|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-458 |
0e+00 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 750.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 1 MTDFSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTR 80
Cdd:PRK11776 3 MTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 81 ELADQVGKQIRKLATGIPNLKLLLLVGGVPLGPQLASLEgHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLD 160
Cdd:PRK11776 83 ELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLE-HGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 161 MGFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVTVEGADQAPAIRHLFCEVEPAHRQKALAGLLLKYT 240
Cdd:PRK11776 162 MGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDERLPALQRLLLHHQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 241 PESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDVEELAAVINYELPT 320
Cdd:PRK11776 242 PESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 321 DVESYQHRVGRTGRAGASGLAISLVAGREKTRAEAIEAQMGQPLDWQKTPLATSRPAELPQAAMRTLRIDGGKTDKLRPG 400
Cdd:PRK11776 322 DPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVTLCIDGGKKDKLRPG 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 896565518 401 DILGALTGDAGLSSKFIGKIAIFPTRSYVAIAREQANKAVAKLEAGKIKGRRFRVRMM 458
Cdd:PRK11776 402 DILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRLL 459
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-370 |
8.18e-172 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 488.50 E-value: 8.18e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 1 MTDFSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIR-VQALVLCPT 79
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 80 RELADQVGKQIRKLAT-----------GIPnlkllllvggvpLGPQLASLEGHdPHVVVGTPGRVQELARKRALNLGAVR 148
Cdd:COG0513 81 RELALQVAEELRKLAKylglrvatvygGVS------------IGRQIRALKRG-VDIVVATPGRLLDLIERGALDLSGVE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 149 TLVLDEADRMLDMGFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVTVEGADQ-APAIRHLFCEVEPAH 227
Cdd:COG0513 148 TLVLDEADRMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENAtAETIEQRYYLVDKRD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 228 RQKALAGLLLKYTPESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDV 307
Cdd:COG0513 228 KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDI 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896565518 308 EELAAVINYELPTDVESYQHRVGRTGRAGASGLAISLVAGREKTRAEAIEAQMGQPLDWQKTP 370
Cdd:COG0513 308 DDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELP 370
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
2-365 |
4.25e-90 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 280.68 E-value: 4.25e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 2 TDFSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAI------DPSLIRVqaLV 75
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfprrKSGPPRI--LI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 76 LCPTRELADQVGKQIRKLATGipnlkllllvggvpLGPQLASLEG---HDPH---------VVVGTPGRVQELARKRALN 143
Cdd:PRK11192 79 LTPTRELAMQVADQARELAKH--------------THLDIATITGgvaYMNHaevfsenqdIVVATPGRLLQYIKEENFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 144 LGAVRTLVLDEADRMLDMGFEEPIREIAGRTHKDRQSLLFSATFP-DSIRTMARDLLRDAVEVTVEgadqaPAIR----- 217
Cdd:PRK11192 145 CRAVETLILDEADRMLDMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAE-----PSRRerkki 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 218 ----HLFCEVEpaHRQKALAGLLLKYTPESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCN 293
Cdd:PRK11192 220 hqwyYRADDLE--HKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVN 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896565518 294 VLVASDVAARGLDVEELAAVINYELPTDVESYQHRVGRTGRAGASGLAISLVAGREKTRAEAIEAQMGQPLD 365
Cdd:PRK11192 298 VLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLK 369
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
2-360 |
3.87e-84 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 270.95 E-value: 3.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 2 TDFSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRE 81
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 82 LADQVGKQIRKLATGIPNLKLLLLVGGVPLGPQLASLEgHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDM 161
Cdd:PRK11634 86 LAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALR-QGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 162 GFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVTVEGA-DQAPAIRHLFCEVEPAHRQKALAGLLLKYT 240
Cdd:PRK11634 165 GFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSvTTRPDISQSYWTVWGMRKNEALVRFLEAED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 241 PESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDVEELAAVINYELPT 320
Cdd:PRK11634 245 FDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM 324
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 896565518 321 DVESYQHRVGRTGRAGASGLAISLVAGREKTRAEAIEAQM 360
Cdd:PRK11634 325 DSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTM 364
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
13-206 |
3.70e-81 |
|
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: 249.28 E-value: 3.70e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 13 LQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIR----VQALVLCPTRELADQVGK 88
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKkgrgPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 89 QIRKLATGiPNLKLLLLVGGVPLGPQLASLEGHdPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEPIR 168
Cdd:cd00268 81 VARKLGKG-TGLKVAAIYGGAPIKKQIEALKKG-PDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 896565518 169 EIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVT 206
Cdd:cd00268 159 KILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
4-345 |
7.30e-74 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 239.32 E-value: 7.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIR------VQALVLC 77
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 78 PTRELADQVGKQIRKLATGIpNLKLLLLVGGVPLGPQLASLEGhDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADR 157
Cdd:PRK10590 83 PTRELAAQIGENVRDYSKYL-NIRSLVVFGGVSINPQMMKLRG-GVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 158 MLDMGFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVTV----EGADQAPAIRHLfceVEPAHRQKALA 233
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVarrnTASEQVTQHVHF---VDKKRKRELLS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 234 GLLLKYTPESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDVEELAAV 313
Cdd:PRK10590 238 QMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHV 317
|
330 340 350
....*....|....*....|....*....|..
gi 896565518 314 INYELPTDVESYQHRVGRTGRAGASGLAISLV 345
Cdd:PRK10590 318 VNYELPNVPEDYVHRIGRTGRAAATGEALSLV 349
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
4-357 |
4.05e-72 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 233.18 E-value: 4.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRELA 83
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 84 DQVGKQIRKLATGIpNLKLLLLVGGVPLGPQLASLEgHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGF 163
Cdd:PTZ00424 110 QQIQKVVLALGDYL-KVRCHACVGGTVVRDDINKLK-AGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 164 EEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAV-------EVTVEGadqapaIRHLFCEVE-PAHRQKALAGL 235
Cdd:PTZ00424 188 KGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKrilvkkdELTLEG------IRQFYVAVEkEEWKFDTLCDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 236 LLKYTPESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDVEELAAVIN 315
Cdd:PTZ00424 262 YETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVIN 341
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 896565518 316 YELPTDVESYQHRVGRTGRAGASGLAISLVAGREKTRAEAIE 357
Cdd:PTZ00424 342 YDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIE 383
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
17-343 |
6.73e-72 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 236.59 E-value: 6.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 17 LDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLgllqaidPSLIRVQA------------LVLCPTRELAD 84
Cdd:PTZ00110 145 LKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLL-------PAIVHINAqpllrygdgpivLVLAPTRELAE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 85 QVGKQIRKLAT-----------GIPNLKllllvggvplgpQLASLEgHDPHVVVGTPGRVQELARKRALNLGAVRTLVLD 153
Cdd:PTZ00110 218 QIREQCNKFGAsskirntvaygGVPKRG------------QIYALR-RGVEILIACPGRLIDFLESNVTNLRRVTYLVLD 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 154 EADRMLDMGFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRD-AVEVTVeGADQAPAIRHLFCEV------EPA 226
Cdd:PTZ00110 285 EADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNV-GSLDLTACHNIKQEVfvveehEKR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 227 HRQKALAGLLLKYTPEsAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLD 306
Cdd:PTZ00110 364 GKLKMLLQRIMRDGDK-ILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLD 442
|
330 340 350
....*....|....*....|....*....|....*..
