|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
1-380 |
0e+00 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 667.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 1 MQFADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGFARVLIMT 80
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 81 PTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRML 160
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 161 DMGFRSEMMKICDEATNRRQCFLFSATLEGDSVERFADTILNDPALLEAESSRKEQGKILQWVHLADSRNHKLDLLEAIL 240
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEGDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCHLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 241 KAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVINY 320
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 321 DMPRTADIYVHRIGRTGRAGKKGVAISLVEAHDVGILKKIERYTEQNLKRRNIKGLEAQH 380
Cdd:PRK11192 321 DMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRPKT 380
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-377 |
9.74e-176 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 496.59 E-value: 9.74e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 1 MQFADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPgfaRVLIMT 80
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAP---QALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 81 PTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRML 160
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 161 DMGFRSEMMKICDEATNRRQCFLFSATLEGDsVERFADTILNDPALLEAESSRKEQGKILQWVHLADSRnHKLDLLEAIL 240
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPE-IRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR-DKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 241 KAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVINY 320
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 497524335 321 DMPRTADIYVHRIGRTGRAGKKGVAISLVEAHDVGILKKIERYTEQNLKRRNIKGLE 377
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFE 373
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
3-365 |
3.86e-97 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 296.50 E-value: 3.86e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFP---RRDPGFARVLIM 79
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPapeDRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 80 TPTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRM 159
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 160 LDMGFRSE---MMKICDEATNRRQcFLFSATLEGdSVERFADTILNDPALLEAESSRKeQGKILQWVHLADSRNHKLDLL 236
Cdd:PRK04837 170 FDLGFIKDirwLFRRMPPANQRLN-MLFSATLSY-RVRELAFEHMNNPEYVEVEPEQK-TGHRIKEELFYPSNEEKMRLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 237 EAILKAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISH 316
Cdd:PRK04837 247 QTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTH 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497524335 317 VINYDMPRTADIYVHRIGRTGRAGKKGVAISLVEAHDVGILKKIERYTE 365
Cdd:PRK04837 327 VFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIG 375
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-377 |
1.33e-92 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 285.93 E-value: 1.33e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 1 MQFADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGF--ARVLI 78
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRrpVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 79 MTPTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADR 158
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 159 MLDMGFRSEMMKICDEATNRRQCFLFSATLEgDSVERFADTILNDPALLEAESSRKEQGKILQWVHLADsRNHKLDLLEA 238
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFS-DDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVD-KKRKRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 239 ILKAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVI 318
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 497524335 319 NYDMPRTADIYVHRIGRTGRAGKKGVAISLVEAHDVGILKKIERYTEQNLKRRNIKGLE 377
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYE 377
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
3-378 |
8.66e-90 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 278.99 E-value: 8.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLldfprrDPGFARV--LIMT 80
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL------DVKRFRVqaLVLC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 81 PTRELAYQIHEQCVLFAANTH-LKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRM 159
Cdd:PRK11776 80 PTRELADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 160 LDMGFRSEMMKICDEATNRRQCFLFSATLeGDSVERFADTILNDPALLEAESsRKEQGKILQWVHLADsRNHKLDLLEAI 239
Cdd:PRK11776 160 LDMGFQDAIDAIIRQAPARRQTLLFSATY-PEGIAAISQRFQRDPVEVKVES-THDLPAIEQRFYEVS-PDERLPALQRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 240 LKAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVIN 319
Cdd:PRK11776 237 LLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVIN 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 497524335 320 YDMPRTADIYVHRIGRTGRAGKKGVAISLVEAHDVGILKKIERYTEQNLKRRNIKGLEA 378
Cdd:PRK11776 317 YELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSP 375
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
2-361 |
5.23e-89 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 277.56 E-value: 5.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 2 QFADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFP---RRDPGFARVLI 78
Cdd:PRK01297 88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPppkERYMGEPRALI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 79 MTPTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNN-DILIATPGRLMDYMKTEEFHAENVEILILDEAD 157
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARFcDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 158 RMLDMGFRSEMMKICDEATNR--RQCFLFSATLEGDsVERFADTILNDPALLEAESSRKEQGKILQWVHlADSRNHKLDL 235
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDD-VMNLAKQWTTDPAIVEIEPENVASDTVEQHVY-AVAGSDKYKL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 236 LEAILKAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDIS 315
Cdd:PRK01297 326 LYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGIS 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 497524335 316 HVINYDMPRTADIYVHRIGRTGRAGKKGVAISLVEAHDVGILKKIE 361
Cdd:PRK01297 406 HVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIE 451
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-208 |
3.60e-87 |
|
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: 262.76 E-value: 3.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGFARVLIMTPTRELAYQIHE 91
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 92 QCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMGFRSEMMKI 171
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 497524335 172 CDEATNRRQCFLFSATLEgDSVERFADTILNDPALLE 208
Cdd:cd00268 161 LSALPKDRQTLLFSATLP-EEVKELAKKFLKNPVRIE 196
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-368 |
6.40e-87 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 274.91 E-value: 6.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 1 MQFADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFP---RRDPGFARVL 77
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPalaDRKPEDPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 78 IMTPTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEE---FHAenVEILILD 154
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKvvsLHA--CEICVLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 155 EADRMLDMGFRSEMMKICDEATNR--RQCFLFSATLEGDSVErFADTILNDPALLEAESSRKEQGKILQWVHLAdSRNHK 232
Cdd:PRK04537 167 EADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLE-LAYEHMNEPEKLVVETETITAARVRQRIYFP-ADEEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 233 LDLLEAILKAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVT 312
Cdd:PRK04537 245 QTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHID 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 497524335 313 DISHVINYDMPRTADIYVHRIGRTGRAGKKGVAISLVEAHDVGILKKIERYTEQNL 368
Cdd:PRK04537 325 GVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKI 380
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-362 |
9.68e-78 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 252.46 E-value: 9.68e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 1 MQFADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLlDFPRRDPgfaRVLIMT 80
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL-DPELKAP---QILVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 81 PTRELAYQIHEQCVLFAANTHlKIGVVT--GGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADR 158
Cdd:PRK11634 82 PTRELAVQVAEAMTDFSKHMR-GVNVVAlyGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 159 MLDMGFRSEMMKICDEATNRRQCFLFSATLEgDSVERFADTILNDPALLEAESSRKEQGKILQ--WVHLADSRNhklDLL 236
Cdd:PRK11634 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMP-EAIRRITRRFMKEPQEVRIQSSVTTRPDISQsyWTVWGMRKN---EAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 237 EAILKAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISH 316
Cdd:PRK11634 237 VRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 497524335 317 VINYDMPRTADIYVHRIGRTGRAGKKGVAISLVEAHDVGILKKIER 362
Cdd:PRK11634 317 VVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIER 362
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
12-347 |
1.04e-76 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 247.38 E-value: 1.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGFAR-VLIMTPTRELAYQIH 90
Cdd:PTZ00110 141 ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPiVLVLAPTRELAEQIR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 91 EQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMGFRSEMMK 170
Cdd:PTZ00110 221 EQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRK 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 171 ICDEATNRRQCFLFSATLEGDsVERFADTILNDPAL------LEAESSRKeqgkILQWVHLADSRNHKLDLLEAILKA-E 243
Cdd:PTZ00110 301 IVSQIRPDRQTLMWSATWPKE-VQSLARDLCKEEPVhvnvgsLDLTACHN----IKQEVFVVEEHEKRGKLKMLLQRImR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 244 DMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVINYDMP 323
Cdd:PTZ00110 376 DGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFP 455
|
330 340
....*....|....*....|....
gi 497524335 324 RTADIYVHRIGRTGRAGKKGVAIS 347
Cdd:PTZ00110 456 NQIEDYVHRIGRTGRAGAKGASYT 479
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
1-360 |
4.02e-69 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 226.98 E-value: 4.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 1 MQFADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSI----QYLLDFP--RRDPgFA 74
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsrccTIRSGHPseQRNP-LA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 75 RVLimTPTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILD 154
Cdd:PLN00206 200 MVL--TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 155 EADRMLDMGFRSEMMKICdEATNRRQCFLFSATLEGDsVERFADTILNDPALLEAESSRKEQGKILQWVHLADSRNHKLD 234
Cdd:PLN00206 278 EVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPE-VEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 235 LLEaILKAED--MSKAIVFVKTREKLEELV-GLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDV 311
Cdd:PLN00206 356 LFD-ILKSKQhfKPPAVVFVSSRLGADLLAnAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497524335 312 TDISHVINYDMPRTADIYVHRIGRTGRAGKKGVAISLVEAHDVGILKKI 360
Cdd:PLN00206 435 LRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPEL 483
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
3-363 |
2.06e-68 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 222.01 E-value: 2.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQyLLDFPRRDpgfARVLIMTPT 82
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQ-LIDYDLNA---CQALILAPT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 83 RELAYQIheQCVLFAANTHLKIG--VVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRML 160
Cdd:PTZ00424 106 RELAQQI--QKVVLALGDYLKVRchACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 161 DMGFRSEMMKICDEATNRRQCFLFSATLEGDSVErFADTILNDPALLEAESSRKEQGKILQWVHLADSRNHKLDLLEAIL 240
Cdd:PTZ00424 184 SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILE-LTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 241 KAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVINY 320
Cdd:PTZ00424 263 ETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINY 342
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 497524335 321 DMPRTADIYVHRIGRTGRAGKKGVAISLVEAHDVGILKKIERY 363
Cdd:PTZ00424 343 DLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERH 385
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
2-203 |
2.84e-68 |
|
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: 215.43 E-value: 2.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 2 QFADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFP------RRDPGFAR 75
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGppsvgrGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 76 VLIMTPTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDE 155
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497524335 156 ADRMLDMGFRSEMMKICDEAT----NRRQCFLFSATLEgDSVERFADTILND 203
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHPDmppkGERQTLMFSATFP-REIQRLAADFLKN 211
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
12-204 |
2.23e-65 |
|
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: 207.11 E-value: 2.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGfARVLIMTPTRELAYQIHE 91
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAA-TRVLVLVPTRELAMQCFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 92 QCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMK-TEEFHAENVEILILDEADRMLDMGFRSEMMK 170
Cdd:cd17947 80 VLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRnSPSFDLDSIEILVLDEADRMLEEGFADELKE 159
|
170 180 190
....*....|....*....|....*....|....
