|
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: 1063.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 1 MFDITTrDIKYLQGVGPQRATVLNKeLNLFSLHDLLYYFPYKYVDRSRLYYIHEIDGNMpYIQLKGEILSFETLG-EGRQ 79
Cdd:COG1200 1 MAPLDT-PLTYLKGVGPKRAKLLAK-LGIRTVGDLLFHLPRRYEDRTRLTPIAELRPGE-TVTVEGTVVSVEVVRrRRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 80 RRLVGHFSDGTGIIDLVWFQGiKYLLEHYKTRTEYIVFGKPTVFNGRINVAHPDMDP-SGELTLSTMGLQPYYNTTERmk 158
Cdd:COG1200 78 RILEVTLSDGTGSLTLVFFNQ-PYLKKQLKPGTRVLVSGKVERFRGGLQMVHPEYELlDEEEAELAGRLTPVYPLTEG-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 159 rgfLNSHGLEKLMKNALALLQEPLAETLPPRLVEEHHLMSLDEAIRNIHFPKNPELLRKAQYRLKFEELFYVQLNiLRYS 238
Cdd:COG1200 155 ---LSQKTLRKLIRQALDLLAPDLPEPLPEELRARYGLPSLAEALRNIHFPPSDEDLHPARRRLAFEELLALQLA-LLLR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 239 KDRQRKYRGLRFERVGEIFNTFYsQNLPFELTGAQKRVIKEIRKDMGSGRQMNRLLQGDVGSGKTLVALMSMLIALDNGY 318
Cdd:COG1200 231 RARRRKRKGPALPGDGELLEAFL-AALPFELTGAQKRVIAEIAADLASPHPMNRLLQGDVGSGKTVVALLAMLAAVEAGY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 319 QACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGSVKGKKREKILKDLLTGDVQILIGTHAVLEDTVGFSSLGMVIIDE 398
Cdd:COG1200 310 QAALMAPTEILAEQHYRSLSKLLEPLGIRVALLTGSTKAKERREILAALASGEADIVVGTHALIQDDVEFKNLGLVVIDE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 399 QHRFGVAQRAKLWSKNVcPPHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPIQTIHQFDNRRASLYASIRKQIEE 478
Cdd:COG1200 390 QHRFGVEQRLALREKGE-APHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPIKTRVVPEERRDEVYERIREEIAK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 479 GRQIYIVYPLIKESEKMDIKNLEEGYELICAEFPDCQVSKVHGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPNA 558
Cdd:COG1200 469 GRQAYVVCPLIEESEKLDLQAAEETYEELREAFPGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNA 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 559 SVMVIENAERFGLSQLHQLRGRVGRGADQSYCILVTTYKLTEETRKRLEIMVQTNDGFEIAEADLKLRGPGDLEGTQQSG 638
Cdd:COG1200 549 TVMVIENAERFGLSQLHQLRGRVGRGSAQSYCLLLYDAPLSETARERLEVMRETNDGFEIAEEDLELRGPGEFLGTRQSG 628
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 639 VAfDLKIADIARDGQLLQYVRDVANRIVDEDPAGTrpENAILWQQLqALRKTNINWAAIS 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: 1016.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 1 MFDITTRDIKYLQGVGPQRATVLNKeLNLFSLHDLLYYFPYKYVDRSRLYYIHEI-DGNmpYIQLKGEILSFETLGEGRq 79
Cdd:PRK10917 3 LLLLLDAPLTSLKGVGPKTAEKLAK-LGIHTVQDLLLHLPRRYEDRTRLKPIAELrPGE--KVTVEGEVLSAEVVFGKR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 80 RRLVGHFSDGTGIIDLVWFQ-GIKYLLEHYKTRTEYIVFGKPTVFNGRINVAHPDMDP-SGELTLSTMGLQPYYNTTErm 157
Cdd:PRK10917 79 RRLTVTVSDGTGNLTLRFFNfNQPYLKKQLKVGKRVAVYGKVKRGKYGLEMVHPEYEVlEEESPELEGRLTPVYPLTE-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 158 krgFLNSHGLEKLMKNALALLqEPLAETLPPRLVEEHHLMSLDEAIRNIHFPKNPELLRKAQYRLKFEELFYVQLNILRY 237
Cdd:PRK10917 157 ---GLKQKTLRKLIKQALELL-DALPELLPEELLEKYGLLSLAEALRAIHFPPSDEDLHPARRRLKFEELFALQLSLLLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 238 SKDRQRKYRGLRFERvGEIFNTFYSqNLPFELTGAQKRVIKEIRKDMGSGRQMNRLLQGDVGSGKTLVALMSMLIALDNG 317
Cdd:PRK10917 233 RAGRRSKKAGPLPYD-GELLKKFLA-SLPFELTGAQKRVVAEILADLASPKPMNRLLQGDVGSGKTVVAALAALAAIEAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 318 YQACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGSVKGKKREKILKDLLTGDVQILIGTHAVLEDTVGFSSLGMVIID 397
Cdd:PRK10917 311 YQAALMAPTEILAEQHYENLKKLLEPLGIRVALLTGSLKGKERREILEAIASGEADIVIGTHALIQDDVEFHNLGLVIID 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 398 EQHRFGVAQRAKLWSKNVcPPHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPIQTIHQFDNRRASLYASIRKQIE 477
Cdd:PRK10917 391 EQHRFGVEQRLALREKGE-NPHVLVMTATPIPRTLAMTAYGDLDVSVIDELPPGRKPITTVVIPDSRRDEVYERIREEIA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 478 EGRQIYIVYPLIKESEKMDIKNLEEGYELICAEFPDCQVSKVHGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPN 557
Cdd:PRK10917 470 KGRQAYVVCPLIEESEKLDLQSAEETYEELQEAFPELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPN 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 558 ASVMVIENAERFGLSQLHQLRGRVGRGADQSYCILVTTYKLTEETRKRLEIMVQTNDGFEIAEADLKLRGPGDLEGTQQS 637
Cdd:PRK10917 550 ATVMVIENAERFGLAQLHQLRGRVGRGAAQSYCVLLYKDPLSETARERLKIMRETNDGFVIAEKDLELRGPGELLGTRQS 629
|
650 660 670
....*....|....*....|....*....|...