gi 896565518 307 VEELAAVINYELPTDVESYQHRVGRTGRAGASGLAIS 343
Cdd:PTZ00110 443 VKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYT 479
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
2-378 |
1.51e-68 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 225.95 E-value: 1.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 2 TDFSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLG----LLQAIDPS---LIRVQAL 74
Cdd:PRK01297 87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISiinqLLQTPPPKeryMGEPRAL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 75 VLCPTRELADQVGKQIRKLaTGIPNLKLLLLVGGVPLGPQLASLEGHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDE 154
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAAL-TKYTGLNVMTFVGGMDFDKQLKQLEARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 155 ADRMLDMGFEEPIREIAGRT-HK-DRQSLLFSATFPDSIRTMARDLLRDAVEVTVEGADQAPAI--RHLFCeVEPAHRQK 230
Cdd:PRK01297 246 ADRMLDMGFIPQVRQIIRQTpRKeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTveQHVYA-VAGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 231 ALAGLLLKYTPESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDVEEL 310
Cdd:PRK01297 325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896565518 311 AAVINYELPTDVESYQHRVGRTGRAGASGLAISLVAGREKTRAEAIEAQMGQPLDWQKTPLATSRPAE 378
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAELLKPVP 472
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
4-344 |
4.13e-67 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 220.61 E-value: 4.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLG----LLQAIDPSLIRV---QALVL 76
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKVnqpRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 77 CPTRELADQVGKQIRKLA--TGIpnlKLLLLVGGVPLGPQLASLE-GHDphVVVGTPGRVQELARKRALNLGAVRTLVLD 153
Cdd:PRK04837 90 APTRELAVQIHADAEPLAqaTGL---KLGLAYGGDGYDKQLKVLEsGVD--ILIGTTGRLIDYAKQNHINLGAIQVVVLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 154 EADRMLDMGFEEPIREIAGR--THKDRQSLLFSATFPDSIRTMARDLLRDAVEVTVEgADQAPAIR---HLFcevEPAHR 228
Cdd:PRK04837 165 EADRMFDLGFIKDIRWLFRRmpPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVE-PEQKTGHRikeELF---YPSNE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 229 QKA--LAGLLLKYTPESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLD 306
Cdd:PRK04837 241 EKMrlLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLH 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 896565518 307 VEELAAVINYELPTDVESYQHRVGRTGRAGASGLAISL 344
Cdd:PRK04837 321 IPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
4-380 |
1.06e-58 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 202.49 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAI--DPSLIR-----VQALVL 76
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsRPALADrkpedPRALIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 77 CPTRELADQVGKQIRKLATGIPNLKLLLLVGGVPLGPQLASLEGHDphVVVGTPGR-VQELARKRALNLGAVRTLVLDEA 155
Cdd:PRK04537 91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVD--VIIATPGRlIDYVKQHKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 156 DRMLDMGFEEPIREIAGRTHK--DRQSLLFSATFPDSIRTMARDLLRDAVEVTVEGAD-QAPAIRHLFCEVEPAHRQKAL 232
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETiTAARVRQRIYFPADEEKQTLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 233 AGLLLKYTPESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDVEELAA 312
Cdd:PRK04537 249 LGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896565518 313 VINYELPTDVESYQHRVGRTGRAGASGLAISLVAGREKTRAEAIEAQMGQ--PLDWQKTPLAT--SRPAELP 380
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQkiPVEPVTAELLTplPRPPRVP 400
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
4-207 |
1.10e-54 |
|
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: 181.53 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAI----------DPSLIRVQA 73
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvgrGRRKAYPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 74 LVLCPTRELADQVGKQIRKLA--TGIPNLKLLLLVGGVPLGPQLasLEGhdPHVVVGTPGRVQELARKRALNLGAVRTLV 151
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSyrSGVRSVVVYGGADVVHQQLQL--LRG--CDILVATPGRLVDFIERGRISLSSIKFLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896565518 152 LDEADRMLDMGFEEPIREIAgrTHKD------RQSLLFSATFPDSIRTMARDLLRDAVEVTV 207
Cdd:cd17967 158 LDEADRMLDMGFEPQIRKIV--EHPDmppkgeRQTLMFSATFPREIQRLAADFLKNYIFLTV 217
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
26-192 |
2.21e-54 |
|
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: 178.98 E-value: 2.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 26 TPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRELADQVGKQIRKLATGIpNLKLLLL 105
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 106 VGGVPLGPQLASLEGhdPHVVVGTPGRVQELARKRALnLGAVRTLVLDEADRMLDMGFEEPIREIAGRTHKDRQSLLFSA 185
Cdd:pfam00270 80 LGGDSRKEQLEKLKG--PDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156
|
....*..
gi 896565518 186 TFPDSIR 192
Cdd:pfam00270 157 TLPRNLE 163
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
216-345 |
3.07e-54 |
|
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: 177.31 E-value: 3.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 216 IRHLFCEVEPAHR-QKALAGLLLKYTPESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNV 294
Cdd:cd18787 1 IKQLYVVVEEEEKkLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 896565518 295 LVASDVAARGLDVEELAAVINYELPTDVESYQHRVGRTGRAGASGLAISLV 345
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
3-345 |
1.07e-53 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 187.69 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 3 DFSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIdpSLIRVQ---------A 73
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRC--CTIRSGhpseqrnplA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 74 LVLCPTRELADQVGKQIRKLATGIPnlkllllvggvplgPQLASLEGHDP------------HVVVGTPGRVQELARKRA 141
Cdd:PLN00206 200 MVLTPTRELCVQVEDQAKVLGKGLP--------------FKTALVVGGDAmpqqlyriqqgvELIVGTPGRLIDLLSKHD 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 142 LNLGAVRTLVLDEADRMLDMGFEEPIREIAgRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVTVeGADQAP--AIRHL 219
Cdd:PLN00206 266 IELDNVSVLVLDEVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPEVEKFASSLAKDIILISI-GNPNRPnkAVKQL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 220 FCEVEPAHRQKALAGLLL---KYTPeSAVVFCNTRKDVDEVANSLQQF-GFSALALHGDMEQRDREEVLLLLANRSCNVL 295
Cdd:PLN00206 344 AIWVETKQKKQKLFDILKskqHFKP-PAVVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVI 422
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 896565518 296 VASDVAARGLDVEELAAVINYELPTDVESYQHRVGRTGRAGASGLAISLV 345
Cdd:PLN00206 423 VATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
9-200 |
1.14e-50 |
|
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: 170.84 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 9 LSPALQPGLDALGYTTLTPVQAQSLPAIL-DGRDVIAQAPTGSGKTAAFGLGLLQAI--DPSLIR---VQALVLCPTREL 82
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLlnTKPAGRrsgVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 83 ADQVGKQIRKLATGIPNLKLLLLVGGVPLGPQLASLEGHDPHVVVGTPGRVQELARK--RALNLGAVRTLVLDEADRMLD 160
Cdd:cd17964 81 ALQIAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLENpgVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 896565518 161 MGFEEPIREIAG----RTHKDRQSLLFSATFPDSIRTMARDLLR 200
Cdd:cd17964 161 MGFRPDLEQILRhlpeKNADPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
4-207 |
2.17e-50 |
|
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: 172.07 E-value: 2.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQ--------AIDPSLIR-VQAL 74
Cdd:cd18052 45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTgmmkegltASSFSEVQePQAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 75 VLCPTRELADQVGKQIRKLATGIPnLKLLLLVGGVPLGPQLASLEGhDPHVVVGTPGRVQELARKRALNLGAVRTLVLDE 154
Cdd:cd18052 125 IVAPTRELANQIFLEARKFSYGTC-IRPVVVYGGVSVGHQIRQIEK-GCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 896565518 155 ADRMLDMGFEEPIREI---AGRTHK-DRQSLLFSATFPDSIRTMARDLLR-DAVEVTV 207
Cdd:cd18052 203 ADRMLDMGFGPEIRKLvsePGMPSKeDRQTLMFSATFPEEIQRLAAEFLKeDYLFLTV 260
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
9-206 |
2.56e-48 |
|
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: 164.29 E-value: 2.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 9 LSPALQPGLDALGYTTLTPVQAQSLPAILDG--RDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRELADQV 86
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 87 GKQIRKLA--TGIpnlkllllvggvplGPQLASLEGHDP-------HVVVGTPGRVQELARKRALNLGAVRTLVLDEADR 157
Cdd:cd17963 81 GEVVEKMGkfTGV--------------KVALAVPGNDVPrgkkitaQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 896565518 158 MLDM-GFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVT 206
Cdd:cd17963 147 MLDTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
4-205 |
3.62e-48 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 164.03 E-value: 3.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRELA 83
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 84 DQVGKQIRKLATGIPNLKLLLLVGGVPLGPQLASleGHDPHVVVGTPGR-VQELARKRALNLGAVRTLVLDEADRMLDMG 162
Cdd:cd17954 82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIAL--AKKPHVIVATPGRlVDHLENTKGFSLKSLKFLVMDEADRLLNMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 896565518 163 FEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEV 205
Cdd:cd17954 160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
17-208 |
1.57e-47 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 162.28 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 17 LDALGYTTLTPVQAQSLPAILDG-RDVIAQAPTGSGKTAAFGLGLLQAIDPSLiRVQALVLCPTRELADQVGKQIRKLAT 95
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 96 GIpNLKLLLLVGGVPLGPQLASLEGHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEPIREIAGRTH 175
Cdd:smart00487 80 SL-GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
|
170 180 190
....*....|....*....|....*....|...
