|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
39-203 |
3.18e-82 |
|
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: 258.67 E-value: 3.18e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 39 DNVLLAASTASGKTEAAFFPILTDLYENPSSSVGVLYISPLKALINDQYERLTDLCQ--DVDIPIWRWHGEVAQTQKRKL 116
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDeiDLEIPVAVRHGDTSQSEKAKQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 117 LKHPSGILQITPESLESLMINKHMDipNLFHDLRYVVIDELHSFLRSDRGGQTFCLIERLSKMAGVDPRRIGLSATIGDT 196
Cdd:cd17922 82 LKNPPGILITTPESLELLLVNKKLR--ELFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKLTGRPLRRIGLSATLGNL 159
|
....*..
gi 1706369249 197 ESAARFL 203
Cdd:cd17922 160 EEAAAFL 166
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
2-571 |
2.21e-75 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 260.42 E-value: 2.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 2 DIFTRFAPFIQDYiYEHNWKNLRSIQVGAAETIfNSQDNVLLAASTASGKTEAAFFPILTDLYENPSSS-----VGVLYI 76
Cdd:COG1201 5 DVLSLLHPAVRAW-FAARFGAPTPPQREAWPAI-AAGESTLLIAPTGSGKTLAAFLPALDELARRPRPGelpdgLRVLYI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 77 SPLKALINDQYERLT------DLCQDVDIPIWRW---HGEVAQTQKRKLLKHPSGILQITPESLeSLMINkHMDIPNLFH 147
Cdd:COG1201 83 SPLKALANDIERNLRapleeiGEAAGLPLPEIRVgvrTGDTPASERQRQRRRPPHILITTPESL-ALLLT-SPDARELLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 148 DLRYVVIDELHSFLRSDRGGQTFCLIERLSKMAGVDPRRIGLSATIGDTESAARFL-GAGSKRRTTVPKTeSGGQVWRLS 226
Cdd:COG1201 161 GVRTVIVDEIHALAGSKRGVHLALSLERLRALAPRPLQRIGLSATVGPLEEVARFLvGYEDPRPVTIVDA-GAGKKPDLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 227 MEHfydngPQADSSGFAPAQPVLdeksdqAPQMADPSMAYIFEHtrgKKCLVFTNSREECEAVCQILRqycEINHEPDRF 306
Cdd:COG1201 240 VLV-----PVEDLIERFPWAGHL------WPHLYPRVLDLIEAH---RTTLVFTNTRSQAERLFQRLN---ELNPEDALP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 307 L-IHHGNLSAAYRQTAEAEMKNEDsLMTTCATATLELGIDIGKLERAFQVDAPFTVSGFLQRMGRTG-RRGNPAEMWFVm 384
Cdd:COG1201 303 IaAHHGSLSREQRLEVEEALKAGE-LRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEVSKGRLV- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 385 reshPESRAmlpEiipwsLLQGIALVQLyLEEKWVEPPEPNRLPYSLLYHQTMsTLASSGEMTPAELASRVLTLHYFHNV 464
Cdd:COG1201 381 ----PTHRD---E-----LVECAAALEA-ARAGEIEARRPPRNPLDVLAQHIV-AMAAGGPFDVDELYAEVRRAYPYRDL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 465 SQNDYRVLLRYL--------IKED--HIQQTENGGLIIGLTGERVInnfkfyAVFQ-----ENEEYSVK--SDSEELGTI 527
Cdd:COG1201 447 TREDFDAVLDFLagggpslrAYERyaRIVRDRVDGRLGARRGAARL------ARTNigtipDRGMLKVRlvRGGRRLGEL 520
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1706369249 528 -------VKPppvGDKIAIAGRVWVVEDVdrKRHQVYCYPVKG---RIPAYFGD 571
Cdd:COG1201 521 eeefveeLRP---GDVFVLGGRSLRIERI--RGMRVYVRPAPGkppTVPSWFGE 569
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
16-586 |
2.21e-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: 203.14 E-value: 2.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 16 YEHnwknlrsiQVGAAETIFNSQdNVLLAASTASGKTEAAFFPILTDLYENPSSSvgVLYISPLKALINDQYERLTDLCQ 95
Cdd:COG1205 58 YSH--------QAEAIEAARAGK-NVVIATPTASGKSLAYLLPVLEALLEDPGAT--ALYLYPTKALARDQLRRLRELAE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 96 --DVDIPIWRWHGEVAQTQKRKLLKHPSgILQITPESLESLMINKHMDIPNLFHDLRYVVIDELHSFlrsdRG------G 167
Cdd:COG1205 127 alGLGVRVATYDGDTPPEERRWIREHPD-IVLTNPDMLHYGLLPHHTRWARFFRNLRYVVIDEAHTY----RGvfgshvA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 168 QtfcLIERLSKMA---GVDPRRIGLSATIGD-TESAARFLGagskrrttvpktesggqvwrLSMEHFYDNG-PQADSSgF 242
Cdd:COG1205 202 N---VLRRLRRICrhyGSDPQFILASATIGNpAEHAERLTG--------------------RPVTVVDEDGsPRGERT-F 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 243 APAQPVLDEKSDQAPQMADpsMAYIFEH--TRGKKCLVFTNSREECEAVCQILRQYCEINHEPDRFLIHHGNLSAAYRQT 320
Cdd:COG1205 258 VLWNPPLVDDGIRRSALAE--AARLLADlvREGLRTLVFTRSRRGAELLARYARRALREPDLADRVAAYRAGYLPEERRE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 321 AEAEMKnEDSLMTTCATATLELGIDIGKLERAFQVDAPFTVSGFLQRMGRTGRRGNPAEMWFVMRES--------HPEsr 392
Cdd:COG1205 336 IERGLR-SGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVAGDDpldqyyvrHPE-- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 393 amlpeiipwsllqgialvqLYLEekwvEPPEPNRL----PYSLLYHqtmsTLASSGEM--TPAELAsrvltlhYFhnvsQ 466
Cdd:COG1205 413 -------------------ELFE----RPPEAAVIdpdnPYVLAPH----LLCAAAELplTEGDLE-------LF----G 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 467 NDYRVLLRYLIKEDHIQQTENGGLIIGltGERVINNFKFYAVFQENeeYSV--KSDSEELGTIVKP-------PpvGdki 537
Cdd:COG1205 455 PEARELLDALVEEGLLRRRGDGWYWTG--DDRPARDVSLRGAGGEN--VVIvdATTGRVIGTVDLPralrelhP--G--- 525
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1706369249 538 AI---AGRVWVVEDVDRKRHQVYCYPVKgriPAYFGDVAGDIQPKILQRMRK 586
Cdd:COG1205 526 AIylhQGETYRVEELDLEERKAYVRPVD---VDYYTRALSETDIRILEVLEE 574
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
247-386 |
6.66e-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: 168.98 E-value: 6.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 247 PVLDEKSDQAPQMADPSMA-YIFEHTRGKKCLVFTNSREECEAVCQILRQYCEINHEPDRFLIHHGNLSAAYRQTAEAEM 325
