|
Name |
Accession |
Description |
Interval |
E-value |
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
1-698 |
0e+00 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 1056.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 1 MFDLATrDIKFISGVGPQKAAVLNKeLEIYSLHDLIYYFPYKYIDRSRIYYIHEIDGNMpYIQLKGEILGFETIG-EGRQ 79
Cdd:COG1200 1 MAPLDT-PLTYLKGVGPKRAKLLAK-LGIRTVGDLLFHLPRRYEDRTRLTPIAELRPGE-TVTVEGTVVSVEVVRrRRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 80 RRLTAHFSDGTGVVDLVWFQGiKYILGKYKLHEEYIIFGKPTVFNGRINVAHPDVDKPEDLKLSSVG-LQPYYNTTEKmk 158
Cdd:COG1200 78 RILEVTLSDGTGSLTLVFFNQ-PYLKKQLKPGTRVLVSGKVERFRGGLQMVHPEYELLDEEEAELAGrLTPVYPLTEG-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 159 rsfLNSHAIEKMMATVIQQIQEPLPETLSSKLLAEHHLMPLTEALRNIHFPTNPDVLRRAQYRLKFEELFYVQLNiLRYA 238
Cdd:COG1200 155 ---LSQKTLRKLIRQALDLLAPDLPEPLPEELRARYGLPSLAEALRNIHFPPSDEDLHPARRRLAFEELLALQLA-LLLR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 239 KDRQKRYRGYIFEKVGDVFNTFYtKNLPFQLTGAQKRVLKEIRNDVGSGRQMNRLLQGDVGSGKTLVALMSMLLALDNGY 318
Cdd:COG1200 231 RARRRKRKGPALPGDGELLEAFL-AALPFELTGAQKRVIAEIAADLASPHPMNRLLQGDVGSGKTVVALLAMLAAVEAGY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 319 QACMMAPTEILANQHYETIKELLFGMDIRVELLTGSIKGKRREAILTGLLTGDVKILIGTHAVIEDTVNFSSLGFVVIDE 398
Cdd:COG1200 310 QAALMAPTEILAEQHYRSLSKLLEPLGIRVALLTGSTKAKERREILAALASGEADIVVGTHALIQDDVEFKNLGLVVIDE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 399 QHRFGVAQRARLWSKNvQPPHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPITTIHQFDNRRESMYRSVRKQIEE 478
Cdd:COG1200 390 QHRFGVEQRLALREKG-EAPHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPIKTRVVPEERRDEVYERIREEIAK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 479 GRQVYIVYPLIKESEKIDLKNLEEGYQHVLEEFPKCTVCKVHGKMKPAEKDEQMQLFVSGKAQIMVATTVIEVGVNVPNA 558
Cdd:COG1200 469 GRQAYVVCPLIEESEKLDLQAAEETYEELREAFPGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNA 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 559 SVMIIENAERFGLSQLHQLRGRVGRGAEQSYCILVTNYKLTEDTRKRLEIMVRTNDGFEIAEADLKLRGPGDLEGTQQSG 638
Cdd:COG1200 549 TVMVIENAERFGLSQLHQLRGRVGRGSAQSYCLLLYDAPLSETARERLEVMRETNDGFEIAEEDLELRGPGEFLGTRQSG 628
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 639 IAfDLKIADIVRDGQLLQYVRAIAESIVEQDPAAQnpENEILWRQLkALRKTNVNWAAIS 698
Cdd:COG1200 629 LP-DLRIADLVRDADLLEAAREDAEELLEEDPELA--SHPALRRWL-GLRFRDEDYLEVG 684
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
1-670 |
0e+00 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 1000.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 1 MFDLATRDIKFISGVGPQKAAVLNKeLEIYSLHDLIYYFPYKYIDRSRIYYIHEI-DGNmpYIQLKGEILGFETIGEGRq 79
Cdd:PRK10917 3 LLLLLDAPLTSLKGVGPKTAEKLAK-LGIHTVQDLLLHLPRRYEDRTRLKPIAELrPGE--KVTVEGEVLSAEVVFGKR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 80 RRLTAHFSDGTGVVDLVWFQ-GIKYILGKYKLHEEYIIFGKPTVFNGRINVAHPDVDKPEDLKLSSVG-LQPYYNTTEKm 157
Cdd:PRK10917 79 RRLTVTVSDGTGNLTLRFFNfNQPYLKKQLKVGKRVAVYGKVKRGKYGLEMVHPEYEVLEEESPELEGrLTPVYPLTEG- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 158 krsfLNSHAIEKMMATVIQQIqEPLPETLSSKLLAEHHLMPLTEALRNIHFPTNPDVLRRAQYRLKFEELFYVQLNiLRY 237
Cdd:PRK10917 158 ----LKQKTLRKLIKQALELL-DALPELLPEELLEKYGLLSLAEALRAIHFPPSDEDLHPARRRLKFEELFALQLS-LLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 238 AKDRQKRYRGYIFEKVGDVFNTFYtKNLPFQLTGAQKRVLKEIRNDVGSGRQMNRLLQGDVGSGKTLVALMSMLLALDNG 317
Cdd:PRK10917 232 LRAGRRSKKAGPLPYDGELLKKFL-ASLPFELTGAQKRVVAEILADLASPKPMNRLLQGDVGSGKTVVAALAALAAIEAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 318 YQACMMAPTEILANQHYETIKELLFGMDIRVELLTGSIKGKRREAILTGLLTGDVKILIGTHAVIEDTVNFSSLGFVVID 397
Cdd:PRK10917 311 YQAALMAPTEILAEQHYENLKKLLEPLGIRVALLTGSLKGKERREILEAIASGEADIVIGTHALIQDDVEFHNLGLVIID 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 398 EQHRFGVAQRARLWSKNvQPPHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPITTIHQFDNRRESMYRSVRKQIE 477
Cdd:PRK10917 391 EQHRFGVEQRLALREKG-ENPHVLVMTATPIPRTLAMTAYGDLDVSVIDELPPGRKPITTVVIPDSRRDEVYERIREEIA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 478 EGRQVYIVYPLIKESEKIDLKNLEEGYQHVLEEFPKCTVCKVHGKMKPAEKDEQMQLFVSGKAQIMVATTVIEVGVNVPN 557
Cdd:PRK10917 470 KGRQAYVVCPLIEESEKLDLQSAEETYEELQEAFPELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPN 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 558 ASVMIIENAERFGLSQLHQLRGRVGRGAEQSYCILVTNYKLTEDTRKRLEIMVRTNDGFEIAEADLKLRGPGDLEGTQQS 637
Cdd:PRK10917 550 ATVMVIENAERFGLAQLHQLRGRVGRGAAQSYCVLLYKDPLSETARERLKIMRETNDGFVIAEKDLELRGPGELLGTRQS 629
|
650 660 670
....*....|....*....|....*....|...