gi 492427108 638 GVAfDLKIADIARDGQLLQYVRDVANRIVDEDP 670
Cdd:PRK10917 630 GLP-EFKVADLVRDEELLEEARKDARELLERDP 661
|
|
| recG |
TIGR00643 |
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair] |
27-662 |
0e+00 |
|
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273192 [Multi-domain] Cd Length: 630 Bit Score: 716.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 27 LNLFSLHDLLYYFPYKYVDRSRLYYIHEI-DGNmpYIQLKGEILSFETLGEGRQRRLVGHFSD-GTGIIDLVWFQGiKYL 104
Cdd:TIGR00643 1 LGIHTVQDLLFYFPRRYEDRTLLQTIGELlPGE--RATIVGEVLSHCIFGFKRRKVLKLRLKDgGYKKLELRFFNR-AFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 105 LEHYKTRTEYIVFGKPTVFNGRINVAHPDMDPSGELTLSTMGLQPYYNTTERmkrgfLNSHGLEKLMKNALALLQEPLAE 184
Cdd:TIGR00643 78 KKKFKVGSKVVVYGKVKSSKFKAYLIHPEFISEKDGVEFELKILPVYPLTEG-----LTQKKLRKLIQQALDQLDKSLED 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 185 TLPPRLVEEHHLMSLDEAIRNIHFPKNPELLRKAQYRLKFEELFYVQLNILRYSKDRQRKYRGLRFERVGEIFNTFYSQn 264
Cdd:TIGR00643 153 PLPEELREKYGLLSLEDALRAIHFPKTLSLLELARRRLIFDEFFYLQLAMLARRLGEKQQFSAPPANPSEELLTKFLAS- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 265 LPFELTGAQKRVIKEIRKDMGSGRQMNRLLQGDVGSGKTLVALMSMLIALDNGYQACMMAPTEILAAQHYETIRKFLFGM 344
Cdd:TIGR00643 232 LPFKLTRAQKRVVKEILQDLKSDVPMNRLLQGDVGSGKTLVAALAMLAAIEAGYQVALMAPTEILAEQHYNSLRNLLAPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 345 DVRVELLMGSVKGKKREKILKDLLTGDVQILIGTHAVLEDTVGFSSLGMVIIDEQHRFGVAQRAKLWSK--NVCPPHVLV 422
Cdd:TIGR00643 312 GIEVALLTGSLKGKRRKELLETIASGQIHLVVGTHALIQEKVEFKRLALVIIDEQHRFGVEQRKKLREKgqGGFTPHVLV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 423 MTATPIPRTLAMTLYGDLDVSVIDELPPGRKPIQTIHQFDNRRASLYASIRKQIEEGRQIYIVYPLIKESEKMDIKNLEE 502
Cdd:TIGR00643 392 MSATPIPRTLALTVYGDLDTSIIDELPPGRKPITTVLIKHDEKDIVYEFIEEEIAKGRQAYVVYPLIEESEKLDLKAAEA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 503 GYELICAEFPDCQVSKVHGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPNASVMVIENAERFGLSQLHQLRGRVG 582
Cdd:TIGR00643 472 LYERLKKAFPKYNVGLLHGRMKSDEKEAVMEEFREGEVDILVATTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 583 RGADQSYCILVTTYKLTEETRKRLEIMVQTNDGFEIAEADLKLRGPGDLEGTQQSGvAFDLKIADIARDGQLLQYVRDVA 662
Cdd:TIGR00643 552 RGDHQSYCLLVYKNPKSESAKKRLRVMADTLDGFVIAEEDLELRGPGDLLGTKQSG-YPEFRVADLVRDREILVEAREDA 630
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
222-449 |
1.40e-120 |
|
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: 359.15 E-value: 1.40e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 222 LKFEELFYVQLNILRYSKDRQRKyRGLRFERVGEIFNTFYSQnLPFELTGAQKRVIKEIRKDMGSGRQMNRLLQGDVGSG 301
Cdd:cd17992 1 LAFEELFALQLALLLRRRKIEEL-KGIILEISGELLKKFLEA-LPFELTGAQKRVIDEILRDLASEKPMNRLLQGDVGSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 302 KTLVALMSMLIALDNGYQACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGSVKGKKREKILKDLLTGDVQILIGTHAV 381
Cdd:cd17992 79 KTVVAALAMLAAVENGYQVALMAPTEILAEQHYDSLKKLLEPLGIRVALLTGSTKAKEKREILEKIASGEIDIVIGTHAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492427108 382 LEDTVGFSSLGMVIIDEQHRFGVAQRAKLWSKNVcPPHVLVMTATPIPRTLAMTLYGDLDVSVIDELP 449
Cdd:cd17992 159 IQEDVEFHNLGLVIIDEQHRFGVEQRLKLREKGE-TPHVLVMTATPIPRTLALTLYGDLDVSIIDELP 225
