|
Name |
Accession |
Description |
Interval |
E-value |
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
193-731 |
6.14e-102 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 336.48 E-value: 6.14e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 193 FNKVQSEVFGDVYESDENLVVSAPTGSGKTTIFELAFLHNLSfrtpndsLKPLAVYIAPTKALCNEKAKDWQERLGQALP 272
Cdd:COG1204 23 LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALL-------NGGKALYIVPLRALASEKYREFKRDFEELGI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 273 DVicTEITGDYgnTSTIYNSIRgADLIVTTPEKFDSMTRRSRNLGNmsqRLQLIMIDEVHILR-ESRGATLEVVISRLKG 351
Cdd:COG1204 96 KV--GVSTGDY--DSDDEWLGR-YDILVATPEKLDSLLRNGPSWLR---DVDLVVVDEAHLIDdESRGPTLEVLLARLRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 352 LSRDIRFIALSATVPNIDDIARWLGptrneygqlsrgvlvgrevinakekraltvddmpmAKVYKfgEEYRPVPLQRVTY 431
Cdd:COG1204 168 LNPEAQIVALSATIGNAEEIAEWLD-----------------------------------AELVK--SDWRPVPLNEGVL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 432 giesVGNDWALANRLDKELYPI--LLKHTAGQ--PVLVFCPTRKSCQATVESIfqsyeearAKGLNLPWKHPPGVRLE-- 505
Cdd:COG1204 211 ----YDGVLRFDDGSRRSKDPTlaLALDLLEEggQVLVFVSSRRDAESLAKKL--------ADELKRRLTPEEREELEel 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 506 -----------LQDKKLAELSTCGIAVHHAGLDYADRRAIEDGFRDGKLHMIASTSTLAVGVNLPAHTVVIKGVMawqga 574
Cdd:COG1204 279 aeellevseetHTNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTK----- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 575 SSGFQEYSDIDIQQMVGRAGRPQYDTSGVVVVMCERSK-----VRKY----QSMLNSQTVLESCLHENLteyiNSEIGQG 645
Cdd:COG1204 354 RGGMVPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDeadelFERYilgePEPIRSKLANESALRTHL----LALIASG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 646 TIKSVSSAQEWLKNSFfhiriqqnpkYYALSDAKDkpvegaweewLDHYVEKALINLEKDGFIERsDDDTLTPTETGKIM 725
Cdd:COG1204 430 FANSREELLDFLENTF----------YAYQYDKGD----------LEEVVDDALEFLLENGFIEE-DGDRLRATKLGKLV 488
|
....*.
gi 321261834 726 SSSMIS 731
Cdd:COG1204 489 SRLYID 494
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
192-388 |
2.76e-99 |
|
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: 316.61 E-value: 2.76e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 192 CFNKVQSEVFGDVYESDENLVVSAPTGSGKTTIFELAFLHNLSFRTPNDSLKPLAVYIAPTKALCNEKAKDWQERLGQal 271
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 272 PDVICTEITGDYGNTSTiyNSIRGADLIVTTPEKFDSMTRRSRNLGNMSQRLQLIMIDEVHILRESRGATLEVVISRLKG 351
Cdd:cd18023 79 LGLSCAELTGDTEMDDT--FEIQDADIILTTPEKWDSMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 321261834 352 LSR----------DIRFIALSATVPNIDDIARWLG---PTRNEYGQLSRG 388
Cdd:cd18023 157 LSSsselrgstvrPMRFVAVSATIPNIEDLAEWLGdnpAGCFSFGESFRP 206
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
718-1042 |
5.90e-60 |
|
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl domain) protein in which it was found. This protein is required for assembly of functional endoplasmic reticulum translocons. Other yeast proteins containing this domain include pre-mRNA splicing helicase BRR2, HFM1 protein and putative helicases.
Pssm-ID: 214946 Cd Length: 314 Bit Score: 208.75 E-value: 5.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 718 PTETGKIMSSSMISYGTMCSI-KAMSPRSTVQDLLEILAGSTEFKDLRIRQGESSFLNKLrtNEEIRFPLAEAVK-SYAD 795
Cdd:smart00973 1 PTELGRIASYYYISYETIETFnQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNEL--NKRVPIPVKEGIIdSPHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 796 KVFLLLQVTFGNIILEDIAKKTELTSPIQtlmaiynHAPRIAKAIVQFTLNCEYGVAARSALELHRVVVGKAWEDLPTVF 875
Cdd:smart00973 79 KVNLLLQAHLSRLPLPDFDLVSDLKYILQ-------NAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEDSDSPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 876 RQIPSIGPKSI--RVLGQNGVTNFDQLLDVESEKIQLWLNRGHDFARAIHEQARRMPRFHVTMEEENMDYDGTYNVlnlR 953
Cdd:smart00973 152 KQLPHFLIEDVydKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITRDLTLRV---E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 954 VNIAPKTKVIATESKGKRGGFitqynlsTLFLSQ--TGRFIGYRRLELKKLIKNKDNSFIIAVTL-NKRCDSVTAIVGVD 1030
Cdd:smart00973 229 LEITPVFAWDLPRHKGKSESW-------WLVVGDsdTNELLAIKRVTLRKKKKSNEVKLDFTVPLsEPGPENYTVYLISD 301
|
330
....*....|..
gi 321261834 1031 EVAGSSTVISFN 1042
Cdd:smart00973 302 SYLGCDQEVSFS 313
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
422-609 |
1.05e-57 |
|
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: 196.23 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 422 RPVPLQRVTYGIESVGNDWALANRL----DKELYPILLKHTAGQPVLVFCPTRKSCQATVESIFqsyeearakglnlpwk 497
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNkfdsDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 498 hppgvrlelqdkklaelstcGIAVHHAGLDYADRRAIEDGFRDGKLHMIASTSTLAVGVNLPAHTVVIKGVMAWQGasSG 577
Cdd:cd18795 65 --------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDG--KG 122
|
170 180 190
....*....|....*....|....*....|..
gi 321261834 578 FQEYSDIDIQQMVGRAGRPQYDTSGVVVVMCE 609
Cdd:cd18795 123 YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
193-378 |
2.18e-57 |
|
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: 196.33 E-value: 2.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 193 FNKVQSEVFGDVYESDENLVVSAPTGSGKTTIFELAFLHNLSfrtpndSLKPLAVYIAPTKALCNEKAKDWQERLGQALP 272
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALA------TSGGKAVYIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 273 DVIctEITGDygnTSTIYNSIRGADLIVTTPEKFDSMTRRSRNLgnMSQRLQLIMIDEVHILR-ESRGATLEVVISRLKG 351
Cdd:cd17921 76 NVG--LLTGD---PSVNKLLLAEADILVATPEKLDLLLRNGGER--LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLR 148
|
170 180
....*....|....*....|....*..
