|
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 ... |
760-937 |
1.89e-113 |
|
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: 355.14 E-value: 1.89e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 760 IPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESNEGVVVYVAPTKALVNQVAATVQNRYTKNM-PGGEA 838
Cdd:cd18025 1 NPDAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYpPSGKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 839 LCGVFTRDYRHE-ALNSQVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIRCPFLALSAT 917
Cdd:cd18025 81 LWGVFTRDYRHNnPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWEQLLLLIPCPFLALSAT 160
|
170 180
....*....|....*....|
gi 1958693995 918 ISNPQHLTEWLQSVKRYWKQ 937
Cdd:cd18025 161 IGNPQKFHEWLQSVQRARKA 180
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1193-1336 |
2.08e-35 |
|
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: 132.29 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1193 LDQSIMYEAEHNYLLKSLEKNLEIPKDCTYADQKAIDEETLQIVFgrvkCGKKGDTlKKLAR--RGIGYHHRSMTAKEKQ 1270
Cdd:cd18795 5 LEEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVF----CSSRKEC-EKTAKdlAGIAFHHAGLTREDRE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958693995 1271 LVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQNSVY-------LDALNYRQMSGRAGRRGQDLLGDVYFF 1336
Cdd:cd18795 80 LVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYdgkgyreLSPLEYLQMIGRAGRPGFDTRGEAIIM 152
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
765-1440 |
9.68e-34 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 138.10 E-value: 9.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 765 QRELLD-VVDNYESAVIVAPTSSGKTYASYYCMEKVLKESneGVVVYVAPTKALVNQVAATVQNRYtknmpggEALC--- 840
Cdd:COG1204 27 QAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNG--GKALYIVPLRALASEKYREFKRDF-------EELGikv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 841 GVFTRDYRHEAL---NSQVLITVPACFEILLLapHRQNWVKRIRYVIFDEVHCLG-GEIGAEIwEHLLVMIR--CP---F 911
Cdd:COG1204 98 GVSTGDYDSDDEwlgRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTL-EVLLARLRrlNPeaqI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 912 LALSATISNPQHLTEWLqsvkrywkqvdstmeqgsvsqrnaatrgsyhkdrvqarqsykvrlvlygeryndlekylcsvr 991
Cdd:COG1204 175 VALSATIGNAEEIAEWL--------------------------------------------------------------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 992 qgdvcfdhfhPCAALTTDhiekygfpsdlalspresiqlydtmcqvWKSWPQAQNLCPENFTQFKNKivikkldarkyee 1071
Cdd:COG1204 192 ----------DAELVKSD----------------------------WRPVPLNEGVLYDGVLRFDDG------------- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1072 slkeeftnwVKNGNEKEAQLVLKKLSPDyhdysGQMLDFFPclveklrkmeklpalfflfSLDTVEECAENVCEFLEEKQ 1151
Cdd:COG1204 221 ---------SRRSKDPTLALALDLLEEG-----GQVLVFVS-------------------SRRDAESLAKKLADELKRRL 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1152 EekrpPKADKEAYIMANKLRKVKKSLEKqkidekgqkssrrldqsimyeaehnyllksleknleipkdctyadqkaidee 1231
Cdd:COG1204 268 T----PEEREELEELAEELLEVSEETHT---------------------------------------------------- 291
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1232 tlqivfgrvkcgkkGDTLKKLARRGIGYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFA----QNS 1307
Cdd:COG1204 292 --------------NEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRdtkrGGM 357
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1308 VYLDALNYRQMSGRAGRRGQDLLGDVYFFDIPLPKIGKL----IKSKVPELRGQfpLSITLILRLMLLAT----KADDLE 1379
Cdd:COG1204 358 VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDEADELferyILGEPEPIRSK--LANESALRTHLLALiasgFANSRE 435
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958693995 1380 DgkakALSVLKHSLLSFKQPRatDMLKLYFLYSLQFLVKEGHIDQEGN---PTGFAGLVTHLNY 1440
Cdd:COG1204 436 E----LLDFLENTFYAYQYDK--GDLEEVVDDALEFLLENGFIEEDGDrlrATKLGKLVSRLYI 493
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
765-919 |
1.63e-21 |
|
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: 93.08 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 765 QRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESNEGV-VVYVAPTKALVNQVAATVQNRYTKNMPGGEALCGVF 843
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPqALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGD 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958693995 844 TRDYRHEAL-NSQVLITVPacfEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIR--CPFLALSATIS 919
Cdd:pfam00270 84 SRKEQLEKLkGPDILVGTP---GRLLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPkkRQILLLSATLP 159
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
759-928 |
1.87e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 759 FIPDTWQRELLD-VVDNYESAVIVAPTSSGKTYASYYCMEKVLKESNEGVVVYVAPTKALVNQVAATVQNRYTKNMPGGE 837
Cdd:smart00487 7 EPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 838 ALCGVFTRDYRHEALNS---QVLITVPACFEILLLapHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIR--CPFL 912
Cdd:smart00487 87 GLYGGDSKREQLRKLESgktDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPknVQLL 164
|
170
....*....|....*.
gi 1958693995 913 ALSATISNPQHLTEWL 928
Cdd:smart00487 165 LLSATPPEEIENLLEL 180
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1247-1443 |
5.19e-16 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 83.85 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1247 DTLKKLA---RRGIGYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVV------FAQNS--VYLDALNY 1315
Cdd:PRK02362 293 ETSKDLAdcvAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIirdyrrYDGGAgmQPIPVLEY 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1316 RQMSGRAGRRGQDLLG----------------DVYFFDIPLPkigklIKSKVPELRGqfplsitliLRLMLLATKADDLE 1379
Cdd:PRK02362 373 HQMAGRAGRPGLDPYGeavllaksydeldelfERYIWADPED-----VRSKLATEPA---------LRTHVLSTIASGFA 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958693995 1380 DGKAKALSVLKHSLLSFKQPRaTDMLKLYFLYSLQFLVKEGHIDQEGN---PTGFAGLVTHLnYHEP 1443
Cdd:PRK02362 439 RTRDGLLEFLEATFYATQTDD-TGRLERVVDDVLDFLERNGMIEEDGEtleATELGHLVSRL-YIDP 503
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
765-926 |
1.46e-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: 79.11 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 765 QRELLDVVDNYESAVIVAPTSSGKTYAsyYC---MEKVLKESnEGVVVYVAPTKALVN-QVAATvqNRYTKNMpGGEALC 840
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLA--YLlpvLEALLEDP-GATALYLYPTKALARdQLRRL--RELAEAL-GLGVRV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 841 GVFT----RDYRHEAL-NSQVLITVPacfEIL---LLaPHRQNWV---KRIRYVIFDEVHCLGGEIGAeiweHLLVMIR- 908
Cdd:COG1205 135 ATYDgdtpPEERRWIReHPDIVLTNP---DMLhygLL-PHHTRWArffRNLRYVVIDEAHTYRGVFGS----HVANVLRr 206
|
170 180
....*....|....*....|....*....