gi 1765479064 638 GIAfDLKIADIVRDGQLLQYVRAIAESIVEQDP 670
Cdd:PRK10917 630 GLP-EFKVADLVRDEELLEEARKDARELLERDP 661
|
|
| recG |
TIGR00643 |
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair] |
27-659 |
0e+00 |
|
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273192 [Multi-domain] Cd Length: 630 Bit Score: 703.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 27 LEIYSLHDLIYYFPYKYIDRSRIYYIHEI-DGNmpYIQLKGEILGFETIGEGRQRRLTAHFSD-GTGVVDLVWFQGiKYI 104
Cdd:TIGR00643 1 LGIHTVQDLLFYFPRRYEDRTLLQTIGELlPGE--RATIVGEVLSHCIFGFKRRKVLKLRLKDgGYKKLELRFFNR-AFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 105 LGKYKLHEEYIIFGKPTVFNGRINVAHPDVDKPEDLKLSSVGLQPYYNTTEKMKRSFLnSHAIEKMMATVIQQIQEPLPE 184
Cdd:TIGR00643 78 KKKFKVGSKVVVYGKVKSSKFKAYLIHPEFISEKDGVEFELKILPVYPLTEGLTQKKL-RKLIQQALDQLDKSLEDPLPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 185 tlssKLLAEHHLMPLTEALRNIHFPTNPDVLRRAQYRLKFEELFYVQLNILRYAKDRQKRYRGYIFEKVGDVFNTFYTKn 264
Cdd:TIGR00643 157 ----ELREKYGLLSLEDALRAIHFPKTLSLLELARRRLIFDEFFYLQLAMLARRLGEKQQFSAPPANPSEELLTKFLAS- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 265 LPFQLTGAQKRVLKEIRNDVGSGRQMNRLLQGDVGSGKTLVALMSMLLALDNGYQACMMAPTEILANQHYETIKELLFGM 344
Cdd:TIGR00643 232 LPFKLTRAQKRVVKEILQDLKSDVPMNRLLQGDVGSGKTLVAALAMLAAIEAGYQVALMAPTEILAEQHYNSLRNLLAPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 345 DIRVELLTGSIKGKRREAILTGLLTGDVKILIGTHAVIEDTVNFSSLGFVVIDEQHRFGVAQRARLWSKNVQP--PHVLV 422
Cdd:TIGR00643 312 GIEVALLTGSLKGKRRKELLETIASGQIHLVVGTHALIQEKVEFKRLALVIIDEQHRFGVEQRKKLREKGQGGftPHVLV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 423 MTATPIPRTLAMTLYGDLDVSVIDELPPGRKPITTIHQFDNRRESMYRSVRKQIEEGRQVYIVYPLIKESEKIDLKNLEE 502
Cdd:TIGR00643 392 MSATPIPRTLALTVYGDLDTSIIDELPPGRKPITTVLIKHDEKDIVYEFIEEEIAKGRQAYVVYPLIEESEKLDLKAAEA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 503 GYQHVLEEFPKCTVCKVHGKMKPAEKDEQMQLFVSGKAQIMVATTVIEVGVNVPNASVMIIENAERFGLSQLHQLRGRVG 582
Cdd:TIGR00643 472 LYERLKKAFPKYNVGLLHGRMKSDEKEAVMEEFREGEVDILVATTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVG 551
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1765479064 583 RGAEQSYCILVTNYKLTEDTRKRLEIMVRTNDGFEIAEADLKLRGPGDLEGTQQSGIaFDLKIADIVRDGQLLQYVR 659
Cdd:TIGR00643 552 RGDHQSYCLLVYKNPKSESAKKRLRVMADTLDGFVIAEEDLELRGPGDLLGTKQSGY-PEFRVADLVRDREILVEAR 627
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
222-449 |
7.97e-123 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350750 [Multi-domain] Cd Length: 225 Bit Score: 364.93 E-value: 7.97e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 222 LKFEELFYVQLNILrYAKDRQKRYRGYIFEKVGDVFNTFYtKNLPFQLTGAQKRVLKEIRNDVGSGRQMNRLLQGDVGSG 301
Cdd:cd17992 1 LAFEELFALQLALL-LRRRKIEELKGIILEISGELLKKFL-EALPFELTGAQKRVIDEILRDLASEKPMNRLLQGDVGSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 302 KTLVALMSMLLALDNGYQACMMAPTEILANQHYETIKELLFGMDIRVELLTGSIKGKRREAILTGLLTGDVKILIGTHAV 381
Cdd:cd17992 79 KTVVAALAMLAAVENGYQVALMAPTEILAEQHYDSLKKLLEPLGIRVALLTGSTKAKEKREILEKIASGEIDIVIGTHAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1765479064 382 IEDTVNFSSLGFVVIDEQHRFGVAQRARLWSKNvQPPHVLVMTATPIPRTLAMTLYGDLDVSVIDELP 449
Cdd:cd17992 159 IQEDVEFHNLGLVIIDEQHRFGVEQRLKLREKG-ETPHVLVMTATPIPRTLALTLYGDLDVSIIDELP 225
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
237-670 |
1.11e-108 |
|
transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273152 [Multi-domain] Cd Length: 926 Bit Score: 350.89 E-value: 1.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 237 YAKdrQKRYRGYIFEKVGDVFNTFyTKNLPFQLTGAQKRVLKEIRNDVGSGRQMNRLLQGDVGSGKTLVALMSMLLALDN 316
Cdd:TIGR00580 423 YAK--RKAIKGHAFPPDLEWQQEF-EDSFPFEETPDQLKAIEEIKADMESPRPMDRLVCGDVGFGKTEVAMRAAFKAVLD 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 317 GYQACMMAPTEILANQHYETIKELLFGMDIRVELLTGSIKGKRREAILTGLLTGDVKILIGTHAVIEDTVNFSSLGFVVI 396
Cdd:TIGR00580 500 GKQVAVLVPTTLLAQQHFETFKERFANFPVTIELLSRFRSAKEQNEILKELASGKIDILIGTHKLLQKDVKFKDLGLLII 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 397 DEQHRFGVAQRARL--WSKNVqppHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPITT-IHQFDNR--RESMYRS 471
Cdd:TIGR00580 580 DEEQRFGVKQKEKLkeLRTSV---DVLTLSATPIPRTLHMSMSGIRDLSIIATPPEDRLPVRTfVMEYDPElvREAIRRE 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 472 VRKqieeGRQVYIVYPLIKESEKIDLKnleegyqhvLEEF-PKCTVCKVHGKMKPAEKDEQMQLFVSGKAQIMVATTVIE 550
Cdd:TIGR00580 657 LLR----GGQVFYVHNRIESIEKLATQ---------LRELvPEARIAIAHGQMTENELEEVMLEFYKGEFQVLVCTTIIE 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 551 VGVNVPNASVMIIENAERFGLSQLHQLRGRVGRGAEQSYCILVT--NYKLTEDTRKRLEIMVRTND---GFEIAEADLKL 625
Cdd:TIGR00580 724 TGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKKKAYAYLLYphQKALTEDAQKRLEAIQEFSElgaGFKIALHDLEI 803
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1765479064 626 RGPGDLEGTQQSG----IAFDLKIadivrdgQLLQyvRAIAE------SIVEQDP 670
Cdd:TIGR00580 804 RGAGNLLGEEQSGhiesIGFDLYM-------ELLE--EAIEElkggkpPKLEEET 849
|
|
| Mfd |
COG1197 |
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ... |
237-643 |
2.08e-98 |
|
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription];
Pssm-ID: 440810 [Multi-domain] Cd Length: 1130 Bit Score: 327.41 E-value: 2.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 237 YAKdRQKRyRGYIFEKVGDVF----NTFytknlPFQLTGAQKRVLKEIRNDVGSGRQMNRLLQGDVGSGKTLVALMSMLL 312
Cdd:COG1197 558 YAE-RAAR-KGFAFSPDTPWQrefeAAF-----PYEETPDQLRAIEEVKADMESPRPMDRLVCGDVGFGKTEVALRAAFK 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 313 ALDNGYQACMMAPTEILANQHYETIKELLFGMDIRVELLTGSIKGKRREAILTGLLTGDVKILIGTHAVIEDTVNFSSLG 392
Cdd:COG1197 631 AVMDGKQVAVLVPTTLLAQQHYETFKERFAGFPVRVEVLSRFRTAKEQKETLEGLADGKVDIVIGTHRLLSKDVKFKDLG 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 393 FVVIDEQHRFGVAQRARLwsK----NVqppHVLVMTATPIPRTLAMTLYG--DLdvSVIDELPPGRKPI-TTIHQFDN-- 463
Cdd:COG1197 711 LLIIDEEQRFGVRHKEKL--KalraNV---DVLTLTATPIPRTLQMSLSGirDL--SIIATPPEDRLPVkTFVGEYDDal 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 464 -----RREsMYRsvrkqieeGRQVYIVYPlikesekiDLKNLEEGYQHVLEEFPKCTVCKVHGKMKPAEKDEQMQLFVSG 538
Cdd:COG1197 784 ireaiLRE-LLR--------GGQVFYVHN--------RVEDIEKVAARLQELVPEARIAVAHGQMSERELERVMLDFYEG 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 539 KAQIMVATTVIEVGVNVPNASVMIIENAERFGLSQLHQLRGRVGRGAEQSYCILVT--NYKLTEDTRKRLEIMvRTND-- 614
Cdd:COG1197 847 EFDVLVCTTIIETGIDIPNANTIIIERADRFGLAQLYQLRGRVGRSHRRAYAYLLYppDKVLTEDAEKRLEAI-QEFTel 925
|
410 420 430
....*....|....*....|....*....|....*
gi 1765479064 615 --GFEIAEADLKLRGPGDLEGTQQSG-IA---FDL 643
Cdd:COG1197 926 gaGFKLAMHDLEIRGAGNLLGEEQSGhIAevgFDL 960
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
261-643 |
1.51e-72 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 255.44 E-value: 1.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 261 YTKNLPFQLTGAQKRVLKEIRNDVGSGRQMNRLLQGDVGSGKTLVALMSMLLALDNGYQACMMAPTEILANQHYETIKEL 340
Cdd:PRK10689 593 FCDSFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQHYDNFRDR 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 341 LFGMDIRVELLTGSIKGKRREAILTGLLTGDVKILIGTHAVIEDTVNFSSLGFVVIDEQHRFGVAQRARLWS--KNVQpp 418
Cdd:PRK10689 673 FANWPVRIEMLSRFRSAKEQTQILAEAAEGKIDILIGTHKLLQSDVKWKDLGLLIVDEEHRFGVRHKERIKAmrADVD-- 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 419 hVLVMTATPIPRTLAMTLYGDLDVSVIdELPPGRKPI--TTIHQFDNR--RESMYRSVRKqieeGRQVYIVYPlikesek 494
Cdd:PRK10689 751 -ILTLTATPIPRTLNMAMSGMRDLSII-ATPPARRLAvkTFVREYDSLvvREAILREILR----GGQVYYLYN------- 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 495 iDLKNLEEGYQHVLEEFPKCTVCKVHGKMKPAEKDEQMQLFVSGKAQIMVATTVIEVGVNVPNASVMIIENAERFGLSQL 574
Cdd:PRK10689 818 -DVENIQKAAERLAELVPEARIAIGHGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQL 896