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
209-643 |
3.46e-112 |
|
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: 360.13 E-value: 3.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 209 PKNPELLR---------KAQYRLKFEELFYVQLNIlrYSKdRQRKyRGLRFERVGEIFNTFYSqNLPFELTGAQKRVIKE 279
Cdd:TIGR00580 388 GKNPALDKlggkswektKAKVKKSVREIAAKLIEL--YAK-RKAI-KGHAFPPDLEWQQEFED-SFPFEETPDQLKAIEE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 280 IRKDMGSGRQMNRLLQGDVGSGKTLVALMSMLIALDNGYQACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGSVKGKK 359
Cdd:TIGR00580 463 IKADMESPRPMDRLVCGDVGFGKTEVAMRAAFKAVLDGKQVAVLVPTTLLAQQHFETFKERFANFPVTIELLSRFRSAKE 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 360 REKILKDLLTGDVQILIGTHAVLEDTVGFSSLGMVIIDEQHRFGVAQRAKL--WSKNVcppHVLVMTATPIPRTLAMTLY 437
Cdd:TIGR00580 543 QNEILKELASGKIDILIGTHKLLQKDVKFKDLGLLIIDEEQRFGVKQKEKLkeLRTSV---DVLTLSATPIPRTLHMSMS 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 438 GDLDVSVIDELPPGRKPIQT-IHQFDNrrASLYASIRKQIEEGRQIYIVYPlikesekmDIKNLEEGYELICAEFPDCQV 516
Cdd:TIGR00580 620 GIRDLSIIATPPEDRLPVRTfVMEYDP--ELVREAIRRELLRGGQVFYVHN--------RIESIEKLATQLRELVPEARI 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 517 SKVHGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPNASVMVIENAERFGLSQLHQLRGRVGRGADQSYCILVTTY 596
Cdd:TIGR00580 690 AIAHGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKKKAYAYLLYPH 769
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 492427108 597 --KLTEETRKRLEIMVQTND---GFEIAEADLKLRGPGDLEGTQQSG----VAFDL 643
Cdd:TIGR00580 770 qkALTEDAQKRLEAIQEFSElgaGFKIALHDLEIRGAGNLLGEEQSGhiesIGFDL 825
|
|
| Mfd |
COG1197 |
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ... |
266-643 |
3.46e-103 |
|
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription];
Pssm-ID: 440810 [Multi-domain] Cd Length: 1130 Bit Score: 340.12 E-value: 3.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 266 PFELTGAQKRVIKEIRKDMGSGRQMNRLLQGDVGSGKTLVALMSMLIALDNGYQACMMAPTEILAAQHYETIRKFLFGMD 345
Cdd:COG1197 584 PYEETPDQLRAIEEVKADMESPRPMDRLVCGDVGFGKTEVALRAAFKAVMDGKQVAVLVPTTLLAQQHYETFKERFAGFP 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 346 VRVELLmgS--VKGKKREKILKDLLTGDVQILIGTHAVLEDTVGFSSLGMVIIDEQHRFGVAQRAKLwsK----NVcppH 419
Cdd:COG1197 664 VRVEVL--SrfRTAKEQKETLEGLADGKVDIVIGTHRLLSKDVKFKDLGLLIIDEEQRFGVRHKEKL--KalraNV---D 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 420 VLVMTATPIPRTLAMTLYG--DLdvSVIDELPPGRKPIQT-IHQFDN---RRAslyasIRKQIEEGRQIYIVYPlikese 493
Cdd:COG1197 737 VLTLTATPIPRTLQMSLSGirDL--SIIATPPEDRLPVKTfVGEYDDaliREA-----ILRELLRGGQVFYVHN------ 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 494 kmDIKNLEEGYELICAEFPDCQVSKVHGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPNASVMVIENAERFGLSQ 573
Cdd:COG1197 804 --RVEDIEKVAARLQELVPEARIAVAHGQMSERELERVMLDFYEGEFDVLVCTTIIETGIDIPNANTIIIERADRFGLAQ 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 574 LHQLRGRVGRGADQSYCILvtTYK----LTEETRKRLEIMVQTND---GFEIAEADLKLRGPGDLEGTQQSG----VAFD 642
Cdd:COG1197 882 LYQLRGRVGRSHRRAYAYL--LYPpdkvLTEDAEKRLEAIQEFTElgaGFKLAMHDLEIRGAGNLLGEEQSGhiaeVGFD 959
|
.
