|
Name |
Accession |
Description |
Interval |
E-value |
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
4-936 |
0e+00 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 836.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 4 THLDTFAAGLPYPLDEFQVQGCEAVENGQGVLVCAPTGAGKTVVGEFAVSLALSRGTKCFYTTPIKALSNQKYHDLVAEH 83
Cdd:COG4581 13 EALADFAEERGFELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALARGRRSFYTAPIKALSNQKFFDLVERF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 84 GDDAVGLLTGDVSINADAEIVVMTTEVLRNMIYADSPALDRLTHVVMDEIHFLADASRGAVWEEVILNLADHVSIIGLSA 163
Cdd:COG4581 93 GAENVGLLTGDASVNPDAPIVVMTTEILRNMLYREGADLEDVGVVVMDEFHYLADPDRGWVWEEPIIHLPARVQLVLLSA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 164 TVSNSEEFGEWLATVRGDTSVIVTEHRPVPLDQWMMLGRKIYPLFEpesggqVNSELERriqrleagdsddgradyksgk 243
Cdd:COG4581 173 TVGNAEEFAEWLTRVRGETAVVVSEERPVPLEFHYLVTPRLFPLFR------VNPELLR--------------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 244 gfrararhkgggrsefhgkaggrsgssrpqdryrPLGRPEVLKVLQSQDMLPAITFIFSRAGCDGALYQCLRSRmvLTTQ 323
Cdd:COG4581 226 ----------------------------------PPSRHEVIEELDRGGLLPAIVFIFSRRGCDEAAQQLLSAR--LTTK 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 324 EEAEEIKAIVDAGvegipEEDLQVLDFRRWREALSRGFAAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMPAR 403
Cdd:COG4581 270 EERAEIREAIDEF-----AEDFSVLFGKTLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPAR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 404 TVVLEKLIKFNGEAHVDLTPGQYTQLTGRAGRRGIDTLGNAVVQWAPAMDPRFVAGLASTRTYPLISTFAPGYNMAINLL 483
Cdd:COG4581 345 TVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDTEGHVVVLAPEHDDPKKFARLASARPEPLRSSFRPSYNMVLNLL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 484 GMLGFEDSLRLLEKSFAQFQADGSVVEETReleraehRVRELREQLDDAVAALAPPAKDgedpaevLMDYIRLRRELTAE 563
Cdd:COG4581 425 ARPGLERARELLEDSFAQFQADRSVVGLAR-------RARELERALAGVVERLACDLGD-------LQEYFALRQPLSPL 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 564 EKQSKVDKEHQRtqevvavlarlqlgDVIALAGKKRptlaavvtpanqtEDPRPWVTTESGWSGRidatgisnppiqlgr 643
Cdd:COG4581 491 EALERESPAYAL--------------DVVSVPEATL-------------EDPRPVLLAQDRRARG--------------- 528
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 644 ikipkpvrknprrntkyiqdlfrrekfDRPKRMKSkpRLRPNKRVGELRDAIREHPAHEWPATDREQLagvaqklarrER 723
Cdd:COG4581 529 ---------------------------EAAAAMKA--AIEYDERMERLEEVLRPHPLHECPLERAFEL----------YR 569
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 724 DLEKLQAKVNKATDTLGRTFERIVDLLAEMDYVEssgagsdrTPVITEEGERLAKIHSesdllVAQCLKRGIWDELDPAE 803
Cdd:COG4581 570 ETHPWVRDIELRPKSVARDFDRFCELLREYGYLD--------DLTLTSEGLLLRYLYD-----AAEALRQGVPDDLDPEE 636
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 804 LAGVASLCCFENRKATGGQPEAA-TDRMADAMNATWRIYTELSADERRHRLPptrEPEAGFALaihQWSAGAPLGYCMAA 882
Cdd:COG4581 637 LAALISWLVEEVRRVDSSEWERLpSPANRRAFVLVNALFRRLELLERRHGLP---ELDPGLAG---AWASGADLAEVLDA 710
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 552765374 883 aneagAELTPGDFVRWCRQVVDLlqqiaktgyDGQIQRNARRAIDAIQRGVVAI 936
Cdd:COG4581 711 -----TDLDAGDFVRWVRQVIDP---------DPELRRTARAAVDLIRRGVVAY 750
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
26-528 |
3.77e-61 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 217.46 E-value: 3.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 26 EAVE----NGQGVLVCAPTGAGKTVVGEFAVSLALSRGTKCFYTTPIKALSNQKYHDLVAEHGDDA--VGLLTGDVSIN- 98
Cdd:COG1204 29 EALEagllEGKNLVVSAPTASGKTLIAELAILKALLNGGKALYIVPLRALASEKYREFKRDFEELGikVGVSTGDYDSDd 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 99 ---ADAEIVVMTTEVLRNMIYADSPALDRLTHVVMDEIHFLADASRGAVWEEVI---LNLADHVSIIGLSATVSNSEEFG 172
Cdd:COG1204 109 ewlGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHLIDDESRGPTLEVLLarlRRLNPEAQIVALSATIGNAEEIA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 173 EWLatvrgDTSVIVTEHRPVPLDQWMMLGRKIYplFEPESggqvnSELERRIQRLeagdsddgradyksgkgfrararhk 252
Cdd:COG1204 189 EWL-----DAELVKSDWRPVPLNEGVLYDGVLR--FDDGS-----RRSKDPTLAL------------------------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 253 gggrsefhgkaggrsgssrpqdryrplgrpeVLKVLQSQDmlPAITFIFSRAGCDGA---LYQCLRSRMVLTTQEEAEEI 329
Cdd:COG1204 232 -------------------------------ALDLLEEGG--QVLVFVSSRRDAESLakkLADELKRRLTPEEREELEEL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 330 KAIVDAGVEGIPEEDlqVLdfrrwREALSRGFAAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMPARTVVLEK 409
Cdd:COG1204 279 AEELLEVSEETHTNE--KL-----ADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 410 lIKFNGEahVDLTPGQYTQLTGRAGRRGIDTLGNAVVQWAPAMDP-----RFVAGlastRTYPLISTFAPGYNMAINLLG 484
Cdd:COG1204 352 -TKRGGM--VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDEAdelfeRYILG----EPEPIRSKLANESALRTHLLA 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 552765374 485 MLG------FEDSLRLLEKSFAQFQADGSVVEEtrELERAehrVRELREQ 528
Cdd:COG1204 425 LIAsgfansREELLDFLENTFYAYQYDKGDLEE--VVDDA---LEFLLEN 469
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
14-190 |
4.21e-61 |
|
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: 206.53 E-value: 4.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 14 PYPLDEFQVQGCEAVENGQGVLVCAPTGAGKTVVGEFAVSLALSRGTKCFYTTPIKALSNQKYHDLVAEHGDdaVGLLTG 93
Cdd:cd18024 30 PFTLDPFQKTAIACIERNESVLVSAHTSAGKTVVAEYAIAQSLRDKQRVIYTSPIKALSNQKYRELQEEFGD--VGLMTG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 94 DVSINADAEIVVMTTEVLRNMIYADSPALDRLTHVVMDEIHFLADASRGAVWEEVILNLADHVSIIGLSATVSNSEEFGE 173
Cdd:cd18024 108 DVTINPNASCLVMTTEILRSMLYRGSEIMREVAWVIFDEIHYMRDKERGVVWEETIILLPDKVRYVFLSATIPNARQFAE 187
|
170
....*....|....*...