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1765479064 575 HQLRGRVGRGAEQSYCILVTNY--KLTEDTRKRLEIMVRTND---GFEIAEADLKLRGPGDLEGTQQSG----IAFDL 643
Cdd:PRK10689 897 HQLRGRVGRSHHQAYAWLLTPHpkAMTTDAQKRLEAIASLEDlgaGFALATHDLEIRGAGELLGEEQSGqmetIGFSL 974
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
454-610 |
1.86e-70 |
|
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: 226.46 E-value: 1.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 454 PITTIHQFDNRRESMYRSVRKQIEEGRQVYIVYPLIKESEKIDLKNLEEGYQHVLEEF-PKCTVCKVHGKMKPAEKDEQM 532
Cdd:cd18811 1 PITTYLIFHTRLDKVYEFVREEIAKGRQAYVIYPLIEESEKLDLKAAVAMYEYLKERFrPELNVGLLHGRLKSDEKDAVM 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1765479064 533 QLFVSGKAQIMVATTVIEVGVNVPNASVMIIENAERFGLSQLHQLRGRVGRGAEQSYCILVTNYKLTEDTRKRLEIMV 610
Cdd:cd18811 81 AEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYKDPLTETAKQRLRVMT 158
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
263-446 |
1.94e-65 |
|
DEXH/Q-box 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 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: 350749 [Multi-domain] Cd Length: 193 Bit Score: 214.36 E-value: 1.94e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 263 KNLPFQLTGAQKRVLKEIRNDVGSGRQMNRLLQGDVGSGKTLVALMSMLLALDNGYQACMMAPTEILANQHYETIKELLF 342
Cdd:cd17991 10 ASFPYEETPDQLKAIEEILKDMESGKPMDRLICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQHYETFKERFA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 343 GMDIRVELLTGSIKGKRREAILTGLLTGDVKILIGTHAVIEDTVNFSSLGFVVIDEQHRFGVAQRARL--WSKNVqppHV 420
Cdd:cd17991 90 NFPVNVELLSRFTTAAEQREILEGLKEGKVDIVIGTHRLLSKDVEFKNLGLLIIDEEQRFGVKQKEKLkeLRPNV---DV 166
|
170 180
....*....|....*....|....*.
gi 1765479064 421 LVMTATPIPRTLAMTLYGDLDVSVID 446
Cdd:cd17991 167 LTLSATPIPRTLHMALSGIRDLSVIA 192
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
261-446 |
2.33e-64 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 211.12 E-value: 2.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 261 YTKNLPFQLTGAQKRVLKEIRNDVGSGRQMNRLLQGDVGSGKTLVALMSMLLALDNGYQACMMAPTEILANQHYETIKEL 340
Cdd:cd17918 8 LCKSLPFSLTKDQAQAIKDIEKDLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARKF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 341 LfgMDIRVELLTGSikgkRREAILTGlltgdVKILIGTHAVIEDTVNFSSLGFVVIDEQHRFGVAQRARLwsKNVQPPHV 420
Cdd:cd17918 88 L--PFINVELVTGG----TKAQILSG-----ISLLVGTHALLHLDVKFKNLDLVIVDEQHRFGVAQREAL--YNLGATHF 154
|
170 180
....*....|....*....|....*.
gi 1765479064 421 LVMTATPIPRTLAMTLYGDLDVSVID 446
Cdd:cd17918 155 LEATATPIPRTLALALSGLLDLSVID 180
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
454-609 |
1.74e-63 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain] Cd Length: 160 Bit Score: 207.89 E-value: 1.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 454 PITTIHQFDNRRESMYRSVRKQIEEGRQVYIVYPLIKESEKIDLKNLEEGYQHVLEEFPKCTVCKVHGKMKPAEKDEQMQ 533
Cdd:cd18792 1 PIRTYVIPHDDLDLVYEAIERELARGGQVYYVYPRIEESEKLDLKSIEALAEELKELVPEARVALLHGKMTEDEKEAVML 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1765479064 534 LFVSGKAQIMVATTVIEVGVNVPNASVMIIENAERFGLSQLHQLRGRVGRGAEQSYCILVTN--YKLTEDTRKRLEIM 609
Cdd:cd18792 81 EFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYPdpKKLTETAKKRLRAI 158
|
|
| RecG_dom3_C |
pfam19833 |
ATP-dependent DNA helicase RecG, domain 3, C-terminal; This domain is found in ATP-dependent ... |
612-698 |
3.04e-54 |
|
ATP-dependent DNA helicase RecG, domain 3, C-terminal; This domain is found in ATP-dependent DNA helicase RecG from bacteria the homolog from Arabidopsis, which has a critical role in recombination and DNA repair. This protein comprises three structural domains, the largest N-terminal Domain 1 which interacts with DNA junctions, and Domains 2 and 3 at the C-terminal which contain the characteriztic motifs that identify RecG as an SF2 helicase. This domain represents the C-terminal of Domain 3. Around 50 residues that extend from its end cross back to Domain 1 forming a hook that wraps around the extended alpha-helix. This interaction provides a link between Domain 1 and 3 and it is likely that these residues are involved in conformational changes associated with domain movements arising from ATP binding and hydrolysis.
Pssm-ID: 437665 [Multi-domain] Cd Length: 87 Bit Score: 180.36 E-value: 3.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 612 TNDGFEIAEADLKLRGPGDLEGTQQSGIAFDLKIADIVRDGQLLQYVRAIAESIVEQDPAAQNPENEILWRQLKALRKTN 691
Cdd:pfam19833 1 TNDGFEIAEADLKLRGPGDLEGTQQSGIAFDLKIADIARDGQLLQLARTEAEEIIDNDPECSLPENAVLWRQLKELRKTN 80
|
....*..
gi 1765479064 692 VNWAAIS 698
Cdd:pfam19833 81 INWAAIS 87
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
465-609 |
3.10e-34 |
|
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: 127.84 E-value: 3.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 465 RESMYRSVRKqieeGRQVYIVYPLIKESEKIDLKnleegyqhvLEEF-PKCTVCKVHGKMKPAEKDEQMQLFVSGKAQIM 543
Cdd:cd18810 15 REAIERELLR----GGQVFYVHNRIESIEKLATQ---------LRQLvPEARIAIAHGQMTENELEEVMLEFAKGEYDIL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1765479064 544 VATTVIEVGVNVPNASVMIIENAERFGLSQLHQLRGRVGRGAEQSYCILVT--NYKLTEDTRKRLEIM 609
Cdd:cd18810 82 VCTTIIESGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKERAYAYFLYpdQKKLTEDALKRLEAI 149
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
270-435 |
3.09e-28 |
|
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: 111.18 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 270 TGAQKRVLKEIRndvgSGRQMnrLLQGDVGSGKTLVALMSMLLAL---DNGYQACMMAPTEILANQHYETIKELLFGMDI 346
Cdd:pfam00270 1 TPIQAEAIPAIL----EGRDV--LVQAPTGSGKTLAFLLPALEALdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 347 RVELLTGsikGKRREAILTGLltGDVKILIGTHAVIED----TVNFSSLGFVVIDEQHRFGVAQRARLWSKNV----QPP 418
Cdd:pfam00270 75 KVASLLG---GDSRKEQLEKL--KGPDILVGTPGRLLDllqeRKLLKNLKLLVLDEAHRLLDMGFGPDLEEILrrlpKKR 149
|
170
....*....|....*..
gi 1765479064 419 HVLVMTATPiPRTLAMT 435
Cdd:pfam00270 150 QILLLSATL-PRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
263-453 |
9.24e-28 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 111.04 E-value: 9.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 263 KNLPFQLTGAQKRVLKEIRNdvgsgRQMNRLLQGDVGSGKTLVALMSMLLALDNGY--QACMMAPTEILANQHYETIKEL 340
Cdd:smart00487 3 KFGFEPLRPYQKEAIEALLS-----GLRDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 341 LFGMDIRVELLTGsikGKRREAILTGLLTGDVKILIGT-----HAVIEDTVNFSSLGFVVIDEQHRFGVAQRARLWSKNV 415
Cdd:smart00487 78 GPSLGLKVVGLYG---GDSKREQLRKLESGKTDILVTTpgrllDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1765479064 416 Q----PPHVLVMTATP---IPRTLAMTLYGDLDVSVIDELPPGRK 453
Cdd:smart00487 155 KllpkNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIE 199
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
290-426 |
1.03e-19 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 85.92 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 290 MNRLLQGDVGSGKTLVALMSMLLALD-NGYQACMMAPTEILANQHYETIKElLFGMDIRVELLTGSIKGKRREAiltgLL 368
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLkKGKKVLVLVPTKALALQTAERLRE-LFGPGIRVAVLVGGSSAEEREK----NK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 369 TGDVKILIGTHAVIEDTVN------FSSLGFVVIDEQHRFGVAQRA------RLWSKNVQPPHVLVMTAT 426
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLredrlfLKDLKLIIVDEAHALLIDSRGalildlAVRKAGLKNAQVILLSAT 146
|
|
| RecG_wedge |
pfam17191 |
RecG wedge domain; This DNA-binding domain has an OB-fold with large elaborations. |
8-135 |
4.68e-18 |
|
RecG wedge domain; This DNA-binding domain has an OB-fold with large elaborations.
