|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
761-938 |
1.88e-114 |
|
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: 359.76 E-value: 1.88e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 761 IPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESDEGVVVYVAPTKALVNQVAATVEYRYAKNM-PAGES 839
Cdd:cd18025 1 NPDAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYpPSGKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 840 LCGVFTRDYRHD-ALNCQVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIRCPFLALSAT 918
Cdd:cd18025 81 LWGVFTRDYRHNnPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWEQLLLLIPCPFLALSAT 160
|
170 180
....*....|....*....|
gi 657940862 919 ISNPQHLTEWLQSVKRYWKQ 938
Cdd:cd18025 161 IGNPQKFHEWLQSVQRARKA 180
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
766-1440 |
1.50e-39 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 155.82 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 766 QRELLD-VVDNYESAVIVAPTSSGKTYASYYCMEKVLKESdeGVVVYVAPTKALVNQVAATVEYRYAKNmpaGESLcGVF 844
Cdd:COG1204 27 QAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNG--GKALYIVPLRALASEKYREFKRDFEEL---GIKV-GVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 845 TRDYRHDAL---NCQVLITVPACFEILLLapHRQNWVKRIRYVIFDEVHCLG-GEIGAEIwEHLLVMIR--CP---FLAL 915
Cdd:COG1204 101 TGDYDSDDEwlgRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTL-EVLLARLRrlNPeaqIVAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 916 SATISNPQHLTEWLQSvkrywKQVDSTmeERTVSKRTGtsrgsyykdqaqarqsykvrlVLYGERYNDLEKYLCSVRQGd 995
Cdd:COG1204 178 SATIGNAEEIAEWLDA-----ELVKSD--WRPVPLNEG---------------------VLYDGVLRFDDGSRRSKDPT- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 996 vcfdhfhpcAALTIDHIEKYGfpsdlalspresiqlydtmcqvwkswpqaQSLCpenftqFKNKivikkldaRKYEESLK 1075
Cdd:COG1204 229 ---------LALALDLLEEGG-----------------------------QVLV------FVSS--------RRDAESLA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1076 EEFTNWVKNGNEEEARmvlkklspdyhehsgrmldffpclveklrkmeklpalfflfklnivEECAENAFEFLEKKQEek 1155
Cdd:COG1204 257 KKLADELKRRLTPEER----------------------------------------------EELEELAEELLEVSEE-- 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1156 rppkadkearttanklrkvkkslekqktvdekgqkssrrldesvMHEtehnyllqtleknleipkdctyanqkaiddqll 1235
Cdd:COG1204 289 --------------------------------------------THT--------------------------------- 291
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1236 qrvfhrvrferkGETLKRLAERGIGYHHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFA----QNSVY 1311
Cdd:COG1204 292 ------------NEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRdtkrGGMVP 359
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1312 LDALNYRQMSGRAGRRGQDLLGDVYFFDIPLPKIGKL----IKSKVPELRGQfpLSISLILRLMLLAS----KADDLEDg 1383
Cdd:COG1204 360 IPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDEADELferyILGEPEPIRSK--LANESALRTHLLALiasgFANSREE- 436
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1384 kakALSVLKHSLLSFKQPRaiDMLKLYFLYSLQFLVKEGHIDQEGN---PTGFAGLVSHL 1440
Cdd:COG1204 437 ---LLDFLENTFYAYQYDK--GDLEEVVDDALEFLLENGFIEEDGDrlrATKLGKLVSRL 491
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1195-1338 |
1.27e-34 |
|
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: 130.37 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1195 LDESVMHETEHNYLLQTLEKNLEIPKDCTYANQKAIDD--QLLqrVFhrvRFERKG--ETLKRLAerGIGYHHSSMSAKE 1270
Cdd:cd18795 5 LEEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEgkPVL--VF---CSSRKEceKTAKDLA--GIAFHHAGLTRED 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657940862 1271 KQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQNSVY-------LDALNYRQMSGRAGRRGQDLLGDVYFF 1338
Cdd:cd18795 78 RELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYdgkgyreLSPLEYLQMIGRAGRPGFDTRGEAIIM 152
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
766-920 |
7.17e-22 |
|
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: 94.23 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 766 QRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESDEGV-VVYVAPTKALVNQVAATVEYRYAKNMPAGESLCGVF 844
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPqALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGD 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657940862 845 TRDYRHDAL-NCQVLITVPacfEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIR--CPFLALSATIS 920
Cdd:pfam00270 84 SRKEQLEKLkGPDILVGTP---GRLLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPkkRQILLLSATLP 159
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
760-951 |
5.75e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 84.08 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 760 FIPDTWQRELLD-VVDNYESAVIVAPTSSGKTYASYYCMEKVLKESDEGVVVYVAPTKALVNQVAATVEYRYAKNmpaGE 838
Cdd:smart00487 7 EPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSL---GL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 839 SLCGVFTRDYRHDAL------NCQVLITVPACFEILLLapHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIR--C 910
Cdd:smart00487 84 KVVGLYGGDSKREQLrklesgKTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPknV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 657940862 911 PFLALSATISNPQHLTEWLqsvkrYWKQVDSTMEERTVSKR 951
Cdd:smart00487 162 QLLLLSATPPEEIENLLEL-----FLNDPVFIDVGFTPLEP 197
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1142-1445 |
3.36e-17 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 87.71 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1142 ENAFEFLEKKQEEKRPPKADkeartTANKLRKvkkslekqkTVDEKGQ----KSSRRLDESvmhetehnyllqtleknle 1217
Cdd:PRK02362 212 GGAIHFDDSQREVEVPSKDD-----TLNLVLD---------TLEEGGQclvfVSSRRNAEG------------------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1218 IPKDCTYANQKAIDDQL---LQRVFHRVRFERKGETLKRLA---ERGIGYHHSSMSAKEKQLVEILFRKGFIRVVTATGT 1291
Cdd:PRK02362 259 FAKRAASALKKTLTAAEraeLAELAEEIREVSDTETSKDLAdcvAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPT 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1292 LALGINMPCKSVV------FAQNS--VYLDALNYRQMSGRAGRRGQDLLG----------------DVYFFDIPLPkigk 1347
Cdd:PRK02362 339 LAAGLNLPARRVIirdyrrYDGGAgmQPIPVLEYHQMAGRAGRPGLDPYGeavllaksydeldelfERYIWADPED---- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1348 lIKSKvpelrgqfpLSISLILRLMLLASKADDLEDGKAKALSVLKHSLLSFKQP------RAIDMlklyflySLQFLVKE 1421
Cdd:PRK02362 415 -VRSK---------LATEPALRTHVLSTIASGFARTRDGLLEFLEATFYATQTDdtgrleRVVDD-------VLDFLERN 477
|
330 340
....*....|....*....|....*..
