN 317
Cdd:cd18051 206 QdtMPPTgeRQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
120-321 |
4.19e-46 |
|
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: 161.46 E-value: 4.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 120 DLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKI-IKFNAkhgrgknPQCLVLAP 198
Cdd:cd18046 3 DMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIdTSLKA-------TQALVLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 199 TRELARQVEKEFRESAPSLDTICL--YGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQ 276
Cdd:cd18046 76 TRELAQQIQKVVMALGDYMGIKCHacIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15228722 277 VGFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
141-323 |
5.57e-46 |
|
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: 162.49 E-value: 5.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 141 PIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPiidKIIKFNAKH--GRGKNPQCLVLAPTRELARQVEKEFRE--SAPS 216
Cdd:cd18049 49 AIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLP---AIVHINHQPflERGDGPICLVLAPTRELAQQVQQVAAEygRACR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 217 LDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVEIILQKLPAKRQS 296
Cdd:cd18049 126 LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQT 205
|
170 180
....*....|....*....|....*..
gi 15228722 297 MMFSATMPSWIRSLTKKYLNNPLTIDL 323
Cdd:cd18049 206 LMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
127-321 |
1.22e-45 |
|
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: 159.94 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRGKNPQCLVLAPTRELARQV 206
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 207 EKEFRE-SAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVEI 285
Cdd:cd17958 81 EAECSKySYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 15228722 286 ILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17958 161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
141-323 |
1.46e-45 |
|
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: 162.49 E-value: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 141 PIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIiKFNAKHGRGKNPQCLVLAPTRELARQVEKEFRESAPS--LD 218
Cdd:cd18050 87 PIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI-NHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSsrLK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 219 TICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVEIILQKLPAKRQSMM 298
Cdd:cd18050 166 STCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLM 245
|
170 180
....*....|....*....|....*
gi 15228722 299 FSATMPSWIRSLTKKYLNNPLTIDL 323
Cdd:cd18050 246 WSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
120-321 |
2.14e-45 |
|
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: 159.82 E-value: 2.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 120 DLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIikfnaKHGRGKnPQCLVLAPT 199
Cdd:cd17950 6 DFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL-----EPVDGQ-VSVLVICHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 200 RELARQVEKEF-RESA--PSLDTICLYGGTPIGQQMREL-NYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQML 275
Cdd:cd17950 80 RELAFQISNEYeRFSKymPNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKML 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15228722 276 -QVGFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17950 160 eQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
127-318 |
9.41e-45 |
|
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: 157.43 E-value: 9.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKhgrgknPQCLVLAPTRELARQV 206
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRH------PQVLILAPTREIAVQI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 207 EKEFRESAPSLDTI-CLY--GGTPIGQQMRELNyGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDV 283
Cdd:cd17943 75 HDVFKKIGKKLEGLkCEVfiGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDV 153
|
170 180 190
....*....|....*....|....*....|....*
gi 15228722 284 EIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNP 318
Cdd:cd17943 154 NWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKP 188
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
131-321 |
1.59e-43 |
|
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: 154.24 E-value: 1.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 131 LKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIkfnakhGRGKNPQCLVLAPTRELARQVE--- 207
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL------TEHRNPSALILTPTRELAVQIEdqa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 208 KEFRESAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVEIIL 287
Cdd:cd17962 79 KELMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
|
170 180 190
....*....|....*....|....*....|....
gi 15228722 288 QKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17962 159 ENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
129-321 |
2.56e-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: 150.90 E-value: 2.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 129 KALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIikFNAKHGRGKNPQCLVLAPTRELARQVEK 208
Cdd:cd17941 3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL--YRERWTPEDGLGALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 209 EFRESAP--SLDTICLYGGTPIGQQMRELNyGIDVAVGTPGRIIDLMKRGA-LNLSEVQFVVLDEADQMLQVGFAEDVEI 285
Cdd:cd17941 81 VLRKVGKyhSFSAGLIIGGKDVKEEKERIN-RMNILVCTPGRLLQHMDETPgFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 15228722 286 ILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
127-321 |
3.49e-42 |
|
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: 150.80 E-value: 3.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRGkNPQCLVLAPTRELARQV 206
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKG-QVGALIISPTRELATQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 207 EKEFRE----SAPSLDTICLYGGTPIGQQMREL-NYGIDVAVGTPGRIIDLMKRGA--LNLSEVQFVVLDEADQMLQVGF 279
Cdd:cd17960 80 YEVLQSflehHLPKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15228722 280 AEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17960 160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
131-325 |
8.40e-42 |
|
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: 149.66 E-value: 8.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 131 LKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGrgknPQCLVLAPTRELARQVEKEF 210
Cdd:cd17957 5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKG----LRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 211 RESAPSLD-TICLY--GGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVEIIL 287
Cdd:cd17957 81 LKLSKGTGlRIVLLskSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 15228722 288 QKLPAKR-QSMMFSATMPSWIRSLTKKYLNNPLTIdLVG 325
Cdd:cd17957 161 AACTNPNlQRSLFSATIPSEVEELARSVMKDPIRI-IVG 198
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
127-318 |
2.81e-40 |
|