gi 552765374 174 WLATV-RGDTSVIVTEHR 190
Cdd:cd18024 188 WICKIhKQPCHVVYTDYR 205
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
14-179 |
6.31e-55 |
|
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: 188.24 E-value: 6.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 14 PYPLDEFQVQGCEAVENGQGVLVCAPTGAGKTVVGEFAVSLALSRGTKCFYTTPIKALSNQKYHDLVAEHGDdaVGLLTG 93
Cdd:cd18027 6 PFELDVFQKQAILHLEAGDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGD--VGLITG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 94 DVSINADAEIVVMTTEVLRNMIYADSPALDRLTHVVMDEIHFLADASRGAVWEEVILNLADHVSIIGLSATVSNSEEFGE 173
Cdd:cd18027 84 DVQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDHVSIILLSATVPNTVEFAD 163
|
....*.
gi 552765374 174 WLATVR 179
Cdd:cd18027 164 WIGRIK 169
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
16-175 |
5.74e-47 |
|
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: 165.90 E-value: 5.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 16 PLDEFQVQG-CEAVENGQGVLVCAPTGAGKTVVGEFAVSLALSR-GTKCFYTTPIKALSNQKYHDL--VAEHGDDAVGLL 91
Cdd:cd17921 1 LLNPIQREAlRALYLSGDSVLVSAPTSSGKTLIAELAILRALATsGGKAVYIAPTRALVNQKEADLreRFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 92 TGDVSIN----ADAEIVVMTTEVLRNMIYAD-SPALDRLTHVVMDEIHFLADASRGAVWEEVI---LNLADHVSIIGLSA 163
Cdd:cd17921 81 TGDPSVNklllAEADILVATPEKLDLLLRNGgERLIQDVRLVVVDEAHLIGDGERGVVLELLLsrlLRINKNARFVGLSA 160
|
170
....*....|..
gi 552765374 164 TVSNSEEFGEWL 175
Cdd:cd17921 161 TLPNAEDLAEWL 172
|
|
| DSHCT |
pfam08148 |
DSHCT (NUC185) domain; This C terminal domain is found in DOB1/SK12/helY-like DEAD box ... |
768-934 |
2.17e-41 |
|
DSHCT (NUC185) domain; This C terminal domain is found in DOB1/SK12/helY-like DEAD box helicases.
Pssm-ID: 462374 Cd Length: 154 Bit Score: 148.75 E-value: 2.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 768 VITEEGERLAKIHSESDLLVAQCLKRGIWDELDPAELAGVASLCCFENRKATggqPEAATDRMADAmnatwriYTELsaD 847
Cdd:pfam08148 2 VVTLKGRVACEIRSENELLLTELLFSGVFDDLDPEELAALLSAFVFEEKRRE---PYLPSPELAEA-------LRLL--E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 848 ERRHRLPPTREPEAGFALAIHQWSAGAPLGYCMAAANeagaeLTPGDFVRWCRQVVDLLQQI---AKTGYDGQIQRNARR 924
Cdd:pfam08148 70 EIAHRIAVSRFLDFGLMEVVYAWARGASFAEICKLTD-----LDEGDIVRLIRRLDELLRQIanaAKIIGDPELREKAEE 144
|
170
....*....|
gi 552765374 925 AIDAIQRGVV 934
Cdd:pfam08148 145 AIELIKRDIV 154
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
26-519 |
1.45e-39 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 157.43 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 26 EAVE----NGQGVLVCAPTGAGKTVVGEFAVSLALSRGTKCFYTTPIKALSNQKYHDLVA--EHGDDaVGLLTGDVSIN- 98
Cdd:PRK02362 30 EAVEagllDGKNLLAAIPTASGKTLIAELAMLKAIARGGKALYIVPLRALASEKFEEFERfeELGVR-VGISTGDYDSRd 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 99 ---ADAEIVVMTTE----VLRNmiyaDSPALDRLTHVVMDEIHFLADASRGAVWEEVI-----LNLAdhVSIIGLSATVS 166
Cdd:PRK02362 109 ewlGDNDIIVATSEkvdsLLRN----GAPWLDDITCVVVDEVHLIDSANRGPTLEVTLaklrrLNPD--LQVVALSATIG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 167 NSEEFGEWLatvrgDTSVIVTEHRPVPLDQWMMLGRKIYplFepesggqvnSELERRIQRLEAGDSDDGRADYKsgkgfr 246
Cdd:PRK02362 183 NADELADWL-----DAELVDSEWRPIDLREGVFYGGAIH--F---------DDSQREVEVPSKDDTLNLVLDTL------ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 247 ararhkgggrsefhgKAGGRSgssrpqdryrplgrpevlkvlqsqdmlpaITFIFSRAGCDGA---LYQCLRSRMVLTTQ 323
Cdd:PRK02362 241 ---------------EEGGQC-----------------------------LVFVSSRRNAEGFakrAASALKKTLTAAER 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 324 EEAEEIKAIVDAGVEGIPEEDLQvldfrrwrEALSRGFAAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMPAR 403
Cdd:PRK02362 277 AELAELAEEIREVSDTETSKDLA--------DCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPAR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 404 TVVLEKLIKFNGEAHVDLTP-GQYTQLTGRAGRRGIDTLGNAVVQ---------------WAPAMDPRF-VAGLASTRTY 466
Cdd:PRK02362 349 RVIIRDYRRYDGGAGMQPIPvLEYHQMAGRAGRPGLDPYGEAVLLaksydeldelferyiWADPEDVRSkLATEPALRTH 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 552765374 467 pLISTFAPGYnmAINLLGMLGFedslrlLEKSFAQFQAD-----GSVVEETRE-LERAE 519
Cdd:PRK02362 429 -VLSTIASGF--ARTRDGLLEF------LEATFYATQTDdtgrlERVVDDVLDfLERNG 478
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
282-446 |
2.00e-39 |
|
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: 143.08 E-value: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 282 PEVLKVLQSQDMLPAITFIFSRAGCDGAlyqclrsrmvlttqeeAEEIkaivdagvegipeedlqvldfrrwrealsRGF 361
Cdd:cd18795 32 IVLLKIETVSEGKPVLVFCSSRKECEKT----------------AKDL-----------------------------AGI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 362 AAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMPARTVVLEKLIKFNGEAHVDLTPGQYTQLTGRAGRRGIDTL 441
Cdd:cd18795 67 AFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELSPLEYLQMIGRAGRPGFDTR 146
|
....*
gi 552765374 442 GNAVV 446
Cdd:cd18795 147 GEAII 151
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
3-511 |
4.04e-33 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 136.94 E-value: 4.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 3 ETHLDTFAaGLPYPLDEFQVQGCEAVENGQGVLVCAPTGAGKTVVGEFAVSLALSRGTKCFYTTPIKALSNQKYHDLVAE 82
Cdd:PRK01172 10 DEFLNLFT-GNDFELYDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELSRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 83 HG-DDAVGLLTGDVSINAD----AEIVVMTTEVLRNMIYADSPALDRLTHVVMDEIHFLADASRGAVWEEVIlNLADHVS 157
Cdd:PRK01172 89 RSlGMRVKISIGDYDDPPDfikrYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTLETVL-SSARYVN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 158 ----IIGLSATVSNSEEFGEWLatvrgDTSVIVTEHRPVPLDQWMMLGRKIYPLFEPESGGQVNSELERRIQrleagdsD 233
Cdd:PRK01172 168 pdarILALSATVSNANELAQWL-----NASLIKSNFRPVPLKLGILYRKRLILDGYERSQVDINSLIKETVN-------D 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 234 DGRadyksgkgfrararhkgggrsefhgkaggrsgssrpqdryrplgrpevlkvlqsqdmlpAITFIFSRAGCDGAlyqc 313