gi 1958693995 909 ----CP-------FLALSATISNPQHLTE 926
Cdd:COG1205 207 lrriCRhygsdpqFILASATIGNPAEHAE 235
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1250-1326 |
1.30e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 67.62 E-value: 1.30e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958693995 1250 KKLARRGIGY--HHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFaQNSVYLDALNYRQMSGRAGRRG 1326
Cdd:smart00490 5 ELLKELGIKVarLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVI-IYDLPWSPASYIQRIGRAGRAG 82
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1249-1372 |
1.76e-12 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 72.16 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1249 LKKLARRGIGYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQNSVYLD-------ALNYRQMSGR 1321
Cdd:PRK00254 290 LKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNfgwedipVLEIQQMMGR 369
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958693995 1322 AGRRGQDLLGD---VYFFDIPLPKIGKLIKSKVPELRGQfpLSITLILRLMLLA 1372
Cdd:PRK00254 370 AGRPKYDEVGEaiiVATTEEPSKLMERYIFGKPEKLFSM--LSNESAFRSQVLA 421
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
776-938 |
2.61e-11 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 68.31 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 776 ESAVIVAPTSSGKTYASYYCM-EKVLKESneGVVVYVAPTKALVNQvaatvqnRYtKNMPGGEAL---CGVFTRDY--RH 849
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMvNKLLREG--GKAVYLVPLKALAEE-------KY-REFKDWEKLglrVAMTTGDYdsTD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 850 EALNS-QVLITVPACFEILLlaPHRQNWVKRIRYVIFDEVHCLGG-EIGAE---IWEHLLVmiRCPFLALSATISNPQHL 924
Cdd:PRK00254 110 EWLGKyDIIIATAEKFDSLL--RHGSSWIKDVKLVVADEIHLIGSyDRGATlemILTHMLG--RAQILGLSATVGNAEEL 185
|
170
....*....|....*.
gi 1958693995 925 TEWLQS--VKRYWKQV 938
Cdd:PRK00254 186 AEWLNAelVVSDWRPV 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1235-1326 |
5.05e-08 |
|
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: 52.60 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1235 IVFGRVKCGKKGDTLKKLARRGIGYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFaQNSVYLDALN 1314
Cdd:pfam00271 19 LIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVI-NYDLPWNPAS 97
|
90
....*....|..
gi 1958693995 1315 YRQMSGRAGRRG 1326
Cdd:pfam00271 98 YIQRIGRAGRAG 109
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1235-1345 |
2.90e-05 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 48.73 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1235 IVF--GRVKCgkkgdtlKKLARR-GIG--YHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQNSVY 1309
Cdd:COG1202 431 IIFtnSRRRC-------HEIARAlGYKaaPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSLAMG 503
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958693995 1310 LDALN---YRQMSGRAGRRGQDLLGDVYFfdipLPKIGK 1345
Cdd:COG1202 504 IEWLSvqeFHQMLGRAGRPDYHDRGKVYL----LVEPGK 538
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
779-931 |
2.45e-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: 42.06 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 779 VIVAPTSSGKTYASYYCMEKVLKESNEGVVVYVAPTKALVNQVAATV---------------QNRYTKNMPGGEALCGVF 843
Cdd:TIGR01587 3 VIEAPTGYGKTEAALLWALHSIKSQKADRVIIALPTRATINAMYRRAkelfgselvglhhssSFSRIKEMGDSEEFEHLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 844 TRDYRHEALNSQVLITVPACFEIL----LLAPHRQNWVKRIRY--VIFDEVHClggeIGAEIWEHLLVMIR------CPF 911
Cdd:TIGR01587 83 PLYIHSNDKLFLDPITVCTIDQVLksvfGEFGHYEFTLASIANslLIFDEVHF----YDEYTLALILAVLEvlkdndVPI 158
|
170 180
....*....|....*....|
gi 1958693995 912 LALSATIsnPQHLTEWLQSV 931
Cdd:TIGR01587 159 LLMSATL--PKFLKEYAEKI 176
|
|
| |
|
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 ... |
760-937 |
1.89e-113 |
|
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: 355.14 E-value: 1.89e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 760 IPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESNEGVVVYVAPTKALVNQVAATVQNRYTKNM-PGGEA 838
Cdd:cd18025 1 NPDAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYpPSGKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 839 LCGVFTRDYRHE-ALNSQVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIRCPFLALSAT 917
Cdd:cd18025 81 LWGVFTRDYRHNnPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWEQLLLLIPCPFLALSAT 160
|
170 180
....*....|....*....|
gi 1958693995 918 ISNPQHLTEWLQSVKRYWKQ 937
Cdd:cd18025 161 IGNPQKFHEWLQSVQRARKA 180
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
762-931 |
8.92e-48 |
|
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: 168.98 E-value: 8.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 762 DTWQRELLDVVDNY-ESAVIVAPTSSGKTYASYYCMEKVLKESnEGVVVYVAPTKALVNQVAATVQNRYTKNMPGGEALC 840
Cdd:cd17921 3 NPIQREALRALYLSgDSVLVSAPTSSGKTLIAELAILRALATS-GGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 841 GVFTRDYRHEAlNSQVLITVPACFEILLLAPHrQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIR-----CPFLALS 915
Cdd:cd17921 82 GDPSVNKLLLA-EADILVATPEKLDLLLRNGG-ERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrinknARFVGLS 159
|
170
....*....|....*.