gi 321261834 352 LSRDIRFIALSATVPNIDDIARWLGPT 378
Cdd:cd17921 149 INKNARFVGLSATLPNAEDLAEWLGVE 175
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
209-776 |
1.70e-54 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 204.42 E-value: 1.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 209 ENLVVSAPTGSGKTTIFELAFLHNLSfrtpndsLKPLAVYIAPTKALCNEKAKDWQ--ERLGqalpdvICTEI-TGDYGN 285
Cdd:PRK02362 40 KNLLAAIPTASGKTLIAELAMLKAIA-------RGGKALYIVPLRALASEKFEEFErfEELG------VRVGIsTGDYDS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 286 TSTiYNSIRgaDLIVTTPEKFDSMTRrsrNLGNMSQRLQLIMIDEVHIL-RESRGATLEVVISRLKGLSRDIRFIALSAT 364
Cdd:PRK02362 107 RDE-WLGDN--DIIVATSEKVDSLLR---NGAPWLDDITCVVVDEVHLIdSANRGPTLEVTLAKLRRLNPDLQVVALSAT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 365 VPNIDDIARWLG---------PTRneygqLSRGVLVGRevinakekrALTvddmpmakvykFGEEYRPVPLQRvtygies 435
Cdd:PRK02362 181 IGNADELADWLDaelvdsewrPID-----LREGVFYGG---------AIH-----------FDDSQREVEVPS------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 436 vgNDWALANRLD--KElypillkhtAGQpVLVFCPTRKSCQA-------TVESIFQSYEEARAKGLnlpwkhPPGVRlEL 506
Cdd:PRK02362 229 --KDDTLNLVLDtlEE---------GGQ-CLVFVSSRRNAEGfakraasALKKTLTAAERAELAEL------AEEIR-EV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 507 QDKKLAE-LSTC---GIAVHHAGLDYADRRAIEDGFRDGKLHMIASTSTLAVGVNLPAHTVVIKgvmAWQ--GASSGFQE 580
Cdd:PRK02362 290 SDTETSKdLADCvakGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIR---DYRryDGGAGMQP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 581 YSDIDIQQMVGRAGRPQYDTSGVVVVMC----ERSKVRKYQSMLNSQTVLESCLHEN-LTEYINSEIGQGTIKSVSSAQE 655
Cdd:PRK02362 367 IPVLEYHQMAGRAGRPGLDPYGEAVLLAksydELDELFERYIWADPEDVRSKLATEPaLRTHVLSTIASGFARTRDGLLE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 656 WLKNSFFhiriqqnpkyyalsdAKDKPVEGAweewLDHYVEKALINLEKDGFIERsDDDTLTPTETGKI--------MSS 727
Cdd:PRK02362 447 FLEATFY---------------ATQTDDTGR----LERVVDDVLDFLERNGMIEE-DGETLEATELGHLvsrlyidpLSA 506
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 321261834 728 SMISYGtMCSIKAMSPRStvqdLLEILAGSTEFKDLRIRQGESSFLNKL 776
Cdd:PRK02362 507 AEIIDG-LEAAKKPTDLG----LLHLVCSTPDMYELYLRSGDYEWLNEY 550
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
206-607 |
1.05e-49 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 190.15 E-value: 1.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 206 ESDENLVVSAPTGSGKTTIFElaFLHNLSFRTPNDSlkplaVYIAPTKALCNEKAKDWQERLGQA---LpdvicteITGD 282
Cdd:COG4581 38 EAGRSVLVAAPTGSGKTLVAE--FAIFLALARGRRS-----FYTAPIKALSNQKFFDLVERFGAEnvgL-------LTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 283 ygntstiyNSI-RGADLIVTTPEKFDSMT-RRSRNLgnmsQRLQLIMIDEVHILRE-SRGATLEVVISrlkGLSRDIRFI 359
Cdd:COG4581 104 --------ASVnPDAPIVVMTTEILRNMLyREGADL----EDVGVVVMDEFHYLADpDRGWVWEEPII---HLPARVQLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 360 ALSATVPNIDDIARWLGPTRNEygqlsrgvlvgREVINakekraltvddmpmakvykfgEEYRPVPL-QRVtygieSVGN 438
Cdd:COG4581 169 LLSATVGNAEEFAEWLTRVRGE-----------TAVVV---------------------SEERPVPLeFHY-----LVTP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 439 DWALANRLDKELYPIL--------LKHTAGQPVLVFCPTRKSCQATVESI----FQSYEEARA-KGLNLPWKHPPGVrle 505
Cdd:COG4581 212 RLFPLFRVNPELLRPPsrhevieeLDRGGLLPAIVFIFSRRGCDEAAQQLlsarLTTKEERAEiREAIDEFAEDFSV--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 506 LQDKKLAELSTCGIAVHHAGLDYADRRAIEDGFRDGKLHMIASTSTLAVGVNLPAHTVVIKGVMAWQGasSGFQEYSDID 585
Cdd:COG4581 289 LFGKTLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDG--ERHRPLTARE 366
|
410 420
....*....|....*....|..
gi 321261834 586 IQQMVGRAGRPQYDTSGVVVVM 607
Cdd:COG4581 367 FHQIAGRAGRRGIDTEGHVVVL 388
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
209-730 |
1.68e-48 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 185.09 E-value: 1.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 209 ENLVVSAPTGSGKTTIFELAFlhnlsFRTPNDSLKplAVYIAPTKALCNEKakdWQERLGQALPDVICTEITGDYGNTST 288
Cdd:PRK01172 38 ENVIVSVPTAAGKTLIAYSAI-----YETFLAGLK--SIYIVPLRSLAMEK---YEELSRLRSLGMRVKISIGDYDDPPD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 289 IynsIRGADLIVTTPEKFDSMTRRSRNLGNmsqRLQLIMIDEVHILR-ESRGATLEVVISRLKGLSRDIRFIALSATVPN 367
Cdd:PRK01172 108 F---IKRYDVVILTSEKADSLIHHDPYIIN---DVGLIVADEIHIIGdEDRGPTLETVLSSARYVNPDARILALSATVSN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 368 IDDIARWLgptrneygqlsrgvlvgreviNAkekrALTVDDmpmakvykfgeeYRPVPLQRVTYGIESVGNDWALANRLD 447
Cdd:PRK01172 182 ANELAQWL---------------------NA----SLIKSN------------FRPVPLKLGILYRKRLILDGYERSQVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 448 KELypiLLKHTA--GQPVLVFCPTRKSCQATVESIFQSYEEARakglNLPWKHPPGvrlELQDKKLAELSTCGIAVHHAG 525
Cdd:PRK01172 225 INS---LIKETVndGGQVLVFVSSRKNAEDYAEMLIQHFPEFN----DFKVSSENN---NVYDDSLNEMLPHGVAFHHAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 526 LDYADRRAIEDGFRDGKLHMIASTSTLAVGVNLPAHTVVIKGVMAWqgASSGFQEYSDIDIQQMVGRAGRPQYDTSGVVV 605
Cdd:PRK01172 295 LSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDITRY--GNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 606 VmcerskvrkYQSMLNSQTVLESCLHENlTEYINSEIGQ------GTIKSVSSAqewLKNSFFHIRIQQNPKYYALSDAK 679
Cdd:PRK01172 373 I---------YAASPASYDAAKKYLSGE-PEPVISYMGSqrkvrfNTLAAISMG---LASSMEDLILFYNETLMAIQNGV 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 321261834 680 DKpvegaweewLDHYVEKALINLEKDGFIErsDDDTLTPTETGKIMSSSMI 730
Cdd:PRK01172 440 DE---------IDYYIESSLKFLKENGFIK--GDVTLRATRLGKLTSDLYI 479
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
209-628 |
2.37e-48 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 185.41 E-value: 2.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 209 ENLVVSAPTGSGKTTIFELAFLHNLsfrtpndsLKP--LAVYIAPTKALCNEKA---KDWqERLGQALpdvicTEITGDY 283
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKL--------LREggKAVYLVPLKALAEEKYrefKDW-EKLGLRV-----AMTTGDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 284 GNTStiyNSIRGADLIVTTPEKFDSMTRR-SRNLGNmsqrLQLIMIDEVHIL-RESRGATLEVVISRLKGLSRdirFIAL 361
Cdd:PRK00254 106 DSTD---EWLGKYDIIIATAEKFDSLLRHgSSWIKD----VKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ---ILGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 362 SATVPNIDDIARWLgptrneygqlsrgvlvgreviNAKekraLTVDDmpmakvykfgeeYRPVPLQR-VTY--------- 431
Cdd:PRK00254 176 SATVGNAEELAEWL---------------------NAE----LVVSD------------WRPVKLRKgVFYqgflfwedg 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 432 GIESVGNDWalanrlDKELYPILLKhtaGQPVLVFCPTRKSCQAT-------VESIFQSYEEARAKGLNLPWKHPPgvrl 504
Cdd:PRK00254 219 KIERFPNSW------ESLVYDAVKK---GKGALVFVNTRRSAEKEalelakkIKRFLTKPELRALKELADSLEENP---- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 505 elQDKKLAELSTCGIAVHHAGLDYADRRAIEDGFRDGKLHMIASTSTLAVGVNLPAHTVVIKGVmaWQGASSGFQEYSDI 584
Cdd:PRK00254 286 --TNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDT--KRYSNFGWEDIPVL 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 321261834 585 DIQQMVGRAGRPQYDTSG--VVVVMCE----------RSKVRKYQSMLNSQTVLES 628
Cdd:PRK00254 362 EIQQMMGRAGRPKYDEVGeaIIVATTEepsklmeryiFGKPEKLFSMLSNESAFRS 417
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
190-376 |
4.58e-48 |
|
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: 170.13 E-value: 4.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 190 FPCFNKVQSEVFGDVYESDENLVVSAPTGSGKTTIFELAFLHnlSFRTPNDSlkpLAVYIAPTKALCNEKAKDWQERLGQ 269
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLR--HWRQNPKG---RAVYIAPMQELVDARYKDWRAKFGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 270 ALPDVIcTEITGDygnTSTIYNSIRGADLIVTTPEKFDSMTRRSRNLGNMsQRLQLIMIDEVHILRESRGATLEVVISRL 349
Cdd:cd18021 76 LLGKKV-VKLTGE---TSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNV-QSVELFIADELHLIGGENGPVYEVVVSRM 150
|
170 180 190
....*....|....*....|....*....|.
gi 321261834 350 K----GLSRDIRFIALSATVPNIDDIARWLG 376
Cdd:cd18021 151 RyissQLEKPIRIVGLSSSLANARDVGEWLG 181
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
193-376 |
1.02e-44 |
|
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: 160.23 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 193 FNKVQSEVFGDVYESDENLVVSAPTGSGKTTIFELAFlhnlsFRTPNDSLKPLAVYIAPTKALCNEKAKDWQERLGQALP 272
Cdd:cd18022 2 FNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAM-----FRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 273 DVIcTEITGDYgnTSTIyNSIRGADLIVTTPEKFDSMTrRSRNLGNMSQRLQLIMIDEVHILRESRGATLEVVISRLKGL 352
Cdd:cd18022 77 KKV-VELTGDV--TPDM-KALADADIIITTPEKWDGIS-RSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYI 151
|
170 180
....*....|....*....|....*...