Pssm-ID: 407316 [Multi-domain] Cd Length: 162 Bit Score: 81.72 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 8 DIKFISGVGPQKAAVLnKELEIYSLHDLIYYFPYKYIDRSRIYYIHEIDGNMPyIQLKGEILGFETIGEGRQRRLTAHFS 87
Cdd:pfam17191 1 PIKYAKGVGPKREKIL-KKLGIETIGDLIWYFPRDYEDRRKIIPISDIRHDEK-VTTKGKIVNFETKKIGSLVIISAVLS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1765479064 88 DGTGVVDLVWFQGiKYILGKYKLHEEYIIFGKPT-VFNGRINVAHPDVD 135
Cdd:pfam17191 79 DGIGQVLLKWFNQ-EYIKKFLQKGKEVYITGTVKeGPFGPIEMNNPEIE 126
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
475-583 |
5.83e-18 |
|
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: 79.95 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 475 QIEEGRQVYIVYPLIKESEKIDLKNlEEGYQhvleefpkctVCKVHGKMKPAEKDEQMQLFVSGKAQIMVATTVIEVGVN 554
Cdd:pfam00271 11 KKERGGKVLIFSQTKKTLEAELLLE-KEGIK----------VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100
....*....|....*....|....*....
gi 1765479064 555 VPNASVMIIENAErFGLSQLHQLRGRVGR 583
Cdd:pfam00271 80 LPDVDLVINYDLP-WNPASYIQRIGRAGR 107
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
221-586 |
2.62e-16 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 82.77 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 221 RLKFEELFYVQLNILRYAKDRQKRYRGYIFEKVGDVFNTFY-----TKNLPFQLTGAQKRVLKEIRNDVGSGRQMNrLLQ 295
Cdd:COG1061 28 LSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALeagdeASGTSFELRPYQQEALEALLAALERGGGRG-LVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 296 GDVGSGKTLVALMSMLlALDNGYQACMMAPTEILANQHYETIKELLfgmdiRVELLTGSIKGKRReailtglltgdvKIL 375
Cdd:COG1061 107 APTGTGKTVLALALAA-ELLRGKRVLVLVPRRELLEQWAEELRRFL-----GDPLAGGGKKDSDA------------PIT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 376 IGTHAVIEDTVNFSSL----GFVVIDEQHRFGvaqrARLWSK---NVQPPHVLVMTATPI---PRTLAMTLYGDL--DVS 443
Cdd:COG1061 169 VATYQSLARRAHLDELgdrfGLVIIDEAHHAG----APSYRRileAFPAAYRLGLTATPFrsdGREILLFLFDGIvyEYS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 444 -----------------VIDELPPGRKPITTIHQFDNRR--------ESMYRSVRKQIEEGRQVYIVYPLIKESEKIdlk 498
Cdd:COG1061 245 lkeaiedgylappeyygIRVDLTDERAEYDALSERLREAlaadaerkDKILRELLREHPDDRKTLVFCSSVDHAEAL--- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 499 nleegYQHVLEEFPKCTVckVHGKMKPAEKDEQMQLFVSGKAQIMVATTVIEVGVNVPNASVMII----ENaerfgLSQL 574
Cdd:COG1061 322 -----AELLNEAGIRAAV--VTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILlrptGS-----PREF 389
|
410
....*....|..
gi 1765479064 575 HQLRGRVGRGAE 586
Cdd:COG1061 390 IQRLGRGLRPAP 401
|
|
| RecG_wedge_OBF |
cd04488 |
RecG_wedge_OBF: A subfamily of OB folds corresponding to the OB fold found in the N-terminal ... |
63-137 |
3.64e-16 |
|
RecG_wedge_OBF: A subfamily of OB folds corresponding to the OB fold found in the N-terminal (wedge) domain of Escherichia coli RecG. RecG is a branched-DNA-specific helicase, which catalyzes the interconversion of a DNA replication fork to a four-stranded (Holliday) junction in vivo and in vitro. This interconversion provides a route to repair stalled forks. The RecG monomer contains three domains. The N-terminal domain is named for its wedge structure, and may provide the specificity of RecG for binding branched-DNA structures. During the reversal of fork to Holliday junction, the wedge domain is fixed at the junction of the fork where the leading and lagging strand duplex arms meet, and is thought to promote the unwinding of the nascent leading and lagging strands. In order to form the Holliday junction, these nascent strands would be annealed, and the parental strands reannealed. The wedge domain may also be a processivity factor of RecG on these branched chain substrates.
Pssm-ID: 239934 [Multi-domain] Cd Length: 75 Bit Score: 73.38 E-value: 3.64e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765479064 63 QLKGEILGFETIGEGRQRRLTAHFSDGTGVVDLVWFQGIKYILGKYKLHEEYIIFGKPTVFNGRINVAHPDVDKP 137
Cdd:cd04488 1 TVEGTVVSVEVVPRRGRRRLKVTLSDGTGTLTLVFFNFQPYLKKQLPPGTRVRVSGKVKRFRGGLQIVHPEYELL 75
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
506-583 |
1.08e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 72.24 E-value: 1.08e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1765479064 506 HVLEEFpKCTVCKVHGKMKPAEKDEQMQLFVSGKAQIMVATTVIEVGVNVPNASVMIIENAeRFGLSQLHQLRGRVGR 583
Cdd:smart00490 5 ELLKEL-GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL-PWSPASYIQRIGRAGR 80
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
299-427 |
3.12e-14 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 76.31 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSMLLALDN-GYQACMMAPTEILANQHYETIKELLFGMDIRVELLTGSIKGKRREAiltglLTGDVKILIG 377
Cdd:COG1111 27 GLGKTAVALLVIAERLHKkGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKRKE-----LWEKARIIVA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1765479064 378 THAVIED-----TVNFSSLGFVVIDEQHR-------FGVAQRARLWSKNvqpPHVLVMTATP 427
Cdd:COG1111 102 TPQVIENdliagRIDLDDVSLLIFDEAHRavgnyayVYIAERYHEDAKD---PLILGMTASP 160
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
299-583 |
1.79e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 73.39 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSMLLALDNGYQACMMAPTEILANQHYETIKELLFGMDIRVELLTGSIkgkrreaILTGLLTGDVKILIGT 378
Cdd:COG1204 48 ASGKTLIAELAILKALLNGGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTGDY-------DSDDEWLGRYDILVAT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 379 H-----------AVIEDtvnfssLGFVVIDEQHRFG----------VAQRARLWSKNVQpphVLVMTAT-----PIPRTL 432
Cdd:COG1204 121 PekldsllrngpSWLRD------VDLVVVDEAHLIDdesrgptlevLLARLRRLNPEAQ---IVALSATignaeEIAEWL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 433 AMTLYG------DLDVSVIDElppgrkpiTTIHQFDNRRESMYRS---VRKQIEEGRQVyIVY----------------- 486
Cdd:COG1204 192 DAELVKsdwrpvPLNEGVLYD--------GVLRFDDGSRRSKDPTlalALDLLEEGGQV-LVFvssrrdaeslakklade 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 487 --PLIKESEKIDLKNLEEGYQHVLEEFP------KCTVCKV---HGKMKPAEKDEQMQLFVSGKAQIMVATTVIEVGVNV 555
Cdd:COG1204 263 lkRRLTPEEREELEELAEELLEVSEETHtneklaDCLEKGVafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNL 342
|
330 340 350
....*....|....*....|....*....|...