gi 492427108 643 L 643
Cdd:COG1197 960 L 960
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
247-638 |
6.92e-74 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 259.29 E-value: 6.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 247 GLRFERVGEIFNTFySQNLPFELTGAQKRVIKEIRKDMGSGRQMNRLLQGDVGSGKTLVALMSMLIALDNGYQACMMAPT 326
Cdd:PRK10689 580 GFAFKHDREQYQLF-CDSFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPT 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 327 EILAAQHYETIRKFLFGMDVRVELLMGSVKGKKREKILKDLLTGDVQILIGTHAVLEDTVGFSSLGMVIIDEQHRFGV-- 404
Cdd:PRK10689 659 TLLAQQHYDNFRDRFANWPVRIEMLSRFRSAKEQTQILAEAAEGKIDILIGTHKLLQSDVKWKDLGLLIVDEEHRFGVrh 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 405 AQRAKLWSKNVcppHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPIQT-IHQFDNrrASLYASIRKQIEEGRQIY 483
Cdd:PRK10689 739 KERIKAMRADV---DILTLTATPIPRTLNMAMSGMRDLSIIATPPARRLAVKTfVREYDS--LVVREAILREILRGGQVY 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 484 IVYPlikesekmDIKNLEEGYELICAEFPDCQVSKVHGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPNASVMVI 563
Cdd:PRK10689 814 YLYN--------DVENIQKAAERLAELVPEARIAIGHGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIII 885
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 564 ENAERFGLSQLHQLRGRVGRGADQSYCILVTTY--KLTEETRKRLEIMVQTND---GFEIAEADLKLRGPGDLEGTQQSG 638
Cdd:PRK10689 886 ERADHFGLAQLHQLRGRVGRSHHQAYAWLLTPHpkAMTTDAQKRLEAIASLEDlgaGFALATHDLEIRGAGELLGEEQSG 965
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
454-611 |
6.88e-69 |
|
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: 222.22 E-value: 6.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 454 PIQTIHQFDNRRASLYASIRKQIEEGRQIYIVYPLIKESEKMDIKNLEEGYELICAEF-PDCQVSKVHGKMKPAEKDAEM 532
Cdd:cd18811 1 PITTYLIFHTRLDKVYEFVREEIAKGRQAYVIYPLIEESEKLDLKAAVAMYEYLKERFrPELNVGLLHGRLKSDEKDAVM 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492427108 533 QRFVSGETQIMVATTVIEVGVNVPNASVMVIENAERFGLSQLHQLRGRVGRGADQSYCILVTTYKLTEETRKRLEIMVQ 611
Cdd:cd18811 81 AEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYKDPLTETAKQRLRVMTE 159
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
266-446 |
2.13e-68 |
|
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: 222.45 E-value: 2.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 266 PFELTGAQKRVIKEIRKDMGSGRQMNRLLQGDVGSGKTLVALMSMLIALDNGYQACMMAPTEILAAQHYETIRKFLFGMD 345
Cdd:cd17991 13 PYEETPDQLKAIEEILKDMESGKPMDRLICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQHYETFKERFANFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 346 VRVELLMGSVKGKKREKILKDLLTGDVQILIGTHAVLEDTVGFSSLGMVIIDEQHRFGVAQRAKL--WSKNVcppHVLVM 423
Cdd:cd17991 93 VNVELLSRFTTAAEQREILEGLKEGKVDIVIGTHRLLSKDVEFKNLGLLIIDEEQRFGVKQKEKLkeLRPNV---DVLTL 169
|
170 180
....*....|....*....|...
gi 492427108 424 TATPIPRTLAMTLYGDLDVSVID 446
Cdd:cd17991 170 SATPIPRTLHMALSGIRDLSVIA 192
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
261-446 |
2.58e-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: 2.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 261 YSQNLPFELTGAQKRVIKEIRKDMGSGRQMNRLLQGDVGSGKTLVALMSMLIALDNGYQACMMAPTEILAAQHYETIRKF 340
Cdd:cd17918 8 LCKSLPFSLTKDQAQAIKDIEKDLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARKF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 341 LfgMDVRVELlmgsVKGKKREKILKdlltgDVQILIGTHAVLEDTVGFSSLGMVIIDEQHRFGVAQRAKLwsKNVCPPHV 420
Cdd:cd17918 88 L--PFINVEL----VTGGTKAQILS-----GISLLVGTHALLHLDVKFKNLDLVIVDEQHRFGVAQREAL--YNLGATHF 154
|
170 180
....*....|....*....|....*.
gi 492427108 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 ... |
454-611 |
5.52e-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: 206.73 E-value: 5.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 454 PIQTIHQFDNRRASLYASIRKQIEEGRQIYIVYPLIKESEKMDIKNLEEGYELICAEFPDCQVSKVHGKMKPAEKDAEMQ 533
Cdd:cd18792 1 PIRTYVIPHDDLDLVYEAIERELARGGQVYYVYPRIEESEKLDLKSIEALAEELKELVPEARVALLHGKMTEDEKEAVML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 534 RFVSGETQIMVATTVIEVGVNVPNASVMVIENAERFGLSQLHQLRGRVGRGADQSYCILVT--TYKLTEETRKRLEIMVQ 611
Cdd:cd18792 81 EFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYpdPKKLTETAKKRLRAIAE 160
|
|
| RecG_dom3_C |
pfam19833 |
ATP-dependent DNA helicase RecG, domain 3, C-terminal; This domain is found in ATP-dependent ... |
612-698 |
1.74e-56 |
|
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: 186.53 E-value: 1.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 612 TNDGFEIAEADLKLRGPGDLEGTQQSGVAFDLKIADIARDGQLLQYVRDVANRIVDEDPAGTRPENAILWQQLQALRKTN 691
Cdd:pfam19833 1 TNDGFEIAEADLKLRGPGDLEGTQQSGIAFDLKIADIARDGQLLQLARTEAEEIIDNDPECSLPENAVLWRQLKELRKTN 80
|
....*..