Cdd:cd18796 11 PVAPEIFPWAGESGADAYAeVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRVPPDFIALHHGSLSRELREEVEAAL 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1706369249 326 KnEDSLMTTCATATLELGIDIGKLERAFQVDAPFTVSGFLQRMGRTGRRGNPAEMWFVMRE 386
Cdd:cd18796 91 K-RGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLVPT 150
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
2-374 |
1.40e-39 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 156.97 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 2 DIFTRFAPFIQDYIYEhNWKNLRSIQVGAAETIFNSQdNVLLAASTASGKTEAAFFPILTDLY--------ENpssSVGV 73
Cdd:PRK13767 13 EILDLLRPYVREWFKE-KFGTFTPPQRYAIPLIHEGK-NVLISSPTGSGKTLAAFLAIIDELFrlgregelED---KVYC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 74 LYISPLKALINDQY----ERLTDLCQ-----DVDIPIWRW---HGEVAQTQKRKLLKHPSGILQITPESL---------- 131
Cdd:PRK13767 88 LYVSPLRALNNDIHrnleEPLTEIREiakerGEELPEIRVairTGDTSSYEKQKMLKKPPHILITTPESLaillnspkfr 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 132 ESLminkhmdipnlfHDLRYVVIDELHSFLRSDRGGQTFCLIERLSKMAGVDPRRIGLSATIGDTESAARFLGAgskrrt 211
Cdd:PRK13767 168 EKL------------RTVKWVIVDEIHSLAENKRGVHLSLSLERLEELAGGEFVRIGLSATIEPLEEVAKFLVG------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 212 tvpktesggqvwrlsmehFYDNGPQAD----SSGFAPA------QPVLD------EKSDQA--PQMADpsmaYIFEHtrg 273
Cdd:PRK13767 230 ------------------YEDDGEPRDceivDARFVKPfdikviSPVDDlihtpaEEISEAlyETLHE----LIKEH--- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 274 KKCLVFTNSREECEAVCQILRQYCEINHEPDRFLIHHGNLSAAYRQTAEAEMKNEDSLMTTCATaTLELGIDIGKLERAF 353
Cdd:PRK13767 285 RTTLIFTNTRSGAERVLYNLRKRFPEEYDEDNIGAHHSSLSREVRLEVEEKLKRGELKVVVSST-SLELGIDIGYIDLVV 363
|
410 420
....*....|....*....|.
gi 1706369249 354 QVDAPFTVSGFLQRMGRTGRR 374
Cdd:PRK13767 364 LLGSPKSVSRLLQRIGRAGHR 384
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
23-194 |
3.68e-31 |
|
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: 120.00 E-value: 3.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 23 LRSIQVGAAETIfNSQDNVLLAASTASGKTEAAFFPILTDLYENPSSSVgvLYISPLKALINDQYERLTDLCQDV--DIP 100
Cdd:cd17923 1 LYSHQAEAIEAA-RAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRA--LYLYPTKALAQDQLRSLRELLEQLglGIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 101 IWRWHGEVAQTQKRKLLKHPSGILQITPESLESLMINKHMDIPNLFHDLRYVVIDELHSFlrsdRGGQ---TFCLIERLS 177
Cdd:cd17923 78 VATYDGDTPREERRAIIRNPPRILLTNPDMLHYALLPHHDRWARFLRNLRYVVLDEAHTY----RGVFgshVALLLRRLR 153
|
170 180
....*....|....*....|
gi 1706369249 178 ---KMAGVDPRRIGLSATIG 194
Cdd:cd17923 154 rlcRRYGADPQFILTSATIG 173
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
45-571 |
3.54e-30 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 128.12 E-value: 3.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 45 ASTASGKTEAAFFPILTDLYE---------NPSSSVGVLYISPLKAL--------------INDQYERLTDLcqDVDIPI 101
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFReggedtreaHKRKTSRILYISPIKALgtdvqrnlqiplkgIADERRRRGET--EVNLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 102 WRWHGEVAQTQKRKLLKHPSGILQITPESLESLMINKHMDIpnlFHDLRYVVIDELHSFLRSDRGGQTFCLIERLSKMAG 181
Cdd:PRK09751 81 GIRTGDTPAQERSKLTRNPPDILITTPESLYLMLTSRARET---LRGVETVIIDEVHAVAGSKRGAHLALSLERLDALLH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 182 VDPRRIGLSATIGDTESAARFLGaGSKRRTTVPKTESGGQVWRLSMehfydngPQADSSGFA--PAQPVLDEKSDQAPQM 259
Cdd:PRK09751 158 TSAQRIGLSATVRSASDVAAFLG-GDRPVTVVNPPAMRHPQIRIVV-------PVANMDDVSsvASGTGEDSHAGREGSI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 260 ADPSMAYIFEHT-RGKKCLVFTNSREECEAVCQILRQ-YCE-INHEP-----------------------DRFLI--HHG 311
Cdd:PRK09751 230 WPYIETGILDEVlRHRSTIVFTNSRGLAEKLTARLNElYAArLQRSPsiavdaahfestsgatsnrvqssDVFIArsHHG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 312 NLSAAYRQTAEAEMKNEDsLMTTCATATLELGIDIGKLERAFQVDAPFTVSGFLQRMGRTGRRGNPAEMWFVmresHPES 391
Cdd:PRK09751 310 SVSKEQRAITEQALKSGE-LRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVGGVSKGLF----FPRT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 392 RAmlpeiipwSLLQGIALVQLYLEEKwVEPPEPNRLPYSLLYHQTMSTLAssgeMTPAELA---SRVLTLHYFHNVSQND 468
Cdd:PRK09751 385 RR--------DLVDSAVIVECMFAGR-LENLTPPHNPLDVLAQQTVAAAA----MDALQVDewySRVRRAAPWKDLPRRV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 469 YRVLL-----RY-----------LI--KEDHIQQTENGGLIIGLT-GERVINNFKFYAVFQENEEysvKSDSEELGTI-- 527
Cdd:PRK09751 452 FDATLdmlsgRYpsgdfsafrpkLVwnRETGILTARPGAQLLAVTsGGTIPDRGMYSVLLPEGEE---QAGSRRVGELde 528
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1706369249 528 --VKPPPVGDKIAIAGRVWVVEDVDRKrhQVYCYPVKG---RIPAYFGD 571
Cdd:PRK09751 529 emVYESRVNDIITLGATSWRIQQITRD--QVIVTPAPGrsaRLPFWRGE 575
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
24-196 |
7.23e-30 |
|
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: 115.80 E-value: 7.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 24 RSIQVGAAETIFNSQDnVLLAASTASGKTEAAFFPILTDLYENPSSSVgVLYISPLKALINDQYERLTDLCQDVDIPIWR 103
Cdd:pfam00270 1 TPIQAEAIPAILEGRD-VLVQAPTGSGKTLAFLLPALEALDKLDNGPQ-ALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 104 WHGEVAQTQKRKLLKHPSgILQITPESLESLMINKhmdipNLFHDLRYVVIDELHSFLRSDRGGQtfclIERLSKMAGVD 183
Cdd:pfam00270 79 LLGGDSRKEQLEKLKGPD-ILVGTPGRLLDLLQER-----KLLKNLKLLVLDEAHRLLDMGFGPD----LEEILRRLPKK 148
|
170
....*....|...