gi 1765479064 556 PnASVMIIENAERFGLSQL-----HQLRGRVGR 583
Cdd:COG1204 343 P-ARRVIIRDTKRGGMVPIpvlefKQMAGRAGR 374
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
299-427 |
3.12e-11 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 66.82 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSMLLALDN-GYQACMMAPTEILANQHYETIKELLFGMDIRVELLTGSIKGKRREAiltglLTGDVKILIG 377
Cdd:PRK13766 39 GLGKTAIALLVIAERLHKkGGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKRAE-----LWEKAKVIVA 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1765479064 378 THAVIE-DTV----NFSSLGFVVIDEQHR--------FgVAQRARLWSKNvqpPHVLVMTATP 427
Cdd:PRK13766 114 TPQVIEnDLIagriSLEDVSLLIFDEAHRavgnyayvY-IAERYHEDAKN---PLVLGLTASP 172
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
273-400 |
8.99e-11 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350687 [Multi-domain] Cd Length: 178 Bit Score: 61.46 E-value: 8.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 273 QKRVLKEIRNDVGSGRQMnrLLQGDVGSGKTLVALMSMLLALDNGYQACMMAPtEI-LANQhyeTIKEL--LFGMDIRVe 349
Cdd:cd17929 1 QRKAYEAIVSSLGGFKTF--LLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVP-EIsLTPQ---LIKRFkkRFGDKVAV- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1765479064 350 lLTGSIKGKRREAILTGLLTGDVKILIGTHAVIedTVNFSSLGFVVIDEQH 400
Cdd:cd17929 74 -LHSKLSDKERADEWRKIKRGEAKVVIGARSAL--FAPFKNLGLIIVDEEH 121
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
299-427 |
1.64e-10 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 60.61 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSMLLALDN-GYQACMMAPTEILANQHYETIKELLFGMDiRVELLTGSIKGKRREAILTGlltgdVKILIG 377
Cdd:cd18035 26 GLGKTIIAILVAADRLTKkGGKVLILAPSRPLVEQHAENLKRVLNIPD-KITSLTGEVKPEERAERWDA-----SKIIVA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1765479064 378 THAVIEDT-----VNFSSLGFVVIDEQHR----FGVAQRARLWSKNVQPPHVLVMTATP 427
Cdd:cd18035 100 TPQVIENDllagrITLDDVSLLIFDEAHHavgnYAYVYIAHRYKREANNPLILGLTASP 158
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
265-583 |
5.63e-10 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 62.65 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 265 LPFQLTGAQKRVLKEI--RNDVgsgrqmnrLLQGDVGSGKTLVALMSMLLALDNGYQACMMAPTEILANQHYETIKElLF 342
Cdd:COG4581 22 RGFELDPFQEEAILALeaGRSV--------LVAAPTGSGKTLVAEFAIFLALARGRRSFYTAPIKALSNQKFFDLVE-RF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 343 GMDiRVelltgsikgkrreailtGLLTGDVK------ILIGTHAV-----IEDTVNFSSLGFVVIDEQHRFGVAQRARLW 411
Cdd:COG4581 93 GAE-NV-----------------GLLTGDASvnpdapIVVMTTEIlrnmlYREGADLEDVGVVVMDEFHYLADPDRGWVW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 412 sknvQ------PPHV--LVMTAT-----PIPRTLAmTLYGDLDVsVIDE-----------LPPGRKPITTIHQFDNRRES 467
Cdd:COG4581 155 ----EepiihlPARVqlVLLSATvgnaeEFAEWLT-RVRGETAV-VVSEerpvplefhylVTPRLFPLFRVNPELLRPPS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 468 MYRSVRkQIEEGRQ--VYIVY----------------PLIKESEKIDLK--------NLEEGYQHVLEEFPKCTVCKVHG 521
Cdd:COG4581 229 RHEVIE-ELDRGGLlpAIVFIfsrrgcdeaaqqllsaRLTTKEERAEIReaidefaeDFSVLFGKTLSRLLRRGIAVHHA 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 522 KMKPAEKDEQMQLFVSGKAQIMVATTVIEVGVNVPNASVmIIENAERF-GL-------SQLHQLRGRVGR 583
Cdd:COG4581 308 GMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTV-VFTKLSKFdGErhrpltaREFHQIAGRAGR 376
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
299-593 |
6.86e-10 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 62.55 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSMLLALDNGYQAC--MMAPTEILANQHYETIKELL--FGMDIRVELLTGSIKGKRREAILTGlltGDVKI 374
Cdd:COG1205 81 ASGKSLAYLLPVLEALLEDPGATalYLYPTKALARDQLRRLRELAeaLGLGVRVATYDGDTPPEERRWIREH---PDIVL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 375 ---------LIGTHAVIEDtvNFSSLGFVVIDEQHR----FG--VA------QR--ARLWSKnvqpPHVLVMTATpI--P 429
Cdd:COG1205 158 tnpdmlhygLLPHHTRWAR--FFRNLRYVVIDEAHTyrgvFGshVAnvlrrlRRicRHYGSD----PQFILASAT-IgnP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 430 RTLAMTLYGdLDVSVIDEL--PPGRK-------PITTihqfDNRRESMYRSVRKQ----IEEGRQVyIVY-PLIKESEKI 495
Cdd:COG1205 231 AEHAERLTG-RPVTVVDEDgsPRGERtfvlwnpPLVD----DGIRRSALAEAARLladlVREGLRT-LVFtRSRRGAELL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 496 dLKNLEEGYQHvlEEFPKctvcKV---HGKMKPAEKDE-QMQLFvSGKAQIMVATTVIEVGVNVPNASVMIIEnaerfG- 570
Cdd:COG1205 305 -ARYARRALRE--PDLAD----RVaayRAGYLPEERREiERGLR-SGELLGVVSTNALELGIDIGGLDAVVLA-----Gy 371
|
330 340
....*....|....*....|....*.
gi 1765479064 571 ---LSQLHQLRGRVGRGAEQSYCILV 593
Cdd:COG1205 372 pgtRASFWQQAGRAGRRGQDSLVVLV 397
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
293-398 |
1.69e-09 |
|
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: 57.84 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 293 LLQG-DV------GSGKTLVALMSMLLALD-------NGYQACMMAPTEILANQHYETIKELLFGMDIRVELLTGSIKGK 358
Cdd:cd00268 24 ILSGrDVigqaqtGSGKTLAFLLPILEKLLpepkkkgRGPQALVLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIK 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1765479064 359 RREAiltgLLTGDVKILIGT----HAVIED-TVNFSSLGFVVIDE 398
Cdd:cd00268 104 KQIE----ALKKGPDIVVGTpgrlLDLIERgKLDLSNVKYLVLDE 144
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
299-434 |
3.67e-09 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 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: 350717 [Multi-domain] Cd Length: 205 Bit Score: 57.31 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSMLLALDN-----GYQACMMAPTEILANQHYETIKELLFGMDIRVELLTGsikGKRREAILtGLLTGDVK 373
Cdd:cd17959 48 GSGKTAAFLIPMIEKLKAhsptvGARALILSPTRELALQTLKVTKELGKFTDLRTALLVG---GDSLEEQF-EALASNPD 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1765479064 374 ILIGT-----HAVIEDTVNFSSLGFVVIDEQHRF---GVAQR-----ARLwSKNVQpphVLVMTATpIPRTLAM 434
Cdd:cd17959 124 IIIATpgrllHLLVEMNLKLSSVEYVVFDEADRLfemGFAEQlheilSRL-PENRQ---TLLFSAT-LPKLLVE 192
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
299-426 |
1.23e-08 |
|