gi 1958693995 916 ATISNPQHLTEWLQSV 931
Cdd:cd17921 160 ATLPNAEDLAEWLGVE 175
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1193-1336 |
2.08e-35 |
|
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: 132.29 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1193 LDQSIMYEAEHNYLLKSLEKNLEIPKDCTYADQKAIDEETLQIVFgrvkCGKKGDTlKKLAR--RGIGYHHRSMTAKEKQ 1270
Cdd:cd18795 5 LEEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVF----CSSRKEC-EKTAKdlAGIAFHHAGLTREDRE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958693995 1271 LVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQNSVY-------LDALNYRQMSGRAGRRGQDLLGDVYFF 1336
Cdd:cd18795 80 LVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYdgkgyreLSPLEYLQMIGRAGRPGFDTRGEAIIM 152
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
765-1440 |
9.68e-34 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 138.10 E-value: 9.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 765 QRELLD-VVDNYESAVIVAPTSSGKTYASYYCMEKVLKESneGVVVYVAPTKALVNQVAATVQNRYtknmpggEALC--- 840
Cdd:COG1204 27 QAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNG--GKALYIVPLRALASEKYREFKRDF-------EELGikv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 841 GVFTRDYRHEAL---NSQVLITVPACFEILLLapHRQNWVKRIRYVIFDEVHCLG-GEIGAEIwEHLLVMIR--CP---F 911
Cdd:COG1204 98 GVSTGDYDSDDEwlgRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTL-EVLLARLRrlNPeaqI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 912 LALSATISNPQHLTEWLqsvkrywkqvdstmeqgsvsqrnaatrgsyhkdrvqarqsykvrlvlygeryndlekylcsvr 991
Cdd:COG1204 175 VALSATIGNAEEIAEWL--------------------------------------------------------------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 992 qgdvcfdhfhPCAALTTDhiekygfpsdlalspresiqlydtmcqvWKSWPQAQNLCPENFTQFKNKivikkldarkyee 1071
Cdd:COG1204 192 ----------DAELVKSD----------------------------WRPVPLNEGVLYDGVLRFDDG------------- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1072 slkeeftnwVKNGNEKEAQLVLKKLSPDyhdysGQMLDFFPclveklrkmeklpalfflfSLDTVEECAENVCEFLEEKQ 1151
Cdd:COG1204 221 ---------SRRSKDPTLALALDLLEEG-----GQVLVFVS-------------------SRRDAESLAKKLADELKRRL 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1152 EekrpPKADKEAYIMANKLRKVKKSLEKqkidekgqkssrrldqsimyeaehnyllksleknleipkdctyadqkaidee 1231
Cdd:COG1204 268 T----PEEREELEELAEELLEVSEETHT---------------------------------------------------- 291
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1232 tlqivfgrvkcgkkGDTLKKLARRGIGYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFA----QNS 1307
Cdd:COG1204 292 --------------NEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRdtkrGGM 357
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1308 VYLDALNYRQMSGRAGRRGQDLLGDVYFFDIPLPKIGKL----IKSKVPELRGQfpLSITLILRLMLLAT----KADDLE 1379
Cdd:COG1204 358 VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDEADELferyILGEPEPIRSK--LANESALRTHLLALiasgFANSRE 435
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958693995 1380 DgkakALSVLKHSLLSFKQPRatDMLKLYFLYSLQFLVKEGHIDQEGN---PTGFAGLVTHLNY 1440
Cdd:COG1204 436 E----LLDFLENTFYAYQYDK--GDLEEVVDDALEFLLENGFIEEDGDrlrATKLGKLVSRLYI 493
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
757-1401 |
3.61e-33 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 138.92 E-value: 3.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 757 QDFIPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESneGVVVYVAPTKALVNQVAATVQNRYtknmpgG 836
Cdd:COG4581 22 RGFELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALARG--RRSFYTAPIKALSNQKFFDLVERF------G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 837 EALCGVFTRDyrhEALNSQVLITVpaC-FEILL-LAPHRQNWVKRIRYVIFDEVHCLG-GEIGAeIWEhlLVMIRCP--- 910
Cdd:COG4581 94 AENVGLLTGD---ASVNPDAPIVV--MtTEILRnMLYREGADLEDVGVVVMDEFHYLAdPDRGW-VWE--EPIIHLParv 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 911 -FLALSATISNPQHLTEWLQSVkrywkqvdstmeqgsvsqrnaatRGSyhkdrvqarqsykVRLVLYGERyndlekylcs 989
Cdd:COG4581 166 qLVLLSATVGNAEEFAEWLTRV-----------------------RGE-------------TAVVVSEER---------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 990 vrqgdvcfdhfhpcaalttdhiekygfPSDLALSPRESiqlydtmcqvwkswpqaqnlcPENFTQFKnkiVIKKLdarky 1069
Cdd:COG4581 200 ---------------------------PVPLEFHYLVT---------------------PRLFPLFR---VNPEL----- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1070 eeslkeeftnwvkngnekeaqlvlkKLSPDYHDysgqmldffpcLVEKLRKMEKLPALFFLFS----LDTVEECAE-NVC 1144
Cdd:COG4581 224 -------------------------LRPPSRHE-----------VIEELDRGGLLPAIVFIFSrrgcDEAAQQLLSaRLT 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1145 efleekqeekrppkaDKEayimanklrkvkkslEKQKIDEkgqkssrrldqsimyeaehnyllksleknleipkdctYAD 1224
Cdd:COG4581 268 ---------------TKE---------------ERAEIRE-------------------------------------AID 280
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1225 QKAIDEETLQivfgrvkcgkkGDTLKKLARRGIGYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFA 1304
Cdd:COG4581 281 EFAEDFSVLF-----------GKTLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFT 349
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1305 QNS-------VYLDALNYRQMSGRAGRRGQDLLGDVY----FFDIPlPKIGKLIKSKVPELRGQFPLSITLILRlmLLAT 1373
Cdd:COG4581 350 KLSkfdgerhRPLTAREFHQIAGRAGRRGIDTEGHVVvlapEHDDP-KKFARLASARPEPLRSSFRPSYNMVLN--LLAR 426
|
650 660
....*....|....*....|....*...