gi 1706369249 184 PRRIGLSATIGDT 196
Cdd:pfam00270 149 RQILLLSATLPRN 161
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
15-195 |
1.92e-29 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 116.05 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 15 IYEHNWKNLRSIQVGAAETIFNSQDNVLLAASTASGKTEAAFFPILTDLYENPSSSVgvLYISPLKALINDQYERLTDLC 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV--LVLVPTRELAEQWAEELKKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 95 QDVDI-PIWRWHGEVAQTQKRKLLKHPSGILQITPESLESLMINKHMDipnlFHDLRYVVIDELHSFLRSDRGGQTFCLI 173
Cdd:smart00487 79 PSLGLkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLS----LSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180
....*....|....*....|..
gi 1706369249 174 ERLSKmagvDPRRIGLSATIGD 195
Cdd:smart00487 155 KLLPK----NVQLLLLSATPPE 172
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
27-502 |
5.60e-29 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 121.93 E-value: 5.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 27 QVGAAETIFNSQDNVLLAASTASGKTEAAFFPILTDLYENPSssvgVLYISPLKALINDQYERLTDLCQDVDIPI----- 101
Cdd:COG1204 27 QAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK----ALYIVPLRALASEKYREFKRDFEELGIKVgvstg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 102 -WRWHGEVAQTqkrkllkhpSGILQITPESLESLMINKhmdiPNLFHDLRYVVIDELHSFLRSDRGGQTFCLIERLsKMA 180
Cdd:COG1204 103 dYDSDDEWLGR---------YDILVATPEKLDSLLRNG----PSWLRDVDLVVVDEAHLIDDESRGPTLEVLLARL-RRL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 181 GVDPRRIGLSATIGDTESAARFLGA---GSKRRtTVPKTE---SGGQVwrlsmeHFYDNGPQADSSGFAPAQPVLDEksd 254
Cdd:COG1204 169 NPEAQIVALSATIGNAEEIAEWLDAelvKSDWR-PVPLNEgvlYDGVL------RFDDGSRRSKDPTLALALDLLEE--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 255 qapqmadpsmayifehtrGKKCLVFTNSREECEAVCQILRQYCEINH----------------------EPDRFLI---- 308
Cdd:COG1204 239 ------------------GGQVLVFVSSRRDAESLAKKLADELKRRLtpeereeleelaeellevseetHTNEKLAdcle 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 309 -----HHGNLSAAYRQTAEAEMKNEDsLMTTCATATLELGID-------IGKLERAFQVdaPFTVSGFLQRMGRTGRRG- 375
Cdd:COG1204 301 kgvafHHAGLPSELRRLVEDAFREGL-IKVLVATPTLAAGVNlparrviIRDTKRGGMV--PIPVLEFKQMAGRAGRPGy 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 376 NPAEMWFVMRESHPESRamlpeiipwsllqgiALVQLYLEEKwVEPPEPNRLPYSLLYHQTMSTLASSGEMTPAELASRV 455
Cdd:COG1204 378 DPYGEAILVAKSSDEAD---------------ELFERYILGE-PEPIRSKLANESALRTHLLALIASGFANSREELLDFL 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1706369249 456 LTLHYFHNVSQNDYRVL----LRYLIKEDHIQQtENGGLIIGLTGERVINN 502
Cdd:COG1204 442 ENTFYAYQYDKGDLEEVvddaLEFLLENGFIEE-DGDRLRATKLGKLVSRL 491
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
26-204 |
1.69e-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: 92.32 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 26 IQVGAAETIFNSQDNVLLAASTASGKTEAAFFPILTDLYENPSSsvgVLYISPLKALINDQYERLTDLCQDVDIPIWRWH 105
Cdd:cd17921 5 IQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK---AVYIAPTRALVNQKEADLRERFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 106 GEVaQTQKRKLLKhpSGILQITPESLESLMINKHMDipnLFHDLRYVVIDELHSFLRSDRGGQTFCLIERLSKMAGvDPR 185
Cdd:cd17921 82 GDP-SVNKLLLAE--ADILVATPEKLDLLLRNGGER---LIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRINK-NAR 154
|
170
....*....|....*....
gi 1706369249 186 RIGLSATIGDTESAARFLG 204
Cdd:cd17921 155 FVGLSATLPNAEDLAEWLG 173
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
246-378 |
4.43e-18 |
|
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: 81.53 E-value: 4.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 246 QPVLDEKSDQAPQMADPSMAYIFEH--TRGKKCLVFTNSREECEAVCQILRQ-YCEINHEPDRFLIHHGNLSAAYRQTAE 322
Cdd:cd18797 6 NPPLLDRKDGERGSARREAARLFADlvRAGVKTIVFCRSRKLAELLLRYLKArLVEEGPLASKVASYRAGYLAEDRREIE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1706369249 323 AEMKNEDsLMTTCATATLELGIDIGKLERAFQVDAPFTVSGFLQRMGRTGRRGNPA 378
Cdd:cd18797 86 AELFNGE-LLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDS 140
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
40-192 |
5.41e-18 |
|
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: 81.30 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 40 NVLLAASTASGKTEAAFFPILTDLYENPSssvGVLYISPLKALINDQYERLTDLcQDVDIPIWRWHGEVAQTQKRKLLKH 119
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKGK---KVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSSAEEREKNKLG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706369249 120 PSGILQITPESLESLMINKHMDipnLFHDLRYVVIDELHSFLRSDRGGQTFCLIERLSKMAgvDPRRIGLSAT 192
Cdd:cd00046 79 DADIIIATPDMLLNLLLREDRL---FLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLK--NAQVILLSAT 146
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
27-205 |
2.64e-17 |
|
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: 80.07 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 27 QVGAAETIFNSQDNVLLAASTASGKTEAAFFPILTDLYENPSSsvgvLYISPLKALINDQYERLTDlcqdvdipiWRWHG 106
Cdd:cd18028 6 QAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGKA----LYLVPLRALASEKYEEFKK---------LEEIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 107 -EVA------QTQKRKLLKHPsgILQITPESLESLMINKhmdiPNLFHDLRYVVIDELHSFLRSDRGGQTFCLIERLSKM 179
Cdd:cd18028 73 lKVGistgdyDEDDEWLGDYD--IIVATYEKFDSLLRHS----PSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRRL 146
|
170 180
....*....|....*....|....*.