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: 145.58 E-value: 2.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKI--IKFNAKHGRGknpqCLVLAPTRELAR 204
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLykLKFKPRNGTG----VIIISPTRELAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 205 QVEKEFRE--SAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIID-LMKRGALNLSEVQFVVLDEADQMLQVGFAE 281
Cdd:cd17942 77 QIYGVAKEllKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEE 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 15228722 282 DVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNP 318
Cdd:cd17942 157 EMRQIIKLLPKRRQTMLFSATQTRKVEDLARISLKKK 193
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
120-322 |
1.53e-39 |
|
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: 143.62 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 120 DLGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIdKIIkfnakhgrgknpQCLVLAPT 199
Cdd:cd17938 3 ELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-QIV------------VALILEPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 200 RELARQVEKEFRE-----SAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQM 274
Cdd:cd17938 70 RELAEQTYNCIENfkkylDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15228722 275 LQVGFAEDVEIILQKLP-----AKR-QSMMFSATMPSW-IRSLTKKYLNNPLTID 322
Cdd:cd17938 150 LSQGNLETINRIYNRIPkitsdGKRlQVIVCSATLHSFeVKKLADKIMHFPTWVD 204
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
127-322 |
1.01e-38 |
|
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: 141.57 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGR-GIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRGKNPQCLVLAPTRELARQ 205
Cdd:cd17949 1 LVSHLKSKmGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDGTLALVLVPTRELALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 206 VEKEFRE---SAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIID-LMKRGALNLSEVQFVVLDEADQMLQVGFAE 281
Cdd:cd17949 81 IYEVLEKllkPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15228722 282 DVEIILQKL-------------PAKRQSMMFSATMPSWIRSLTKKYLNNPLTID 322
Cdd:cd17949 161 DITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
121-321 |
3.67e-38 |
|
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: 139.91 E-value: 3.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 121 LGISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIdKIIKFNAKhgrgkNPQCLVLAPTR 200
Cdd:cd18045 4 MGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDIQVR-----ETQALILSPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 201 ELARQVEKEFRESAPSLDTIC--LYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVG 278
Cdd:cd18045 78 ELAVQIQKVLLALGDYMNVQChaCIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15228722 279 FAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd18045 158 FKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
346-455 |
1.12e-35 |
|
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: 129.64 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 346 GRASIIGPLVKEHgKGGKCIVFTQTKRDADRLAFGLAKSYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLD 425
Cdd:pfam00271 1 EKLEALLELLKKE-RGGKVLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 15228722 426 VPNVDLVIHYELPNNTETFVHRTGRTGRAG 455
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
123-321 |
2.84e-35 |
|
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: 131.54 E-value: 2.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 123 ISPEIVKALKGRGIEKLFPIQKAVLePAMEG---RDMIGRARTGTGKTLAFGIPIIDKIikfnakHGRGKNPQCLVLAPT 199
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETAL-PLILSdppENLIAQSQSGTGKTAAFVLAMLSRV------DPTLKSPQALCLAPT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 200 RELARQVEKEFRE--SAPSLDTIC------LYGGTPIGQQmrelnygidVAVGTPGRIIDLMKRGALNLSEVQFVVLDEA 271
Cdd:cd17963 74 RELARQIGEVVEKmgKFTGVKVALavpgndVPRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15228722 272 DQML-QVGFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTI 321
Cdd:cd17963 145 DVMLdTQGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
127-316 |
4.30e-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: 118.24 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRGKN-PQCLVLAPTRELARQ 205
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNaPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 206 VEKEFRESAPSLD--TICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDV 283
Cdd:cd17948 81 IGSVAQSLTEGLGlkVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15228722 284 EIILQKLP-------------AKRQSMMFSATMPSWIRSLTKKYLN 316
Cdd:cd17948 161 SHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSKVID 206
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
127-322 |
5.47e-29 |
|
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: 115.04 E-value: 5.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 127 IVKALKGRGIEKLFPIQKAVL---------EPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGRgknpqCLVLA 197
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIpwllpssksTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLR-----ALIVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 198 PTRELARQVEKEFRE--SAPSLDTICLYGGTPIGQQMRELNYG--------IDVAVGTPGRIID--LMKRGaLNLSEVQF 265
Cdd:cd17956 76 PTKELVQQVYKVFESlcKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDhlNSTPG-FTLKHLRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 266 VVLDEADQMLQVGFAEDVEIILQKL-------------------PAKR-QSMMFSATM---PSWIRSLTkkyLNNPLTID 322
Cdd:cd17956 155 LVIDEADRLLNQSFQDWLETVMKALgrptapdlgsfgdanllerSVRPlQKLLFSATLtrdPEKLSSLK---LHRPRLFT 231
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
375-455 |
1.31e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 100.36 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 375 DRLAFGL-AKSYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLVIHYELPNNTETFVHRTGRTGR 453
Cdd:smart00490 1 EELAELLkELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 15228722 454 AG 455
Cdd:smart00490 81 AG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
138-433 |
1.66e-21 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 98.56 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 138 KLFPIQKAVLE-----PAMEGRDMIGRARTGTGKTLaFGIPIIDKIikfnakhgrGKNPQCLVLAPTRELARQVEKEFRE 212
Cdd:COG1061 80 ELRPYQQEALEallaaLERGGGRGLVVAPTGTGKTV-LALALAAEL---------LRGKRVLVLVPRRELLEQWAEELRR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 213 sapsldticLYGGTPIGQQMRELNYGIDVA-VGTpgriidLMKRGALNL--SEVQFVVLDEAdqmlQVGFAEDVEIILQK 289
Cdd:COG1061 150 ---------FLGDPLAGGGKKDSDAPITVAtYQS------LARRAHLDElgDRFGLVIIDEA----HHAGAPSYRRILEA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 290 LPAKRQsMMFSATmP--------------------SWIRSLTKKYLNNPLTIDLVGDSDQKLADGITMYS-----IAADS 344
Cdd:COG1061 211 FPAAYR-LGLTAT-PfrsdgreillflfdgivyeySLKEAIEDGYLAPPEYYGIRVDLTDERAEYDALSErlreaLAADA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 345 YGRASIIGPLVKEHGKGGKCIVFTQTKRDADRLA--FGLAKsYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAAR 422
Cdd:COG1061 289 ERKDKILRELLREHPDDRKTLVFCSSVDHAEALAelLNEAG-IRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNE 367
|
330
....*....|.