gi 492427108 692 INWAAIS 698
Cdd:pfam19833 81 INWAAIS 87
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
470-611 |
2.92e-33 |
|
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: 124.76 E-value: 2.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 470 ASIRKQIEEGRQIYIVYPlikesekmDIKNLEEGYELICAEFPDCQVSKVHGKMKPAEKDAEMQRFVSGETQIMVATTVI 549
Cdd:cd18810 16 EAIERELLRGGQVFYVHN--------RIESIEKLATQLRQLVPEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTII 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492427108 550 EVGVNVPNASVMVIENAERFGLSQLHQLRGRVGRGADQSYCILVT--TYKLTEETRKRLEIMVQ 611
Cdd:cd18810 88 ESGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKERAYAYFLYpdQKKLTEDALKRLEAIQE 151
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
262-453 |
1.30e-29 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 116.44 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 262 SQNLPFELTGAQKRVIKEIRKDMgsgrqMNRLLQGDVGSGKTLVALMSMLIALDNGY--QACMMAPTEILAAQHYETIRK 339
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGL-----RDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 340 FLFGMDVRVELLMGsvkGKKREKILKDLLTGDVQILIGT-----HAVLEDTVGFSSLGMVIIDEQHRFGVAQRAKLWSKN 414
Cdd:smart00487 77 LGPSLGLKVVGLYG---GDSKREQLRKLESGKTDILVTTpgrllDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492427108 415 VC----PPHVLVMTATP---IPRTLAMTLYGDLDVSVIDELPPGRK 453
Cdd:smart00487 154 LKllpkNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIE 199
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
270-435 |
1.83e-29 |
|
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: 114.65 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 270 TGAQKRVIKEIRkdmgSGRQMnrLLQGDVGSGKTLVALMSMLIAL---DNGYQACMMAPTEILAAQHYETIRKFLFGMDV 346
Cdd:pfam00270 1 TPIQAEAIPAIL----EGRDV--LVQAPTGSGKTLAFLLPALEALdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 347 RVELLMGsvkGKKREKILKDLltGDVQILIGTHAVLED----TVGFSSLGMVIIDEQHRFGVAQRAKLWSKNV--CPPH- 419
Cdd:pfam00270 75 KVASLLG---GDSRKEQLEKL--KGPDILVGTPGRLLDllqeRKLLKNLKLLVLDEAHRLLDMGFGPDLEEILrrLPKKr 149
|
170
....*....|....*..
gi 492427108 420 -VLVMTATPiPRTLAMT 435
Cdd:pfam00270 150 qILLLSATL-PRNLEDL 165
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
200-581 |
1.04e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 87.00 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 200 DEAIRNIHFPKNPELLRKAQYRLKFEELFYVQLNILRYSKDRQRKYRGLRFERVGEIFNTFYSQN-----LPFELTGAQK 274
Cdd:COG1061 7 AERGADKLRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGdeasgTSFELRPYQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 275 RVIKEIRKDMGSGRQMNrLLQGDVGSGKTLVALMSMLiALDNGYQACMMAPTEILAAQHYETIRKFLfgmdvrveLLMGS 354
Cdd:COG1061 87 EALEALLAALERGGGRG-LVVAPTGTGKTVLALALAA-ELLRGKRVLVLVPRRELLEQWAEELRRFL--------GDPLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 355 VKGKKREkilkdlltgDVQILIGTHAVLEDTVGFSSL----GMVIIDEQHRFGvaqrAKLWSK---NVCPPHVLVMTATP 427
Cdd:COG1061 157 GGGKKDS---------DAPITVATYQSLARRAHLDELgdrfGLVIIDEAHHAG----APSYRRileAFPAAYRLGLTATP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 428 IpRTLAMTLYGDLDVSVIDELPPGR-------KPIQTIHQFD------NRRASLYASIRKQI--EEGRQIYIVYPLIKES 492
Cdd:COG1061 224 F-RSDGREILLFLFDGIVYEYSLKEaiedgylAPPEYYGIRVdltderAEYDALSERLREALaaDAERKDKILRELLREH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 493 EKM--------DIKNLEEGYELICAEFPDCQVskVHGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPNASVMVI- 563
Cdd:COG1061 303 PDDrktlvfcsSVDHAEALAELLNEAGIRAAV--VTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILl 380
|
410 420
....*....|....*....|.
gi 492427108 564 ---ENaerfgLSQLHQLRGRV 581
Cdd:COG1061 381 rptGS-----PREFIQRLGRG 396
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
290-426 |
1.34e-17 |
|
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: 80.14 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 290 MNRLLQGDVGSGKTLVALMSMLIALD-NGYQACMMAPTEILAAQHYETIRkFLFGMDVRVELLMGSVKGKKREKILKDll 368
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLkKGKKVLVLVPTKALALQTAERLR-ELFGPGIRVAVLVGGSSAEEREKNKLG-- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 369 tgDVQILIGTHAVL------EDTVGFSSLGMVIIDEQHRFGVAQRAKL------WSKNVCPPHVLVMTAT 426
Cdd:cd00046 79 --DADIIIATPDMLlnlllrEDRLFLKDLKLIIVDEAHALLIDSRGALildlavRKAGLKNAQVILLSAT 146
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
475-583 |
2.55e-17 |
|
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: 78.02 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 475 QIEEGRQIYIVYPLIKESEKMDIKNlEEGYElicaefpdcqVSKVHGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVN 554
Cdd:pfam00271 11 KKERGGKVLIFSQTKKTLEAELLLE-KEGIK----------VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100
....*....|....*....|....*....
gi 492427108 555 VPNASVMVIENAErFGLSQLHQLRGRVGR 583
Cdd:pfam00271 80 LPDVDLVINYDLP-WNPASYIQRIGRAGR 107
|
|
| RecG_wedge |
pfam17191 |
RecG wedge domain; This DNA-binding domain has an OB-fold with large elaborations. |
8-155 |
6.39e-15 |
|
RecG wedge domain; This DNA-binding domain has an OB-fold with large elaborations.