gi 896565518 176 KDRQSLLFSATFPDSIRTMARDLLRDAVEVTVE 208
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDVG 191
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
19-206 |
1.13e-46 |
|
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: 159.89 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 19 ALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFglgllqaIDPSLIRVQ------------ALVLCPTRELADQV 86
Cdd:cd17952 7 KQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAF-------IWPMLVHIMdqrelekgegpiAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 87 GKQIRKLATgIPNLKLLLLVGGVPLGPQLASLEgHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEP 166
Cdd:cd17952 80 YLEAKKFGK-AYNLRVVAVYGGGSKWEQAKALQ-EGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 896565518 167 IREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVT 206
Cdd:cd17952 158 VRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
17-207 |
1.28e-46 |
|
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: 159.68 E-value: 1.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 17 LDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIR--VQALVLCPTRELADQVGKQIRKLA 94
Cdd:cd17957 5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIYRELLKLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 95 TGIPNLKLLLLVGGVPLGPQ-LASLEGHDphVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEPIREI-AG 172
Cdd:cd17957 85 KGTGLRIVLLSKSLEAKAKDgPKSITKYD--ILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIlAA 162
|
170 180 190
....*....|....*....|....*....|....*
gi 896565518 173 RTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVTV 207
Cdd:cd17957 163 CTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
4-205 |
2.42e-46 |
|
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: 159.39 E-value: 2.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRELA 83
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 84 DQVGKQIRKLA--TGIPNLKLLLLVGGVPLGPQLASleghDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDM 161
Cdd:cd17940 81 LQTSQVCKELGkhMGVKVMVTTGGTSLRDDIMRLYQ----TVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 896565518 162 GFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEV 205
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
16-205 |
8.10e-46 |
|
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: 157.80 E-value: 8.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 16 GLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAI--DPSLIRV-QALVLCPTRELADQVGKQIRK 92
Cdd:cd17947 4 ALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyRPKKKAAtRVLVLVPTRELAMQCFSVLQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 93 LA--TGIpnlKLLLLVGGVPLGPQLASLEGHdPHVVVGTPGRVQELARK-RALNLGAVRTLVLDEADRMLDMGFEEPIRE 169
Cdd:cd17947 84 LAqfTDI---TFALAVGGLSLKAQEAALRAR-PDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFADELKE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 896565518 170 IAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEV 205
Cdd:cd17947 160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
4-192 |
2.24e-45 |
|
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: 156.62 E-value: 2.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAI--DPSliRVQALVLCPTRE 81
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLseDPY--GIFALVLTPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 82 LADQVGKQIRKLATGIpNLKLLLLVGGVPLGPQLASLEGHdPHVVVGTPGRVQELARKRAL---NLGAVRTLVLDEADRM 158
Cdd:cd17955 79 LAYQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKR-PHIVVATPGRLADHLRSSDDttkVLSRVKFLVLDEADRL 156
|
170 180 190
....*....|....*....|....*....|....
gi 896565518 159 LDMGFEEPIREIAGRTHKDRQSLLFSATFPDSIR 192
Cdd:cd17955 157 LTGSFEDDLATILSALPPKRQTLLFSATLTDALK 190
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
4-203 |
8.74e-45 |
|
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: 155.16 E-value: 8.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRV--QALVLCPTRE 81
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVgaRALILSPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 82 LADQVGKQIRKLATGIpNLKLLLLVGGVPLGPQLASLEGhDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDM 161
Cdd:cd17959 83 LALQTLKVTKELGKFT-DLRTALLVGGDSLEEQFEALAS-NPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 896565518 162 GFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAV 203
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPV 202
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
6-205 |
4.44e-44 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 153.25 E-value: 4.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 6 TLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRELADQ 85
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 86 VGKQIRKLA--TGIPNLKLLLLVGGVPLGPQLASleghDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGF 163
Cdd:cd17939 81 IQKVVKALGdyMGVKVHACIGGTSVREDRRKLQY----GPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 896565518 164 EEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEV 205
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
13-206 |
6.99e-44 |
|
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: 152.73 E-value: 6.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 13 LQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAI-----DPSLIRVQALVLCPTRELADQVG 87
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 88 KQIRK-LATGIPNLKLLLLVGGVPLGPQLASLEGHDPHVVVGTPGRVQEL--ARKRALNLGAVRTLVLDEADRMLDMGFE 164
Cdd:cd17960 81 EVLQSfLEHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELlsRKADKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 896565518 165 EPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVT 206
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
1-206 |
1.13e-43 |
|
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: 152.92 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 1 MTDFSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAI--DPSLIRVQ---ALV 75
Cdd:cd17953 11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIkdQRPVKPGEgpiGLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 76 LCPTRELADQVGKQIRKLATGIpNLKLLLLVGGVPLGPQLASLE-GHDphVVVGTPGRVQEL---ARKRALNLGAVRTLV 151
Cdd:cd17953 91 MAPTRELALQIYVECKKFSKAL-GLRVVCVYGGSGISEQIAELKrGAE--IVVCTPGRMIDIltaNNGRVTNLRRVTYVV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 896565518 152 LDEADRMLDMGFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVT 206
Cdd:cd17953 168 LDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
28-207 |
3.69e-43 |
|
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: 150.96 E-value: 3.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 28 VQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRELADQVGKQIRKLATGIPNLKLLLLVG 107
Cdd:cd17950 28 VQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISNEYERFSKYMPNVKTAVFFG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 108 GVPLGPQLASLEGHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRML-DMGFEEPIREIAGRTHKDRQSLLFSAT 186
Cdd:cd17950 108 GVPIKKDIEVLKNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDMRRDVQEIFRATPHDKQVMMFSAT 187
|
170 180
....*....|....*....|.