Cdd:PRK01172 236 GGQ-----------------------------------------------------------VLVFVSSRKNAEDY---- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 314 lrSRMVLTTQEEAEEIKaivdagvegIPEEDLQVLDfRRWREALSRGFAAHHAGMLPAFRHIVEDLFVRGLVRAVFATET 393
Cdd:PRK01172 253 --AEMLIQHFPEFNDFK---------VSSENNNVYD-DSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPT 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 394 LALGINMPARTVVLEKLIKFNGEAHVDLTPGQYTQLTGRAGRRGIDTLGNAVVQWAPAMDPRFVAGLASTRTYPLISTFA 473
Cdd:PRK01172 321 LAAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYIYAASPASYDAAKKYLSGEPEPVISYMG 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 552765374 474 PGYNMAINLLGMLGF------EDSLRLLEKSFAQFQADGSVVEE 511
Cdd:PRK01172 401 SQRKVRFNTLAAISMglassmEDLILFYNETLMAIQNGVDEIDY 444
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
31-525 |
3.65e-32 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 134.17 E-value: 3.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 31 GQGVLVCAPTGAGKTVVGEFA-VSLALSRGTKCFYTTPIKALSNQKYHDLVA-EHGDDAVGLLTGDVSINAD----AEIV 104
Cdd:PRK00254 39 GKNLVLAIPTASGKTLVAEIVmVNKLLREGGKAVYLVPLKALAEEKYREFKDwEKLGLRVAMTTGDYDSTDEwlgkYDII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 105 VMTTEVLRNMIYADSPALDRLTHVVMDEIHFLADASRGAVWEEVILNLADHVSIIGLSATVSNSEEFGEWLatvrgDTSV 184
Cdd:PRK00254 119 IATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQILGLSATVGNAEELAEWL-----NAEL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 185 IVTEHRPVPLDQWMM-LGRKIYplfepESGGqvnseLERRIQRLEAGDSDdgraDYKSGKGfrararhkgggrsefhgka 263
Cdd:PRK00254 194 VVSDWRPVKLRKGVFyQGFLFW-----EDGK-----IERFPNSWESLVYD----AVKKGKG------------------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 264 ggrsgssrpqdryrplgrpevlkvlqsqdmlpAITFIFSRAGCDGALYQCLRSRMVLTTQEEAEEIKAIVDAGVEGIPEE 343
Cdd:PRK00254 241 --------------------------------ALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKELADSLEENPTNE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 344 DLqvldfrrwREALSRGFAAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMPARTVVLEKLIKFNGEAHVDLTP 423
Cdd:PRK00254 289 KL--------KKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 424 GQYTQLTGRAGRRGIDTLGNAVVQwAPAMDP-----RFVAG--------LASTRTY-----PLISTFapgynmainllGM 485
Cdd:PRK00254 361 LEIQQMMGRAGRPKYDEVGEAIIV-ATTEEPsklmeRYIFGkpeklfsmLSNESAFrsqvlALITNF-----------GV 428
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 552765374 486 LGFEDSLRLLEKSFAQFQAdgsvveetRELERAEHRVREL 525
Cdd:PRK00254 429 SNFKELVNFLERTFYAHQR--------KDLYSLEEKAKEI 460
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
28-175 |
6.85e-30 |
|
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: 116.66 E-value: 6.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 28 VENGQGVLVCAPTGAGKTVVGEFAVSLALSRGTKCFYTTPIKALSNQKYHDLVA-EHGDDAVGLLTGDVSIN----ADAE 102
Cdd:cd18028 14 LLKGENLLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKKlEEIGLKVGISTGDYDEDdewlGDYD 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552765374 103 IVVMTTEVLRNMIYADSPALDRLTHVVMDEIHFLADASRGAVWEEVI---LNLADHVSIIGLSATVSNSEEFGEWL 175
Cdd:cd18028 94 IIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVarlRRLNPNTQIIGLSATIGNPDELAEWL 169
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
27-446 |
6.31e-27 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 118.07 E-value: 6.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 27 AVENG----QGVLVCAPTGAGKTVVGEFA-VSLALSRGTKCFYTTPIKALSNQKYHDLVAEHGDDA-VGLLTGDVSINA- 99
Cdd:COG1202 217 AVENGllegKDQLVVSATATGKTLIGELAgIKNALEGKGKMLFLVPLVALANQKYEDFKDRYGDGLdVSIRVGASRIRDd 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 100 ------DAEIVVMTTEVLRNMIYAdSPALDRLTHVVMDEIHFLADASRGAVWEEVILNL---ADHVSIIGLSATVSNSEE 170
Cdd:COG1202 297 gtrfdpNADIIVGTYEGIDHALRT-GRDLGDIGTVVIDEVHMLEDPERGHRLDGLIARLkyyCPGAQWIYLSATVGNPEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 171 FGEWLatvrgDTSVIVTEHRPVPLDQwmmlgrkiYPLFEPESGgqvNSELERRIQRLEagdsddgrADYKSGKGFRArar 250
Cdd:COG1202 376 LAKKL-----GAKLVEYEERPVPLER--------HLTFADGRE---KIRIINKLVKRE--------FDTKSSKGYRG--- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 251 hkgggrsefhgkaggrsgssrpqdryrplgrpevlkvlQSqdmlpaITFIFSRAGCdgalyqclrsrmvlttqeeaEEIK 330
Cdd:COG1202 429 --------------------------------------QT------IIFTNSRRRC--------------------HEIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 331 aivdagvegipeedlqvldfrrwrEALSRGFAAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMPARTVVLEKL 410
Cdd:COG1202 445 ------------------------RALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSL 500
|
410 420 430
....*....|....*....|....*....|....*....
gi 552765374 411 ---IKFngeahvdLTPGQYTQLTGRAGRRGIDTLGNAVV 446
Cdd:COG1202 501 amgIEW-------LSVQEFHQMLGRAGRPDYHDRGKVYL 532
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
9-197 |
1.06e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 108.35 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 9 FAAGLPYPLDEFQVQGCEAVENG-QGVLVCAPTGAGKTVVGEFAVSLALSRG--TKCFYTTPIKALSNQKYHDLVAEHGD 85
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGkgGRVLVLVPTRELAEQWAEELKKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 86 DA---VGLLTGDVS-------INADAEIVVMTTEVLRNMIYADSPALDRLTHVVMDEIHFLADASRGAVWEEVILNLADH 155
Cdd:smart00487 81 LGlkvVGLYGGDSKreqlrklESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 552765374 156 VSIIGLSATVSNSEEFGEWLaTVRGDTSVIVTEHRPVPLDQW 197
Cdd:smart00487 161 VQLLLLSATPPEEIENLLEL-FLNDPVFIDVGFTPLEPIEQF 201
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
19-170 |
1.52e-26 |
|
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: 106.56 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 19 EFQVQGCEAVENGQGVLVCAPTGAGKTVVGEFAVSLALSR---GTKCFYTTPIKALSNQKYHDL--VAEHGDDAVGLLTG 93
Cdd:pfam00270 2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKldnGPQALVLAPTRELAEQIYEELkkLGKGLGLKVASLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 94 DVSINADAE------IVVMTTEVLRNMIYaDSPALDRLTHVVMDEIHFLADASRGAVWEEVILNLADHVSIIGLSATVSN 167
Cdd:pfam00270 82 GDSRKEQLEklkgpdILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATLPR 160
|
...