gi 15228722 423 GLDVPNVDLVI 433
Cdd:COG1061 368 GVDVPRLDVAI 378
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
122-467 |
2.61e-20 |
|
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: 95.29 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 122 GISPEIVKALKGRGIEKLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIkfnakhgRGKNPQCLVLAPTRE 201
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL-------EDPGATALYLYPTKA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 202 LAR-QVEK--EFRESAPSLDTICLY-GGTPigQQMRElnygidvAVGTPGRII----DLMKRGALN--------LSEVQF 265
Cdd:COG1205 113 LARdQLRRlrELAEALGLGVRVATYdGDTP--PEERR-------WIREHPDIVltnpDMLHYGLLPhhtrwarfFRNLRY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 266 VVLDEA---------------DQMLQvgfaedveiILQKLPAKRQSMMFSATMPswirsltkkylnNP------LT---I 321
Cdd:COG1205 184 VVIDEAhtyrgvfgshvanvlRRLRR---------ICRHYGSDPQFILASATIG------------NPaehaerLTgrpV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 322 DLVGDsdqklaDG-------ITMYSIAADSYGR--------ASIIGPLVKEhgkGGKCIVFTQTKRDADRLAFGLAKSYK 386
Cdd:COG1205 243 TVVDE------DGsprgertFVLWNPPLVDDGIrrsalaeaARLLADLVRE---GLRTLVFTRSRRGAELLARYARRALR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 387 CEALHGDISQ-------AQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLVIHYELPNNTETFVHRTGRTGRAGKKGS 459
Cdd:COG1205 314 EPDLADRVAAyragylpEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSL 393
|
....*...
gi 15228722 460 AILIHGQD 467
Cdd:COG1205 394 VVLVAGDD 401
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
141-320 |
3.46e-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: 90.13 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 141 PIQKAVLePAMEGRDMIGR-----------------ARTGTGKTLAFGIPIIDKIIK-----FN------AKHGRGKNPQ 192
Cdd:cd17965 33 PIQTLAI-KKLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYLAPLLDYLKRqeqepFEeaeeeyESAKDTGRPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 193 CLVLAPTRELARQVEkefrESAPSLDTICLYGGTPIG-------QQMRELNYG-IDVAVGTPGRIIDLMKRGALNLSEVQ 264
Cdd:cd17965 112 SVILVPTHELVEQVY----SVLKKLSHTVKLGIKTFSsgfgpsyQRLQLAFKGrIDILVTTPGKLASLAKSRPKILSRVT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15228722 265 FVVLDEADQMLQVGFAEDVEIILQKLPAKRQSMMFSATMP-SWIRSLTKKYLN-NPLT 320
Cdd:cd17965 188 HLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPkEFDKTLRKLFPDvVRIA 245
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
118-463 |
1.34e-18 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 89.18 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 118 IADLGIsPEIVKALKGRGIEKLFPIQKAVLEPA-MEGRDMIGRARTGTGKTLAFGIPIIDKIikfnAKHGRgknpqCLVL 196
Cdd:COG1204 3 VAELPL-EKVIEFLKERGIEELYPPQAEALEAGlLEGKNLVVSAPTASGKTLIAELAILKAL----LNGGK-----ALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 197 APTRELARQVEKEFRESAPSL--DTICLYGGtpigqqmRELNYGI----DVAVGTPGRIIDLMKRGALNLSEVQFVVLDE 270
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELgiKVGVSTGD-------YDSDDEWlgryDILVATPEKLDSLLRNGPSWLRDVDLVVVDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 271 AdQMLqvgfaED------VEIILQKLPAKRQSMMF---SATMPswirsltkkylnNP------LTIDLVGDS----DQKL 331
Cdd:COG1204 146 A-HLI-----DDesrgptLEVLLARLRRLNPEAQIvalSATIG------------NAeeiaewLDAELVKSDwrpvPLNE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 332 A---DGITMYsiaADSYGR-ASIIGPLVKEH-GKGGKCIVFTQTKRDADRLAFGLAKSYK-------------------- 386
Cdd:COG1204 208 GvlyDGVLRF---DDGSRRsKDPTLALALDLlEEGGQVLVFVSSRRDAESLAKKLADELKrrltpeereeleelaeelle 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 387 -------CEAL-----------HGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVP--NVdlVIH-YELPNNTE--- 442
Cdd:COG1204 285 vseethtNEKLadclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLParRV--IIRdTKRGGMVPipv 362
|
410 420
....*....|....*....|....
