|
Name |
Accession |
Description |
Interval |
E-value |
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1-639 |
7.38e-85 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 286.23 E-value: 7.38e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 1 MSTSSAFHSLHPGIQRYlWAEQWEALREVQEMAIPAVLlADRDVVIAASTASGKTEAAFLPALTHLLN-----GDTDGL- 74
Cdd:COG1201 1 MSAEDVLSLLHPAVRAW-FAARFGAPTPPQREAWPAIA-AGESTLLIAPTGSGKTLAAFLPALDELARrprpgELPDGLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 75 IVYISPLKALINDQFGRLDRLCEDLD----IPVWPW-----HGDIGSTTKQRFFRKPTGVLLITPESLEAMLCNRGTsvA 145
Cdd:COG1201 79 VLYISPLKALANDIERNLRAPLEEIGeaagLPLPEIrvgvrTGDTPASERQRQRRRPPHILITTPESLALLLTSPDA--R 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 146 GIFKGAAFVIVDELHAFIGSERGKQLQSLMHRMEVVLERRVPRIGLSATLGDMQAAATFL---RSDGRAAIVDAQSGNN- 221
Cdd:COG1201 157 ELLRGVRTVIVDEIHALAGSKRGVHLALSLERLRALAPRPLQRIGLSATVGPLEEVARFLvgyEDPRPVTIVDAGAGKKp 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 222 ELQLIL--KGFEEPPAPQdakhEEVAPLAVAKHLHEVLCGTNNLIFPNSRREVERYTHLLNEISEQASRPREfwPHHGNL 299
Cdd:COG1201 237 DLEVLVpvEDLIERFPWA----GHLWPHLYPRVLDLIEAHRTTLVFTNTRSQAERLFQRLNELNPEDALPIA--AHHGSL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 300 SKEIRSDTEAALKQKERPAtAICTNTLELGIDIGAVKSVAQIGTPPSVASLRQRMGRSGRRKGEPAilRGYVIedaidsn 379
Cdd:COG1201 311 SREQRLEVEEALKAGELRA-VVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGHRVGEVS--KGRLV------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 380 sdlkTRLRLDTVQsiASALL------LIDKwfEPPVAGGahLSTLVQQLLS-AIAqyGGLRAPQAYQLLCASgAPFQGLS 452
Cdd:COG1201 381 ----PTHRDELVE--CAAALeaaragEIEA--RRPPRNP--LDVLAQHIVAmAAG--GPFDVDELYAEVRRA-YPYRDLT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 453 SESFVELLrhlgkqDVLTQDSSGL--------LLHGPTGDKLVNHYSFYAAF-------VADEEF--RIVAAGKTLGTLP 515
Cdd:COG1201 448 REDFDAVL------DFLAGGGPSLrayeryarIVRDRVDGRLGARRGAARLArtnigtiPDRGMLkvRLVRGGRRLGELE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 516 ---ITQmLAAGQRILFGGRTWLVEQVDETqkTIYVLAAKGGSP--PIFNGSG-------GRvhtRIRQTMHALYRGE--- 580
Cdd:COG1201 522 eefVEE-LRPGDVFVLGGRSLRIERIRGM--RVYVRPAPGKPPtvPSWFGERlplstelAR---AVGAFLRELAEWEaar 595
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2755244177 581 --LRPTFLDATASR----FLEEGKSAYEHLGLDENVLL------DQGSHFLLLTWAGDAANEAIACLLGAR 639
Cdd:COG1201 596 awLREYGLDEPAARalreYLEEQRAATSALPTDDTLLVerfrdeEGDWHLVVHPFEGRRVHEALGLLLAYR 666
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
41-205 |
6.01e-72 |
|
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: 231.32 E-value: 6.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 41 DRDVVIAASTASGKTEAAFLPALTHLLNGDTDGL-IVYISPLKALINDQFGRLDRLCE--DLDIPVWPWHGDIGSTTKQR 117
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVqVLYISPLKALINDQERRLEEPLDeiDLEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 118 FFRKPTGVLLITPESLEAMLCNRGTSvaGIFKGAAFVIVDELHAFIGSERGKQLQSLMHRMEVVLERRVPRIGLSATLGD 197
Cdd:cd17922 81 QLKNPPGILITTPESLELLLVNKKLR--ELFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKLTGRPLRRIGLSATLGN 158
|
....*...
gi 2755244177 198 MQAAATFL 205
Cdd:cd17922 159 LEEAAAFL 166
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
13-547 |
6.91e-55 |
|
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: 201.22 E-value: 6.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 13 GIQRyLWAEQWEALREVqemaipavlLADRDVVIAASTASGKTEAAFLPALTHLLNgDTDGLIVYISPLKALINDQFGRL 92
Cdd:COG1205 53 GIER-LYSHQAEAIEAA---------RAGKNVVIATPTASGKSLAYLLPVLEALLE-DPGATALYLYPTKALARDQLRRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 93 DRLCE--DLDIPVWPWHGDIGSTTKQRFFRKPTgVLLITPESLEAMLCNRGTSVAGIFKGAAFVIVDELHAFIGSErGKQ 170
Cdd:COG1205 122 RELAEalGLGVRVATYDGDTPPEERRWIREHPD-IVLTNPDMLHYGLLPHHTRWARFFRNLRYVVIDEAHTYRGVF-GSH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 171 LQSLMHRMEVVLER--RVPR-IGLSATLGDMQAAATFLrSDGRAAIVD---AQSGnnELQLIlkgFEEPPAPQDAkhEEV 244
Cdd:COG1205 200 VANVLRRLRRICRHygSDPQfILASATIGNPAEHAERL-TGRPVTVVDedgSPRG--ERTFV---LWNPPLVDDG--IRR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 245 APLAVAKHL--HEVLCGTNNLIFPNSRREVERYTHLLNEISEQASRPREFWPHHGNLSKEIRSDTEAALKQKErPATAIC 322
Cdd:COG1205 272 SALAEAARLlaDLVREGLRTLVFTRSRRGAELLARYARRALREPDLADRVAAYRAGYLPEERREIERGLRSGE-LLGVVS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 323 TNTLELGIDIGAVKSVAQIGTPPSVASLRQRMGRSGRRKGEpailrGYVI----EDAIDS----NSDlktrlrldtvqsi 394
Cdd:COG1205 351 TNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQD-----SLVVlvagDDPLDQyyvrHPE------------- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 395 asalLLIDKWFEPPVAGGAHLSTLVQQLLSAiaqygglrapqAYQL-LCASGAPFQGlssESFVELLRHLGKQDVLTQDS 473
Cdd:COG1205 413 ----ELFERPPEAAVIDPDNPYVLAPHLLCA-----------AAELpLTEGDLELFG---PEARELLDALVEEGLLRRRG 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2755244177 474 SGLLLHGPtgDKLVNHYSFYAAfvADEEFRIVAA--GKTLGTLPITQ---MLAAGQRILFGGRTWLVEQVDETQKTIYV 547
Cdd:COG1205 475 DGWYWTGD--DRPARDVSLRGA--GGENVVIVDAttGRVIGTVDLPRalrELHPGAIYLHQGETYRVEELDLEERKAYV 549
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
10-463 |
3.07e-50 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 189.33 E-value: 3.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 10 LHPGIQRYlWAEQWEALREVQEMAIPAVLlADRDVVIAASTASGKTEAAFLPALTHLLN-GDTDGL-----IVYISPLKA 83
Cdd:PRK13767 18 LRPYVREW-FKEKFGTFTPPQRYAIPLIH-EGKNVLISSPTGSGKTLAAFLAIIDELFRlGREGELedkvyCLYVSPLRA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 84 LINDQFGRLD-----------RLCEDL-DIPVWPWHGDIGSTTKQRFFRKPTGVLLITPESLEAMLcnrgtsVAGIF--- 148
Cdd:PRK13767 96 LNNDIHRNLEeplteireiakERGEELpEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILL------NSPKFrek 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 149 -KGAAFVIVDELHAFIGSERGKQLQSLMHRMEVVLERRVPRIGLSATLGDMQAAATFL---RSDGR---AAIVDAQsgnn 221
Cdd:PRK13767 170 lRTVKWVIVDEIHSLAENKRGVHLSLSLERLEELAGGEFVRIGLSATIEPLEEVAKFLvgyEDDGEprdCEIVDAR---- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 222 elqlILKGFE---EPPAP----------QDAKHEEVAPLaVAKHlhevlcgTNNLIFPNSRREVERYTHLLNEISEQASR 288
Cdd:PRK13767 246 ----FVKPFDikvISPVDdlihtpaeeiSEALYETLHEL-IKEH-------RTTLIFTNTRSGAERVLYNLRKRFPEEYD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 289 PREFWPHHGNLSKEIRSDTEAALKQKErpATAICTNT-LELGIDIGAVKSVAQIGTPPSVASLRQRMGRSGRRKGEpaIL 367
Cdd:PRK13767 314 EDNIGAHHSSLSREVRLEVEEKLKRGE--LKVVVSSTsLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAGHRLGE--VS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 368 RGYVIedAIDsnsdlktrlRLDTVQsiaSALLL-------IDKWFEPPVAggahLSTLVQQLLS-AIAQYGGLRapQAYQ 439
Cdd:PRK13767 390 KGRII--VVD---------RDDLVE---CAVLLkkaregkIDRVHIPKNP----LDVLAQHIVGmAIERPWDIE--EAYN 449
|
490 500
....*....|....*....|....