gi 321261834 353 SRD----IRFIALSATVPNIDDIARWLG 376
Cdd:cd18022 152 SSQtekpVRLVGLSTALANAGDLANWLG 179
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
173-731 |
1.93e-38 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 155.82 E-value: 1.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 173 PLVPLSRLPMDqrKLFKFPCFNK------VQS-EVFGDVYESDENLVVSApTGSGKTTIFELAFLHNLSfrtpNDSLKPL 245
Cdd:COG1202 186 DTVPVDDLDLP--PELKDLLEGRgeellpVQSlAVENGLLEGKDQLVVSA-TATGKTLIGELAGIKNAL----EGKGKML 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 246 avYIAPTKALCNEKAKDWQERLGQALpDVicTEITGdygnTSTI----YNSIRGADLIVTTPEKFDSMTRRSRNLGNMSQ 321
Cdd:COG1202 259 --FLVPLVALANQKYEDFKDRYGDGL-DV--SIRVG----ASRIrddgTRFDPNADIIVGTYEGIDHALRTGRDLGDIGT 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 322 rlqlIMIDEVHILRES-RGATLEVVISRLKGLSRDIRFIALSATVPNIDDIARWLGPTRNEYgqlsrgvlvgrevinake 400
Cdd:COG1202 330 ----VVIDEVHMLEDPeRGHRLDGLIARLKYYCPGAQWIYLSATVGNPEELAKKLGAKLVEY------------------ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 401 kraltvddmpmakvykfgeEYRPVPLQR-VTYGIESvgNDWALANRLDKELYpillKHTA-----GQpVLVFCPTRKSCq 474
Cdd:COG1202 388 -------------------EERPVPLERhLTFADGR--EKIRIINKLVKREF----DTKSskgyrGQ-TIIFTNSRRRC- 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 475 atvESIfqsyeeARAKGLNlpwkhppgvrlelqdkklaelstcgIAVHHAGLDYADRRAIEDGFRDGKLHMIASTSTLAV 554
Cdd:COG1202 441 ---HEI------ARALGYK-------------------------AAPYHAGLDYGERKKVERRFADQELAAVVTTAALAA 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 555 GVNLPAHTVV-------IKGVMAwqgassgfQEYsdidiQQMVGRAGRPQYDTSGVVVVMCERSKvrKYQ-SMLNSQ--- 623
Cdd:COG1202 487 GVDFPASQVIfdslamgIEWLSV--------QEF-----HQMLGRAGRPDYHDRGKVYLLVEPGK--SYHrSMEMTEdev 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 624 --TVLESCLHENLTEYINSEIGQGTIKSVSSAQewlknsffhiriqqnpkyyalSDAKDKPVEGAWEEWLDHYVEKalin 701
Cdd:COG1202 552 afKLLKGEMEDVAVEYDEEAAVEETLANVVVGG---------------------GKAKRLNDRMLGEIPTKHALGK---- 606
|
570 580 590
....*....|....*....|....*....|
gi 321261834 702 LEKDGFIERsdddtLTPTETGKIMSSSMIS 731
Cdd:COG1202 607 LLEYGFIDG-----LEPTPLGRAVARHFLG 631
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
177-375 |
3.54e-37 |
|
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: 139.81 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 177 LSRLPMDQRKLFK-FPCFNKVQSEVFGDVYESDENLVVSAPTGSGKTTIFELAFLHNLS-FRTPNDSLKPLA---VYIAP 251
Cdd:cd18019 1 IEELPDWAQPAFEgFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGkHRNPDGTINLDAfkiVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 252 TKALCNEKAKDWQERLgqALPDVICTEITGDYGNTStiyNSIRGADLIVTTPEKFDSMTRRSRNLGNMsQRLQLIMIDEV 331
Cdd:cd18019 81 MKALVQEMVGNFSKRL--APYGITVAELTGDQQLTK---EQISETQIIVTTPEKWDIITRKSGDRTYT-QLVRLIIIDEI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 321261834 332 HILRESRGATLEVVISR----LKGLSRDIRFIALSATVPNIDDIARWL 375
Cdd:cd18019 155 HLLHDDRGPVLESIVARtirqIEQTQEYVRLVGLSATLPNYEDVATFL 202
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
194-376 |
4.87e-37 |
|
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: 138.72 E-value: 4.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 194 NKVQSEVFGDVYESDENLVVSAPTGSGKTTIFELAFLHNLS-FRTPNDSLKP---LAVYIAPTKALCNEKAKDWQERLgq 269
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRqHVNQGGVIKKddfKIVYIAPMKALAAEMVEKFSKRL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 270 ALPDVICTEITGDYGNTSTiynSIRGADLIVTTPEKFDSMTRRSRNLGNMSQRLQLIMIDEVHILRESRGATLEVVISR- 348
Cdd:cd18020 81 APLGIKVKELTGDMQLTKK---EIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARt 157
|
170 180 190
....*....|....*....|....*....|.
gi 321261834 349 LKGLSRD---IRFIALSATVPNIDDIARWLG 376
Cdd:cd18020 158 LRQVESTqsmIRIVGLSATLPNYLDVADFLR 188
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
193-376 |
6.31e-37 |
|
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: 137.47 E-value: 6.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 193 FNKVQSEVFGDVYESDENLVVSAPTGSGKTTIFELAFLHNLSfrtpnDSLKplAVYIAPTKALCNEKAKDWQ--ERLGqa 270
Cdd:cd18028 2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLL-----EGGK--ALYLVPLRALASEKYEEFKklEEIG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 271 lpdVICTEITGDYGNTStiyNSIRGADLIVTTPEKFDSMTRRSRNLGNmsqRLQLIMIDEVHILR-ESRGATLEVVISRL 349
Cdd:cd18028 73 ---LKVGISTGDYDEDD---EWLGDYDIIVATYEKFDSLLRHSPSWLR---DVGVVVVDEIHLISdEERGPTLESIVARL 143
|
170 180
....*....|....*....|....*..
gi 321261834 350 KGLSRDIRFIALSATVPNIDDIARWLG 376
Cdd:cd18028 144 RRLNPNTQIIGLSATIGNPDELAEWLN 170
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
194-371 |
5.89e-36 |
|
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: 134.29 E-value: 5.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 194 NKVQSEVFGDVYEsDENLVVSAPTGSGKTTIFELAFLHNLSFRTPndslKPLAVYIAPTKALCNEKAKDWQERlGQALPD 273
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDKLDN----GPQALVLAPTRELAEQIYEELKKL-GKGLGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 274 VICTEITGDygNTSTIYNSIRGADLIVTTPEKFDSMTRRSRNLgnmsQRLQLIMIDEVH-ILRESRGATLEVVISRLKgl 352
Cdd:pfam00270 75 KVASLLGGD--SRKEQLEKLKGPDILVGTPGRLLDLLQERKLL----KNLKLLVLDEAHrLLDMGFGPDLEEILRRLP-- 146
|
170 180
....*....|....*....|
gi 321261834 353 sRDIRFIALSATVP-NIDDI 371
Cdd:pfam00270 147 -KKRQILLLSATLPrNLEDL 165
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
718-958 |
6.25e-35 |
|
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.