gi 552765374 168 SEE 170
Cdd:pfam00270 161 NLE 163
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
18-190 |
2.00e-23 |
|
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: 98.59 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 18 DEFQVQGCEAVENGQGVLVCAPTGAGKTVVGEFAVSLALSRGTK--CFYTTPIKALSNQKYHDLVAEH-------GDDAV 88
Cdd:cd18025 3 DAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDgvVVYVAPTKALVNQVVAEVYARFskkyppsGKSLW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 89 GLLTGDVSINA--DAEIVVMTTEVLRNMIYADSPA--LDRLTHVVMDEIHFLADASRGAVWEEvILNLADhVSIIGLSAT 164
Cdd:cd18025 83 GVFTRDYRHNNpmNCQVLITVPECLEILLLSPHNAswVPRIKYVIFDEIHSIGQSEDGAVWEQ-LLLLIP-CPFLALSAT 160
|
170 180 190
....*....|....*....|....*....|
gi 552765374 165 VSNSEEFGEWLATVRGDTSV----IVTEHR 190
Cdd:cd18025 161 IGNPQKFHEWLQSVQRARKAelkkIEHNHR 190
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
27-191 |
2.19e-20 |
|
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: 90.49 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 27 AVENGQGVLVCAPTGAGKTVVGEFAV------SLALSRG-TKCFYTTPIKALSNQKYHDLVAEHGDDA--VGLLTGDVSI 97
Cdd:cd18023 13 LLYSDKNFVVSAPTGSGKTVLFELAIlrllkeRNPLPWGnRKVVYIAPIKALCSEKYDDWKEKFGPLGlsCAELTGDTEM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 98 N-----ADAEIVVMTTEVLRNMI--YADSPALDRLTHVVM-DEIHFLADaSRGAVWEEVILNL-------------ADHV 156
Cdd:cd18023 93 DdtfeiQDADIILTTPEKWDSMTrrWRDNGNLVQLVALVLiDEVHIIKE-NRGATLEVVVSRMktlsssselrgstVRPM 171
|
170 180 190
....*....|....*....|....*....|....*
gi 552765374 157 SIIGLSATVSNSEEFGEWLATVRGDTSVIVTEHRP 191
Cdd:cd18023 172 RFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
31-164 |
2.04e-19 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 85.53 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 31 GQGVLVCAPTGAGKTVVGE-FAVSLALSRGTKCFYTTPIKALSNQKYHDLVAEHGDDA-VGLLTGDVS-------INADA 101
Cdd:cd00046 1 GENVLITAPTGSGKTLAALlAALLLLLKKGKKVLVLVPTKALALQTAERLRELFGPGIrVAVLVGGSSaeereknKLGDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552765374 102 EIVVMTTEVLRNMI-YADSPALDRLTHVVMDEIHFLADASRGAV-WEEVILNLADH-VSIIGLSAT 164
Cdd:cd00046 81 DIIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRGALiLDLAVRKAGLKnAQVILLSAT 146
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
31-175 |
2.62e-16 |
|
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: 77.24 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 31 GQGVLVCAPTGAGKTvvgEFAVSLALSR-------GTKCFYTTPIKALSNQKY---HDLVAEHGDD-AVGLLTGDVS--- 96
Cdd:cd17922 1 GRNVLIAAPTGSGKT---EAAFLPALSSladepekGVQVLYISPLKALINDQErrlEEPLDEIDLEiPVAVRHGDTSqse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 97 ----INADAEIVVMTTEVLRNMIyaDSPALDR----LTHVVMDEIHFLADASRGaVWEEVILNLADHVSI-----IGLSA 163
Cdd:cd17922 78 kakqLKNPPGILITTPESLELLL--VNKKLRElfagLRYVVVDEIHALLGSKRG-VQLELLLERLRKLTGrplrrIGLSA 154
|
170
....*....|..
gi 552765374 164 TVSNSEEFGEWL 175
Cdd:cd17922 155 TLGNLEEAAAFL 166
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
34-175 |
7.58e-16 |
|
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: 76.64 E-value: 7.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 34 VLVCAPTGAGKTVVGEFAVSLALSR--GTKCFYTTPIKALSNQKYHD----LVAEHGDDAVGlLTGDVSIN----ADAEI 103
Cdd:cd18022 20 VLLGAPTGSGKTIAAELAMFRAFNKypGSKVVYIAPLKALVRERVDDwkkrFEEKLGKKVVE-LTGDVTPDmkalADADI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 104 VVMTTE----VLRNmiYADSPALDRLTHVVMDEIHFLADaSRGAVWeEVILNLADHVS--------IIGLSATVSNSEEF 171
Cdd:cd18022 99 IITTPEkwdgISRS--WQTREYVQQVSLIIIDEIHLLGS-DRGPVL-EVIVSRMNYISsqtekpvrLVGLSTALANAGDL 174
|
....
gi 552765374 172 GEWL 175
Cdd:cd18022 175 ANWL 178
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
34-175 |
4.46e-15 |
|
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: 74.60 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 34 VLVCAPTGAGKTVVGEFAVSLALSRGT--KCFYTTPIKALSNQKYHD---LVAEHGDDAVGLLTGDVSIN----ADAEIV 104
Cdd:cd18021 22 VFVGAPTGSGKTVCAELALLRHWRQNPkgRAVYIAPMQELVDARYKDwraKFGPLLGKKVVKLTGETSTDlkllAKSDVI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 105 VMTTE---VL------RNMIyadspalDRLTHVVMDEIHFLAdASRGAVWEEVI-------LNLADHVSIIGLSATVSNS 168
Cdd:cd18021 102 LATPEqwdVLsrrwkqRKNV-------QSVELFIADELHLIG-GENGPVYEVVVsrmryisSQLEKPIRIVGLSSSLANA 173
|
....*..
gi 552765374 169 EEFGEWL 175
Cdd:cd18021 174 RDVGEWL 180
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
20-200 |
6.89e-14 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 76.05 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 20 FQVQGCEAVENGQGVLVCAPTGAGKTVVGEFAVSLAL-------SRGTKCFYTTPIKALSNQKYHDL---VAEHGDD-AV 88
Cdd:TIGR04121 17 FQLEMWAAALEGRSGLLIAPTGSGKTLAGFLPSLIDLagpeapkEKGLHTLYITPLRALAVDIARNLqapIEELGLPiRV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 89 GLLTGDVSINADA-------EIVVMTTEVLRNMI-YADSPALDR-LTHVVMDEIHFLADASRGAVWEeviLNLA------ 153
Cdd:TIGR04121 97 ETRTGDTSSSERArqrkkppDILLTTPESLALLLsYPDAARLFKdLRCVVVDEWHELAGSKRGDQLE---LALArlrrla 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 552765374 154 DHVSIIGLSATVSNSEEFGEWLATVRGDTSVIVTEHRPVPLDQWMML 200
Cdd:TIGR04121 174 PGLRRWGLSATIGNLEEARRVLLGVGGAPAVLVRGKLPKAIEVISLL 220
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
19-176 |
9.55e-13 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 72.44 E-value: 9.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 19 EFQVQGCEAVENGQGVLVCAPTGAGKT------VVGEFA---VSLALSRGTKCFYTTPIKALSNqkyhDL-------VAE 82
Cdd:COG1201 27 PPQREAWPAIAAGESTLLIAPTGSGKTlaaflpALDELArrpRPGELPDGLRVLYISPLKALAN----DIernlrapLEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 83 HGDDA--------VGLLTGDVSINADA-------EIVVMTTEVLRNMI-YADSPA-LDRLTHVVMDEIHFLADASRGAvw 145
Cdd:COG1201 103 IGEAAglplpeirVGVRTGDTPASERQrqrrrppHILITTPESLALLLtSPDARElLRGVRTVIVDEIHALAGSKRGV-- 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 552765374 146 eEVILNLA-------DHVSIIGLSATVSNSEEFGEWLA 176
Cdd:COG1201 181 -HLALSLErlralapRPLQRIGLSATVGPLEEVARFLV 217
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
28-191 |
2.99e-12 |
|
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: 66.47 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 28 VENGQGVLVCAPTGAGKTVVGE-FAVSLALSRGTKCFYTTPIKALSNQK----------YHDLVAEHGDDAVGLLTGDVS 96
Cdd:cd18026 30 LLEGRNLVYSLPTSGGKTLVAEiLMLKRLLERRKKALFVLPYVSIVQEKvdalsplfeeLGFRVEGYAGNKGRSPPKRRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 97 inaDAEIVVMTTE----VLRNMIYADSpaLDRLTHVVMDEIHFLADASRGAVWEEVILNL----ADHVSIIGLSATVSNS 168
Cdd:cd18026 110 ---SLSVAVCTIEkansLVNSLIEEGR--LDELGLVVVDELHMLGDGHRGALLELLLTKLlyaaQKNIQIVGMSATLPNL 184
|
170 180
....*....|....*....|...
