|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
151-352 |
4.90e-110 |
|
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: 336.88 E-value: 4.90e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 151 LPERDMEMYRKiKKLDKFYDWQQECLSDKRLLDGENCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVLPYVAIVQEKI 230
Cdd:cd18026 1 LPDAVREAYAK-KGIKKLYDWQKECLSLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRLLERRKKALFVLPYVSIVQEKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 231 SALAPFEDAFGINIEEYASNKGRFPPiKRRKRVSVYVATIEKANMLINSLITQGQLDRVGMVVVDELHMIGDGGRGAILE 310
Cdd:cd18026 80 DALSPLFEELGFRVEGYAGNKGRSPP-KRRKSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDGHRGALLE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 71995032 311 QLLAKFLY--KGTGQIVGMSATLPNIDDLKFALRAFVYSTNFRP 352
Cdd:cd18026 159 LLLTKLLYaaQKNIQIVGMSATLPNLEELASWLRAELYTTNFRP 202
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
157-687 |
3.21e-100 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 323.39 E-value: 3.21e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 157 EMYRKiKKLDKFYDWQQECLsDKRLLDGENCILSLPTGAGKTLIAEVLMLReAIVRKRNAILVLPYVAIVQEKISAL-AP 235
Cdd:COG1204 13 EFLKE-RGIEELYPPQAEAL-EAGLLEGKNLVVSAPTASGKTLIAELAILK-ALLNGGKALYIVPLRALASEKYREFkRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 236 FEDaFGINIeeYASNKGRFPPIKRRKRVSVYVATIEKANmlinSLITQGQ--LDRVGMVVVDELHMIGDGGRGAILEQLL 313
Cdd:COG1204 90 FEE-LGIKV--GVSTGDYDSDDEWLGRYDILVATPEKLD----SLLRNGPswLRDVDLVVVDEAHLIDDESRGPTLEVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 314 AKFLYKGTG-QIVGMSATLPNIDDLKFALRAFVYSTNFRPVELTEFVKIGQTMHqvsengdlnpagdLPTNNLKSTDPdg 392
Cdd:COG1204 163 ARLRRLNPEaQIVALSATIGNAEEIAEWLDAELVKSDWRPVPLNEGVLYDGVLR-------------FDDGSRRSKDP-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 393 ICQLLAKLIPKN-SAVIFCPNKKNCENVAVLIAKTLPAHIRQAKRAESDAFLQSYLSDNDDERMDAVLKQCILSGVAYHH 471
Cdd:COG1204 228 TLALALDLLEEGgQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTNEKLADCLEKGVAFHH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 472 SGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLPVRRVIIKAPM-VGRERLGKAQYLQMAGRAGRAGFDTKGDCITII 550
Cdd:COG1204 308 AGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKrGGMVPIPVLEFKQMAGRAGRPGYDPYGEAILVA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 551 KAGEE-ERWFREMLKSDIPRCMSSLSSEESMGSFILDCVVLKLAENIEEIMTAVRYSLFYAQESPENIRKLVESSVKRLE 629
Cdd:COG1204 388 KSSDEaDELFERYILGEPEPIRSKLANESALRTHLLALIASGFANSREELLDFLENTFYAYQYDKGDLEEVVDDALEFLL 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 71995032 630 EHYFITiepleqdvasepsaqassipRVPGKISPSDLGNAVFNAGFDPDEATRLHADL 687
Cdd:COG1204 468 ENGFIE--------------------EDGDRLRATKLGKLVSRLYIDPLTAAELVDGL 505
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
151-881 |
6.11e-66 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 235.62 E-value: 6.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 151 LPERDMEMYRK--IKKLdkfYDWQQECLsDKRLLDGENCILSLPTGAGKTLIAEVLMLReAIVRKRNAILVLPYVAIVQE 228
Cdd:PRK02362 8 LPEGVIEFYEAegIEEL---YPPQAEAV-EAGLLDGKNLLAAIPTASGKTLIAELAMLK-AIARGGKALYIVPLRALASE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 229 KISALAPFEDaFGINI----------EEYASNKgrfppikrrkrvSVYVATIEKANmlinSLITQGQ--LDRVGMVVVDE 296
Cdd:PRK02362 83 KFEEFERFEE-LGVRVgistgdydsrDEWLGDN------------DIIVATSEKVD----SLLRNGApwLDDITCVVVDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 297 LHMIGDGGRGAILEQLLAKFLYKGTG-QIVGMSATLPNIDDLKFALRAFVYSTNFRPVELTEFVKIGQTMHQVSENGDLN 375
Cdd:PRK02362 146 VHLIDSANRGPTLEVTLAKLRRLNPDlQVVALSATIGNADELADWLDAELVDSEWRPIDLREGVFYGGAIHFDDSQREVE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 376 PAGDLPTNNLkstdpdgicqLLAKLIPKNSAVIFCPNKKNCENVAVLIAKTLPAHIRQAKRAESDAFLQSYLSDNDDErM 455
Cdd:PRK02362 226 VPSKDDTLNL----------VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVSDTE-T 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 456 DAVLKQCILSGVAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLPVRRVIIK-----APMVGRERLGKAQYLQ 530
Cdd:PRK02362 295 SKDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRdyrryDGGAGMQPIPVLEYHQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 531 MAGRAGRAGFDTKGDCITIIKAGEE-ERWFREMLKSDIPRCMSSLSSEESMGSFILDCVVLKLAENIEEIMTAVRYSLF- 608
Cdd:PRK02362 375 MAGRAGRPGLDPYGEAVLLAKSYDElDELFERYIWADPEDVRSKLATEPALRTHVLSTIASGFARTRDGLLEFLEATFYa 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 609 YAQESPENIRKLVESSVKRLEEHYFITiepleqdvasepsaqassipRVPGKISPSDLGNAVFNAGFDPDEAtrlhADLV 688
Cdd:PRK02362 455 TQTDDTGRLERVVDDVLDFLERNGMIE--------------------EDGETLEATELGHLVSRLYIDPLSA----AEII 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 689 SSLnQGVIFASHFHLLFII--TPyeqvcninwDLFLLmYnaLPSSERKLLAECGLE--EKFILEA-----IITRVDLTAG 759
Cdd:PRK02362 511 DGL-EAAKKPTDLGLLHLVcsTP---------DMYEL-Y--LRSGDYEWLNEYLYEheDELLGDVpsefeDDEFEDFLSA 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 760 tprmrLYIALMLQKiWNHE-PMYTVAERFGVEKGWLQATLQSS---ISQAASIAKFsekitTMWPLRKLLPELVQRLSEA 835
Cdd:PRK02362 578 -----VKTALLLED-WIDEvDEERITERYGVGPGDIRGKVETAewlLHAAERLASE-----LDLDLARAARELEKRVEYG 646
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 71995032 836 AQPELLPLMTVDGIKKARAAILFKAGYKTVGMIARANPLKLVQELG 881
Cdd:PRK02362 647 VREELLDLVGLRGVGRVRARRLYNAGIESRADLRAADKSVVLAILG 692
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
167-898 |
6.19e-57 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 208.58 E-value: 6.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 167 KFYDWQQECLsdKRLLDGENCILSLPTGAGKTLIAeVLMLREAIVRKRNAILVLPYVAIVQEKISALAPFED---AFGIN 243
Cdd:PRK01172 22 ELYDHQRMAI--EQLRKGENVIVSVPTAAGKTLIA-YSAIYETFLAGLKSIYIVPLRSLAMEKYEELSRLRSlgmRVKIS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 244 IEEYASnkgrfPPiKRRKRVSVYVATIEKANMLINSliTQGQLDRVGMVVVDELHMIGDGGRGAILEQLLAKFLY-KGTG 322
Cdd:PRK01172 99 IGDYDD-----PP-DFIKRYDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSARYvNPDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 323 QIVGMSATLPNIDDLKFALRAFVYSTNFRPVELtefvKIGqTMHQVSENGDLNPAGDLPTNNL-KSTDPDGicqllakli 401
Cdd:PRK01172 171 RILALSATVSNANELAQWLNASLIKSNFRPVPL----KLG-ILYRKRLILDGYERSQVDINSLiKETVNDG--------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 402 pkNSAVIFCPNKKNCENVAVLIAKTLPahirqakraeSDAFLQSYLSDNDDerMDAVLKQCILSGVAYHHSGLTQDERKC 481