gi 15228722 443 -TFVHRTGRTGRAGK--KGSAILI 463
Cdd:COG1204 363 lEFKQMAGRAGRPGYdpYGEAILV 386
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
120-323 |
9.61e-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: 9.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 120 DLGISPEIVKALKGRGIEKLFPIQKAVLePAMEG---RDMIGRARTGTGKTLAFGIPIIDKIikfNAKHgrgKNPQCLVL 196
Cdd:cd18048 22 ELHLKEELLRGIYAMGFNRPSKIQENAL-PMMLAdppQNLIAQSQSGTGKTAAFVLAMLSRV---DALK---LYPQCLCL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 197 APTRELARQ---VEKEFRESAPSLDTICLYGGTPIGQQMRelnYGIDVAVGTPGRIID-LMKRGALNLSEVQFVVLDEAD 272
Cdd:cd18048 95 SPTFELALQtgkVVEEMGKFCVGIQVIYAIRGNRPGKGTD---IEAQIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15228722 273 QMLQV-GFAEDVEIILQKLPAKRQSMMFSATMPSWIRSLTKKYLNNPLTIDL 323
Cdd:cd18048 172 VMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKL 223
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
354-463 |
3.14e-17 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 85.55 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 354 LVKEH---GKGGKCIVFTQTkRD-----ADRLA---------FGLAKSYKCEALhgdiSQAQRERTLAGFRDGNFSILVA 416
Cdd:COG1111 343 ILKEQlgtNPDSRIIVFTQY-RDtaemiVEFLSepgikagrfVGQASKEGDKGL----TQKEQIEILERFRAGEFNVLVA 417
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15228722 417 TDVAARGLDVPNVDLVIHYELPNNTETFVHRTGRTGRAGKKGSAILI 463
Cdd:COG1111 418 TSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGRVVVLI 464
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
354-476 |
1.52e-16 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 82.50 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 354 LVKEHgKGGKCIVFTQTKRDADRLAFGL-AKSYKCEALHGDISQAQRERTLAGFRDGNFSILVATdVA-ARGLDVPNVDL 431
Cdd:COG0514 224 FLKEH-PGGSGIVYCLSRKKVEELAEWLrEAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRF 301
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15228722 432 VIHYELPNNTETFVHRTGRTGRAGKKGSAILIHG-QDQTRAVKMIE 476
Cdd:COG0514 302 VIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGpEDVAIQRFFIE 347
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
162-302 |
4.49e-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: 75.52 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 162 TGTGKTLAFGIPIIDKIIKfnakhgrgKNPQCLVLAPTRELARQVEKEFRE-SAPSLDTICLYGGTPIGQQMRELNYGID 240
Cdd:cd00046 10 TGSGKTLAALLAALLLLLK--------KGKKVLVLVPTKALALQTAERLRElFGPGIRVAVLVGGSSAEEREKNKLGDAD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228722 241 VAVGTPGRIIDLMKR-GALNLSEVQFVVLDEADQMLQVGFAEDV--EIILQKLPAKRQSMMFSAT 302
Cdd:cd00046 82 IIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALIldLAVRKAGLKNAQVILLSAT 146
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
120-318 |
1.12e-14 |
|
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: 73.22 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 120 DLGISPEIVKALKGRGIEKLFPIQKAVLePAMEG---RDMIGRARTGTGKTLAFGIPIIDKIikfnakHGRGKNPQCLVL 196
Cdd:cd18047 5 ELRLKPQLLQGVYAMGFNRPSKIQENAL-PLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQV------EPANKYPQCLCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 197 APTRELARQVEKEFRESAPSLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIID-LMKRGALNLSEVQFVVLDEADQML 275
Cdd:cd18047 78 SPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15228722 276 QVGFAEDVEIILQK-LPAKRQSMMFSATMPSWIRSLTKKYLNNP 318
Cdd:cd18047 158 ATQGHQDQSIRIQRmLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
355-462 |
3.80e-14 |
|
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: 69.54 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 355 VKEHGKGGKCIVFTQTKRDADRLAFGLAKS-YKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLVI 433
Cdd:cd18794 24 IKVEHLGGSGIIYCLSRKECEQVAARLQSKgISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVI 103
|
90 100
....*....|....*....|....*....
gi 15228722 434 HYELPNNTETFVHRTGRTGRAGKKGSAIL 462
Cdd:cd18794 104 HYSLPKSMESYYQESGRAGRDGLPSECIL 132
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
336-463 |
4.93e-14 |
|
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: 69.97 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 336 TMYSIAADSYGRASIIGPLVKEHGKGGKCIVFTQTKRDADRLAFGLAKsykcEALHGDISQAQRERTLAGFRDGNFSILV 415
Cdd:cd18789 24 KRRLLAAMNPNKLRALEELLKRHEQGDKIIVFTDNVEALYRYAKRLLK----PFITGETPQSEREEILQNFREGEYNTLV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15228722 416 ATDVAARGLDVPNVDLVI----HYelpNNTETFVHRTGRTGRAGKKG--SAILI 463
Cdd:cd18789 100 VSKVGDEGIDLPEANVAIqisgHG---GSRRQEAQRLGRILRPKKGGgkNAFFY 150
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
354-464 |
6.19e-14 |
|
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: 69.60 E-value: 6.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 354 LVKEHGKGGKCIVFTQTKRDADRLAFGLAKsyKCEAL---------HGDISQAQRERTLAGFRDGNFSILVATDVAARGL 424
Cdd:cd18796 31 VIFLLERHKSTLVFTNTRSQAERLAQRLRE--LCPDRvppdfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGI 108
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15228722 425 DVPNVDLVIHYELPNNTETFVHRTGRTGRagKKGSAILIH 464
Cdd:cd18796 109 DIGDVDLVIQIGSPKSVARLLQRLGRSGH--RPGAASKGR 146
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
354-461 |
2.27e-13 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 73.37 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 354 LVKE---HGKGGKCIVFTQTkRD-----ADRLA---------FGLAKSYKCEALhgdiSQAQRERTLAGFRDGNFSILVA 416
Cdd:PRK13766 355 IVKEqlgKNPDSRIIVFTQY-RDtaekiVDLLEkegikavrfVGQASKDGDKGM----SQKEQIEILDKFRAGEFNVLVS 429
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15228722 417 TDVAARGLDVPNVDLVIHYElPNNTET-FVHRTGRTGRaGKKGSAI 461
Cdd:PRK13766 430 TSVAEEGLDIPSVDLVIFYE-PVPSEIrSIQRKGRTGR-QEEGRVV 473
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
356-454 |
8.19e-13 |
|
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: 66.08 E-value: 8.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 356 KEHGKGGKCIVFTQTKRDADRLAFGLA------KSYKCEAL--HGDISQAQR--------ERTLAGFRDGNFSILVATDV 419
Cdd:cd18802 20 FPKTPDFRGIIFVERRATAVVLSRLLKehpstlAFIRCGFLigRGNSSQRKRslmtqrkqKETLDKFRDGELNLLIATSV 99
|
90 100 110
....*....|....*....|....*....|....*
gi 15228722 420 AARGLDVPNVDLVIHYELPNNTETFVHRTGRtGRA 454
Cdd:cd18802 100 LEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
139-309 |
1.83e-12 |
|
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: 66.13 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 139 LFPIQKAVLEPAM-EGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKhgrgknpqCLVLAPTRELARQVEKEFRESAPSL 217
Cdd:cd17921 2 LNPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATSGGK--------AVYIAPTRALVNQKEADLRERFGPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 218 --DTICLYGGTPI-GQQMRELnygiDVAVGTPgRIIDLM--KRGALNLSEVQFVVLDEAdQMLQVG-FAEDVEIILQKLP 291
Cdd:cd17921 74 gkNVGLLTGDPSVnKLLLAEA----DILVATP-EKLDLLlrNGGERLIQDVRLVVVDEA-HLIGDGeRGVVLELLLSRLL 147
|
170 180
....*....|....*....|....*..