Pssm-ID: 407316 [Multi-domain] Cd Length: 162 Bit Score: 72.86 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 8 DIKYLQGVGPQRATVLnKELNLFSLHDLLYYFPYKYVDRSRLYYIHEIDGNMPyIQLKGEILSFETLGEGRQRRLVGHFS 87
Cdd:pfam17191 1 PIKYAKGVGPKREKIL-KKLGIETIGDLIWYFPRDYEDRRKIIPISDIRHDEK-VTTKGKIVNFETKKIGSLVIISAVLS 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 88 DGTGIIDLVWFQGiKYLLEHYKTRTEYIVFGKPT-VFNGRINVAHPDMDP-SGELTLSTMglqPYYNTTE 155
Cdd:pfam17191 79 DGIGQVLLKWFNQ-EYIKKFLQKGKEVYITGTVKeGPFGPIEMNNPEIEEiTGEQEREIL---PVYPLTE 144
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
516-583 |
7.02e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 69.93 E-value: 7.02e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492427108 516 VSKVHGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPNASVMVIENAeRFGLSQLHQLRGRVGR 583
Cdd:smart00490 14 VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL-PWSPASYIQRIGRAGR 80
|
|
| RecG_wedge_OBF |
cd04488 |
RecG_wedge_OBF: A subfamily of OB folds corresponding to the OB fold found in the N-terminal ... |
63-133 |
8.65e-14 |
|
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: 66.83 E-value: 8.65e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492427108 63 QLKGEILSFETLGEGRQRRLVGHFSDGTGIIDLVWFQGIKYLLEHYKTRTEYIVFGKPTVFNGRINVAHPD 133
Cdd:cd04488 1 TVEGTVVSVEVVPRRGRRRLKVTLSDGTGTLTLVFFNFQPYLKKQLPPGTRVRVSGKVKRFRGGLQIVHPE 71
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
299-427 |
1.17e-12 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 71.30 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSMLIALDN-GYQACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGSVKGKKREKILKdlltgDVQILIG 377
Cdd:COG1111 27 GLGKTAVALLVIAERLHKkGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKRKELWE-----KARIIVA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492427108 378 THAVLE-DTVG----FSSLGMVIIDEQHR-------FGVAQRAKLWSKNvcpPHVLVMTATP 427
Cdd:COG1111 102 TPQVIEnDLIAgridLDDVSLLIFDEAHRavgnyayVYIAERYHEDAKD---PLILGMTASP 160
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
273-400 |
1.97e-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: 63.00 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 273 QKRVIKEIRKDMGSGRQMnrLLQGDVGSGKTLVALMSMLIALDNGYQACMMAPtEI-LAAQhyeTIRKF--LFGMDVRVe 349
Cdd:cd17929 1 QRKAYEAIVSSLGGFKTF--LLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVP-EIsLTPQ---LIKRFkkRFGDKVAV- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 492427108 350 lLMGSVKGKKREKILKDLLTGDVQILIGTHAVLedTVGFSSLGMVIIDEQH 400
Cdd:cd17929 74 -LHSKLSDKERADEWRKIKRGEAKVVIGARSAL--FAPFKNLGLIIVDEEH 121
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
260-583 |
1.02e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 64.53 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 260 FYSQNLPFELTGAQKRVIKeirkdmgsgrqmNRLLQGD-------VGSGKTLVALMSMLIALDNGYQACMMAPTEILAAQ 332
Cdd:COG1204 14 FLKERGIEELYPPQAEALE------------AGLLEGKnlvvsapTASGKTLIAELAILKALLNGGKALYIVPLRALASE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 333 HYETIRKFLFGMDVRVELLMGsvkgkkrEKILKDLLTGDVQILIGTH-----------AVLEDtvgfssLGMVIIDEQHR 401
Cdd:COG1204 82 KYREFKRDFEELGIKVGVSTG-------DYDSDDEWLGRYDILVATPekldsllrngpSWLRD------VDLVVVDEAHL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 402 FGVAQR--------AKLwsKNVCPP-HVLVMTAT-----PIPRTLAMTLYG------DLDVSVIDElppgrkpiQTIHQF 461
Cdd:COG1204 149 IDDESRgptlevllARL--RRLNPEaQIVALSATignaeEIAEWLDAELVKsdwrpvPLNEGVLYD--------GVLRFD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 462 DNRRASLYASI---RKQIEEGRQIyIVY------------PLIKESEKMDIKNLEEGYELICAEFPDCQ----------- 515
Cdd:COG1204 219 DGSRRSKDPTLalaLDLLEEGGQV-LVFvssrrdaeslakKLADELKRRLTPEEREELEELAEELLEVSeethtneklad 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492427108 516 -VSK-V---HGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPnASVMVIENAERFGLSQL-----HQLRGRVGR 583
Cdd:COG1204 298 cLEKgVafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIIRDTKRGGMVPIpvlefKQMAGRAGR 374
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
299-427 |
1.62e-10 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 64.51 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSMLIALDN-GYQACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGSVKGKKREKILKdlltgDVQILIG 377