Cdd:PRK01172 237 --GQVLVFVSSRKNAEDYAEMLIQHFP----------EFNDFKVSSENNNV--YDDSLNEMLPHGVAFHHAGLSNEQRRF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 482 VEAAFMEGLIYVVCATSTLAAGVNLPVRRVIIKApmVGRERLGKAQYL------QMAGRAGRAGFDTKGdcITIIKAGEE 555
Cdd:PRK01172 303 IEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRD--ITRYGNGGIRYLsnmeikQMIGRAGRPGYDQYG--IGYIYAASP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 556 ERW--FREMLKSDiPRCMSSLSSEESMGSF-ILDCVVLKLAENIEEIMTAVRYSLFYAQESPENIRKLVESSVKRLEEHY 632
Cdd:PRK01172 379 ASYdaAKKYLSGE-PEPVISYMGSQRKVRFnTLAAISMGLASSMEDLILFYNETLMAIQNGVDEIDYYIESSLKFLKENG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 633 FItieplEQDVAsepsaqassiprvpgkISPSDLGNAVFNAGFDPDEATRlhadLVSSLNQgvifashfhllfiitpyeq 712
Cdd:PRK01172 458 FI-----KGDVT----------------LRATRLGKLTSDLYIDPESALI----LKSAFDH------------------- 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 713 vcniNWDLFLLMYNALPSSErklLAECGLEEKFILEAIITRVDLTAGTPRMRlYIALMLQKIWNHEPMYTVAERFGVEKG 792
Cdd:PRK01172 494 ----DYDEDLALYYISLCRE---IIPANTRDDYYAMEFLEDIGVIDGDISAA-KTAMVLRGWISEASMQKITDTYGIAPG 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 793 WLQATLQSSISQAASIAKFSEKITTmwPLRKLLPELVQRLSEAAQPELLPLMTVDGIKKARAAILFKAGYKTVGMIARAN 872
Cdd:PRK01172 566 DVQARASSADWISYSLARLSSIYKP--EMRRKLEILNIRIKEGIREDLIDLVLIPKVGRVRARRLYDAGFKTVDDIARSS 643
|
730 740
....*....|....*....|....*.
gi 71995032 873 PLKLVQELGtIRMAQANSIIASARMV 898
Cdd:PRK01172 644 PERIKKIYG-FSDTLANAIVNRAMKI 668
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
153-878 |
1.38e-52 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 196.58 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 153 ERDMEMYRKiKKLDKFYDWQQECLSDKrLLDGENCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVLPYVAIVQEKISA 232
Cdd:PRK00254 10 ERIKRVLKE-RGIEELYPPQAEALKSG-VLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGGKAVYLVPLKALAEEKYRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 233 LAPFEDaFGINIE----EYASNK---GRFPPIkrrkrvsvyVATIEKanmlINSLITQGQ--LDRVGMVVVDELHMIGDG 303
Cdd:PRK00254 88 FKDWEK-LGLRVAmttgDYDSTDewlGKYDII---------IATAEK----FDSLLRHGSswIKDVKLVVADEIHLIGSY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 304 GRGAILEQLLAKFLykGTGQIVGMSATLPNIDDLKFALRAFVYSTNFRPVELTEFVkigqtMHQ---VSENGDLnpagDL 380
Cdd:PRK00254 154 DRGATLEMILTHML--GRAQILGLSATVGNAEELAEWLNAELVVSDWRPVKLRKGV-----FYQgflFWEDGKI----ER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 381 PTNNLKSTDPDGICQllaklipKNSAVIFCPNKKNCENVAVLIAKTLPAHIRQAKRAESDAFLQSYLSDNDDERmdavLK 460
Cdd:PRK00254 223 FPNSWESLVYDAVKK-------GKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKELADSLEENPTNEK----LK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 461 QCILSGVAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLPVRRVIIKAPM----VGRERLGKAQYLQMAGRAG 536
Cdd:PRK00254 292 KALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKrysnFGWEDIPVLEIQQMMGRAG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 537 RAGFDTKGDCITIIKAGEEERWFREMLKSDIPRCMSSLSSEESMGSFILDCVVLKLAENIEEIMTAVRYSLFYAQES-PE 615
Cdd:PRK00254 372 RPKYDEVGEAIIVATTEEPSKLMERYIFGKPEKLFSMLSNESAFRSQVLALITNFGVSNFKELVNFLERTFYAHQRKdLY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 616 NIRKLVESSVKRLEEHYFITIEpLEQdvasepsaqassiprvpgKISPSDLGNAVFNAGFDPDEAtRLHADLVSSLNQGV 695
Cdd:PRK00254 452 SLEEKAKEIVYFLLENEFIDID-LED------------------RFIPLPLGIRTSQLYIDPLTA-KKFKDAFPKIEKNP 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 696 IFASHFHLLfIITPYEQVCNINWDLFLLMYNALPSSERKLLAECGLEEKFILEAIITRVDltagtprmrlyIALMLQKIW 775
Cdd:PRK00254 512 NPLGIFQLI-ASTPDMTPLNYSRKEMEDLLDEAYEMEDRLYFNIPYWEDYKFQKFLRAFK-----------TAKVLLDWI 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 776 NHEPMYTVAERFGVEKGWLQATLQS------SISQAASIAKFSEKITtmwplrKLLPELVQRLSEAAQPELLPLMTVDGI 849
Cdd:PRK00254 580 NEVPEGEIVETYNIDPGDLYRILELadwlmySLIELYKLFEPKQEVL------DYLETLHLRVKHGVREELLELMRLPMI 653
|
730 740
....*....|....*....|....*....
gi 71995032 850 KKARAAILFKAGYKTVGMIARANPLKLVQ 878
Cdd:PRK00254 654 GRKRARALYNAGFRSIEDIVNAKPSELLK 682
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
351-551 |
8.76e-46 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 161.18 E-value: 8.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 351 RPVELTEFVKIGQTMHQVSENGDLNPAGDLPTNNLKstdpdgICQLLakliPKNSAVIFCPNKKNCENVAVliaktlpah 430
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKFDSDIIVLLK------IETVS----EGKPVLVFCSSRKECEKTAK--------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 431 irqakraesdaflqsylsdnddermdavlkqcILSGVAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLPVRR 510
Cdd:cd18795 62 --------------------------------DLAGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPART 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 71995032 511 VIIKAPMV----GRERLGKAQYLQMAGRAGRAGFDTKGDCITIIK 551
Cdd:cd18795 110 VIIKGTQRydgkGYRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
169-566 |
3.93e-42 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 165.50 E-value: 3.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 169 YDWQQE-CLSdkrLLDGENCILSLPTGAGKTLIAEVlMLREAIVRKRNAILVLPYVAIVQEKISALApfeDAFG------ 241
Cdd:COG4581 27 DPFQEEaILA---LEAGRSVLVAAPTGSGKTLVAEF-AIFLALARGRRSFYTAPIKALSNQKFFDLV---ERFGaenvgl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 242 ------INIEeyasnkgrfPPIkrrkrvsVyVATIEkanMLINSLITQGQ-LDRVGMVVVDELHMIGDGGRGAILEQLLa 314
Cdd:COG4581 100 ltgdasVNPD---------API-------V-VMTTE---ILRNMLYREGAdLEDVGVVVMDEFHYLADPDRGWVWEEPI- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 315 kfLY-KGTGQIVGMSATLPNIDDLKFALR------AFVYSTnFRPVELTEFVKIGQTMHqvsengdlnpagDLPTNNLKS 387
Cdd:COG4581 159 --IHlPARVQLVLLSATVGNAEEFAEWLTrvrgetAVVVSE-ERPVPLEFHYLVTPRLF------------PLFRVNPEL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 388 TDPDGICQLLAKLIPKN--SAVIFCPNKKNCENVAVLIAKTlpahiRQAKRAESDAFLQsyLSDNDDERMDAV----LKQ 461
Cdd:COG4581 224 LRPPSRHEVIEELDRGGllPAIVFIFSRRGCDEAAQQLLSA-----RLTTKEERAEIRE--AIDEFAEDFSVLfgktLSR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 462 CILSGVAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLPVRRVII----KAPMVGRERLGKAQYLQMAGRAGR 537
Cdd:COG4581 297 LLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFtklsKFDGERHRPLTAREFHQIAGRAGR 376
|
410 420
....*....|....*....|....*....