gi 2755244177 440 LLCASgAPFQGLSSESFVELLRHL 463
Cdd:PRK13767 450 IVRRA-YPYRDLSDEDFESVLRYL 472
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
222-373 |
1.37e-49 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 170.52 E-value: 1.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 222 ELQLILKGFEEPPAPQDAkhEEVAPLAVAKHLHEVLCGTNNLIFPNSRREVERYTHLLNEISEQASRPREFWPHHGNLSK 301
Cdd:cd18796 3 KLDIKVILPVAPEIFPWA--GESGADAYAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRVPPDFIALHHGSLSR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2755244177 302 EIRSDTEAALKQKErPATAICTNTLELGIDIGAVKSVAQIGTPPSVASLRQRMGRSGRRKGePAILRGYVIE 373
Cdd:cd18796 81 ELREEVEAALKRGD-LKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG-AASKGRLVPT 150
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
46-405 |
1.39e-38 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 154.70 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 46 IAASTASGKTEAAFLPALTHLLNGDTDGL----------IVYISPLKALIND------------QFGRLDRLCEDLDIPV 103
Cdd:PRK09751 1 VIAPTGSGKTLAAFLYALDRLFREGGEDTreahkrktsrILYISPIKALGTDvqrnlqiplkgiADERRRRGETEVNLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 104 WPWHGDIGSTTKQRFFRKPTGVLLITPESLEAMLCNRGTSVagiFKGAAFVIVDELHAFIGSERGKQLQSLMHRMEVVLE 183
Cdd:PRK09751 81 GIRTGDTPAQERSKLTRNPPDILITTPESLYLMLTSRARET---LRGVETVIIDEVHAVAGSKRGAHLALSLERLDALLH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 184 RRVPRIGLSATLGDMQAAATFLRSDGRAAIVDAQSGNN-ELQLIL------KGFEEPPAPQDAKHE----EVAPLAVAKH 252
Cdd:PRK09751 158 TSAQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRHpQIRIVVpvanmdDVSSVASGTGEDSHAgregSIWPYIETGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 253 LHEVLCGTNNLIFPNSRREVERYTHLLNEI-------SEQASRPREFW--------------------PHHGNLSKEIRS 305
Cdd:PRK09751 238 LDEVLRHRSTIVFTNSRGLAEKLTARLNELyaarlqrSPSIAVDAAHFestsgatsnrvqssdvfiarSHHGSVSKEQRA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 306 DTEAALKQKERpATAICTNTLELGIDIGAVKSVAQIGTPPSVASLRQRMGRSGRRKGepAILRGYVI----EDAIDS--- 378
Cdd:PRK09751 318 ITEQALKSGEL-RCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVG--GVSKGLFFprtrRDLVDSavi 394
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2755244177 379 -NSDLKTRLR--------LD-----TVQSIASALLLIDKWF 405
Cdd:PRK09751 395 vECMFAGRLEnltpphnpLDvlaqqTVAAAAMDALQVDEWY 435
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
27-197 |
5.47e-32 |
|
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: 121.97 E-value: 5.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 27 REVQEMAIPAvLLADRDVVIAASTASGKTEAAFLPALTHLLNGDTDGLIVYISPLKALINDQFGRLDRLCEDLDIPVwpw 106
Cdd:pfam00270 1 TPIQAEAIPA-ILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 107 HGDIGSTTKQRFFRKPTG--VLLITPESLEAMLCNRGTsvagiFKGAAFVIVDELHAFIGSERGKQLQSLMHRmevvLER 184
Cdd:pfam00270 77 ASLLGGDSRKEQLEKLKGpdILVGTPGRLLDLLQERKL-----LKNLKLLVLDEAHRLLDMGFGPDLEEILRR----LPK 147
|
170
....*....|...
gi 2755244177 185 RVPRIGLSATLGD 197
Cdd:pfam00270 148 KRQILLLSATLPR 160
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
24-428 |
1.09e-30 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 126.93 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 24 EALREVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHLLNGdtdGLIVYISPLKALINDQFGRLDRLCEDLDIPV 103
Cdd:COG1204 21 EELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNG---GKALYIVPLRALASEKYREFKRDFEELGIKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 104 wpwhgdIGST----TKQRFFRKPTgVLLITPESLEAMLCNRgtsvAGIFKGAAFVIVDELHaFIGSE-RGKQLQSLMHRM 178
Cdd:COG1204 98 ------GVSTgdydSDDEWLGRYD-ILVATPEKLDSLLRNG----PSWLRDVDLVVVDEAH-LIDDEsRGPTLEVLLARL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 179 eVVLERRVPRIGLSATLGDMQAAA-----TFLRSDGRAaivdaqsgnNELQlilKGFEEPPA---PQDAKHEEVAPLAVA 250
Cdd:COG1204 166 -RRLNPEAQIVALSATIGNAEEIAewldaELVKSDWRP---------VPLN---EGVLYDGVlrfDDGSRRSKDPTLALA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 251 KHLheVLCGTNNLIFPNSRREVERY----------------THLLNEISEQASRPRE-----------------FwpHHG 297
Cdd:COG1204 233 LDL--LEEGGQVLVFVSSRRDAESLakkladelkrrltpeeREELEELAEELLEVSEethtnekladclekgvaF--HHA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 298 NLSKEIRSDTEAALKQKERPATaICTNTLELGIDIGA----VKSVAQIG-TPPSVASLRQRMGRSGRR----KGEpailr 368
Cdd:COG1204 309 GLPSELRRLVEDAFREGLIKVL-VATPTLAAGVNLPArrviIRDTKRGGmVPIPVLEFKQMAGRAGRPgydpYGE----- 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 369 GYVIEDAIDSNSDLKTRLRLDTVQSIASALllidkwfeppvAGGAHLSTlvqQLLSAIAQ 428
Cdd:COG1204 383 AILVAKSSDEADELFERYILGEPEPIRSKL-----------ANESALRT---HLLALIAS 428
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
23-197 |
1.64e-28 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 113.36 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 23 WEALREVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHLLNGDtDGLIVYISPLKALINDQFGRLDRLCEDLDIP 102
Cdd:smart00487 6 FEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELAEQWAEELKKLGPSLGLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 103 VWP-WHGDIGSTTKQRFFRKPTGVLLITPESLEAMLCNRGTSVAGIfkgaAFVIVDELHAFIGSERGKQLQSLMHRmevv 181
Cdd:smart00487 85 VVGlYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNV----DLVILDEAHRLLDGGFGDQLEKLLKL---- 156
|
170
....*....|....*.
