|
Name |
Accession |
Description |
Interval |
E-value |
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
7-534 |
1.87e-78 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 262.14 E-value: 1.87e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 7 YPWQLECLSRVARTSRSLVYTAPTGAGKSRVADALLEETLASdgGGRALVVLPYVALVRERAMALAKTLRARGIGVRAYA 86
Cdd:COG1204 24 YPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEELGIKVGVST 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 87 GG-ESEGWALGgDARCAVTTIEKAANAVSRaleRGSF-DELRIVVVDELHMVSEDERGGVLEGMLARIRHatrsgraRRG 164
Cdd:COG1204 102 GDyDSDDEWLG-RYDILVATPEKLDSLLRN---GPSWlRDVDLVVVDEAHLIDDESRGPTLEVLLARLRR-------LNP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 165 GPRIVCMSATV-NArslERLAKWLDAETYVGTYRPVELREhvvredGVFVKtgeGLTRVRDAPRAGgseRERELGVVAEL 243
Cdd:COG1204 171 EAQIVALSATIgNA---EEIAEWLDAELVKSDWRPVPLNE------GVLYD---GVLRFDDGSRRS---KDPTLALALDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 244 VGEvfvhGHSTLVFCASKAQCSNVAKRLAGIFHRHPAAMSLRE-RFVERLFDACEGA--PDVDLVQAILSGIAWHHAGLT 320
Cdd:COG1204 236 LEE----GGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREElEELAEELLEVSEEthTNEKLADCLEKGVAFHHAGLP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 321 TAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRtIIIPGYIAGTRTP-SMAQYKQMAGRAGRKGQSDVGESFLIVMKK 399
Cdd:COG1204 312 SELRRLVEDAFREGLIKVLVATPTLAAGVNLPARR-VIIRDTKRGGMVPiPVLEFKQMAGRAGRPGYDPYGEAILVAKSS 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 400 DAV-AWAQNLVCGDLPPLESRLfppsRGRDAPPTaeqkkFYLESIACGILKTKEDAGELACRTFAWTSEDDYSsilLRQE 478
Cdd:COG1204 391 DEAdELFERYILGEPEPIRSKL----ANESALRT-----HLLALIASGFANSREELLDFLENTFYAYQYDKGD---LEEV 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1275576587 479 V--SLKQIHDEGvvMVRRTGENSTewcSTPEGFAFYRCSLPIAHAKKLRSELDDALRN 534
Cdd:COG1204 459 VddALEFLLENG--FIEEDGDRLR---ATKLGKLVSRLYIDPLTAAELVDGLRKADEE 511
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
7-198 |
3.01e-53 |
|
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: 183.19 E-value: 3.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 7 YPWQLECLSR-VARTSRSLVYTAPTGAGKSRVADALLEETLASDGGgRALVVLPYVALVRERAMALAKTLRARGIGVRAY 85
Cdd:cd18026 18 YDWQKECLSLpGLLEGRNLVYSLPTSGGKTLVAEILMLKRLLERRK-KALFVLPYVSIVQEKVDALSPLFEELGFRVEGY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 86 AGGESEGWALG-GDARCAVTTIEKAANAVSRALERGSFDELRIVVVDELHMVSEDERGGVLEGMLARIRHatrsgrARRG 164
Cdd:cd18026 97 AGNKGRSPPKRrKSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDGHRGALLELLLTKLLY------AAQK 170
|
170 180 190
....*....|....*....|....*....|....
gi 1275576587 165 GPRIVCMSATVNarSLERLAKWLDAETYVGTYRP 198
Cdd:cd18026 171 NIQIVGMSATLP--NLEELASWLRAELYTTNFRP 202
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
7-736 |
8.43e-51 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 190.17 E-value: 8.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 7 YPWQLECLSRVARTSRSLVYTAPTGAGKSRVAD-ALLEETLAsdgGGRALVVLPYVALVRERAmalAKTLRARGIGVR-A 84
Cdd:PRK02362 25 YPPQAEAVEAGLLDGKNLLAAIPTASGKTLIAElAMLKAIAR---GGKALYIVPLRALASEKF---EEFERFEELGVRvG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 85 YAGG--ESEGWALGgDARCAVTTIEKAANAVSRalERGSFDELRIVVVDELHMVSEDERGGVLEGMLARIRHatrsgraR 162
Cdd:PRK02362 99 ISTGdyDSRDEWLG-DNDIIVATSEKVDSLLRN--GAPWLDDITCVVVDEVHLIDSANRGPTLEVTLAKLRR-------L 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 163 RGGPRIVCMSATV-NARSLerlAKWLDAETYVGTYRPVELREHVVREDGVFVKTGEgltrvRDAPRAGGSErerELGVVA 241
Cdd:PRK02362 169 NPDLQVVALSATIgNADEL---ADWLDAELVDSEWRPIDLREGVFYGGAIHFDDSQ-----REVEVPSKDD---TLNLVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 242 ELVGEvfvhGHSTLVFCASKAQCSNVAKRLAGIFHRH--PAAMSLRERFVERLFDACEGAPDVDLVQAILSGIAWHHAGL 319
Cdd:PRK02362 238 DTLEE----GGQCLVFVSSRRNAEGFAKRAASALKKTltAAERAELAELAEEIREVSDTETSKDLADCVAKGAAFHHAGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 320 TTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRTII------IPGYiaGTRTPSMAQYKQMAGRAGRKGQSDVGESF 393
Cdd:PRK02362 314 SREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIrdyrryDGGA--GMQPIPVLEYHQMAGRAGRPGLDPYGEAV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 394 LIVMKKDAVA-WAQNLVCGDLPPLESRLfppsrGRDapptAEQKKFYLESIACGILKTKEDAGELACRTFAWTSEDDYSS 472
Cdd:PRK02362 392 LLAKSYDELDeLFERYIWADPEDVRSKL-----ATE----PALRTHVLSTIASGFARTRDGLLEFLEATFYATQTDDTGR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 473 ILLRQEVSLKQIHDEGvvMVRRTGENSTewcSTPEGFAFYRCSL-PIAHAkklrsELDDALRNGLNLTSRTHLLFFCISN 551
Cdd:PRK02362 463 LERVVDDVLDFLERNG--MIEEDGETLE---ATELGHLVSRLYIdPLSAA-----EIIDGLEAAKKPTDLGLLHLVCSTP 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 552 --ESNFLANnlnwhvwSDWLEHDSVLHQLGEKHLGVTREYAEHAQYRLGVSAesravrsrherLAAAHLLSElLANDDTI 629
Cdd:PRK02362 533 dmYELYLRS-------GDYEWLNEYLYEHEDELLGDVPSEFEDDEFEDFLSA-----------VKTALLLED-WIDEVDE 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 630 FDIEQKWSLmsnGAID-RGKIQSLQNMAATTAGMASVLANECGwSALAGLMLNVSEelqaGARRELLPLMRLDGMTGARA 708
Cdd:PRK02362 594 ERITERYGV---GPGDiRGKVETAEWLLHAAERLASELDLDLA-RAARELEKRVEY----GVREELLDLVGLRGVGRVRA 665
|
730 740
....*....|....*....|....*...