gi 15228722 292 AKRQSMMF---SATMP------SWIRS 309
Cdd:cd17921 148 RINKNARFvglSATLPnaedlaEWLGV 174
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
395-463 |
3.92e-11 |
|
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: 61.22 E-value: 3.92e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228722 395 SQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLVIHYELPNNTETFVHRTGRTGRaGKKGSAILI 463
Cdd:cd18801 75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVL 142
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
363-461 |
7.52e-11 |
|
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: 58.48 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 363 KCIVFTQTKRDADRLAfglakSYkcealhgdisqaqrertlagfrdgnFSILVATDVAARGLDVPNVDLVIHYELPNNTE 442
Cdd:cd18785 5 KIIVFTNSIEHAEEIA-----SS-------------------------LEILVATNVLGEGIDVPSLDTVIFFDPPSSAA 54
|
90
....*....|....*....
gi 15228722 443 TFVHRTGRTGRAGKKGSAI 461
Cdd:cd18785 55 SYIQRVGRAGRGGKDEGEV 73
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
116-433 |
9.28e-10 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 61.76 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 116 LAIADLGISPEIVKALKGRGIEKLFPIQKAVLEP-AMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKhgrgknpqCL 194
Cdd:PRK00254 1 MKVDELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGGK--------AV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 195 VLAPTRELARQVEKEFREsapsLDTICLYGGTPIG--QQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEAD 272
Cdd:PRK00254 73 YLVPLKALAEEKYREFKD----WEKLGLRVAMTTGdyDSTDEWLGKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 273 QMLQVGFAEDVEIILQKLPAKRQSMMFSATMPSwiRSLTKKYLNNPLTIdlvgdSDQ---KLADGITMYSI------AAD 343
Cdd:PRK00254 149 LIGSYDRGATLEMILTHMLGRAQILGLSATVGN--AEELAEWLNAELVV-----SDWrpvKLRKGVFYQGFlfwedgKIE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 344 SYGRA--SIIGPLVKehgKGGKCIVFTQTKRDADRLAFGLAKSYK---------------------------CEALHGDI 394
Cdd:PRK00254 222 RFPNSweSLVYDAVK---KGKGALVFVNTRRSAEKEALELAKKIKrfltkpelralkeladsleenptneklKKALRGGV 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15228722 395 S-----QAQRERTLA--GFRDGNFSILVATDVAARGLDVPNVDLVI 433
Cdd:PRK00254 299 AfhhagLGRTERVLIedAFREGLIKVITATPTLSAGINLPAFRVII 344
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
354-438 |
1.16e-09 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 56.72 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 354 LVKEHGKGG-KCIVFTQTKRDADRLAFGLAK-SYKCEALHGDISQAQRERTLAGFRDGN--FSILVATDVAARGLDVPNV 429
Cdd:cd18793 19 LLEELREPGeKVLIFSQFTDTLDILEEALRErGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAA 98
|
....*....
gi 15228722 430 DLVIHYELP 438
Cdd:cd18793 99 NRVILYDPW 107
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
346-465 |
1.14e-08 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain] Cd Length: 160 Bit Score: 54.58 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 346 GRASIIGPLVKEHGKggkcivftQTKRDADRLAFGLAK---SYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAAR 422
Cdd:cd18792 27 GQVYYVYPRIEESEK--------LDLKSIEALAEELKElvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEV 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15228722 423 GLDVPNVDLVIhyelPNNTETF----VHR-TGRTGRAGKKGSAILIHG 465
Cdd:cd18792 99 GIDVPNANTMI----IEDADRFglsqLHQlRGRVGRGKHQSYCYLLYP 142
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
346-473 |
1.56e-08 |
|
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: 54.27 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 346 GR-ASIIGPLVKEHGK-GGKCIVFTqtkrdADRLAFGLAKSYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARG 423
Cdd:cd18811 26 GRqAYVIYPLIEESEKlDLKAAVAM-----YEYLKERFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15228722 424 LDVPNVDLVIHYelpnNTETF----VHR-TGRTGRAGKKGSAILIHGQDQTRAVK 473
Cdd:cd18811 101 VDVPNATVMVIE----DAERFglsqLHQlRGRVGRGDHQSYCLLVYKDPLTETAK 151
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
143-271 |
2.15e-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: 54.58 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 143 QKAVLEPAMEgRDMIGRARTGTGKTLafgIPI--IDKIIKFNAKHGRGKnPQCLVLAPTRELARQVEKEFRESAPsLDTI 220
Cdd:cd18034 7 QLELFEAALK-RNTIVVLPTGSGKTL---IAVmlIKEMGELNRKEKNPK-KRAVFLVPTVPLVAQQAEAIRSHTD-LKVG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15228722 221 CLYGGTPIGQQMRELNYG----IDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEA 271
Cdd:cd18034 81 EYSGEMGVDKWTKERWKEelekYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
358-464 |
5.44e-08 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 55.87 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 358 HGKGGKC-IVFTQTKRDADRLAFGLAKS-YKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLVIHY 435
Cdd:PRK11057 232 QEQRGKSgIIYCNSRAKVEDTAARLQSRgISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHF 311
|
90 100
....*....|....*....|....*....