gi 2755244177 182 LERRVPRIGLSATLGD 197
Cdd:smart00487 157 LPKNVQLLLLSATPPE 172
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
18-202 |
4.58e-26 |
|
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: 105.74 E-value: 4.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 18 LWAEQWEALREVQemaipavllADRDVVIAASTASGKTEAAFLPALTHLLNgDTDGLIVYISPLKALINDQFGRLDRLCE 97
Cdd:cd17923 1 LYSHQAEAIEAAR---------AGRSVVVTTGTASGKSLCYQLPILEALLR-DPGSRALYLYPTKALAQDQLRSLRELLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 98 DL--DIPVWPWHGDIGSTTKQRFFRKPTGVLLITPESLEAMLCNRGTSVAGIFKGAAFVIVDELHAFIGSErGKQLQSLM 175
Cdd:cd17923 71 QLglGIRVATYDGDTPREERRAIIRNPPRILLTNPDMLHYALLPHHDRWARFLRNLRYVVLDEAHTYRGVF-GSHVALLL 149
|
170 180 190
....*....|....*....|....*....|
gi 2755244177 176 HRMEVVLERRVPR---IGLSATLGDMQAAA 202
Cdd:cd17923 150 RRLRRLCRRYGADpqfILTSATIGNPAEHA 179
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
30-209 |
4.61e-21 |
|
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: 91.17 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 30 QEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHLLNGdtDGLIVYISPLKALINDQFGRLDRLCEDLDIPVWPWHGD 109
Cdd:cd17921 6 QREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS--GGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLTGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 110 IgSTTKQRFFRKPtgVLLITPESLEAMLCNRGTsvaGIFKGAAFVIVDELHAFIGSERGKQLQSLMHRMeVVLERRVPRI 189
Cdd:cd17921 84 P-SVNKLLLAEAD--ILVATPEKLDLLLRNGGE---RLIQDVRLVVVDEAHLIGDGERGVVLELLLSRL-LRINKNARFV 156
|
170 180
....*....|....*....|
gi 2755244177 190 GLSATLGDMQAAATFLRSDG 209
Cdd:cd17921 157 GLSATLPNAEDLAEWLGVED 176
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
232-363 |
2.20e-19 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 85.39 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 232 EPPAPQDAKHEEVAPLAVAKHL--HEVLCGTNNLIFPNSRREVERYT-HLLNEISEQASRPREFWPHHGNLSKEIRSDTE 308
Cdd:cd18797 6 NPPLLDRKDGERGSARREAARLfaDLVRAGVKTIVFCRSRKLAELLLrYLKARLVEEGPLASKVASYRAGYLAEDRREIE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2755244177 309 AALKQKERPATaICTNTLELGIDIGAVKSVAQIGTPPSVASLRQRMGRSGRRKGE 363
Cdd:cd18797 86 AELFNGELLGV-VATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKD 139
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
26-205 |
4.30e-18 |
|
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: 82.38 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 26 LREVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHLLNGdtdGLIVYISPLKALINDQFGRLDRLcEDLDIPVWP 105
Cdd:cd18028 2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEG---GKALYLVPLRALASEKYEEFKKL-EEIGLKVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 106 WHGDIGSTTKqrfFRKPTGVLLITPESLEAMLCNRgtsvAGIFKGAAFVIVDELHaFIGS-ERGKQLQSLMHRME-VVLE 183
Cdd:cd18028 78 STGDYDEDDE---WLGDYDIIVATYEKFDSLLRHS----PSWLRDVGVVVVDEIH-LISDeERGPTLESIVARLRrLNPN 149
|
170 180
....*....|....*....|..
gi 2755244177 184 RRVprIGLSATLGDMQAAATFL 205
Cdd:cd18028 150 TQI--IGLSATIGNPDELAEWL 169
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
19-208 |
1.90e-17 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350777 [Multi-domain] Cd Length: 214 Bit Score: 81.65 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 19 WA----EQWEALREVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHL-LNGDTDGL-------IVYISPLKALIN 86
Cdd:cd18019 7 WAqpafEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIgKHRNPDGTinldafkIVYIAPMKALVQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 87 DQFGRLDRLCEDLDIPVWPWHGDiGSTTKQRFFRkpTGVLLITPESLEAMLCNRG-TSVAGIFKgaaFVIVDELHaFIGS 165
Cdd:cd18019 87 EMVGNFSKRLAPYGITVAELTGD-QQLTKEQISE--TQIIVTTPEKWDIITRKSGdRTYTQLVR---LIIIDEIH-LLHD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2755244177 166 ERGKQLQSLMHR----MEVVLErRVPRIGLSATLGDMQAAATFLRSD 208
Cdd:cd18019 160 DRGPVLESIVARtirqIEQTQE-YVRLVGLSATLPNYEDVATFLRVD 205
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
28-206 |
5.11e-16 |
|
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: 77.40 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 28 EVQEMAIPAVLLADRDVVIAASTASGKT---EAAFLPALTHLLNGDTDGL-IVYISPLKALINDQ-------FGRLDRLC 96
Cdd:cd18023 4 RIQSEVFPDLLYSDKNFVVSAPTGSGKTvlfELAILRLLKERNPLPWGNRkVVYIAPIKALCSEKyddwkekFGPLGLSC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 97 EDLdipvwpwhgdIGSTTKQRFFR-KPTGVLLITPESLEAMlCNRGTSVAGIFKGAAFVIVDELHaFIGSERGKQLQSLM 175
Cdd:cd18023 84 AEL----------TGDTEMDDTFEiQDADIILTTPEKWDSM-TRRWRDNGNLVQLVALVLIDEVH-IIKENRGATLEVVV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2755244177 176 HRMEVVLE---------RRVPRIGLSATLGDMQAAATFLR 206
Cdd:cd18023 152 SRMKTLSSsselrgstvRPMRFVAVSATIPNIEDLAEWLG 191
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
43-379 |
1.01e-13 |
|
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: 73.23 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 43 DVVIAASTASGKTEAAFLPALTHLLNGDTDGLIvYISPLKALINDQFGRL----------------DRLCEDLDIPVWPW 106
Cdd:cd09639 1 LLVIEAPTGYGKTEAALLWALHSLKSQKADRVI-IALPTRATINAMYRRAkeafgetglyhssilsSRIKEMGDSEEFEH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 107 HGDIGSTTKQRFFRKPtgvllITPESLEAMLCNRGTSVAGIFK-----GAAFVIVDELHAFIGSERGKQLQSLMHRMEVv 181
Cdd:cd09639 80 LFPLYIHSNDTLFLDP-----ITVCTIDQVLKSVFGEFGHYEFtlasiANSLLIFDEVHFYDEYTLALILAVLEVLKDN- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 182 lerRVPRIGLSATLGDmqaaatFLRSDGRAAIVDAqsgNNELqLILKGFEEPPAPQDAKHEEVAPLAVAKHLHEVLCGTN 261
Cdd:cd09639 154 ---DVPILLMSATLPK------FLKEYAEKIGYVE---ENEP-LDLKPNERAPFIKIESDKVGEISSLERLLEFIKKGGS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 262 NLIFPNS-RREVERYTHLLNEISEQasrprEFWPHHGNLSKEIRSDTEAALK---QKERPATAICTNTLELGIDIGAVKS 337
Cdd:cd09639 221 VAIIVNTvDRAQEFYQQLKEKGPEE-----EIMLIHSRFTEKDRAKKEAELLlefKKSEKFVIVATQVIEASLDISVDVM 295
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2755244177 338 VAQIgTPPSvaSLRQRMGRSgRRKGEPAILRGYVIEDAIDSN 379
Cdd:cd09639 296 ITEL-APID--SLIQRLGRL-HRYGEKNGEEVYIITDAPDGK 333
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
43-194 |
1.45e-13 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 68.58 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 43 DVVIAASTASGKTEAAFLPALTHLLngDTDGLIVYISPLKALINDQFGRLDRLcEDLDIPVWPWHGDIGSTTKQRFFRKP 122
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLL--KKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSSAEEREKNKLGD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2755244177 123 TGVLLITPESLeAMLCNRgtSVAGIFKGAAFVIVDELHAFIGSERGKQLQSLMHRmeVVLERRVPRIGLSAT 194
Cdd:cd00046 80 ADIIIATPDML-LNLLLR--EDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVR--KAGLKNAQVILLSAT 146
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
23-195 |
2.49e-13 |
|
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: 69.49 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 23 WEALREVQEMAIPAVLlADRDVVIAASTASGKTEAAFLPALthLLNGDTdglIVyISPLKALINDQFGRLDRlcedLDIP 102
Cdd:cd17920 10 YDEFRPGQLEAINAVL-AGRDVLVVMPTGGGKSLCYQLPAL--LLDGVT---LV-VSPLISLMQDQVDRLQQ----LGIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 103 VWPWHGDIGSTTKQRFFRK-PTG---VLLITPESLEAMLCNRGTSVAGIFKGAAFVIVDELHafIGSERGKQLQSLMHRM 178
Cdd:cd17920 79 AAALNSTLSPEEKREVLLRiKNGqykLLYVTPERLLSPDFLELLQRLPERKRLALIVVDEAH--CVSQWGHDFRPDYLRL 156
|
170
....*....|....*....