gi 1275576587 709 RSLYNAGFKTPtiiASLATEKLDKLVEA 736
Cdd:PRK02362 666 RRLYNAGIESR---ADLRAADKSVVLAI 690
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
197-396 |
3.32e-42 |
|
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: 150.78 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 197 RPVELREHVVREDGVFVKTGEGLTRVRDAPraggsererelgVVAELVGEVFVHGHSTLVFCASKAQCSNVAKRLAGIfh 276
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKFDSD------------IIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLAGI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 277 rhpaamslrerfverlfdacegapdvdlvqailsgiAWHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRT 356
Cdd:cd18795 67 ------------------------------------AFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTV 110
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1275576587 357 II--IPGYIAGTRTP-SMAQYKQMAGRAGRKGQSDVGESFLIV 396
Cdd:cd18795 111 IIkgTQRYDGKGYRElSPLEYLQMIGRAGRPGFDTRGEAIIMT 153
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
7-400 |
6.88e-40 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 157.29 E-value: 6.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 7 YPWQLECLSRVARTSRSLVYTAPTGAGKSRVADALLEETLASDGGgRALVVLPYVALVRERAMALaKTLRARGIGVRAYA 86
Cdd:PRK00254 25 YPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGG-KAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 87 GG--ESEGWALGGDarCAVTTIEKaanaVSRALERGS--FDELRIVVVDELHMVSEDERGGVLEGMLARIrhatrSGRAR 162
Cdd:PRK00254 103 GDydSTDEWLGKYD--IIIATAEK----FDSLLRHGSswIKDVKLVVADEIHLIGSYDRGATLEMILTHM-----LGRAQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 163 rggprIVCMSATV-NArslERLAKWLDAETYVGTYRPVELREHVVREDGVFVKTGEgltrvrdapraggseRERELGVVA 241
Cdd:PRK00254 172 -----ILGLSATVgNA---EELAEWLNAELVVSDWRPVKLRKGVFYQGFLFWEDGK---------------IERFPNSWE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 242 ELVGEVFVHGHSTLVFCASKAQCSNVAKRLAGIFHRHPAAMSLRErfVERLFDACEGAP-DVDLVQAILSGIAWHHAGLT 320
Cdd:PRK00254 229 SLVYDAVKKGKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRA--LKELADSLEENPtNEKLKKALRGGVAFHHAGLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 321 TAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRTII--IPGY--IAGTRTPSMaQYKQMAGRAGRKGQSDVGESfLIV 396
Cdd:PRK00254 307 RTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIrdTKRYsnFGWEDIPVL-EIQQMMGRAGRPKYDEVGEA-IIV 384
|
....
gi 1275576587 397 MKKD 400
Cdd:PRK00254 385 ATTE 388
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
7-733 |
2.37e-37 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 149.26 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 7 YPWQLECLSRVaRTSRSLVYTAPTGAGKSRVADALLEETLASdgGGRALVVLPYVALVRERAMALAKtLRARGIGVRAYA 86
Cdd:PRK01172 24 YDHQRMAIEQL-RKGENVIVSVPTAAGKTLIAYSAIYETFLA--GLKSIYIVPLRSLAMEKYEELSR-LRSLGMRVKISI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 87 GGESEGWALGGDARCAVTTIEKAANAVSRalERGSFDELRIVVVDELHMVSEDERGGVLEGMLARIRHATRSGRarrggp 166
Cdd:PRK01172 100 GDYDDPPDFIKRYDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSARYVNPDAR------ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 167 rIVCMSATVNarSLERLAKWLDAETYVGTYRPVELREHVVREDGVFVktgegltrvrDAPRAGGSErerELGVVAELVGE 246
Cdd:PRK01172 172 -ILALSATVS--NANELAQWLNASLIKSNFRPVPLKLGILYRKRLIL----------DGYERSQVD---INSLIKETVND 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 247 vfvhGHSTLVFCASKAQCSNVAKRLAGIFhrhPAAMSLRERFverlfDACEGAPDVdLVQAILSGIAWHHAGLTTAEKNV 326
Cdd:PRK01172 236 ----GGQVLVFVSSRKNAEDYAEMLIQHF---PEFNDFKVSS-----ENNNVYDDS-LNEMLPHGVAFHHAGLSNEQRRF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 327 IEEGFRDGAILALTCTTTLAAGVNLPTRRTII--IPGYIAGTRTP-SMAQYKQMAGRAGRKGQSDVGESFLIVMKKDAVA 403
Cdd:PRK01172 303 IEEMFRNRYIKVIVATPTLAAGVNLPARLVIVrdITRYGNGGIRYlSNMEIKQMIGRAGRPGYDQYGIGYIYAASPASYD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 404 WAQNLVCGDLPPLESRLFPPSRGRdapptaeqkkF-YLESIACGILKTKEDAGELACRTFaWTSEDDYSSILLRQEVSLK 482
Cdd:PRK01172 383 AAKKYLSGEPEPVISYMGSQRKVR----------FnTLAAISMGLASSMEDLILFYNETL-MAIQNGVDEIDYYIESSLK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 483 QIHDEGVV------MVRRTGENSTEWCSTPEGfafyrcslpiahAKKLRSELDDalrnglNLTSRTHLLFFCISNESnFL 556
Cdd:PRK01172 452 FLKENGFIkgdvtlRATRLGKLTSDLYIDPES------------ALILKSAFDH------DYDEDLALYYISLCREI-IP 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 557 ANNLNWHVWSDWLEHDSVLHQLGE--KHLGVTREYAEHAQYRLGVSAESRAVRSRHERLAAAHLLSELLANDDTIFDIEQ 634
Cdd:PRK01172 513 ANTRDDYYAMEFLEDIGVIDGDISaaKTAMVLRGWISEASMQKITDTYGIAPGDVQARASSADWISYSLARLSSIYKPEM 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 635 KwslmsngaidrgkiqslqnmaattagmasvlanecgwSALAGLMLNVSEelqaGARRELLPLMRLDGMTGARARSLYNA 714
Cdd:PRK01172 593 R-------------------------------------RKLEILNIRIKE----GIREDLIDLVLIPKVGRVRARRLYDA 631
|
730
....*....|....*....