gi 896565518 187 FPDSIRTMARDLLRDAVEVTV 207
Cdd:cd17950 188 LSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
16-205 |
4.59e-43 |
|
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: 150.57 E-value: 4.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 16 GLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLL-----QAIDPSLIRVQ---ALVLCPTRELADQ-- 85
Cdd:cd17951 4 GLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleQEKKLPFIKGEgpyGLIVCPSRELARQth 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 86 -VGKQIRKL--ATGIPNLKLLLLVGGVPLGPQLASLEgHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMG 162
Cdd:cd17951 84 eVIEYYCKAlqEGGYPQLRCLLCIGGMSVKEQLEVIR-KGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 896565518 163 FEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEV 205
Cdd:cd17951 163 FEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
17-206 |
3.05e-42 |
|
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: 148.29 E-value: 3.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 17 LDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLgllqaidPSLIRVQA------------LVLCPTRELAD 84
Cdd:cd17966 5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLL-------PAIVHINAqpplergdgpivLVLAPTRELAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 85 QVGKQIRKLAtGIPNLKLLLLVGGVPLGPQLASLEgHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFE 164
Cdd:cd17966 78 QIQQEANKFG-GSSRLRNTCVYGGAPKGPQIRDLR-RGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 896565518 165 EPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVT 206
Cdd:cd17966 156 PQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
1-207 |
1.67e-40 |
|
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: 145.18 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 1 MTDFSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAI-----DPSLIRVQ--- 72
Cdd:cd18051 20 IETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpGESLPSESgyy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 73 --------ALVLCPTRELADQVGKQIRKLATGiPNLKLLLLVGGVPLGPQLASLEgHDPHVVVGTPGRVQELARKRALNL 144
Cdd:cd18051 100 grrkqyplALVLAPTRELASQIYDEARKFAYR-SRVRPCVVYGGADIGQQMRDLE-RGCHLLVATPGRLVDMLERGKIGL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896565518 145 GAVRTLVLDEADRMLDMGFEEPIREIAGRTHK----DRQSLLFSATFPDSIRTMARDLLRDAVEVTV 207
Cdd:cd18051 178 DYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMpptgERQTLMFSATFPKEIQMLARDFLDNYIFLAV 244
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
9-207 |
1.98e-40 |
|
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: 143.88 E-value: 1.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 9 LSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAI------DPSLIRVQALVLCPTREL 82
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 83 ADQVGKQIRKLATGI-PNLKLLLLVGGVPLGPQLASLEGHdPHVVVGTPGR-VQELARKRALNLGAVRTLVLDEADRMLD 160
Cdd:cd17961 81 AQQVSKVLEQLTAYCrKDVRVVNLSASSSDSVQRALLAEK-PDIVVSTPARlLSHLESGSLLLLSTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 896565518 161 MGFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVTV 207
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
4-205 |
2.98e-40 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 143.23 E-value: 2.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAidpslirVQALVLCPTRELA 83
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------VVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 84 DQVGKQIRKLATGI--PNLKLLLLVGGVPLGPQLASLEGhDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDM 161
Cdd:cd17938 74 EQTYNCIENFKKYLdnPKLRVALLIGGVKAREQLKRLES-GVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 896565518 162 GFEEPIREIAGRTHK-----DR-QSLLFSATF-PDSIRTMARDLLRDAVEV 205
Cdd:cd17938 153 GNLETINRIYNRIPKitsdgKRlQVIVCSATLhSFEVKKLADKIMHFPTWV 203
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
13-206 |
4.45e-40 |
|
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: 142.30 E-value: 4.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 13 LQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFglgLLQAIDPSLIRVQ---ALVLCPTRELADQVGKQ 89
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAF---LLPVIIRCLTEHRnpsALILTPTRELAVQIEDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 90 IRKLATGIPNLKLLLLVGGVPLGPQLASLEGHdPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEPIRE 169
Cdd:cd17962 78 AKELMKGLPPMKTALLVGGLPLPPQLYRLQQG-VKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 896565518 170 IAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVT 206
Cdd:cd17962 157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
4-205 |
7.65e-40 |
|
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: 142.20 E-value: 7.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRELA 83
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 84 DQVGKQIRKLATGIpNLKLLLLVGGVPLGPQLASLEGhDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGF 163
Cdd:cd18046 81 QQIQKVVMALGDYM-GIKCHACIGGTSVRDDAQKLQA-GPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 896565518 164 EEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEV 205
Cdd:cd18046 159 KDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
17-206 |
2.43e-39 |
|
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: 141.30 E-value: 2.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 17 LDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAID-----PSLIRVQ---ALVLCPTRELADQVGK 88
Cdd:cd17945 5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlpplDEETKDDgpyALILAPTRELAQQIEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 89 QIRKLATGIPNLKLLLLVGGVPLGPQLASLEGHDphVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEPIR 168
Cdd:cd17945 85 ETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCE--ILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 896565518 169 EI--------------------AGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVT 206
Cdd:cd17945 163 KIldampvsnkkpdteeaeklaASGKHRYRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
16-205 |
9.53e-39 |
|
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: 138.94 E-value: 9.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 16 GLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRELADQVGKQIRKLAT 95
Cdd:cd17943 4 GLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 96 GIPNLKLLLLVGGVPLGPQLASLEGhdPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEPIREIAGRTH 175
Cdd:cd17943 84 KLEGLKCEVFIGGTPVKEDKKKLKG--CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLP 161
|
170 180 190
....*....|....*....|....*....|
gi 896565518 176 KDRQSLLFSATFPDSIRTMARDLLRDAVEV 205
Cdd:cd17943 162 KNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
4-205 |
1.44e-37 |
|
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: 136.06 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRELA 83
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 84 DQVGKQIRKLATGIpNLKLLLLVGGVPLGPQLASLEgHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGF 163
Cdd:cd18045 81 VQIQKVLLALGDYM-NVQCHACIGGTSVGDDIRKLD-YGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 896565518 164 EEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEV 205
Cdd:cd18045 159 KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
14-208 |
1.79e-36 |
|
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: 132.80 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 14 QPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAidpsLIRVQ--------ALVLCPTRELADQ 85
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEK----LYRERwtpedglgALIISPTRELAMQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 86 VGKQIRKLATgipNLKLLLLVGGVPLGPQLASLEGHDPHVVVGTPGRV-QELARKRALNLGAVRTLVLDEADRMLDMGFE 164
Cdd:cd17941 78 IFEVLRKVGK---YHSFSAGLIIGGKDVKEEKERINRMNILVCTPGRLlQHMDETPGFDTSNLQMLVLDEADRILDMGFK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 896565518 165 EPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVTVE 208
Cdd:cd17941 155 ETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
16-187 |
1.80e-36 |
|
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: 133.90 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 16 GLDALGYTTLTPVQAQSLP-AILDGRDVIAQAPTGSGKTAAFGLGLLQAI--------DPSLIR-VQALVLCPTRELADQ 85
Cdd:cd17946 4 ALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssngVGGKQKpLRALILTPTRELAVQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 86 VGKQIRKLA--TGIpnlkllllvggvplgpQLASLEG------------HDPHVVVGTPGRVQELARKR---ALNLGAVR 148
Cdd:cd17946 84 VKDHLKAIAkyTNI----------------KIASIVGglavqkqerllkKRPEIVVATPGRLWELIQEGnehLANLKSLR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 896565518 149 TLVLDEADRMLDMG-FEEpIREIAGRTHKD-------RQSLLFSATF 187
Cdd:cd17946 148 FLVLDEADRMLEKGhFAE-LEKILELLNKDragkkrkRQTFVFSATL 193
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
21-206 |
1.82e-34 |
|
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: 127.58 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 21 GYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGL-GLLQAIDPSLIRVQ-----ALVLCPTRELADQVGKQIRKLA 94
Cdd:cd17958 9 GFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLpGFIHLDLQPIPREQrngpgVLVLTPTRELALQIEAECSKYS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 95 TGipNLKLLLLVGGVPLGPQLASLEGhDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEPIREIAGRT 174
Cdd:cd17958 89 YK--GLKSVCVYGGGNRNEQIEDLSK-GVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKILLDI 165
|
170 180 190
....*....|....*....|....*....|..
gi 896565518 175 HKDRQSLLFSATFPDSIRTMARDLLRDAVEVT 206
Cdd:cd17958 166 RPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
22-207 |
6.20e-34 |
|
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: 127.43 E-value: 6.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 22 YTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFglgLLQAI-----DPSLIRVQA---LVLCPTRELADQV------- 86
Cdd:cd18049 44 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSY---LLPAIvhinhQPFLERGDGpicLVLAPTRELAQQVqqvaaey 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 87 GKQIRKLATGIpnlkllllVGGVPLGPQLASLEgHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEP 166
Cdd:cd18049 121 GRACRLKSTCI--------YGGAPKGPQIRDLE-RGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQ 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 896565518 167 IREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVTV 207
Cdd:cd18049 192 IRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
22-207 |
1.41e-33 |
|
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: 127.43 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 22 YTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAID--PSLIRVQA---LVLCPTRELADQV-------GKQ 89
Cdd:cd18050 82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINhqPYLERGDGpicLVLAPTRELAQQVqqvaddyGKS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 90 IRKLATGIpnlkllllVGGVPLGPQLASLEgHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEPIRE 169
Cdd:cd18050 162 SRLKSTCI--------YGGAPKGPQIRDLE-RGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRK 232
|
170 180 190
....*....|....*....|....*....|....*...