gi 2755244177 179 EVVLER--RVPRIGLSATL 195
Cdd:cd17920 157 GRLRRAlpGVPILALTATA 175
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
30-398 |
5.02e-13 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 72.61 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 30 QEMAIPAvLLADRDVVIAASTASGKTEAAFLPALTHLLNGDTDgliVYISPLKALINDQFGRLDRLcEDLDIPVWPWHGD 109
Cdd:PRK01172 27 QRMAIEQ-LRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKS---IYIVPLRSLAMEKYEELSRL-RSLGMRVKISIGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 110 IGSTTKqrfFRKPTGVLLITPESLEAMLCNRgtsvAGIFKGAAFVIVDELHaFIGSE-RGKQLQSLMHRMEVV-LERRVp 187
Cdd:PRK01172 102 YDDPPD---FIKRYDVVILTSEKADSLIHHD----PYIINDVGLIVADEIH-IIGDEdRGPTLETVLSSARYVnPDARI- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 188 rIGLSATLGDMQAAATFL-----RSDGRAAIV--------------DAQSGNNELQLILKGFEEPPAPQDAKHEEVAPLA 248
Cdd:PRK01172 173 -LALSATVSNANELAQWLnasliKSNFRPVPLklgilyrkrlildgYERSQVDINSLIKETVNDGGQVLVFVSSRKNAED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 249 VAKHLHEVLCGTNNliFPNSRREVERYTHLLNEISeqasrPREFWPHHGNLSKEIRSDTEAALKQKeRPATAICTNTLEL 328
Cdd:PRK01172 252 YAEMLIQHFPEFND--FKVSSENNNVYDDSLNEML-----PHGVAFHHAGLSNEQRRFIEEMFRNR-YIKVIVATPTLAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 329 GIDIGA----VKSVAQIG----TPPSVASLRQRMGRSGRRK-----------GEPA---ILRGYVIED--AIDSNSDLKT 384
Cdd:PRK01172 324 GVNLPArlviVRDITRYGnggiRYLSNMEIKQMIGRAGRPGydqygigyiyaASPAsydAAKKYLSGEpePVISYMGSQR 403
|
410
....*....|....
gi 2755244177 385 RLRLDTVQSIASAL 398
Cdd:PRK01172 404 KVRFNTLAAISMGL 417
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
26-206 |
1.78e-12 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350778 [Multi-domain] Cd Length: 199 Bit Score: 66.68 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 26 LREVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHLLNGDTDGL--------IVYISPLKAL---INDQFGRldR 94
Cdd:cd18020 2 LNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQGGvikkddfkIVYIAPMKALaaeMVEKFSK--R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 95 LcEDLDIPVWPWHGDIGSTTKQrffRKPTGVLLITPESLEaMLCNRGTSVAGIFKGAAFVIVDELHaFIGSERGKQLQSL 174
Cdd:cd18020 80 L-APLGIKVKELTGDMQLTKKE---IAETQIIVTTPEKWD-VVTRKSSGDVALSQLVRLLIIDEVH-LLHDDRGPVIESL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 2755244177 175 MHRMEVVLERRVPRI---GLSATLGDMQAAATFLR 206
Cdd:cd18020 154 VARTLRQVESTQSMIrivGLSATLPNYLDVADFLR 188
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
40-211 |
3.93e-12 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 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: 350783 [Multi-domain] Cd Length: 192 Bit Score: 65.47 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 40 ADRDVVIAASTASGKTEAAFLpALTHLLNGDTDGLIVYISPLKALIN----DQFGRLDRLCEDLDIPVWpwhgdiGSTTK 115
Cdd:cd18025 15 RRESALIVAPTSSGKTFISYY-CMEKVLRESDDGVVVYVAPTKALVNqvvaEVYARFSKKYPPSGKSLW------GVFTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 116 QRFFRKPTG--VLLITPESLEAMLCNRGTsvAGIFKGAAFVIVDELHAFIGSERGKQLQSLMhrmevvLERRVPRIGLSA 193
Cdd:cd18025 88 DYRHNNPMNcqVLITVPECLEILLLSPHN--ASWVPRIKYVIFDEIHSIGQSEDGAVWEQLL------LLIPCPFLALSA 159
|
170
....*....|....*...
gi 2755244177 194 TLGDMQAAATFLRSDGRA 211
Cdd:cd18025 160 TIGNPQKFHEWLQSVQRA 177
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
247-361 |
4.47e-12 |
|
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: 63.00 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 247 LAVAKHLHEVLCGTNNLIFPNSRREVErYTHLLNEISEQASRprefwpHHGNLSKEIRSDTEAALKQKERPaTAICTNTL 326
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVAR------LHGDLSQEEREEILEDFRKGKID-VLVATDVA 74
|
90 100 110
....*....|....*....|....*....|....*
gi 2755244177 327 ELGIDIGAVKSVAQIGTPPSVASLRQRMGRSGRRK 361
Cdd:pfam00271 75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
273-361 |
6.27e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 61.84 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 273 ERYTHLLNEiseqasRPREFWPHHGNLSKEIRSDTEAALKQKERPaTAICTNTLELGIDIGAVKSVAQIGTPPSVASLRQ 352
Cdd:smart00490 1 EELAELLKE------LGIKVARLHGGLSQEEREEILDKFNNGKIK-VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQ 73
|
....*....
gi 2755244177 353 RMGRSGRRK 361
Cdd:smart00490 74 RIGRAGRAG 82
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
41-205 |
5.62e-11 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350780 [Multi-domain] Cd Length: 189 Bit Score: 62.39 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 41 DRDVVIAASTASGKTEAAFLpALTHLLNGDTDGLIVYISPLKALINDqfgRLD----RLCEDLDIPVWPWHGDigSTTKQ 116
Cdd:cd18022 17 DNNVLLGAPTGSGKTIAAEL-AMFRAFNKYPGSKVVYIAPLKALVRE---RVDdwkkRFEEKLGKKVVELTGD--VTPDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 117 RFFRKPTgVLLITPESLEAMlcNRGTSVAGIFKGAAFVIVDELHaFIGSERGKQLQSLMHRMEVV---LERRVPRIGLSA 193
Cdd:cd18022 91 KALADAD-IIITTPEKWDGI--SRSWQTREYVQQVSLIIIDEIH-LLGSDRGPVLEVIVSRMNYIssqTEKPVRLVGLST 166
|
170
....*....|..