gi 657940862 1422 GHIDQEGN---PTGFAGLVSHLhYHEP 1445
Cdd:PRK02362 478 GMIEEDGEtleATELGHLVSRL-YIDP 503
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1252-1328 |
1.14e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 70.70 E-value: 1.14e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657940862 1252 KRLAERGIGY--HHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFaQNSVYLDALNYRQMSGRAGRRG 1328
Cdd:smart00490 5 ELLKELGIKVarLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVI-IYDLPWSPASYIQRIGRAGRAG 82
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
766-927 |
3.11e-14 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 78.34 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 766 QRELLDVVDNYESAVIVAPTSSGKTYAsyYC---MEKVLKESDeGVVVYVAPTKALVN-QVAATVEyrYAKNMPAGESlC 841
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLA--YLlpvLEALLEDPG-ATALYLYPTKALARdQLRRLRE--LAEALGLGVR-V 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 842 GVFT----RDYRHDAL-NCQVLITVPacfEIL---LLaPHRQNWV---KRIRYVIFDEVHCLGGEIGAeiweHLLVMIR- 909
Cdd:COG1205 135 ATYDgdtpPEERRWIReHPDIVLTNP---DMLhygLL-PHHTRWArffRNLRYVVIDEAHTYRGVFGS----HVANVLRr 206
|
170 180
....*....|....*....|....*....
gi 657940862 910 ----CP-------FLALSATISNPQHLTE 927
Cdd:COG1205 207 lrriCRhygsdpqFILASATIGNPAEHAE 235
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
777-939 |
2.96e-12 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 71.77 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 777 ESAVIVAPTSSGKTYASYYCM-EKVLKESdeGVVVYVAPTKALvnqvaATVEYRYAKNMPAGESLCGVFTRDY------- 848
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMvNKLLREG--GKAVYLVPLKAL-----AEEKYREFKDWEKLGLRVAMTTGDYdstdewl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 849 -RHDalncqVLITVPACFEILLlaPHRQNWVKRIRYVIFDEVHCLGG-EIGAE---IWEHLLVmiRCPFLALSATISNPQ 923
Cdd:PRK00254 113 gKYD-----IIIATAEKFDSLL--RHGSSWIKDVKLVVADEIHLIGSyDRGATlemILTHMLG--RAQILGLSATVGNAE 183
|
170
....*....|....*...
gi 657940862 924 HLTEWLQS--VKRYWKQV 939
Cdd:PRK00254 184 ELAEWLNAelVVSDWRPV 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1238-1328 |
3.33e-09 |
|
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: 56.06 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1238 VFHRVRFERKGETLKRLAERGIGYHHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFaQNSVYLDALNY 1317
Cdd:pfam00271 20 IFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVI-NYDLPWNPASY 98
|
90
....*....|.
gi 657940862 1318 RQMSGRAGRRG 1328
Cdd:pfam00271 99 IQRIGRAGRAG 109
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
761-938 |
1.88e-114 |
|
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: 359.76 E-value: 1.88e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 761 IPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESDEGVVVYVAPTKALVNQVAATVEYRYAKNM-PAGES 839
Cdd:cd18025 1 NPDAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYpPSGKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 840 LCGVFTRDYRHD-ALNCQVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIRCPFLALSAT 918
Cdd:cd18025 81 LWGVFTRDYRHNnPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWEQLLLLIPCPFLALSAT 160
|
170 180
....*....|....*....|
gi 657940862 919 ISNPQHLTEWLQSVKRYWKQ 938
Cdd:cd18025 161 IGNPQKFHEWLQSVQRARKA 180
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
763-932 |
8.40e-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: 166.28 E-value: 8.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 763 DTWQRELLDVVDNY-ESAVIVAPTSSGKTYASYYCMEKVLKESdEGVVVYVAPTKALVNQVAATVEYRYAKNMpageSLC 841
Cdd:cd17921 3 NPIQREALRALYLSgDSVLVSAPTSSGKTLIAELAILRALATS-GGKAVYIAPTRALVNQKEADLRERFGPLG----KNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 842 GVFTRDYRHDAL---NCQVLITVPACFEILLLAPHrQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIR-----CPFL 913
Cdd:cd17921 78 GLLTGDPSVNKLllaEADILVATPEKLDLLLRNGG-ERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrinknARFV 156
|
170
....*....|....*....