gi 15228722 436 ELPNNTETFVHRTGRTGRAGKKGSAILIH 464
Cdd:PRK11057 312 DIPRNIESYYQETGRAGRDGLPAEAMLFY 340
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
360-463 |
8.03e-08 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 51.87 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 360 KGGKCIVFTQTKRDA--------DRLAFGLAKSYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDL 431
Cdd:cd18797 34 AGVKTIVFCRSRKLAelllrylkARLVEEGPLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDA 113
|
90 100 110
....*....|....*....|....*....|..
gi 15228722 432 VIHYELPNNTETFVHRTGRTGRAGKKGSAILI 463
Cdd:cd18797 114 VVLAGYPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
360-440 |
8.79e-08 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 55.23 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 360 KGGKCIVFTQTKRDADRLAFGLAKS-YKCEALHGDISQAQRERTLAGFRDG-NFS-ILVATDVAARGLDVPNVDLVIHYE 436
Cdd:COG0553 548 EGEKVLVFSQFTDTLDLLEERLEERgIEYAYLHGGTSAEERDELVDRFQEGpEAPvFLISLKAGGEGLNLTAADHVIHYD 627
|
....
gi 15228722 437 LPNN 440
Cdd:COG0553 628 LWWN 631
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
363-433 |
1.30e-06 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 47.55 E-value: 1.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228722 363 KCIVFTQTKRDADRLAFGLAKSY-KCEALHGDISQAQRER---TLAGFRDGNFSILVATDVAARGLDVPNVDLVI 433
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGiDAVALNSDYSDRERGDealILLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
365-475 |
1.48e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 51.44 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 365 IVFTQTKRDADRLAFGLAK-SYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLVIHYELPNNTET 443
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEfGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90 100 110
....*....|....*....|....*....|...
gi 15228722 444 FVHRTGRTGRAGKKGSAILIHG-QDQTRAVKMI 475
Cdd:PLN03137 764 YHQECGRAGRDGQRSSCVLYYSySDYIRVKHMI 796
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
163-274 |
1.73e-06 |
|
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: 48.57 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 163 GTGKTLAFGIPIIDkiikfNAKHGRgknpQCLVLAPTRELARQVEKEFRESAPSLDTICLYGGTPigQQMRElnyGIDVA 242
Cdd:cd17918 46 GSGKTLVALGAALL-----AYKNGK----QVAILVPTEILAHQHYEEARKFLPFINVELVTGGTK--AQILS---GISLL 111
|
90 100 110
....*....|....*....|....*....|..
gi 15228722 243 VGTPGRIIDLMKRGALNLsevqfVVLDEADQM 274
Cdd:cd17918 112 VGTHALLHLDVKFKNLDL-----VIVDEQHRF 138
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
143-271 |
2.64e-06 |
|
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: 47.96 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 143 QKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIkfnakhgRGKNPQCLVLAPTRELARQVEKEFRESAPSLD---T 219
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL-------RDPGSRALYLYPTKALAQDQLRSLRELLEQLGlgiR 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228722 220 ICLYGG-TPigqqmRELNYGIdvaVGTPGRII----D-----LMKRGAL---NLSEVQFVVLDEA 271
Cdd:cd17923 78 VATYDGdTP-----REERRAI---IRNPPRILltnpDmlhyaLLPHHDRwarFLRNLRYVVLDEA 134
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
390-463 |
1.05e-05 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350197 [Multi-domain] Cd Length: 151 Bit Score: 45.80 E-value: 1.05e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228722 390 LHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLVIhyelPNNTETF----VHR-TGRTGRAGKKGSAILI 463
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTII----IERADKFglaqLYQlRGRVGRSKERAYAYFL 131
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
153-270 |
6.03e-05 |
|
DEXH-box helicase domain of LHR; 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 from 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: 350680 [Multi-domain] Cd Length: 166 Bit Score: 43.73 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 153 GRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGrgknpQCLVLAPTRELARQVEKEFR----ESAPSLDTICLYGGTPI 228
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV-----QVLYISPLKALINDQERRLEepldEIDLEIPVAVRHGDTSQ 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15228722 229 GQQMRELNYGIDVAVGTPGRIIDLM--KRGALNLSEVQFVVLDE 270
Cdd:cd17922 76 SEKAKQLKNPPGILITTPESLELLLvnKKLRELFAGLRYVVVDE 119
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
162-302 |
6.09e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 43.81 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 162 TGTGKTLafgipIIDKIIKFNAKHGRGKNpqCLVLAPTRELARQVEKEFRESAPSLDTICLYGGtpiGQQMRELNYGIDV 241
Cdd:pfam04851 32 TGSGKTL-----TAAKLIARLFKKGPIKK--VLFLVPRKDLLEQALEEFKKFLPNYVEIGEIIS---GDKKDESVDDNKI 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228722 242 AVGTP---GRIIDLMKRGALNLSEVQFVVlDEADQmlqvGFAEDVEIILQKLPAKRQsMMFSAT 302
Cdd:pfam04851 102 VVTTIqslYKALELASLELLPDFFDVIII-DEAHR----SGASSYRNILEYFKPAFL-LGLTAT 159
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
138-270 |
7.64e-05 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain] Cd Length: 204 Bit Score: 44.00 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 138 KLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAfGIPIIDKIIKfnAKHGRGKNPQCLVLAPTRELA-RQVEKEFRESAPS 216