gi 552765374 169 EEFGEWLatvrgDTSVIVTEHRP 191
Cdd:cd18026 185 EELASWL-----RAELYTTNFRP 202
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
27-164 |
3.73e-12 |
|
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: 64.63 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 27 AVENGQGVLVCAPTGAGKTVVGeFAVSLALSRGtKCFYTTPIKALSNQKYHDLVAEHGDDAVGLLTGDVSI-NADAEIVV 105
Cdd:cd17926 14 AHKNNRRGILVLPTGSGKTLTA-LALIAYLKEL-RTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGGKKKdFDDANVVV 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 552765374 106 MTTEVLRNMIYADSPALDRLTHVVMDEIHFLADASrgavWEEVILNLADHVsIIGLSAT 164
Cdd:cd17926 92 ATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKT----FSEILKELNAKY-RLGLTAT 145
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
27-175 |
1.67e-10 |
|
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: 61.62 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 27 AVENGQGVLVCAPTGAGKTVVGEFAVSLALSR-----GT------KCFYTTPIKALSNQKYHDL---VAEHGdDAVGLLT 92
Cdd:cd18019 29 AFETDENLLLCAPTGAGKTNVALLTILREIGKhrnpdGTinldafKIVYIAPMKALVQEMVGNFskrLAPYG-ITVAELT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 93 GDVSIN----ADAEIVVMTTE----VLRNMIYADSPALDRLthVVMDEIHFLADaSRGAVWEEVILNL-------ADHVS 157
Cdd:cd18019 108 GDQQLTkeqiSETQIIVTTPEkwdiITRKSGDRTYTQLVRL--IIIDEIHLLHD-DRGPVLESIVARTirqieqtQEYVR 184
|
170
....*....|....*...
gi 552765374 158 IIGLSATVSNSEEFGEWL 175
Cdd:cd18019 185 LVGLSATLPNYEDVATFL 202
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
355-437 |
1.87e-10 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 57.99 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 355 EALSRGFAAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMP-ARTVVLEklikfngeaHVDLTPGQYTQLTGRA 433
Cdd:smart00490 8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIY---------DLPWSPASYIQRIGRA 78
|
....
gi 552765374 434 GRRG 437
Cdd:smart00490 79 GRAG 82
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
19-437 |
4.68e-10 |
|
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: 63.70 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 19 EFQVQGCEAVENGQGVLVCAPTGAGKTVVgeFAV----SLALSRGTKCFYTTPIKALSN---QKYHDLVAEHGDDA-VGL 90
Cdd:COG1205 59 SHQAEAIEAARAGKNVVIATPTASGKSLA--YLLpvleALLEDPGATALYLYPTKALARdqlRRLRELAEALGLGVrVAT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 91 LTGDVS------INADAEIVVMTTEVLRNMIYADSPA----LDRLTHVVMDEIHfladasrgaVWEEV-----------I 149
Cdd:COG1205 137 YDGDTPpeerrwIREHPDIVLTNPDMLHYGLLPHHTRwarfFRNLRYVVIDEAH---------TYRGVfgshvanvlrrL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 150 LNLADHVS----IIGLSATVSNSEEFGEWLAtvrGDTSVIVTE-HRPVpldqwmmlGRKIYPLFEPEsggqVNSELERRI 224
Cdd:COG1205 208 RRICRHYGsdpqFILASATIGNPAEHAERLT---GRPVTVVDEdGSPR--------GERTFVLWNPP----LVDDGIRRS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 225 QRLEAgdsddgradyksgkgfrararhkgggrsefhgkaggrsgssrpqdryrplgrPEVLKVLQSQDmLPAITFIFSRA 304
Cdd:COG1205 273 ALAEA----------------------------------------------------ARLLADLVREG-LRTLVFTRSRR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 305 GCDgalyqclrsRMVLTTQEEAEEikaivdagvegiPEEDLQVldfrrwrealsrgfAAHHAGMLPAFRHIVEDLFVRGL 384
Cdd:COG1205 300 GAE---------LLARYARRALRE------------PDLADRV--------------AAYRAGYLPEERREIERGLRSGE 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552765374 385 VRAVFATETLALGINMPartvvleklikfngeaHVDLT-----PGQYTQL---TGRAGRRG 437
Cdd:COG1205 345 LLGVVSTNALELGIDIG----------------GLDAVvlagyPGTRASFwqqAGRAGRRG 389
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
28-175 |
2.36e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 61.44 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 28 VENGQGVLVCAPTGAGKTVvgefAVSLA-----LSRGTK--------CFYTTPIKALSNQKYHDL----------VAEHG 84
Cdd:PRK13767 44 IHEGKNVLISSPTGSGKTL----AAFLAiidelFRLGREgeledkvyCLYVSPLRALNNDIHRNLeeplteireiAKERG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 85 DDA----VGLLTGDVSinaDAE----------IVVMTTEVLrnMIYADSPAL-DRLTH---VVMDEIHFLADASRG---A 143
Cdd:PRK13767 120 EELpeirVAIRTGDTS---SYEkqkmlkkpphILITTPESL--AILLNSPKFrEKLRTvkwVIVDEIHSLAENKRGvhlS 194
|
170 180 190
....*....|....*....|....*....|...
gi 552765374 144 VWEEVILNLADHVSI-IGLSATVSNSEEFGEWL 175
Cdd:PRK13767 195 LSLERLEELAGGEFVrIGLSATIEPLEEVAKFL 227
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
20-167 |
2.95e-09 |
|
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: 57.83 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 20 FQVQGCEAVENGQGVLVCAPTGAGKTVVgefAVSLA--LSRGTKCFYTTPIKALSNQKyhDLVAEH--------GDDA-- 87
Cdd:cd17927 6 YQLELAQPALKGKNTIICLPTGSGKTFV---AVLICehHLKKFPAGRKGKVVFLANKV--PLVEQQkevfrkhfERPGyk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 88 VGLLTGDVSIN-------ADAEIVVMTTEVLRNMI-YADSPALDRLTHVVMDEIHflaDASRGAVWEEVILNLADHVS-- 157
Cdd:cd17927 81 VTGLSGDTSENvsveqivESSDVIIVTPQILVNDLkSGTIVSLSDFSLLVFDECH---NTTKNHPYNEIMFRYLDQKLgs 157
|
170
....*....|....*.