gi 1275576587 715 GFKTPTIIASLATEKLDKL 733
Cdd:PRK01172 632 GFKTVDDIARSSPERIKKI 650
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
7-190 |
7.57e-37 |
|
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: 136.62 E-value: 7.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 7 YPWQLECLSRVARTSRSLVYTAPTGAGKSRVADALLEETLASdGGGRALVVLPYVALVRERAMALAKTLRARGIGVRAYA 86
Cdd:cd17921 3 NPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALAT-SGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 87 GGESEGWALGGDARCAVTTIEKAANAvSRALERGSFDELRIVVVDELHMVSEDERGGVLEGMLARIRHATRsgrarrgGP 166
Cdd:cd17921 82 GDPSVNKLLLAEADILVATPEKLDLL-LRNGGERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRINK-------NA 153
|
170 180
....*....|....*....|....*
gi 1275576587 167 RIVCMSATV-NARSlerLAKWLDAE 190
Cdd:cd17921 154 RFVGLSATLpNAED---LAEWLGVE 175
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
5-422 |
4.87e-33 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 136.61 E-value: 4.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 5 PPYPWQLE-CLSRVARtsRSLVYTAPTGAGKSRVADALLEETLAsdGGGRALVVLPYVALVRERAMALAKTLRARGIGVr 83
Cdd:COG4581 25 ELDPFQEEaILALEAG--RSVLVAAPTGSGKTLVAEFAIFLALA--RGRRSFYTAPIKALSNQKFFDLVERFGAENVGL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 84 ayAGGESegwALGGDARCAVTTIEKAANavsRALERG-SFDELRIVVVDELHMVSEDERGGVLE----GMLARIrhatrs 158
Cdd:COG4581 100 --LTGDA---SVNPDAPIVVMTTEILRN---MLYREGaDLEDVGVVVMDEFHYLADPDRGWVWEepiiHLPARV------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 159 grarrggpRIVCMSATV-NArslERLAKWL-----DAETYVGTYRPVELREHVVREDGVFVKTGEGLTRVRDAPRAggse 232
Cdd:COG4581 166 --------QLVLLSATVgNA---EEFAEWLtrvrgETAVVVSEERPVPLEFHYLVTPRLFPLFRVNPELLRPPSRH---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 233 rerelGVVAELVGEvfvHGHSTLVFCASKAQCSNVAKRLAGIFHRHPAAMSLRERFVERLFDACEGAPDVDLVQAILSGI 312
Cdd:COG4581 231 -----EVIEELDRG---GLLPAIVFIFSRRGCDEAAQQLLSARLTTKEERAEIREAIDEFAEDFSVLFGKTLSRLLRRGI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 313 AWHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRTII-----IPGYiaGTR--TPSmaQYKQMAGRAGRKG 385
Cdd:COG4581 303 AVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFtklskFDGE--RHRplTAR--EFHQIAGRAGRRG 378
|
410 420 430
....*....|....*....|....*....|....*..
gi 1275576587 386 QSDVGESFLIVMKKDAVAWAQNLVCGDLPPLESRLFP 422
Cdd:COG4581 379 IDTEGHVVVLAPEHDDPKKFARLASARPEPLRSSFRP 415
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
6-386 |
7.85e-24 |
|
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: 107.61 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 6 PYPWQLECLSRvARTSRSLVYTAPTGAGKSRVADALLEETLASDGGGRALVVLPYVALVRERAMALAKTLRARGIGVRA- 84
Cdd:COG1205 57 LYSHQAEAIEA-ARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGATALYLYPTKALARDQLRRLRELAEALGLGVRVa 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 85 -YAGG--ESEGWALGGDARCAVTT-------IEKAANAVSRALERgsfdeLRIVVVDELHMVSedergGVLeGM-----L 149
Cdd:COG1205 136 tYDGDtpPEERRWIREHPDIVLTNpdmlhygLLPHHTRWARFFRN-----LRYVVIDEAHTYR-----GVF-GShvanvL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 150 ARIRHatrsgRARRGG--PRIVCMSATV-NARSLerlakwldAETYVGtyRPVelreHVVREDG--------VFVKTGEG 218
Cdd:COG1205 205 RRLRR-----ICRHYGsdPQFILASATIgNPAEH--------AERLTG--RPV----TVVDEDGsprgertfVLWNPPLV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 219 LTRVRdapRAGGSErerelgvVAELVGEVFVHGHSTLVFCASKAQcsnvAKRLAGIFHRHPAAMSLRERfverlfdaceg 298
Cdd:COG1205 266 DDGIR---RSALAE-------AARLLADLVREGLRTLVFTRSRRG----AELLARYARRALREPDLADR----------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 299 apdvdlvqailsgIAWHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRTIIIPGYiagtrTPSMAQYKQMA 378
Cdd:COG1205 321 -------------VAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGY-----PGTRASFWQQA 382
|
....*...
gi 1275576587 379 GRAGRKGQ 386
Cdd:COG1205 383 GRAGRRGQ 390
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
7-193 |
1.83e-22 |
|
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: 95.09 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 7 YPWQLECLSRVARTSRSLVYTAPTGAGKSRVAD-ALLEETLAsdgGGRALVVLPYVALVRERAMALaKTLRARGIGVRAY 85
Cdd:cd18028 3 YPPQAEAVRAGLLKGENLLISIPTASGKTLIAEmAMVNTLLE---GGKALYLVPLRALASEKYEEF-KKLEEIGLKVGIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 86 AGGESEGWALGGDARCAVTTIEKAanavsRALERGSFDELR---IVVVDELHMVSEDERGGVLEGMLARIRHATrsgrar 162
Cdd:cd18028 79 TGDYDEDDEWLGDYDIIVATYEKF-----DSLLRHSPSWLRdvgVVVVDEIHLISDEERGPTLESIVARLRRLN------ 147
|
170 180 190
....*....|....*....|....*....|..