gi 1706369249 180 AGvDPRRIGLSATIGDTESAARFLGA 205
Cdd:cd18028 147 NP-NTQIIGLSATIGNPDELAEWLNA 171
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
22-206 |
1.50e-14 |
|
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: 73.16 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 22 NLRSIQVGAAETIFNSQDNVLLAASTASGKT---EAAFFPILTDLYENPSSSVGVLYISPLKALINDQYERLTDLCQDVD 98
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTvlfELAILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 99 IPIWRWHGEVAQTQKRKlLKHPSGILQiTPESLESlMINKHMDIPNLFHDLRYVVIDELHsFLRSDRGGQTFCLIERLSK 178
Cdd:cd18023 81 LSCAELTGDTEMDDTFE-IQDADIILT-TPEKWDS-MTRRWRDNGNLVQLVALVLIDEVH-IIKENRGATLEVVVSRMKT 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1706369249 179 M--------AGVDPRRIG-LSATIGDTESAARFLGAG 206
Cdd:cd18023 157 LsssselrgSTVRPMRFVaVSATIPNIEDLAEWLGDN 193
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
266-375 |
1.81e-14 |
|
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: 69.93 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 266 YIFEHTRGKKCLVFTNSREECEavCQILRQyceinHEPDRFLIHHGNLSAAYRQTAEAEMKNEDS--LMttcATATLELG 343
Cdd:pfam00271 8 ELLKKERGGKVLIFSQTKKTLE--AELLLE-----KEGIKVARLHGDLSQEEREEILEDFRKGKIdvLV---ATDVAERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 1706369249 344 IDIGKLERAFQVDAPFTVSGFLQRMGRTGRRG 375
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
19-203 |
8.34e-14 |
|
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: 71.25 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 19 NWKNLRSIQVGAAETIFNSQDNVLLAASTASGKTEAAFFPILTDL--YENPSSSVG-----VLYISPLKALINDQYERLT 91
Cdd:cd18019 14 GFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIgkHRNPDGTINldafkIVYIAPMKALVQEMVGNFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 92 DLCQDVDIPIWRWHGEvAQTQKRKLlkHPSGILQITPESLEsLMINKHMDIP--NLfhdLRYVVIDELHsFLRSDRGGQT 169
Cdd:cd18019 94 KRLAPYGITVAELTGD-QQLTKEQI--SETQIIVTTPEKWD-IITRKSGDRTytQL---VRLIIIDEIH-LLHDDRGPVL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1706369249 170 FCLIERL---SKMAGVDPRRIGLSATIGDTESAARFL 203
Cdd:cd18019 166 ESIVARTirqIEQTQEYVRLVGLSATLPNYEDVATFL 202
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
23-205 |
4.33e-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: 65.91 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 23 LRSIQVGAAETIFNSQDNVLLAASTASGKTEAAFFPILTDLYENPSS-------SVGVLYISPLKALINDQYERLTDLCQ 95
Cdd:cd18020 2 LNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQggvikkdDFKIVYIAPMKALAAEMVEKFSKRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 96 DVDIPIWRWHGEVaQTQKRKLLKhpSGILQITPESLEsLMINKHMDIPNLFHDLRYVVIDELHsFLRSDRGGQTFCLI-- 173
Cdd:cd18020 82 PLGIKVKELTGDM-QLTKKEIAE--TQIIVTTPEKWD-VVTRKSSGDVALSQLVRLLIIDEVH-LLHDDRGPVIESLVar 156
|
170 180 190
....*....|....*....|....*....|...
gi 1706369249 174 -ERLSKMAGVDPRRIGLSATIGDTESAARFLGA 205
Cdd:cd18020 157 tLRQVESTQSMIRIVGLSATLPNYLDVADFLRV 189
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
264-376 |
9.56e-12 |
|
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: 62.91 E-value: 9.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 264 MAYIFEHTRGKKCLVFTNSREECEAVCQILRQyCEINHepdrFLIHhGNLSAAYRQTAEAEMKNEDS--LMTTcatatlE 341
Cdd:cd18787 18 LLLLLEKLKPGKAIIFVNTKKRVDRLAELLEE-LGIKV----AALH-GDLSQEERERALKKFRSGKVrvLVAT------D 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 1706369249 342 L---GIDIGKLERAFQVDAPFTVSGFLQRMGRTGRRGN 376
Cdd:cd18787 86 VaarGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGR 123
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
26-204 |
2.10e-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: 63.55 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 26 IQVGAAETIFNSQDNVLLAASTASGKTEAAFFPILTDLYENPSSSvgVLYISPLKALINdqyERLTDlcqdvdipiwrWH 105
Cdd:cd18022 5 IQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSK--VVYIAPLKALVR---ERVDD-----------WK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 106 GEVAQTQKRKLLK------------HPSGILQITPESLESlmINKHMDIPNLFHDLRYVVIDELHsFLRSDRGGQTFCLI 173
Cdd:cd18022 69 KRFEEKLGKKVVEltgdvtpdmkalADADIIITTPEKWDG--ISRSWQTREYVQQVSLIIIDEIH-LLGSDRGPVLEVIV 145
|
170 180 190
....*....|....*....|....*....|....
gi 1706369249 174 ER---LSKMAGVDPRRIGLSATIGDTESAARFLG 204
Cdd:cd18022 146 SRmnyISSQTEKPVRLVGLSTALANAGDLANWLG 179
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
23-370 |
7.90e-11 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 65.43 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 23 LRSIQVGAAETIF----NSQDNVLLAASTASGKTEAAFFpILTDLYENPSssvgVLYISPLKALINDQYERLTdlcqdvd 98
Cdd:COG1061 81 LRPYQQEALEALLaaleRGGGRGLVVAPTGTGKTVLALA-LAAELLRGKR----VLVLVPRRELLEQWAEELR------- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 99 ipiwRWHGEVAQTQKRKllkHPSGILQITpeSLESLMINKHMDipNLFHDLRYVVIDELH-----SFLRsdrggqtfcLI 173
Cdd:COG1061 149 ----RFLGDPLAGGGKK---DSDAPITVA--TYQSLARRAHLD--ELGDRFGLVIIDEAHhagapSYRR---------IL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 174 ERLSkmagvDPRRIGLSATI--GDTESAARFLGAGSKRRTTVPKTESGGqvwRLSMEHFY--DNGPQADSSGFAPAQPVL 249
Cdd:COG1061 209 EAFP-----AAYRLGLTATPfrSDGREILLFLFDGIVYEYSLKEAIEDG---YLAPPEYYgiRVDLTDERAEYDALSERL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 250 DEKSDQAPQMADPSM-AYIFEHTRGKKCLVFTNSREECEAVCQILRqycEINHEPDRFlihHGNLSAAYRQTAEAEMKN- 327
Cdd:COG1061 281 REALAADAERKDKILrELLREHPDDRKTLVFCSSVDHAEALAELLN---EAGIRAAVV---TGDTPKKEREEILEAFRDg 354
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1706369249 328 EDSLMTTCATATlElGIDIGKLERAFQVDAPFTVSGFLQRMGR 370
Cdd:COG1061 355 ELRILVTVDVLN-E-GVDVPRLDVAILLRPTGSPREFIQRLGR 395
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
296-375 |
1.11e-10 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 58.38 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 296 YCEINHEPDRFLIHHGNLSAAYRQTAEAEMKNEDSLMTtCATATLELGIDIGKLERAFQVDAPFTVSGFLQRMGRTGRRG 375
Cdd:smart00490 4 AELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVL-VATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
15-346 |
2.69e-10 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 63.75 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 15 IYEHNWKNLRSIQVGAAETIFNSQdNVLLAASTASGKTEAAFFPIltdlYENPSSSVGVLYISPLKALINDQYE---RLT 91
Cdd:PRK01172 15 LFTGNDFELYDHQRMAIEQLRKGE-NVIVSVPTAAGKTLIAYSAI----YETFLAGLKSIYIVPLRSLAMEKYEelsRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 92 DLCQDVDIPIwrwhGEVAQTQkrKLLKHPSGILqITPESLESLMinkHMDiPNLFHDLRYVVIDELHSFLRSDRgGQTFC 171
Cdd:PRK01172 90 SLGMRVKISI----GDYDDPP--DFIKRYDVVI-LTSEKADSLI---HHD-PYIINDVGLIVADEIHIIGDEDR-GPTLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 172 LIERLSKMAGVDPRRIGLSATIGDTESAARFLGAGSKRRTTVPKTESGGQVWRLSMehFYDNGPQADSSGFAPAQPVLDE 251
Cdd:PRK01172 158 TVLSSARYVNPDARILALSATVSNANELAQWLNASLIKSNFRPVPLKLGILYRKRL--ILDGYERSQVDINSLIKETVND 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 252 ksdqapqmadpsmayifehtrGKKCLVFTNSREECEAVCQILRQY-----------CEINHEPDRFL--------IHHGN 312
Cdd:PRK01172 236 ---------------------GGQVLVFVSSRKNAEDYAEMLIQHfpefndfkvssENNNVYDDSLNemlphgvaFHHAG 294
|
330 340 350
....*....|....*....|....*....|....