gi 2755244177 194 TLGDMQAAATFL 205
Cdd:cd18022 167 ALANAGDLANWL 178
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
9-359 |
5.71e-11 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 66.13 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 9 SLHPGIQRYLWAEQWEALREVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHLLNGdtdGLIVYISPLKALINDQ 88
Cdd:PRK02362 7 PLPEGVIEFYEAEGIEELYPPQAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIARG---GKALYIVPLRALASEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 89 FGRLDRLcEDLDIPVWPWHGDIGSTTKqrfFRKPTGVLLITPESLEAMLCNRgtsvAGIFKGAAFVIVDELHaFIGSE-R 167
Cdd:PRK02362 84 FEEFERF-EELGVRVGISTGDYDSRDE---WLGDNDIIVATSEKVDSLLRNG----APWLDDITCVVVDEVH-LIDSAnR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 168 GKQLqslmhrmEVV---LERRVPR---IGLSATLGDMQAAATFLrsdgRAAIVDAQSGNNELQ--------LILKGfEEP 233
Cdd:PRK02362 155 GPTL-------EVTlakLRRLNPDlqvVALSATIGNADELADWL----DAELVDSEWRPIDLRegvfyggaIHFDD-SQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 234 PAPQDAKHEEVAplAVAKHLHEvlcGTNNLIFPNSRREVERY---------THLLNEISEQ----ASRPRE--------- 291
Cdd:PRK02362 223 EVEVPSKDDTLN--LVLDTLEE---GGQCLVFVSSRRNAEGFakraasalkKTLTAAERAElaelAEEIREvsdtetskd 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 292 ----------FwpHHGNLSKEIRSDTEAALKQKERPATAiCTNTLELGIDIGAVKSV--------AQIGTPP-SVASLRQ 352
Cdd:PRK02362 298 ladcvakgaaF--HHAGLSREHRELVEDAFRDRLIKVIS-STPTLAAGLNLPARRVIirdyrrydGGAGMQPiPVLEYHQ 374
|
....*..
gi 2755244177 353 RMGRSGR 359
Cdd:PRK02362 375 MAGRAGR 381
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
14-367 |
1.03e-10 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 65.22 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 14 IQRYLWAEQWEALREVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHLLNgdTDGLIVYISPLKALINDQFgRLD 93
Cdd:PRK00254 12 IKRVLKERGIEELYPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR--EGGKAVYLVPLKALAEEKY-REF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 94 RLCEDLDIPVWPWHGDIGSTTKqrfFRKPTGVLLITPESLEAMLcNRGTSvagIFKGAAFVIVDELHaFIGS-ERGKQLQ 172
Cdd:PRK00254 89 KDWEKLGLRVAMTTGDYDSTDE---WLGKYDIIIATAEKFDSLL-RHGSS---WIKDVKLVVADEIH-LIGSyDRGATLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 173 SLMHRMevvlERRVPRIGLSATLGDMQAAATFL-----RSDGRAaiVDAQSGnnelqLILKGF---EEPPAPQ-DAKHEE 243
Cdd:PRK00254 161 MILTHM----LGRAQILGLSATVGNAEELAEWLnaelvVSDWRP--VKLRKG-----VFYQGFlfwEDGKIERfPNSWES 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 244 VAPLAVAKhlhevlcGTNNLIFPNSRREVERYTHLLN-EISEQASRPR-----------EFWP---------------HH 296
Cdd:PRK00254 230 LVYDAVKK-------GKGALVFVNTRRSAEKEALELAkKIKRFLTKPElralkeladslEENPtneklkkalrggvafHH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 297 GNLSKEIRSDTEAALKqKERPATAICTNTLELGIDIGA-------VKSVAQIG-TPPSVASLRQRMGRSGRRK----GEP 364
Cdd:PRK00254 303 AGLGRTERVLIEDAFR-EGLIKVITATPTLSAGINLPAfrviirdTKRYSNFGwEDIPVLEIQQMMGRAGRPKydevGEA 381
|
...
gi 2755244177 365 AIL 367
Cdd:PRK00254 382 IIV 384
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
8-394 |
1.92e-09 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 60.87 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 8 HSLHPGIQRYL-----WAEQWEALR-EVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHLLNGDTDGLIvYISPL 81
Cdd:COG1203 108 HLLAERLERLLpkkskPRTPINPLQnEALELALEAAEEEPGLFILTAPTGGGKTEAALLFALRLAAKHGGRRII-YALPF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 82 KALINDQFGRLDRLCED--------LDIPVWPWHGDIGSTTKQ-----RFFRKPTGVLliTPESL-EAMLCNRGTSVAGI 147
Cdd:COG1203 187 TSIINQTYDRLRDLFGEdvllhhslADLDLLEEEEEYESEARWlkllkELWDAPVVVT--TIDQLfESLFSNRKGQERRL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 148 FKGA-AFVIVDELHAFiGSERGKQLQSLMHRME-----VVLerrvprigLSATLgdmqaaATFLRSDGRAAIvdaqsgnn 221
Cdd:COG1203 265 HNLAnSVIILDEVQAY-PPYMLALLLRLLEWLKnlggsVIL--------MTATL------PPLLREELLEAY-------- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 222 elQLILKGFEEPPAPQDA--------KHEEVAPLAVAKHLHEVLCGTNN-LIFPNSRREVERYTHLLNEISEQasrpREF 292
Cdd:COG1203 322 --ELIPDEPEELPEYFRAfvrkrvelKEGPLSDEELAELILEALHKGKSvLVIVNTVKDAQELYEALKEKLPD----EEV 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 293 WPHHGNLSKEIRSDTEAALKQ---KERPATAICTNTLELGIDIGAVKSVAQIGTPPSVAslrQRMG---RSGRRKGEPAI 366
Cdd:COG1203 396 YLLHSRFCPADRSEIEKEIKErleRGKPCILVSTQVVEAGVDIDFDVVIRDLAPLDSLI---QRAGrcnRHGRKEEEGNV 472
|
410 420
....*....|....*....|....*...
gi 2755244177 367 lrgYVIEDAIDSNSDLKTRLRLDTVQSI 394
Cdd:COG1203 473 ---YVFDPEDEGGGYVYDKPLLERTREL 497
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
38-208 |
2.62e-09 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 57.61 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 38 LLADRDVVIAASTASGKTEAAFLPALTHLLNGDTDGLIVYisPLKALINDQFGRLDRLCEDLDIPVWPWHGDIGSTTKQR 117
Cdd:cd18026 30 LLEGRNLVYSLPTSGGKTLVAEILMLKRLLERRKKALFVL--PYVSIVQEKVDALSPLFEELGFRVEGYAGNKGRSPPKR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 118 ffRKPTGVLLITPESLeAMLCNRGTSvAGIFKGAAFVIVDELHAFIGSERGKQLQSLMHRMEVVLERRVPRIGLSATLGD 197
Cdd:cd18026 108 --RKSLSVAVCTIEKA-NSLVNSLIE-EGRLDELGLVVVDELHMLGDGHRGALLELLLTKLLYAAQKNIQIVGMSATLPN 183
|
170
....*....|.
gi 2755244177 198 MQAAATFLRSD 208
Cdd:cd18026 184 LEELASWLRAE 194
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
41-195 |
9.07e-09 |
|
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: 55.76 E-value: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 41 DRDVVIAASTASGKTEAAFLPALTHLLNGDTDGLIvYISPLKALINDQFGRLDRLCEDLDIPV----------------- 103
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWALKLAARGGKRRII-YALPTRATINQMYERIREILGRLDDEDkvlllhskaalellesd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 104 WPWHGDIGSTTKQRFFRK-----PTGVLliTPES-LEAMLCNRGtsvaGIFKGAAF----VIVDELHAFigseRGKQLQS 173
Cdd:cd17930 80 EEPDDDPVEAVDWALLLKrswlaPIVVT--TIDQlLESLLKYKH----FERRLHGLansvVVLDEVQAY----DPEYMAL 149
|
170 180
....*....|....*....|...
gi 2755244177 174 LMHRMEVVLER-RVPRIGLSATL 195
Cdd:cd17930 150 LLKALLELLGElGGPVVLMTATL 172
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
10-158 |
1.33e-08 |
|
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: 55.67 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 10 LHPGIQRYLWAEQWEALREVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHLLNGDTDG-----LIVYISPLKAL 84
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGrrsgvSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 85 ---INDQFGRLDRLCEDLDIpvwpwHGDIGSTTK----QRFFRKPTGVLLITPESLEAMLcnRGTSVAGIFKGAAFVIVD 157
Cdd:cd17964 81 alqIAAEAKKLLQGLRKLRV-----QSAVGGTSRraelNRLRRGRPDILVATPGRLIDHL--ENPGVAKAFTDLDYLVLD 153
|
.