gi 657940862 914 ALSATISNPQHLTEWLQSV 932
Cdd:cd17921 157 GLSATLPNAEDLAEWLGVE 175
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
766-1440 |
1.50e-39 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 155.82 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 766 QRELLD-VVDNYESAVIVAPTSSGKTYASYYCMEKVLKESdeGVVVYVAPTKALVNQVAATVEYRYAKNmpaGESLcGVF 844
Cdd:COG1204 27 QAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNG--GKALYIVPLRALASEKYREFKRDFEEL---GIKV-GVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 845 TRDYRHDAL---NCQVLITVPACFEILLLapHRQNWVKRIRYVIFDEVHCLG-GEIGAEIwEHLLVMIR--CP---FLAL 915
Cdd:COG1204 101 TGDYDSDDEwlgRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTL-EVLLARLRrlNPeaqIVAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 916 SATISNPQHLTEWLQSvkrywKQVDSTmeERTVSKRTGtsrgsyykdqaqarqsykvrlVLYGERYNDLEKYLCSVRQGd 995
Cdd:COG1204 178 SATIGNAEEIAEWLDA-----ELVKSD--WRPVPLNEG---------------------VLYDGVLRFDDGSRRSKDPT- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 996 vcfdhfhpcAALTIDHIEKYGfpsdlalspresiqlydtmcqvwkswpqaQSLCpenftqFKNKivikkldaRKYEESLK 1075
Cdd:COG1204 229 ---------LALALDLLEEGG-----------------------------QVLV------FVSS--------RRDAESLA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1076 EEFTNWVKNGNEEEARmvlkklspdyhehsgrmldffpclveklrkmeklpalfflfklnivEECAENAFEFLEKKQEek 1155
Cdd:COG1204 257 KKLADELKRRLTPEER----------------------------------------------EELEELAEELLEVSEE-- 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1156 rppkadkearttanklrkvkkslekqktvdekgqkssrrldesvMHEtehnyllqtleknleipkdctyanqkaiddqll 1235
Cdd:COG1204 289 --------------------------------------------THT--------------------------------- 291
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1236 qrvfhrvrferkGETLKRLAERGIGYHHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFA----QNSVY 1311
Cdd:COG1204 292 ------------NEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRdtkrGGMVP 359
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1312 LDALNYRQMSGRAGRRGQDLLGDVYFFDIPLPKIGKL----IKSKVPELRGQfpLSISLILRLMLLAS----KADDLEDg 1383
Cdd:COG1204 360 IPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDEADELferyILGEPEPIRSK--LANESALRTHLLALiasgFANSREE- 436
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1384 kakALSVLKHSLLSFKQPRaiDMLKLYFLYSLQFLVKEGHIDQEGN---PTGFAGLVSHL 1440
Cdd:COG1204 437 ---LLDFLENTFYAYQYDK--GDLEEVVDDALEFLLENGFIEEDGDrlrATKLGKLVSRL 491
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1195-1338 |
1.27e-34 |
|
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: 130.37 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1195 LDESVMHETEHNYLLQTLEKNLEIPKDCTYANQKAIDD--QLLqrVFhrvRFERKG--ETLKRLAerGIGYHHSSMSAKE 1270
Cdd:cd18795 5 LEEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEgkPVL--VF---CSSRKEceKTAKDLA--GIAFHHAGLTRED 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657940862 1271 KQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQNSVY-------LDALNYRQMSGRAGRRGQDLLGDVYFF 1338
Cdd:cd18795 78 RELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYdgkgyreLSPLEYLQMIGRAGRPGFDTRGEAIIM 152
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
758-1403 |
8.58e-32 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 134.68 E-value: 8.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 758 QDFIPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESdeGVVVYVAPTKALVNQ-VAATVEyRYaknmpa 836
Cdd:COG4581 22 RGFELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALARG--RRSFYTAPIKALSNQkFFDLVE-RF------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 837 GESLCGVFTRDYR--HDAlncQVLI-TVpacfEILL-LAPHRQNWVKRIRYVIFDEVHCLG-GEIGAeIWEhlLVMIRCP 911
Cdd:COG4581 93 GAENVGLLTGDASvnPDA---PIVVmTT----EILRnMLYREGADLEDVGVVVMDEFHYLAdPDRGW-VWE--EPIIHLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 912 ----FLALSATISNPQHLTEWLQSVkrywkqvdstmeertvskrtgtsRGSyykdqaqarqsykVRLVLYGERyndleky 987
Cdd:COG4581 163 arvqLVLLSATVGNAEEFAEWLTRV-----------------------RGE-------------TAVVVSEER------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 988 lcsvrqgdvcfdhfhpcaaltidhiekygfPSDLalspresIQLYdtmcqvwkswpqaqSLCPENFTQFKnkiVIKKLda 1067
Cdd:COG4581 200 ------------------------------PVPL-------EFHY--------------LVTPRLFPLFR---VNPEL-- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1068 rkyeeslkeeftnwvkngneeearmvlkKLSPDYHEhsgrmldffpcLVEKLRKMEKLPALFFLFklniveecaenafef 1147
Cdd:COG4581 224 ----------------------------LRPPSRHE-----------VIEELDRGGLLPAIVFIF--------------- 249
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1148 lekkqeekrppkadkearttanklrkvkkslekqktvdekgqksSRR-LDESVMhetehnyllQTLEKNLeipkdCTYAN 1226
Cdd:COG4581 250 --------------------------------------------SRRgCDEAAQ---------QLLSARL-----TTKEE 271
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1227 QKAIDDQLLQRvfhRVRFE-RKGETLKRLAERGIGYHHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVF 1305
Cdd:COG4581 272 RAEIREAIDEF---AEDFSvLFGKTLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVF 348
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1306 AQNS-------VYLDALNYRQMSGRAGRRGQDLLGDVY----FFDIPlPKIGKLIKSKVPELRGQFPLSISLILRlmLLA 1374
Cdd:COG4581 349 TKLSkfdgerhRPLTAREFHQIAGRAGRRGIDTEGHVVvlapEHDDP-KKFARLASARPEPLRSSFRPSYNMVLN--LLA 425
|
650 660
....*....|....*....|....*....
gi 657940862 1375 SkaddleDGKAKALSVLKHSLLSFKQPRA 1403
Cdd:COG4581 426 R------PGLERARELLEDSFAQFQADRS 448
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
766-920 |
7.17e-22 |
|
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: 94.23 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 766 QRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESDEGV-VVYVAPTKALVNQVAATVEYRYAKNMPAGESLCGVF 844
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPqALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGD 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657940862 845 TRDYRHDAL-NCQVLITVPacfEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIR--CPFLALSATIS 920
Cdd:pfam00270 84 SRKEQLEKLkGPDILVGTP---GRLLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPkkRQILLLSATLP 159
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
760-951 |
5.75e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 84.08 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 760 FIPDTWQRELLD-VVDNYESAVIVAPTSSGKTYASYYCMEKVLKESDEGVVVYVAPTKALVNQVAATVEYRYAKNmpaGE 838
Cdd:smart00487 7 EPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSL---GL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 839 SLCGVFTRDYRHDAL------NCQVLITVPACFEILLLapHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIR--C 910
Cdd:smart00487 84 KVVGLYGGDSKREQLrklesgKTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPknV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 657940862 911 PFLALSATISNPQHLTEWLqsvkrYWKQVDSTMEERTVSKR 951
Cdd:smart00487 162 QLLLLSATPPEEIENLLEL-----FLNDPVFIDVGFTPLEP 197
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
777-929 |
3.03e-17 |
|
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: 80.71 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 777 ESAVIVAPTSSGKTYASYYC-MEKVLKESDEGV-VVYVAPTKALVNQVAATVEyRYAKNMPAGESLcGVFTRDY----RH 850
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPaLSSLADEPEKGVqVLYISPLKALINDQERRLE-EPLDEIDLEIPV-AVRHGDTsqseKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 851 DALNC--QVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCL-GGEIGAEI---WEHLLVMIRCPF--LALSATISNP 922
Cdd:cd17922 80 KQLKNppGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHALlGSKRGVQLellLERLRKLTGRPLrrIGLSATLGNL 159
|
....*..