gi 497524335 171 ICDEATNRRQCFLFSATLeGDSVERFADTILNDP 204
Cdd:cd17947 160 ILRLCPRTRQTMLFSATM-TDEVKDLAKLSLNKP 192
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
2-208 |
4.11e-62 |
|
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: 199.08 E-value: 4.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 2 QFADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRrdPGFArvLIMTP 81
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ--RFFA--LVLAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 82 TRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMK-TEEFHAENVEILILDEADRML 160
Cdd:cd17954 77 TRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEnTKGFSLKSLKFLVMDEADRLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497524335 161 DMGFRSEMMKICDEATNRRQCFLFSATLEgDSVERFADTILNDPALLE 208
Cdd:cd17954 157 NMDFEPEIDKILKVIPRERTTYLFSATMT-TKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-202 |
2.75e-61 |
|
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: 199.04 E-value: 2.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 1 MQFADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGFARV---- 76
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVqepq 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 77 -LIMTPTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDE 155
Cdd:cd18052 123 aLIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497524335 156 ADRMLDMGFRSEMMKICDE----ATNRRQCFLFSATLEgDSVERFADTILN 202
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEpgmpSKEDRQTLMFSATFP-EEIQRLAAEFLK 252
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
219-349 |
3.75e-56 |
|
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: 180.78 E-value: 3.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 219 ILQWVHLADSRNHKLDLLEAILKAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANI 298
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 497524335 299 LVATDVAARGIDVTDISHVINYDMPRTADIYVHRIGRTGRAGKKGVAISLV 349
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-204 |
3.32e-55 |
|
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: 180.86 E-value: 3.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDfPRRDPGFaRVLIMTPTRELAYQIHE 91
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK-PRKKKGL-RALILAPTRELASQIYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 92 QCVLFAANTHLKIGVVTGGINYGSHKDIFEKNN-DILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMGFRSEMMK 170
Cdd:cd17957 79 ELLKLSKGTGLRIVLLSKSLEAKAKDGPKSITKyDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDE 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 497524335 171 I---CDEATNRRQcfLFSATLeGDSVERFADTILNDP 204
Cdd:cd17957 159 IlaaCTNPNLQRS--LFSATI-PSEVEELARSVMKDP 192
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
12-204 |
1.47e-53 |
|
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: 176.71 E-value: 1.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQ--YLLDFPRRDpGFArVLIMTPTRELAYQI 89
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEklYRERWTPED-GLG-ALIISPTRELAMQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 90 HEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNdILIATPGRLMDYM-KTEEFHAENVEILILDEADRMLDMGFRSEM 168
Cdd:cd17941 79 FEVLRKVGKYHSFSAGLIIGGKDVKEEKERINRMN-ILVCTPGRLLQHMdETPGFDTSNLQMLVLDEADRILDMGFKETL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 497524335 169 MKICDEATNRRQCFLFSATLEgDSVERFADTILNDP 204
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQT-KSVKDLARLSLKNP 192
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
12-204 |
3.21e-53 |
|
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: 175.68 E-value: 3.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGFARV-LIMTPTRELAYQIH 90
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIaVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 91 EQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMGFRSEMMK 170
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....
gi 497524335 171 ICDEATNRRQCFLFSATLEgDSVERFADTILNDP 204
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFK-KKIEQLARDILSDP 193
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
3-207 |
9.68e-53 |
|
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: 174.80 E-value: 9.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLldfPRRDPGF-ARVLIMTP 81
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL---KAHSPTVgARALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 82 TRELAYQIHEQCVLFAANTHLKIGVVTGGinyGSHKDIFE---KNNDILIATPGRLMDYMKTEEFHAENVEILILDEADR 158
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGG---DSLEEQFEalaSNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497524335 159 MLDMGFRSEMMKICDEATNRRQCFLFSATLEGDSVErFADTILNDPALL 207
Cdd:cd17959 157 LFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVE-FAKAGLNEPVLI 204
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
8-204 |
1.17e-51 |
|
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: 172.56 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 8 LDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGFARV-LIMTPTRELA 86
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEGPIgLIMAPTRELA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 87 YQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAEN---VEILILDEADRMLDMG 163
Cdd:cd17953 99 LQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNlrrVTYVVLDEADRMFDMG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497524335 164 FRSEMMKICDEATNRRQCFLFSATLEgDSVERFADTILNDP 204
Cdd:cd17953 179 FEPQIMKIVNNIRPDRQTVLFSATFP-RKVEALARKVLHKP 218
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
8-202 |
1.96e-51 |
|
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: 171.61 E-value: 1.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 8 LDKKILNAIDKAGYKTPTSIQQLAIPEAMA-GRDILASAPTGTGKTAAFLLPSIQYLL-DFPRRDPGFARVLIMTPTREL 85
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLnTKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 86 AYQIHEQCV-LFAANTHLKIGVVTGGINYGSHKDIFEKNN-DILIATPGRLMDYMKTEEFHAE--NVEILILDEADRMLD 161
Cdd:cd17964 81 ALQIAAEAKkLLQGLRKLRVQSAVGGTSRRAELNRLRRGRpDILVATPGRLIDHLENPGVAKAftDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497524335 162 MGFRSEMMKICDEATNR----RQCFLFSATLEGDsVERFADTILN 202
Cdd:cd17964 161 MGFRPDLEQILRHLPEKnadpRQTLLFSATVPDE-VQQIARLTLK 204
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
12-205 |
2.53e-51 |
|
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: 171.01 E-value: 2.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGFA-RVLIMTPTRELAYQIH 90
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGpIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 91 EQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMGFRSEMMK 170
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 497524335 171 ICDEATNRRQCFLFSATLEGDsVERFADTILNDPA 205
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKE-VRRLAEDFLKDYI 194
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
3-208 |
2.36e-50 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 168.56 E-value: 2.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLldfpRRDPG--FArvLIMT 80
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL----SEDPYgiFA--LVLT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 81 PTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKT---EEFHAENVEILILDEAD 157
Cdd:cd17955 75 PTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSsddTTKVLSRVKFLVLDEAD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497524335 158 RMLDMGFRSEMMKICDEATNRRQCFLFSATLEgDSVERFADTILNDPALLE 208
Cdd:cd17955 155 RLLTGSFEDDLATILSALPPKRQTLLFSATLT-DALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
12-205 |
2.91e-49 |
|
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: 166.34 E-value: 2.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRD-------PgfaRVLIMTPTRE 84
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetkddgP---YALILAPTRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 85 LAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMGF 164
Cdd:cd17945 78 LAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497524335 165 RSEMMKICD------------EATNR--------RQCFLFSATLEgDSVERFADTILNDPA 205
Cdd:cd17945 158 EPQVTKILDampvsnkkpdteEAEKLaasgkhryRQTMMFTATMP-PAVEKIAKGYLRRPV 217
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
12-206 |
2.95e-49 |
|
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: 165.61 E-value: 2.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQ--YLLDF-PRRDPGfarVLIMTPTRELAYQ 88
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllYKLKFkPRNGTG---VIIISPTRELALQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 89 IHeqCVL--FAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMK-TEEFHAENVEILILDEADRMLDMGFR 165
Cdd:cd17942 78 IY--GVAkeLLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQnTKGFLYKNLQCLIIDEADRILEIGFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497524335 166 SEMMKICDEATNRRQCFLFSATlEGDSVERFADTILNDPAL 206
Cdd:cd17942 156 EEMRQIIKLLPKRRQTMLFSAT-QTRKVEDLARISLKKKPL 195
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
25-196 |
7.02e-49 |
|
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: 163.18 E-value: 7.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 25 TSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDfprRDPGFaRVLIMTPTRELAYQIHEQCVLFAANTHLKI 104
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDK---LDNGP-QALVLAPTRELAEQIYEELKKLGKGLGLKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 105 GVVTGGINYGSHKDIFeKNNDILIATPGRLMDYMKtEEFHAENVEILILDEADRMLDMGFRSEMMKICDEATNRRQCFLF 184
Cdd:pfam00270 77 ASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
|
170
....*....|..