gi 1275576587 163 rGGPRIVCMSATV-NArslERLAKWLDAETYV 193
Cdd:cd18028 148 -PNTQIIGLSATIgNP---DELAEWLNAELVE 175
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
4-185 |
1.46e-19 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 87.55 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 4 PPPYPWQLECLSRVARTSRSLVYTAPTGAGKSRVADALLEETLASDGGGRALVVLPYVALVRERAMALAKTLRARGIGVR 83
Cdd:smart00487 7 EPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 84 AYAGGESEGWAL----GGDARCAVTTIEKAANAVSRalERGSFDELRIVVVDELHMVSEDERGGVLEGMLARIRHAtrsg 159
Cdd:smart00487 87 GLYGGDSKREQLrkleSGKTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKN---- 160
|
170 180
....*....|....*....|....*.
gi 1275576587 160 rarrggPRIVCMSATVNaRSLERLAK 185
Cdd:smart00487 161 ------VQLLLLSATPP-EEIENLLE 179
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
128-396 |
2.11e-19 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 93.42 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 128 VVVDELHMVSEDERGGVLEGMLARIRHATRsgrarrgGPRIVCMSATV-NArslERLAKWLDAETYVGTYRPVELREHVv 206
Cdd:COG1202 330 VVIDEVHMLEDPERGHRLDGLIARLKYYCP-------GAQWIYLSATVgNP---EELAKKLGAKLVEYEERPVPLERHL- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 207 redgVFVKtgegltrvrdapraggsEREReLGVVAELVGEVFVH----GH--STLVFCASKAQCSNVAKRLaGIfhrhpa 280
Cdd:COG1202 399 ----TFAD-----------------GREK-IRIINKLVKREFDTksskGYrgQTIIFTNSRRRCHEIARAL-GY------ 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 281 amslrerfverlfdacegapdvdlvqailsGIAWHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTrRTIIIP 360
Cdd:COG1202 450 ------------------------------KAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPA-SQVIFD 498
|
250 260 270
....*....|....*....|....*....|....*.
gi 1275576587 361 GYIAGTRTPSMAQYKQMAGRAGRKGQSDVGESFLIV 396
Cdd:COG1202 499 SLAMGIEWLSVQEFHQMLGRAGRPDYHDRGKVYLLV 534
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
3-384 |
3.81e-18 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 88.54 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 3 TPPPYPWQLECLSRVART----SRSLVYTAPTGAGKSRVADALLEETLAsdgGGRALVVLPYVALVREramaLAKTLRaR 78
Cdd:COG1061 78 SFELRPYQQEALEALLAAlergGGRGLVVAPTGTGKTVLALALAAELLR---GKRVLVLVPRRELLEQ----WAEELR-R 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 79 GIGVRAYAGGESEgwalgGDARCAVTTIEKAANAVSRALERGSFDelrIVVVDELHMVSEDERGGVLEGMLARirhatrs 158
Cdd:COG1061 150 FLGDPLAGGGKKD-----SDAPITVATYQSLARRAHLDELGDRFG---LVIIDEAHHAGAPSYRRILEAFPAA------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 159 grarrggpRIVCMSATvnarsLERL-AKWLDAETYVG---TYRPVEL-REHVVREDGVFVKTGEgLTRVRDAPRAGGSER 233
Cdd:COG1061 215 --------YRLGLTAT-----PFRSdGREILLFLFDGivyEYSLKEAiEDGYLAPPEYYGIRVD-LTDERAEYDALSERL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 234 ERELGVVAELVGEVF-------VHGHSTLVFCASKAQcsnvAKRLAGIFHRHPAAmslrerfverlfdacegAPDVdlvq 306
Cdd:COG1061 281 REALAADAERKDKILrellrehPDDRKTLVFCSSVDH----AEALAELLNEAGIR-----------------AAVV---- 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1275576587 307 ailsgiawhHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRTIIIpgyIAGTRTPSmaQYKQMAGRAGRK 384
Cdd:COG1061 336 ---------TGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIL---LRPTGSPR--EFIQRLGRGLRP 399
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
7-183 |
3.25e-17 |
|
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: 79.59 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 7 YPWQLECLSrVARTSRSLVYTAPTGAGKSRVAD-ALLEETLASDGGGRALVVLPYVALVRERAMALAKTLRARGIGVRAY 85
Cdd:pfam00270 1 TPIQAEAIP-AILEGRDVLVQAPTGSGKTLAFLlPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 86 AGGESEG--WALGGDARCAVTTIEKAANAVsraLERGSFDELRIVVVDELHMVSEDERGGVLEGMLARIrhatrsgrarR 163
Cdd:pfam00270 80 LGGDSRKeqLEKLKGPDILVGTPGRLLDLL---QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL----------P 146
|
170 180
....*....|....*....|
gi 1275576587 164 GGPRIVCMSATVNaRSLERL 183
Cdd:pfam00270 147 KKRQILLLSATLP-RNLEDL 165
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
27-174 |
1.25e-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: 74.75 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 27 TAPTGAGKSRVADALLEEtLASDGGGRALVVLPYVALVRERAMALaKTLRARGIGVRAYAGGES---EGWALGGDARCAV 103
Cdd:cd00046 7 TAPTGSGKTLAALLAALL-LLLKKGKKVLVLVPTKALALQTAERL-RELFGPGIRVAVLVGGSSaeeREKNKLGDADIII 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1275576587 104 TTIEKAANAVSRALeRGSFDELRIVVVDELHMVSEDERGGVLegMLARIRhatrsgRARRGGPRIVCMSAT 174
Cdd:cd00046 85 ATPDMLLNLLLRED-RLFLKDLKLIIVDEAHALLIDSRGALI--LDLAVR------KAGLKNAQVILLSAT 146
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
10-191 |
1.65e-13 |
|
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: 70.08 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 10 QLECLSRVARTSRSLVYTAPTGAGKSRVADA----LLEETLASDGGGRALVVL-PYVALVRERAMALAKTLRARGIGVrA 84
Cdd:cd18023 6 QSEVFPDLLYSDKNFVVSAPTGSGKTVLFELailrLLKERNPLPWGNRKVVYIaPIKALCSEKYDDWKEKFGPLGLSC-A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 85 YAGGESEGWALGG--DARCAVTTIEKAANAVSRALERGSFDEL-RIVVVDELHMVSEdERGGVLEGMLARIR-----HAT 156
Cdd:cd18023 85 ELTGDTEMDDTFEiqDADIILTTPEKWDSMTRRWRDNGNLVQLvALVLIDEVHIIKE-NRGATLEVVVSRMKtlsssSEL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1275576587 157 RSGRARRggPRIVCMSATVNarSLERLAKWLDAET 191
Cdd:cd18023 164 RGSTVRP--MRFVAVSATIP--NIEDLAEWLGDNP 194
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
311-385 |
3.96e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 65.31 E-value: 3.96e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1275576587 311 GIAWHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRTIIIPGYiagtrTPSMAQYKQMAGRAGRKG 385