gi 2755244177 158 E 158
Cdd:cd17964 154 E 154
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
14-158 |
7.41e-08 |
|
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: 53.21 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 14 IQRYLWAEQWEALREVQEMAIPAvLLADRDVVIAASTASGKTeAAF-LPALTHLLNGDTDG------LIvyISPLKAL-- 84
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPL-ILSGRDVIGQAQTGSGKT-LAFlLPILEKLLPEPKKKgrgpqaLV--LAPTRELam 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2755244177 85 -INDQFgrlDRLCEDLDIPVWPWHGDIGSTTKQRFFRKPTGVLLITPESLEAMLCNRGTSVAGIfkgaAFVIVDE 158
Cdd:cd00268 77 qIAEVA---RKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNV----KYLVLDE 144
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
24-160 |
8.16e-08 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 53.03 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 24 EALREVQEMAIpAVLLADRDVVIAASTASGKTEAAFLPALthLLNGDTDGLIVYISPLKALINDQFGRLDRLcedldIPV 103
Cdd:cd18018 11 PSFRPGQEEAI-ARLLSGRSTLVVLPTGAGKSLCYQLPAL--LLRRRGPGLTLVVSPLIALMKDQVDALPRA-----IKA 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2755244177 104 WPWHGDIGSTTKQRFFRK----PTGVLLITPESLeamlcnRGTSVAGIFKGA---AFVIVDELH 160
Cdd:cd18018 83 AALNSSLTREERRRILEKlragEVKILYVSPERL------VNESFRELLRQTppiSLLVVDEAH 140
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
23-195 |
1.17e-07 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 52.65 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 23 WEALREVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHLLNGDtDGLIVYISPLKALIndqfgrlDRLCEDldip 102
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNP-KGRAVYIAPMQELV-------DARYKD---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 103 vwpWHGDIGSTTKQRFFRKpTG-------------VLLITPESLEaMLCNRGTSVAGIfKGAAFVIVDELHaFIGSERGK 169
Cdd:cd18021 69 ---WRAKFGPLLGKKVVKL-TGetstdlkllaksdVILATPEQWD-VLSRRWKQRKNV-QSVELFIADELH-LIGGENGP 141
|
170 180
....*....|....*....|....*....
gi 2755244177 170 QLQ---SLMHRMEVVLERRVPRIGLSATL 195
Cdd:cd18021 142 VYEvvvSRMRYISSQLEKPIRIVGLSSSL 170
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
27-194 |
1.93e-07 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 52.14 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 27 REVQEMAIPAVLLADrDVVIAASTASGKTEAAFLPALThllngdTDGLIVYISPLKALINDQFGRLdrlcEDLDIPVWPW 106
Cdd:cd18016 19 RTNQLEAINAALLGE-DCFVLMPTGGGKSLCYQLPACV------SPGVTVVISPLRSLIVDQVQKL----TSLDIPATYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 107 HGDIGSTTKQRFFRK-----PTGVLL-ITPESLEAmlCNRGTSVAGIFKG----AAFVIvDELHAFigSERGKQLQSLMH 176
Cdd:cd18016 88 TGDKTDAEATKIYLQlskkdPIIKLLyVTPEKISA--SNRLISTLENLYErkllARFVI-DEAHCV--SQWGHDFRPDYK 162
|
170 180
....*....|....*....|
gi 2755244177 177 RMEVVLER--RVPRIGLSAT 194
Cdd:cd18016 163 RLNMLRQKfpSVPMMALTAT 182
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
44-358 |
2.65e-07 |
|
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D
Pssm-ID: 187841 [Multi-domain] Cd Length: 353 Bit Score: 53.34 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 44 VVIAASTASGKTEAAFLPALThllNGDTdglIVYISPLKALINDQFGRLDRLCEDLD------------IPVWPWH---- 107
Cdd:cd09710 17 IFNTAPTGAGKTLAWLTPLLH---GENK---AIALYPTNALIEDQTEAIKEFVDDANprhqvkslsasdITLWPNDknvg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 108 ---GDIGSTTKQRFFRKPTGVLLIT-PE----SLEAMLCNRGTSVAGIFKGAAFVIVDELHAFigseRGKQLQSLMHRME 179
Cdd:cd09710 91 sskGEKLYNLLRNDIGTSTPIILLTnPDifvyLTRFAYIDRGDIAAGFYTKFSTVIFDEFHLY----DAKQLVGLLFYLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 180 VVL-----ERRVPRIGLSAT--------LGDM-QAAATFLRSDGRAaivDAQSGNNELQLILK-----------GFEEPP 234
Cdd:cd09710 167 YMQlirffECRRKFVFLSATpdpalilrLQNAkQAGVKIAPIDGEA---GQFPDNPELEQQLKntsfrpvlppvELELIP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 235 APqDAKHEEVAPLA--VAKHLHEvLCGTNNLIFPNSRREVERYTHLLNEiseqasrprefwPHHGNLSKEIRSDTEAALK 312
Cdd:cd09710 244 AP-DFKEEWLAELAaeVIERFRQ-LPGERGAIILDSLDEVNRLSDLLQQ------------QGLGDDIGRITGFAPKKDR 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2755244177 313 QKERPA-TAICTNTLELGIDIgavKSVAQIGTPPSVASLRQRMGRSG 358
Cdd:cd09710 310 ERAMQFdILLGTSTVDVGVDF---KRDWLIFSARDAAAFWQRLGRLG 353
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
38-195 |
3.73e-07 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L 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: 350785 [Multi-domain] Cd Length: 179 Bit Score: 50.73 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 38 LLADRDVVIAASTASGKT---EAAFLPALTHLLNgdtdglIVYISPLKALINDQFgrldrlcEDLDIPVwpwhGDIGSTT 114
Cdd:cd18027 20 LEAGDSVFVAAHTSAGKTvvaEYAIALAQKHMTR------TIYTSPIKALSNQKF-------RDFKNTF----GDVGLIT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 115 KQRFFRKPTGVLLITPESLEAMLCNRgtsvAGIFKGAAFVIVDELHAFIGSERGKQLQSLMhrmeVVLERRVPRIGLSAT 194
Cdd:cd18027 83 GDVQLNPEASCLIMTTEILRSMLYNG----SDVIRDLEWVIFDEVHYINDAERGVVWEEVL----IMLPDHVSIILLSAT 154
|
.