gi 497524335 185 SATLeGDSVERF 196
Cdd:pfam00270 155 SATL-PRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
16-204 |
1.22e-46 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 158.81 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 16 IDKAGYKTPTSIQQLAIPEAMAG-RDILASAPTGTGKTAAFLLPSIQYLLDFPRRdpgfaRVLIMTPTRELAYQIHEQCV 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG-----RVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 95 LFAANTHLKIGVVTGGINYGSHKDIFEKNN-DILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMGFRSEMMKICD 173
Cdd:smart00487 76 KLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
|
170 180 190
....*....|....*....|....*....|.
gi 497524335 174 EATNRRQCFLFSATLEGDsVERFADTILNDP 204
Cdd:smart00487 156 LLPKNVQLLLLSATPPEE-IENLLELFLNDP 185
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
3-187 |
2.70e-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: 159.44 E-value: 2.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLD------FPRRDPGFAR- 75
Cdd:cd18051 23 FSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEqgpgesLPSESGYYGRr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 76 -----VLIMTPTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEI 150
Cdd:cd18051 103 kqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKY 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497524335 151 LILDEADRMLDMGFRSEMMKICDE----ATNRRQCFLFSAT 187
Cdd:cd18051 183 LVLDEADRMLDMGFEPQIRRIVEQdtmpPTGERQTLMFSAT 223
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
12-204 |
3.29e-46 |
|
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: 158.13 E-value: 3.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPR---RDPGfARVLIMTPTRELAYQ 88
Cdd:cd17949 2 VSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPrvdRSDG-TLALVLVPTRELALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 89 IHEQCVLFAANTH-LKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMK-TEEFHAENVEILILDEADRMLDMGFRS 166
Cdd:cd17949 81 IYEVLEKLLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKnTQSFDVSNLRWLVLDEADRLLDMGFEK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497524335 167 EMMKI-------------CDEATNRRQCFLFSATLEgDSVERFADTILNDP 204
Cdd:cd17949 161 DITKIlellddkrskaggEKSKPSRRQTVLVSATLT-DGVKRLAGLSLKDP 210
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
12-204 |
1.39e-45 |
|
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: 156.20 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDfPRRDPGFARV--LIMTPTRELAYQI 89
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLK-RKANLKKGQVgaLIISPTRELATQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 90 HEQCVLFAA--NTHLKIGVVTGGINYGSHKDIFEKNN-DILIATPGRLMDY--MKTEEFHAENVEILILDEADRMLDMGF 164
Cdd:cd17960 80 YEVLQSFLEhhLPKLKCQLLIGGTNVEEDVKKFKRNGpNILVGTPGRLEELlsRKADKVKVKSLEVLVLDEADRLLDLGF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 497524335 165 RSEMMKICDEATNRRQCFLFSATLEgDSVERFADTILNDP 204
Cdd:cd17960 160 EADLNRILSKLPKQRRTGLFSATQT-DAVEELIKAGLRNP 198
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
8-207 |
9.97e-45 |
|
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: 153.89 E-value: 9.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 8 LDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDF--PRRDPGFARVLIMTPTREL 85
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAkaESGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 86 AYQIH---EQCVLFAANtHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHA-ENVEILILDEADRMLD 161
Cdd:cd17961 81 AQQVSkvlEQLTAYCRK-DVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497524335 162 MGFRSEMMKICDEATNRRQCFLFSATLeGDSVERFADTILNDPALL 207
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLMSATL-SEDVEALKKLVLHNPAIL 204
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
12-207 |
1.38e-44 |
|
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: 153.09 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLdFPRRDPGfarVLIMTPTRELAYQIHE 91
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL-TEHRNPS---ALILTPTRELAVQIED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 92 QC-VLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMGFRSEMMK 170
Cdd:cd17962 77 QAkELMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 497524335 171 ICDEATNRRQCFLFSATLEGdSVERFADTILNDPALL 207
Cdd:cd17962 157 ILENISHDHQTILVSATIPR-GIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
12-204 |
2.47e-44 |
|
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: 152.88 E-value: 2.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPgFAR-----VLIMTPTRELA 86
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLP-FIKgegpyGLIVCPSRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 87 YQIHEQCVLFAANTH------LKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRML 160
Cdd:cd17951 80 RQTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 497524335 161 DMGFRSEMMKICDEATNRRQCFLFSATLEgDSVERFADTILNDP 204
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMP-KKIQNFAKSALVKP 202
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
12-236 |
5.79e-44 |
|
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: 152.78 E-value: 5.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMA-GRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDP-----GFARVLIMTPTREL 85
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGvggkqKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 86 AYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAEN---VEILILDEADRMLDM 162
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANlksLRFLVLDEADRMLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 163 G----FRS--EMMKICDEATNR-RQCFLFSATLegdsverfadtiLNDPALLEAESSRKEQGKIlqwvhladSRNHKLDL 235
Cdd:cd17946 161 GhfaeLEKilELLNKDRAGKKRkRQTFVFSATL------------TLDHQLPLKLNSKKKKKKK--------EKKQKLEL 220
|
.
gi 497524335 236 L 236
Cdd:cd17946 221 L 221
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
3-204 |
1.34e-43 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 150.91 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQylldfpRRDP--GFARVLIMT 80
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILE------KIDPkkDVIQALILV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 81 PTRELAYQIHEQCVLFAANTHLKIGVVTGGINygSHKDIFEKNND--ILIATPGRLMDYMKTEEFHAENVEILILDEADR 158
Cdd:cd17940 75 PTRELALQTSQVCKELGKHMGVKVMVTTGGTS--LRDDIMRLYQTvhVLVGTPGRILDLAKKGVADLSHCKTLVLDEADK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497524335 159 MLDMGFRSEMMKICDEATNRRQCFLFSATLEgDSVERFADTILNDP 204
Cdd:cd17940 153 LLSQDFQPIIEKILNFLPKERQILLFSATFP-LTVKNFMDRHMHNP 197
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
3-204 |
1.40e-42 |
|
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: 148.24 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQylldfprrdpgFARVLIMTPT 82
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-----------IVVALILEPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 83 RELAYQIHEQCVLFAA---NTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRM 159
Cdd:cd17938 70 RELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497524335 160 LDMGFRSEMMKICD------EATNRRQCFLFSATLEGDSVERFADTILNDP 204
Cdd:cd17938 150 LSQGNLETINRIYNripkitSDGKRLQVIVCSATLHSFEVKKLADKIMHFP 200
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
12-204 |
1.26e-41 |
|
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: 145.68 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLL--DFPRRDPGFARVLIMTPTRELAYQI 89
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDlqPIPREQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 90 HEQCVLFAANThLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMGFRSEMM 169
Cdd:cd17958 81 EAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*
gi 497524335 170 KICDEATNRRQCFLFSATLEgDSVERFADTILNDP 204
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWP-DGVRRLAQSYLKDP 193
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
1-203 |
1.14e-37 |
|
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: 136.29 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 1 MQFADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGFARV-LIM 79
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPIcLVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 80 TPTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRM 159
Cdd:cd18049 104 APTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 497524335 160 LDMGFRSEMMKICDEATNRRQCFLFSATLEGDsVERFADTILND 203
Cdd:cd18049 184 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKE-VRQLAEDFLKD 226
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
2-188 |
1.22e-37 |
|
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: 135.17 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 2 QFADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLldfpRRDPGFARVLIMTP 81
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL----EPVDGQVSVLVICH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 82 TRELAYQIHEQCVLFAAN-THLKIGVVTGGINYGSHKDIFEKNN-DILIATPGRLMDYMKTEEFHAENVEILILDEADRM 159
Cdd:cd17950 79 TRELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKM 158
|
170 180 190
....*....|....*....|....*....|
gi 497524335 160 L-DMGFRSEMMKICDEATNRRQCFLFSATL 188
Cdd:cd17950 159 LeQLDMRRDVQEIFRATPHDKQVMMFSATL 188
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
3-203 |
7.82e-37 |
|
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: 135.14 E-value: 7.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGFARV-LIMTP 81