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: 54.96 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSMLLALDNGYQACM-MAPTEILANQHYETIKELLFGMDIRVELLTGSIKgkrreaiLTGLLTGDVKILIG 377
Cdd:cd17921 27 SSGKTLIAELAILRALATSGGKAVyIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPS-------VNKLLLAEADILVA 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1765479064 378 ThAVIEDTV-------NFSSLGFVVIDEQHRFGVAQRARLW----------SKNVQpphVLVMTAT 426
Cdd:cd17921 100 T-PEKLDLLlrnggerLIQDVRLVVVDEAHLIGDGERGVVLelllsrllriNKNAR---FVGLSAT 161
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
293-607 |
3.19e-08 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 56.28 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 293 LLQGDVGSGKTLVALMSMLLALDNGY--QACMMAPTEILANQHYETIKELlFGMDIRVELltgSIKGKRREAI------- 363
Cdd:cd09639 3 VIEAPTGYGKTEAALLWALHSLKSQKadRVIIALPTRATINAMYRRAKEA-FGETGLYHS---SILSSRIKEMgdseefe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 364 -LTGLLTGDVKILIGT--------HAVIEDTVNFS---------SLGFVVIDEQHRFGVAQRARLWS-----KNVQPPHv 420
Cdd:cd09639 79 hLFPLYIHSNDTLFLDpitvctidQVLKSVFGEFGhyeftlasiANSLLIFDEVHFYDEYTLALILAvlevlKDNDVPI- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 421 LVMTATpIPRTLaMTLYGDLDVSVIDELPP----GRKPITTIHQFDNRRESMYRSVRKQIEEGRQVYIVYPLIKESEKId 496
Cdd:cd09639 158 LLMSAT-LPKFL-KEYAEKIGYVEENEPLDlkpnERAPFIKIESDKVGEISSLERLLEFIKKGGSVAIIVNTVDRAQEF- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 497 lknleegYQHVLEEFPKCTVCKVHGKMKP---AEKDEQMQLFVSGKAQ-IMVATTVIEVGVNVpNASVMIIENAErfgLS 572
Cdd:cd09639 235 -------YQQLKEKGPEEEIMLIHSRFTEkdrAKKEAELLLEFKKSEKfVIVATQVIEASLDI-SVDVMITELAP---ID 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1765479064 573 QLHQLRGRVGR----GAEQSYCI---------LVTNYKLTEDTRKRLE 607
Cdd:cd09639 304 SLIQRLGRLHRygekNGEEVYIItdapdgkgqKPYPYDLVERTIELLE 351
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
299-398 |
3.93e-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: 54.13 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSMLLAL-----DNGYQACMMAPTEILANQHYETIKELLFGMDIRVELLTGSIKGKRREAILTGLltgDVK 373
Cdd:cd17957 37 GSGKTLAFLIPILQKLgkprkKKGLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSIT---KYD 113
|
90 100 110
....*....|....*....|....*....|
gi 1765479064 374 ILIGT-----HAVIEDTVNFSSLGFVVIDE 398
Cdd:cd17957 114 ILVSTplrlvFLLKQGPIDLSSVEYLVLDE 143
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
293-607 |
4.63e-08 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 55.54 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 293 LLQGDVGSGKTLVALMSMLLALDNGY--QACMMAPTEILANQHYETIKELlFGmDIRVELLTGSIKGKRREAILTG---- 366
Cdd:TIGR01587 3 VIEAPTGYGKTEAALLWALHSIKSQKadRVIIALPTRATINAMYRRAKEL-FG-SELVGLHHSSSFSRIKEMGDSEefeh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 367 ---LLTGDVKILIGT--------HAVIEDTVNFS---------SLGFVVIDEQHRFGVAQRARLWS-----KNVQPPHvL 421
Cdd:TIGR01587 81 lfpLYIHSNDKLFLDpitvctidQVLKSVFGEFGhyeftlasiANSLLIFDEVHFYDEYTLALILAvlevlKDNDVPI-L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 422 VMTATpIPRTLaMTLYGDLDVSVIDELPP-------GRKPITTIHQFDNRRESMYRSVRKQIEEGRQVYIVYPLIKESEK 494
Cdd:TIGR01587 160 LMSAT-LPKFL-KEYAEKIGYVEFNEPLDlkeerrfENHRFILIESDKVGEISSLERLLEFIKKGGSIAIIVNTVDRAQE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 495 IdlknleegYQHVLEEFPKCTVCKVHGKMKP---AEKDEQM--QLFVSGKAQIMVATTVIEVGVNVpNASVMIIENAErf 569
Cdd:TIGR01587 238 F--------YQQLKEKAPEEEIILYHSRFTEkdrAKKEAELlrEMKKSNEKFVIVATQVIEASLDI-SADVMITELAP-- 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1765479064 570 gLSQLHQLRGRVGRGAEQ--------------SYCILVTNYKLTEDTRKRLE 607
Cdd:TIGR01587 307 -IDSLIQRLGRLHRYGRKigenfevyiitiapEGKLFPYPYELVERTIQKLE 357
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
273-428 |
1.29e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 51.90 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 273 QKRVLKEIRNDVGSGRQmNRLLQGDVGSGKTLVALMSMLLALDNGYQ--ACMMAPTEILANQHYETIKELLFGMDIRVEL 350
Cdd:pfam04851 8 QIEAIENLLESIKNGQK-RGLIVMATGSGKTLTAAKLIARLFKKGPIkkVLFLVPRKDLLEQALEEFKKFLPNYVEIGEI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 351 LTGsiKGKRREailtgllTGDVKILIGTH-----AVIEDTVNFSSLGF--VVIDEQHRFGvAQRARLWSKNVQPPHVLVM 423
Cdd:pfam04851 87 ISG--DKKDES-------VDDNKIVVTTIqslykALELASLELLPDFFdvIIIDEAHRSG-ASSYRNILEYFKPAFLLGL 156
|
....*
gi 1765479064 424 TATPI 428
Cdd:pfam04851 157 TATPE 161
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
257-397 |
1.33e-07 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 52.33 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 257 FNTFYTKNLPFQLTGAQKRVLKeirndvgsgrqmnRLLQGD-------VGSGKTLVALMSMLLALDNGYQACMMAPTEIL 329
Cdd:cd17924 6 FEEFFKKKTGFPPWGAQRTWAK-------------RLLRGKsfaiiapTGVGKTTFGLATSLYLASKGKRSYLIFPTKSL 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765479064 330 ANQHYETIKELLFGMDIRVELLT--GSIKGKRREAILTGLLTGDVKILIGTHAVIEDtvNFSSLG-----FVVID 397
Cdd:cd17924 73 VKQAYERLSKYAEKAGVEVKILVyhSRLKKKEKEELLEKIEKGDFDILVTTNQFLSK--NFDLLSnkkfdFVFVD 145
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
541-594 |
2.57e-07 |
|
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: 48.47 E-value: 2.57e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1765479064 541 QIMVATTVIEVGVNVPNASVMIIENAERFgLSQLHQLRGRVGRGA-EQSYCILVT 594
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDPPSS-AASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
246-400 |
4.73e-07 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 53.24 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 246 RGYIFEKVGDVFNTFYTKNLPFQ---LTGAQKRVLKEIRNDVGSGrqmNRLLQGDVGSGKTLVALMSMLLALDNGYQACM 322
Cdd:PRK05580 119 KGLIELEEVEVLRLRPPPDPAFEpptLNPEQAAAVEAIRAAAGFS---PFLLDGVTGSGKTEVYLQAIAEVLAQGKQALV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 323 MAPtEI-LANQhyeTIKELL--FGmdIRVELLTGSIKGKRREAILTGLLTGDVKILIGTH-AVIedtVNFSSLGFVVIDE 398
Cdd:PRK05580 196 LVP-EIaLTPQ---MLARFRarFG--APVAVLHSGLSDGERLDEWRKAKRGEAKVVIGARsALF---LPFKNLGLIIVDE 266
|
..