Pssm-ID: 460740 Cd Length: 307 Bit Score: 136.18 E-value: 6.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 718 PTETGKIMSSSMISYGTMCSI-KAMSPRSTVQDLLEILAGSTEFKDLRIRQGESSFLNKLrtNEEIRFPLAEAVKSYADK 796
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFnQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKL--LEKVPIPVKGDIEDPHAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 797 VFLLLQVTFGNIILEDIAKKTELTSPIQtlmaiynHAPRIAKAIVQFTLNCEYGVAARSALELHRVVVGKAWEDlPTVFR 876
Cdd:pfam02889 79 VNILLQAYISRLKLPGFALVSDMNYILQ-------NAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDS-DSPLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 877 QIPSIGPKSIRVLGQNGVTNFDQLLDVESEKIQLWLNRGHDFARAIHEQARRMPRFhvtmeeeNMDYD---GTYNVLNLR 953
Cdd:pfam02889 151 QFPGIPPELIKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKI-------EIEAEvqpITRSVLRVE 223
|
....*
gi 321261834 954 VNIAP 958
Cdd:pfam02889 224 VTITP 228
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
205-568 |
1.06e-30 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 131.14 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 205 YESDENLVVSAPTGSGKT------TIFELAFLHNlsfrTPNDSLKPLavYIAPTKALcnekAKDWQERLGQALPDV---I 275
Cdd:TIGR04121 25 ALEGRSGLLIAPTGSGKTlagflpSLIDLAGPEA----PKEKGLHTL--YITPLRAL----AVDIARNLQAPIEELglpI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 276 CTEI-TGDygnTSTiynSIRGA------DLIVTTPEKFDSMTRRSRNLGNMSQrLQLIMIDEVHILRES-RGATLEVVIS 347
Cdd:TIGR04121 95 RVETrTGD---TSS---SERARqrkkppDILLTTPESLALLLSYPDAARLFKD-LRCVVVDEWHELAGSkRGDQLELALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 348 RLKGLSRDIRFIALSATVPNIDDIARWLGPTRNEygqlsrgvlvGREVINAKEKRALTVDDMpmakvykFGEEYRPVPlq 427
Cdd:TIGR04121 168 RLRRLAPGLRRWGLSATIGNLEEARRVLLGVGGA----------PAVLVRGKLPKAIEVISL-------LPESEERFP-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 428 rvtygiesvgndWA--LANRLDKELYPILLKHTAgqpVLVFCPTRKscQAtvESIFQSYEEARAKgLNLPwkhppgvrle 505
Cdd:TIGR04121 229 ------------WAghLGLRALPEVYAEIDQART---TLVFTNTRS--QA--ELWFQALWEANPE-FALP---------- 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 321261834 506 lqdkklaelstcgIAVHHAGLDYADRRAIEDGFRDGKLHMIASTSTLAVGVNLPAHTVVI-----KGV 568
Cdd:TIGR04121 279 -------------IALHHGSLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVIqigspKGV 333
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
176-594 |
8.65e-27 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 118.67 E-value: 8.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 176 PLSRLPMDQRKLF--KFPCFNKVQSEVFgDVYESDENLVVSAPTGSGKT-TIFeLAFLHNLSFRTPNDSLKP--LAVYIA 250
Cdd:COG1201 6 VLSLLHPAVRAWFaaRFGAPTPPQREAW-PAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDglRVLYIS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 251 PTKALCN--EKAKDW-----QERLGQALPDvICTEI-TGDygnTSTiynSIRGA------DLIVTTPE---------KFD 307
Cdd:COG1201 84 PLKALANdiERNLRApleeiGEAAGLPLPE-IRVGVrTGD---TPA---SERQRqrrrppHILITTPEslallltspDAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 308 SMtrrsrnLGNmsqrLQLIMIDEVHILRES-RGATLEVVISRLKGLS-RDIRFIALSATVPNIDDIARWLGPTRNEygql 385
Cdd:COG1201 157 EL------LRG----VRTVIVDEIHALAGSkRGVHLALSLERLRALApRPLQRIGLSATVGPLEEVARFLVGYEDP---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 386 sRGVlvgrEVINAKEKRALTVDDMpmakvykfgeeyrpVPLQRVTYGIESVGNDWAlanRLDKELYPILLKHTAgqpVLV 465
Cdd:COG1201 223 -RPV----TIVDAGAGKKPDLEVL--------------VPVEDLIERFPWAGHLWP---HLYPRVLDLIEAHRT---TLV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 466 FCPTRKscQAtvESIFQSYEEARAKGlnlpwkhppgvrlelqdkklAELstcgIAVHHAGLDYADRRAIEDGFRDGKLHM 545
Cdd:COG1201 278 FTNTRS--QA--ERLFQRLNELNPED--------------------ALP----IAAHHGSLSREQRLEVEEALKAGELRA 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 321261834 546 IASTSTLAVGVNLPAHTVVI-----KGVmawqgaSSGFQEysdidiqqmVGRAG 594
Cdd:COG1201 330 VVATSSLELGIDIGDVDLVIqvgspKSV------ARLLQR---------IGRAG 368
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
197-595 |
1.53e-26 |
|
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: 117.63 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 197 QSEVFgDVYESDENLVVSAPTGSGKTTIFELAFLHNLSfRTPNDSlkplAVYIAPTKALCNEKAKDWQERLGQALPDVIC 276
Cdd:COG1205 61 QAEAI-EAARAGKNVVIATPTASGKSLAYLLPVLEALL-EDPGAT----ALYLYPTKALARDQLRRLRELAEALGLGVRV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 277 TEITGDygnTST-----IYNSirgADLIVTTPEkfdsM---------TRRSRNLGNmsqrLQLIMIDEVHILRESRGATL 342
Cdd:COG1205 135 ATYDGD---TPPeerrwIREH---PDIVLTNPD----MlhygllphhTRWARFFRN----LRYVVIDEAHTYRGVFGSHV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 343 EVVISRLKGLSR----DIRFIALSATVPNIDDIArwlgptrneygqlSRgvLVGREVinakekRALTVDDMPmakvykFG 418
Cdd:COG1205 201 ANVLRRLRRICRhygsDPQFILASATIGNPAEHA-------------ER--LTGRPV------TVVDEDGSP------RG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 419 EE----YRPVPLQRVtygieSVGNDWALANRLDKELYpillkhTAGQPVLVFCPTRKScqatVESIFQSyeearakglnl 494
Cdd:COG1205 254 ERtfvlWNPPLVDDG-----IRRSALAEAARLLADLV------REGLRTLVFTRSRRG----AELLARY----------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 495 pwkhppgVRLELQDKKLAELstcgIAVHHAGLDYADRRAIEDGFRDGKLHMIASTSTLAVGVNLPAHTVVIkgVMAWQGA 574
Cdd:COG1205 308 -------ARRALREPDLADR----VAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVV--LAGYPGT 374
|
410 420
....*....|....*....|.
gi 321261834 575 SSGFqeysdidiQQMVGRAGR 595
Cdd:COG1205 375 RASF--------WQQAGRAGR 387
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
186-376 |
6.25e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.81 E-value: 6.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 186 KLFKFPCFNKVQSEVFGDVYESDENLVVSAPTGSGKTTIFELAFLHNLSfrtpnDSLKPLAVYIAPTKALcnekAKDWQE 265
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALK-----RGKGGRVLVLVPTREL----AEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 266 RLGQALPD--VICTEITGDYGNTSTIYNSIRG-ADLIVTTPEKFDSMTRRSRNLgnmSQRLQLIMIDEVH-ILRESRGAT 341
Cdd:smart00487 73 ELKKLGPSlgLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLS---LSNVDLVILDEAHrLLDGGFGDQ 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 321261834 342 LEVVISRLKglsRDIRFIALSATVP-NIDDIARWLG 376
Cdd:smart00487 150 LEKLLKLLP---KNVQLLLLSATPPeEIENLLELFL 182
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
208-375 |
1.23e-25 |
|
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: 104.59 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 208 DENLVVSAPTGSGKTtifELAFLHNLS--FRTPNDSLKplAVYIAPTKALcnekAKDWQERLgQALPDVICTEI-----T 280
Cdd:cd17922 1 GRNVLIAAPTGSGKT---EAAFLPALSslADEPEKGVQ--VLYISPLKAL----INDQERRL-EEPLDEIDLEIpvavrH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 281 GDygnTSTiynSIRGA------DLIVTTPEKFDSM---TRRSRNLGNmsqrLQLIMIDEVHILRES-RGATLEVVISRLK 350
Cdd:cd17922 71 GD---TSQ---SEKAKqlknppGILITTPESLELLlvnKKLRELFAG----LRYVVVDEIHALLGSkRGVQLELLLERLR 140
|
170 180
....*....|....*....|....*.
gi 321261834 351 GLS-RDIRFIALSATVPNIDDIARWL 375
Cdd:cd17922 141 KLTgRPLRRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
208-375 |
1.33e-25 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 105.76 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 208 DENLVVSAPTGSGKTTIFELAFLHNLSFRtpndslKPLAVYIAPTKALCNEKAkDWQERLGQALPdvicTEITGDYGNTS 287
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLLER------RKKALFVLPYVSIVQEKV-DALSPLFEELG----FRVEGYAGNKG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 288 TIYNSIRGA-DLIVTTPEKFDSMTRRSRNLGNMSqRLQLIMIDEVHILRE-SRGATLEVVISRLKGLS-RDIRFIALSAT 364
Cdd:cd18026 102 RSPPKRRKSlSVAVCTIEKANSLVNSLIEEGRLD-ELGLVVVDELHMLGDgHRGALLELLLTKLLYAAqKNIQIVGMSAT 180
|
170
....*....|.
gi 321261834 365 VPNIDDIARWL 375
Cdd:cd18026 181 LPNLEELASWL 191
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
715-961 |
1.58e-23 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 103.11 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 715 TLTPTETGKIMSSSMISYGTMCS-IKAMSPRSTVQDLLEILAGSTEFKDLRIRQGESSFLNKLRTNEEIRFPLaEAVKSY 793
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTfNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLEN-PSLDDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 794 ADKVFLLLQVTFGNIILEDiakkTELTSPIQTLMAiynHAPRIAKAIVQFTLNCEYGVAARSALELHRVVVGKAWEDlPT 873
Cdd:smart00611 80 HVKANLLLQAHLSRLKLPS----FALESDTVYVLQ---NAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPT-DS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 874 VFRQIPSIGPKSIRVLGQNGVTNFDQLLDVESEKIQLWLN----RGHDFARAIHeqarRMPRFHVTMEEENMdydgTYNV 949
Cdd:smart00611 152 PLLQLPHLPEEILKRLEKKKVLSLEDLLELEDEERGELLGlldaEGERVYKVLS----RLPKLNIEISLEPI----TRTV 223
|
250
....*....|..
gi 321261834 950 LNLRVNIAPKTK 961
Cdd:smart00611 224 LGVEVTLTVDLT 235
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
206-373 |
4.25e-22 |
|
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: 94.96 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 206 ESDENLVVSAPTGSGKTTIFELAFLHNLsFRTPNDSlkplAVYIAPTKALCNEKAKDWQERLGQALPDVICTEITGDYGN 285
Cdd:cd17923 13 RAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSR----ALYLYPTKALAQDQLRSLRELLEQLGLGIRVATYDGDTPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 286 TSTIYNSIRGADLIVTTPEKFD-SMTRRSRNLGNMSQRLQLIMIDEVHILRESRGATLEVVISRLKGLSR----DIRFIA 360
Cdd:cd17923 88 EERRAIIRNPPRILLTNPDMLHyALLPHHDRWARFLRNLRYVVLDEAHTYRGVFGSHVALLLRRLRRLCRrygaDPQFIL 167
|
170
....*....|...