Cdd:cd18050 64 FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPIcLVLAP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 82 TRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLD 161
Cdd:cd18050 144 TRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLD 223
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497524335 162 MGFRSEMMKICDEATNRRQCFLFSATLEGDsVERFADTILND 203
Cdd:cd18050 224 MGFEPQIRKIVDQIRPDRQTLMWSATWPKE-VRQLAEDFLRD 264
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
5-204 |
8.78e-37 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 132.83 E-value: 8.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 5 DLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQyLLDFPRRDPgfaRVLIMTPTRE 84
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQ-RIDTTVRET---QALVLAPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 85 LAYQIheQCVLFAANTHLKIGV--VTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDM 162
Cdd:cd17939 77 LAQQI--QKVVKALGDYMGVKVhaCIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497524335 163 GFRSEMMKICDEATNRRQCFLFSATLEGDSVErFADTILNDP 204
Cdd:cd17939 155 GFKDQIYDIFQFLPPETQVVLFSATMPHEVLE-VTKKFMRDP 195
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
12-207 |
3.72e-35 |
|
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: 129.29 E-value: 3.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAG---------RDILASAPTGTGKTAAFLLPSIQYLLDFPRRDpgfARVLIMTPT 82
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPR---LRALIVVPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 83 RELAYQIHEQCVLFAANTHLKIGVVTG---------GINYGSHKDiFEKNNDILIATPGRLMDYMK-TEEFHAENVEILI 152
Cdd:cd17956 78 KELVQQVYKVFESLCKGTGLKVVSLSGqksfkkeqkLLLVDTSGR-YLSRVDILVATPGRLVDHLNsTPGFTLKHLRFLV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497524335 153 LDEADRMLDMGFR---SEMMKICDEAT---------------NRRQC--FLFSATLEGDsVERFADTILNDPALL 207
Cdd:cd17956 157 IDEADRLLNQSFQdwlETVMKALGRPTapdlgsfgdanllerSVRPLqkLLFSATLTRD-PEKLSSLKLHRPRLF 230
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
232-340 |
1.09e-34 |
|
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: 124.25 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 232 KLDLLEAILKAEDMSKAIVFVKTREKLEELVgLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDV 311
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 497524335 312 TDISHVINYDMPRTADIYVHRIGRTGRAG 340
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
8-204 |
4.11e-33 |
|
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: 123.07 E-value: 4.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 8 LDKKILNAIDKAGYKTPTSIQQLAIPEAMAG--RDILASAPTGTGKTAAFLLPSIQYLlDFPRRDPgfaRVLIMTPTREL 85
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-DPTLKSP---QALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 86 AYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIfekNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDM-GF 164
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKI---TAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 497524335 165 RSEMMKICDEATNRRQCFLFSATLEgDSVERFADTILNDP 204
Cdd:cd17963 154 GDQSIRIKRMLPRNCQILLFSATFP-DSVRKFAEKIAPNA 192
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
3-204 |
1.96e-32 |
|
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: 121.42 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQyLLDFPRRDPgfaRVLIMTPT 82
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ-CLDIQVRET---QALILSPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 83 RELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDM 162
Cdd:cd18045 77 RELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497524335 163 GFRSEMMKICDEATNRRQCFLFSATLEGDSVErFADTILNDP 204
Cdd:cd18045 157 GFKEQIYDVYRYLPPATQVVLVSATLPQDILE-MTNKFMTDP 197
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
12-171 |
1.11e-30 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 117.47 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPG---FARVLIMTPTRELAYQ 88
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfnAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 89 IHEQCVLFAANTHLKIGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMGFRSEM 168
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
...
gi 497524335 169 MKI 171
Cdd:cd17948 161 SHF 163
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
12-208 |
1.25e-30 |
|
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: 116.21 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQyLLDFPRRDPgfaRVLIMTPTRELAYQIHE 91
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALE-SLDLERRHP---QVLILAPTREIAVQIHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 92 qCVLFAAN--THLKIGVVTGGInygSHKDIFEKNND--ILIATPGRL-----MDYMKTEEfhaenVEILILDEADRMLDM 162
Cdd:cd17943 77 -VFKKIGKklEGLKCEVFIGGT---PVKEDKKKLKGchIAVGTPGRIkqlieLGALNVSH-----VRLFVLDEADKLMEG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497524335 163 GFRSEMMKICDEATNRRQCFLFSATLEGDSVERFAdTILNDPALLE 208
Cdd:cd17943 148 SFQKDVNWIFSSLPKNKQVIAFSATYPKNLDNLLA-RYMRKPVLVR 192
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
3-194 |
1.54e-29 |
|
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: 113.69 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYlLDFPRRDPgfaRVLIMTPT 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQ-IDTSLKAT---QALVLAPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 83 RELAYQIheQCVLFAANTHLKIGV--VTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRML 160
Cdd:cd18046 77 RELAQQI--QKVVMALGDYMGIKChaCIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEML 154
|
170 180 190
....*....|....*....|....*....|....
gi 497524335 161 DMGFRSEMMKICDEATNRRQCFLFSATLEGDSVE 194
Cdd:cd18046 155 SRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLE 188
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
259-340 |
2.73e-26 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 100.75 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 259 EELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVINYDMPRTADIYVHRIGRTGR 338
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 497524335 339 AG 340
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
27-187 |
8.09e-25 |
|
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: 100.69 E-value: 8.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 27 IQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLL--DFPRRDPGFARVLIMTPTRELAYQIHEQcvlFAANTH-LK 103
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQedQQPRKRGRAPKVLVLAPTRELANQVTKD---FKDITRkLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 104 IGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMGFRSEMMKICDEA-----TNR 178
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSykkdsEDN 172
|
....*....
gi 497524335 179 RQCFLFSAT 187
Cdd:cd17944 173 PQTLLFSAT 181
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
3-216 |
7.87e-24 |
|
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: 98.94 E-value: 7.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAG--RDILASAPTGTGKTAAFLLPsiqyLLDFPRRDPGFARVLIMT 80
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLA----MLSRVDALKLYPQCLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 81 PTRELAYQ---IHEQCVLFAANTHLKIGVVTGGINYGShkdifEKNNDILIATPGRLMDY-MKTEEFHAENVEILILDEA 156
Cdd:cd18048 96 PTFELALQtgkVVEEMGKFCVGIQVIYAIRGNRPGKGT-----DIEAQIVIGTPGTVLDWcFKLRLIDVTNISVFVLDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497524335 157 DRMLDM-GFRSEMMKICDEATNRRQCFLFSATLEgDSVERFADTILNDPALLEAessRKEQ 216
Cdd:cd18048 171 DVMINVqGHSDHSVRVKRSMPKECQMLLFSATFE-DSVWAFAERIVPDPNIIKL---KKEE 227
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
3-208 |
3.87e-21 |
|
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: 90.55 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 3 FADLDLDKKILNAIDKAGYKTPTSIQQLAIPEAMAG--RDILASAPTGTGKTAAFLLPSIQYLldfprrDPG--FARVLI 78
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV------EPAnkYPQCLC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 79 MTPTRELAYQ---IHEQCVLFAANTHLKIGVVTGGINYGshkdiFEKNNDILIATPGRLMDY-MKTEEFHAENVEILILD 154
Cdd:cd18047 77 LSPTYELALQtgkVIEQMGKFYPELKLAYAVRGNKLERG-----QKISEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497524335 155 EADRML-DMGFRSEMMKICDEATNRRQCFLFSATLEgDSVERFADTILNDPALLE 208
Cdd:cd18047 152 EADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFE-DSVWKFAQKVVPDPNVIK 205
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
37-360 |
4.84e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 92.01 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 37 AGRDILASAPTGTGKT--AAFLLpsiqylldfpRRDPGFARVLIMTPTRELAYQIHEQcvlFAANTHLKIgvvtggiNYG 114
Cdd:COG1061 99 GGGRGLVVAPTGTGKTvlALALA----------AELLRGKRVLVLVPRRELLEQWAEE---LRRFLGDPL-------AGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 115 SHKDIfekNNDILIATPGRLMDYMKTEEFhAENVEILILDEADRMLDMGFRsemmKICDEATNRRqCFLFSATLE-GDS- 192
Cdd:COG1061 159 GKKDS---DAPITVATYQSLARRAHLDEL-GDRFGLVIIDEAHHAGAPSYR----RILEAFPAAY-RLGLTATPFrSDGr 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 193 ---VERFADTI--------LNDPAL-----------LEAESSRKEQGKILQWVHLADSRNHKLDLLEAILKAE-DMSKAI 249
Cdd:COG1061 230 eilLFLFDGIVyeyslkeaIEDGYLappeyygirvdLTDERAEYDALSERLREALAADAERKDKILRELLREHpDDRKTL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 250 VFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVINYDMPRTADIY 329
Cdd:COG1061 310 VFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREF 389
|
330 340 350
....*....|....*....|....*....|...