gi 2755244177 195 L 195
Cdd:cd18027 155 V 155
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
10-69 |
4.31e-07 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 52.84 E-value: 4.31e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2755244177 10 LHPGIQRYLWAEQWEALREVQEMAIPAVLlADRDVVIAASTASGKTeAAF-LPALTHLLNG 69
Cdd:COG0513 9 LSPPLLKALAELGYTTPTPIQAQAIPLIL-AGRDVLGQAQTGTGKT-AAFlLPLLQRLDPS 67
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
28-196 |
6.29e-07 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 50.55 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 28 EVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHllngdtDGLIVYISPLKALINDQFGRLDRlcedLDIPVWPWH 107
Cdd:cd18014 16 PLQEKATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLA------KGITIVISPLIALIQDQVDHLKT----LKIRVDSLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 108 GDIGSTTKQRFF------RKPTGVLLITPES--------LEAMLCNRGTsvagifkgAAFVIVDELHAFigSERGKQLQS 173
Cdd:cd18014 86 SKLSAQERKRIIadleseKPQTKFLYITPEMaatssfqpLLSSLVSRNL--------LSYLVVDEAHCV--SQWGHDFRP 155
|
170 180
....*....|....*....|....*
gi 2755244177 174 LMHRMEVVLER--RVPRIGLSATLG 196
Cdd:cd18014 156 DYLRLGALRSRygHVPWVALTATAT 180
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
321-371 |
1.91e-06 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 46.16 E-value: 1.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2755244177 321 ICTNTLELGIDIGAVKSVAQIGTPPSVASLRQRMGRSGRRKGEPAILRGYV 371
Cdd:cd18785 27 VATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
24-102 |
2.94e-06 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 48.90 E-value: 2.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2755244177 24 EALREVQEMAIPAVLlADRDVVIAASTASGKTEAAFLPALThllngdTDGLIVYISPLKALINDQFgrldRLCEDLDIP 102
Cdd:cd18015 17 EKFRPLQLETINATM-AGRDVFLVMPTGGGKSLCYQLPALC------SDGFTLVVSPLISLMEDQL----MALKKLGIS 84
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
29-86 |
3.12e-06 |
|
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: 49.20 E-value: 3.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2755244177 29 VQEMAIPAVLlADRDVVIAASTASGKTEAAFLPALTHLLNGDTDG---------LIVYISPLKALIN 86
Cdd:cd18052 69 VQKYAIPIIL-AGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTAssfsevqepQALIVAPTRELAN 134
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
22-158 |
3.17e-06 |
|
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: 48.91 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 22 QWEALREVQEMAIPAVLlADRDVVIAASTASGKTEAAFLPALTHLLN----GDTDGLIVYI-SPLKALINDQFGRLDRLC 96
Cdd:cd17953 31 GYEKPTPIQAQALPAIM-SGRDVIGIAKTGSGKTLAFLLPMFRHIKDqrpvKPGEGPIGLImAPTRELALQIYVECKKFS 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2755244177 97 EDLDIPVWPWHGdiGSTTKQRF--FRKPTGVLLITPESLEAMLCNRGTSVAGIfKGAAFVIVDE 158
Cdd:cd17953 110 KALGLRVVCVYG--GSGISEQIaeLKRGAEIVVCTPGRMIDILTANNGRVTNL-RRVTYVVLDE 170
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
36-168 |
1.14e-05 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 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: 350782 [Multi-domain] Cd Length: 205 Bit Score: 47.05 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 36 AVLLADRD--VVIAASTASGKTEAAFLPALTHLLNGDTdglIVYISPLKALINDQFGRLDrlcEDLdipvwpwhGDIGST 113
Cdd:cd18024 40 AIACIERNesVLVSAHTSAGKTVVAEYAIAQSLRDKQR---VIYTSPIKALSNQKYRELQ---EEF--------GDVGLM 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2755244177 114 TKQRFFRKPTGVLLITPESLEAMLcNRGTSvagIFKGAAFVIVDELHAFIGSERG 168
Cdd:cd18024 106 TGDVTINPNASCLVMTTEILRSML-YRGSE---IMREVAWVIFDEIHYMRDKERG 156
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
263-367 |
1.47e-05 |
|
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: 45.19 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 263 LIFPNSRREVERYTHLLNEISEQASrprefwPHHGNLSKEIRSDTEAALKQKERPaTAICTNTLELGIDIGAVKSVAQIG 342
Cdd:cd18787 31 IIFVNTKKRVDRLAELLEELGIKVA------ALHGDLSQEERERALKKFRSGKVR-VLVATDVAARGLDIPGVDHVINYD 103
|
90 100
....*....|....*....|....*..
gi 2755244177 343 TPPSVASLRQRMGRSGR--RKGEpAIL 367
Cdd:cd18787 104 LPRDAEDYVHRIGRTGRagRKGT-AIT 129
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
24-71 |
2.42e-05 |
|
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: 46.04 E-value: 2.42e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2755244177 24 EALREVQEMAIPaVLLADRDVVIAASTASGKTEAAFLPALTHLLNGDT 71
Cdd:cd17949 12 EKPTAIQKLAIP-VLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEP 58
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
14-84 |
2.67e-05 |
|
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: 45.74 E-value: 2.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2755244177 14 IQRYLWAEQWEALREVQEMAIPaVLLADRDVVIAASTASGKTEAAFLPALTHLLN---GDTDGL-IVYISPLKAL 84
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIP-HALQGRDILGAAKTGSGKTLAFLVPLLEKLYRerwTPEDGLgALIISPTREL 74
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
23-89 |
4.07e-05 |
|
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: 45.39 E-value: 4.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 23 WEALREVQEMAIPaVLLADRDVVIAASTASGKTEAAFLPALTHLLNGDTDGLIVYISPLKAL---INDQF 89
Cdd:cd17954 20 WKKPTKIQEEAIP-VALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELaqqISEQF 88
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
24-67 |
4.87e-05 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 46.47 E-value: 4.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2755244177 24 EALRE--------VQEMAIPAVLLAdRDVVIAASTASGKTEAAFLPALTHLL 67
Cdd:PRK11192 14 EALQDkgytrptaIQAEAIPPALDG-RDVLGSAPTGTGKTAAFLLPALQHLL 64
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
29-197 |
5.85e-05 |
|
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: 44.87 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 29 VQEMAIPaVLLADRDVVIAASTASGKTEAAFLPALTHLLNGDTD-------GLIvyISPLKALINDQFGRLDRLCEDLDI 101
Cdd:cd17960 16 VQAATIP-LFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANlkkgqvgALI--ISPTRELATQIYEVLQSFLEHHLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 102 PVWP--WHGDIGSTTKQRFFRKPTGVLLI-TPESLEAMLCNRGTSVAgiFKGAAFVIVDELHAFIGSERGKQLQSLMHRM 178
Cdd:cd17960 93 KLKCqlLIGGTNVEEDVKKFKRNGPNILVgTPGRLEELLSRKADKVK--VKSLEVLVLDEADRLLDLGFEADLNRILSKL 170
|
170 180
....*....|....*....|...
gi 2755244177 179 evvlerrvP---RIGL-SATLGD 197
Cdd:cd17960 171 --------PkqrRTGLfSATQTD 185
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
232-372 |
8.32e-05 |
|
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: 43.11 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 232 EPPAPQDAKHEEVaplaVAKHLHEVLCGTNN--LIFPNSRREVERYTHLLNEISEQAsRPREFWphhGNLSKEirsdTEA 309
Cdd:cd18801 5 EKIHPKLEKLEEI----VKEHFKKKQEGSDTrvIIFSEFRDSAEEIVNFLSKIRPGI-RATRFI---GQASGK----SSK 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2755244177 310 ALKQKERPA-----------TAICTNTLELGIDIGAVKSVAQIGTPPSVASLRQRMGRSGRRKGepailrGYVI 372
Cdd:cd18801 73 GMSQKEQKEvieqfrkggynVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQ------GRVV 140
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
23-158 |
9.89e-05 |
|
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: 43.89 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 23 WEALREVQEMAIPAvLLADRDVVIAASTASGKTEAAFLPALTHLL-------NGdTDGLIvyISPLKALINDQFGRLDRL 95
Cdd:cd17942 10 FTKMTEIQAKSIPP-LLEGRDVLGAAKTGSGKTLAFLIPAIELLYklkfkprNG-TGVII--ISPTRELALQIYGVAKEL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2755244177 96 CEDLDIPvwpwHGDI--GSTTKQRFFRKPTGVLLI--TPESLEAMLCNrgtSVAGIFKGAAFVIVDE 158
Cdd:cd17942 86 LKYHSQT----FGIVigGANRKAEAEKLGKGVNILvaTPGRLLDHLQN---TKGFLYKNLQCLIIDE 145
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
26-196 |
1.40e-04 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 43.62 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 26 LREVQ-EMAIPAvlLADRDVVIAASTASGKTEAAFLPALTHL----LNGDTdGLIVYISPLKALINDQFGRLDRLCEDLd 100
Cdd:cd18036 3 LRNYQlELVLPA--LRGKNTIICAPTGSGKTRVAVYICRHHLekrrSAGEK-GRVVVLVNKVPLVEQQLEKFFKYFRKG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 101 IPVWPWHGDIGSTTKQRFFRKPTGVLLITPESLEAMLCNRGTSVAGIFKGAAFVIVDELHAFIGSERGKQLQSLMHRMEV 180
Cdd:cd18036 79 YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEERVYLSDFSLLIFDECHHTQKEHPYNKIMRMYLDKKL 158
|
170
....*....|....*..