gi 71995032 538 AGFDTKGDCITIIKAGEEERWFREMLKSD 566
Cdd:COG4581 377 RGIDTEGHVVVLAPEHDDPKKFARLASAR 405
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
168-337 |
1.16e-33 |
|
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: 127.76 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 168 FYDWQQECLsDKRLLDGENCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVLPYVAIVQEKISALAPFEDAFGINIEEY 247
Cdd:cd17921 2 LNPIQREAL-RALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 248 ASNKGRFPPIKRRKRvsVYVATIEKANMLINSLITQGqLDRVGMVVVDELHMIGDGGRGAILEQLLAKFLYKGTG-QIVG 326
Cdd:cd17921 81 TGDPSVNKLLLAEAD--ILVATPEKLDLLLRNGGERL-IQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRINKNaRFVG 157
|
170
....*....|.
gi 71995032 327 MSATLPNIDDL 337
Cdd:cd17921 158 LSATLPNAEDL 168
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
172-337 |
1.03e-26 |
|
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: 107.81 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 172 QQECLSDKRLLDGENCILSLPTGAGKTLIAEVLMLREAIVRKRnAILVLPYVAIVQEKISALAPFEDA---FGINIEEYA 248
Cdd:cd18028 5 PQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGK-ALYLVPLRALASEKYEEFKKLEEIglkVGISTGDYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 249 SnkgrfpPIKRRKRVSVYVATIEKanmlINSLITQGQ--LDRVGMVVVDELHMIGDGGRGAILEQLLAKFLYKGTG-QIV 325
Cdd:cd18028 84 E------DDEWLGDYDIIVATYEK----FDSLLRHSPswLRDVGVVVVDEIHLISDEERGPTLESIVARLRRLNPNtQII 153
|
170
....*....|..
gi 71995032 326 GMSATLPNIDDL 337
Cdd:cd18028 154 GLSATIGNPDEL 165
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
172-337 |
6.21e-24 |
|
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: 99.24 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 172 QQECLsdKRLLDGENCILSLPTGAGKTLIAEVLMLrEAIVRKRN---AILVLPYVAIVQEKISALAPFEDAFGINIEEYA 248
Cdd:pfam00270 4 QAEAI--PAILEGRDVLVQAPTGSGKTLAFLLPAL-EALDKLDNgpqALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 249 SNKGRFPPIKRRKRVSVYVATIEKanmLINSLITQGQLDRVGMVVVDELHMIGDGGRGAILEQLLAKFLYKgtGQIVGMS 328
Cdd:pfam00270 81 GGDSRKEQLEKLKGPDILVGTPGR---LLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKK--RQILLLS 155
|
170
....*....|
gi 71995032 329 ATLP-NIDDL 337
Cdd:pfam00270 156 ATLPrNLEDL 165
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
181-544 |
7.49e-22 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 101.51 E-value: 7.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 181 LLDGENCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVLPYVAIVQEKISAL-APFEDAFGINIEEYAS----NKGRFP 255
Cdd:COG1202 222 LLEGKDQLVVSATATGKTLIGELAGIKNALEGKGKMLFLVPLVALANQKYEDFkDRYGDGLDVSIRVGASrirdDGTRFD 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 256 PikrrkRVSVYVATIEKANMLINsliTQGQLDRVGMVVVDELHMIGDGGRGAILEQLLA--KFLYKGTgQIVGMSATLPN 333
Cdd:COG1202 302 P-----NADIIVGTYEGIDHALR---TGRDLGDIGTVVIDEVHMLEDPERGHRLDGLIArlKYYCPGA-QWIYLSATVGN 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 334 IDDLKFALRAFVYSTNFRPVELTEFVKIGQtmhqvsENGDLNPAGDLPTNNLKSTDPDGIcqllaklipKNSAVIFCPNK 413
Cdd:COG1202 373 PEELAKKLGAKLVEYEERPVPLERHLTFAD------GREKIRIINKLVKREFDTKSSKGY---------RGQTIIFTNSR 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 414 KNCENvavlIAKTLPahirqakraesdaflqsylsdndderMDAvlkqcilsgvAYHHSGLTQDERKCVEAAFMEGLIYV 493
Cdd:COG1202 438 RRCHE----IARALG--------------------------YKA----------APYHAGLDYGERKKVERRFADQELAA 477
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 71995032 494 VCATSTLAAGVNLPVRRVIIKAPMVGRERLGKAQYLQMAGRAGRAGFDTKG 544
Cdd:COG1202 478 VVTTAALAAGVDFPASQVIFDSLAMGIEWLSVQEFHQMLGRAGRPDYHDRG 528
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
163-333 |
2.77e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 84.08 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 163 KKLDKFYDWQQECLsdKRLLDGE-NCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVL-PYVAIVQEKISALAP-FEDA 239
Cdd:smart00487 4 FGFEPLRPYQKEAI--EALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLvPTRELAEQWAEELKKlGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 240 FGINIEEY-ASNKGRFPPIKRRKRVSVYVATIEKA-NMLINSLItqgQLDRVGMVVVDELHMIGDGGRGAILEQLLAKFl 317
Cdd:smart00487 82 GLKVVGLYgGDSKREQLRKLESGKTDILVTTPGRLlDLLENDKL---SLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL- 157
|
170
....*....|....*.
gi 71995032 318 yKGTGQIVGMSATLPN 333
Cdd:smart00487 158 -PKNVQLLLLSATPPE 172
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
184-330 |
8.63e-17 |
|
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: 78.21 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 184 GENCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVLPYVAIVQEKISALAPFEDAfGINIEEY--ASNKGRfPPIKRRK 261
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLvgGSSAEE-REKNKLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71995032 262 RVSVYVATIEKANMLINSLiTQGQLDRVGMVVVDELHMIGDGGRGAILEQLLAKFLYKGTGQIVGMSAT 330
Cdd:cd00046 79 DADIIIATPDMLLNLLLRE-DRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
453-539 |
9.81e-17 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 75.71 E-value: 9.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 453 ERMDAVLKQCILSgVAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLP-VRRVIIKAPmvgreRLGKAQYLQM 531
Cdd:smart00490 1 EELAELLKELGIK-VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL-----PWSPASYIQR 74
|
....*...