gi 497524335 330 VHRIGRT--GRAGKKGVAISLVEAHDVGILKKI 360
Cdd:COG1061 390 IQRLGRGlrPAPGKEDALVYDFVGNDVPVLEEL 422
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
38-187 |
7.87e-20 |
|
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: 85.15 E-value: 7.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 38 GRDILASAPTGTGKTAAFLLPSIQYLLDFPRrdpgfaRVLIMTPTRELAYQIHEQcVLFAANTHLKIGVVTGGINYGSHK 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGK------KVLVLVPTKALALQTAER-LRELFGPGIRVAVLVGGSSAEERE 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497524335 118 DIFEKNNDILIATPGRL-MDYMKTEEFHAENVEILILDEADRMLDMGFRSEMMKICDEATNRRQC--FLFSAT 187
Cdd:cd00046 74 KNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAqvILLSAT 146
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
12-188 |
3.57e-19 |
|
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: 86.28 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 12 ILNAIDKAGYKT-----PTSIQQLAIPeAMAGRDI-----------------LASAPTGTGKTAAFLLPSIQYLLDF--- 66
Cdd:cd17965 14 IIKEILKGSNKTdeeikPSPIQTLAIK-KLLKTLMrkvtkqtsneepklevfLLAAETGSGKTLAYLAPLLDYLKRQeqe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 67 ----------PRRDPGFARVLIMTPTRELAYQIHEqcVLFAANTHLKIGVVTGGINYG-SHKDIFEKNN---DILIATPG 132
Cdd:cd17965 93 pfeeaeeeyeSAKDTGRPRSVILVPTHELVEQVYS--VLKKLSHTVKLGIKTFSSGFGpSYQRLQLAFKgriDILVTTPG 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497524335 133 RLMDYMKTEEFHAENVEILILDEADRMLDMGFRSEMMKICDEATNRRQCFLFSATL 188
Cdd:cd17965 171 KLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATI 226
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
2-353 |
3.90e-16 |
|
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: 80.26 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 2 QFADL--DLDKKILNAIDKAGYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRrdpgfARVLIM 79
Cdd:COG1205 33 RYAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPG-----ATALYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 80 TPTRELAY-Q---IHEqcvLF-AANTHLKIGVVTGGINYGSHKDIFEkNNDILIATP-----GRLMDYMKTEEFHaENVE 149
Cdd:COG1205 108 YPTKALARdQlrrLRE---LAeALGLGVRVATYDGDTPPEERRWIRE-HPDIVLTNPdmlhyGLLPHHTRWARFF-RNLR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 150 ILILDEA---------------DRMLdmgfrsemmKICDEATNRRQCFLFSATLeGDSVErFADTILNDPALLEAESSRK 214
Cdd:COG1205 183 YVVIDEAhtyrgvfgshvanvlRRLR---------RICRHYGSDPQFILASATI-GNPAE-HAERLTGRPVTVVDEDGSP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 215 EQGK-ILQWVHLADSRNHKL-------DLLEAILKAEdmSKAIVFVKTReKLEELVGLLVARDIKTAWL-------RGEM 279
Cdd:COG1205 252 RGERtFVLWNPPLVDDGIRRsalaeaaRLLADLVREG--LRTLVFTRSR-RGAELLARYARRALREPDLadrvaayRAGY 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497524335 280 PQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVINYDMPRTADIYVHRIGRTGRAGKKGVAIsLVEAHD 353
Cdd:COG1205 329 LPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGDD 401
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-370 |
5.92e-15 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 76.47 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 1 MQFADLDLDKkILNAIDKAGYKTPTSIQQLAIPEA-MAGRDILASAPTGTGKTAAFLLPSIQYLLDFPrrdpgfaRVLIM 79
Cdd:COG1204 1 MKVAELPLEK-VIEFLKERGIEELYPPQAEALEAGlLEGKNLVVSAPTASGKTLIAELAILKALLNGG-------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 80 TPTRELAYQIHEQCVLFAANTHLKIGVVTGgiNYGSHKDIFEkNNDILIATPGRLMDYMKTEEFHAENVEILILDEAdRM 159
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTG--DYDSDDEWLG-RYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 160 LDMGFR--------SEMMKICDEAtnrrQCFLFSATLEgdSVERFADTIlnDPALLEAE--SSRKEQGKILQW-VHLAD- 227
Cdd:COG1204 149 IDDESRgptlevllARLRRLNPEA----QIVALSATIG--NAEEIAEWL--DAELVKSDwrPVPLNEGVLYDGvLRFDDg 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 228 SRNHKLDLLEAILKA-EDMSKAIVFVKTR-------EKLEELVGLLVARDIKTAWLR----------------------- 276
Cdd:COG1204 221 SRRSKDPTLALALDLlEEGGQVLVFVSSRrdaeslaKKLADELKRRLTPEEREELEElaeellevseethtnekladcle 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 277 -------GEMPQDKRMAAMANFQSGRANILVATD-------VAARGIDVTDISHVINYDMPrTADIYvHRIGRTGRAGK- 341
Cdd:COG1204 301 kgvafhhAGLPSELRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIP-VLEFK-QMAGRAGRPGYd 378
|
410 420 430
....*....|....*....|....*....|
gi 497524335 342 -KGVAIsLVEAHDVGILKKIERYTEQNLKR 370
Cdd:COG1204 379 pYGEAI-LVAKSSDEADELFERYILGEPEP 407
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
200-336 |
1.17e-13 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 72.57 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 200 ILNDPALLEAESSRKEQgkilqwvhladsRNHKLDLLEAILK--AEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRG 277
Cdd:COG0553 514 ICSHPALLLEEGAELSG------------RSAKLEALLELLEelLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHG 581
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497524335 278 EMPQDKRMAAMANFQSGRAN--ILVATDVAARGIDVTDISHVINYDMP-----------RtadiyVHRIGRT 336
Cdd:COG0553 582 GTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWwnpaveeqaidR-----AHRIGQT 648
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
229-339 |
2.54e-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: 66.85 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 229 RNHKLDLLEAILKAEDM----SKAIVFVKTR-------EKLEELVGLLVarDIKTAWLRG----------EMPQDKRMAA 287
Cdd:cd18802 5 VIPKLQKLIEILREYFPktpdFRGIIFVERRatavvlsRLLKEHPSTLA--FIRCGFLIGrgnssqrkrsLMTQRKQKET 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 497524335 288 MANFQSGRANILVATDVAARGIDVTDISHVINYDMPRTADIYVHRIGRtGRA 339
Cdd:cd18802 83 LDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
233-346 |
6.38e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 70.53 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 233 LDLLEAILKAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGE--------MPQDKRMAAMANFQSGRANILVATDV 304
Cdd:COG1111 341 REILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSV 420
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 497524335 305 AARGIDVTDISHVINYDmPRTADI-YVHRIGRTGRAGKKGVAI 346
Cdd:COG1111 421 AEEGLDIPEVDLVIFYE-PVPSEIrSIQRKGRTGRKREGRVVV 462
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
235-378 |
8.43e-13 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 69.78 E-value: 8.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 235 LLEAILKAEDMSkAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATdVA-ARGIDVTD 313
Cdd:COG0514 221 LLDFLKEHPGGS-GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPD 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497524335 314 ISHVINYDMPRTADIYVHRIGRTGRAGKKGVAISLVEAHDVGILKKI--ERYTEQNLKRRNIKGLEA 378
Cdd:COG0514 299 VRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFieQSPPDEERKRVERAKLDA 365
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
233-334 |
3.50e-12 |
|
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: 63.26 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 233 LDLLEAILKAEDmsKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRAN--ILVATDVAARGID 310
Cdd:cd18793 17 LELLEELREPGE--KVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLN 94
|
90 100 110
....*....|....*....|....*....|....*
gi 497524335 311 VTDISHVINYDMP-----------RtadiyVHRIG 334
Cdd:cd18793 95 LTAANRVILYDPWwnpaveeqaidR-----AHRIG 124
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
245-346 |
3.75e-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: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 245 MSKAIVFVKTREKLEELVGLLvardiktawlrgempqdkrmaamanfqsgraNILVATDVAARGIDVTDISHVINYDMPR 324
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASSL-------------------------------EILVATNVLGEGIDVPSLDTVIFFDPPS 51
|
90 100
....*....|....*....|..
gi 497524335 325 TADIYVHRIGRTGRAGKKGVAI 346
Cdd:cd18785 52 SAASYIQRVGRAGRGGKDEGEV 73
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
200-349 |
1.15e-10 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 63.35 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 200 ILNDPALLEAESSRKEQGKilqwvhladsrNH-KLD----LLEAILKAEDMSKAIVFVKTREKLEELVGLLVARDIKTAW 274
Cdd:PRK13766 326 LVEDPRFRKAVRKAKELDI-----------EHpKLEklreIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 275 LRGE--------MPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVINYDMPRTADIYVHRIGRTGRaGKKGVAI 346
Cdd:PRK13766 395 FVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGR-QEEGRVV 473
|
...