gi 1958693995 1374 kaddleDGKAKALSVLKHSLLSFKQPRA 1401
Cdd:COG4581 427 ------PGLERARELLEDSFAQFQADRS 448
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
765-919 |
1.63e-21 |
|
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: 93.08 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 765 QRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESNEGV-VVYVAPTKALVNQVAATVQNRYTKNMPGGEALCGVF 843
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPqALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGD 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958693995 844 TRDYRHEAL-NSQVLITVPacfEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIR--CPFLALSATIS 919
Cdd:pfam00270 84 SRKEQLEKLkGPDILVGTP---GRLLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPkkRQILLLSATLP 159
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
759-928 |
1.87e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 759 FIPDTWQRELLD-VVDNYESAVIVAPTSSGKTYASYYCMEKVLKESNEGVVVYVAPTKALVNQVAATVQNRYTKNMPGGE 837
Cdd:smart00487 7 EPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 838 ALCGVFTRDYRHEALNS---QVLITVPACFEILLLapHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIR--CPFL 912
Cdd:smart00487 87 GLYGGDSKREQLRKLESgktDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPknVQLL 164
|
170
....*....|....*.
gi 1958693995 913 ALSATISNPQHLTEWL 928
Cdd:smart00487 165 LLSATPPEEIENLLEL 180
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
776-928 |
8.65e-18 |
|
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: 82.25 E-value: 8.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 776 ESAVIVAPTSSGKTYASYYC-MEKVLKESNEGV-VVYVAPTKALVNQVAatvqnrytKNMpggEALC---------GVFT 844
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPaLSSLADEPEKGVqVLYISPLKALINDQE--------RRL---EEPLdeidleipvAVRH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 845 RDY----RHEALNS--QVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCL-GGEIGAEI---WEHLLVMIRCPF--L 912
Cdd:cd17922 71 GDTsqseKAKQLKNppGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHALlGSKRGVQLellLERLRKLTGRPLrrI 150
|
170
....*....|....*.
gi 1958693995 913 ALSATISNPQHLTEWL 928
Cdd:cd17922 151 GLSATLGNLEEAAAFL 166
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1247-1443 |
5.19e-16 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 83.85 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1247 DTLKKLA---RRGIGYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVV------FAQNS--VYLDALNY 1315
Cdd:PRK02362 293 ETSKDLAdcvAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIirdyrrYDGGAgmQPIPVLEY 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1316 RQMSGRAGRRGQDLLG----------------DVYFFDIPLPkigklIKSKVPELRGqfplsitliLRLMLLATKADDLE 1379
Cdd:PRK02362 373 HQMAGRAGRPGLDPYGeavllaksydeldelfERYIWADPED-----VRSKLATEPA---------LRTHVLSTIASGFA 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958693995 1380 DGKAKALSVLKHSLLSFKQPRaTDMLKLYFLYSLQFLVKEGHIDQEGN---PTGFAGLVTHLnYHEP 1443
Cdd:PRK02362 439 RTRDGLLEFLEATFYATQTDD-TGRLERVVDDVLDFLERNGMIEEDGEtleATELGHLVSRL-YIDP 503
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
776-928 |
7.90e-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: 77.41 E-value: 7.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 776 ESAVIVAPTSSGKTYASYYCMEKVLKESNEGVVVYVAPTKALVNQVAATVQNRYTKNMpGGEA--LCGVFTRDYRhEALN 853
Cdd:cd18022 18 NNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKL-GKKVveLTGDVTPDMK-ALAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 854 SQVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGA----------EIWEHLLVMIRcpFLALSATISNPQH 923
Cdd:cd18022 96 ADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPvlevivsrmnYISSQTEKPVR--LVGLSTALANAGD 173
|
....*
gi 1958693995 924 LTEWL 928
Cdd:cd18022 174 LANWL 178
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1247-1452 |
1.54e-15 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 81.85 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1247 DTLKKLARRGIGYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQ-------NSVYLDALNYRQMS 1319
Cdd:PRK01172 278 DSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDitrygngGIRYLSNMEIKQMI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1320 GRAGRRGQDLLGDVYFF---------------DIPLPKIGKLIKSKVPELRgqfplsiTLILRLMLLATKADDLEDgkak 1384
Cdd:PRK01172 358 GRAGRPGYDQYGIGYIYaaspasydaakkylsGEPEPVISYMGSQRKVRFN-------TLAAISMGLASSMEDLIL---- 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1385 alsvLKHSLLSFKQpRATDMLKLYFLYSLQFLVKEGHIDQEG--NPTGFAGLVTHLNYHEPSNLVFVSFL 1452
Cdd:PRK01172 427 ----FYNETLMAIQ-NGVDEIDYYIESSLKFLKENGFIKGDVtlRATRLGKLTSDLYIDPESALILKSAF 491
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
765-928 |
2.88e-15 |
|
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: 75.45 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 765 QRELLD-VVDNYESAVIVAPTSSGKTYASYYCMEKVLkeSNEGVVVYVAPTKALVNQVAATVQNRYTknmPGGEalCGVF 843
Cdd:cd18028 6 QAEAVRaGLLKGENLLISIPTASGKTLIAEMAMVNTL--LEGGKALYLVPLRALASEKYEEFKKLEE---IGLK--VGIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 844 TRDYRHEAL---NSQVLITVPACFEILLlaPHRQNWVKRIRYVIFDEVHCLGGEIGAEIWEHLLVMIR-----CPFLALS 915
Cdd:cd18028 79 TGDYDEDDEwlgDYDIIVATYEKFDSLL--RHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnpnTQIIGLS 156
|
170
....*....|...
gi 1958693995 916 ATISNPQHLTEWL 928
Cdd:cd18028 157 ATIGNPDELAEWL 169
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
765-929 |
5.91e-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: 75.09 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 765 QRELL-DVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESNEG-----VVVYVAPTKALVNQVAATVQNRYtknmpGGEA 838
Cdd:cd18023 6 QSEVFpDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLpwgnrKVVYIAPIKALCSEKYDDWKEKF-----GPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 839 L-CGVFTRDYR----HEALNSQVLITVPACFE-ILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAEIwE---------HL 903
Cdd:cd18023 81 LsCAELTGDTEmddtFEIQDADIILTTPEKWDsMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATL-EvvvsrmktlSS 159
|
170 180 190
....*....|....*....|....*....|..