gi 321261834 361 LSATVPNIDDIAR 373
Cdd:cd17923 168 TSATIGNPAEHAR 180
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
197-375 |
7.72e-18 |
|
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: 83.19 E-value: 7.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 197 QSEVFgDVYESDENLVVSAPTGSGKTTIFELAFLHNLsfRTPNDSLkplAVYIAPTKALCNEKAKDWQERLGQALPD--- 273
Cdd:cd18025 6 QRELL-DIVDRRESALIVAPTSSGKTFISYYCMEKVL--RESDDGV---VVYVAPTKALVNQVVAEVYARFSKKYPPsgk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 274 VICTEITGDYGntstiYNSIRGADLIVTTPEKFDSMTrRSRNLGNMSQRLQLIMIDEVHILRESRGAtleVVISRLKGLS 353
Cdd:cd18025 80 SLWGVFTRDYR-----HNNPMNCQVLITVPECLEILL-LSPHNASWVPRIKYVIFDEIHSIGQSEDG---AVWEQLLLLI 150
|
170 180
....*....|....*....|..
gi 321261834 354 RdIRFIALSATVPNIDDIARWL 375
Cdd:cd18025 151 P-CPFLALSATIGNPQKFHEWL 171
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
210-606 |
3.23e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 87.00 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 210 NLVVSAPTGSGKTTIFeLAFLHNLSFRTPndslkplAVYIAPTKALCnekaKDWQERLGQALPDVICTEITGDygntsti 289
Cdd:COG1061 102 RGLVVAPTGTGKTVLA-LALAAELLRGKR-------VLVLVPRRELL----EQWAEELRRFLGDPLAGGGKKD------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 290 ynsiRGADLIVTTpekFDSMTRRSRnLGNMSQRLQLIMIDEVHilrESRGATLEVVISRLKglsrDIRFIALSATvPNID 369
Cdd:COG1061 163 ----SDAPITVAT---YQSLARRAH-LDELGDRFGLVIIDEAH---HAGAPSYRRILEAFP----AAYRLGLTAT-PFRS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 370 DiarwlgpTRNEYGQLSRGVLVGREVINAKEKRALtvddmpmAKVYKFGeeyRPVPLQ--RVTYGIESVGNDWALAN--- 444
Cdd:COG1061 227 D-------GREILLFLFDGIVYEYSLKEAIEDGYL-------APPEYYG---IRVDLTdeRAEYDALSERLREALAAdae 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 445 RLDKELYPILLKHTAGQPVLVFCPTRKSCQAtvesIFQSYEEArakglnlpwkhppGVRlelqdkklaelstcgIAVHHA 524
Cdd:COG1061 290 RKDKILRELLREHPDDRKTLVFCSSVDHAEA----LAELLNEA-------------GIR---------------AAVVTG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 525 GLDYADRRAIEDGFRDGKLHMIASTSTLAVGVNLPAHTVVIkgvMAwqgASSGfqeySDIDIQQMVGRAGRPQYDTSGVV 604
Cdd:COG1061 338 DTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI---LL---RPTG----SPREFIQRLGRGLRPAPGKEDAL 407
|
..
gi 321261834 605 VV 606
Cdd:COG1061 408 VY 409
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
209-364 |
4.92e-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: 73.59 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 209 ENLVVSAPTGSGKTTIFELAFLHNLSFRTPNdslkplAVYIAPTKALcnekAKDWQERLGQALPDVICTEITGDYGNTST 288
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKKGKK------VLVLVPTKAL----ALQTAERLRELFGPGIRVAVLVGGSSAEE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321261834 289 IYNSIRG-ADLIVTTPEKFDSMTRRSRNLGnmSQRLQLIMIDEVHILRESRGATLEVVISRLKGLSRDIRFIALSAT 364
Cdd:cd00046 72 REKNKLGdADIIIATPDMLLNLLLREDRLF--LKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
206-375 |
4.44e-14 |
|
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: 72.86 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 206 ESDENLVVSAPTGSGKTTIFELAFLhnLSFRTpndslKPLAVYIAPTKALCNEKAKDWQERLGqalpDVicTEITGDYgn 285
Cdd:cd18024 45 ERNESVLVSAHTSAGKTVVAEYAIA--QSLRD-----KQRVIYTSPIKALSNQKYRELQEEFG----DV--GLMTGDV-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 286 tsTIYNSirgADLIVTTPEKFDSMTRRSRNLgnMSQRLQLIMiDEVHILRES-RGATLEVVISRLkglSRDIRFIALSAT 364
Cdd:cd18024 110 --TINPN---ASCLVMTTEILRSMLYRGSEI--MREVAWVIF-DEIHYMRDKeRGVVWEETIILL---PDKVRYVFLSAT 178
|
170
....*....|.
gi 321261834 365 VPNIDDIARWL 375
Cdd:cd18024 179 IPNARQFAEWI 189
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
518-596 |
4.05e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 66.08 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 518 GIAVHHAGLDYADRRAIEDGFRDGKLHMIASTSTLAVGVNLP-AHTVVIKgvmawqGASSGFQEYsdidiQQMVGRAGRP 596
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIY------DLPWSPASY-----IQRIGRAGRA 81
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
213-594 |
5.53e-13 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 74.19 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 213 VSAPTGSGKTTIfelAFLHNLS--FR-------TPNDSLKPLAVYIAPTKALCNEKAKDWQ----------ERLGQALPD 273
Cdd:PRK09751 1 VIAPTGSGKTLA---AFLYALDrlFReggedtrEAHKRKTSRILYISPIKALGTDVQRNLQiplkgiaderRRRGETEVN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 274 VICTEITGDYGNTSTIYNSIRGADLIVTTPEKFDSM-TRRSRNlgnMSQRLQLIMIDEVHILRES-RGATLEVVISRLKG 351
Cdd:PRK09751 78 LRVGIRTGDTPAQERSKLTRNPPDILITTPESLYLMlTSRARE---TLRGVETVIIDEVHAVAGSkRGAHLALSLERLDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 352 L--SRDIRfIALSATVPNIDDIARWLGPTRNEygqlsrgvlvgrEVINAKEKRALTV---------DDMPmAKVYKFGEE 420
Cdd:PRK09751 155 LlhTSAQR-IGLSATVRSASDVAAFLGGDRPV------------TVVNPPAMRHPQIrivvpvanmDDVS-SVASGTGED 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 421 YRPVPLQRVTYGIEsvgndwalANRLDKelypiLLKHTAgqpVLVFCPTRKSCQATVESIFQSYEE--ARAKGLNLPWKH 498
Cdd:PRK09751 221 SHAGREGSIWPYIE--------TGILDE-----VLRHRS---TIVFTNSRGLAEKLTARLNELYAArlQRSPSIAVDAAH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 499 PPGVRLELQdKKLAELSTCGIAVHHAGLDYADRRAIEDGFRDGKLHMIASTSTLAVGVNLPAHTVVIKgVMAWQGASSGF 578
Cdd:PRK09751 285 FESTSGATS-NRVQSSDVFIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQ-VATPLSVASGL 362
|
410
....*....|....*.