gi 497524335 347 SLV 349
Cdd:PRK13766 474 VLI 476
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
23-156 |
1.41e-10 |
|
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: 59.97 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 23 TPTSIQQLAIPEAM-AGRDILASAPTGTGKTAAFLLPSIQYLLDFPRrdpgfaRVLIMTPTRELAYQIHEQCVLFAANTH 101
Cdd:cd17921 1 LLNPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATSGG------KAVYIAPTRALVNQKEADLRERFGPLG 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 497524335 102 LKIGVVTGGInygSHKDIFEKNNDILIATPGRLmDYM--KTEEFHAENVEILILDEA 156
Cdd:cd17921 75 KNVGLLTGDP---SVNKLLLAEADILVATPEKL-DLLlrNGGERLIQDVRLVVVDEA 127
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
217-338 |
1.83e-10 |
|
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: 58.52 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 217 GKILQWVHlaDSRNHKLDLLEAILKAEDM---SKAIVFVKTREKLEELVGLL--VARDIKTAWLRGE--------MPQDK 283
Cdd:cd18801 1 KRKVEKIH--PKLEKLEEIVKEHFKKKQEgsdTRVIIFSEFRDSAEEIVNFLskIRPGIRATRFIGQasgksskgMSQKE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 497524335 284 RMAAMANFQSGRANILVATDVAARGIDVTDISHVINYDMPRTADIYVHRIGRTGR 338
Cdd:cd18801 79 QKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
22-156 |
5.48e-10 |
|
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: 58.43 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 22 KTPTSIQQLAIPEAMAgRDILASAPTGTGKT--AAFLLP---SIQYLLDFPRRdpgfaRVLIMTPTRELAYQiheQCVLF 96
Cdd:cd18034 1 FTPRSYQLELFEAALK-RNTIVVLPTGSGKTliAVMLIKemgELNRKEKNPKK-----RAVFLVPTVPLVAQ---QAEAI 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497524335 97 AANTHLKIGVVTGGIN----YGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEA 156
Cdd:cd18034 72 RSHTDLKVGEYSGEMGvdkwTKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
223-346 |
8.38e-10 |
|
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: 56.45 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 223 VHLADSRNHKLDLLEAILKAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVAT 302
Cdd:cd18794 8 VRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 497524335 303 DVAARGIDVTDISHVINYDMPRTADIYVHRIGRTGRAGKKGVAI 346
Cdd:cd18794 88 VAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECI 131
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
21-90 |
1.25e-09 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 60.12 E-value: 1.25e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497524335 21 YKTPTSIQQLAIPEAMAGRDILASAPTGTGKT-AAFlLPSIQYLLDFPRRDPGFA--RVLIMTPTRELAYQIH 90
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDglRVLYISPLKALANDIE 93
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-188 |
1.69e-09 |
|
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: 56.82 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 28 QQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLdfprRDPGfARVLIMTPTRELAYQIHEQCVLFAANTHLKIGV- 106
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL----RDPG-SRALYLYPTKALAQDQLRSLRELLEQLGLGIRVa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 107 -VTGGINYGSHKDIFEKNNDILIATPGRLmDYM-----KTEEFHAENVEILILDEAdRMLDMGFRSEM-------MKICD 173
Cdd:cd17923 80 tYDGDTPREERRAIIRNPPRILLTNPDML-HYAllphhDRWARFLRNLRYVVLDEA-HTYRGVFGSHValllrrlRRLCR 157
|
170
....*....|....*
gi 497524335 174 EATNRRQCFLFSATL 188
Cdd:cd17923 158 RYGADPQFILTSATI 172
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
44-188 |
7.78e-09 |
|
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: 54.23 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 44 SAPTGTGKTA-AFLLpsIQYLldfprrdpGFARVLIMTPTRELAYQIHEQCVlfAANTHLKIGVVTGGINygshkdIFEK 122
Cdd:cd17926 24 VLPTGSGKTLtALAL--IAYL--------KELRTLIVVPTDALLDQWKERFE--DFLGDSSIGLIGGGKK------KDFD 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497524335 123 NNDILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMGFRsEMMKICDEatNRRqcFLFSATL 188
Cdd:cd17926 86 DANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFS-EILKELNA--KYR--LGLTATP 146
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
231-343 |
9.27e-09 |
|
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: 54.18 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 231 HKLDLLEAILKA-EDMSKAIVFVKTREKLEELvgllvARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGI 309
Cdd:cd18789 34 NKLRALEELLKRhEQGDKIIVFTDNVEALYRY-----AKRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGI 108
|
90 100 110
....*....|....*....|....*....|....*...
gi 497524335 310 DVTDISHVI----NYDMPRTadiYVHRIGRTGRAGKKG 343
Cdd:cd18789 109 DLPEANVAIqisgHGGSRRQ---EAQRLGRILRPKKGG 143
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
23-352 |
4.33e-08 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 55.25 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 23 TPTSIQQLAIPEAMAGRDILASAPTGTGKT-AAFLLPSIQYLLDFPRRDPGFaRVLIMTPTRELAYQIHE--QCVLFAAN 99
Cdd:TIGR04121 13 TPRPFQLEMWAAALEGRSGLLIAPTGSGKTlAGFLPSLIDLAGPEAPKEKGL-HTLYITPLRALAVDIARnlQAPIEELG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 100 THLKIGVVTGGINYGSHKDIFEKNNDILIATPgrlmdymkteefhaENVEILILD-EADRMldmgFRSEMMKICDE---- 174
Cdd:TIGR04121 92 LPIRVETRTGDTSSSERARQRKKPPDILLTTP--------------ESLALLLSYpDAARL----FKDLRCVVVDEwhel 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 175 ATNRR--QCFL----------------FSATLEgdSVERFADTIL----NDPALLEAESSRK--------EQGKILQWV- 223
Cdd:TIGR04121 154 AGSKRgdQLELalarlrrlapglrrwgLSATIG--NLEEARRVLLgvggAPAVLVRGKLPKAievisllpESEERFPWAg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 224 HLAdsrnhkLDLLEAILKAEDMSK-AIVFVKTR-----------EKLEELVGLLvardiktAWLRGEMPQDKRMAAMANF 291
Cdd:TIGR04121 232 HLG------LRALPEVYAEIDQARtTLVFTNTRsqaelwfqalwEANPEFALPI-------ALHHGSLDREQRRWVEAAM 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497524335 292 QSGRANILVATDVAARGIDVTDISHVINYDMPRTADIYVHRIGRTG-RAGKKGVAIsLVEAH 352
Cdd:TIGR04121 299 AAGRLRAVVCTSSLDLGVDFGPVDLVIQIGSPKGVARLLQRAGRSNhRPGEPSRAL-LVPTN 359
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
252-350 |
1.37e-07 |
|
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: 50.73 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 252 VKTREKLEELVGllvarDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVINYDMPR--TADIY 329
Cdd:cd18792 48 EALAEELKELVP-----EARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRfgLSQLH 122
|
90 100
....*....|....*....|.
gi 497524335 330 VHRiGRTGRAGKKGVAISLVE 350
Cdd:cd18792 123 QLR-GRVGRGKHQSYCYLLYP 142
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
269-349 |
1.73e-07 |
|
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: 50.42 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 269 DIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVINYDMPRTADIYVHRI-GRTGRAGKKGVAIS 347
Cdd:cd18811 61 ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGRGDHQSYCLL 140
|
..
gi 497524335 348 LV 349
Cdd:cd18811 141 VY 142
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
20-363 |
1.89e-07 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 53.18 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 20 GYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIqyLLDfprrdpgfARVLIMTPTREL---------AYQIH 90
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL--VLD--------GLTLVVSPLISLmkdqvdqllANGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 91 EQCvLFAANTHLKIGVVTGGINYGSHKdifeknndILIATPGRLMDYMKTEEFHAENVEILILDEADRMLDMG--FRSEM 168
Cdd:PRK11057 92 AAC-LNSTQTREQQLEVMAGCRTGQIK--------LLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGhdFRPEY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 169 MKIcdeatnrrqcflfsatleGDSVERFADTilndPAL-LEAESSRKEQGKILQWVHLADS-----------------RN 230
Cdd:PRK11057 163 AAL------------------GQLRQRFPTL----PFMaLTATADDTTRQDIVRLLGLNDPliqissfdrpnirytlvEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 231 HK-LDLLEAILKAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGI 309
Cdd:PRK11057 221 FKpLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGI 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497524335 310 DVTDISHVINYDMPRTADIYVHRIGRTGRAGKKGVAISL------------VEAHDVGILKKIERY 363
Cdd:PRK11057 301 NKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFydpadmawlrrcLEEKPAGQQQDIERH 366
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
22-172 |
1.99e-07 |
|
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: 51.28 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 22 KTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGfaRVLIMTPTRELAYQIHEQCVLFAANTH 101
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKG--KVVFLANKVPLVEQQKEVFRKHFERPG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497524335 102 LKIGVVTGGInygSHKDIFE---KNNDILIATPGRLMDYMKT-EEFHAENVEILILDEADRMLDMGFRSEMMKIC 172
Cdd:cd17927 79 YKVTGLSGDT---SENVSVEqivESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDECHNTTKNHPYNEIMFRY 150
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
237-370 |
2.25e-07 |
|
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: 50.03 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 237 EAILKAEDMSKAIVFVKTR----EKLEELVGLLVArDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVT 312
Cdd:cd18810 16 EAIERELLRGGQVFYVHNRiesiEKLATQLRQLVP-EARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIP 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 313 DISHVI--NYDMPRTADIYVHRiGRTGRAGKKGVAISLVEAHdvgilkkiERYTEQNLKR 370
Cdd:cd18810 95 NANTIIieRADKFGLAQLYQLR-GRVGRSKERAYAYFLYPDQ--------KKLTEDALKR 145
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
17-160 |
4.82e-07 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 49.63 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 17 DKAGYKtPTSIQQLAIPEAMAGRDILASAPTGTGKTAaFLLPSIQYLLDFPRRdpgfarVLIMTPTRELAYQIHEQCVLF 96
Cdd:cd17924 12 KKTGFP-PWGAQRTWAKRLLRGKSFAIIAPTGVGKTT-FGLATSLYLASKGKR------SYLIFPTKSLVKQAYERLSKY 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 97 A--ANTHLKIGVVTGGINYGSHKDIFEKNN----DILIATPGRLMDYMktEEFHAENVEILILDEADRML 160
Cdd:cd17924 84 AekAGVEVKILVYHSRLKKKEKEELLEKIEkgdfDILVTTNQFLSKNF--DLLSNKKFDFVFVDDVDAVL 151
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
25-155 |
6.03e-07 |
|
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: 49.66 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 25 TSIQQLAIPEAM-AGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGFARVLIMTPTRELAYQIHEQCVLFAANTHLK 103
Cdd:cd18023 3 NRIQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLS 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 497524335 104 IGVVTGGINYGSHKDIFekNNDILIATPGRLmDYM----KTEEFHAENVEILILDE 155
Cdd:cd18023 83 CAELTGDTEMDDTFEIQ--DADIILTTPEKW-DSMtrrwRDNGNLVQLVALVLIDE 135
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
38-155 |
8.10e-07 |
|
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: 48.73 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 38 GRDILASAPTGTGKTAAFLLPSIQYLLDFPrrDPGFaRVLIMTPTRELAYQIHE--QCVLFAANTHLKIGVVTGGINYGS 115
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEP--EKGV-QVLYISPLKALINDQERrlEEPLDEIDLEIPVAVRHGDTSQSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 497524335 116 HKDIFEKNNDILIATPGRLmDYMKTEEFHAE---NVEILILDE 155
Cdd:cd17922 78 KAKQLKNPPGILITTPESL-ELLLVNKKLRElfaGLRYVVVDE 119
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
247-346 |
1.01e-06 |
|
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: 48.02 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 247 KAIVFVKTREKLEELVGLLVARDIKTAWL-------RGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVIN 319
Cdd:cd18797 37 KTIVFCRSRKLAELLLRYLKARLVEEGPLaskvasyRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
|
90 100
....*....|....*....|....*..