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL-----PWSPASYIQRIGRAGRAG 82
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
6-349 |
1.20e-11 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 68.21 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 6 PYPWQLECLSRVARTSRSLVyTAPTGAGKSRVA-----DALLEETLASDG--GGRALVVLPYVALVREramaLAKTLRAR 78
Cdd:COG1201 25 PTPPQREAWPAIAAGESTLL-IAPTGSGKTLAAflpalDELARRPRPGELpdGLRVLYISPLKALAND----IERNLRAP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 79 GIGVRAYAGGESEGWALG---GD------AR-------CAVTTIEKAANAVSRALERGSFDELRIVVVDELHMVSEDERG 142
Cdd:COG1201 100 LEEIGEAAGLPLPEIRVGvrtGDtpaserQRqrrrpphILITTPESLALLLTSPDARELLRGVRTVIVDEIHALAGSKRG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 143 GVLEGMLARIRHATrsgrarRGGPRIVCMSATVnaRSLERLAKWLdaetyVG--TYRPVElrehVVreDGVFVKT----- 215
Cdd:COG1201 180 VHLALSLERLRALA------PRPLQRIGLSATV--GPLEEVARFL-----VGyeDPRPVT----IV--DAGAGKKpdlev 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 216 ---GEGLTRVRDAPRAGGSERERElgvVAELVGEvfvHGhSTLVFCASKAQCsnvakrlagifhrhpaamslrERFVERL 292
Cdd:COG1201 241 lvpVEDLIERFPWAGHLWPHLYPR---VLDLIEA---HR-TTLVFTNTRSQA---------------------ERLFQRL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1275576587 293 FDACEGAPDVdlvqailsgIAWHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGV 349
Cdd:COG1201 293 NELNPEDALP---------IAAHHGSLSREQRLEVEEALKAGELRAVVATSSLELGI 340
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
22-187 |
1.74e-11 |
|
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: 63.37 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 22 RSLVYTAPTGAGKSRVA-----DALLEETLAsdgGGRALVVLPYVALVRERAMALAKTLRARGIGVRAyaggesEGWAlg 96
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAflpalSSLADEPEK---GVQVLYISPLKALINDQERRLEEPLDEIDLEIPV------AVRH-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 97 GDARCA-------------VTTIEK-AANAVSRALERgSFDELRIVVVDELHMVSEDERGGVLEGMLARIRHATrsgrar 162
Cdd:cd17922 71 GDTSQSekakqlknppgilITTPESlELLLVNKKLRE-LFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKLT------ 143
|
170 180
....*....|....*....|....*
gi 1275576587 163 RGGPRIVCMSATVnaRSLERLAKWL 187
Cdd:cd17922 144 GRPLRRIGLSATL--GNLEEAAAFL 166
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
312-385 |
2.04e-11 |
|
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: 61.46 E-value: 2.04e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1275576587 312 IAWHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRTIIIPGYiagtrTPSMAQYKQMAGRAGRKG 385
Cdd:pfam00271 41 VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDL-----PWNPASYIQRIGRAGRAG 109
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
228-387 |
6.86e-11 |
|
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: 61.12 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 228 AGGSERERELGVVAELVGEVFVHGHSTLVFCASKAQCSNVAKrlagifhrhpaamSLRERFVErlfdaceGAPDVDLVQA 307
Cdd:cd18797 12 RKDGERGSARREAARLFADLVRAGVKTIVFCRSRKLAELLLR-------------YLKARLVE-------EGPLASKVAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 308 ilsgiawHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRTIIIPGYiagtrTPSMAQYKQMAGRAGRKGQS 387
Cdd:cd18797 72 -------YRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGY-----PGSLASLWQQAGRAGRRGKD 139
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
6-177 |
1.20e-10 |
|
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: 61.06 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 6 PYPWQLECLSRvARTSRSLVYTAPTGAGKSRVADALLEETLASDGGGRALVVLPYVALVRERAMALAKTLRA--RGIGVR 83
Cdd:cd17923 1 LYSHQAEAIEA-ARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQDQLRSLRELLEQlgLGIRVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 84 AYAGGESEG---WALGGDARCAVTTIEKAANAVSR--ALERGSFDELRIVVVDELHMVsedeRG--GV-LEGMLARIRHA 155
Cdd:cd17923 80 TYDGDTPREerrAIIRNPPRILLTNPDMLHYALLPhhDRWARFLRNLRYVVLDEAHTY----RGvfGShVALLLRRLRRL 155
|
170 180
....*....|....*....|..
gi 1275576587 156 TRSGRARrggPRIVCMSATVNA 177
Cdd:cd17923 156 CRRYGAD---PQFILTSATIGN 174
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
19-174 |
2.79e-10 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350777 [Multi-domain] Cd Length: 214 Bit Score: 60.85 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 19 RTSRSLVYTAPTGAGKSRVAD-ALLEET---LASDGGGRA-----LVVLPYVALVRERAMALAKTLRARGIGVRAYAGGE 89
Cdd:cd18019 31 ETDENLLLCAPTGAGKTNVALlTILREIgkhRNPDGTINLdafkiVYIAPMKALVQEMVGNFSKRLAPYGITVAELTGDQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 90 SEGWALGGDARCAVTTIEKAANAVSRALERGSFDELRIVVVDELHMVsEDERGGVLEGMLAR-IRHATRSGRArrggPRI 168
Cdd:cd18019 111 QLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLL-HDDRGPVLESIVARtIRQIEQTQEY----VRL 185
|
....*.
gi 1275576587 169 VCMSAT 174
Cdd:cd18019 186 VGLSAT 191
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
20-187 |
5.46e-09 |
|
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: 56.61 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 20 TSRSLVYTAPTGAGKSRVADALLEETLASDGGGRALVVLPYVALVRERAMALAKTLRAR-GIGVRAYAGGESEGWALGGD 98
Cdd:cd18022 16 TDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKlGKKVVELTGDVTPDMKALAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 99 ARCAVTTIEKAaNAVSRALE-RGSFDELRIVVVDELHMVSEDeRGGVLEGMLARIRHATRsgraRRGGP-RIVCMS-ATV 175
Cdd:cd18022 96 ADIIITTPEKW-DGISRSWQtREYVQQVSLIIIDEIHLLGSD-RGPVLEVIVSRMNYISS----QTEKPvRLVGLStALA 169
|
170
....*....|..