gi 1765479064 399 QH 400
Cdd:PRK05580 267 EH 268
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
280-443 |
7.04e-07 |
|
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: 50.03 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 280 IRNDVGSGRqmNRLLQGDVGSGKTLVALMSMLLALDNGYQACMMAPTEILANQHYETIKElLFGMDIRVELLTGSIkgKR 359
Cdd:cd18028 10 VRAGLLKGE--NLLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKK-LEEIGLKVGISTGDY--DE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 360 REAILtglltGDVKILIGTHAVIEDTVNFSS-----LGFVVIDEQHRFG----------VAQRARLWSKNVQpphVLVMT 424
Cdd:cd18028 85 DDEWL-----GDYDIIVATYEKFDSLLRHSPswlrdVGVVVVDEIHLISdeergptlesIVARLRRLNPNTQ---IIGLS 156
|
170 180
....*....|....*....|
gi 1765479064 425 AT-PIPRTLAMTLYGDLDVS 443
Cdd:cd18028 157 ATiGNPDELAEWLNAELVES 176
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
299-404 |
2.21e-06 |
|
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: 48.35 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSMLLAL--DNGYQACMMAPTEILANQHYETIKELLFGM--DIRVELLTGSIKGKRREAILTG----LLTG 370
Cdd:cd17923 25 ASGKSLCYQLPILEALlrDPGSRALYLYPTKALAQDQLRSLRELLEQLglGIRVATYDGDTPREERRAIIRNppriLLTN 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1765479064 371 DVKI---LIGTHAVIEDTvnFSSLGFVVIDEQH----RFGV 404
Cdd:cd17923 105 PDMLhyaLLPHHDRWARF--LRNLRYVVLDEAHtyrgVFGS 143
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
266-400 |
3.13e-06 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 50.50 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 266 PFQLTGAQKRVLKEIRNDVGSGRQMnrLLQGDVGSGKTLVALMSMLLALDNGYQACMMAPtEI-LANQhyeTIKELL--F 342
Cdd:COG1198 193 PPTLNEEQQAAVEAIRAAAGGFSVF--LLHGVTGSGKTEVYLQAIAEVLAQGKQALVLVP-EIaLTPQ---TVERFRarF 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1765479064 343 GmdIRVELLTGSIKGKRREAILTGLLTGDVKILIGTH-AViedtvnF---SSLGFVVIDEQH 400
Cdd:COG1198 267 G--ARVAVLHSGLSDGERLDEWRRARRGEARIVIGTRsAL------FapfPNLGLIIVDEEH 320
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
299-624 |
4.71e-06 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 49.69 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSML-LALDNGYQACMMA-PTEILANQHYETIKELLfgmDIRVELLTGSIK------------GKRREAIL 364
Cdd:COG1203 157 GGGKTEAALLFALrLAAKHGGRRIIYAlPFTSIINQTYDRLRDLF---GEDVLLHHSLADldlleeeeeyesEARWLKLL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 365 TGLLTGDvkILIGTH----AVIEDTVNFSSLGF-------VVIDE------------------QHRFGVaqrarlwsknv 415
Cdd:COG1203 234 KELWDAP--VVVTTIdqlfESLFSNRKGQERRLhnlansvIILDEvqayppymlalllrllewLKNLGG----------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 416 qppHVLVMTATpIPrtlamTLYGDLDVSVIDELPPGRKPITT-IHQFDNRR----------ESMYRSVRKQIEEGRQVYI 484
Cdd:COG1203 301 ---SVILMTAT-LP-----PLLREELLEAYELIPDEPEELPEyFRAFVRKRvelkegplsdEELAELILEALHKGKSVLV 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 485 VYPLIKESEKIdlknleegYQHVLEEFPKCTVCKVHGKMKPAEKDEQ----MQLFVSGKAQIMVATTVIEVGVNVpNASV 560
Cdd:COG1203 372 IVNTVKDAQEL--------YEALKEKLPDEEVYLLHSRFCPADRSEIekeiKERLERGKPCILVSTQVVEAGVDI-DFDV 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1765479064 561 MIIENAerfGLSQLHQLRGRV---GRGAEQSYCILvtnYKLTEDTRKRleimVRTNDGFEIAEADLK 624
Cdd:COG1203 443 VIRDLA---PLDSLIQRAGRCnrhGRKEEEGNVYV---FDPEDEGGGY----VYDKPLLERTRELLR 499
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
330-428 |
2.11e-05 |
|
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: 45.41 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 330 ANQHYETIKELLFGmDIRVELLTGSIKGKRREAILTGLLTGDVKILIGThAVIEDTVNFSSLGFVVIDEQHRFGVAQ--- 406
Cdd:cd18811 47 AVAMYEYLKERFRP-ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVST-TVIEVGVDVPNATVMVIEDAERFGLSQlhq 124
|
90 100
....*....|....*....|...
gi 1765479064 407 -RARLWSKNVQpPHVLVMTATPI 428
Cdd:cd18811 125 lRGRVGRGDHQ-SYCLLVYKDPL 146
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
273-402 |
2.20e-05 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It 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: 350714 [Multi-domain] Cd Length: 231 Bit Score: 46.47 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 273 QKRVLKEIRNDVGSGRQmnrLLQGDV------GSGKTLVALMSMLLALDNG----YQACMMAPTEILANQHYETIKELLF 342
Cdd:cd17956 17 QAAVIPWLLPSSKSTPP---YRPGDLcvsaptGSGKTLAYVLPIVQALSKRvvprLRALIVVPTKELVQQVYKVFESLCK 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1765479064 343 GMDIRVELLTG--SIKGKRREAILTGLLTGDVK--ILIGT------HavIEDTVNFS--SLGFVVIDEQHRF 402
Cdd:cd17956 94 GTGLKVVSLSGqkSFKKEQKLLLVDTSGRYLSRvdILVATpgrlvdH--LNSTPGFTlkHLRFLVIDEADRL 163
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
265-428 |
2.97e-05 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA 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: 350769 [Multi-domain] Cd Length: 207 Bit Score: 45.74 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 265 LPFQLTGaqkrVLKEIRndvgsgRQMNRLLQGD-VGSGKTLVALMSM-LLALDNGYQACMMAPTEILANQHyetIKELLF 342
Cdd:cd18011 2 LPHQIDA----VLRALR------KPPVRLLLADeVGLGKTIEAGLIIkELLLRGDAKRVLILCPASLVEQW---QDELQD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 343 GMDIRVELLTGSIKGKRREAILTGLLTGDVKI----LIGTHAVIEDTVNFSSLGFVVIDEQHRFGVA---------QRAR 409
Cdd:cd18011 69 KFGLPFLILDRETAAQLRRLIGNPFEEFPIVIvsldLLKRSEERRGLLLSEEWDLVVVDEAHKLRNSgggketkryKLGR 148
|
170
....*....|....*....
gi 1765479064 410 LWSKNVqpPHVLVMTATPI 428
Cdd:cd18011 149 LLAKRA--RHVLLLTATPH 165
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
266-432 |
3.36e-05 |
|
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: 44.95 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 266 PFQLTGAQKRVLKEIRndvgsgRQMNRLLQGDVGSGKTLVALMSMLLALDNGYQACMMAPTEILANQHYETIKElLFGmD 345
Cdd:cd18027 6 PFELDVFQKQAILHLE------AGDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFKN-TFG-D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 346 IrvelltgsikgkrreailtGLLTGDVKILIGTHAVIEDTVNFSS-----------LGFVVIDEQHRFGVAQRARLWSKN 414
Cdd:cd18027 78 V-------------------GLITGDVQLNPEASCLIMTTEILRSmlyngsdvirdLEWVIFDEVHYINDAERGVVWEEV 138
|
170 180
....*....|....*....|.
gi 1765479064 415 V--QPPHV-LVMTATPIPRTL 432
Cdd:cd18027 139 LimLPDHVsIILLSATVPNTV 159
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
297-429 |
3.49e-05 |
|
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: 44.86 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 297 DVGSGKTLVALmSMLLALDNGYQACMM----APTEILANQHYETIKellFGMDIRVELLTGSIKGKRREAILTGLLTGDV 372
Cdd:cd17919 27 EMGLGKTLQAI-AFLAYLLKEGKERGPvlvvCPLSVLENWEREFEK---WTPDLRVVVYHGSQRERAQIRAKEKLDKFDV 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1765479064 373 kILIGTHAVIEDTVNFSSLGF--VVIDEQHRF--GVAQRARlWSKNVQPPHVLVMTATPIP 429
Cdd:cd17919 103 -VLTTYETLRRDKASLRKFRWdlVVVDEAHRLknPKSQLSK-ALKALRAKRRLLLTGTPLQ 161
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
293-398 |
4.87e-05 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 46.29 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 293 LLQG-DV------GSGKTLVALMSMLLALDNGY----QACMMAPTEILANQHYETIKELLFGMDIRVELLTG--SIKGKR 359
Cdd:COG0513 36 ILAGrDVlgqaqtGTGKTAAFLLPLLQRLDPSRprapQALILAPTRELALQVAEELRKLAKYLGLRVATVYGgvSIGRQI 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1765479064 360 REailtglLTGDVKILIGT------HaVIEDTVNFSSLGFVVIDE 398
Cdd:COG0513 116 RA------LKRGVDIVVATpgrlldL-IERGALDLSGVETLVLDE 153
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
265-429 |
1.19e-04 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 45.22 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 265 LPFQLTGAQkRVLKEIRNDVGSgrqmnrLLQGDVGSGKTLVALMSMLLALDNGYQACMM--APTEILANQHYETIKellF 342
Cdd:COG0553 243 RPYQLEGAA-WLLFLRRLGLGG------LLADDMGLGKTIQALALLLELKERGLARPVLivAPTSLVGNWQRELAK---F 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 343 GMDIRVELLTGSIKGKRREA-------ILT--GLLTGDVKILIGthaviedtVNFSslgFVVIDEQHRF--GVAQRARLw 411
Cdd:COG0553 313 APGLRVLVLDGTRERAKGANpfedadlVITsyGLLRRDIELLAA--------VDWD---LVILDEAQHIknPATKRAKA- 380
|
170
....*....|....*...
gi 1765479064 412 SKNVQPPHVLVMTATPIP 429
Cdd:COG0553 381 VRALKARHRLALTGTPVE 398
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
296-402 |
1.57e-04 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 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: 350696 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 296 GDV------GSGKTLVALMSMLLALdngyQACMMAPTEILANQHYETIKELLFGMD---IRVELLTGSIKGKRReailTG 366
Cdd:cd17938 37 GDVlmaaetGSGKTGAFCLPVLQIV----VALILEPSRELAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQ----LK 108
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1765479064 367 LLTGDVKILIGTHAVIEDTVN-----FSSLGFVVIDEQHRF 402
Cdd:cd17938 109 RLESGVDIVVGTPGRLEDLIKtgkldLSSVRFFVLDEADRL 149
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
299-402 |
2.23e-04 |
|
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: 42.19 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSMLLAL----DNGYQACMMAPTEILANQHYETIKELL--FGMDIRVELLTGSIKGKRREAILTGLLTgdv 372
Cdd:cd17922 11 GSGKTEAAFLPALSSLadepEKGVQVLYISPLKALINDQERRLEEPLdeIDLEIPVAVRHGDTSQSEKAKQLKNPPG--- 87
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1765479064 373 kILIGT----HAVIedtVN------FSSLGFVVIDEQHRF 402
Cdd:cd17922 88 -ILITTpeslELLL---VNkklrelFAGLRYVVVDEIHAL 123
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
299-402 |
2.49e-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: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTL---VALMSMLL-----ALDNGYQACMMAPTEILANQHYETIKELL--FGMDIRVELLTGsikGKRREAILTGLL 368
Cdd:cd17960 37 GSGKTLaflIPVLEILLkrkanLKKGQVGALIISPTRELATQIYEVLQSFLehHLPKLKCQLLIG---GTNVEEDVKKFK 113
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1765479064 369 TGDVKILIGTHAVIED-------TVNFSSLGFVVIDEQHRF 402
Cdd:cd17960 114 RNGPNILVGTPGRLEEllsrkadKVKVKSLEVLVLDEADRL 154
|
|
| DEAD-like_helicase_N |
cd17912 |
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ... |
291-339 |
2.77e-04 |
|
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.