gi 1958693995 904 LVMIRCP------FLALSATISNPQHLTEWLQ 929
Cdd:cd18023 160 SSELRGStvrpmrFVAVSATIPNIEDLAEWLG 191
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
776-917 |
6.62e-15 |
|
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: 73.21 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 776 ESAVIVAPTSSGKTYASYYCMEKVLkESNEGVVVYVAPTKALVNQVAATVQNRYTKNMPggealCGVFTRDYRHE----- 850
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLL-LKKGKKVLVLVPTKALALQTAERLRELFGPGIR-----VAVLVGGSSAEerekn 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958693995 851 -ALNSQVLITVPACFEILLLAPHRQnWVKRIRYVIFDEVHCLGGeIGAEIWEHLLVMIR-----CPFLALSAT 917
Cdd:cd00046 76 kLGDADIIIATPDMLLNLLLREDRL-FLKDLKLIIVDEAHALLI-DSRGALILDLAVRKaglknAQVILLSAT 146
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
743-933 |
7.12e-15 |
|
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: 75.17 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 743 YLIREERKDPDPRVQDFIPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKESNEgvVVYVAPTKALVNQVA 822
Cdd:cd18024 15 PISAHKPPGNPARTYPFTLDPFQKTAIACIERNESVLVSAHTSAGKTVVAEYAIAQSLRDKQR--VIYTSPIKALSNQKY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 823 ATVQNRYtKNMpggealcGVFTRDYRHEALNSQVLITVpacfEILLLAPHRQNWVKR-IRYVIFDEVHCLGGEIGAEIWE 901
Cdd:cd18024 93 RELQEEF-GDV-------GLMTGDVTINPNASCLVMTT----EILRSMLYRGSEIMReVAWVIFDEIHYMRDKERGVVWE 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958693995 902 HLLV----MIRcpFLALSATISNPQHLTEWLQSVKR 933
Cdd:cd18024 161 ETIIllpdKVR--YVFLSATIPNARQFAEWICKIHK 194
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
765-926 |
1.46e-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: 79.11 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 765 QRELLDVVDNYESAVIVAPTSSGKTYAsyYC---MEKVLKESnEGVVVYVAPTKALVN-QVAATvqNRYTKNMpGGEALC 840
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLA--YLlpvLEALLEDP-GATALYLYPTKALARdQLRRL--RELAEAL-GLGVRV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 841 GVFT----RDYRHEAL-NSQVLITVPacfEIL---LLaPHRQNWV---KRIRYVIFDEVHCLGGEIGAeiweHLLVMIR- 908
Cdd:COG1205 135 ATYDgdtpPEERRWIReHPDIVLTNP---DMLhygLL-PHHTRWArffRNLRYVVIDEAHTYRGVFGS----HVANVLRr 206
|
170 180
....*....|....*....|....*....
gi 1958693995 909 ----CP-------FLALSATISNPQHLTE 926
Cdd:COG1205 207 lrriCRhygsdpqFILASATIGNPAEHAE 235
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
759-941 |
3.55e-14 |
|
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: 72.30 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 759 FIPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMekVLKESNEGVVVYVAPTKALVNQvaatvQNRYTKNMPGGea 838
Cdd:cd18027 7 FELDVFQKQAILHLEAGDSVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQ-----KFRDFKNTFGD-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 839 lCGVFTRDYRHEALNSQVLITVpacfEILLLAPHRQNWVKR-IRYVIFDEVHCLGGEIGAEIWEHLLVMI--RCPFLALS 915
Cdd:cd18027 78 -VGLITGDVQLNPEASCLIMTT----EILRSMLYNGSDVIRdLEWVIFDEVHYINDAERGVVWEEVLIMLpdHVSIILLS 152
|
170 180
....*....|....*....|....*.
gi 1958693995 916 ATISNPQHLTEWLQSVKRYWKQVDST 941
Cdd:cd18027 153 ATVPNTVEFADWIGRIKKKNIYVIST 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 ... |
776-928 |
8.67e-14 |
|
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: 71.52 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 776 ESAVIVAPTSSGKTYASYYCMEKVLKESNEGVVVYVAPTKALVNQVAATVQNRYTKNMPGG-EALCGVFTRDYRHEAlNS 854
Cdd:cd18021 20 DNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPLLGKKvVKLTGETSTDLKLLA-KS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 855 QVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGAeIWEHLLVMIR---------CPFLALSATISNPQHLT 925
Cdd:cd18021 99 DVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGP-VYEVVVSRMRyissqlekpIRIVGLSSSLANARDVG 177
|
...
gi 1958693995 926 EWL 928
Cdd:cd18021 178 EWL 180
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
742-917 |
8.75e-14 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 76.22 E-value: 8.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 742 HYLIREERKDPDPRVQ-DFIPDTWQRELLD-----VVDNYESAVIVAPTSSGKTYASYYCMEKVLkesNEGVVVYVAPTK 815
Cdd:COG1061 61 ELAEAEALEAGDEASGtSFELRPYQQEALEallaaLERGGGRGLVVAPTGTGKTVLALALAAELL---RGKRVLVLVPRR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 816 ALVNQVAATVQNRYTKNMPGGealcgvftrdyRHEALNSQVLITVPAcfeILLLAPHRQNWVKRIRYVIFDEVHclggEI 895
Cdd:COG1061 138 ELLEQWAEELRRFLGDPLAGG-----------GKKDSDAPITVATYQ---SLARRAHLDELGDRFGLVIIDEAH----HA 199
|
170 180
....*....|....*....|...
gi 1958693995 896 GAEIWEHLLVMIRCPF-LALSAT 917
Cdd:COG1061 200 GAPSYRRILEAFPAAYrLGLTAT 222
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1250-1326 |
1.30e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 67.62 E-value: 1.30e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958693995 1250 KKLARRGIGY--HHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFaQNSVYLDALNYRQMSGRAGRRG 1326
Cdd:smart00490 5 ELLKELGIKVarLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVI-IYDLPWSPASYIQRIGRAGRAG 82
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
764-917 |
1.05e-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: 66.95 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 764 WQRELLDVVDNYES---AVIVAPTSSGKTyasyYCMEKVLKESNEGVVVYVAPTKALVNQVAATVQNrytknmPGGEALC 840
Cdd:cd17926 4 YQEEALEAWLAHKNnrrGILVLPTGSGKT----LTALALIAYLKELRTLIVVPTDALLDQWKERFED------FLGDSSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 841 GVFTRDYRHEALNSQVLITVP----ACFEILLLAPHRQNwvkrirYVIFDEVHclggEIGAEIWEHLLVMIRCPF-LALS 915
Cdd:cd17926 74 GLIGGGKKKDFDDANVVVATYqslsNLAEEEKDLFDQFG------LLIVDEAH----HLPAKTFSEILKELNAKYrLGLT 143
|
..