gi 1275576587 176 NARSlerLAKWL 187
Cdd:cd18022 170 NAGD---LANWL 178
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
19-196 |
6.35e-08 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350778 [Multi-domain] Cd Length: 199 Bit Score: 53.59 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 19 RTSRSLVYTAPTGAGKSRVADALLEETLAS--DGGGRA-------LVVLPYVALVRERAMALAKTLRARGIGVRAYAGGE 89
Cdd:cd18020 15 KTNENMLICAPTGAGKTNIAMLTILHEIRQhvNQGGVIkkddfkiVYIAPMKALAAEMVEKFSKRLAPLGIKVKELTGDM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 90 SEGWALGGDARCAVTTIEKAANAVSRALERGSFDEL-RIVVVDELHMVsEDERGGVLEGMLAR-IRHATRSgrarRGGPR 167
Cdd:cd18020 95 QLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLvRLLIIDEVHLL-HDDRGPVIESLVARtLRQVEST----QSMIR 169
|
170 180
....*....|....*....|....*....
gi 1275576587 168 IVCMSATVNarSLERLAKWLDAETYVGTY 196
Cdd:cd18020 170 IVGLSATLP--NYLDVADFLRVNPYKGLF 196
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
8-190 |
2.23e-07 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 51.88 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 8 PWQLECLSRVARTSRSLVYTAPTGAGKSRVADALLEETLASDGGGRALVVLPYVALVRERAMAL-AKTLRARGIGVRAYA 86
Cdd:cd18021 6 PIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWrAKFGPLLGKKVVKLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 87 GGESEGWALGGDARCAVTTIEKAaNAVSRAL-ERGSFDELRIVVVDELHMVSEDErGGVLEGMLARIRH-ATRSGRARrg 164
Cdd:cd18021 86 GETSTDLKLLAKSDVILATPEQW-DVLSRRWkQRKNVQSVELFIADELHLIGGEN-GPVYEVVVSRMRYiSSQLEKPI-- 161
|
170 180
....*....|....*....|....*..
gi 1275576587 165 gpRIVCMSATV-NARSlerLAKWLDAE 190
Cdd:cd18021 162 --RIVGLSSSLaNARD---VGEWLGAS 183
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
6-134 |
5.50e-07 |
|
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: 49.61 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 6 PYPWQLECLSRV--ARTSRSLVYTAPTGAGKSRVADALLEETLAsdggGRALVVLPYVALVRERAMALAKTLRARGIGvr 83
Cdd:cd17926 1 LRPYQEEALEAWlaHKNNRRGILVLPTGSGKTLTALALIAYLKE----LRTLIVVPTDALLDQWKERFEDFLGDSSIG-- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1275576587 84 aYAGGESEGWALGGDARcaVTTIEKAANAVSRALERGSFDELriVVVDELH 134
Cdd:cd17926 75 -LIGGGKKKDFDDANVV--VATYQSLSNLAEEEKDLFDQFGL--LIVDEAH 120
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
225-387 |
1.93e-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: 48.03 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 225 APRAGGSERERELGVVAELVGEVfVHGHSTLVFCASKAQCsnvakrlagifhrhpaamslrERFVERLFDACEGAPDVDL 304
Cdd:cd18796 13 APEIFPWAGESGADAYAEVIFLL-ERHKSTLVFTNTRSQA---------------------ERLAQRLRELCPDRVPPDF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 305 vqailsgIAWHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRTIIIPGyiagtRTPSMAQYKQMAGRAGRK 384
Cdd:cd18796 71 -------IALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG-----SPKSVARLLQRLGRSGHR 138
|
...
gi 1275576587 385 GQS 387
Cdd:cd18796 139 PGA 141
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
29-386 |
3.73e-06 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 50.14 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 29 PTGAGKS---RVADALLEetlasdggGRALVVLPYVALVRERAMALaktlRARGIGVRAYAGGESEgwalggdarcavtt 105
Cdd:COG0514 40 PTGGGKSlcyQLPALLLP--------GLTLVVSPLIALMKDQVDAL----RAAGIRAAFLNSSLSA-------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 106 ieKAANAVSRALERGSFD-------------------ELRI--VVVDELHMVSE-------DERggvlegmlaRIRHAtr 157
Cdd:COG0514 94 --EERREVLRALRAGELKllyvaperllnprflellrRLKIslFAIDEAHCISQwghdfrpDYR---------RLGEL-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 158 sgRARRGGPRIVCMSATVNARSLERLAKWL---DAETYVGT-YRPvELREHVVredgvfvktgegltrvrdaPRAGGSER 233
Cdd:COG0514 161 --RERLPNVPVLALTATATPRVRADIAEQLgleDPRVFVGSfDRP-NLRLEVV-------------------PKPPDDKL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 234 ERELGVVAELVGEvfvhghSTLVFCASKAQCSNVAKRLAGifHRHPAAMslrerfverlfdacegapdvdlvqailsgia 313
Cdd:COG0514 219 AQLLDFLKEHPGG------SGIVYCLSRKKVEELAEWLRE--AGIRAAA------------------------------- 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1275576587 314 wHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRTII---IPGyiagtrtpSMAQYKQMAGRAGRKGQ 386
Cdd:COG0514 260 -YHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIhydLPK--------SIEAYYQEIGRAGRDGL 326
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
8-190 |
5.73e-06 |
|
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: 48.02 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 8 PWQLECLSRVARtSRSLVYTAPTGAGKSRVAD--ALLeetLASDGGGRALVVLPYVALVRERAMALAKTLRArgigvRAY 85
Cdd:cd18018 15 PGQEEAIARLLS-GRSTLVVLPTGAGKSLCYQlpALL---LRRRGPGLTLVVSPLIALMKDQVDALPRAIKA-----AAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 86 AGGESEGWA-------LGGDARCAVTTIEKAANAVSRALERGSfDELRIVVVDELHMVSE---DERGGVLegMLARIRha 155
Cdd:cd18018 86 NSSLTREERrrileklRAGEVKILYVSPERLVNESFRELLRQT-PPISLLVVDEAHCISEwshNFRPDYL--RLCRVL-- 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1275576587 156 trsgRARRGGPRIVCMSATVNARSLERLAKWLDAE 190
Cdd:cd18018 161 ----RELLGAPPVLALTATATKRVVEDIASHLGIP 191
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
114-384 |
1.21e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 49.15 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 114 SRAleRGSFDELRIVVVDELHMVSEDERGGVLEGMLARIrHATRSGRARRGGprivcMSATVnaRSLERLAKWLDAETYV 193
Cdd:PRK09751 116 SRA--RETLRGVETVIIDEVHAVAGSKRGAHLALSLERL-DALLHTSAQRIG-----LSATV--RSASDVAAFLGGDRPV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 194 GTYRPVELREHVVRedgVFVKTGEGLTRVRDAPRAGGSERERELGVV-----AELVGEVFVHgHSTLVFCASKAQCSNVA 268
Cdd:PRK09751 186 TVVNPPAMRHPQIR---IVVPVANMDDVSSVASGTGEDSHAGREGSIwpyieTGILDEVLRH-RSTIVFTNSRGLAEKLT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 269 KRLAGIF-HRHPAAMSLRERFVErlFDACEGAPDVDLVQAILSGIAWHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAA 347
Cdd:PRK09751 262 ARLNELYaARLQRSPSIAVDAAH--FESTSGATSNRVQSSDVFIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLEL 339
|
250 260 270
....*....|....*....|....*....|....*..