gi 657940862 923 QHLTEWL 929
Cdd:cd17922 160 EEAAAFL 166
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1142-1445 |
3.36e-17 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 87.71 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1142 ENAFEFLEKKQEEKRPPKADkeartTANKLRKvkkslekqkTVDEKGQ----KSSRRLDESvmhetehnyllqtleknle 1217
Cdd:PRK02362 212 GGAIHFDDSQREVEVPSKDD-----TLNLVLD---------TLEEGGQclvfVSSRRNAEG------------------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1218 IPKDCTYANQKAIDDQL---LQRVFHRVRFERKGETLKRLA---ERGIGYHHSSMSAKEKQLVEILFRKGFIRVVTATGT 1291
Cdd:PRK02362 259 FAKRAASALKKTLTAAEraeLAELAEEIREVSDTETSKDLAdcvAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPT 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1292 LALGINMPCKSVV------FAQNS--VYLDALNYRQMSGRAGRRGQDLLG----------------DVYFFDIPLPkigk 1347
Cdd:PRK02362 339 LAAGLNLPARRVIirdyrrYDGGAgmQPIPVLEYHQMAGRAGRPGLDPYGeavllaksydeldelfERYIWADPED---- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1348 lIKSKvpelrgqfpLSISLILRLMLLASKADDLEDGKAKALSVLKHSLLSFKQP------RAIDMlklyflySLQFLVKE 1421
Cdd:PRK02362 415 -VRSK---------LATEPALRTHVLSTIASGFARTRDGLLEFLEATFYATQTDdtgrleRVVDD-------VLDFLERN 477
|
330 340
....*....|....*....|....*..
gi 657940862 1422 GHIDQEGN---PTGFAGLVSHLhYHEP 1445
Cdd:PRK02362 478 GMIEEDGEtleATELGHLVSRL-YIDP 503
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
744-934 |
5.82e-17 |
|
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: 81.34 E-value: 5.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 744 YLIREERKDPDPRVQDFIPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESDEgvVVYVAPTKALVNQva 823
Cdd:cd18024 15 PISAHKPPGNPARTYPFTLDPFQKTAIACIERNESVLVSAHTSAGKTVVAEYAIAQSLRDKQR--VIYTSPIKALSNQ-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 824 atvEYRyakNMPAGESLCGVFTRDYR-HDALNCQVLITvpacfEILLLAPHRQNWVKR-IRYVIFDEVHCLGGEIGAEIW 901
Cdd:cd18024 91 ---KYR---ELQEEFGDVGLMTGDVTiNPNASCLVMTT-----EILRSMLYRGSEIMReVAWVIFDEIHYMRDKERGVVW 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 657940862 902 EHLLV----MIRcpFLALSATISNPQHLTEWLQSVKR 934
Cdd:cd18024 160 EETIIllpdKVR--YVFLSATIPNARQFAEWICKIHK 194
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
766-929 |
4.09e-16 |
|
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: 78.14 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 766 QRELLD-VVDNYESAVIVAPTSSGKTYASYYCMEKVLkeSDEGVVVYVAPTKALVNQvaatvEYRYAKNMPAGESLCGVF 844
Cdd:cd18028 6 QAEAVRaGLLKGENLLISIPTASGKTLIAEMAMVNTL--LEGGKALYLVPLRALASE-----KYEEFKKLEEIGLKVGIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 845 TRDYRHDAL---NCQVLITVPACFEILLlaPHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIR-----CPFLALS 916
Cdd:cd18028 79 TGDYDEDDEwlgDYDIIVATYEKFDSLL--RHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnpnTQIIGLS 156
|
170
....*....|...
gi 657940862 917 ATISNPQHLTEWL 929
Cdd:cd18028 157 ATIGNPDELAEWL 169
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1249-1454 |
1.04e-15 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 83.01 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1249 ETLKRLAERGIGYHHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQ-------NSVYLDALNYRQMS 1321
Cdd:PRK01172 278 DSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDitrygngGIRYLSNMEIKQMI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1322 GRAGRRGQDLLGDVYFF---------------DIPLPKIGKLIKSKvpELRGQFPLSISlilrlMLLASKADDLEDgkak 1386
Cdd:PRK01172 358 GRAGRPGYDQYGIGYIYaaspasydaakkylsGEPEPVISYMGSQR--KVRFNTLAAIS-----MGLASSMEDLIL---- 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1387 alsvLKHSLLSFKQpRAIDMLKLYFLYSLQFLVKEGHIDQEG--NPTGFAGLVSHLHYHEPSNLVFVSFL 1454
Cdd:PRK01172 427 ----FYNETLMAIQ-NGVDEIDYYIESSLKFLKENGFIKGDVtlRATRLGKLTSDLYIDPESALILKSAF 491
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
766-930 |
1.67e-15 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 77.01 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 766 QRELL-DVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESDEG-----VVVYVAPTKALVNQVAAtvEYRyAKNMPAGES 839
Cdd:cd18023 6 QSEVFpDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLpwgnrKVVYIAPIKALCSEKYD--DWK-EKFGPLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 840 lCGVFTRDYRHDAL----NCQVLITVPACFE-ILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAEIwE---------HLL 905
Cdd:cd18023 83 -CAELTGDTEMDDTfeiqDADIILTTPEKWDsMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATL-EvvvsrmktlSSS 160
|
170 180 190
....*....|....*....|....*....|.
gi 657940862 906 VMIRCP------FLALSATISNPQHLTEWLQ 930
Cdd:cd18023 161 SELRGStvrpmrFVAVSATIPNIEDLAEWLG 191
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
777-929 |
4.27e-15 |
|
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: 75.49 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 777 ESAVIVAPTSSGKTYASYYCMEKVLKESDEGVVVYVAPTKALVNQVAATVEYRYAKNMpaGES---LCGVFTRDYRhDAL 853
Cdd:cd18022 18 NNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKL--GKKvveLTGDVTPDMK-ALA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 854 NCQVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGA----------EIWEHLLVMIRcpFLALSATISNPQ 923
Cdd:cd18022 95 DADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPvlevivsrmnYISSQTEKPVR--LVGLSTALANAG 172
|
....*.