gi 552765374 158 ------IIGLSATVSN 167
Cdd:cd17927 158 sgplpqILGLTASPGV 173
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
35-170 |
8.94e-09 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 59.36 E-value: 8.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 35 LVCAPTGAGKTVVGEFAVSLALSR-GTKCFYTTPIKALSNQKYHDL--VAEHGDDAVGLLTGDVSIN------ADAEIVV 105
Cdd:COG1111 21 LVVLPTGLGKTAVALLVIAERLHKkGGKVLFLAPTKPLVEQHAEFFkeALNIPEDEIVVFTGEVSPEkrkelwEKARIIV 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552765374 106 MTTEVLRNMIYADSPALDRLTHVVMDEIH---------FLAdasrgavweEVILNLADHVSIIGLSATVSNSEE 170
Cdd:COG1111 101 ATPQVIENDLIAGRIDLDDVSLLIFDEAHravgnyayvYIA---------ERYHEDAKDPLILGMTASPGSDEE 165
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
10-164 |
1.20e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 58.88 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 10 AAGLPYPLDEFQVqgcEAVE--------NGQGVLVCAPTGAGKTVVGEFAVSlALSRGTKCFYTTPIKALSNQKYHDLVA 81
Cdd:COG1061 74 ASGTSFELRPYQQ---EALEallaalerGGGRGLVVAPTGTGKTVLALALAA-ELLRGKRVLVLVPRRELLEQWAEELRR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 82 EHGDDAVglltGDVSINADAEIVVMTTEVLRNMIYADSPAlDRLTHVVMDEIHFLADASrgavWEEvILNLADHVSIIGL 161
Cdd:COG1061 150 FLGDPLA----GGGKKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPS----YRR-ILEAFPAAYRLGL 219
|
...
gi 552765374 162 SAT 164
Cdd:COG1061 220 TAT 222
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
27-167 |
5.26e-08 |
|
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: 53.97 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 27 AVENGQGVLVCAPTGAGKTVVGEFAVSLALSRGT-----------KCFYTTPIKALSNQ---KYHDLVAEHGdDAVGLLT 92
Cdd:cd18020 13 AYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVnqggvikkddfKIVYIAPMKALAAEmveKFSKRLAPLG-IKVKELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 93 GDVSIN----ADAEIVVMTTE---VLRNMIYADSPALDRLTHVVMDEIHFLADaSRGAVWEEVILNLADHVS-------I 158
Cdd:cd18020 92 GDMQLTkkeiAETQIIVTTPEkwdVVTRKSSGDVALSQLVRLLIIDEVHLLHD-DRGPVIESLVARTLRQVEstqsmirI 170
|
....*....
gi 552765374 159 IGLSATVSN 167
Cdd:cd18020 171 VGLSATLPN 179
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
17-166 |
6.95e-08 |
|
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: 54.02 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 17 LDEFQVQGCEAVENGQGVLVCAPTGAGKTVVGEFAVSLALSRGTKCFYTTPIKALSNQ----------------KYHDLV 80
Cdd:cd18036 3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVNKvplveqqlekffkyfrKGYKVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 81 AEHGDDAVGLLTGDVSINADaeIVVMTTEVLRNMIYA----DSPALDRLTHVVMDEIHflaDASRGAVWEEVILNLADHV 156
Cdd:cd18036 83 GLSGDSSHKVSFGQIVKASD--VIICTPQILINNLLSgreeERVYLSDFSLLIFDECH---HTQKEHPYNKIMRMYLDKK 157
|
170
....*....|....*...
gi 552765374 157 --------SIIGLSATVS 166
Cdd:cd18036 158 lssqgplpQILGLTASPG 175
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
19-173 |
7.51e-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: 53.36 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 19 EFQVQGCEAVENGQGVLVCAPTGAGKTVVGEFAV--SLALSRGTKCFYTTPIKALSN---QKYHDLVAEHGDD-AVGLLT 92
Cdd:cd17923 3 SHQAEAIEAARAGRSVVVTTGTASGKSLCYQLPIleALLRDPGSRALYLYPTKALAQdqlRSLRELLEQLGLGiRVATYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 93 GDVSINA-------DAEIVVMTTEVLRNMI----YADSPALDRLTHVVMDEIHfladASRGAVWEEV------ILNLAD- 154
Cdd:cd17923 83 GDTPREErraiirnPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEAH----TYRGVFGSHValllrrLRRLCRr 158
|
170 180
....*....|....*....|..
gi 552765374 155 ---HVSIIGLSATVSNSEEFGE 173
Cdd:cd17923 159 ygaDPQFILTSATIGNPAEHAR 180
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
390-439 |
2.06e-07 |
|
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: 51.02 E-value: 2.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 552765374 390 ATETLALGINMPARTVVLEKLIKFNGEAHVDLTPGQYTQLTGRAGRRGID 439
Cdd:cd18805 76 ASDAIGMGLNLNIRRVIFSSLSKFDGNEMRPLSPSEVKQIAGRAGRFGSH 125
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
32-171 |
9.25e-07 |
|
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to 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: 438707 [Multi-domain] Cd Length: 159 Bit Score: 49.38 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 32 QGVLVCAPTGAGKTV-VGEFAVSLALSRGTKC--FYTTP--IKALSNQKYhdlVAEHGDDAVGLLTG-----DVSINADA 101
Cdd:cd17917 2 QVVVIVGETGSGKTTqVPQFLLEDGLAKGGKGriVCTQPrrIAAISVAER---VAEERGEKLGEEVGyqirfESKTSSKT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552765374 102 EIVVMTTEVLRNMIYADsPALDRLTHVVMDEIHF---LADASRGAVweEVILNLADHVSIIGLSATVsNSEEF 171
Cdd:cd17917 79 RIKFCTDGILLRELLSD-PLLSGYSHVILDEAHErslDTDFLLGLL--KDLLRKRPDLKVILMSATL-DAEKF 147
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
34-102 |
1.33e-06 |
|
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: 49.60 E-value: 1.33e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552765374 34 VLVCAPTGAGKTvvgEFAVSLAL-----SRGTKCFYTTPIKALSNQKYHDLV----AEHGDDAVGLLTGDVSINADAE 102
Cdd:cd17930 4 VILEAPTGSGKT---EAALLWALklaarGGKRRIIYALPTRATINQMYERIReilgRLDDEDKVLLLHSKAALELLES 78
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
348-437 |
1.63e-06 |
|
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: 47.59 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 348 LDFRRWREALSRGFAAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMPARTVVleklIKFNgeahVDLTPGQYT 427
Cdd:pfam00271 28 LEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLV----INYD----LPWNPASYI 99
|
90
....*....|
gi 552765374 428 QLTGRAGRRG 437
Cdd:pfam00271 100 QRIGRAGRAG 109
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
3-164 |
3.06e-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: 50.85 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 3 ETHLDTFAAgLPYPLDEFQVQ----GCEAVENGQG-VLVCAPTGAGKTvvgEFAVSLAL-----SRGTKCFYTTPIKALS 72
Cdd:COG1203 115 ERLLPKKSK-PRTPINPLQNEalelALEAAEEEPGlFILTAPTGGGKT---EAALLFALrlaakHGGRRIIYALPFTSII 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 73 NQKYhDLVAEHGDDAVGLLTGDVSINA---------------------DAEIVVMTTEVLRNMIYADSPALDRLTH---- 127
Cdd:COG1203 191 NQTY-DRLRDLFGEDVLLHHSLADLDLleeeeeyesearwlkllkelwDAPVVVTTIDQLFESLFSNRKGQERRLHnlan 269
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 552765374 128 --VVMDEIHFLADASRGAVweEVILNLADH--VSIIGLSAT 164
Cdd:COG1203 270 svIILDEVQAYPPYMLALL--LRLLEWLKNlgGSVILMTAT 308
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
17-187 |
7.12e-06 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350831 [Multi-domain] Cd Length: 202 Bit Score: 47.89 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 17 LDEFQVQGCEAVENGQGVLVCAPTGAGKTVvgefaVSLALS-----------RGTKCFYTTPIKALSNQKyhDLVAEHGD 85
Cdd:cd18073 3 PRNYQLELALPAMKGKNTIICAPTGCGKTF-----VSLLICehhlkkfpqgqKGKVVFFATKVPVYEQQK--SVFSKYFE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 86 DA---VGLLTGDVSINA-------DAEIVVMTTEVLRNMIY-ADSPALDRLTHVVMDEIHflaDASRGAVWEEVILNLAD 154
Cdd:cd18073 76 RHgyrVTGISGATAENVpveqiieNNDIIILTPQILVNNLKkGTIPSLSIFTLMIFDECH---NTSGNHPYNMIMFRYLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 552765374 155 HV---------SIIGLSATV-----SNSEEFGEWLATVRG--DTSVIVT 187
Cdd:cd18073 153 QKlggssgplpQIIGLTASVgvgdaKNTDEALDYICKLCAslDASVIAT 201
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
26-164 |
8.76e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.90 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 26 EAVENGQ-GVLVCAPTGAGKTVVGEFAVSLALSRGT--KCFYTTPIKALSNQKYHDL--VAEHGDDAVGLLTGD--VSIN 98
Cdd:pfam04851 17 ESIKNGQkRGLIVMATGSGKTLTAAKLIARLFKKGPikKVLFLVPRKDLLEQALEEFkkFLPNYVEIGEIISGDkkDESV 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552765374 99 ADAEIVVMTTEVL--RNMIYADSPALDRLTHVVMDEIHFLADASrgavWEEVILNLaDHVSIIGLSAT 164
Cdd:pfam04851 97 DDNKIVVTTIQSLykALELASLELLPDFFDVIIIDEAHRSGASS----YRNILEYF-KPAFLLGLTAT 159
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
9-164 |
1.10e-05 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 47.03 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 9 FAAGLPYPLDEFQVQGCEAVENG--QGV----LVCAPTGAGKTVVGEFAVSLALSRGTKCFYTTPIKALSNQKYHDLVAE 82
Cdd:cd17918 8 LCKSLPFSLTKDQAQAIKDIEKDlhSPEpmdrLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARKF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 83 HGDDAVGLLTGDV--SINADAEIVVMTTEVlrnmIYADSPALDrLTHVVMDEIHFLADASRGAvweeviLNLADHVSIIG 160
Cdd:cd17918 88 LPFINVELVTGGTkaQILSGISLLVGTHAL----LHLDVKFKN-LDLVIVDEQHRFGVAQREA------LYNLGATHFLE 156
|
....