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRV-AVYICRHHLE--KRRSAGEKGRVVVLVNKVPLVeQQLEKFFKYFRKG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15228722 217 LDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGALN----LSEVQFVVLDE 270
Cdd:cd18036 79 YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEervyLSDFSLLIFDE 136
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
160-452 |
1.20e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 45.30 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 160 ARTGTGKTLAFGIPIIDKIIKFNAKH----GRGKNPQCLVLAPTRELARQVEKEFR--------------ESAPSLDTIC 221
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFREGGEDtreaHKRKTSRILYISPIKALGTDVQRNLQiplkgiaderrrrgETEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 222 LYGGTPIGQQMRELNYGIDVAVGTPGRI-IDLMKRGALNLSEVQFVVLDEADQMLQVGFAEDVEIILQKL----PAKRQS 296
Cdd:PRK09751 83 RTGDTPAQERSKLTRNPPDILITTPESLyLMLTSRARETLRGVETVIIDEVHAVAGSKRGAHLALSLERLdallHTSAQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 297 MMFSATMPSWIRSLTKKYLNNPLTIdLVGDSDQKLADGIT-----MYSIAADS--------YGRASIIGPLVK-----EH 358
Cdd:PRK09751 163 IGLSATVRSASDVAAFLGGDRPVTV-VNPPAMRHPQIRIVvpvanMDDVSSVAsgtgedshAGREGSIWPYIEtgildEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 359 GKGGKCIVFTQTKRDADRLAFGLAKSYK----------------------------------CEALHGDISQAQRERTLA 404
Cdd:PRK09751 242 LRHRSTIVFTNSRGLAEKLTARLNELYAarlqrspsiavdaahfestsgatsnrvqssdvfiARSHHGSVSKEQRAITEQ 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15228722 405 GFRDGNFSILVATDVAARGLDVPNVDLVIHYELPNNTETFVHRTGRTG 452
Cdd:PRK09751 322 ALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
162-302 |
1.30e-04 |
|
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: 42.29 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 162 TGTGKTLaFGIPIIDKIikfnakhgrgKNPQCLVLAPTRELARQVEKEFRESAPSlDTICLYGGTPIgqqmrELNYGIDV 241
Cdd:cd17926 27 TGSGKTL-TALALIAYL----------KELRTLIVVPTDALLDQWKERFEDFLGD-SSIGLIGGGKK-----KDFDDANV 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228722 242 AVGTPGRIIDLMKRGALNLSEVQFVVLDEADQMLQVGFAEdveiILQKLPAKRQsMMFSAT 302
Cdd:cd17926 90 VVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSE----ILKELNAKYR-LGLTAT 145
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
360-432 |
2.78e-04 |
|
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: 41.85 E-value: 2.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228722 360 KGGKCIVFTQTKRDADRLAFGLAK-SYKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDLV 432
Cdd:cd18790 26 RGERVLVTTLTKRMAEDLTEYLQElGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLV 99
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
123-308 |
3.59e-04 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 42.20 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 123 ISPEIVKALKGRGIEKLFPIQKAVL--EPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKfnakhgRGKNpqCLVLAP-- 198
Cdd:cd18026 1 LPDAVREAYAKKGIKKLYDWQKECLslPGLLEGRNLVYSLPTSGGKTLVAEILMLKRLLE------RRKK--ALFVLPyv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 199 --TRELARQVEKEFRESAPSLDTicLYGGTpiGQQMRELNYGIDVAVGTPGRIIDLMKRG--ALNLSEVQFVVLDEAdQM 274
Cdd:cd18026 73 siVQEKVDALSPLFEELGFRVEG--YAGNK--GRSPPKRRKSLSVAVCTIEKANSLVNSLieEGRLDELGLVVVDEL-HM 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15228722 275 LQVGF-AEDVEIILQKL----PAKRQSMMFSATMP------SWIR 308
Cdd:cd18026 148 LGDGHrGALLELLLTKLlyaaQKNIQIVGMSATLPnleelaSWLR 192
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
150-271 |
5.27e-04 |
|
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: 41.35 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 150 AMEGRDMIgRARTGTGKTLAFGIPIIDKIIKFNAKhgrgknpqCLVLAPTRELARQVEKEFRESAPSLDTICLYGGTPIG 229
Cdd:cd18035 14 ALNGNTLI-VLPTGLGKTIIAILVAADRLTKKGGK--------VLILAPSRPLVEQHAENLKRVLNIPDKITSLTGEVKP 84
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15228722 230 QQMRELNYGIDVAVGTPGRIIDLMKRGALNLSEVQFVVLDEA 271
Cdd:cd18035 85 EERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
138-271 |
6.11e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex 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. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 41.26 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 138 KLFPIQKAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHGrGKnpqCLVLAPTREL-ARQVEKEFRE-SAP 215
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRK-GK---VVFLANKVPLvEQQKEVFRKHfERP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228722 216 SLDTICLYGGTPIGQQMRELNYGIDVAVGTPGRIIDLMKRGAL-NLSEVQFVVLDEA 271
Cdd:cd17927 78 GYKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDEC 134
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
390-463 |
6.44e-04 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 42.83 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 390 LHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDL-VIhyElpnNTETF----VH--RtGRTGRAGKKGSAIL 462
Cdd:PRK10917 511 LHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVmVI--E---NAERFglaqLHqlR-GRVGRGAAQSYCVL 584
|
.
gi 15228722 463 I 463
Cdd:PRK10917 585 L 585
|
|
| CMS1 |
pfam14617 |
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant ... |
239-269 |
7.93e-04 |
|
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant CMS1-like proteins. The family has similarity to the DEAD-box helicases.