gi 896565518 170 IAGRTHKDRQSLLFSATFPDSIRTMARDLLRDAVEVTV 207
Cdd:cd18050 233 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
20-206 |
2.03e-33 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 125.39 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 20 LGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQ------ALVLCPTRELADQVGKQIRKL 93
Cdd:cd17949 9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 94 ATGIPNLKLLLLVGGVPLGPQLASLEGHDPhVVVGTPGR-VQELARKRALNLGAVRTLVLDEADRMLDMGFEEPIREI-- 170
Cdd:cd17949 89 LKPFHWIVPGYLIGGEKRKSEKARLRKGVN-ILIATPGRlLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKIle 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 896565518 171 ---AGRTHKD--------RQSLLFSATFPDSIRTMARDLLRDAVEVT 206
Cdd:cd17949 168 lldDKRSKAGgekskpsrRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| RRM_EcDbpA_like |
cd12501 |
RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; ... |
386-458 |
2.03e-33 |
|
RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of dbpA. E. coli dbpA is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity for RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions. As a non-processive ATP-dependent helicase, DbpA destabilizes and unwinds short <9bp (base pairs) RNA duplexes as well as long duplex RNA stretches. It disrupts RNA helices exclusively in a 3'- 5' direction and requires a single-stranded loading site 3' of the substrate helix. dbpA contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain binds specifically to hairpin 92.
Pssm-ID: 409924 [Multi-domain] Cd Length: 73 Bit Score: 120.42 E-value: 2.03e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896565518 386 TLRIDGGKTDKLRPGDILGALTGDAGLSSKFIGKIAIFPTRSYVAIAREQANKAVAKLEAGKIKGRRFRVRMM 458
Cdd:cd12501 1 TIQIDGGKKQKLRPGDILGALTGDNGIDGEDIGKINITDFVSYVAVKRSVAKDALKKLREGKIKGRKFRVRLL 73
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
17-204 |
3.32e-32 |
|
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: 121.49 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 17 LDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGL---LQAIDPSLIRVQA---LVLCPTRELADQVGKQI 90
Cdd:cd17944 5 LQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLiekLQEDQQPRKRGRApkvLVLAPTRELANQVTKDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 91 RKLATGIPNLKLLLLVGGVPLGPQLASleGHDphVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEPIREI 170
Cdd:cd17944 85 KDITRKLSVACFYGGTPYQQQIFAIRN--GID--ILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 896565518 171 AGRTHK-----DRQSLLFSATFPDSIRTMARDLLRDAVE 204
Cdd:cd17944 161 LSVSYKkdsedNPQTLLFSATCPDWVYNVAKKYMKSQYE 199
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
230-336 |
1.29e-30 |
|
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: 114.23 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 230 KALAGLLLKYTPESAVVFCNTRKDVDEvANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDVEE 309
Cdd:pfam00271 4 EALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
|
90 100
....*....|....*....|....*..
gi 896565518 310 LAAVINYELPTDVESYQHRVGRTGRAG 336
Cdd:pfam00271 83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
16-196 |
2.80e-28 |
|
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: 110.91 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 16 GLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFglgLLQAIDpSLIRVQ--------ALVLCPTRELADQV- 86
Cdd:cd17942 4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAF---LIPAIE-LLYKLKfkprngtgVIIISPTRELALQIy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 87 -----------------------GKQIRKLATGIPnlkllllvggvplgpqlasleghdphVVVGTPGRV-QELARKRAL 142
Cdd:cd17942 80 gvakellkyhsqtfgivigganrKAEAEKLGKGVN--------------------------ILVATPGRLlDHLQNTKGF 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 896565518 143 NLGAVRTLVLDEADRMLDMGFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMAR 196
Cdd:cd17942 134 LYKNLQCLIIDEADRILEIGFEEEMRQIIKLLPKRRQTMLFSATQTRKVEDLAR 187
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
17-186 |
1.31e-27 |
|
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: 110.03 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 17 LDALGYTTLTPVQAQSLPAILDG---------RDVIAQAPTGSGKTAAFGLGLLQAIDPSLI-RVQALVLCPTRELADQV 86
Cdd:cd17956 5 LQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVpRLRALIVVPTKELVQQV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 87 GKQIRKLATGIPNLKLLLLVGGVPLGPQLASLEGHDPH------VVVGTPGR-VQELARKRALNLGAVRTLVLDEADRML 159
Cdd:cd17956 85 YKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGRylsrvdILVATPGRlVDHLNSTPGFTLKHLRFLVIDEADRLL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 896565518 160 DMGFEE---------------PIREIAGRTHKDR-----QSLLFSAT 186
Cdd:cd17956 165 NQSFQDwletvmkalgrptapDLGSFGDANLLERsvrplQKLLFSAT 211
|
|
| DbpA |
pfam03880 |
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of ... |
386-456 |
3.43e-27 |
|
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of DEAD helicase proteins. It is sufficient to confer specificity for hairpin 92 of 23S rRNA, which is part of the ribosomal A-site. However, several members of this family lack specificity for 23S rRNA. These can proteins can generally be distinguished by a basic region that extends beyond this domain [Karl Kossen, unpublished data].
Pssm-ID: 461082 [Multi-domain] Cd Length: 72 Bit Score: 103.61 E-value: 3.43e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896565518 386 TLRIDGGKTDKLRPGDILGALTGDAGLSSKFIGKIAIFPTRSYVAIAREQANKAVAKLEAGKIKGRRFRVR 456
Cdd:pfam03880 1 RLFINVGKKDGVRPGDIVGALANEAGLPGDDIGKIDIFDNFSFVEVPAEKAEKVLKALKGTKIKGRKVRVE 71
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
255-336 |
7.20e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 97.67 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 255 DEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDVEELAAVINYELPTDVESYQHRVGRTGR 334
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 896565518 335 AG 336
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
4-201 |
1.92e-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: 101.25 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAILDG--RDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRE 81
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 82 LADQVGK---QIRKLATGIpnlkllllvggvplgPQLASLEGHDP--------HVVVGTPGRVQELARK-RALNLGAVRT 149
Cdd:cd18048 100 LALQTGKvveEMGKFCVGI---------------QVIYAIRGNRPgkgtdieaQIVIGTPGTVLDWCFKlRLIDVTNISV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 896565518 150 LVLDEADRMLDM-GFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRD 201
Cdd:cd18048 165 FVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPD 217
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
17-205 |
2.00e-24 |
|
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: 100.90 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 17 LDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAI--DPSLIRVQ-----ALVLCPTRELADQVGKQ 89
Cdd:cd17948 5 LQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrYKLLAEGPfnaprGLVITPSRELAEQIGSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 90 IRKLATGIPNLKLLLLVGGVPLGPQLASLEghDPHVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEPIRE 169
Cdd:cd17948 85 AQSLTEGLGLKVKVITGGRTKRQIRNPHFE--EVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSH 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 896565518 170 IAGRTH-------------KDRQSLLFSATFPDSirtmARDLLRDAVEV 205
Cdd:cd17948 163 FLRRFPlasrrsentdgldPGTQLVLVSATMPSG----VGEVLSKVIDV 207
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
4-201 |
5.42e-22 |
|
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: 93.63 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSPALQPGLDALGYTTLTPVQAQSLPAIL--DGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVQALVLCPTRE 81
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLaePPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 82 LADQVGKQIRKLATGIPNLKLLLlvggvplgpqlaSLEGH--------DPHVVVGTPGRVQELARK-RALNLGAVRTLVL 152
Cdd:cd18047 83 LALQTGKVIEQMGKFYPELKLAY------------AVRGNklergqkiSEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 896565518 153 DEADRML-DMGFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDLLRD 201
Cdd:cd18047 151 DEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 200
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
222-344 |
1.83e-17 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 84.42 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 222 EVEPAHRQKALAGLLLKYTPESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVA---- 297
Cdd:COG0514 211 PKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAtiaf 290
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 896565518 298 ------SDVaaRgldveelaAVINYELPTDVESYQHRVGRTGRAGASGLAISL 344
Cdd:COG0514 291 gmgidkPDV--R--------FVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
4-206 |
2.93e-17 |
|
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: 81.27 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 4 FSTLPLSP---------ALQPGLDALGYTTLTPVQAQSLPAIL---------------DGRDV--IAqAPTGSGKTAAFG 57
Cdd:cd17965 1 FDQLKLLPsvreaiikeILKGSNKTDEEIKPSPIQTLAIKKLLktlmrkvtkqtsneePKLEVflLA-AETGSGKTLAYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 58 LGLLQAID-----------------PSLIRVQALVLCPTRELADQVGKQIRKLA--TGIPNLKLLLLVGGVPLGPQLASL 118
Cdd:cd17965 80 APLLDYLKrqeqepfeeaeeeyesaKDTGRPRSVILVPTHELVEQVYSVLKKLShtVKLGIKTFSSGFGPSYQRLQLAFK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 119 EGHDphVVVGTPGRVQELARKRALNLGAVRTLVLDEADRMLDMGFEEPIREIAGRTHKDRQSLLFSATFPDSIRTMARDL 198
Cdd:cd17965 160 GRID--ILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKL 237
|
....*...