gi 1275576587 348 GVNLPtrrtiIIPGYIAGTRTPSMAQYKQMAGRAGRK 384
Cdd:PRK09751 340 GIDMG-----AVDLVIQVATPLSVASGLQRIGRAGHQ 371
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
126-382 |
1.24e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 48.73 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 126 RIVVVDELHMVSEDERGGVLEGMLARIRHATRSGRARRGgprivcMSATVNarSLERLAKWLDAETYVGTYRPVElrehV 205
Cdd:PRK13767 174 KWVIVDEIHSLAENKRGVHLSLSLERLEELAGGEFVRIG------LSATIE--PLEEVAKFLVGYEDDGEPRDCE----I 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 206 VreDGVFVK--TGEGLTRVRDAPRAGGSE-RERELGVVAELVGEvfvhgH-STLVFCASKaqcsNVAKRLAgiFHrhpaa 281
Cdd:PRK13767 242 V--DARFVKpfDIKVISPVDDLIHTPAEEiSEALYETLHELIKE-----HrTTLIFTNTR----SGAERVL--YN----- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 282 msLRERFVERLfdacegapDVDLVQAilsgiawHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRTIIIPG 361
Cdd:PRK13767 304 --LRKRFPEEY--------DEDNIGA-------HHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLG 366
|
250 260
....*....|....*....|..
gi 1275576587 362 yiagtrTP-SMAQYKQMAGRAG 382
Cdd:PRK13767 367 ------SPkSVSRLLQRIGRAG 382
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
336-396 |
1.36e-05 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 43.85 E-value: 1.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1275576587 336 ILALTCTTTLAAGVNLPTRRTIIIPGYIagtrtPSMAQYKQMAGRAGRKGQsDVGESFLIV 396
Cdd:cd18785 23 LEILVATNVLGEGIDVPSLDTVIFFDPP-----SSAASYIQRVGRAGRGGK-DEGEVILFV 77
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
24-183 |
1.88e-05 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438711 [Multi-domain] Cd Length: 174 Bit Score: 45.79 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 24 LVYTAPTGAGKS-RVADALLEEtlASDGGGRALVVLPYVALVRERAMALAKTLRArgigvrayAGGESEGWALGGDARCA 102
Cdd:cd17990 20 VVLEAPPGAGKTtRVPLALLAE--LWIAGGKIIVLEPRRVAARAAARRLATLLGE--------APGETVGYRVRGESRVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 103 -VTTIEKAANAV--SRALERGSFDELRIVVVDELHmvsedERG---GVLEGMLARIRhatrsgRARRGGPRIVCMSATVN 176
Cdd:cd17990 90 rRTRVEVVTEGVllRRLQRDPELSGVGAVILDEFH-----ERSldaDLALALLLEVQ------QLLRDDLRLLAMSATLD 158
|
....*..
gi 1275576587 177 ARSLERL 183
Cdd:cd17990 159 GDGLAAL 165
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
28-185 |
5.96e-05 |
|
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: 44.83 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 28 APTGAGKSRVAD--ALLEEtlasdggGRALVVLPYVALVRERAMALaktlRARGIGVRAYAGGESEGWALGGDARCA--- 102
Cdd:cd17920 34 MPTGGGKSLCYQlpALLLD-------GVTLVVSPLISLMQDQVDRL----QQLGIRAAALNSTLSPEEKREVLLRIKngq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 103 -----VTTiEKAAN-AVSRALER-GSFDELRIVVVDELHMVSEDerggvleGM--------LARIrhatrsgRARRGGPR 167
Cdd:cd17920 103 ykllyVTP-ERLLSpDFLELLQRlPERKRLALIVVDEAHCVSQW-------GHdfrpdylrLGRL-------RRALPGVP 167
|
170
....*....|....*...