gi 71995032 532 AGRAGRAG 539
Cdd:smart00490 75 IGRAGRAG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
169-569 |
4.30e-16 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 82.77 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 169 YDWQQECLS---DKRLLDGENCILSLPTGAGKTLIAeVLMLREAIVRKRnaILVL-PYVAIVQekiSALAPFEDAFGIni 244
Cdd:COG1061 82 RPYQQEALEallAALERGGGRGLVVAPTGTGKTVLA-LALAAELLRGKR--VLVLvPRRELLE---QWAEELRRFLGD-- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 245 eeyASNKGRFPPIKRRkrvsVYVATIEKANMLINSLITQgqlDRVGMVVVDELHMIGDGGRGAILEQLLAKFlykgtgqI 324
Cdd:COG1061 154 ---PLAGGGKKDSDAP----ITVATYQSLARRAHLDELG---DRFGLVIIDEAHHAGAPSYRRILEAFPAAY-------R 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 325 VGMSATLPNIDDLKFALRAF---VYstNFRPVE------LTEFVKIGQTMHQVSENGDLNPAGDLPTNNLKSTDP---DG 392
Cdd:COG1061 217 LGLTATPFRSDGREILLFLFdgiVY--EYSLKEaiedgyLAPPEYYGIRVDLTDERAEYDALSERLREALAADAErkdKI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 393 ICQLLAKLIPKNSAVIFCPNKKNCENVAvliaktlpahirqakraesDAFLQSYLSdnddermdavlkqcilsgVAYHHS 472
Cdd:COG1061 295 LRELLREHPDDRKTLVFCSSVDHAEALA-------------------ELLNEAGIR------------------AAVVTG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 473 GLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLP-VRRVIIKAPmVGRERlgkaQYLQMAGRAGRAgFDTKGDCITIIK 551
Cdd:COG1061 338 DTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPrLDVAILLRP-TGSPR----EFIQRLGRGLRP-APGKEDALVYDF 411
|
410
....*....|....*...
gi 71995032 552 AGEEERWFREMLKSDIPR 569
Cdd:COG1061 412 VGNDVPVLEELAKDLRDL 429
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
151-342 |
8.55e-15 |
|
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: 74.33 E-value: 8.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 151 LPERDMEMYRKIKKLDKFydwqQECLSDKRLLDGENCILSLPTGAGKTLIAEVLMLREaIVRKRNA-----------ILV 219
Cdd:cd18019 4 LPDWAQPAFEGFKSLNRI----QSKLFPAAFETDENLLLCAPTGAGKTNVALLTILRE-IGKHRNPdgtinldafkiVYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 220 LPYVAIVQEKISALAPFEDAFGINIEEYASNKGRfppikRRKRVS---VYVATIEKANmlinsLITQGQLDR-----VGM 291
Cdd:cd18019 79 APMKALVQEMVGNFSKRLAPYGITVAELTGDQQL-----TKEQISetqIIVTTPEKWD-----IITRKSGDRtytqlVRL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 71995032 292 VVVDELHMIGDgGRGAILEQLLAKFLY--KGTGQ---IVGMSATLPNIDDLKFALR 342
Cdd:cd18019 149 IIIDEIHLLHD-DRGPVLESIVARTIRqiEQTQEyvrLVGLSATLPNYEDVATFLR 203
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
136-539 |
8.35e-14 |
|
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: 75.64 E-value: 8.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 136 PEKRPETLTLDPSkcLPERDMEMYRKiKKLDKFYDWQQECLsdKRLLDGENCILSLPTGAGKTLIAEVLMLrEAIVRKRN 215
Cdd:COG1205 28 PAREARYAPWPDW--LPPELRAALKK-RGIERLYSHQAEAI--EAARAGKNVVIATPTASGKSLAYLLPVL-EALLEDPG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 216 --AILVLPYVAIVQEKISALAPFEDAFG--INIEEYasnKGRFPPIKRRKrvsVYvatiEKANMLI------NSLITQGQ 285
Cdd:COG1205 102 atALYLYPTKALARDQLRRLRELAEALGlgVRVATY---DGDTPPEERRW---IR----EHPDIVLtnpdmlHYGLLPHH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 286 ------LDRVGMVVVDELHMIgdggRGA-------ILEQL--LAKFlYKGTGQIVGMSATLPNiddlkfalrafvystnf 350
Cdd:COG1205 172 trwarfFRNLRYVVIDEAHTY----RGVfgshvanVLRRLrrICRH-YGSDPQFILASATIGN----------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 351 rPVELTEFVkIGQTMHQVSENGdlNPAGD----------LPTNNLKSTDPDGIcQLLAKLIPKNSAVI-FCPNKKNCENV 419
Cdd:COG1205 230 -PAEHAERL-TGRPVTVVDEDG--SPRGErtfvlwnpplVDDGIRRSALAEAA-RLLADLVREGLRTLvFTRSRRGAELL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 420 AvliaktlpahiRQAKRAesdaflqsyLSDNDDErmdavlkqcilSGVAYHHSGLTQDERKCVEAAFMEGLIYVVCATST 499
Cdd:COG1205 305 A-----------RYARRA---------LREPDLA-----------DRVAAYRAGYLPEERREIERGLRSGELLGVVSTNA 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 71995032 500 LAAGVNLP-VRRVIikapMVG----RerlgkAQYLQMAGRAGRAG 539
Cdd:COG1205 354 LELGIDIGgLDAVV----LAGypgtR-----ASFWQQAGRAGRRG 389
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
172-352 |
2.30e-13 |
|
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: 70.08 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 172 QQECLSDKRLLDgENCILSLPTGAGKTLIAEVLMLReaIVRKRNAILVLPYVAIVQEKISALAPfedafginiEEYASNK 251
Cdd:cd18023 6 QSEVFPDLLYSD-KNFVVSAPTGSGKTVLFELAILR--LLKERNPLPWGNRKVVYIAPIKALCS---------EKYDDWK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 252 GRFPPIKrrkrVSVYVAT----------IEKANMLINS-----LITQGQLDRVGM------VVVDELHMIGDgGRGAILE 310
Cdd:cd18023 74 EKFGPLG----LSCAELTgdtemddtfeIQDADIILTTpekwdSMTRRWRDNGNLvqlvalVLIDEVHIIKE-NRGATLE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71995032 311 QLLA--KFLYKGTG---------QIVGMSATLPNIDDLKFALRA-----FVYSTNFRP 352
Cdd:cd18023 149 VVVSrmKTLSSSSElrgstvrpmRFVAVSATIPNIEDLAEWLGDnpagcFSFGESFRP 206
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
185-337 |
6.61e-13 |
|
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: 68.17 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 185 ENCILSLPTGAGKTLIAEVLMLReaIVRKR---NAILVLPYVAIVQEKISA-LAPFEDAFGINIEEYASNKGrfPPIKRR 260
Cdd:cd18022 18 NNVLLGAPTGSGKTIAAELAMFR--AFNKYpgsKVVYIAPLKALVRERVDDwKKRFEEKLGKKVVELTGDVT--PDMKAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 261 KRVSVYVATIEKANMLINSLITQGQLDRVGMVVVDELHMIGDgGRGAILEQLLA--KFLYKGTGQ---IVGMSATLPNID 335
Cdd:cd18022 94 ADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGS-DRGPVLEVIVSrmNYISSQTEKpvrLVGLSTALANAG 172
|
..
gi 71995032 336 DL 337
Cdd:cd18022 173 DL 174
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
467-539 |
2.26e-11 |
|
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: 61.46 E-value: 2.26e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71995032 467 VAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLP-VRRVII-KAPmvgrerLGKAQYLQMAGRAGRAG 539
Cdd:pfam00271 41 VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVINyDLP------WNPASYIQRIGRAGRAG 109
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
168-331 |
2.94e-11 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 62.32 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 168 FYDWQQECLsdKRLLDGEN---CILSLPTGAGKTLIAEVLMlreAIVRKRNAILVLPYVAIVqEKISAlapfedafgiNI 244
Cdd:cd17926 1 LRPYQEEAL--EAWLAHKNnrrGILVLPTGSGKTLTALALI---AYLKELRTLIVVPTDALL-DQWKE----------RF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 245 EEYASNK--GRF--PPIKRRKRVSVYVATIEKANMLINSliTQGQLDRVGMVVVDELHMIGDGGRGAILEQLLAKFLykg 320
Cdd:cd17926 65 EDFLGDSsiGLIggGKKKDFDDANVVVATYQSLSNLAEE--EKDLFDQFGLLIVDEAHHLPAKTFSEILKELNAKYR--- 139
|
170
....*....|.