gi 896565518 199 LRDAVEVT 206
Cdd:cd17965 238 FPDVVRIA 245
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
12-314 |
5.83e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 83.15 E-value: 5.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 12 ALQPGLDALGYT-TLTPVQAQSLPAIL-----DGRDVIAQAPTGSGKTAAFglglLQAIDPSLIRVQALVLCPTRELADQ 85
Cdd:COG1061 67 ALEAGDEASGTSfELRPYQQEALEALLaalerGGGRGLVVAPTGTGKTVLA----LALAAELLRGKRVLVLVPRRELLEQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 86 VGKQIRKLATGIPNLKLLLLVggvplgpqlasleghDPHVVVGTpgrVQELARKRALN-LGAVRTLV-LDEADRMLDMGF 163
Cdd:COG1061 143 WAEELRRFLGDPLAGGGKKDS---------------DAPITVAT---YQSLARRAHLDeLGDRFGLViIDEAHHAGAPSY 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 164 EEpIREIAGRTHKdrqsLLFSAT------------------FPDSIRTMARD-LLRDA------VEVTVEGADQAPAIRH 218
Cdd:COG1061 205 RR-ILEAFPAAYR----LGLTATpfrsdgreillflfdgivYEYSLKEAIEDgYLAPPeyygirVDLTDERAEYDALSER 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 219 LFCEVEPAHRQK--ALAGLLLKYTPESAV-VFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVL 295
Cdd:COG1061 280 LREALAADAERKdkILRELLREHPDDRKTlVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRIL 359
|
330
....*....|....*....
gi 896565518 296 VASDVAARGLDVEELAAVI 314
Cdd:COG1061 360 VTVDVLNEGVDVPRLDVAI 378
|
|
| RRM_DbpA |
cd12252 |
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; ... |
386-456 |
2.48e-16 |
|
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; This subfamily corresponds to the C-terminal RRM homology domain of dbpA proteins implicated in ribosome biogenesis. They bind with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92), which is part of the ribosomal A-site. The majority of dbpA proteins contain two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding. Several members of this family lack specificity for 23S rRNA. These proteins can generally be distinguished by a basic region that extends beyond the C-terminal domain.
Pssm-ID: 409698 [Multi-domain] Cd Length: 71 Bit Score: 73.35 E-value: 2.48e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896565518 386 TLRIDGGKTDKLRPGDILGALTGDAGLSSKFIGKIAIFPTRSYVAIAREQANKAVAKLEAGKIKGRRFRVR 456
Cdd:cd12252 1 RLFINVGRKDGIDPRDLLGAICRAGGISRDDIGAIRIFDNFSFVEVPEAEAERVIEALNGKKIKGKKLRVE 71
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
242-336 |
1.13e-15 |
|
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: 73.40 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 242 ESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASdVA-ARGLDVEELAAVINYELPT 320
Cdd:cd18794 31 GSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-VAfGMGIDKPDVRFVIHYSLPK 109
|
90
....*....|....*.
gi 896565518 321 DVESYQHRVGRTGRAG 336
Cdd:cd18794 110 SMESYYQESGRAGRDG 125
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
39-186 |
8.98e-15 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 71.28 E-value: 8.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 39 GRDVIAQAPTGSGKTAAFGLGLLQAIDPSliRVQALVLCPTRELADQVGKQIRKLATGipnLKLLLLVGGVPLGPQLASL 118
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKK--GKKVLVLVPTKALALQTAERLRELFGP---GIRVAVLVGGSSAEEREKN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896565518 119 EGHDPHVVVGTPGRVQE-LARKRALNLGAVRTLVLDEADRMLDMGFEEPIREIAGRTH--KDRQSLLFSAT 186
Cdd:cd00046 76 KLGDADIIIATPDMLLNlLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAglKNAQVILLSAT 146
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
8-347 |
9.50e-15 |
|
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: 76.80 E-value: 9.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 8 PLSPALQPGLDALGYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAI--DPsliRVQALVLCPTRELA-D 84
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALleDP---GATALYLYPTKALArD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 85 QVGKqIRKLATgipnlkllllvggvplgpqlASLEGHDPHVVVG-TPGRVQELARKRA---------LNLG--------- 145
Cdd:COG1205 117 QLRR-LRELAE--------------------ALGLGVRVATYDGdTPPEERRWIREHPdivltnpdmLHYGllphhtrwa 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 146 ----AVRTLVLDEA---------------DRMldmgfeepiREIAGRTHKDRQSLLFSATFPDSiRTMARDLL-RDAVEV 205
Cdd:COG1205 176 rffrNLRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRHYGSDPQFILASATIGNP-AEHAERLTgRPVTVV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 206 TVEGADQAPAiRHLFceVEPAHRQKalaGLLLKYTPESA-------------VVFCNTRKDVDEVANSLQQ------FGF 266
Cdd:COG1205 246 DEDGSPRGER-TFVL--WNPPLVDD---GIRRSALAEAArlladlvreglrtLVFTRSRRGAELLARYARRalrepdLAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 267 SALALHGDMEQRDREEV---LlllanRSCNVLVasdVAAR-----GLDVEELAAVINYELPTDVESYQHRVGRTGRAGAS 338
Cdd:COG1205 320 RVAAYRAGYLPEERREIergL-----RSGELLG---VVSTnalelGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQD 391
|
....*....
gi 896565518 339 GLAIsLVAG 347
Cdd:COG1205 392 SLVV-LVAG 399
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
242-387 |
2.33e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 72.46 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 242 ESAVVFCNTRKDVDEVANSLQQFGFSALALHGD--------MEQRDREEVLLLLANRSCNVLVASDVAARGLDVEELAAV 313
Cdd:COG1111 354 SRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLV 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 314 INYEL-PTDVESYQhRVGRTGRAGAsGLAISLVAgrEKTRAEAI-------EAQMGQPLDWQKTPLATSRPAELPQAAMR 385
Cdd:COG1111 434 IFYEPvPSEIRSIQ-RKGRTGRKRE-GRVVVLIA--KGTRDEAYywssrrkEKKMKSILKKLKKLLDKQEKEKLKESAQA 509
|
..
gi 896565518 386 TL 387
Cdd:COG1111 510 TL 511
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
242-355 |
1.25e-11 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 66.82 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 242 ESAVVFCNTRKDVDEVANSLQQFGFSALALHGD--------MEQRDREEVLLLLANRSCNVLVASDVAARGLDVEELAAV 313
Cdd:PRK13766 366 SRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLV 445
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 896565518 314 INYE-LPTDVESYQhRVGRTGRaGASGLAISLVAgrEKTRAEA 355
Cdd:PRK13766 446 IFYEpVPSEIRSIQ-RKGRTGR-QEEGRVVVLIA--KGTRDEA 484
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
3-155 |
5.03e-11 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 64.53 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 3 DFSTLPLsPALQPGLDALGYTTLTPVQAQSLPA-ILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIrvqALVLCPTRE 81
Cdd:COG1204 2 KVAELPL-EKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK---ALYIVPLRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 82 LADQVGKQIRKL----------ATGIPNLKLLLLVggvplgpqlasleghDPHVVVGTPGRVQELARKRALNLGAVRTLV 151
Cdd:COG1204 78 LASEKYREFKRDfeelgikvgvSTGDYDSDDEWLG---------------RYDILVATPEKLDSLLRNGPSWLRDVDLVV 142
|
....