gi 2755244177 181 VLERRVPRI-GLSATLG 196
Cdd:cd18036 159 SSQGPLPQIlGLTASPG 175
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
20-158 |
2.74e-04 |
|
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: 42.79 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 20 AEQWEALREVQEMAIPaVLLADRDVVIAASTASGKTEAAFLPALTHL-----LNGDTDGLIVYISPLKALINDQFGRLDR 94
Cdd:cd17952 7 KQEYEQPTPIQAQALP-VALSGRDMIGIAKTGSGKTAAFIWPMLVHImdqreLEKGEGPIAVIVAPTRELAQQIYLEAKK 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2755244177 95 LCEDLDIPVWPWHGDIGSTTKQRFFRKPTGVLLITPESLEAMLCNRGTSvagiFKGAAFVIVDE 158
Cdd:cd17952 86 FGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATN----LQRVTYLVLDE 145
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
29-68 |
2.88e-04 |
|
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: 42.86 E-value: 2.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2755244177 29 VQEMAIPAVLlADRDVVIAASTASGKTeAAFL-PALTHLLN 68
Cdd:cd17967 26 VQKYAIPIIL-AGRDLMACAQTGSGKT-AAFLlPIISKLLE 64
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
28-158 |
3.03e-04 |
|
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: 42.58 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 28 EVQEMAIPaVLLADRDVVIAASTASGKTeAAFL-PALTHLLNGDTDGLI--VYISPLKALINDQFGRLDRLCEDLDIPVW 104
Cdd:cd17957 15 PIQMQAIP-ILLHGRDLLACAPTGSGKT-LAFLiPILQKLGKPRKKKGLraLILAPTRELASQIYRELLKLSKGTGLRIV 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2755244177 105 PWHGdiGSTTKQRFFRKPT---GVLLITPESLEAMLCNRGTSVAGIfkgaAFVIVDE 158
Cdd:cd17957 93 LLSK--SLEAKAKDGPKSItkyDILVSTPLRLVFLLKQGPIDLSSV----EYLVLDE 143
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
16-362 |
3.41e-04 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 43.66 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 16 RYLWAEQWEALREVQEMAIPAvLLADRDVVIAASTASGKTeAAFLPALTHLLNGDTDGLIVYI-SPLKALINDQFGRLDR 94
Cdd:PTZ00424 41 RGIYSYGFEKPSAIQQRGIKP-ILDGYDTIGQAQSGTGKT-ATFVIAALQLIDYDLNACQALIlAPTRELAQQIQKVVLA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 95 LCEDLDIPVwpwHGDIGSTTKQRFFRK-PTGVLLI--TPESLEAMLCNRgtsvagifkgaaFVIVDELHAFIGSERGKQL 171
Cdd:PTZ00424 119 LGDYLKVRC---HACVGGTVVRDDINKlKAGVHMVvgTPGRVYDMIDKR------------HLRVDDLKLFILDEADEML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 172 -QSLMHRMEVVLERRVPRIGL---SATLGD--MQAAATFLRSDGRAAIvdaqsgnNELQLILKGFEEPPAPQDAKHEEVA 245
Cdd:PTZ00424 184 sRGFKGQIYDVFKKLPPDVQValfSATMPNeiLELTTKFMRDPKRILV-------KKDELTLEGIRQFYVAVEKEEWKFD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 246 PLavaKHLHEVLCGTNNLIFPNSRREVERYTHLLNEISEQASrprefwPHHGNLSKEirsDTEAALKQKERPATA--ICT 323
Cdd:PTZ00424 257 TL---CDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVS------CMHGDMDQK---DRDLIMREFRSGSTRvlITT 324
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2755244177 324 NTLELGIDIGAVKSVAQIGTPPSVASLRQRMGRSGR--RKG 362
Cdd:PTZ00424 325 DLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRfgRKG 365
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
28-85 |
3.61e-04 |
|
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: 42.61 E-value: 3.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2755244177 28 EVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHLL-NGDTDGLIVYISPLKALI 85
Cdd:cd17946 15 PIQALALPAAIRDGKDVIGAAETGSGKTLAFGIPILERLLsQKSSNGVGGKQKPLRALI 73
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
29-68 |
6.40e-04 |
|
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: 41.47 E-value: 6.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2755244177 29 VQEMAIPAVLLAdRDVVIAASTASGKTEAAFLPALTHLLN 68
Cdd:cd17947 16 IQAAAIPLALLG-KDICASAVTGSGKTAAFLLPILERLLY 54
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
12-63 |
8.89e-04 |
|
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: 41.15 E-value: 8.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2755244177 12 PGIQRYLWAEQWEALREVQEMAIPAVLlADRDVVIAASTASGKTEAAFLPAL 63
Cdd:cd17938 8 PELIKAVEELDWLLPTDIQAEAIPLIL-GGGDVLMAAETGSGKTGAFCLPVL 58
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
10-89 |
1.01e-03 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 42.57 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 10 LHPGIQRYLwAEQWEALREVQEMAIPAVLLADRDVVIAASTASGKTEAAFLPALTHLLNGdtDGLIVYISPLKALIN--- 86
Cdd:COG1202 195 LPPELKDLL-EGRGEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAGIKNALEG--KGKMLFLVPLVALANqky 271
|
...
gi 2755244177 87 DQF 89
Cdd:COG1202 272 EDF 274
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
29-68 |
1.84e-03 |
|
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: 40.26 E-value: 1.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2755244177 29 VQEMAIPaVLLADRDVVIAASTASGKTEAAFLPALTHLLN 68
Cdd:cd17961 20 IQSKAIP-LALEGKDILARARTGSGKTAAYALPIIQKILK 58
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
27-89 |
2.04e-03 |
|
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: 40.29 E-value: 2.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2755244177 27 REVQEMAIPAVLlADRDVVIAASTASGKTeAAF-LPALtHLLNGDTDGLI-VYISPLKAL---INDQF 89
Cdd:cd17955 23 TPIQKLCIPEIL-AGRDVIGGAKTGSGKT-AAFaLPIL-QRLSEDPYGIFaLVLTPTRELayqIAEQF 87
|
|
| PRK09694 |
PRK09694 |
CRISPR-associated helicase/endonuclease Cas3; |
27-99 |
2.43e-03 |
|
CRISPR-associated helicase/endonuclease Cas3;
Pssm-ID: 182031 [Multi-domain] Cd Length: 878 Bit Score: 41.33 E-value: 2.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2755244177 27 REVQEMaIPAVLLADRDVVIAASTASGKTEAAFLPALTHLLNGDTDGlIVYISPLKALINDQFGRLDRLCEDL 99
Cdd:PRK09694 288 RQLQTL-VDALPLQPGLTIIEAPTGSGKTEAALAYAWRLIDQGLADS-IIFALPTQATANAMLSRLEALASKL 358
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
29-103 |
3.04e-03 |
|
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: 40.04 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 29 VQEMAIPaVLLADRDVVIAASTASGKTEAAFLPALTHLL-------NGDTDGLIVYISPLKALInDQFGRLDR-LCEDLD 100
Cdd:cd17948 16 VQKQGIP-SILRGRNTLCAAETGSGKTLTYLLPIIQRLLrykllaeGPFNAPRGLVITPSRELA-EQIGSVAQsLTEGLG 93
|
...
gi 2755244177 101 IPV 103
Cdd:cd17948 94 LKV 96
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
29-69 |
5.48e-03 |
|
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: 38.82 E-value: 5.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2755244177 29 VQEMAIPaVLLADRDVVIAASTASGKTeAAFLPALTHLLNG 69
Cdd:cd17959 27 IQRKTIP-LILDGRDVVAMARTGSGKT-AAFLIPMIEKLKA 65
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
251-366 |
8.23e-03 |
|
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: 37.19 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755244177 251 KHLHEvlCGtnnLIFPNSRREVERYTHLLNEISEQASRprefwpHHGNLSKEIRSDTEAA-LKQKERpaTAICTNTLELG 329
Cdd:cd18794 27 EHLGG--SG---IIYCLSRKECEQVAARLQSKGISAAA------YHAGLEPSDRRDVQRKwLRDKIQ--VIVATVAFGMG 93
|
90 100 110
....*....|....*....|....*....|....*..
gi 2755244177 330 IDIGAVKSVAQIGTPPSVASLRQRMGRSGrRKGEPAI 366
Cdd:cd18794 94 IDKPDVRFVIHYSLPKSMESYYQESGRAG-RDGLPSE 129
|
|
| |