gi 1706369249 313 LSAAYRQTAEAEMKNEdSLMTTCATATLELGIDI 346
Cdd:PRK01172 295 LSNEQRRFIEEMFRNR-YIKVIVATPTLAAGVNL 327
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
40-205 |
1.59e-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: 58.38 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 40 NVLLAASTASGKTEAAFFPILTDLYENPSSsvgVLYISPLKALINDQYERLTDLCQDVDIPIWRWHGevaqTQKRKLLKH 119
Cdd:cd18026 35 NLVYSLPTSGGKTLVAEILMLKRLLERRKK---ALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAG----NKGRSPPKR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 120 PSG--ILQITPESLESLmINKHMDIPNLfHDLRYVVIDELHSFLRSDRGGQTFCLIERLSKMAGVDPRRIGLSATIGDTE 197
Cdd:cd18026 108 RKSlsVAVCTIEKANSL-VNSLIEEGRL-DELGLVVVDELHMLGDGHRGALLELLLTKLLYAAQKNIQIVGMSATLPNLE 185
|
....*...
gi 1706369249 198 SAARFLGA 205
Cdd:cd18026 186 ELASWLRA 193
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
8-375 |
3.55e-09 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 60.34 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 8 APFIQDYIYEH--NWKNLRSI-----QVGAAETIfNSQDNVLLAASTASGKTEAAFFPILTDLYENPSssvgVLYISPLK 80
Cdd:COG4581 4 SPARADARLEAlaDFAEERGFeldpfQEEAILAL-EAGRSVLVAAPTGSGKTLVAEFAIFLALARGRR----SFYTAPIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 81 ALINDQYErltDLCqdvdipiwRWHGEVAqtqkrkllkhpSGIL----------QI---TPESLEslmiNKHMDIPNLFH 147
Cdd:COG4581 79 ALSNQKFF---DLV--------ERFGAEN-----------VGLLtgdasvnpdaPIvvmTTEILR----NMLYREGADLE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 148 DLRYVVIDELHsFLrSDRggqtfcliERlskmaGVD--------PRR---IGLSATIGDTESAARFLGagSKRRTT---- 212
Cdd:COG4581 133 DVGVVVMDEFH-YL-ADP--------DR-----GWVweepiihlPARvqlVLLSATVGNAEEFAEWLT--RVRGETavvv 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 213 -----VPktesggqvwrlsMEHFYDNGPQ--------ADSSGFAPAQPVLDE--KSDQAPqmadpsmAYIFEHTRgKKC- 276
Cdd:COG4581 196 seerpVP------------LEFHYLVTPRlfplfrvnPELLRPPSRHEVIEEldRGGLLP-------AIVFIFSR-RGCd 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 277 -----LVFTN--SREECEAVCQILRQYCE-----INHEPDRFL-----IHHGNLSAAYRQTAEAemknedsLMTT----- 334
Cdd:COG4581 256 eaaqqLLSARltTKEERAEIREAIDEFAEdfsvlFGKTLSRLLrrgiaVHHAGMLPKYRRLVEE-------LFQAgllkv 328
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1706369249 335 -CATATLELGID-------IGKLERaF--QVDAPFTVSGFLQRMGRTGRRG 375
Cdd:COG4581 329 vFATDTLAVGINmpartvvFTKLSK-FdgERHRPLTAREFHQIAGRAGRRG 378
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
18-372 |
5.24e-09 |
|
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: 58.73 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 18 HNWKNLRSIQVGAAETIFNSqdnvllaASTASGKTEAAFFPILTDlyENPSssvgvLYISPLKALINDQYERLTDLCQDV 97
Cdd:cd09710 1 HQVATFEALQSKDADIIFNT-------APTGAGKTLAWLTPLLHG--ENKA-----IALYPTNALIEDQTEAIKEFVDDA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 98 D------------IPIWRWH-------GEVAQTQKRKLLKHPSGILQIT-PE----SLESLMINKHMDIPNLFHDLRYVV 153
Cdd:cd09710 67 NprhqvkslsasdITLWPNDknvgsskGEKLYNLLRNDIGTSTPIILLTnPDifvyLTRFAYIDRGDIAAGFYTKFSTVI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 154 IDELHSFLRSDRGGQTFCLIErlSKMAGVDPRR---IGLSATiGDTESAARFLGAGSKRRTTVPKTESGGQvwrlsmehF 230
Cdd:cd09710 147 FDEFHLYDAKQLVGLLFYLAY--MQLIRFFECRrkfVFLSAT-PDPALILRLQNAKQAGVKIAPIDGEAGQ--------F 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 231 YDN---GPQADSSGFAPAQPVLD-----EKSDQAPQMADPSmAYIFEHTR---GKKCLVFTNSREECEAVCQILRQ---- 295
Cdd:cd09710 216 PDNpelEQQLKNTSFRPVLPPVElelipAPDFKEEWLAELA-AEVIERFRqlpGERGAIILDSLDEVNRLSDLLQQqglg 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1706369249 296 --YCEINhepdrflihhgnlsaAYRQTAEAEMKNedSLMTTCATATLELGIDigkLERAFQVDAPFTVSGFLQRMGRTG 372
Cdd:cd09710 295 ddIGRIT---------------GFAPKKDRERAM--QFDILLGTSTVDVGVD---FKRDWLIFSARDAAAFWQRLGRLG 353
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
41-210 |
6.50e-09 |
|
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: 56.22 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 41 VLLAASTASGKTEAAFFPILTDLYEnpsSSVGVL-YISPLKALIN----DQYERLTDLCQDVDIPIWrwhgeVAQTQKRK 115
Cdd:cd18025 19 ALIVAPTSSGKTFISYYCMEKVLRE---SDDGVVvYVAPTKALVNqvvaEVYARFSKKYPPSGKSLW-----GVFTRDYR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 116 LLKHPSGILQIT-PESLESLMINKHMDipNLFHDLRYVVIDELHSfLRSDRGGQTFcliERLSKMAgvDPRRIGLSATIG 194
Cdd:cd18025 91 HNNPMNCQVLITvPECLEILLLSPHNA--SWVPRIKYVIFDEIHS-IGQSEDGAVW---EQLLLLI--PCPFLALSATIG 162
|
170
....*....|....*.