gi 896565518 152 LDEA 155
Cdd:COG1204 143 VDEA 146
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
24-200 |
7.53e-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: 58.04 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 24 TLTPVQAQSL-PAILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSLIRVqaLVLCPTRELADQVGKQIRKLATGIPNLKL 102
Cdd:cd17921 1 LLNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKA--VYIAPTRALVNQKEADLRERFGPLGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 103 LLLVGGVPLGPQLAsleghDPHVVVGTPGRVQELARK-RALNLGAVRTLVLDEAdRMLDMG-----FEEPIREIAgRTHK 176
Cdd:cd17921 79 LLTGDPSVNKLLLA-----EADILVATPEKLDLLLRNgGERLIQDVRLVVVDEA-HLIGDGergvvLELLLSRLL-RINK 151
|
170 180
....*....|....*....|....
gi 896565518 177 DRQSLLFSATFPDsirtmARDLLR 200
Cdd:cd17921 152 NARFVGLSATLPN-----AEDLAE 170
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
242-336 |
8.64e-09 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 57.98 E-value: 8.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 242 ESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDVEELAAVINYELPTD 321
Cdd:PLN03137 681 ECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKS 760
|
90
....*....|....*
gi 896565518 322 VESYQHRVGRTGRAG 336
Cdd:PLN03137 761 IEGYHQECGRAGRDG 775
|
|
| RRM_EcCsdA_like |
cd12499 |
RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and ... |
386-429 |
1.35e-08 |
|
RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of E. coli CsdA, also termed ATP-dependent RNA helicase deaD, or translation factor W2, a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. CsdA may be involved in translation initiation, gene regulation after cold-shock, mRNA decay and biogenesis of the large or small ribosomal subunit. It contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.
Pssm-ID: 409922 [Multi-domain] Cd Length: 73 Bit Score: 51.42 E-value: 1.35e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 896565518 386 TLRIDGGKTDKLRPGDILGALTGDAGLSSKFIGKIAIFPTRSYV 429
Cdd:cd12499 1 RYRIEVGRKDGVKPGNIVGAIANEAGIDSRFIGRIKIFDDHSTV 44
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
244-336 |
1.86e-08 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 51.17 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 244 AVVFCNTRKDVDEVANSLQqfgfsalalhgdmeqrdreevllllanrscnVLVASDVAARGLDVEELAAVINYELPTDVE 323
Cdd:cd18785 6 IIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSAA 54
|
90
....*....|...
gi 896565518 324 SYQHRVGRTGRAG 336
Cdd:cd18785 55 SYIQRVGRAGRGG 67
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
243-336 |
3.88e-08 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 55.49 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 243 SAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDVEELAAVINYELPTDV 322
Cdd:PRK11057 238 SGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI 317
|
90
....*....|....
gi 896565518 323 ESYQHRVGRTGRAG 336
Cdd:PRK11057 318 ESYYQETGRAGRDG 331
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
265-339 |
5.07e-08 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 51.82 E-value: 5.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896565518 265 GFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDVEELAAVINYELPTDVESYqhrVGRTGRAGASG 339
Cdd:cd18802 64 GNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSY---IQSRGRARAPN 135
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
41-336 |
1.46e-07 |
|
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: 53.20 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 41 DVIAQAPTGSGKTAAFGLGLLQAIDPSlIRVQALVLCPTRELADQVGKQIRKLAtGIPNLKLLLLVGGVPLG-------P 113
Cdd:cd09639 1 LLVIEAPTGYGKTEAALLWALHSLKSQ-KADRVIIALPTRATINAMYRRAKEAF-GETGLYHSSILSSRIKEmgdseefE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 114 QLASLEGHDPHVV------VGTPGRVQ-------ELARKRALNLGAVRtLVLDEADRMLD--MGFEEPIREIAGRthKDR 178
Cdd:cd09639 79 HLFPLYIHSNDTLfldpitVCTIDQVLksvfgefGHYEFTLASIANSL-LIFDEVHFYDEytLALILAVLEVLKD--NDV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 179 QSLLFSATFPDSIRTMARDLLRDAVEvtvEGADQAPAIRHLF--CEVEPAHRQKALAGLLLKY-TPESAVVFCNTRKDVD 255
Cdd:cd09639 156 PILLMSATLPKFLKEYAEKIGYVEEN---EPLDLKPNERAPFikIESDKVGEISSLERLLEFIkKGGSVAIIVNTVDRAQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 256 EVANSLQQFG--FSALALHGDMEQRDR----EEVLLLLANRSCNVLVASDVAARGLDVEelAAVINYEL-PTDveSYQHR 328
Cdd:cd09639 233 EFYQQLKEKGpeEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDIS--VDVMITELaPID--SLIQR 308
|
....*...
gi 896565518 329 VGRTGRAG 336
Cdd:cd09639 309 LGRLHRYG 316
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
29-97 |
1.82e-07 |
|
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: 51.05 E-value: 1.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896565518 29 QAQSLPAILDGRDVIAQAPTGSGKTAAFGLGLLQAI--DPsliRVQALVLCPTRELA-DQVGKqIRKLATGI 97
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALlrDP---GSRALYLYPTKALAqDQLRS-LRELLEQL 72
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
41-336 |
5.72e-07 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 51.30 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 41 DVIAQAPTGSGKTAAFGLGLLQAIDPSlIRVQALVLCPTRELADQVGKQIRKLaTGIPNLKLLLLVGGVPLGPQLASLE- 119
Cdd:TIGR01587 1 LLVIEAPTGYGKTEAALLWALHSIKSQ-KADRVIIALPTRATINAMYRRAKEL-FGSELVGLHHSSSFSRIKEMGDSEEf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 120 -------GHDPHVV------VGTPGRVQ-------ELARKRALNLGAVRtLVLDEADRMLD--MGFEEPIREIAGRthKD 177
Cdd:TIGR01587 79 ehlfplyIHSNDKLfldpitVCTIDQVLksvfgefGHYEFTLASIANSL-LIFDEVHFYDEytLALILAVLEVLKD--ND 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 178 RQSLLFSATFPDSIRTMARDLLRDAVEVTVEGADQAPAIRHLF--CEVEPAHRQKALAGLLLKY-TPESAVVFCNTRKDV 254
Cdd:TIGR01587 156 VPILLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFilIESDKVGEISSLERLLEFIkKGGSIAIIVNTVDRA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 255 DEVANSLQQFG--FSALALHGDMEQRDRE--EVLLLLANRSCN---VLVASDVAARGLDVEelAAVINYEL-PTDveSYQ 326
Cdd:TIGR01587 236 QEFYQQLKEKApeEEIILYHSRFTEKDRAkkEAELLREMKKSNekfVIVATQVIEASLDIS--ADVMITELaPID--SLI 311
|
330
....*....|
gi 896565518 327 HRVGRTGRAG 336
Cdd:TIGR01587 312 QRLGRLHRYG 321
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
39-215 |
5.78e-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: 49.12 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 39 GRDVIAQAPTGSGKT-AAFGLGLLQAIDPSLIRVQALVLCPTRELADQVGKQIRKLATGIPNLKLLLLVGGVPLGPQLAS 117
Cdd:cd17922 1 GRNVLIAAPTGSGKTeAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 118 LEGHDPHVVVGTPGRVQEL--ARKRALNLGAVRTLVLDEadrmldmgfeepIREIAGrthKDRQSLLFSATFpdSIRTMA 195
Cdd:cd17922 81 QLKNPPGILITTPESLELLlvNKKLRELFAGLRYVVVDE------------IHALLG---SKRGVQLELLLE--RLRKLT 143
|
170 180
....*....|....*....|.
gi 896565518 196 -RDLLRDAVEVTVEGADQAPA 215
Cdd:cd17922 144 gRPLRRIGLSATLGNLEEAAA 164
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
244-334 |
1.13e-06 |
|
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: 48.12 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 244 AVVFCNTRKDVDEVANSLQQF----------GFSALALHGDMEQRDREEVLLLLANRSCNVLVASDVAARGLDVEELAAV 313
Cdd:cd18801 33 VIIFSEFRDSAEEIVNFLSKIrpgiratrfiGQASGKSSKGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112
|
90 100
....*....|....*....|..
gi 896565518 314 INYE-LPTDVESYQhRVGRTGR 334
Cdd:cd18801 113 ICYDaSPSPIRMIQ-RMGRTGR 133
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
22-65 |
2.36e-06 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 50.10 E-value: 2.36e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 896565518 22 YTTLTPVQAQSLPAILDGRDVIAQAPTGSGKT-AAFglglLQAID 65
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF----LPALD 62
|
|
| RRM_BsYxiN_like |
cd12500 |
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and ... |
387-456 |
2.14e-05 |
|
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of YxiN. B. subtilis YxiN is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions in an ATP-dependent manner. YxiN contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.