gi 71995032 321 tgqiVGMSATL 331
Cdd:cd17926 140 ----LGLTATP 146
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
185-337 |
5.53e-11 |
|
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: 62.66 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 185 ENCILSLPTGAGKTLIAEVLMLReAIVRKRNAILVlpYVAIVQEKISALAP-----FEDAFGINIE----EYASNkgrfp 255
Cdd:cd18021 20 DNVFVGAPTGSGKTVCAELALLR-HWRQNPKGRAV--YIAPMQELVDARYKdwrakFGPLLGKKVVkltgETSTD----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 256 pIKRRKRVSVYVATIEKANMLINSLITQGQLDRVGMVVVDELHMIGdGGRGAILEQLLAKFLYKGTGQ-----IVGMSAT 330
Cdd:cd18021 92 -LKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIG-GENGPVYEVVVSRMRYISSQLekpirIVGLSSS 169
|
....*..
gi 71995032 331 LPNIDDL 337
Cdd:cd18021 170 LANARDV 176
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
182-332 |
2.33e-10 |
|
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: 60.95 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 182 LDGENCILSLPTGAGKTLIAeVLMLREAIVRKRNA------ILVLPYVAIVQEKISALA-PFEDAFGIN-IEEYASNKGR 253
Cdd:cd18036 15 LRGKNTIICAPTGSGKTRVA-VYICRHHLEKRRSAgekgrvVVLVNKVPLVEQQLEKFFkYFRKGYKVTgLSGDSSHKVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 254 FPPIKRRKRVSVYVATIekanmLINSLITQGQLDRV-----GMVVVDELHMIGDGGRGAILEQLLAKFLYKGTG---QIV 325
Cdd:cd18036 94 FGQIVKASDVIICTPQI-----LINNLLSGREEERVylsdfSLLIFDECHHTQKEHPYNKIMRMYLDKKLSSQGplpQIL 168
|
....*..
gi 71995032 326 GMSATLP 332
Cdd:cd18036 169 GLTASPG 175
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
185-350 |
6.25e-10 |
|
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: 59.75 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 185 ENCILSLPTGAGKTLIAEVLMLREAivrkRNAILVLPYVAIVQEKISALAPFEdAFGINIEEYASNKGRFPPIKRR---- 260
Cdd:cd18020 18 ENMLICAPTGAGKTNIAMLTILHEI----RQHVNQGGVIKKDDFKIVYIAPMK-ALAAEMVEKFSKRLAPLGIKVKeltg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 261 ---------KRVSVYVATIEKANMLINSLITQGQL-DRVGMVVVDELHMIGDgGRGAILEQLLAKFLYK-GTGQ----IV 325
Cdd:cd18020 93 dmqltkkeiAETQIIVTTPEKWDVVTRKSSGDVALsQLVRLLIIDEVHLLHD-DRGPVIESLVARTLRQvESTQsmirIV 171
|
170 180
....*....|....*....|....*
gi 71995032 326 GMSATLPNIDDLKFALRAFVYSTNF 350
Cdd:cd18020 172 GLSATLPNYLDVADFLRVNPYKGLF 196
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
167-330 |
1.12e-09 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 58.07 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 167 KFYDWQQECLSD---KRLLDGENCILSLPTGAGKTLIAEVLMLR-EAIVRKRNAILVLPYVAIVQEKISALAPFEDAFGI 242
Cdd:pfam04851 3 ELRPYQIEAIENlleSIKNGQKRGLIVMATGSGKTLTAAKLIARlFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 243 NIEEYASNKGRFPPIKRRkrvsVYVATIEKANMLINSLITQGQLDRVGMVVVDELHMIGDGGRGAILEQLLAKFLykgtg 322
Cdd:pfam04851 83 IGEIISGDKKDESVDDNK----IVVTTIQSLYKALELASLELLPDFFDVIIIDEAHRSGASSYRNILEYFKPAFL----- 153
|
....*...
gi 71995032 323 qiVGMSAT 330
Cdd:pfam04851 154 --LGLTAT 159
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
405-539 |
1.69e-09 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 56.83 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 405 SAVIFCPNKKNCENVAvliaktlpahirqakraesdaflqsylsdnddermdAVLKQCILSGVAYHHsGLTQDERKCVEA 484
Cdd:cd18794 32 SGIIYCLSRKECEQVA------------------------------------ARLQSKGISAAAYHA-GLEPSDRRDVQR 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 71995032 485 AFMEGLIYVVCATSTLAAGVNLP-VRRVI---IKAPMVGrerlgkaqYLQMAGRAGRAG 539
Cdd:cd18794 75 KWLRDKIQVIVATVAFGMGIDKPdVRFVIhysLPKSMES--------YYQESGRAGRDG 125
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
467-537 |
1.77e-08 |
|
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: 54.19 E-value: 1.77e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995032 467 VAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNL-PVRRVI-IKAPmvgrerLGKAQYLQMAGRAGR 537
Cdd:cd18796 71 IALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIgDVDLVIqIGSP------KSVARLLQRLGRSGH 137
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
184-336 |
1.96e-08 |
|
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: 54.51 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 184 GENCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVLpYVAivqeKISALApfEDAFGiNIEEYAsnKGRFPPI------ 257
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVL-YIS----PLKALI--NDQER-RLEEPL--DEIDLEIpvavrh 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 258 -------KRRKRVS---VYVATIEKANMLINSLITQGQLDRVGMVVVDELHMIGDGGRGAILEQLLAKF--LYKGTGQIV 325
Cdd:cd17922 71 gdtsqseKAKQLKNppgILITTPESLELLLVNKKLRELFAGLRYVVVDEIHALLGSKRGVQLELLLERLrkLTGRPLRRI 150
|
170
....*....|.
gi 71995032 326 GMSATLPNIDD 336
Cdd:cd17922 151 GLSATLGNLEE 161
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
179-334 |
9.43e-08 |
|
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: 52.97 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 179 KRLLDGENCILSLPTGAGKTLIAEVLMLREAIVRKRN-AILVLPYVAIVQEKISALAPFEDAFGINIeEYASNKGRFPPI 257
Cdd:cd17923 10 EAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSrALYLYPTKALAQDQLRSLRELLEQLGLGI-RVATYDGDTPRE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 258 KRRKRVsvyvatIEKANMLI-N------SLITQGQLDRVGM-----VVVDELHMIgDGGRGAILEQLLAKFL-----YKG 320
Cdd:cd17923 89 ERRAII------RNPPRILLtNpdmlhyALLPHHDRWARFLrnlryVVLDEAHTY-RGVFGSHVALLLRRLRrlcrrYGA 161
|
170
....*....|....
gi 71995032 321 TGQIVGMSATLPNI 334
Cdd:cd17923 162 DPQFILTSATIGNP 175
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
167-330 |
9.02e-07 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 50.51 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 167 KFYDWQQECLsdKRLLDGENCILSLPTGAGKTLIAEVLM---LREAIVRKRNAILVL-PYVAIVQEKISALAPFEDAFGI 242
Cdd:cd17927 2 KPRNYQLELA--QPALKGKNTIICLPTGSGKTFVAVLICehhLKKFPAGRKGKVVFLaNKVPLVEQQKEVFRKHFERPGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 243 NIEEYA---SNKGRFPpiKRRKRVSVYVATiekANMLINSLI--TQGQLDRVGMVVVDELHM-IGDGGRGAILEQLLAKF 316
Cdd:cd17927 80 KVTGLSgdtSENVSVE--QIVESSDVIIVT---PQILVNDLKsgTIVSLSDFSLLVFDECHNtTKNHPYNEIMFRYLDQK 154
|
170
....*....|....*.