gi 1706369249 195 DTESAARFLGAGSKRR 210
Cdd:cd18025 163 NPQKFHEWLQSVQRAR 178
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
20-158 |
1.56e-08 |
|
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: 55.23 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 20 WKNLRSIQVGAAETIFNSQDnVLLAASTASGKT-----EAAFFPILTdlyenpsssvgvLYISPLKALINDQYERLTDLc 94
Cdd:cd17920 10 YDEFRPGQLEAINAVLAGRD-VLVVMPTGGGKSlcyqlPALLLDGVT------------LVVSPLISLMQDQVDRLQQL- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706369249 95 qdvDIPIWRWHGEVAQTQKRK-LLKHPSG---ILQITPESLESLMINKHMDIPNLFHDLRYVVIDELH 158
Cdd:cd17920 76 ---GIRAAALNSTLSPEEKREvLLRIKNGqykLLYVTPERLLSPDFLELLQRLPERKRLALIVVDEAH 140
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
40-205 |
4.66e-08 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 56.75 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 40 NVLLAASTASGKTEAAFFPILTDLYENPSSSVgvlYISPLKALINDQYERLTDlcqdvdipiWRWHG-EVAQT------Q 112
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMVNKLLREGGKAV---YLVPLKALAEEKYREFKD---------WEKLGlRVAMTtgdydsT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 113 KRKLLKHpsGILQITPESLESLMINKHMDIpnlfHDLRYVVIDELHSFLRSDRGGqTFCLIerLSKMAGvDPRRIGLSAT 192
Cdd:PRK00254 109 DEWLGKY--DIIIATAEKFDSLLRHGSSWI----KDVKLVVADEIHLIGSYDRGA-TLEMI--LTHMLG-RAQILGLSAT 178
|
170
....*....|...
gi 1706369249 193 IGDTESAARFLGA 205
Cdd:PRK00254 179 VGNAEELAEWLNA 191
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
40-375 |
9.33e-08 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 55.73 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 40 NVLLAASTASGKTEAAFFPILtdlyenpsSSVG----VLYISPLKALINDQYERLTDLCQD-VDIPIW--------RWHG 106
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAML--------KAIArggkALYIVPLRALASEKFEEFERFEELgVRVGIStgdydsrdEWLG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 107 EvaqtqkrkllkhpSGILQITPESLESLMINKH--MDipnlfhDLRYVVIDELHSFLRSDRGGQTFCLIERLSKMaGVDP 184
Cdd:PRK02362 113 D-------------NDIIVATSEKVDSLLRNGApwLD------DITCVVVDEVHLIDSANRGPTLEVTLAKLRRL-NPDL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 185 RRIGLSATIGDTESAARFLGAGskrrttVPKTEsggqvWR---LSMEHFYDNGPQADSSgfapAQPVLDEKSDQAPQMAD 261
Cdd:PRK02362 173 QVVALSATIGNADELADWLDAE------LVDSE-----WRpidLREGVFYGGAIHFDDS----QREVEVPSKDDTLNLVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 262 PSMAyifehtRGKKCLVFTNSREECEA----VCQILRQYCEINHEP------DRFL--------------------IHHG 311
Cdd:PRK02362 238 DTLE------EGGQCLVFVSSRRNAEGfakrAASALKKTLTAAERAelaelaEEIRevsdtetskdladcvakgaaFHHA 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706369249 312 NLSAAYRQTAEAEMKNEDsLMTTCATATLELGID------IGKLERAFQVDA---PFTVSGFLQRMGRTGRRG 375
Cdd:PRK02362 312 GLSREHRELVEDAFRDRL-IKVISSTPTLAAGLNlparrvIIRDYRRYDGGAgmqPIPVLEYHQMAGRAGRPG 383
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
23-193 |
1.04e-07 |
|
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: 52.83 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 23 LRSIQVGAAETIFNSQdNVLLAASTASGKTEAAFFPILTDLYENPSssvgVLYISPLKALINDQYERLTDLCQDV----- 97
Cdd:cd18024 33 LDPFQKTAIACIERNE-SVLVSAHTSAGKTVVAEYAIAQSLRDKQR----VIYTSPIKALSNQKYRELQEEFGDVglmtg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 98 DIPIwrwhgevaqtqkrkllkHPS-GILQITPESLESlMINKHMDIpnlFHDLRYVVIDELHSFLRSDRG---GQTFCLi 173
Cdd:cd18024 108 DVTI-----------------NPNaSCLVMTTEILRS-MLYRGSEI---MREVAWVIFDEIHYMRDKERGvvwEETIIL- 165
|
170 180
....*....|....*....|
gi 1706369249 174 erLSKMAgvdpRRIGLSATI 193
Cdd:cd18024 166 --LPDKV----RYVFLSATI 179
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
11-187 |
1.51e-07 |
|
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: 52.44 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 11 IQDYIYEHNWKNLRSIQVGAAETIFNSQDnVLLAASTASGKTeAAF-FPILTDLYENP---SSSVGVLYISPLKAL---I 83
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRD-VIGQAQTGSGKT-LAFlLPILEKLLPEPkkkGRGPQALVLAPTRELamqI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 84 NDQYERLtdlCQDVDIPIWRWHGEVAQTQKRKLLKHPSGILQITPESLESLMINKHMDipnlFHDLRYVVIDE------- 156
Cdd:cd00268 79 AEVARKL---GKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLD----LSNVKYLVLDEadrmldm 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1706369249 157 --------LHSFLRSDRggQTFCL-------IERLSKMAGVDPRRI 187
Cdd:cd00268 152 gfeedvekILSALPKDR--QTLLFsatlpeeVKELAKKFLKNPVRI 195
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
269-375 |
1.85e-07 |
|
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: 51.01 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 269 EHTRGKKCLVFTNSREECEAVCQILRQyceinhepdrFLIHHGNLSAAYRQTAEaEMKNEDSLMTTCATATLELGID--- 345
Cdd:cd18795 39 TVSEGKPVLVFCSSRKECEKTAKDLAG----------IAFHHAGLTREDRELVE-ELFREGLIKVLVATSTLAAGVNlpa 107
|
90 100 110
....*....|....*....|....*....|....*
gi 1706369249 346 ----IGKLERAFQVDA-PFTVSGFLQRMGRTGRRG 375
Cdd:cd18795 108 rtviIKGTQRYDGKGYrELSPLEYLQMIGRAGRPG 142
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
39-181 |
2.80e-07 |
|
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: 51.52 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 39 DNVLLAASTASGKTEAAFFPILTDLYENPSSsvGVLYISPLKALINDQYERLTDLCQDVDIP------------------ 100
Cdd:cd17930 2 GLVILEAPTGSGKTEAALLWALKLAARGGKR--RIIYALPTRATINQMYERIREILGRLDDEdkvlllhskaalellesd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 101 IWRWHGEVAQTQKRKLLKH----PSGIL---QItpesLESLMINKHMDIPnlFHDL--RYVVIDELHSFlrSDRggQTFC 171