Cdd:PRK13766 39 GLGKTAIALLVIAERLHKkGGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKRAELWE-----KAKVIVA 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492427108 378 THAVLE-DTVG-------FSslgMVIIDEQHR--------FgVAQRAKLWSKNvcpPHVLVMTATP 427
Cdd:PRK13766 114 TPQVIEnDLIAgrisledVS---LLIFDEAHRavgnyayvY-IAERYHEDAKN---PLVLGLTASP 172
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
299-427 |
3.07e-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: 59.84 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSMLIALDN-GYQACMMAPTEILAAQHYETIRKFLFGMDvRVELLMGSVKGKKREKILKdlltgDVQILIG 377
Cdd:cd18035 26 GLGKTIIAILVAADRLTKkGGKVLILAPSRPLVEQHAENLKRVLNIPD-KITSLTGEVKPEERAERWD-----ASKIIVA 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492427108 378 THAVLEDT-----VGFSSLGMVIIDEQHRFG-------VAQRAKLWSKNvcpPHVLVMTATP 427
Cdd:cd18035 100 TPQVIENDllagrITLDDVSLLIFDEAHHAVgnyayvyIAHRYKREANN---PLILGLTASP 158
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
266-400 |
9.25e-10 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 62.06 E-value: 9.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 266 PFELTGAQKRVIKEIRKDMGSGRQMnrLLQGDVGSGKTLVALMSMLIALDNGYQACMMAPtEI-LAAQhyeTIRKFL--F 342
Cdd:COG1198 193 PPTLNEEQQAAVEAIRAAAGGFSVF--LLHGVTGSGKTEVYLQAIAEVLAQGKQALVLVP-EIaLTPQ---TVERFRarF 266
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 492427108 343 GmdVRVELLMGSVKGKKREKILKDLLTGDVQILIGTH-AVLedtVGFSSLGMVIIDEQH 400
Cdd:COG1198 267 G--ARVAVLHSGLSDGERLDEWRRARRGEARIVIGTRsALF---APFPNLGLIIVDEEH 320
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
268-398 |
2.56e-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: 57.45 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 268 ELTGAQKRVIKEIRkdmgSGRqmnrllqgDV------GSGKTLVALMSMLIALD-------NGYQACMMAPTEILAAQHY 334
Cdd:cd00268 12 KPTPIQAQAIPLIL----SGR--------DVigqaqtGSGKTLAFLLPILEKLLpepkkkgRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492427108 335 ETIRKFLFGMDVRVELLMGSVKGKKREKILKdlltGDVQILIGT-----HAVLEDTVGFSSLGMVIIDE 398
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALK----KGPDIVVGTpgrllDLIERGKLDLSNVKYLVLDE 144
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
266-400 |
2.66e-09 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 60.56 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 266 PFELTGAQKRVIKEIRKDMGSGrqmNRLLQGDVGSGKTLVALMsmLIA--LDNGYQACMMAPtEI-LAAQhyeTIRKFL- 341
Cdd:PRK05580 142 PPTLNPEQAAAVEAIRAAAGFS---PFLLDGVTGSGKTEVYLQ--AIAevLAQGKQALVLVP-EIaLTPQ---MLARFRa 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492427108 342 -FGmdVRVELLMGSVKGKKREKILKDLLTGDVQILIGTH-AVLedtVGFSSLGMVIIDEQH 400
Cdd:PRK05580 213 rFG--APVAVLHSGLSDGERLDEWRKAKRGEAKVVIGARsALF---LPFKNLGLIIVDEEH 268
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
249-583 |
1.51e-08 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 58.03 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 249 RFERVGEIFNTFYSQnLPFELTGAQKRVIKEIrkdmGSGRqmNRLLQGDVGSGKTLVALMSMLIALDNGYQACMMAPTEI 328
Cdd:COG4581 7 RADARLEALADFAEE-RGFELDPFQEEAILAL----EAGR--SVLVAAPTGSGKTLVAEFAIFLALARGRRSFYTAPIKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 329 LAAQHYETIRKfLFGMDvRVellmGsvkgkkrekilkdLLTGDV------QILIGTHAVL-----EDTVGFSSLGMVIID 397
Cdd:COG4581 80 LSNQKFFDLVE-RFGAE-NV----G-------------LLTGDAsvnpdaPIVVMTTEILrnmlyREGADLEDVGVVVMD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 398 EQHRFGVAQRAKLWSkNV---CPPHV--LVMTAT-----PIPRTLAmTLYGDLDVsVIDE-----------LPPGRKPIQ 456
Cdd:COG4581 141 EFHYLADPDRGWVWE-EPiihLPARVqlVLLSATvgnaeEFAEWLT-RVRGETAV-VVSEerpvplefhylVTPRLFPLF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 457 TIHQFDNRRASLYASIRkQIEEGRQ--IYIVY----------------PLIKESEKMDIK--------NLEEGYELICAE 510
Cdd:COG4581 218 RVNPELLRPPSRHEVIE-ELDRGGLlpAIVFIfsrrgcdeaaqqllsaRLTTKEERAEIReaidefaeDFSVLFGKTLSR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 511 FPDCQVSKVHGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPNASVmVIENAERF-GL-------SQLHQLRGRVG 582
Cdd:COG4581 297 LLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTV-VFTKLSKFdGErhrpltaREFHQIAGRAG 375
|
.