gi 497524335 320 YDMPRTADIYVHRIGRTGRAGKKGVAI 346
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
42-158 |
2.27e-06 |
|
DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 47.70 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 42 LASAPTGTGKT--AAFLLpsIQYLLDFPRrdpgfARVLIMTPTRELAYQIHEQCVLFAANTHLKIGVVTGGINYGSHKDI 119
Cdd:cd18033 20 LVALPTGLGKTfiAAVVM--LNYYRWFPK-----GKIVFMAPTKPLVSQQIEACYKITGIPSSQTAELTGSVPPTKRAEL 92
|
90 100 110
....*....|....*....|....*....|....*....
gi 497524335 120 FEKNNdILIATPGRLMDYMKTEEFHAENVEILILDEADR 158
Cdd:cd18033 93 WASKR-VFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHR 130
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
21-56 |
3.78e-06 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 49.11 E-value: 3.78e-06
10 20 30
....*....|....*....|....*....|....*..
gi 497524335 21 YKTPTSIQQLAIPEAMAGRDILASAPTGTGKT-AAFL 56
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL 66
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
39-189 |
4.12e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.51 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 39 RDILASAPTGTGKT--AAFLlpsIQYLLDFPRRDpgfaRVLIMTPTRELAYQIHEQCVLFAANTHLKIGVVTGGinygsH 116
Cdd:pfam04851 24 KRGLIVMATGSGKTltAAKL---IARLFKKGPIK----KVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGD-----K 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497524335 117 KDIFEKNNDILIATPGRLM--DYMKTEEFHAENVEILILDEADRmldmgFRSEMMKICDEATNRRQCFLFSATLE 189
Cdd:pfam04851 92 KDESVDDNKIVVTTIQSLYkaLELASLELLPDFFDVIIIDEAHR-----SGASSYRNILEYFKPAFLLGLTATPE 161
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
27-158 |
4.37e-06 |
|
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: 46.74 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 27 IQQLAIPEAMAGRDILASAPTGTGKTAafllpsIQYLLDFPRRDPGFARVLIMTPTRELAYQiHEQCVLFAANTHLKIGV 106
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTI------IAILVAADRLTKKGGKVLILAPSRPLVEQ-HAENLKRVLNIPDKITS 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 497524335 107 VTGGINYGSHKDIFEKNNdILIATPGRLMDYMKTEEFHAENVEILILDEADR 158
Cdd:cd18035 78 LTGEVKPEERAERWDASK-IIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
239-341 |
5.49e-06 |
|
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: 46.10 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 239 ILKAEDMSKAIVFVKTREKLEELVGLLVARDIKTAWL------RGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVT 312
Cdd:cd18796 32 IFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRVPPdfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIG 111
|
90 100
....*....|....*....|....*....
gi 497524335 313 DISHVINYDMPRTADIYVHRIGRTGRAGK 341
Cdd:cd18796 112 DVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
27-159 |
9.01e-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: 45.87 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 27 IQQLAIPEAMagrDILASAPTGTGKTAAFLLPSIQYLldfprrDPGFaRVLIMTPTRELAYQIHEQCVLFAANthLKIGV 106
Cdd:cd17918 28 EKDLHSPEPM---DRLLSGDVGSGKTLVALGAALLAY------KNGK-QVAILVPTEILAHQHYEEARKFLPF--INVEL 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 497524335 107 VTGGinygsHKDIFEKNNDILIATPGRLMdymktEEFHAENVEILILDEADRM 159
Cdd:cd17918 96 VTGG-----TKAQILSGISLLVGTHALLH-----LDVKFKNLDLVIVDEQHRF 138
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1-351 |
1.34e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 44.10 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 1 MQFADLDLDKKILNAIDKAGYKTPTSiQQLAIPEAMAGRDILASAPTGTGKTAafllpsIQYLLDFPRRDPGFARVLIMt 80
Cdd:PRK01172 1 MKISDLGYDDEFLNLFTGNDFELYDH-QRMAIEQLRKGENVIVSVPTAAGKTL------IAYSAIYETFLAGLKSIYIV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 81 PTRELAYQIHEQcVLFAANTHLKIGVVTGgiNYGSHKDiFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADRML 160
Cdd:PRK01172 73 PLRSLAMEKYEE-LSRLRSLGMRVKISIG--DYDDPPD-FIKRYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 161 D--MGFRSEMMKICDEATNRRQCFL-FSATLEGDS-VERF--ADTILND--PALLEAESSRKEQgkilqwVHLADSRNHK 232
Cdd:PRK01172 149 DedRGPTLETVLSSARYVNPDARILaLSATVSNANeLAQWlnASLIKSNfrPVPLKLGILYRKR------LILDGYERSQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 233 LDLLEAILKA-EDMSKAIVFVKTREKLEELVGLLVA-----RDIKT--------------------AWLRGEMPQDKRMA 286
Cdd:PRK01172 223 VDINSLIKETvNDGGQVLVFVSSRKNAEDYAEMLIQhfpefNDFKVssennnvyddslnemlphgvAFHHAGLSNEQRRF 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497524335 287 AMANFQSGRANILVATDVAARGIDVTdISHVINYDMPRTADIYV---------HRIGRTGRAGKKGVAISLVEA 351
Cdd:PRK01172 303 IEEMFRNRYIKVIVATPTLAAGVNLP-ARLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPGYDQYGIGYIYA 375
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
20-188 |
1.40e-04 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 42.52 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 20 GYKTPTSIQQLAIPEAMAGRDILASAPTGTGKTAAFLLPSiqYLLDfprrdpGFarVLIMTPTRELayqIHEQCvlfaan 99
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPA--LLLD------GV--TLVVSPLISL---MQDQV------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 100 THLK-IGVVTGGINygSHKDIFEKNN----------DILIATPGRLMdymkTEEFHA------ENVEI--LILDEADRML 160
Cdd:cd17920 70 DRLQqLGIRAAALN--STLSPEEKREvllrikngqyKLLYVTPERLL----SPDFLEllqrlpERKRLalIVVDEAHCVS 143
|
170 180 190
....*....|....*....|....*....|..