Cdd:cd17930 80 EEPDDDPVEAVDWALLLKRswlaPIVVTtidQL----LESLLKYKHFERR--LHGLanSVVVLDEVQAY--DPE--YMAL 149
|
170
....*....|
gi 1706369249 172 LIERLSKMAG 181
Cdd:cd17930 150 LLKALLELLG 159
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
20-207 |
7.64e-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: 50.33 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 20 WKNLRSIQVGAAETIFNSQDNVLLAASTASGKTEAAFFPILTDLYENPSSSvgVLYISPLKALINDQYErltdlcqdvdi 99
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGR--AVYIAPMQELVDARYK----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 100 pIWR------WHGEVAQ-----TQKRKLLKHpSGILQITPESLESL----MINKHMDIPNLFhdlryvVIDELHsFLRSD 164
Cdd:cd18021 68 -DWRakfgplLGKKVVKltgetSTDLKLLAK-SDVILATPEQWDVLsrrwKQRKNVQSVELF------IADELH-LIGGE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1706369249 165 RGGQTFCLIERLSKMAG--VDPRRI-GLSATIGDTESAARFLGAGS 207
Cdd:cd18021 139 NGPVYEVVVSRMRYISSqlEKPIRIvGLSSSLANARDVGEWLGASK 184
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
39-216 |
2.00e-06 |
|
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: 48.80 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 39 DNVLLAASTASGKTEAAFFPILTDLYENPSSsvgvLYISPLKALINDQYERLTDLCQDVDIPIwrwhGEVAQtqkrkllk 118
Cdd:cd18027 24 DSVFVAAHTSAGKTVVAEYAIALAQKHMTRT----IYTSPIKALSNQKFRDFKNTFGDVGLIT----GDVQL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 119 HPSG-ILQITPESLESLMINKhmdiPNLFHDLRYVVIDELHSFLRSDRGgqtfCLIERLSKMAGVDPRRIGLSATIGDTE 197
Cdd:cd18027 88 NPEAsCLIMTTEILRSMLYNG----SDVIRDLEWVIFDEVHYINDAERG----VVWEEVLIMLPDHVSIILLSATVPNTV 159
|
170
....*....|....*....
gi 1706369249 198 SAARFLGAGSKRRTTVPKT 216
Cdd:cd18027 160 EFADWIGRIKKKNIYVIST 178
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
152-373 |
7.68e-06 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 49.50 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 152 VVIDELHSFLRSDRGGQTFCLIERLSKMAGvDPRRIGLSATIGDTESAARFLGA---------------------GSKRR 210
Cdd:COG1202 330 VVIDEVHMLEDPERGHRLDGLIARLKYYCP-GAQWIYLSATVGNPEELAKKLGAklveyeerpvplerhltfadgREKIR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 211 TtvpktesggqVWRLSMEHFydngpqadssgfapaqpvlDEKSdqapqmadpSMAYifehtRGkKCLVFTNSREECEavc 290
Cdd:COG1202 409 I----------INKLVKREF-------------------DTKS---------SKGY-----RG-QTIIFTNSRRRCH--- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 291 qILRQYCEINHEPdrfliHHGNLSAAYRQTAEAEMKNEDsLMTTCATATLELGIDIGklerAFQVdaPF----------T 360
Cdd:COG1202 442 -EIARALGYKAAP-----YHAGLDYGERKKVERRFADQE-LAAVVTTAALAAGVDFP----ASQV--IFdslamgiewlS 508
|
250
....*....|...
gi 1706369249 361 VSGFLQRMGRTGR 373
Cdd:COG1202 509 VQEFHQMLGRAGR 521
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
41-156 |
1.30e-05 |
|
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: 47.23 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 41 VLLAASTASGKTEAAFFPILTDLYENPSSSVGVLYISPLKALI-------NDQYER-LTDLCQDVDIPIWRWHGEVA-QT 111
Cdd:cd17946 31 VIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALIltptrelAVQVKDhLKAIAKYTNIKIASIVGGLAvQK 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1706369249 112 QKRKLLKHPSgILQITPESLESLMI--NKHMdipNLFHDLRYVVIDE 156
Cdd:cd17946 111 QERLLKKRPE-IVVATPGRLWELIQegNEHL---ANLKSLRFLVLDE 153
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
15-156 |
5.38e-05 |
|
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: 44.89 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 15 IYEHNWKNLRSIQVGAAETIFNSQDnVLLAASTASGKTEAAFFPILTDLYENPSSS-VGVLYISPLKALINDQYERLTDL 93
Cdd:cd17957 5 LEESGYREPTPIQMQAIPILLHGRD-LLACAPTGSGKTLAFLIPILQKLGKPRKKKgLRALILAPTRELASQIYRELLKL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706369249 94 CQDVDIpiwRWH-----GEVAQTQKRKLLKHPSgILQITPESLESLMINKHMDIPNlfhdLRYVVIDE 156
Cdd:cd17957 84 SKGTGL---RIVllsksLEAKAKDGPKSITKYD-ILVSTPLRLVFLLKQGPIDLSS----VEYLVLDE 143
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
11-381 |
1.64e-04 |
|
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: 45.07 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 11 IQDYIYEHnwknlrsiqvgAAETIFNSQDNVLLAASTASGKTEAAFFPILTDLYENPSSsvGVLYISPLKALINDQYERL 90
Cdd:COG1203 131 LQNEALEL-----------ALEAAEEEPGLFILTAPTGGGKTEAALLFALRLAAKHGGR--RIIYALPFTSIINQTYDRL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 91 TDL-CQDV-------DIPIWRWHGEV-AQTQKRKLLKH----PSGIL---QItpesLESLMIN-KHMDIPnlFHDLRY-- 151
Cdd:COG1203 198 RDLfGEDVllhhslaDLDLLEEEEEYeSEARWLKLLKElwdaPVVVTtidQL----FESLFSNrKGQERR--LHNLANsv 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 152 VVIDELHSFlrsDRggQTFCLIERLSKMAgvdpRRIG-----LSAT---------------IGD-TESAARFLGAGSKRR 210
Cdd:COG1203 272 IILDEVQAY---PP--YMLALLLRLLEWL----KNLGgsvilMTATlppllreelleayelIPDePEELPEYFRAFVRKR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 211 TTVPKTEsggqvwrLSMEHFydngpqadssgfapAQPVLDEKSDqapqmadpsmayifehtrGKKCLVFTNSREECEAVC 290
Cdd:COG1203 343 VELKEGP-------LSDEEL--------------AELILEALHK------------------GKSVLVIVNTVKDAQELY 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 291 QILRQyceiNHEPDRFLIHHGNLSAAYRQTAEAEMKNEDSLMTTC---ATATLELGIDIgklerafqvDAPFTVSGF--- 364
Cdd:COG1203 384 EALKE----KLPDEEVYLLHSRFCPADRSEIEKEIKERLERGKPCilvSTQVVEAGVDI---------DFDVVIRDLapl 450
|
410 420
....*....|....*....|...