gi 321261834 579 QEysdidiqqmVGRAG 594
Cdd:PRK09751 363 QR---------IGRAG 369
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
206-379 |
2.81e-12 |
|
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: 66.90 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 206 ESDENLVVSAPTGSGKTTIFELAFLHNLSFRTPndslkplAVYIAPTKALCNEKAKDWQERLGqalpDVicTEITGDYgn 285
Cdd:cd18027 21 EAGDSVFVAAHTSAGKTVVAEYAIALAQKHMTR-------TIYTSPIKALSNQKFRDFKNTFG----DV--GLITGDV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 286 tsTIYNsirGADLIVTTPEKFDSMTRRSRNLgnmSQRLQLIMIDEVHILRES-RGATLEVVISRLkglSRDIRFIALSAT 364
Cdd:cd18027 86 --QLNP---EASCLIMTTEILRSMLYNGSDV---IRDLEWVIFDEVHYINDAeRGVVWEEVLIML---PDHVSIILLSAT 154
|
170
....*....|....*
gi 321261834 365 VPNIDDIARWLGPTR 379
Cdd:cd18027 155 VPNTVEFADWIGRIK 169
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
209-606 |
6.28e-11 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 67.22 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 209 ENLVVSAPTGSGKT-TIFeLAFLHNLSFRTPNDSL--KPLAVYIAPTKALCNekakDWQERLGQALPDVicTEITGDYGN 285
Cdd:PRK13767 48 KNVLISSPTGSGKTlAAF-LAIIDELFRLGREGELedKVYCLYVSPLRALNN----DIHRNLEEPLTEI--REIAKERGE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 286 TST-IYNSIRGAD----------------LIvTTPE---------KFdsmtrrsrnlgnmSQRL---QLIMIDEVHILRE 336
Cdd:PRK13767 121 ELPeIRVAIRTGDtssyekqkmlkkpphiLI-TTPEslaillnspKF-------------REKLrtvKWVIVDEIHSLAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 337 S-RGATLEVVISRLKGL-SRDIRFIALSATVPNIDDIARWLGPtrNEYGQLSRGVlvgrEVINAKEKRALT------VDD 408
Cdd:PRK13767 187 NkRGVHLSLSLERLEELaGGEFVRIGLSATIEPLEEVAKFLVG--YEDDGEPRDC----EIVDARFVKPFDikvispVDD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 409 MpmakVYKFGEEyrpvplqrvtygiesvgndwaLANRLDKELYPILLKHTAgqpVLVFCPTRKSCQATVESIFQSYEEar 488
Cdd:PRK13767 261 L----IHTPAEE---------------------ISEALYETLHELIKEHRT---TLIFTNTRSGAERVLYNLRKRFPE-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 489 akglnlpwkhppgvrlelqdkklaELSTCGIAVHHAGLDYADRRAIEDGFRDGKLHMIASTSTLAVGVNLPAHTVVI--- 565
Cdd:PRK13767 311 ------------------------EYDEDNIGAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVllg 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 321261834 566 --KGVMAwqgassgfqeysdidIQQMVGRAGRPQYDTS-GVVVV 606
Cdd:PRK13767 367 spKSVSR---------------LLQRIGRAGHRLGEVSkGRIIV 395
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
454-595 |
1.01e-10 |
|
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: 60.30 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 454 LLKHTAGQPVLVFCPTRKSCQAtvesifqsyeearakglnlpwkhppgvrlelqdKKLAELSTCGIAVHHAGLDYADRRA 533
Cdd:pfam00271 9 LLKKERGGKVLIFSQTKKTLEA---------------------------------ELLLEKEGIKVARLHGDLSQEEREE 55
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321261834 534 IEDGFRDGKLHMIASTSTLAVGVNLP-AHTVVIKGVmawqgassgfqEYSDIDIQQMVGRAGR 595
Cdd:pfam00271 56 ILEDFRKGKIDVLVATDVAERGLDLPdVDLVINYDL-----------PWNPASYIQRIGRAGR 107
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
184-375 |
1.19e-10 |
|
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: 62.46 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 184 QRKLFKFPcfNKVQSEVFGDVYeSDENLVVSAPTGSGKTtifeLAF----LHNLSFRTPNDSLKPLAVYIAPTKALCNEK 259
Cdd:cd00268 6 KKLGFEKP--TPIQAQAIPLIL-SGRDVIGQAQTGSGKT----LAFllpiLEKLLPEPKKKGRGPQALVLAPTRELAMQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 260 AKDWqERLGQALPDVICTeITGDYGNTSTIYNSIRGADLIVTTPEK-FDSMTRRSRNLGNmsqrLQLIMIDEV-HILRES 337
Cdd:cd00268 79 AEVA-RKLGKGTGLKVAA-IYGGAPIKKQIEALKKGPDIVVGTPGRlLDLIERGKLDLSN----VKYLVLDEAdRMLDMG 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 321261834 338 RGATLEVVISRlkgLSRDIRFIALSATVPN-IDDIARWL 375
Cdd:cd00268 153 FEEDVEKILSA---LPKDRQTLLFSATLPEeVKELAKKF 188
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
194-595 |
1.55e-10 |
|
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: 65.49 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 194 NKVQSEVFGDVYESDEN----LVVSAPTGSGKtTIFELAFLHNLSFRTPNDSLkplaVYIAPTKALCNEKAkdwqERLGQ 269
Cdd:COG1203 129 NPLQNEALELALEAAEEepglFILTAPTGGGK-TEAALLFALRLAAKHGGRRI----IYALPFTSIINQTY----DRLRD 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 270 ALPDvictEITGDYGNTSTIYNSIRG-----------------ADLIVTTPEK-----FDSMTRRSRNLGNMSQRlqLIM 327
Cdd:COG1203 200 LFGE----DVLLHHSLADLDLLEEEEeyesearwlkllkelwdAPVVVTTIDQlfeslFSNRKGQERRLHNLANS--VII 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 328 IDEVHILRESRGATLEVVISRLKGLsrDIRFIALSATVPNIDdiarwlgptrneygqlsrgvlvgreVINAKEKRALtVD 407
Cdd:COG1203 274 LDEVQAYPPYMLALLLRLLEWLKNL--GGSVILMTATLPPLL-------------------------REELLEAYEL-IP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 408 DMPmakvYKFGEEYRPVPLQRVTYGIESVGNDwALANRLDKELypillkhTAGQPVLVFCPTRKSCQATvesifqsYEEA 487
Cdd:COG1203 326 DEP----EELPEYFRAFVRKRVELKEGPLSDE-ELAELILEAL-------HKGKSVLVIVNTVKDAQEL-------YEAL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 488 RAKGLNLPWKHppgvrlelqdkklaelstcgiavHHAGLDYADRRAIE----DGFRDGKLHMIASTSTLAVGVNLPAHTV 563
Cdd:COG1203 387 KEKLPDEEVYL-----------------------LHSRFCPADRSEIEkeikERLERGKPCILVSTQVVEAGVDIDFDVV 443
|
410 420 430
....*....|....*....|....*....|....
gi 321261834 564 VIkgvmawqgassgfqEYSDID--IQqmvgRAGR 595
Cdd:COG1203 444 IR--------------DLAPLDslIQ----RAGR 459
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
205-364 |
3.68e-10 |
|
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: 59.63 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 205 YESDENLVVSAPTGSGKTTIFELAFLHNLSFRTpndslkplaVYIAPTKALcnekAKDWQERLGQALPDVIcteitgDYG 284
Cdd:cd17926 15 HKNNRRGILVLPTGSGKTLTALALIAYLKELRT---------LIVVPTDAL----LDQWKERFEDFLGDSS------IGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 285 NTSTIYNSIRGADLIVTTPekfDSMTRRSRNLGNMSQRLQLIMIDEVHILresrGA-TLEVVISRLKGlsrdIRFIALSA 363
Cdd:cd17926 76 IGGGKKKDFDDANVVVATY---QSLSNLAEEEKDLFDQFGLLIVDEAHHL----PAkTFSEILKELNA----KYRLGLTA 144
|
.
gi 321261834 364 T 364
Cdd:cd17926 145 T 145
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
185-376 |
5.84e-10 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 60.63 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 185 RKLFKFPCFNKVQSEVFGDVyESDENLVVSAPTGSGKTTIFELAFLHnlsfrtpndsLKPLAVYIAPTKALcnekAKDWQ 264
Cdd:cd17920 5 KEVFGYDEFRPGQLEAINAV-LAGRDVLVVMPTGGGKSLCYQLPALL----------LDGVTLVVSPLISL----MQDQV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 265 ERLGQAlpDVICTEITG--DYGNTSTIYNSIR--GADLIVTTPEKF--DSMTRRSRNLgNMSQRLQLIMIDEVHILRES- 337
Cdd:cd17920 70 DRLQQL--GIRAAALNStlSPEEKREVLLRIKngQYKLLYVTPERLlsPDFLELLQRL-PERKRLALIVVDEAHCVSQWg 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 321261834 338 ---RGATLEvvISRLKGLSRDIRFIALSATVPNI--DDIARWLG 376
Cdd:cd17920 147 hdfRPDYLR--LGRLRRALPGVPILALTATATPEvrEDILKRLG 188
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
464-606 |
1.78e-09 |
|
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: 57.65 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 464 LVFCPTRKSCqatvESIFQsyeEARAkglnlpwkhppgvRLElqdkKLAELSTCgIAVHHAGLDYADRRAIEDGFRDGKL 543
Cdd:cd18797 39 IVFCRSRKLA----ELLLR---YLKA-------------RLV----EEGPLASK-VASYRAGYLAEDRREIEAELFNGEL 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321261834 544 HMIASTSTLAVGVNLPAHTVVIkgvmawqgaSSGFqEYSDIDIQQMVGRAGRPQYDTSGVVVV 606
Cdd:cd18797 94 LGVVATNALELGIDIGGLDAVV---------LAGY-PGSLASLWQQAGRAGRRGKDSLVILVA 146
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
188-373 |
1.37e-08 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 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: 350722 [Multi-domain] Cd Length: 211 Bit Score: 56.82 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 188 FKFPCFNKVQSEVFGDVYESDENLVVSAPTGSGKTtifeLAFL-----HNLSFRTPNDSLKPLAVYIAPTKALCNEKAKD 262