gi 657940862 924 HLTEWL 929
Cdd:cd18022 173 DLANWL 178
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
760-942 |
4.43e-15 |
|
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: 74.99 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 760 FIPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESDEgvVVYVAPTKALVNQvaatvEYRYAKNMPAGes 839
Cdd:cd18027 7 FELDVFQKQAILHLEAGDSVFVAAHTSAGKTVVAEYAIALAQKHMTR--TIYTSPIKALSNQ-----KFRDFKNTFGD-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 840 lCGVFTRDYR-HDALNCQVLITvpacfEILLLAPHRQNWVKR-IRYVIFDEVHCLGGEIGAEIWEHLLVMI--RCPFLAL 915
Cdd:cd18027 78 -VGLITGDVQlNPEASCLIMTT-----EILRSMLYNGSDVIRdLEWVIFDEVHYINDAERGVVWEEVLIMLpdHVSIILL 151
|
170 180
....*....|....*....|....*..
gi 657940862 916 SATISNPQHLTEWLQSVKRYWKQVDST 942
Cdd:cd18027 152 SATVPNTVEFADWIGRIKKKNIYVIST 178
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1252-1328 |
1.14e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 70.70 E-value: 1.14e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657940862 1252 KRLAERGIGY--HHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFaQNSVYLDALNYRQMSGRAGRRG 1328
Cdd:smart00490 5 ELLKELGIKVarLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVI-IYDLPWSPASYIQRIGRAGRAG 82
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
766-927 |
3.11e-14 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 78.34 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 766 QRELLDVVDNYESAVIVAPTSSGKTYAsyYC---MEKVLKESDeGVVVYVAPTKALVN-QVAATVEyrYAKNMPAGESlC 841
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLA--YLlpvLEALLEDPG-ATALYLYPTKALARdQLRRLRE--LAEALGLGVR-V 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 842 GVFT----RDYRHDAL-NCQVLITVPacfEIL---LLaPHRQNWV---KRIRYVIFDEVHCLGGEIGAeiweHLLVMIR- 909
Cdd:COG1205 135 ATYDgdtpPEERRWIReHPDIVLTNP---DMLhygLL-PHHTRWArffRNLRYVVIDEAHTYRGVFGS----HVANVLRr 206
|
170 180
....*....|....*....|....*....
gi 657940862 910 ----CP-------FLALSATISNPQHLTE 927
Cdd:COG1205 207 lrriCRhygsdpqFILASATIGNPAEHAE 235
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
765-918 |
1.54e-13 |
|
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: 69.64 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 765 WQRELLDVVDNYES---AVIVAPTSSGKTYASYYCMEKVLKESdegvVVYVAPTKALVNQVAAtveyRYAKnmPAGESLC 841
Cdd:cd17926 4 YQEEALEAWLAHKNnrrGILVLPTGSGKTLTALALIAYLKELR----TLIVVPTDALLDQWKE----RFED--FLGDSSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 842 GVFTRDYRHDALNCQVLITVP----ACFEILLLAPHRQNwvkrirYVIFDEVHclggEIGAEIWEHLLVMIRCPF-LALS 916
Cdd:cd17926 74 GLIGGGKKKDFDDANVVVATYqslsNLAEEEKDLFDQFG------LLIVDEAH----HLPAKTFSEILKELNAKYrLGLT 143
|
..
gi 657940862 917 AT 918
Cdd:cd17926 144 AT 145
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
777-929 |
3.50e-13 |
|
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: 69.98 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 777 ESAVIVAPTSSGKTYASYYCMEKVLKESDEGVVVYVAPTKALVNQVAATVEYRYAKNMPAG-ESLCGVFTRDYRHDALNc 855
Cdd:cd18021 20 DNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPLLGKKvVKLTGETSTDLKLLAKS- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 856 QVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAeIWEHLLVMIR---------CPFLALSATISNPQHLT 926
Cdd:cd18021 99 DVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGP-VYEVVVSRMRyissqlekpIRIVGLSSSLANARDVG 177
|
...
gi 657940862 927 EWL 929
Cdd:cd18021 178 EWL 180
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
743-918 |
4.01e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 74.29 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 743 HYLIREERKDPDPRVQ-DFIPDTWQRELLD-----VVDNYESAVIVAPTSSGKTYASYYCMEKVLKesdEGVVVYVAPTK 816
Cdd:COG1061 61 ELAEAEALEAGDEASGtSFELRPYQQEALEallaaLERGGGRGLVVAPTGTGKTVLALALAAELLR---GKRVLVLVPRR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 817 ALVNQVAATveyrYAKNMPAGESLCGVFTRDYRHdalncqVLITVpacfEILLLAPHRQNWVKRIRYVIFDEVHclggEI 896
Cdd:COG1061 138 ELLEQWAEE----LRRFLGDPLAGGGKKDSDAPI------TVATY----QSLARRAHLDELGDRFGLVIIDEAH----HA 199
|
170 180
....*....|....*....|...