gi 71995032 317 LYKGTG--QIVGMSAT 330
Cdd:cd17927 155 LGSSGPlpQILGLTAS 170
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
286-536 |
1.16e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 52.62 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 286 LDRVGMVVVDELHMIGDGGRGAILEQLLAKF--LYKGTGQIVGMSATLPNIDDLKFALRA-----FVYSTNFRPVELTEF 358
Cdd:PRK09751 122 LRGVETVIIDEVHAVAGSKRGAHLALSLERLdaLLHTSAQRIGLSATVRSASDVAAFLGGdrpvtVVNPPAMRHPQIRIV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 359 VKIgQTMHQVSENGDlNPAGDLPTNNLKSTDPDGICQLLAKLIPKNSAVIFCPNKKNCENVAVLIAKTLPAHIRQAKRAE 438
Cdd:PRK09751 202 VPV-ANMDDVSSVAS-GTGEDSHAGREGSIWPYIETGILDEVLRHRSTIVFTNSRGLAEKLTARLNELYAARLQRSPSIA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 439 SDAFLQSYLSDNDDERMDAVLKQCILSgvayHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLPVRRVIIK--AP 516
Cdd:PRK09751 280 VDAAHFESTSGATSNRVQSSDVFIARS----HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQvaTP 355
|
250 260
....*....|....*....|
gi 71995032 517 mvgrerLGKAQYLQMAGRAG 536
Cdd:PRK09751 356 ------LSVASGLQRIGRAG 369
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
169-330 |
1.26e-06 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 49.10 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 169 YDWQQECLS--DKRLLDGENCIL-SLPTGAGKTLIAEVLMLR--EAIVRKRnaILVLPY-VAIV-QekisALAPFEDAFG 241
Cdd:cd18032 2 RYYQQEAIEalEEAREKGQRRALlVMATGTGKTYTAAFLIKRllEANRKKR--ILFLAHrEELLeQ----AERSFKEVLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 242 INiEEYASNKGRFPPIKRRkrvsVYVATIEKanmlINSLITQGQL--DRVGMVVVDELHMIGDGGRGAILEQLLAKFLyk 319
Cdd:cd18032 76 DG-SFGNLKGGKKKPDDAR----VVFATVQT----LNKRKRLEKFppDYFDLIIIDEAHHAIASSYRKILEYFEPAFL-- 144
|
170
....*....|.
gi 71995032 320 gtgqiVGMSAT 330
Cdd:cd18032 145 -----LGLTAT 150
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
430-568 |
1.30e-06 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 52.07 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 430 HIRQAKRAESDAFLQSYLSDNDD-------------ERMDAVLKQCILSGVAYHhSGLTQDERKCVEAAFMEGLIYVVCA 496
Cdd:COG0514 208 EVVPKPPDDKLAQLLDFLKEHPGgsgivyclsrkkvEELAEWLREAGIRAAAYH-AGLDAEEREANQDRFLRDEVDVIVA 286
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71995032 497 TSTLAAGVNLP-VRRVI-IKAP--MVGrerlgkaqYLQMAGRAGRAGfdTKGDCITIIKAGEEERWfREMLKSDIP 568
Cdd:COG0514 287 TIAFGMGIDKPdVRFVIhYDLPksIEA--------YYQEIGRAGRDG--LPAEALLLYGPEDVAIQ-RFFIEQSPP 351
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
160-332 |
1.49e-06 |
|
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: 49.84 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 160 RKIKKLDKFYDWQQECLsdKRLLDGENCILSLPTGAGKTLIAEVlmlrEAIVRKRNAILVLPYVAIVQEKISALApfedA 239
Cdd:cd17920 5 KEVFGYDEFRPGQLEAI--NAVLAGRDVLVVMPTGGGKSLCYQL----PALLLDGVTLVVSPLISLMQDQVDRLQ----Q 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 240 FGINIEEYASNKGRFPPIKRRKRVS------VYVaTIEKA--NMLINSLITQGQLDRVGMVVVDELHMI---GDGGR--- 305
Cdd:cd17920 75 LGIRAAALNSTLSPEEKREVLLRIKngqyklLYV-TPERLlsPDFLELLQRLPERKRLALIVVDEAHCVsqwGHDFRpdy 153
|
170 180 190
....*....|....*....|....*....|
gi 71995032 306 ---GAILEQLlakflykGTGQIVGMSATLP 332
Cdd:cd17920 154 lrlGRLRRAL-------PGVPILALTATAT 176
|
|
| HTH_61 |
pfam20470 |
Helix-turn-helix domain; This entry represents a presumed helix-turn-helix domain found in DNA ... |
584-635 |
3.05e-06 |
|
Helix-turn-helix domain; This entry represents a presumed helix-turn-helix domain found in DNA polymerase theta.
Pssm-ID: 466619 [Multi-domain] Cd Length: 92 Bit Score: 46.39 E-value: 3.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 71995032 584 ILDCVVLKLAENIEEIMTAVRYSLFYAQESPENIRKLVESSVKRLEEHYFIT 635
Cdd:pfam20470 41 LLEIIALGLATSPEDVDEYMSCTLLSVQQKELDVEKSIESSLEELVENGLIT 92
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
158-339 |
4.12e-06 |
|
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: 50.47 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 158 MYRKIKKLDKFYDWQQECL---SDKRLLDGENCILSLPTGAGKTLIAEVLMLREAI-VRKRNAILVLPYVAIvqekISAL 233
Cdd:COG1203 118 LPKKSKPRTPINPLQNEALelaLEAAEEEPGLFILTAPTGGGKTEAALLFALRLAAkHGGRRIIYALPFTSI----INQT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 234 AP-FEDAFGINI--------------EEYASNKGRFppIKRRKRV---SVYVATIEKanmLINSLITQ---------GQL 286
Cdd:COG1203 194 YDrLRDLFGEDVllhhsladldlleeEEEYESEARW--LKLLKELwdaPVVVTTIDQ---LFESLFSNrkgqerrlhNLA 268
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 71995032 287 DRVgmVVVDELHMIgDGGRGAILEQLLaKFLYKGTGQIVGMSATLPNIDDLKF 339
Cdd:COG1203 269 NSV--IILDEVQAY-PPYMLALLLRLL-EWLKNLGGSVILMTATLPPLLREEL 317
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
185-298 |
6.13e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 50.11 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 185 ENCILSLPTGAGKTLIAeVLMLREAIVRKRNAILVL-PYVAIVQEKisaLAPFEDAFGINIEEYASNKGRFPPIKRR--- 260
Cdd:COG1111 18 KNTLVVLPTGLGKTAVA-LLVIAERLHKKGGKVLFLaPTKPLVEQH---AEFFKEALNIPEDEIVVFTGEVSPEKRKelw 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 71995032 261 KRVSVYVAT---IEkaNMLINSLITqgqLDRVGMVVVDELH 298
Cdd:COG1111 94 EKARIIVATpqvIE--NDLIAGRID---LDDVSLLIFDEAH 129
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
395-539 |
7.39e-06 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 46.48 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 395 QLLAKLIPKNSAVI-FCPNKKNCENVAVLIAKTLPAHIRQAKRaesdaflqsylsdnddermdavlkqcilsgVAYHHSG 473
Cdd:cd18797 26 RLFADLVRAGVKTIvFCRSRKLAELLLRYLKARLVEEGPLASK------------------------------VASYRAG 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71995032 474 LTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLPVRRVIIkapMVGRErLGKAQYLQMAGRAGRAG 539
Cdd:cd18797 76 YLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVV---LAGYP-GSLASLWQQAGRAGRRG 137
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
172-332 |
1.42e-05 |
|
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: 46.67 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 172 QQECLsdKRLLDGENCILSLPTGAGKTL-----IAEVLMLREAIVRKRNAILVLpyV-----AI-VQEKISALAPFEDAF 240
Cdd:cd00268 17 QAQAI--PLILSGRDVIGQAQTGSGKTLafllpILEKLLPEPKKKGRGPQALVL--AptrelAMqIAEVARKLGKGTGLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 241 ------GINIEEYASNKgrfppikrRKRVSVYVATIEKanmlINSLITQG--QLDRVGMVVVDELHMIGDGGRGAILEQL 312