Cdd:cd17964 12 MGFETMTPVQQKTLKPILSTGDDVLARAKTGTGKT----LAFLlpaiqSLLNTKPAGRRSGVSALIISPTRELALQIAAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 263 WQeRLGQALPDVIC-TEITGDYGNTSTIYNSIRGADLIVTTPEKFDSMTRRSRnLGNMSQRLQLIMIDEVHILRESrG-- 339
Cdd:cd17964 88 AK-KLLQGLRKLRVqSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLENPG-VAKAFTDLDYLVLDEADRLLDM-Gfr 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 321261834 340 ATLEVVISRLKGLSRDIRFIAL-SATVP-NIDDIAR 373
Cdd:cd17964 165 PDLEQILRHLPEKNADPRQTLLfSATVPdEVQQIAR 200
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
207-337 |
1.48e-08 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 59.03 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 207 SDENLVVSAPTGSGKTTIFELAFL-HNLSFRT--PNDSLKPLAVYIAPTKALC---NEKAKdwqeRLGQALPDVICTEIT 280
Cdd:PLN00206 157 SGRSLLVSADTGSGKTASFLVPIIsRCCTIRSghPSEQRNPLAMVLTPTRELCvqvEDQAK----VLGKGLPFKTALVVG 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 321261834 281 GDyGNTSTIYNSIRGADLIVTTPEKF-DSMTRRSRNLGNMSqrlqLIMIDEVHILRES 337
Cdd:PLN00206 233 GD-AMPQQLYRIQQGVELIVGTPGRLiDLLSKHDIELDNVS----VLVLDEVDCMLER 285
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
209-373 |
3.73e-08 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 55.29 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 209 ENLVVSAPTGSGKTTIFELAFLHNLsfRTPNDSLKPLAVYIAPTKALCNEKAKDWQeRLGQALPdVICTEIT-GDYGNTS 287
Cdd:cd17957 28 RDLLACAPTGSGKTLAFLIPILQKL--GKPRKKKGLRALILAPTRELASQIYRELL-KLSKGTG-LRIVLLSkSLEAKAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 288 TIYNSIRGADLIVTTPEKFDSMTRrsRNLGNMSQRLQLIMiDEVHILRES--RGATLEVvisrLKGL-SRDIRFIALSAT 364
Cdd:cd17957 104 DGPKSITKYDILVSTPLRLVFLLK--QGPIDLSSVEYLVL-DEADKLFEPgfREQTDEI----LAACtNPNLQRSLFSAT 176
|
170
....*....|
gi 321261834 365 VP-NIDDIAR 373
Cdd:cd17957 177 IPsEVEELAR 186
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
208-370 |
4.26e-08 |
|
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: 54.60 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 208 DENLVVSAPTGSGKtTIFELAFLHNLSFRTPNDSLkplaVYIAPTKALCNEKAKDWQERLGQALPDVICTEITGDYG--- 284
Cdd:cd17930 1 PGLVILEAPTGSGK-TEAALLWALKLAARGGKRRI----IYALPTRATINQMYERIREILGRLDDEDKVLLLHSKAAlel 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 285 -------------NTSTIYNSIRG--ADLIVTTPEK-FDSM---TRRSRNLGNMSQRlqLIMIDEVHILRESRGATLevv 345
Cdd:cd17930 76 lesdeepdddpveAVDWALLLKRSwlAPIVVTTIDQlLESLlkyKHFERRLHGLANS--VVVLDEVQAYDPEYMALL--- 150
|
170 180
....*....|....*....|....*..
gi 321261834 346 ISRLKGLSR--DIRFIALSATVPNIDD 370
Cdd:cd17930 151 LKALLELLGelGGPVVLMTATLPALLR 177
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
210-366 |
4.54e-08 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 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: 350720 [Multi-domain] Cd Length: 193 Bit Score: 54.86 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 210 NLVVSAPTGSGKTTifelAFLHNLSFRTPNDSLKPLAVYIAPTKALCNEKAKDWQErLGQALPDVICTEITGDYGNTSTI 289
Cdd:cd17962 29 DILASADTGSGKTA----AFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE-LMKGLPPMKTALLVGGLPLPPQL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 321261834 290 YNSIRGADLIVTTPEK-FDSMTRRSRNLGNmsqrLQLIMIDEVHILREsRGATlEVVISRLKGLSRDIRFIALSATVP 366
Cdd:cd17962 104 YRLQQGVKVIIATPGRlLDILKQSSVELDN----IKIVVVDEADTMLK-MGFQ-QQVLDILENISHDHQTILVSATIP 175
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
208-332 |
8.80e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 50.36 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 208 DENLVVSAPTGSGKT-TIFELAFLHNLSFRTPNdslkplAVYIAPTKALCnekaKDWQERLGQALPD--VICTEITGDyg 284
Cdd:pfam04851 23 QKRGLIVMATGSGKTlTAAKLIARLFKKGPIKK------VLFLVPRKDLL----EQALEEFKKFLPNyvEIGEIISGD-- 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 321261834 285 NTSTIYNSIRgadLIVTTPEKF--DSMTRRSRNLGNmsqRLQLIMIDEVH 332
Cdd:pfam04851 91 KKDESVDDNK---IVVTTIQSLykALELASLELLPD---FFDVIIIDEAH 134
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
453-607 |
3.38e-06 |
|
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: 48.41 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 453 ILLKHTAGQPVLVFCPTRKscqaTVESIFQSYEEARAKglnLPWKHPpgvrlelqdkklaelstcgIAVHHAGLDYADRR 532
Cdd:cd18796 31 VIFLLERHKSTLVFTNTRS----QAERLAQRLRELCPD---RVPPDF-------------------IALHHGSLSRELRE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 321261834 533 AIEDGFRDGKLHMIASTSTLAVGVNLPAHTVVIKgVMAWQGASSGFQEysdidiqqmVGRAG-RPQYDTSGVVVVM 607
Cdd:cd18796 85 EVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQ-IGSPKSVARLLQR---------LGRSGhRPGAASKGRLVPT 150
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
215-330 |
6.28e-06 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 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: 350711 [Multi-domain] Cd Length: 222 Bit Score: 48.91 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 215 APTGSGKTTIFELA-FLHNLSFRTPNDSLKPLAVYIAPTKALCNEKAKDWQeRLGQALpDVICTEITGDYGNTSTIYNSI 293
Cdd:cd17953 56 AKTGSGKTLAFLLPmFRHIKDQRPVKPGEGPIGLIMAPTRELALQIYVECK-KFSKAL-GLRVVCVYGGSGISEQIAELK 133
|
90 100 110
....*....|....*....|....*....|....*...
gi 321261834 294 RGADLIVTTPEKF-DSMTRRSRNLGNMsQRLQLIMIDE 330
Cdd:cd17953 134 RGAEIVVCTPGRMiDILTANNGRVTNL-RRVTYVVLDE 170
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
209-381 |
6.93e-06 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members 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: 350721 [Multi-domain] Cd Length: 196 Bit Score: 48.34 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 209 ENLVVSAPTGSGKTTIFELAFLHNLsfrtpNDSLK-PLAVYIAPTKALCNEKAkDWQERLGQaLPDVICT----EITGDY 283
Cdd:cd17963 34 ENLIAQSQSGTGKTAAFVLAMLSRV-----DPTLKsPQALCLAPTRELARQIG-EVVEKMGK-FTGVKVAlavpGNDVPR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 284 GNTSTiynsirgADLIVTTPEK-FDSMTRRSRNLgnmsQRLQLIMIDEVHILRESRGATlEVVISRLKGLSRDIRFIALS 362
Cdd:cd17963 107 GKKIT-------AQIVIGTPGTvLDWLKKRQLDL----KKIKILVLDEADVMLDTQGHG-DQSIRIKRMLPRNCQILLFS 174
|
170 180
....*....|....*....|
gi 321261834 363 ATVP-NIDDIARWLGPTRNE 381
Cdd:cd17963 175 ATFPdSVRKFAEKIAPNANT 194
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
193-364 |
4.00e-05 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 45.78 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 193 FNKVQSEVFgdvyesdENLVVSAPTGSGKTTIFELAfLHNLSFRTPNDSLkplaVYIAPTKALCNEKAKDWQERLGqaLP 272
Cdd:cd18033 8 FTIVQKALF-------QNTLVALPTGLGKTFIAAVV-MLNYYRWFPKGKI----VFMAPTKPLVSQQIEACYKITG--IP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 273 DVICTEITgdyGNTST-----IYNSIRgadLIVTTPEKFDSMTRRSRNLgnmSQRLQLIMIDEVHilRESRGATLEVVIS 347
Cdd:cd18033 74 SSQTAELT---GSVPPtkraeLWASKR---VFFLTPQTLENDLKEGDCD---PKSIVCLVIDEAH--RATGNYAYCQVVR 142
|
170
....*....|....*..
gi 321261834 348 RLKGLSRDIRFIALSAT 364
Cdd:cd18033 143 ELMRYNSHFRILALTAT 159
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
210-373 |
4.00e-05 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 47.83 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 210 NLVVSAPTGSGKTTIFELAFLHNLSFRTPNdslKPLAVYIAPTKALCNEKAKDWQeRLGQALpDVICTEItgdYGNTSti 289
Cdd:COG0513 41 DVLGQAQTGTGKTAAFLLPLLQRLDPSRPR---APQALILAPTRELALQVAEELR-KLAKYL-GLRVATV---YGGVS-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 290 YNS-----IRGADLIVTTPEK-FDSMTRRSRNLGNmsqrLQLIMIDEV-HILREsrgatlevvisrlkGLSRDIRFIA-- 360
Cdd:COG0513 111 IGRqiralKRGVDIVVATPGRlLDLIERGALDLSG----VETLVLDEAdRMLDM--------------GFIEDIERILkl 172
|
170 180
....*....|....*....|...