gi 657940862 897 GAEIWEHLLVMIRCPF-LALSAT 918
Cdd:COG1061 200 GAPSYRRILEAFPAAYrLGLTAT 222
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1249-1374 |
6.07e-13 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 74.08 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1249 ETLKRLAERGIGYHHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQNSVYLD-------ALNYRQMS 1321
Cdd:PRK00254 288 EKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNfgwedipVLEIQQMM 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 657940862 1322 GRAGRRGQDLLGD---VYFFDIPLPKIGKLIKSKVPELRGQfpLSISLILRLMLLA 1374
Cdd:PRK00254 368 GRAGRPKYDEVGEaiiVATTEEPSKLMERYIFGKPEKLFSM--LSNESAFRSQVLA 421
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
777-918 |
1.12e-12 |
|
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: 67.04 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 777 ESAVIVAPTSSGKTYASYYCMEKVLkESDEGVVVYVAPTKALVNQVAATVEYRYAKNMPageslCGVFTRD------YRH 850
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLL-LKKGKKVLVLVPTKALALQTAERLRELFGPGIR-----VAVLVGGssaeerEKN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657940862 851 DALNCQVLITVPACFEILLLAPHRQnWVKRIRYVIFDEVHCLGGeIGAEIWEHLLVMIR-----CPFLALSAT 918
Cdd:cd00046 76 KLGDADIIIATPDMLLNLLLREDRL-FLKDLKLIIVDEAHALLI-DSRGALILDLAVRKaglknAQVILLSAT 146
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
777-939 |
2.96e-12 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 71.77 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 777 ESAVIVAPTSSGKTYASYYCM-EKVLKESdeGVVVYVAPTKALvnqvaATVEYRYAKNMPAGESLCGVFTRDY------- 848
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMvNKLLREG--GKAVYLVPLKAL-----AEEKYREFKDWEKLGLRVAMTTGDYdstdewl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 849 -RHDalncqVLITVPACFEILLlaPHRQNWVKRIRYVIFDEVHCLGG-EIGAE---IWEHLLVmiRCPFLALSATISNPQ 923
Cdd:PRK00254 113 gKYD-----IIIATAEKFDSLL--RHGSSWIKDVKLVVADEIHLIGSyDRGATlemILTHMLG--RAQILGLSATVGNAE 183
|
170
....*....|....*...
gi 657940862 924 HLTEWLQS--VKRYWKQV 939
Cdd:PRK00254 184 ELAEWLNAelVVSDWRPV 201
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
779-918 |
3.07e-11 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 63.46 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 779 AVIVAPTSSGKTYASYYCMEKVLKESDEGVVVYVAPTKALVNQvaaTVEyRYAKNMPAGESLCGVFT-RDYRHDALNCQV 857
Cdd:pfam04851 26 GLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQ---ALE-EFKKFLPNYVEIGEIISgDKKDESVDDNKI 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657940862 858 LI-TVPACFEILLLAPHrQNWVKRIRYVIFDEVHclggEIGAEIWEHLLVMIRCPF-LALSAT 918
Cdd:pfam04851 102 VVtTIQSLYKALELASL-ELLPDFFDVIIIDEAH----RSGASSYRNILEYFKPAFlLGLTAT 159
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
766-924 |
4.36e-11 |
|
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: 63.37 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 766 QRELLDVVDNYESAVIVAPTSSGKTYAsyY---CMEKVLKESdEGVVVYVAPTKALVN-QVAATVEyrYAKNMPAGESlC 841
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLC--YqlpILEALLRDP-GSRALYLYPTKALAQdQLRSLRE--LLEQLGLGIR-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 842 GVFTRDYRHDA------LNCQVLITVPACFEILLLAPHRQ--NWVKRIRYVIFDEVHCLGGEIGAeiweHLLVMIR---- 909
Cdd:cd17923 79 ATYDGDTPREErraiirNPPRILLTNPDMLHYALLPHHDRwaRFLRNLRYVVLDEAHTYRGVFGS----HVALLLRrlrr 154
|
170 180
....*....|....*....|....
gi 657940862 910 -CP-------FLALSATISNP-QH 924
Cdd:cd17923 155 lCRrygadpqFILTSATIGNPaEH 178
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1238-1328 |
3.33e-09 |
|
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: 56.06 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1238 VFHRVRFERKGETLKRLAERGIGYHHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFaQNSVYLDALNY 1317
Cdd:pfam00271 20 IFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVI-NYDLPWNPASY 98
|
90
....*....|.
gi 657940862 1318 RQMSGRAGRRG 1328
Cdd:pfam00271 99 IQRIGRAGRAG 109
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
1238-1329 |
7.40e-09 |
|
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: 56.12 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1238 VFH--RVRFERKGETLKRLAERG-----IGYHHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINM-PCKSVVfaQNS 1309
Cdd:cd18796 43 VFTntRSQAERLAQRLRELCPDRvppdfIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIgDVDLVI--QIG 120
|
90 100
....*....|....*....|
gi 657940862 1310 VYLDALNYRQMSGRAGRRGQ 1329
Cdd:cd18796 121 SPKSVARLLQRLGRSGHRPG 140
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
754-929 |
1.05e-07 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 57.03 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 754 DPRVQDFIPDTW------QRELLDVVDNYESAVIVAPTSSGKTYASY------YCMEKVLKESDEGV-VVYVAPTKALVN 820
Cdd:COG1201 11 HPAVRAWFAARFgaptppQREAWPAIAAGESTLLIAPTGSGKTLAAFlpaldeLARRPRPGELPDGLrVLYISPLKALAN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 821 QVaatveyryAKNM---------PAGESLCGV----------------FTRDYRHdalncqVLITVPACFEILLLAPHRQ 875
Cdd:COG1201 91 DI--------ERNLrapleeigeAAGLPLPEIrvgvrtgdtpaserqrQRRRPPH------ILITTPESLALLLTSPDAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657940862 876 NWVKRIRYVIFDEVHCLGG-------EIGAEIWEHL----LVMIrcpflALSATISNPQHLTEWL 929
Cdd:COG1201 157 ELLRGVRTVIVDEIHALAGskrgvhlALSLERLRALaprpLQRI-----GLSATVGPLEEVARFL 216
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
760-890 |
2.61e-07 |
|
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: 52.86 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 760 FIPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKE----SDEGVVVYVAPTKALVNQvAATVEYRYAKNMP 835
Cdd:cd18036 1 LELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKrrsaGEKGRVVVLVNKVPLVEQ-QLEKFFKYFRKGY 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657940862 836 AGESLCGVFTRD--YRHDALNCQVLITVPACFEILLLAPhRQNwvKRIRY-----VIFDEVH 890
Cdd:cd18036 80 KVTGLSGDSSHKvsFGQIVKASDVIICTPQILINNLLSG-REE--ERVYLsdfslLIFDECH 138
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
780-918 |
6.35e-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: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 780 VIVAPTSSGKTYASYYCMEKVLKESDEGVVVYVAPTKALVNQVA----------------------ATVEYRYAKNMPAG 837
Cdd:cd17930 5 ILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINQMYerireilgrlddedkvlllhskAALELLESDEEPDD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 838 ESLCGVFTRDYRHDALNCQVLITVPacFEILL-LAPHRQNWVK--RI--RYVIFDEVHCLGGEIGAEIWEHLLVMIR--- 909
Cdd:cd17930 85 DPVEAVDWALLLKRSWLAPIVVTTI--DQLLEsLLKYKHFERRlhGLanSVVVLDEVQAYDPEYMALLLKALLELLGelg 162
|
....*....