gi 1958693995 916 AT 917
Cdd:cd17926 144 AT 145
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
765-923 |
1.11e-12 |
|
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: 68.00 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 765 QRELLDVVDNYESAVIVAPTSSGKTYAsyY---CMEKVLKESNeGVVVYVAPTKALVN-QVAATvqNRYTKNMpGGEALC 840
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLC--YqlpILEALLRDPG-SRALYLYPTKALAQdQLRSL--RELLEQL-GLGIRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 841 GVFTRDYRHEA------LNSQVLITVPACFEILLLAPHRQ--NWVKRIRYVIFDEVHCLGGEIGAeiweHLLVMIR---- 908
Cdd:cd17923 79 ATYDGDTPREErraiirNPPRILLTNPDMLHYALLPHHDRwaRFLRNLRYVVLDEAHTYRGVFGS----HVALLLRrlrr 154
|
170 180
....*....|....*....|....
gi 1958693995 909 -CP-------FLALSATISNP-QH 923
Cdd:cd17923 155 lCRrygadpqFILTSATIGNPaEH 178
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1249-1372 |
1.76e-12 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 72.16 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1249 LKKLARRGIGYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQNSVYLD-------ALNYRQMSGR 1321
Cdd:PRK00254 290 LKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNfgwedipVLEIQQMMGR 369
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958693995 1322 AGRRGQDLLGD---VYFFDIPLPKIGKLIKSKVPELRGQfpLSITLILRLMLLA 1372
Cdd:PRK00254 370 AGRPKYDEVGEaiiVATTEEPSKLMERYIFGKPEKLFSM--LSNESAFRSQVLA 421
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
778-917 |
7.87e-12 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 65.00 E-value: 7.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 778 AVIVAPTSSGKTYASYYCMEKVLKESNEGVVVYVAPTKALVNQvaatVQNRYTKNMPGGEALCGVFT-RDYRHEALNSQV 856
Cdd:pfam04851 26 GLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQ----ALEEFKKFLPNYVEIGEIISgDKKDESVDDNKI 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958693995 857 LI-TVPACFEILLLAPHrQNWVKRIRYVIFDEVHclggEIGAEIWEHLLVMIRCPF-LALSAT 917
Cdd:pfam04851 102 VVtTIQSLYKALELASL-ELLPDFFDVIIIDEAH----RSGASSYRNILEYFKPAFlLGLTAT 159
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
776-938 |
2.61e-11 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 68.31 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 776 ESAVIVAPTSSGKTYASYYCM-EKVLKESneGVVVYVAPTKALVNQvaatvqnRYtKNMPGGEAL---CGVFTRDY--RH 849
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMvNKLLREG--GKAVYLVPLKALAEE-------KY-REFKDWEKLglrVAMTTGDYdsTD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 850 EALNS-QVLITVPACFEILLlaPHRQNWVKRIRYVIFDEVHCLGG-EIGAE---IWEHLLVmiRCPFLALSATISNPQHL 924
Cdd:PRK00254 110 EWLGKyDIIIATAEKFDSLL--RHGSSWIKDVKLVVADEIHLIGSyDRGATlemILTHMLG--RAQILGLSATVGNAEEL 185
|
170
....*....|....*.
gi 1958693995 925 TEWLQS--VKRYWKQV 938
Cdd:PRK00254 186 AEWLNAelVVSDWRPV 201
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
753-928 |
1.46e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 59.73 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 753 DPRVQDFIPDTW------QRELLDVVDNYESAVIVAPTSSGKTYASY------YCMEKVLKESNEGV-VVYVAPTKALVN 819
Cdd:COG1201 11 HPAVRAWFAARFgaptppQREAWPAIAAGESTLLIAPTGSGKTLAAFlpaldeLARRPRPGELPDGLrVLYISPLKALAN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 820 QVAatvqnrytKNM--PGGE--ALCGVFTRDYRHEALNS---------------QVLITVPACFEILLLAPHRQNWVKRI 880
Cdd:COG1201 91 DIE--------RNLraPLEEigEAAGLPLPEIRVGVRTGdtpaserqrqrrrppHILITTPESLALLLTSPDARELLRGV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958693995 881 RYVIFDEVHCLGG-------EIGAEIWEHL----LVMIrcpflALSATISNPQHLTEWL 928
Cdd:COG1201 163 RTVIVDEIHALAGskrgvhlALSLERLRALaprpLQRI-----GLSATVGPLEEVARFL 216
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
759-889 |
1.72e-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: 56.33 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 759 FIPDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLKE----SNEGVVVYVAPTKALVNQvAATVQNRYTKNMP 834
Cdd:cd18036 1 LELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKrrsaGEKGRVVVLVNKVPLVEQ-QLEKFFKYFRKGY 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958693995 835 GGEALCGVFTRD--YRHEALNSQVLITVPACFEILLLAPhRQNwvKRIRY-----VIFDEVH 889
Cdd:cd18036 80 KVTGLSGDSSHKvsFGQIVKASDVIICTPQILINNLLSG-REE--ERVYLsdfslLIFDECH 138
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1235-1326 |
5.05e-08 |
|
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: 52.60 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1235 IVFGRVKCGKKGDTLKKLARRGIGYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFaQNSVYLDALN 1314
Cdd:pfam00271 19 LIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVI-NYDLPWNPAS 97
|
90
....*....|..
gi 1958693995 1315 YRQMSGRAGRRG 1326
Cdd:pfam00271 98 YIQRIGRAGRAG 109
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
764-917 |
3.74e-07 |
|
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: 54.70 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 764 WQRELLDVVDNYESA-----VIVAPTSSGKTYASYYCMEKVLKESNEGVVVYVAPTKALVNQVAATVQNRYTK------- 831
Cdd:COG1203 131 LQNEALELALEAAEEepglfILTAPTGGGKTEAALLFALRLAAKHGGRRIIYALPFTSIINQTYDRLRDLFGEdvllhhs 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 832 ----NMPGGEALCGVFTRDYRH--EALNSQVLITVPACFEILLLAPHRQNWVKRIRY----VIFDEVHClggeIGAEIWE 901
Cdd:COG1203 211 ladlDLLEEEEEYESEARWLKLlkELWDAPVVVTTIDQLFESLFSNRKGQERRLHNLansvIILDEVQA----YPPYMLA 286
|
170 180
....*....|....*....|..