Cdd:cd00268 93 vaaiygGAPIKKQIEAL--------KKGPDIVVGTPGR----LLDLIERGklDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180
....*....|....*....|
gi 71995032 313 LAKFLYKgtGQIVGMSATLP 332
Cdd:cd00268 161 LSALPKD--RQTLLFSATLP 178
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
185-330 |
1.89e-05 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 46.16 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 185 ENCILSLPTGAGKTLIAEVLMLReaIVR---KRNAILVLPYVAIVQEKISAlapFEDAFGINIEEYASNKGRFPPIKRR- 260
Cdd:cd18033 17 QNTLVALPTGLGKTFIAAVVMLN--YYRwfpKGKIVFMAPTKPLVSQQIEA---CYKITGIPSSQTAELTGSVPPTKRAe 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71995032 261 ----KRvsVYVATIEkanmLINSLITQGQLD--RVGMVVVDELHMigdgGRGAILEQLLAKFLYKGTGQ--IVGMSAT 330
Cdd:cd18033 92 lwasKR--VFFLTPQ----TLENDLKEGDCDpkSIVCLVIDEAHR----ATGNYAYCQVVRELMRYNSHfrILALTAT 159
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
185-329 |
4.48e-05 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 45.34 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 185 ENCILSLPTGAGKTLIAeVLMLREAIVR-------KRNAILVLPYVAIVQEKISALapfEDAFGINIEEYASNKG----- 252
Cdd:cd18034 17 RNTIVVLPTGSGKTLIA-VMLIKEMGELnrkeknpKKRAVFLVPTVPLVAQQAEAI---RSHTDLKVGEYSGEMGvdkwt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 253 --RFPPIKRRKRVSVYVATIEKaNMLINSLITqgqLDRVGMVVVDELHMigdggrgAILEQ---LLAKFLYKGTGQ---- 323
Cdd:cd18034 93 keRWKEELEKYDVLVMTAQILL-DALRHGFLS---LSDINLLIFDECHH-------ATGDHpyaRIMKEFYHLEGRtsrp 161
|
....*..
gi 71995032 324 -IVGMSA 329
Cdd:cd18034 162 rILGLTA 168
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
467-539 |
5.06e-05 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 44.64 E-value: 5.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995032 467 VAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLPVRRVIIkapMVGRERLGKAQYLQMAGRAGRAG 539
Cdd:cd18811 64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMV---IEDAERFGLSQLHQLRGRVGRGD 133
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
179-300 |
8.66e-05 |
|
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: 44.55 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 179 KRLLDGENCILSLPTGAGKTLIAEV--LMLREaivRKRNAILVL-PYVAIVQEKISALAPFEDAFGINIEEYASNKGRFP 255
Cdd:cd18018 22 ARLLSGRSTLVVLPTGAGKSLCYQLpaLLLRR---RGPGLTLVVsPLIALMKDQVDALPRAIKAAALNSSLTREERRRIL 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 71995032 256 PIKRRKRVSVYVATIEKanmLINS--LITQGQLDRVGMVVVDELHMI 300
Cdd:cd18018 99 EKLRAGEVKILYVSPER---LVNEsfRELLRQTPPISLLVVDEAHCI 142
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
186-298 |
9.12e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 46.41 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 186 NCILSLPTGAGKTLIAevLMLREAIVRKRNA-ILVL-PYVAIVQEKisaLAPFEDAFGINIEEYASNKGRFPPIKRRK-- 261
Cdd:PRK13766 31 NTLVVLPTGLGKTAIA--LLVIAERLHKKGGkVLILaPTKPLVEQH---AEFFRKFLNIPEEKIVVFTGEVSPEKRAElw 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 71995032 262 -RVSVYVAT---IEkaNMLINSLITqgqLDRVGMVVVDELH 298
Cdd:PRK13766 106 eKAKVIVATpqvIE--NDLIAGRIS---LEDVSLLIFDEAH 141
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
167-539 |
9.26e-05 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 46.24 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 167 KFYDWQQECLSDkrLLDGENCILSLPTGAGKTLIAEVlmlrEAIVRKRNAILVLPYVAIVQEKISALApfedAFGINIEE 246
Cdd:PRK11057 25 QFRPGQQEIIDA--VLSGRDCLVVMPTGGGKSLCYQI----PALVLDGLTLVVSPLISLMKDQVDQLL----ANGVAAAC 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 247 YASNKGR---FPPIKRRKRVSVYVATIEKANMLINSLITQGQLDRVGMVVVDELHMIGDGGRGAILEqllakflYKGTGQ 323
Cdd:PRK11057 95 LNSTQTReqqLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPE-------YAALGQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 324 IVGMSATLPNIddlkfALRAFVYSTnfrpveltefvkigqTMHQVSENGDLNPagdlPTNNLKSTD-PDGICQLLAKLIP 402
Cdd:PRK11057 168 LRQRFPTLPFM-----ALTATADDT---------------TRQDIVRLLGLND----PLIQISSFDrPNIRYTLVEKFKP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 403 ------------KNSAVIFCPNKKNCENVAvliAKTLPAHIRqakraesdaflqsylsdnddermdavlkqcilsgVAYH 470
Cdd:PRK11057 224 ldqlmryvqeqrGKSGIIYCNSRAKVEDTA---ARLQSRGIS----------------------------------AAAY 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71995032 471 HSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLP-VRRVI-------IKApmvgrerlgkaqYLQMAGRAGRAG 539
Cdd:PRK11057 267 HAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPnVRFVVhfdiprnIES------------YYQETGRAGRDG 331
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
492-548 |
1.07e-04 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350192 [Multi-domain] Cd Length: 135 Bit Score: 42.93 E-value: 1.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71995032 492 YVVCATSTLAAGVNLPVRRVI----IKAPMVGRERLGKAQYLQMAGRAGRAGFDTKGDCIT 548
Cdd:cd18805 72 DVLVASDAIGMGLNLNIRRVIfsslSKFDGNEMRPLSPSEVKQIAGRAGRFGSHFPEGEVT 132
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
172-539 |
1.89e-04 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 45.48 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 172 QQECLsdKRLLDGENCILSLPTGAGKTL------IAEvLMLREAIVRKRNAILVLpYvaivqekIS---ALA-------- 234
Cdd:COG1201 29 QREAW--PAIAAGESTLLIAPTGSGKTLaaflpaLDE-LARRPRPGELPDGLRVL-Y-------ISplkALAndiernlr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 235 -PFEDafginIEEYAsnKGRFPPIK----------------RRKRVSVYVATIEKANMLINSLITQGQLDRVGMVVVDEL 297
Cdd:COG1201 98 aPLEE-----IGEAA--GLPLPEIRvgvrtgdtpaserqrqRRRPPHILITTPESLALLLTSPDARELLRGVRTVIVDEI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 298 HMIGDGGRGAILEQLLAKF--LYKGTGQIVGMSATLPNIDDlkfALRAFVYSTNFRPVELTEfVKIGQTMHQVSEngdln 375
Cdd:COG1201 171 HALAGSKRGVHLALSLERLraLAPRPLQRIGLSATVGPLEE---VARFLVGYEDPRPVTIVD-AGAGKKPDLEVL----- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 376 pagdLPTNNLKSTDP------DGICQLLAKLIPKN-SAVIFCPNKKNCENVAvliaktlpAHIRQAkraesdaflqsyls 448
Cdd:COG1201 242 ----VPVEDLIERFPwaghlwPHLYPRVLDLIEAHrTTLVFTNTRSQAERLF--------QRLNEL-------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 449 dNDDermDAVLkqcilsgVAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNL-PVRRVI-IKAPmvgrerLGKA 526
Cdd:COG1201 296 -NPE---DALP-------IAAHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIgDVDLVIqVGSP------KSVA 358
|
410
....*....|...