gi 657940862 910 CPFLALSAT 918
Cdd:cd17930 163 GPVVLMTAT 171
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
635-918 |
7.46e-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: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 635 KAQVERVGLQACLKAWKEHCQAEGETTKDLSIAVNMMKRIHSLLDKHSELLQEADQKLIARCLKYLGFCELAVSLYPTQD 714
Cdd:COG1203 11 GALALAALLLLLLALLLAALLLLLLAALLLALLLALLLLAALELALLLLLLLLLLLLLLLLLLDLLLDDLAFLFLLLLID 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 715 A----SDGIKMKKKNKysvgigpARFQLQYMGHYLirEERKDPDPRVqdfipDTWQRELLDVVDNYESA-----VIVAPT 785
Cdd:COG1203 91 AdwldSANFDMARQAL-------DHLLAERLERLL--PKKSKPRTPI-----NPLQNEALELALEAAEEepglfILTAPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 786 SSGKTYASYYCMEKVLKESDEGVVVYVAPTKALVNQVA-----------------ATVEYRYAKNMPAGESlcgvftRDY 848
Cdd:COG1203 157 GGGKTEAALLFALRLAAKHGGRRIIYALPFTSIINQTYdrlrdlfgedvllhhslADLDLLEEEEEYESEA------RWL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 849 RH--DALNCQVLITVPACFEILLLAPHRQNWVKRIRY----VIFDEVHClggeIGAEIWEHLLVMIR------CPFLALS 916
Cdd:COG1203 231 KLlkELWDAPVVVTTIDQLFESLFSNRKGQERRLHNLansvIILDEVQA----YPPYMLALLLRLLEwlknlgGSVILMT 306
|
..
gi 657940862 917 AT 918
Cdd:COG1203 307 AT 308
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
762-925 |
1.94e-05 |
|
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: 47.43 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 762 PDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLK---ESDEGVVVYVAPTKALVNQvAATVEYRYAKNMP--- 835
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKkfpAGRKGKVVFLANKVPLVEQ-QKEVFRKHFERPGykv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 836 ---AGESLCGVFTRDYrhdALNCQVLITVPACFEILLLAPhRQNWVKRIRYVIFDEVHCLGGEigaeiWEHLLVMIRCPF 912
Cdd:cd17927 82 tglSGDTSENVSVEQI---VESSDVIIVTPQILVNDLKSG-TIVSLSDFSLLVFDECHNTTKN-----HPYNEIMFRYLD 152
|
170
....*....|...
gi 657940862 913 LALSATISNPQHL 925
Cdd:cd17927 153 QKLGSSGPLPQIL 165
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
1225-1329 |
2.11e-05 |
|
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: 45.66 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1225 ANQKAIDDQLLQRVFHR-------VRFERKGETL-KRLAERGI--GYHHSSMSAKEKQLVEILFRKGFIRVVTATGTLAL 1294
Cdd:cd18794 13 KKDEKLDLLKRIKVEHLggsgiiyCLSRKECEQVaARLQSKGIsaAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGM 92
|
90 100 110
....*....|....*....|....*....|....*.
gi 657940862 1295 GINMPckSVVF-AQNSVYLDALNYRQMSGRAGRRGQ 1329
Cdd:cd18794 93 GIDKP--DVRFvIHYSLPKSMESYYQESGRAGRDGL 126
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1261-1347 |
2.70e-05 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 49.12 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1261 YHHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQNSVYLDALN---YRQMSGRAGRRGQDLLGDVYF 1337
Cdd:COG1202 453 PYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSLAMGIEWLSvqeFHQMLGRAGRPDYHDRGKVYL 532
|
90
....*....|
gi 657940862 1338 fdipLPKIGK 1347
Cdd:COG1202 533 ----LVEPGK 538
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1252-1332 |
3.22e-05 |
|
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: 48.68 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1252 KRLAERGIGY----HHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCksvvfaqnsvyLDA----------LNY 1317
Cdd:COG1205 310 RALREPDLADrvaaYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGG-----------LDAvvlagypgtrASF 378
|
90
....*....|....*
gi 657940862 1318 RQMSGRAGRRGQDLL 1332
Cdd:COG1205 379 WQQAGRAGRRGQDSL 393
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
777-921 |
8.17e-05 |
|
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: 45.82 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 777 ESAVIVAPTSSGKTYASYYCM----EKVLKES-----DEGVVVYVAPTKALVNQVAATVEYRYAK-NMPAGE-----SLC 841
Cdd:cd18019 34 ENLLLCAPTGAGKTNVALLTIlreiGKHRNPDgtinlDAFKIVYIAPMKALVQEMVGNFSKRLAPyGITVAEltgdqQLT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 842 gvftrdyRHDALNCQVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGA--------EIW--EHLLVMIRcp 911
Cdd:cd18019 114 -------KEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDDRGPvlesivarTIRqiEQTQEYVR-- 184
|
170
....*....|
gi 657940862 912 FLALSATISN 921
Cdd:cd18019 185 LVGLSATLPN 194
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
777-921 |
1.58e-04 |
|
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: 44.73 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 777 ESAVIVAPTSSGKTYASYYCMEKVLKES---------DEGVVVYVAPTKALVNQVAATVEYRYAK-NMPAGEslcgvFTR 846
Cdd:cd18020 18 ENMLICAPTGAGKTNIAMLTILHEIRQHvnqggvikkDDFKIVYIAPMKALAAEMVEKFSKRLAPlGIKVKE-----LTG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 847 DY---RHDALNCQVLITVPACFEILLLAPHRQN-WVKRIRYVIFDEVHCLGGEIGAEIwEHLLV-----------MIRcp 911
Cdd:cd18020 93 DMqltKKEIAETQIIVTTPEKWDVVTRKSSGDVaLSQLVRLLIIDEVHLLHDDRGPVI-ESLVArtlrqvestqsMIR-- 169
|
170
....*....|
gi 657940862 912 FLALSATISN 921
Cdd:cd18020 170 IVGLSATLPN 179
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
781-890 |
1.77e-04 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 46.26 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 781 IVAPTSSGKTYASYYCMEKVLKESDeGVVVYVAPTKALVNQVAATveyrYAKNMPAGESLCGVFTRDYRHD---AL--NC 855
Cdd:COG1111 22 VVLPTGLGKTAVALLVIAERLHKKG-GKVLFLAPTKPLVEQHAEF----FKEALNIPEDEIVVFTGEVSPEkrkELweKA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 657940862 856 QVLITVPACFEILLLAphrqnwvKRIR-----YVIFDEVH 890
Cdd:COG1111 97 RIIVATPQVIENDLIA-------GRIDlddvsLLIFDEAH 129
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
760-921 |
2.81e-04 |
|
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: 43.79 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 760 FIPDTWQRELLDVVDNyESAVIVAPTSSGKTYASyyCM------EKVLKESDEG-VVVYVAPTKALVNQVAATVE-YRYA 831
Cdd:cd18034 1 FTPRSYQLELFEAALK-RNTIVVLPTGSGKTLIA--VMlikemgELNRKEKNPKkRAVFLVPTVPLVAQQAEAIRsHTDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 832 KNMP-AGESLCGVFTRDYRHDAL-NCQVLITVPACFEILLlaphRQNWVK--RIRYVIFDEVH-CLGGEIGAEI---WEH 903
Cdd:cd18034 78 KVGEySGEMGVDKWTKERWKEELeKYDVLVMTAQILLDAL----RHGFLSlsDINLLIFDECHhATGDHPYARImkeFYH 153
|
170
....*....|....*....