gi 1958693995 902 HLLVMIR------CPFLALSAT 917
Cdd:COG1203 287 LLLRLLEwlknlgGSVILMTAT 308
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
779-917 |
4.51e-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: 51.91 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 779 VIVAPTSSGKTYASYYCMEKVLKESNEGVVVYVAPTKALVNQVAATVQN----------------------RYTKNMPGG 836
Cdd:cd17930 5 ILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINQMYERIREilgrlddedkvlllhskaalelLESDEEPDD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 837 EALCGVFTRDYRHEALNSQVLITVPacFEILL-LAPHRQNWVK--RI--RYVIFDEVHCLGGEIGAEIWEHLLVMIR--- 908
Cdd:cd17930 85 DPVEAVDWALLLKRSWLAPIVVTTI--DQLLEsLLKYKHFERRlhGLanSVVVLDEVQAYDPEYMALLLKALLELLGelg 162
|
....*....
gi 1958693995 909 CPFLALSAT 917
Cdd:cd17930 163 GPVVLMTAT 171
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
776-920 |
9.64e-07 |
|
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: 51.22 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 776 ESAVIVAPTSSGKTYASYYCM-EKVLKESNE--GV------VVYVAPTKALVNQVAATVQNRYT------KNMPGGEALC 840
Cdd:cd18019 34 ENLLLCAPTGAGKTNVALLTIlREIGKHRNPdgTInldafkIVYIAPMKALVQEMVGNFSKRLApygitvAELTGDQQLT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 841 gvftrdyRHEALNSQVLITVPACFEILLLAPHRQNWVKRIRYVIFDEVHCLGGEIGA--------EIW--EHLLVMIRcp 910
Cdd:cd18019 114 -------KEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDDRGPvlesivarTIRqiEQTQEYVR-- 184
|
170
....*....|
gi 1958693995 911 FLALSATISN 920
Cdd:cd18019 185 LVGLSATLPN 194
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
776-920 |
1.06e-05 |
|
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: 47.81 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 776 ESAVIVAPTSSGKTYASYYCMEKVLKES---------NEGVVVYVAPTKALvnqvAATVQNRYTKNMpggeALCGVFTRD 846
Cdd:cd18020 18 ENMLICAPTGAGKTNIAMLTILHEIRQHvnqggvikkDDFKIVYIAPMKAL----AAEMVEKFSKRL----APLGIKVKE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 847 Y-------RHEALNSQVLITVPACFEILLLAPHRQN-WVKRIRYVIFDEVHCLGGEIGAEIwEHLLV-----------MI 907
Cdd:cd18020 90 LtgdmqltKKEIAETQIIVTTPEKWDVVTRKSSGDVaLSQLVRLLIIDEVHLLHDDRGPVI-ESLVArtlrqvestqsMI 168
|
170
....*....|...
gi 1958693995 908 RcpFLALSATISN 920
Cdd:cd18020 169 R--IVGLSATLPN 179
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1235-1345 |
2.90e-05 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 48.73 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1235 IVF--GRVKCgkkgdtlKKLARR-GIG--YHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCKSVVFAQNSVY 1309
Cdd:COG1202 431 IIFtnSRRRC-------HEIARAlGYKaaPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSLAMG 503
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958693995 1310 LDALN---YRQMSGRAGRRGQDLLGDVYFfdipLPKIGK 1345
Cdd:COG1202 504 IEWLSvqeFHQMLGRAGRPDYHDRGKVYL----LVEPGK 538
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
1257-1327 |
3.15e-05 |
|
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: 45.72 E-value: 3.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958693995 1257 IGYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINM-PCKSVVfaQNSVYLDALNYRQMSGRAGRRGQ 1327
Cdd:cd18796 71 IALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIgDVDLVI--QIGSPKSVARLLQRLGRSGHRPG 140
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
759-920 |
3.34e-05 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 46.49 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 759 FIPDTWQRELLDVVDNyESAVIVAPTSSGKTYASyyCM------EKVLKESNEG-VVVYVAPTKALVNQVAATVQNrYTK 831
Cdd:cd18034 1 FTPRSYQLELFEAALK-RNTIVVLPTGSGKTLIA--VMlikemgELNRKEKNPKkRAVFLVPTVPLVAQQAEAIRS-HTD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 832 nmPGGEALCG-----VFTRDYRHEAL-NSQVLITVPACFEILLlaphRQNWVK--RIRYVIFDEVH-CLGGEIGAEI--- 899
Cdd:cd18034 77 --LKVGEYSGemgvdKWTKERWKEELeKYDVLVMTAQILLDAL----RHGFLSlsDINLLIFDECHhATGDHPYARImke 150
|
170 180
....*....|....*....|..
gi 1958693995 900 WEHLLVMIRCP-FLALSATISN 920
Cdd:cd18034 151 FYHLEGRTSRPrILGLTASPVN 172
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
761-924 |
4.41e-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: 46.27 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 761 PDTWQRELLDVVDNYESAVIVAPTSSGKTYASYYCMEKVLK---ESNEGVVVYVAPTKALVNQvAATVQNRYTkNMPGGE 837
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKkfpAGRKGKVVFLANKVPLVEQ-QKEVFRKHF-ERPGYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 838 --ALCG---VFTRDYrHEALNSQVLITVPACFEILLLAPhRQNWVKRIRYVIFDEVHCLGGEigaeiWEHLLVMIRCPFL 912
Cdd:cd17927 81 vtGLSGdtsENVSVE-QIVESSDVIIVTPQILVNDLKSG-TIVSLSDFSLLVFDECHNTTKN-----HPYNEIMFRYLDQ 153
|
170
....*....|..
gi 1958693995 913 ALSATISNPQHL 924
Cdd:cd17927 154 KLGSSGPLPQIL 165
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1261-1330 |
6.55e-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: 47.52 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1261 HRS-MTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCksvvfaqnsvyLDA----------LNYRQMSGRAGRRGQDL 1329
Cdd:COG1205 324 YRAgYLPEERREIERGLRSGELLGVVSTNALELGIDIGG-----------LDAvvlagypgtrASFWQQAGRAGRRGQDS 392
|
.