gi 552765374 161 LSAT 164
Cdd:cd17918 157 ATAT 160
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
362-451 |
1.62e-05 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129701 [Multi-domain] Cd Length: 470 Bit Score: 48.61 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 362 AAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMP-ARTVVleklikfngeaHVDLTPG--QYTQLTGRAGRRGI 438
Cdd:TIGR00614 254 GAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPdVRFVI-----------HYSLPKSmeSYYQESGRAGRDGL 322
|
90
....*....|...
gi 552765374 439 DTlgNAVVQWAPA 451
Cdd:TIGR00614 323 PS--ECHLFYAPA 333
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
26-174 |
4.99e-05 |
|
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as G4-resolvase 1 or G4R1, MLE-like protein 1 and RNA helicase associated with AU-rich element or RHAU) unwinds a G4-quadruplex in human telomerase RNA. DHX36 belongs to 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: 350739 [Multi-domain] Cd Length: 180 Bit Score: 44.83 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 26 EAVENGQGVLVCAPTGAGKTV-VGEFAVSLALSRG--TKCFY--TTP--IKALSNQKYhdLVAEHGDD-AVGLLTGdVSI 97
Cdd:cd17981 12 NMIDNNQVTVISGETGCGKTTqVTQFILDDAIERGkgSSCRIvcTQPrrISAISVAER--VAAERAEScGLGNSTG-YQI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 98 NAD-------AEIVVMTTEVLRNMIYADsPALDRLTHVVMDEIH---FLADASRGAVweEVILNLADHVSIIGLSATVsN 167
Cdd:cd17981 89 RLEsrkprkqGSILYCTTGIVLQWLQSD-PHLSNVSHLVLDEIHernLQSDVLMGIV--KDLLPFRSDLKVILMSATL-N 164
|
....*..
gi 552765374 168 SEEFGEW 174
Cdd:cd17981 165 AEKFSDY 171
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
358-438 |
7.43e-05 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 46.63 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 358 SRGF--AAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMPARTVVLEKLIKFNGEAhvdltpgqYTQLTGRAGR 435
Cdd:PRK11057 258 SRGIsaAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES--------YYQETGRAGR 329
|
...
gi 552765374 436 RGI 438
Cdd:PRK11057 330 DGL 332
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
16-134 |
8.52e-05 |
|
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to 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: 350745 [Multi-domain] Cd Length: 176 Bit Score: 44.05 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 16 PLDEFQVQGCEAVENGQGVLVCAPTGAGKTV-VGEFAVSLALSRGTKC--FYTTPiKALSNQKYHDLVAEHGDDAVGLLT 92
Cdd:cd17987 2 PVFEKQEQIVRIIKENKVVLIVGETGSGKTTqIPQFLLDDCYANGIPCriFCTQP-RRLAAIAVAERVAAERGEKIGQTV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 552765374 93 G-----DVSINADAEIVVMTTEVLRNMIYADSPALDRLTHVVMDEIH 134
Cdd:cd17987 81 GyqirlESRVSPKTLLTFCTNGVLLRTLMAGDSALSTVTHVIVDEVH 127
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
26-168 |
8.68e-05 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to 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: 438711 [Multi-domain] Cd Length: 174 Bit Score: 44.24 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 26 EAVENGQGVLVCAPTGAGKTVVGEFAVSLALS-RGTKCFYTTP--IKALS-NQKYHDLVAEHGDDAVGL-LTGDVSINAD 100
Cdd:cd17990 12 AALDAGGQVVLEAPPGAGKTTRVPLALLAELWiAGGKIIVLEPrrVAARAaARRLATLLGEAPGETVGYrVRGESRVGRR 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552765374 101 AEIVVMTTEVLRNMIYADsPALDRLTHVVMDEIH---FLADASRGAVWeEVILNLADHVSIIGLSATVSNS 168
Cdd:cd17990 92 TRVEVVTEGVLLRRLQRD-PELSGVGAVILDEFHersLDADLALALLL-EVQQLLRDDLRLLAMSATLDGD 160
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
27-177 |
9.66e-05 |
|
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to 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: 350746 [Multi-domain] Cd Length: 180 Bit Score: 44.03 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 27 AVENGQGVLVCAPTGAGKTV-VGEFAVSLALSRGTKC--FYTTP--IKALSNQKYhdlVAEHGDDAVGLLTG-DVSI--- 97
Cdd:cd17988 13 LIEANSVVIIKGATGCGKTTqLPQFILDHYYKRGKYCniVVTQPrrIAAISIARR---VSQEREWTLGSLVGyQVGLerp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 98 -NADAEIVVMTTEVLRNMIyADSPALDRLTHVVMDEIH-------FLAdasrgAVWEEVILNLADHVSIIGLSATVSnSE 169
Cdd:cd17988 90 aSEETRLIYCTTGVLLQKL-INNKTLTEYTHIILDEVHerdqeldFLL-----LVVRRLLRTNSRHVKIILMSATIS-CK 162
|
....*...
gi 552765374 170 EFGEWLAT 177
Cdd:cd17988 163 EFADYFTT 170
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
35-170 |
1.04e-04 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 46.02 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 35 LVCAPTGAGKTVVGEF-AVSLALSRGTKCFYTTPIKALSNQKYHDL--VAEHGDDAVGLLTGDVS------INADAEIVV 105
Cdd:PRK13766 33 LVVLPTGLGKTAIALLvIAERLHKKGGKVLILAPTKPLVEQHAEFFrkFLNIPEEKIVVFTGEVSpekraeLWEKAKVIV 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552765374 106 MTTEVLRNMIYADSPALDRLTHVVMDEIH---------FLAdasrgavweEVILNLADHVSIIGLSATVSNSEE 170
Cdd:PRK13766 113 ATPQVIENDLIAGRISLEDVSLLIFDEAHravgnyayvYIA---------ERYHEDAKNPLVLGLTASPGSDEE 177
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
358-435 |
1.42e-04 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 45.52 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 358 SRGF--AAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMP-ARTVVleklikfngeaHVDLtPGQ---YTQLTG 431
Cdd:COG0514 252 EAGIraAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPdVRFVI-----------HYDL-PKSieaYYQEIG 319
|
....