gi 657940862 904 LLVMIRCP-FLALSATISN 921
Cdd:cd18034 154 LEGRTSRPrILGLTASPVN 172
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
1241-1332 |
3.97e-04 |
|
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: 42.63 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1241 RVRFERKGETLKRLAE-RGiGYhhssmSAKEKQLVEILFRKGFIRVVTATGTLALGINMPCksvvfaqnsvyLDAL---- 1315
Cdd:cd18797 56 KARLVEEGPLASKVASyRA-GY-----LAEDRREIEAELFNGELLGVVATNALELGIDIGG-----------LDAVvlag 118
|
90 100
....*....|....*....|...
gi 657940862 1316 ------NYRQMSGRAGRRGQDLL 1332
Cdd:cd18797 119 ypgslaSLWQQAGRAGRRGKDSL 141
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1237-1299 |
7.78e-04 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 44.32 E-value: 7.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657940862 1237 RVFHRvrferkgetLKRLAERG---IGYHHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMP 1299
Cdd:COG1201 287 RLFQR---------LNELNPEDalpIAAHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIG 343
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
778-890 |
1.66e-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: 41.35 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 778 SAVIVAPTSSGKTYASYYCMEKVLKESDeGVVVYVAPTKALVNQVAATveYRYAKNMPAG-ESLCGVFTRDYRHDALN-C 855
Cdd:cd18035 18 NTLIVLPTGLGKTIIAILVAADRLTKKG-GKVLILAPSRPLVEQHAEN--LKRVLNIPDKiTSLTGEVKPEERAERWDaS 94
|
90 100 110
....*....|....*....|....*....|....*
gi 657940862 856 QVLITVPACFEILLLApHRQNwVKRIRYVIFDEVH 890
Cdd:cd18035 95 KIIVATPQVIENDLLA-GRIT-LDDVSLLIFDEAH 127
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
1249-1328 |
2.32e-03 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 42.78 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1249 ETLKRLAERGI--GYHHSSMSAKEKQLVEILFRKGFIRVVTATGTLALGINMPckSVVFAqnsVYLD----ALNYRQMSG 1322
Cdd:PRK11057 251 DTAARLQSRGIsaAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKP--NVRFV---VHFDiprnIESYYQETG 325
|
....*.
gi 657940862 1323 RAGRRG 1328
Cdd:PRK11057 326 RAGRDG 331
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1241-1299 |
2.66e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 42.57 E-value: 2.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1241 RVRFERKGETLKRLAERGIGYHHSSMSaKEKQL-VEILFRKGFIRVVTATGTLALGINMP 1299
Cdd:PRK13767 299 RVLYNLRKRFPEEYDEDNIGAHHSSLS-REVRLeVEEKLKRGELKVVVSSTSLELGIDIG 357
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
1252-1338 |
5.44e-03 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 41.40 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 1252 KRLAERGIGYHHSSMSA-KEKqlVEIlFRKGFIRVVTATGTLALGINMPCKSV--VFAQNSVY-LDALnyRQMSGRAGRR 1327
Cdd:COG4098 341 KLFPEERIAGVHAEDPErKEK--VQA-FRDGEIPILVTTTILERGVTFPNVDVavLGADHPVFtEAAL--VQIAGRVGRS 415
|
90
....*....|.
gi 657940862 1328 GQDLLGDVYFF 1338
Cdd:COG4098 416 ADYPTGEVIFF 426
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
771-888 |
6.42e-03 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 40.44 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 771 DVVDNYESAVIVAPTSSGKTYAsyYCMEKV--LKESDEGV------------------VVYVAPTKALVNQVAATVEyry 830
Cdd:cd17965 56 NEEPKLEVFLLAAETGSGKTLA--YLAPLLdyLKRQEQEPfeeaeeeyesakdtgrprSVILVPTHELVEQVYSVLK--- 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657940862 831 AKNMPAGESLCGV---FTRDYRHDALN----CQVLITVPacFEILLLAPHRQNWVKRIRYVIFDE 888
Cdd:cd17965 131 KLSHTVKLGIKTFssgFGPSYQRLQLAfkgrIDILVTTP--GKLASLAKSRPKILSRVTHLVVDE 193
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
780-889 |
7.05e-03 |
|
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: 39.73 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657940862 780 VIVAPTSSGKTYAsyYCM---EKVLKESDEG-----VVVyVAPTKALVNQVAATVEyRYAKNMPAgESLC---GVftrDY 848
Cdd:cd00268 31 IGQAQTGSGKTLA--FLLpilEKLLPEPKKKgrgpqALV-LAPTRELAMQIAEVAR-KLGKGTGL-KVAAiygGA---PI 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 657940862 849 RHDAL----NCQVLITVPACFeILLLAPHRQNwVKRIRYVIFDEV 889
Cdd:cd00268 103 KKQIEalkkGPDIVVGTPGRL-LDLIERGKLD-LSNVKYLVLDEA 145
|
|
| |