gi 497524335 161 DMG--FRSEMMKICD--EATNRRQCFLFSATL 188
Cdd:cd17920 144 QWGhdFRPDYLRLGRlrRALPGVPILALTATA 175
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1-363 |
2.90e-04 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 43.27 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 1 MQFADLDLDKKILNAIDKAGyktptsIQQLAIPEAMA-------GRDILASAPTGTGKTAAFLLPSIQYLLdfprRDPGF 73
Cdd:PRK00254 1 MKVDELRVDERIKRVLKERG------IEELYPPQAEAlksgvleGKNLVLAIPTASGKTLVAEIVMVNKLL----REGGK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 74 ARVLImtPTRELAYQIHEQcVLFAANTHLKIGVVTGgiNYGShKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILIL 153
Cdd:PRK00254 71 AVYLV--PLKALAEEKYRE-FKDWEKLGLRVAMTTG--DYDS-TDEWLGKYDIIIATAEKFDSLLRHGSSWIKDVKLVVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 154 DEADRM--LDMGFRSEMmkICDEATNRRQCFLFSATLeGDSVERF----ADTILND--PALLeaessRK----------E 215
Cdd:PRK00254 145 DEIHLIgsYDRGATLEM--ILTHMLGRAQILGLSATV-GNAEELAewlnAELVVSDwrPVKL-----RKgvfyqgflfwE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 216 QGKI----LQWVHLAdsrnhkldlLEAILKAEdmsKAIVFVKTREKLEElVGLLVARDIKTAWLRGE------------- 278
Cdd:PRK00254 217 DGKIerfpNSWESLV---------YDAVKKGK---GALVFVNTRRSAEK-EALELAKKIKRFLTKPElralkeladslee 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 279 ---------------------MPQDKRMAAMANFQSGRANILVATDVAARGID-------VTDISHVINYDMPRTADIYV 330
Cdd:PRK00254 284 nptneklkkalrggvafhhagLGRTERVLIEDAFREGLIKVITATPTLSAGINlpafrviIRDTKRYSNFGWEDIPVLEI 363
|
410 420 430
....*....|....*....|....*....|....*.
gi 497524335 331 HR-IGRTGRA--GKKGVAISLVEAHDVGILkkIERY 363
Cdd:PRK00254 364 QQmMGRAGRPkyDEVGEAIIVATTEEPSKL--MERY 397
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
249-342 |
5.71e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 42.19 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 249 IVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMANFQSGRANILVATDVAARGIDVTDISHVINYDMPRTADI 328
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|....
gi 497524335 329 YVHRIGRTGRAGKK 342
Cdd:PLN03137 764 YHQECGRAGRDGQR 777
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
31-83 |
8.43e-04 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 41.45 E-value: 8.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 497524335 31 AIPEAMA-GRDILASAPTGTGKTAAFLLPSIQYLLDFPRrdpgfaRVLIMTPTR 83
Cdd:COG1199 25 AVARALAeGRHLLIEAGTGTGKTLAYLVPALLAARETGK------KVVISTATK 72
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
29-155 |
1.28e-03 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain] Cd Length: 202 Bit Score: 39.80 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 29 QLAIPeAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGfaRVLIMTpTRELAYQihEQCVLFA---ANTHLKIG 105
Cdd:cd18073 9 ELALP-AMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKG--KVVFFA-TKVPVYE--QQKSVFSkyfERHGYRVT 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 497524335 106 VVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENV-EILILDE 155
Cdd:cd18073 83 GISGATAENVPVEQIIENNDIIILTPQILVNNLKKGTIPSLSIfTLMIFDE 133
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
24-158 |
1.51e-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: 39.08 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 24 PTSIQQLAIPEAMAGRD-----ILASAPTGTGKT--AAFLLPsiqyllDFPRRDPgFARVLIMTPTRELAYQIHEQcvLF 96
Cdd:cd18032 1 PRYYQQEAIEALEEAREkgqrrALLVMATGTGKTytAAFLIK------RLLEANR-KKRILFLAHREELLEQAERS--FK 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497524335 97 AANTHLKIGVVTGGinygshkDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDEADR 158
Cdd:cd18032 72 EVLPDGSFGNLKGG-------KKKPDDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHH 126
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
45-342 |
1.73e-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: 40.11 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 45 APTGTGKT-AAFLLPSiqYLLDFPRRDpgfaRVLIMTPTRELAYQIHEQCV-LFAANTHLKIGVVTGGINYGSHKDIFE- 121
Cdd:cd09639 6 APTGYGKTeAALLWAL--HSLKSQKAD----RVIIALPTRATINAMYRRAKeAFGETGLYHSSILSSRIKEMGDSEEFEh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 122 ------KNND------ILIATPGRLMDYMKTEEFHAE--NVEI----LILDEADRMLD--MGFRSEMMKICDEatNRRQC 181
Cdd:cd09639 80 lfplyiHSNDtlfldpITVCTIDQVLKSVFGEFGHYEftLASIanslLIFDEVHFYDEytLALILAVLEVLKD--NDVPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 182 FLFSATLEgDSVERFADTILNDpalLEAESSRKEQGKILQWVHLADSRNHKLDLLEAILKA-EDMSKAIVFVKTREKLEE 260
Cdd:cd09639 158 LLMSATLP-KFLKEYAEKIGYV---EENEPLDLKPNERAPFIKIESDKVGEISSLERLLEFiKKGGSVAIIVNTVDRAQE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 261 LVGLL--VARDIKTAWLRGEMPQ----DKRMAAMANFQSGRANILVATDVAARGIdvtDISHVINYDMPRTADIYVHRIG 334
Cdd:cd09639 234 FYQQLkeKGPEEEIMLIHSRFTEkdraKKEAELLLEFKKSEKFVIVATQVIEASL---DISVDVMITELAPIDSLIQRLG 310
|
....*...
gi 497524335 335 RTGRAGKK 342
Cdd:cd09639 311 RLHRYGEK 318
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
28-187 |
1.93e-03 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 39.16 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 28 QQLAIPEAMAGRDILASAPTGTGKTAAFLLPSiqYLLDfpRRDPGFArvLIMTPTRELayqIHEQcvLFAANTHLKIGVV 107
Cdd:cd18018 17 QEEAIARLLSGRSTLVVLPTGAGKSLCYQLPA--LLLR--RRGPGLT--LVVSPLIAL---MKDQ--VDALPRAIKAAAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 108 TGGINYGSHKDIFEKNN----DILIATPGRLmdymKTEEF-----HAENVEILILDEADRMLDMG--FRSEMMKICD--E 174
Cdd:cd18018 86 NSSLTREERRRILEKLRagevKILYVSPERL----VNESFrellrQTPPISLLVVDEAHCISEWShnFRPDYLRLCRvlR 161
|
170
....*....|....
gi 497524335 175 ATNRRQCFL-FSAT 187
Cdd:cd18018 162 ELLGAPPVLaLTAT 175
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
243-314 |
4.24e-03 |
|
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: 36.77 E-value: 4.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497524335 243 EDMSKAIVFVKTREKLEELVGLLVARDIKTAWLRGEMPQDKRMAAMA---NFQSGRANILVATDVAARGIDVTDI 314
Cdd:cd18799 4 YVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEALillFFGELKPPILVTVDLLTTGVDIPEV 78
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
33-155 |
6.03e-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: 37.31 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 33 PEAMA-------GRDILASAPTGTGKTAAFLLPSIQYLLDfprrdpgFARVLIMTPTRELAYQIHEQcvlFAA--NTHLK 103
Cdd:cd18028 5 PQAEAvragllkGENLLISIPTASGKTLIAEMAMVNTLLE-------GGKALYLVPLRALASEKYEE---FKKleEIGLK 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 497524335 104 IGVVTGgiNYGShKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEILILDE 155
Cdd:cd18028 75 VGISTG--DYDE-DDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE 123
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
29-155 |
7.25e-03 |
|
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: 37.46 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 29 QLAIPeAMAGRDILASAPTGTGKTAAFLLPSIQYLLDFPRRDPGfARVLIMTPTRELAyqihEQCVLFAANTHLKIGVVT 108
Cdd:cd18036 9 ELVLP-ALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEK-GRVVVLVNKVPLV----EQQLEKFFKYFRKGYKVT 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 497524335 109 GGINYGSHKDIFE---KNNDILIATPGRLMDYMKT----EEFHAENVEILILDE 155
Cdd:cd18036 83 GLSGDSSHKVSFGqivKASDVIICTPQILINNLLSgreeERVYLSDFSLLIFDE 136
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
29-198 |
9.87e-03 |
|
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; 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; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D
Pssm-ID: 187841 [Multi-domain] Cd Length: 353 Bit Score: 37.93 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 29 QLAIPEAMAGRD---ILASAPTGTGKTAAFLLPSIQYLLDFprrdpgfarvLIMTPTRELAYQIHEQC------------ 93
Cdd:cd09710 2 QVATFEALQSKDadiIFNTAPTGAGKTLAWLTPLLHGENKA----------IALYPTNALIEDQTEAIkefvddanprhq 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497524335 94 VLFAANTHLK-------IGVVTGGINYGSHKDIFEKNNDILIATPGRLMDYMKTEEFHAENVEI---------LILDE-- 155
Cdd:cd09710 72 VKSLSASDITlwpndknVGSSKGEKLYNLLRNDIGTSTPIILLTNPDIFVYLTRFAYIDRGDIAagfytkfstVIFDEfh 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497524335 156 ---ADRMLDMGFRSEMMKICDEATNRRQCFLFSATLEGDSVERFAD 198
Cdd:cd09710 152 lydAKQLVGLLFYLAYMQLIRFFECRRKFVFLSATPDPALILRLQN 197
|
|
| |