gi 552765374 432 RAGR 435
Cdd:COG0514 320 RAGR 323
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
36-184 |
2.43e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 45.30 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 36 VCAPTGAGKTVVgefAVSLALSR----------------GTKCFYTTPIKALSNQ-------KYHDLVAEH---GDDAV- 88
Cdd:PRK09751 1 VIAPTGSGKTLA---AFLYALDRlfreggedtreahkrkTSRILYISPIKALGTDvqrnlqiPLKGIADERrrrGETEVn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 89 ---GLLTGDVSINADA-------EIVVMTTEVLRNMIYADS-PALDRLTHVVMDEIHFLADASRGA----VWEEVILNLA 153
Cdd:PRK09751 78 lrvGIRTGDTPAQERSkltrnppDILITTPESLYLMLTSRArETLRGVETVIIDEVHAVAGSKRGAhlalSLERLDALLH 157
|
170 180 190
....*....|....*....|....*....|.
gi 552765374 154 DHVSIIGLSATVSNSEEFGEWLATVRGDTSV 184
Cdd:PRK09751 158 TSAQRIGLSATVRSASDVAAFLGGDRPVTVV 188
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
361-437 |
4.82e-04 |
|
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: 41.48 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 361 FAAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMPartvvleklikfngeaHVDLTPgQYT---------QLTG 431
Cdd:cd18796 71 IALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIG----------------DVDLVI-QIGspksvarllQRLG 133
|
....*.
gi 552765374 432 RAGRRG 437
Cdd:cd18796 134 RSGHRP 139
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
361-437 |
1.44e-03 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 39.88 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 361 FAAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMP-ARTVVleklikfngeaHVDLtPGQ---YTQLTGRAGRR 436
Cdd:cd18794 57 AAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPdVRFVI-----------HYSL-PKSmesYYQESGRAGRD 124
|
.
gi 552765374 437 G 437
Cdd:cd18794 125 G 125
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
362-441 |
1.87e-03 |
|
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: 39.55 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 362 AAHHAGMLPAFRHIVEDLFVRGLVRAVFATETLALGINMPARTVVLekLIKFngeahvdltPGQYT---QLTGRAGRRGI 438
Cdd:cd18797 70 ASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVV--LAGY---------PGSLAslwQQAGRAGRRGK 138
|
...
gi 552765374 439 DTL 441
Cdd:cd18797 139 DSL 141
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
34-232 |
2.12e-03 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 41.29 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 34 VLVCAPTGAGKTvvgEFAVSLAL-----SRGTKCFYTTPIKALSNQKYHDLVAEHGDDAVGLLTGDVSINADAEIVVMTT 108
Cdd:TIGR01587 2 LVIEAPTGYGKT---EAALLWALhsiksQKADRVIIALPTRATINAMYRRAKELFGSELVGLHHSSSFSRIKEMGDSEEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 109 EVLRNMIYADSPAL----------DRL--------------------THVVMDEIHFLADASRGavweeVILNLADH--- 155
Cdd:TIGR01587 79 EHLFPLYIHSNDKLfldpitvctiDQVlksvfgefghyeftlasianSLLIFDEVHFYDEYTLA-----LILAVLEVlkd 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 156 --VSIIGLSATVSNS-EEFGEwlatvrgdTSVIVTEHRPVPLDQWMMLGRKIYPLFEPESGGQVNSeLERRIQRLEAGDS 232
Cdd:TIGR01587 154 ndVPILLMSATLPKFlKEYAE--------KIGYVEFNEPLDLKEERRFENHRFILIESDKVGEISS-LERLLEFIKKGGS 224
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
28-159 |
4.17e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.48 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 28 VENGQGVL-VCAPTGAGKTVVGEFAVSLALSRGTKCFYTTPiKALSNQK--YHDLVAEHGDDAVGLLTgdvsinadaeiv 104
Cdd:pfam13401 1 IRFGAGILvLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDL-PSGTSPKdlLRALLRALGLPLSGRLS------------ 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 552765374 105 vmtTEVLRNMIYADSPALDRLTHVVMDEIHFLadasRGAVWEEV--ILNLADH-VSII 159
Cdd:pfam13401 68 ---KEELLAALQQLLLALAVAVVLIIDEAQHL----SLEALEELrdLLNLSSKlLQLI 118
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
35-164 |
4.92e-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: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 35 LVCAPTGAGKTVVgefAVSLALSR----GTKCFYTTPIKALSNQKYHDLV-AEHGDDAVGLLTGDVSINADAE------I 103
Cdd:cd18035 20 LIVLPTGLGKTII---AILVAADRltkkGGKVLILAPSRPLVEQHAENLKrVLNIPDKITSLTGEVKPEERAErwdaskI 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552765374 104 VVMTTEVLRNMIYADSPALDRLTHVVMDEIHFLADASRGAVWEEVILNLADHVSIIGLSAT 164
Cdd:cd18035 97 IVATPQVIENDLLAGRITLDDVSLLIFDEAHHAVGNYAYVYIAHRYKREANNPLILGLTAS 157
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
32-134 |
6.50e-03 |
|
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: 38.79 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 32 QGVLVCAPTGAGKTVVgefAVSL---------ALSRGTK-CFYTTPIKALSNQKYhDLVAEHGDDAVGLLTGDVSIN--- 98
Cdd:cd18034 17 RNTIVVLPTGSGKTLI---AVMLikemgelnrKEKNPKKrAVFLVPTVPLVAQQA-EAIRSHTDLKVGEYSGEMGVDkwt 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 552765374 99 --------ADAEIVVMTTEVLRNMI---YADspaLDRLTHVVMDEIH 134
Cdd:cd18034 93 kerwkeelEKYDVLVMTAQILLDALrhgFLS---LSDINLLIFDECH 136
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
30-132 |
6.60e-03 |
|
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: 38.72 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 30 NGQGVLVCAPTGAGKTVVgeFAVSLALS-------RGTKCFYTTPIKALSNQKYHDL-----------VAEHGDDAVGLL 91
Cdd:cd17957 26 HGRDLLACAPTGSGKTLA--FLIPILQKlgkprkkKGLRALILAPTRELASQIYRELlklskgtglriVLLSKSLEAKAK 103
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 552765374 92 TGDVSINaDAEIVVMTTEVLRNMIYADSPALDRLTHVVMDE 132
Cdd:cd17957 104 DGPKSIT-KYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDE 143
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
38-164 |
9.85e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 38.08 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765374 38 APTGAGKTVVGEFAVSLALSRGTKCFYTTPIKALSNQKYHDL--VAEHGDDAVGLLTGDVSINA-------------DAE 102
Cdd:cd17924 39 APTGVGKTTFGLATSLYLASKGKRSYLIFPTKSLVKQAYERLskYAEKAGVEVKILVYHSRLKKkekeellekiekgDFD 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552765374 103 IVVMTTEVLRNmiYADSPALDRLTHVVMDEIHFLADASRGAvweEVILNLADHVSIIGLSAT 164
Cdd:cd17924 119 ILVTTNQFLSK--NFDLLSNKKFDFVFVDDVDAVLKSSKNI---DRLLKLLGFGQLVVSSAT 175
|
|
| |