Pssm-ID: 373164 Cd Length: 250 Bit Score: 41.39 E-value: 7.93e-04
10 20 30
....*....|....*....|....*....|.
gi 15228722 239 IDVAVGTPGRIIDLMKRGALNLSEVQFVVLD 269
Cdd:pfam14617 176 IGIGVGTPGRIADLLENESLSVDNLKYIILD 206
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
354-463 |
8.10e-04 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 40.23 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 354 LVKEHGKGGKCIVFTQTKRDADRLA---FGLAksykceALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPnVD 430
Cdd:cd18795 36 KIETVSEGKPVLVFCSSRKECEKTAkdlAGIA------FHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP-AR 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15228722 431 LVI----------HYELPNNTEtfVHR-TGRTGRAGK--KGSAILI 463
Cdd:cd18795 109 TVIikgtqrydgkGYRELSPLE--YLQmIGRAGRPGFdtRGEAIIM 152
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
385-465 |
1.10e-03 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 41.96 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 385 YKCEALHGDISQAQRERTLAGFRDGNFSILVATDVAARGLDVPNVDL-VIhyElpnNTETF----VH--RtGRTGRAGKK 457
Cdd:COG1200 504 LRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVmVI--E---NAERFglsqLHqlR-GRVGRGSAQ 577
|
....*...
gi 15228722 458 GSAILIHG 465
Cdd:COG1200 578 SYCLLLYD 585
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
162-271 |
1.55e-03 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members 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: 350790 [Multi-domain] Cd Length: 163 Bit Score: 39.47 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 162 TGTGKT-LAFGIpiIDKIIKFNAKhgrgknPQCLVLAPTRELARQVEKEFRESAPSLDTICLYGGtpigqQMRELNYGID 240
Cdd:cd18032 29 TGTGKTyTAAFL--IKRLLEANRK------KRILFLAHREELLEQAERSFKEVLPDGSFGNLKGG-----KKKPDDARVV 95
|
90 100 110
....*....|....*....|....*....|..
gi 15228722 241 VA-VGTPGRIIDLMKRGAlnlSEVQFVVLDEA 271
Cdd:cd18032 96 FAtVQTLNKRKRLEKFPP---DYFDLIIIDEA 124
|
|
| HsdR |
COG4096 |
Type I site-specific restriction endonuclease, part of a restriction-modification system ... |
162-225 |
1.66e-03 |
|
Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];
Pssm-ID: 443272 [Multi-domain] Cd Length: 806 Bit Score: 41.37 E-value: 1.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228722 162 TGTGKT-LAFGipIIDKIIkfnaKHGRGKNpqCLVLAPTRELARQVEKEFRESAPSLDTIC-LYGG 225
Cdd:COG4096 187 TGTGKTrTAIA--LIYRLL----KAGRAKR--ILFLADRNALVDQAKNAFKPFLPDLDAFTkLYNK 244
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
118-212 |
2.02e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 41.10 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 118 IADLGISPEIVKALKGRGIEKLFPIQ-KAVLEPAMEGRDMIGRARTGTGKTLAFGIPIIDKIikfnAKHGRgknpqCLVL 196
Cdd:PRK02362 3 IAELPLPEGVIEFYEAEGIEELYPPQaEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAI----ARGGK-----ALYI 73
|
90
....*....|....*.
gi 15228722 197 APTRELARQVEKEFRE 212
Cdd:PRK02362 74 VPLRALASEKFEEFER 89
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
138-304 |
3.14e-03 |
|
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: 38.85 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 138 KLFPIQKAVLEPAM-EGRDMIGRARTGTGKTLAFGIPIIDKIIKfnakHGRGknpqcLVLAPTRELARQVEKEFResapS 216
Cdd:cd18028 1 ELYPPQAEAVRAGLlKGENLLISIPTASGKTLIAEMAMVNTLLE----GGKA-----LYLVPLRALASEKYEEFK----K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 217 LDTICLYGGTPIGQqMRELNYGI---DVAVGTPGRIIDLMKRGALNLSEVQFVVLDEadqmlqVGFAED------VEIIL 287
Cdd:cd18028 68 LEEIGLKVGISTGD-YDEDDEWLgdyDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE------IHLISDeergptLESIV 140
|
170 180
....*....|....*....|
gi 15228722 288 QKLPA---KRQSMMFSATMP 304
Cdd:cd18028 141 ARLRRlnpNTQIIGLSATIG 160
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
266-457 |
5.77e-03 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 39.34 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 266 VVLDEADQMLQVGFAEdVEIILQKLPAKRQS-MMFSATMPSWIRSLTKKYLN--NPLTIDLvgdsdqKLADGITMYSIAA 342
Cdd:cd09639 127 LIFDEVHFYDEYTLAL-ILAVLEVLKDNDVPiLLMSATLPKFLKEYAEKIGYveENEPLDL------KPNERAPFIKIES 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 343 DSYGRASIIGPLVKEHGKGGKCIVFTQTKRDAdRLAFGLAKSYKCEA----LHGDISQAQRERT----LAGFRDGNFSIL 414
Cdd:cd09639 200 DKVGEISSLERLLEFIKKGGSVAIIVNTVDRA-QEFYQQLKEKGPEEeimlIHSRFTEKDRAKKeaelLLEFKKSEKFVI 278
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15228722 415 VATDVAARGLDVpNVDLVIHYELPNNteTFVHRTGRTGRAGKK 457
Cdd:cd09639 279 VATQVIEASLDI-SVDVMITELAPID--SLIQRLGRLHRYGEK 318
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
142-270 |
6.81e-03 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 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: 350781 [Multi-domain] Cd Length: 206 Bit Score: 38.11 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228722 142 IQKAVLEPAMEG-RDMIGRARTGTGKTLAFGIPIIDKIIKFNAKHgRGkNPQCLVLAPTRELARQVEKEFRESAPSLDTI 220
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPLP-WG-NRKVVYIAPIKALCSEKYDDWKEKFGPLGLS 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15228722 221 C--LYGGTPIGqQMRELNyGIDVAVGTPGRiIDLMKR-----GALnLSEVQFVVLDE 270
Cdd:cd18023 83 CaeLTGDTEMD-DTFEIQ-DADIILTTPEK-WDSMTRrwrdnGNL-VQLVALVLIDE 135
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