Pssm-ID: 350670 [Multi-domain] Cd Length: 81 Bit Score: 40.20 E-value: 2.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1765479064 291 NRLLQGDVGSGKTLVALMSMLLALDNGYQACMMAPTEILANQHYETIKE 339
Cdd:cd17912 1 NILHLGPTGSGKTLVAIQKIASAMSSGKSVLVVTPTKLLAHEILIVIDE 49
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
297-428 |
6.95e-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: 41.48 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 297 DVGSGKTLVALMSM-------LLALDNGYQACMMAPTEILANQHYETIKELLfgmDIRVELLTG--SIKGKRREAILTGL 367
Cdd:cd18034 24 PTGSGKTLIAVMLIkemgelnRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHT---DLKVGEYSGemGVDKWTKERWKEEL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1765479064 368 LTGDVkiLIGTHAVIEDT-----VNFSSLGFVVIDEQHR------FGVAQRARLWSKNVQP-PHVLVMTATPI 428
Cdd:cd18034 101 EKYDV--LVMTAQILLDAlrhgfLSLSDINLLIFDECHHatgdhpYARIMKEFYHLEGRTSrPRILGLTASPV 171
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
299-427 |
9.72e-04 |
|
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: 39.98 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVAlmsMLLALDNGYQACM-MAPTEILANQHYETIKEllFGMDIRVELLT-GSIKGKRREAILTGLltgdVKILI 376
Cdd:cd17926 28 GSGKTLTA---LALIAYLKELRTLiVVPTDALLDQWKERFED--FLGDSSIGLIGgGKKKDFDDANVVVAT----YQSLS 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1765479064 377 GTHAVIEDTVNFSslGFVVIDEQHRFGvaqrARLWS---KNVQPPHVLVMTATP 427
Cdd:cd17926 99 NLAEEEKDLFDQF--GLLIVDEAHHLP----AKTFSeilKELNAKYRLGLTATP 146
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
299-432 |
1.25e-03 |
|
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: 40.82 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSML--------LALDNGYQACMMAPTEILANQHYETIKELLFGMDIRVELLTG--SIKGKRREailtglL 368
Cdd:cd17953 59 GSGKTLAFLLPMFrhikdqrpVKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGgsGISEQIAE------L 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765479064 369 TGDVKILIGTHAVIED--------TVNFSSLGFVVIDEQHR---FGVAQRARLWSKNVQPPHVLVMTATPIPRTL 432
Cdd:cd17953 133 KRGAEIVVCTPGRMIDiltanngrVTNLRRVTYVVLDEADRmfdMGFEPQIMKIVNNIRPDRQTVLFSATFPRKV 207
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
520-583 |
1.80e-03 |
|
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: 39.46 E-value: 1.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1765479064 520 HGKMKPAEKDEQMQLFVSGKAQIMVATTVIEVGVNVPnASVMIIENAERFG--------LSQLHQLRGRVGR 583
Cdd:cd18795 70 HAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP-ARTVIIKGTQRYDgkgyrelsPLEYLQMIGRAGR 140
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
520-592 |
2.20e-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: 38.73 E-value: 2.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1765479064 520 HGKMKPAEKDEQMQLFVSGKAQIMVATTVIEVGVNVPNASVMIienaeRFGLSQ----LHQLRGRVGRGAEQSYCIL 592
Cdd:cd18794 61 HAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVI-----HYSLPKsmesYYQESGRAGRDGLPSECIL 132
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
516-583 |
2.32e-03 |
|
C-terminal helicase domain of the 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. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain] Cd Length: 131 Bit Score: 38.64 E-value: 2.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1765479064 516 VCKVHGKMKPAEKDEQMQLFVSGKAQIMVATTVIEVGVNVPNASVMII----ENAERFglsqLHqlR-GRVGR 583
Cdd:cd18787 54 VAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVDHVINydlpRDAEDY----VH--RiGRTGR 120
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
487-583 |
2.42e-03 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350192 [Multi-domain] Cd Length: 135 Bit Score: 38.69 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 487 PLIKESEKIDLK-NLEEG-------------YQHVLEEFPKCTVCKVHGKMKPAEKDEQMQLFVSGK--AQIMVATTVIE 550
Cdd:cd18805 2 PLSVESKPLGSLrNLRPGdcvvafsrkdifsLKREIEKRTGLKCAVIYGALPPETRRQQARLFNDPEsgYDVLVASDAIG 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1765479064 551 VGVNVpNASVMIIENAERFGL--------SQLHQLRGRVGR 583
Cdd:cd18805 82 MGLNL-NIRRVIFSSLSKFDGnemrplspSEVKQIAGRAGR 121
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
293-398 |
2.69e-03 |
|
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: 39.87 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 293 LLQG-DV------GSGKTLVALMSML---------LALDNGYQACMMAPTEILANQHYETIKELLFGMDIRVELLtgSIK 356
Cdd:cd17961 28 ALEGkDIlarartGSGKTAAYALPIIqkilkakaeSGEEQGTRALILVPTRELAQQVSKVLEQLTAYCRKDVRVV--NLS 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1765479064 357 GKRREAILTGLLTGDVKILIGTHAVIED------TVNFSSLGFVVIDE 398
Cdd:cd17961 106 ASSSDSVQRALLAEKPDIVVSTPARLLShlesgsLLLLSTLKYLVIDE 153
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
290-426 |
4.54e-03 |
|
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: 39.10 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 290 MNRLLQGDVGSGKTLVALMSMLLALD---NGYQACMMAPTEILANQHYETIKELLFGMDIRVELLTGSIKGKRREAIltg 366
Cdd:cd17963 34 ENLIAQSQSGTGKTAAFVLAMLSRVDptlKSPQALCLAPTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKI--- 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1765479064 367 lltgDVKILIGT-----HAVIEDTVNFSSLGFVVIDE-------QHRFGVAQR-ARLWSKNVQpphVLVMTAT 426
Cdd:cd17963 111 ----TAQIVIGTpgtvlDWLKKRQLDLKKIKILVLDEadvmldtQGHGDQSIRiKRMLPRNCQ---ILLFSAT 176
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
300-407 |
5.75e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 39.94 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 300 SGKTLVALMSMLLALDNGYQACMMAPTEILANQHYETIKEL-LFGmdIRVELLTGSIkgKRREAILtglltGDVKILIGT 378
Cdd:PRK02362 50 SGKTLIAELAMLKAIARGGKALYIVPLRALASEKFEEFERFeELG--VRVGISTGDY--DSRDEWL-----GDNDIIVAT 120
|
90 100 110
....*....|....*....|....*....|....
gi 1765479064 379 HA-----VIEDTVNFSSLGFVVIDEQHRFGVAQR 407
Cdd:PRK02362 121 SEkvdslLRNGAPWLDDITCVVVDEVHLIDSANR 154
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
299-398 |
6.30e-03 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, 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: 350698 [Multi-domain] Cd Length: 201 Bit Score: 38.43 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765479064 299 GSGKTLVALMSMLLALD---NGYQACMMAPTEILANQHYETIKELLFGMDIRVELLTGSIkgKRREAILTglLTGDVKIL 375
Cdd:cd17940 46 GTGKTGAYLIPILEKIDpkkDVIQALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGT--SLRDDIMR--LYQTVHVL 121
|
90 100
....*....|....*....|....*...
gi 1765479064 376 IGTHAVIED-----TVNFSSLGFVVIDE 398
Cdd:cd17940 122 VGTPGRILDlakkgVADLSHCKTLVLDE 149
|
|
| |