gi 1275576587 168 IVCMSATVNARSLERLAK 185
Cdd:cd17920 168 ILALTATATPEVREDILK 185
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
6-134 |
6.23e-05 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 44.09 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 6 PYPWQLECLSRVART-----SRSLVyTAPTGAGKSRVADALLEETLASDGGGRALVVLPYVALVRERAMALAKTLRARGI 80
Cdd:cd18032 1 PRYYQQEAIEALEEArekgqRRALL-VMATGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLEQAERSFKEVLPDGSF 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1275576587 81 GVraYAGGESEgwalGGDARCAVTTIEKAANAV-SRALERGSFDelrIVVVDELH 134
Cdd:cd18032 80 GN--LKGGKKK----PDDARVVFATVQTLNKRKrLEKFPPDYFD---LIIIDEAH 125
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
8-138 |
7.27e-05 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) 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.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 44.66 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 8 PWQLECLSrVARTSRSLVYTAPTGAGKSrvadaLLEETLASDGGGRALVVLPYVALVRERAMALAKtlrargIGVRA--- 84
Cdd:cd18015 21 PLQLETIN-ATMAGRDVFLVMPTGGGKS-----LCYQLPALCSDGFTLVVSPLISLMEDQLMALKK------LGISAtml 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1275576587 85 --YAGGESEGWALG--GDARCAV----TTIEKAA------NAVSRALERGsfdELRIVVVDELHMVSE 138
Cdd:cd18015 89 naSSSKEHVKWVHAalTDKNSELkllyVTPEKIAkskrfmSKLEKAYNAG---RLARIAIDEVHCCSQ 153
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
5-134 |
7.33e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 43.81 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 5 PPYPWQLECLSRVA----RTSRSLVYTAPTGAGKSRVADALLEETLASDGGGRALVVLPYVALVrERAMalaKTLRARGI 80
Cdd:pfam04851 3 ELRPYQIEAIENLLesikNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLL-EQAL---EEFKKFLP 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1275576587 81 GVRAyAGGESEGWAL---GGDARCAVTTIEKAANAVSRALERGSFDELRIVVVDELH 134
Cdd:pfam04851 79 NYVE-IGEIISGDKKdesVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
6-173 |
1.92e-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: 43.41 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 6 PYPWQLEcLSRVARTSRSLVYtAPTGAGKSRVA----DALLEETLASDGGG-RALVVLPYVALVRERAMALAKTLrarGI 80
Cdd:cd18034 3 PRSYQLE-LFEAALKRNTIVV-LPTGSGKTLIAvmliKEMGELNRKEKNPKkRAVFLVPTVPLVAQQAEAIRSHT---DL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 81 GVRAYAGGESEGWALGGDARCAVTTIEKA---ANAVSRALERG--SFDELRIVVVDELHMvsedergGVLEGMLARI--R 153
Cdd:cd18034 78 KVGEYSGEMGVDKWTKERWKEELEKYDVLvmtAQILLDALRHGflSLSDINLLIFDECHH-------ATGDHPYARImkE 150
|
170 180
....*....|....*....|
gi 1275576587 154 HATRSGRARRggPRIVCMSA 173
Cdd:cd18034 151 FYHLEGRTSR--PRILGLTA 168
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
6-139 |
2.67e-04 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 42.85 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 6 PYPWQLEcLSRVARTSRSLVYTAPTGAGKSRVADAL----LEETLASDGGGRALVVLPYVALVRERAMALAKTLRaRGIG 81
Cdd:cd18036 3 LRNYQLE-LVLPALRGKNTIICAPTGSGKTRVAVYIcrhhLEKRRSAGEKGRVVVLVNKVPLVEQQLEKFFKYFR-KGYK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1275576587 82 VRAYAGGESEgwalggdaRCAVTTIEKAANAV-------------SRALERGSFDELRIVVVDELHMVSED 139
Cdd:cd18036 81 VTGLSGDSSH--------KVSFGQIVKASDVIictpqilinnllsGREEERVYLSDFSLLIFDECHHTQKE 143
|
|
| HTH_61 |
pfam20470 |
Helix-turn-helix domain; This entry represents a presumed helix-turn-helix domain found in DNA ... |
390-468 |
4.29e-04 |
|
Helix-turn-helix domain; This entry represents a presumed helix-turn-helix domain found in DNA polymerase theta.
Pssm-ID: 466619 [Multi-domain] Cd Length: 92 Bit Score: 39.84 E-value: 4.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1275576587 390 GESFLIVMKKDaVAWAQNLVCGDLPPLESRLFPPSRGrdapptaeQKKFYLESIACGILKTKEDAGELACRTFAWTSED 468
Cdd:pfam20470 1 GESILICKEKD-LEKVAELLRAELPPVYSCLLPEKRG--------IKRALLEIIALGLATSPEDVDEYMSCTLLSVQQK 70
|
|
| DEXHc_RLR-3 |
cd18075 |
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ... |
8-139 |
7.45e-04 |
|
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 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: 350833 [Multi-domain] Cd Length: 200 Bit Score: 41.38 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 8 PWQLECLSRVARTSRSLVYTaPTGAGKSRVADALLEETLASDGGGRALVVLPYVALVRERAMALAKTLRARgIGVRAYAG 87
Cdd:cd18075 5 GYQWEVVAPALRGKNSIIWL-PTGAGKTRAAVYVARRHLETKRGAKVAVLVNKVHLVDQHLEKEFHVLLDK-YTVTAISG 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1275576587 88 GESEGWALGGDARCA---VTTIEKAANAVSRALE--RGSFDELRIVVVDELHMVSED 139
Cdd:cd18075 83 DSSHKCFFGQLARGSdvvICTAQILQNALLSGEEeaHVELTDFSLLVIDECHHTHKE 139
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
253-386 |
5.07e-03 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 37.96 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 253 STLVFCASKAQCSNVAKRLAgifhrhpaamslrerfvERLFDAcegapdvdlvqailsgiAWHHAGLTTAEKNVIEEGFR 332
Cdd:cd18794 32 SGIIYCLSRKECEQVAARLQ-----------------SKGISA-----------------AAYHAGLEPSDRRDVQRKWL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1275576587 333 DGAILALTCTTTLAAGVNLPTRRTII---IPgyiagtrtPSMAQYKQMAGRAGRKGQ 386
Cdd:cd18794 78 RDKIQVIVATVAFGMGIDKPDVRFVIhysLP--------KSMESYYQESGRAGRDGL 126
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
253-384 |
5.69e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 37.54 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 253 STLVFCASkaqcsnvakrlagifHRHpaAMSLRERFVERLFDACEGAPDvdlvqailsgiawhHAGLTTAEKNVIEEGFR 332
Cdd:cd18799 8 KTLIFCVS---------------IEH--AEFMAEAFNEAGIDAVALNSD--------------YSDRERGDEALILLFFG 56
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1275576587 333 DGAILALTCTTTLAAGVNLPTRRTIIIpgyiaGTRTPSMAQYKQMAGRAGRK 384
Cdd:cd18799 57 ELKPPILVTVDLLTTGVDIPEVDNVVF-----LRPTESRTLFLQMLGRGLRL 103
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
290-400 |
7.86e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 37.71 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275576587 290 ERLFDACEGAPDVDLVqailsgiawhHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPtRRTIIIpgyIAGTRTP 369
Cdd:cd18811 52 EYLKERFRPELNVGLL----------HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVP-NATVMV---IEDAERF 117
|
90 100 110
....*....|....*....|....*....|.
gi 1275576587 370 SMAQYKQMAGRAGRKGQsdvgESFLIVMKKD 400
Cdd:cd18811 118 GLSQLHQLRGRVGRGDH----QSYCLLVYKD 144
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
312-386 |
9.28e-03 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 37.32 E-value: 9.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1275576587 312 IAWHHAGLTTAEKNVIEEGFRDGAILALTCTTTLAAGVNLPTRRTIIipgyIAGTRTPSMAQYKQMAGRAGRKGQ 386
Cdd:cd18810 54 IAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTII----IERADKFGLAQLYQLRGRVGRSKE 124
|
|
| |