gi 321261834 361 ---------LSATVPN-IDDIAR 373
Cdd:COG0513 173 lpkerqtllFSATMPPeIRKLAK 195
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
188-331 |
7.39e-05 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members 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. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 45.61 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 188 FKFPcfnkVQSEVFGDVYeSDENLVVSAPTGSGKTTIFELAFLHNL--SFRTPNDSLKPLAVYIAPTKALCNEKAKDWQE 265
Cdd:cd17944 12 YLFP----IQVKTFHPVY-SGKDLIAQARTGTGKTFSFAIPLIEKLqeDQQPRKRGRAPKVLVLAPTRELANQVTKDFKD 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 321261834 266 rLGQALpDVICTeitgdYGNTStiYNS----IR-GADLIVTTPEKFDSMTRRSRNlgNMSQrLQLIMIDEV 331
Cdd:cd17944 87 -ITRKL-SVACF-----YGGTP--YQQqifaIRnGIDILVGTPGRIKDHLQNGRL--DLTK-LKHVVLDEV 145
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
210-331 |
1.86e-04 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 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: 350719 [Multi-domain] Cd Length: 206 Bit Score: 44.50 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 210 NLVVSAPTGSGKTTIFELAFLHNLSFRTPNDSLK--PLAVYIAPTKALCNEKAKDWQERLGQALPDVICTEITGDYGNTS 287
Cdd:cd17961 33 DILARARTGSGKTAAYALPIIQKILKAKAESGEEqgTRALILVPTRELAQQVSKVLEQLTAYCRKDVRVVNLSASSSDSV 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 321261834 288 TIYNSIRGADLIVTTPEKFDSMTRRSrNLGNMSQrLQLIMIDEV 331
Cdd:cd17961 113 QRALLAEKPDIVVSTPARLLSHLESG-SLLLLST-LKYLVIDEA 154
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
218-377 |
2.98e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350677 [Multi-domain] Cd Length: 182 Bit Score: 43.32 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 218 GSGKTtIFELAFLHNLSFRtpNDSLKPLAVyIAPTKALCNekakdWQERLGQALPDVICTEITGDYGNTSTIYNSIRG-- 295
Cdd:cd17919 29 GLGKT-LQAIAFLAYLLKE--GKERGPVLV-VCPLSVLEN-----WEREFEKWTPDLRVVVYHGSQRERAQIRAKEKLdk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 296 ADLIVTTPEKFDSMTRRSRnlgnmSQRLQLIMIDEVHILRESRGATLEVvisrLKGLSRDIRfIALSATvP---NIDD-- 370
Cdd:cd17919 100 FDVVLTTYETLRRDKASLR-----KFRWDLVVVDEAHRLKNPKSQLSKA----LKALRAKRR-LLLTGT-PlqnNLEElw 168
|
....*...
gi 321261834 371 -IARWLGP 377
Cdd:cd17919 169 aLLDFLDP 176
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
197-332 |
4.45e-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: 43.02 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 197 QSEVFgdvYES-DENLVVSAPTGSGKTTIFEL---AFLHNLSFRTPNdslKPLAVYIAPTKALCNEKAKDWQERLGqalP 272
Cdd:cd18034 7 QLELF---EAAlKRNTIVVLPTGSGKTLIAVMlikEMGELNRKEKNP---KKRAVFLVPTVPLVAQQAEAIRSHTD---L 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321261834 273 DVI--CTEITGDYGNTSTIYNSIRGADLIVTTPEKF-DSMTRRSRNLGNMSqrlqLIMIDEVH 332
Cdd:cd18034 78 KVGeySGEMGVDKWTKERWKEELEKYDVLVMTAQILlDALRHGFLSLSDIN----LLIFDECH 136
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
210-330 |
5.46e-04 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 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: 350718 [Multi-domain] Cd Length: 202 Bit Score: 42.95 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 210 NLVVSAPTGSGKTTIFELAFLHNLSFRTPNDSLK-PLAVYIAPTKALCNEKAKDWQERLGQALPDVICTEITGDYGNTST 288
Cdd:cd17960 29 DVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGqVGALIISPTRELATQIYEVLQSFLEHHLPKLKCQLLIGGTNVEED 108
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 321261834 289 IYNSIR-GADLIVTTPEKFDSMTRRSRNLGNMSqRLQLIMIDE 330
Cdd:cd17960 109 VKKFKRnGPNILVGTPGRLEELLSRKADKVKVK-SLEVLVLDE 150
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
195-366 |
1.43e-03 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 41.97 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 195 KVQSEVFGDVYESdENLVVSAPTGSGKTTIFELAFLHNLSFRTPNDSLK---PLAVYIAPTKALCNEKAKDwQERLGQAL 271
Cdd:cd17948 15 TVQKQGIPSILRG-RNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfnaPRGLVITPSRELAEQIGSV-AQSLTEGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 272 PDVICTeITGdyGNT-STIYNSIRG-ADLIVTTPEKFDSMTRrsRNLGNMSQRLQLImIDEVH-ILRESRGATLEVVISR 348
Cdd:cd17948 93 GLKVKV-ITG--GRTkRQIRNPHFEeVDILVATPGALSKLLT--SRIYSLEQLRHLV-LDEADtLLDDSFNEKLSHFLRR 166
|
170 180
....*....|....*....|....*...
gi 321261834 349 L----------KGLSRDIRFIALSATVP 366
Cdd:cd17948 167 FplasrrsentDGLDPGTQLVLVSATMP 194
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
215-331 |
1.71e-03 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are 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: 350810 [Multi-domain] Cd Length: 264 Bit Score: 41.88 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 215 APTGSGKTTIFELAFLHNL-SFRTPNDSLK----PLAVYIAPTKALCNEKAKDWQE-RLGQALPDVICteitgdYGNTST 288
Cdd:cd18052 87 AQTGSGKTAAFLLPVLTGMmKEGLTASSFSevqePQALIVAPTRELANQIFLEARKfSYGTCIRPVVV------YGGVSV 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 321261834 289 IYNS---IRGADLIVTTPEKF-DSMTRRSRNLGNmsqrLQLIMIDEV 331
Cdd:cd18052 161 GHQIrqiEKGCHILVATPGRLlDFIGRGKISLSK----LKYLILDEA 203
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
208-369 |
7.08e-03 |
|
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: 39.34 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 208 DENLVVSAPTGSGKTTIFELAFLHNLsfRTPNDSLKPLAVYIAPTKALCNEKAKDWQERLGqaLPDVICTEITGDYGNTS 287
Cdd:cd17927 17 GKNTIICLPTGSGKTFVAVLICEHHL--KKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFE--RPGYKVTGLSGDTSENV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 288 TIYNSIRGADLIVTTPEKFDSMTRRSRN--LGNMSqrlqLIMIDEVHilRESRGATLEVVI-----SRLKGLSRDIRFIA 360
Cdd:cd17927 93 SVEQIVESSDVIIVTPQILVNDLKSGTIvsLSDFS----LLVFDECH--NTTKNHPYNEIMfryldQKLGSSGPLPQILG 166
|
....*....
gi 321261834 361 LSATVPNID 369
Cdd:cd17927 167 LTASPGVGG 175
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
185-377 |
8.15e-03 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 39.16 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 185 RKLFKFPCFNKVQSEVFGDVYeSDENLVVSAPTGSGKTTIFEL-AFLhnLSFRTPNdslkpLAVYIAPTKALcnekAKDw 263
Cdd:cd18018 5 RRVFGHPSFRPGQEEAIARLL-SGRSTLVVLPTGAGKSLCYQLpALL--LRRRGPG-----LTLVVSPLIAL----MKD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 264 QErlgQALPDVICTEITgDYGNTST----IYNSIRGA--DLIVTTPEKFDSmtRRSRNLGNMSQRLQLIMIDEVHILRE- 336
Cdd:cd18018 72 QV---DALPRAIKAAAL-NSSLTREerrrILEKLRAGevKILYVSPERLVN--ESFRELLRQTPPISLLVVDEAHCISEw 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 321261834 337 ---SRGATLEVViSRLKGLSRDIRFIALSATVPN--IDDIARWLGP 377
Cdd:cd18018 146 shnFRPDYLRLC-RVLRELLGAPPVLALTATATKrvVEDIASHLGI 190
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
215-312 |
9.73e-03 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 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: 350703 [Multi-domain] Cd Length: 220 Bit Score: 39.23 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321261834 215 APTGSGKTTIFELAFLHNLSFRTPNDSLK----PLAVYIAPTKALCNEKAKDWQeRLGQALpDVICTEITGDYgNTSTIY 290
Cdd:cd17945 34 AETGSGKTAAFLIPLLVYISRLPPLDEETkddgPYALILAPTRELAQQIEEETQ-KFAKPL-GIRVVSIVGGH-SIEEQA 110
|
90 100
....*....|....*....|....
gi 321261834 291 NSIR-GADLIVTTPEKF-DSMTRR 312
Cdd:cd17945 111 FSLRnGCEILIATPGRLlDCLERR 134
|
|
| |