gi 1706369249 365 ---LQRMGRT---GRRGNPAEMW 381
Cdd:COG1203 451 dslIQRAGRCnrhGRKEEEGNVY 473
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
275-373 |
3.84e-04 |
|
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: 39.61 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 275 KCLVFTNSREECEAVcqilrqYCEINhepdrFLIhhgnlsaayrqtaeaemknedslmttcATATLELGIDIGKLERAFQ 354
Cdd:cd18785 5 KIIVFTNSIEHAEEI------ASSLE-----ILV---------------------------ATNVLGEGIDVPSLDTVIF 46
|
90
....*....|....*....
gi 1706369249 355 VDAPFTVSGFLQRMGRTGR 373
Cdd:cd18785 47 FDPPSSAASYIQRVGRAGR 65
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
41-192 |
3.92e-04 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 42.62 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 41 VLLAASTASGKTEAAFFPILTDLYENPSSSVGVLYISPLKALINDQYERLTDLCQDVDIPIWRWHGEVAQTQKRKLLKHP 120
Cdd:cd17956 39 LCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 121 SG--------ILQITPESL-ESLMINKHMDipnlFHDLRYVVIDE----------------LHSFLRSDRGGQTFCLIER 175
Cdd:cd17956 119 TSgrylsrvdILVATPGRLvDHLNSTPGFT----LKHLRFLVIDEadrllnqsfqdwletvMKALGRPTAPDLGSFGDAN 194
|
170
....*....|....*..
gi 1706369249 176 LSKMAGVDPRRIGLSAT 192
Cdd:cd17956 195 LLERSVRPLQKLLFSAT 211
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
45-182 |
4.46e-04 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 41.93 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 45 ASTASGKTEaafFPILTDLYenpSSSVG--VLYISPLKALINDQYERLTDLCQDVDIP--IWRWHGEVAQTQKRKLLKHP 120
Cdd:cd17924 39 APTGVGKTT---FGLATSLY---LASKGkrSYLIFPTKSLVKQAYERLSKYAEKAGVEvkILVYHSRLKKKEKEELLEKI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1706369249 121 SG----ILQITpesleSLMINKHMD-IPNlfHDLRYVVIDELHSFLRSDRGgqtfclIERLSKMAGV 182
Cdd:cd17924 113 EKgdfdILVTT-----NQFLSKNFDlLSN--KKFDFVFVDDVDAVLKSSKN------IDRLLKLLGF 166
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
15-156 |
7.22e-04 |
|
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: 41.58 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 15 IYEHNWKNLRSIQVGAAETIFNSQDnVLLAASTASGKTEAAFFPILTDLYE---NPSSSVGVLYISPLKALINDQYERLT 91
Cdd:cd17942 5 IEEMGFTKMTEIQAKSIPPLLEGRD-VLGAAKTGSGKTLAFLIPAIELLYKlkfKPRNGTGVIIISPTRELALQIYGVAK 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 92 DLC----QDVDIPIwrwHGEVAQTQKRKLLKHPSgILQITPESLESLMINKhmdiPN-LFHDLRYVVIDE 156
Cdd:cd17942 84 ELLkyhsQTFGIVI---GGANRKAEAEKLGKGVN-ILVATPGRLLDHLQNT----KGfLYKNLQCLIIDE 145
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
277-379 |
7.86e-04 |
|
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: 40.27 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 277 LVFTNSREECEAVCQILRQYCeinhepDRFLIHHGNLSAAYRQTAEAEMkNEDSLMTTCATATLELGIDIGKLERAFQVD 356
Cdd:cd18794 34 IIYCLSRKECEQVAARLQSKG------ISAAAYHAGLEPSDRRDVQRKW-LRDKIQVIVATVAFGMGIDKPDVRFVIHYS 106
|
90 100
....*....|....*....|...
gi 1706369249 357 APFTVSGFLQRMGRTGRRGNPAE 379
Cdd:cd18794 107 LPKSMESYYQESGRAGRDGLPSE 129
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
8-197 |
1.43e-03 |
|
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: 40.77 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 8 APFIQDYIYEHNWKNLRSIQVGAAETIFNSQDnVLLAASTASGKTEAAFFPILtdlyenpsSSVGVLYISPLKALINDQY 87
Cdd:cd17938 7 MPELIKAVEELDWLLPTDIQAEAIPLILGGGD-VLMAAETGSGKTGAFCLPVL--------QIVVALILEPSRELAEQTY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 88 ERLTDLCQDVDIPIWR---WHGEVAQTQKRKLLKHPSGILQITPESLESLMINKHMDIPNlfhdLRYVVIDELHSFLRSD 164
Cdd:cd17938 78 NCIENFKKYLDNPKLRvalLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSS----VRFFVLDEADRLLSQG 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1706369249 165 RGGQTFCLIERLSKMAGVDPR--RIGLSATIGDTE 197
Cdd:cd17938 154 NLETINRIYNRIPKITSDGKRlqVIVCSATLHSFE 188
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
41-156 |
6.92e-03 |
|
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: 38.43 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 41 VLLAASTASGKTEAAFFPILTDLYEN---PSSSVGVLYISPLKALINDQYERLTDlcqdvdipIWRWH---------GEV 108
Cdd:cd17941 30 ILGAAKTGSGKTLAFLVPLLEKLYRErwtPEDGLGALIISPTRELAMQIFEVLRK--------VGKYHsfsagliigGKD 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1706369249 109 AQTQKRKLlkHPSGILQITPESLEslminKHMDIPNLFH--DLRYVVIDE 156
Cdd:cd17941 102 VKEEKERI--NRMNILVCTPGRLL-----QHMDETPGFDtsNLQMLVLDE 144
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
277-381 |
9.01e-03 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 39.35 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706369249 277 LVFTNSREECEAVCQILRQyCEINHEPdrfliHHGNLSAAYRQTAEAE-MKNEDSLMttCATATLELGID---IGklera 352
Cdd:COG0514 234 IVYCLSRKKVEELAEWLRE-AGIRAAA-----YHAGLDAEEREANQDRfLRDEVDVI--VATIAFGMGIDkpdVR----- 300
|
90 100 110
....*....|....*....|....*....|.
gi 1706369249 353 FQV--DAPFTVSGFLQRMGRTGRRGNPAEMW 381
Cdd:COG0514 301 FVIhyDLPKSIEAYYQEIGRAGRDGLPAEAL 331
|
|
| |