gi 71995032 527 QYLQmagRAGRAG 539
Cdd:COG1201 359 RLLQ---RIGRAG 368
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
395-550 |
3.03e-04 |
|
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: 41.72 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 395 QLLAKLIPKNSAVIFCPNKKNCENVAVLiaktlpahirqakraesdaflqsylsdnddermdavLKQCILSGVAYHhSGL 474
Cdd:cd18787 19 LLLLEKLKPGKAIIFVNTKKRVDRLAEL------------------------------------LEELGIKVAALH-GDL 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71995032 475 TQDERKCVEAAFMEGLIYVVCATSTLAAGVNLP-VRRVI-IKAPMvgrerlGKAQYLQMAGRAGRAGfdTKGDCITII 550
Cdd:cd18787 62 SQEERERALKKFRSGKVRVLVATDVAARGLDIPgVDHVInYDLPR------DAEDYVHRIGRTGRAG--RKGTAITFV 131
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
179-332 |
6.08e-04 |
|
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: 42.35 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 179 KRLLDGENCILSLPTGAGKTL------IAEVLMLREAIVRKRNAILVL---PYVAIVQEKISALAPFEDAFGINIEEYAS 249
Cdd:cd17948 22 PSILRGRNTLCAAETGSGKTLtyllpiIQRLLRYKLLAEGPFNAPRGLvitPSRELAEQIGSVAQSLTEGLGLKVKVITG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 250 NKGRFPPIK-RRKRVSVYVATIEKANMLINSLITqgQLDRVGMVVVDELHMIGDGGRGAILEQLLAKF------------ 316
Cdd:cd17948 102 GRTKRQIRNpHFEEVDILVATPGALSKLLTSRIY--SLEQLRHLVLDEADTLLDDSFNEKLSHFLRRFplasrrsentdg 179
|
170
....*....|....*.
gi 71995032 317 LYKGTgQIVGMSATLP 332
Cdd:cd17948 180 LDPGT-QLVLVSATMP 194
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
164-298 |
1.18e-03 |
|
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: 41.20 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 164 KLDKFYDWQQECLSdkRLLDGENCILSLPTGAGKTLIAEVlmlrEAIVRKRNAILVLPYVAIVQEKISALapfeDAFGIN 243
Cdd:cd18015 15 KLEKFRPLQLETIN--ATMAGRDVFLVMPTGGGKSLCYQL----PALCSDGFTLVVSPLISLMEDQLMAL----KKLGIS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71995032 244 IEEYASNKGRfPPIKR-----RKRVS----VYVA--TIEKANMLINSLITQGQLDRVGMVVVDELH 298
Cdd:cd18015 85 ATMLNASSSK-EHVKWvhaalTDKNSelklLYVTpeKIAKSKRFMSKLEKAYNAGRLARIAIDEVH 149
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
181-298 |
2.52e-03 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a 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: 350687 [Multi-domain] Cd Length: 178 Bit Score: 39.88 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 181 LLDGencilslPTGAGKTliaEVLM--LREAIVRKRNAILVLPYVAivqekisaLAP-----FEDAFGINIEEYASNKGR 253
Cdd:cd17929 19 LLHG-------VTGSGKT---EVYIelIEKVLAKGKQVLVLVPEIS--------LTPqlikrFKKRFGDKVAVLHSKLSD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 71995032 254 fppiKRRKRvSVYVATIEKANMLI---NSLITQgqLDRVGMVVVDELH 298
Cdd:cd17929 81 ----KERAD-EWRKIKRGEAKVVIgarSALFAP--FKNLGLIIVDEEH 121
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
493-550 |
3.61e-03 |
|
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: 37.30 E-value: 3.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 71995032 493 VVCATSTLAAGVNLP-VRRVIIkapmVGRERlGKAQYLQMAGRAGRAGfDTKGDCITII 550
Cdd:cd18785 25 ILVATNVLGEGIDVPsLDTVIF----FDPPS-SAASYIQRVGRAGRGG-KDEGEVILFV 77
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
180-298 |
4.32e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 39.03 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 180 RLLDGeNCILSLPTGAGKTLIAevLMLREAIVRKRNA-ILVL-PYVAIVQEKISALAPFedafgINIEE-YASNKGRFPP 256
Cdd:cd18035 13 VALNG-NTLIVLPTGLGKTIIA--ILVAADRLTKKGGkVLILaPSRPLVEQHAENLKRV-----LNIPDkITSLTGEVKP 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 71995032 257 IKRRK---RVSVYVAT---IEkaNMLINSLITqgqLDRVGMVVVDELH 298
Cdd:cd18035 85 EERAErwdASKIIVATpqvIE--NDLLAGRIT---LDDVSLLIFDEAH 127
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
188-333 |
4.73e-03 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 40.11 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 188 ILSLPTGAGKTLIAEVLMLREAIVRKRN-AILVLPYVAIVQEKI-SALAPFEDAFGI-------NIEEYASN---KGRFP 255
Cdd:cd09639 3 VIEAPTGYGKTEAALLWALHSLKSQKADrVIIALPTRATINAMYrRAKEAFGETGLYhssilssRIKEMGDSeefEHLFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 256 -PIKRRKRVSVYVATIEKANMLINSL--------ITQGQLDRvGMVVVDELHMIGDGGRGAILEQLlaKFLYKGTGQIVG 326
Cdd:cd09639 83 lYIHSNDTLFLDPITVCTIDQVLKSVfgefghyeFTLASIAN-SLLIFDEVHFYDEYTLALILAVL--EVLKDNDVPILL 159
|
....*..
gi 71995032 327 MSATLPN 333
Cdd:cd09639 160 MSATLPK 166
|
|
| DEXHc_RLR-2 |
cd18074 |
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma ... |
170-298 |
6.29e-03 |
|
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma differentiation-associated protein 5 or Mda5 and IFIH1) is a viral double-stranded RNA (dsRNA) receptor that shares sequence similarity and signaling pathways with RIG-I, yet plays essential functions in antiviral immunity through distinct specificity for viral RNA. RLR-2 recognizes the internal duplex structure, whereas RIG-I recognizes the terminus of dsRNA. RLR-2 uses direct protein-protein contacts to stack along dsRNA in a head-to-tail arrangement. The signaling domain (tandem CARD), which decorates the outside of the core RLR-2 filament, also has an intrinsic propensity to oligomerize into an elongated structure that activates the signaling adaptor, MAVS. RLR-2 uses long dsRNA as a signaling platform to cooperatively assemble the core filament, which in turn promotes stochastic assembly of the tandem CARD oligomers for signaling. LGP2 appears to positively and negatively regulate RLR-2 and RIG-I signaling, respectively. RLR-2 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: 350832 [Multi-domain] Cd Length: 216 Bit Score: 39.07 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995032 170 DWQQECLsdKRLLDGENCILSLPTGAGKTLIAeVLMLREAIVRKRNA------ILVLPYVAIVQEKISA-LAPF-EDAFG 241
Cdd:cd18074 5 DYQMEVA--KPALEGKNIIICLPTGSGKTRVA-VYITKDHLDKKRKAsepgkvIVLVNKVPLVEQHYRKeFNPFlKHWYQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71995032 242 -INIEEYASNKGRFPPIKRRKRVSVYVATIEKaNMLINSLITQG---QLDRVGMVVVDELH 298
Cdd:cd18074 82 vIGLSGDSQLKISFPEVVKRYDVIICTAQILE-NSLLNATEEEDegvQLSDFSLIIIDECH 141
|
|
| |