gi 1958693995 1330 L 1330
Cdd:COG1205 393 L 393
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
780-889 |
1.86e-04 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 45.88 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 780 IVAPTSSGKTYASYYCMEKVLKESNeGVVVYVAPTKALVNQVAATvqnrYTKNMPGGEALCGVFT----RDYRHEALN-S 854
Cdd:COG1111 22 VVLPTGLGKTAVALLVIAERLHKKG-GKVLFLAPTKPLVEQHAEF----FKEALNIPEDEIVVFTgevsPEKRKELWEkA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958693995 855 QVLITVPACFEILLLAphrqnwvKRIR-----YVIFDEVH 889
Cdd:COG1111 97 RIIVATPQVIENDLIA-------GRIDlddvsLLIFDEAH 129
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
1247-1327 |
2.11e-04 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 42.58 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1247 DTLKKLARRGI--GYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPckSVVF-AQNSVYLDALNYRQMSGRAG 1323
Cdd:cd18794 45 QVAARLQSKGIsaAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKP--DVRFvIHYSLPKSMESYYQESGRAG 122
|
....
gi 1958693995 1324 RRGQ 1327
Cdd:cd18794 123 RDGL 126
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
1255-1330 |
8.95e-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: 41.09 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1255 RGiGYhhrsmTAKEKQLVEILFRKGFIRVVTATGTLALGINMPCksvvfaqnsvyLDAL----------NYRQMSGRAGR 1324
Cdd:cd18797 73 RA-GY-----LAEDRREIEAELFNGELLGVVATNALELGIDIGG-----------LDAVvlagypgslaSLWQQAGRAGR 135
|
....*.
gi 1958693995 1325 RGQDLL 1330
Cdd:cd18797 136 RGKDSL 141
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
777-889 |
1.76e-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: 40.96 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 777 SAVIVAPTSSGKTYASYYCMEKVLkESNEGVVVYVAPTKALVNQVAATVQNRYTKNMPgGEALCGVFTRDYRHEALN-SQ 855
Cdd:cd18035 18 NTLIVLPTGLGKTIIAILVAADRL-TKKGGKVLILAPSRPLVEQHAENLKRVLNIPDK-ITSLTGEVKPEERAERWDaSK 95
|
90 100 110
....*....|....*....|....*....|....
gi 1958693995 856 VLITVPACFEILLLApHRQNwVKRIRYVIFDEVH 889
Cdd:cd18035 96 IIVATPQVIENDLLA-GRIT-LDDVSLLIFDEAH 127
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
779-931 |
2.27e-03 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 42.03 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 779 VIVAPTSSGKTYASYYCMEKVLKESNEGVVVYVAPTKALVNQVAATVQN--------------RYTKNMPGGEALCGVFT 844
Cdd:cd09639 3 VIEAPTGYGKTEAALLWALHSLKSQKADRVIIALPTRATINAMYRRAKEafgetglyhssilsSRIKEMGDSEEFEHLFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 845 RDYRHEALNSQVLITVPACFEIL----LLAPHRQNWVKRIRY--VIFDEVHClggeIGAEIWEHLLVMIR------CPFL 912
Cdd:cd09639 83 LYIHSNDTLFLDPITVCTIDQVLksvfGEFGHYEFTLASIANslLIFDEVHF----YDEYTLALILAVLEvlkdndVPIL 158
|
170
....*....|....*....
gi 1958693995 913 ALSATIsnPQHLTEWLQSV 931
Cdd:cd09639 159 LMSATL--PKFLKEYAEKI 175
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
1239-1326 |
2.34e-03 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 42.39 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1239 RVKCG--------KKGDTLKKLARRGI--GYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPckSVVFAqnsV 1308
Cdd:PRK11057 235 RGKSGiiycnsraKVEDTAARLQSRGIsaAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKP--NVRFV---V 309
|
90 100
....*....|....*....|..
gi 1958693995 1309 YLD----ALNYRQMSGRAGRRG 1326
Cdd:PRK11057 310 HFDiprnIESYYQETGRAGRDG 331
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
779-931 |
2.45e-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: 42.06 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 779 VIVAPTSSGKTYASYYCMEKVLKESNEGVVVYVAPTKALVNQVAATV---------------QNRYTKNMPGGEALCGVF 843
Cdd:TIGR01587 3 VIEAPTGYGKTEAALLWALHSIKSQKADRVIIALPTRATINAMYRRAkelfgselvglhhssSFSRIKEMGDSEEFEHLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 844 TRDYRHEALNSQVLITVPACFEIL----LLAPHRQNWVKRIRY--VIFDEVHClggeIGAEIWEHLLVMIR------CPF 911
Cdd:TIGR01587 83 PLYIHSNDKLFLDPITVCTIDQVLksvfGEFGHYEFTLASIANslLIFDEVHF----YDEYTLALILAVLEvlkdndVPI 158
|
170 180
....*....|....*....|
gi 1958693995 912 LALSATIsnPQHLTEWLQSV 931
Cdd:TIGR01587 159 LLMSATL--PKFLKEYAEKI 176
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
1239-1327 |
5.24e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 41.42 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 1239 RVKCGKKGDTLKKLARRGiGYHHRSMTAKEKQLVEILFRKGFIRVVTATGTLALGINMPckSVVFA-QNSVYLDALNYRQ 1317
Cdd:PLN03137 690 RMDCEKVAERLQEFGHKA-AFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKP--DVRFViHHSLPKSIEGYHQ 766
|
90
....*....|
gi 1958693995 1318 MSGRAGRRGQ 1327
Cdd:PLN03137 767 ECGRAGRDGQ 776
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
1267-1336 |
8.04e-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: 40.63 E-value: 8.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958693995 1267 KEKqlVEIlFRKGFIRVVTATGTLALGINMPCKSV--VFAQNSVY-LDALnyRQMSGRAGRRGQDLLGDVYFF 1336
Cdd:COG4098 359 KEK--VQA-FRDGEIPILVTTTILERGVTFPNVDVavLGADHPVFtEAAL--VQIAGRVGRSADYPTGEVIFF 426
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
770-887 |
9.06e-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: 39.67 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958693995 770 DVVDNYESAVIVAPTSSGKTYAsyYCMEKV--LKESNEGV------------------VVYVAPTKALVNQVAATVQNRY 829
Cdd:cd17965 56 NEEPKLEVFLLAAETGSGKTLA--YLAPLLdyLKRQEQEPfeeaeeeyesakdtgrprSVILVPTHELVEQVYSVLKKLS 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958693995 830 TKNMPGGEALCGVFTRDYRHEALNSQ----VLITVPacFEILLLAPHRQNWVKRIRYVIFDE 887
Cdd:cd17965 134 HTVKLGIKTFSSGFGPSYQRLQLAFKgridILVTTP--GKLASLAKSRPKILSRVTHLVVDE 193
|
|
| |