Pssm-ID: 409923 [Multi-domain] Cd Length: 73 Bit Score: 42.45 E-value: 2.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 387 LRIDGGKTDKLRPGDILGALTGDAGLSSKFIGKIAIFPTRSYVAIAREQANKAVAKLEAGKIKGRRFRVR 456
Cdd:cd12500 2 LYFNGGKKKKIRAVDIVGAISNIDGVTGDDIGIITVQDNCSYVDILNGKGDHVLKVMKNTTIKGKQVKVN 71
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
28-85 |
2.37e-05 |
|
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: 45.04 E-value: 2.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896565518 28 VQAQSLPAILDG-RDVIAQAPTGSGKTAAFGLGLLQAI----DPSLIRVQALVLCPTRELADQ 85
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLkernPLPWGNRKVVYIAPIKALCSE 67
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
22-70 |
2.93e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 46.42 E-value: 2.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 896565518 22 YTTLTPVQAQSLPAILDGRDVIAQAPTGSGKT-AAFglglLQAIDpSLIR 70
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF----LAIID-ELFR 74
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
230-319 |
7.81e-05 |
|
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: 42.46 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 230 KALAGLL--LKYTPESAVVFCNTRKDVDEVANSLQQFGFSALALHGDMEQRDREEVLLLLANR-SCNV-LVASDVAARGL 305
Cdd:cd18793 14 EALLELLeeLREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKAGGVGL 93
|
90
....*....|....*..
gi 896565518 306 DveeLAA---VINYELP 319
Cdd:cd18793 94 N---LTAanrVILYDPW 107
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
24-195 |
8.85e-05 |
|
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: 43.17 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 24 TLTPVQAQSLPAILDG------RDVIAQAPTGSGKTAAFGLGLLQAIDPSLirvQALVLCPTRELADQVGKQIRKLATGI 97
Cdd:cd17918 15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAYKNGK---QVAILVPTEILAHQHYEEARKFLPFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 98 PnlkllllVGGVPLGPQLASLEGHDphVVVGTPGRVQELARKRALNLgavrtLVLDEADRmldMGFEEpiRE---IAGRT 174
Cdd:cd17918 92 N-------VELVTGGTKAQILSGIS--LLVGTHALLHLDVKFKNLDL-----VIVDEQHR---FGVAQ--REalyNLGAT 152
|
170 180
....*....|....*....|..
gi 896565518 175 HkdrqSLLFSAT-FPdsiRTMA 195
Cdd:cd17918 153 H----FLEATATpIP---RTLA 167
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
21-98 |
2.21e-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: 42.14 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 21 GYTTLTPVQAQSLPAILDGRDVIAQAPTGSGKTAAFGLgllqaidPSLIR--VqALVLCPTREL-ADQVgkqIRKLATGI 97
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQL-------PALLLdgV-TLVVSPLISLmQDQV---DRLQQLGI 77
|
.
gi 896565518 98 P 98
Cdd:cd17920 78 R 78
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
242-314 |
2.82e-04 |
|
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: 40.24 E-value: 2.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896565518 242 ESAVVFCNTRKDVDEVANSLQQFGFSALALHGD--MEQRDrEEVLLLLANR--SCNVLVASDVAARGLDVEELAAVI 314
Cdd:cd18799 7 IKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERG-DEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
24-85 |
1.44e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 39.19 E-value: 1.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896565518 24 TLTPVQAQSLPAILDGRD-----VIAQAPTGSGKT--AAFglgLLQAIDPSLIRVQALVLCPTRELADQ 85
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKngqkrGLIVMATGSGKTltAAK---LIARLFKKGPIKKVLFLVPRKDLLEQ 68
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
39-192 |
2.35e-03 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain] Cd Length: 186 Bit Score: 38.81 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 39 GRDVIAQAPTGSGKT-AAFGLGLLQAIDPSLIRVqaLVLCPTRELADQVGKQIRKLATGIP------------------N 99
Cdd:cd17930 1 PGLVILEAPTGSGKTeAALLWALKLAARGGKRRI--IYALPTRATINQMYERIREILGRLDdedkvlllhskaalelleS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 100 LKLLLLVGGVPLGPQLASLEGHDPHVVVGTPgrVQEL--------ARKRALNL-GAVrtLVLDEA----DRMLDMgFEEP 166
Cdd:cd17930 79 DEEPDDDPVEAVDWALLLKRSWLAPIVVTTI--DQLLesllkykhFERRLHGLaNSV--VVLDEVqaydPEYMAL-LLKA 153
|
170 180
....*....|....*....|....*.
gi 896565518 167 IREIAGrtHKDRQSLLFSATFPDSIR 192
Cdd:cd17930 154 LLELLG--ELGGPVVLMTATLPALLR 177
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
24-83 |
2.78e-03 |
|
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: 40.23 E-value: 2.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896565518 24 TLTPVQAQSLPAILDGRDVIAQAPTGSGKT-AAFGLGLLQAI---DPSLIRVQALVLCPTRELA 83
Cdd:TIGR04121 13 TPRPFQLEMWAAALEGRSGLLIAPTGSGKTlAGFLPSLIDLAgpeAPKEKGLHTLYITPLRALA 76
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
24-154 |
2.86e-03 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 38.47 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 24 TLTPVQAQSLPA-ILDGRDVIAQAPTGSGKTAafgLGLLQAIDPSLIRVQALVLCPTRELADQVGKQIRKL--------- 93
Cdd:cd18028 1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTL---IAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKKLeeiglkvgi 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896565518 94 ATGIPNLKLLLLvggvplgpqlaslegHDPHVVVGTPGRVQELARKRALNLGAVRTLVLDE 154
Cdd:cd18028 78 STGDYDEDDEWL---------------GDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE 123
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1-53 |
5.59e-03 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 39.15 E-value: 5.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 896565518 1 MTDFSTLP--LSPALQPGLDALGYTtLTPVQAQSLPAILDGRDVIAQAPTGSGKT 53
Cdd:COG4581 1 MTLSPARAdaRLEALADFAEERGFE-LDPFQEEAILALEAGRSVLVAAPTGSGKT 54
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
36-95 |
6.12e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 37.69 E-value: 6.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565518 36 ILDGRDVIAQAPTGSGKTAafgLGLLQAIDPSLIRVQALVLCPTRELADQVGKQIRKLAT 95
Cdd:cd17924 29 LLRGKSFAIIAPTGVGKTT---FGLATSLYLASKGKRSYLIFPTKSLVKQAYERLSKYAE 85
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
7-83 |
9.38e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 38.40 E-value: 9.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896565518 7 LPLSPALQPGLDALGYTTLTPVQAQSLPA-ILDGRDVIAQAPTGSGKTAAFGLGLLQAIDPSlirVQALVLCPTRELA 83
Cdd:PRK02362 6 LPLPEGVIEFYEAEGIEELYPPQAEAVEAgLLDGKNLLAAIPTASGKTLIAELAMLKAIARG---GKALYIVPLRALA 80
|
|
| |