gi 492427108 583 R 583
Cdd:COG4581 376 R 376
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
299-411 |
4.79e-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: 53.42 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSMLIALDNGYQACM-MAPTEILAAQHYETIRKFLFGMDVRVELLMGSVKgkkrekiLKDLLTGDVQILIG 377
Cdd:cd17921 27 SSGKTLIAELAILRALATSGGKAVyIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPS-------VNKLLLAEADILVA 99
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 492427108 378 T----HAVLED--TVGFSSLGMVIIDEQHRFGVAQRAKLW 411
Cdd:cd17921 100 TpeklDLLLRNggERLIQDVRLVVVDEAHLIGDGERGVVL 139
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
299-593 |
6.15e-08 |
|
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: 56.00 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSMLIALDNGYQAC--MMAPTEILAAQHYETIRKFL--FGMDVRVELLMGSVKGKKREKILKdlltgDVQI 374
Cdd:COG1205 81 ASGKSLAYLLPVLEALLEDPGATalYLYPTKALARDQLRRLRELAeaLGLGVRVATYDGDTPPEERRWIRE-----HPDI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 375 LIGT-----HAVLEDTVG----FSSLGMVIIDEQHR----FG--VAQ---RAKLwsknVCP-----PHVLVMTATpI--P 429
Cdd:COG1205 156 VLTNpdmlhYGLLPHHTRwarfFRNLRYVVIDEAHTyrgvFGshVANvlrRLRR----ICRhygsdPQFILASAT-IgnP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 430 RTLAMTLYGdLDVSVIDEL--PPGRK------PIQTIhqfDNRRASLYAS----IRKQIEEGRQiYIVY-PLIKESEKMd 496
Cdd:COG1205 231 AEHAERLTG-RPVTVVDEDgsPRGERtfvlwnPPLVD---DGIRRSALAEaarlLADLVREGLR-TLVFtRSRRGAELL- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 497 IKNLEEgyELICAEFPDcQVSKVHGKMKPAE-KDAEmQRFVSGETQIMVATTVIEVGVNVPN--ASVMVienaerfG--- 570
Cdd:COG1205 305 ARYARR--ALREPDLAD-RVAAYRAGYLPEErREIE-RGLRSGELLGVVSTNALELGIDIGGldAVVLA-------Gypg 373
|
330 340
....*....|....*....|....
gi 492427108 571 -LSQLHQLRGRVGRGADQSYCILV 593
Cdd:COG1205 374 tRASFWQQAGRAGRRGQDSLVVLV 397
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
299-398 |
1.02e-07 |
|
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: 52.59 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSMLIAL-----DNGYQACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGSVKGKKREKILKDLltgDVQ 373
Cdd:cd17957 37 GSGKTLAFLIPILQKLgkprkKKGLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSIT---KYD 113
|
90 100 110
....*....|....*....|....*....|
gi 492427108 374 ILIGT-----HAVLEDTVGFSSLGMVIIDE 398
Cdd:cd17957 114 ILVSTplrlvFLLKQGPIDLSSVEYLVLDE 143
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
267-428 |
1.08e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 51.90 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 267 FELTGAQKRVIKEIRKDMGSGRQmNRLLQGDVGSGKTLVALMSMLIALDNGYQ--ACMMAPTEILAAQHYETIRKFLFGM 344
Cdd:pfam04851 2 LELRPYQIEAIENLLESIKNGQK-RGLIVMATGSGKTLTAAKLIARLFKKGPIkkVLFLVPRKDLLEQALEEFKKFLPNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 345 DVRVELLMGsvKGKKREKILKDLLTGDVQILIGTHAVLEDTVGFSSLGMVIIDEQHRFGvaqrAKLWSK---NVCPPHVL 421
Cdd:pfam04851 81 VEIGEIISG--DKKDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAHRSG----ASSYRNileYFKPAFLL 154
|
....*..
gi 492427108 422 VMTATPI 428
Cdd:pfam04851 155 GLTATPE 161
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
539-594 |
1.20e-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: 49.24 E-value: 1.20e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 492427108 539 ETQIMVATTVIEVGVNVPNASVMVIENAERFgLSQLHQLRGRVGRGA-DQSYCILVT 594
Cdd:cd18785 22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSS-AASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
255-382 |
1.43e-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: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 255 EIFNTFYSQNLPFELTGAQKRVIKeirkdmgsgrqmnRLLQGD-------VGSGKTLVALMSMLIALDNGYQACMMAPTE 327
Cdd:cd17924 4 EDFEEFFKKKTGFPPWGAQRTWAK-------------RLLRGKsfaiiapTGVGKTTFGLATSLYLASKGKRSYLIFPTK 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 492427108 328 ILAAQHYETIRKFLFGMDVRVELLM--GSVKGKKREKILKDLLTGDVQILIGTHAVL 382
Cdd:cd17924 71 SLVKQAYERLSKYAEKAGVEVKILVyhSRLKKKEKEELLEKIEKGDFDILVTTNQFL 127
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
297-428 |
2.71e-07 |
|
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: 51.50 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 297 DVGSGKTLVALMSMLIALD-------NGYQACMMAPTEILAAQHYETIRKFLfgmDVRVELLMGSVKGKKREKILKDLLT 369
Cdd:cd18034 24 PTGSGKTLIAVMLIKEMGElnrkeknPKKRAVFLVPTVPLVAQQAEAIRSHT---DLKVGEYSGEMGVDKWTKERWKEEL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492427108 370 GDVQILIGTHAVLEDTV--GF---SSLGMVIIDEQHRFG-------VAQR--AKLWSKNVcpPHVLVMTATPI 428
Cdd:cd18034 101 EKYDVLVMTAQILLDALrhGFlslSDINLLIFDECHHATgdhpyarIMKEfyHLEGRTSR--PRILGLTASPV 171
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
299-402 |
2.89e-07 |
|
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: 51.42 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTL---VALMSMLIAL-----DNGYQACMMAPTEILAAQHYETIRKFL--FGMDVRVELLMGsvkGKKREKILKDLL 368
Cdd:cd17960 37 GSGKTLaflIPVLEILLKRkanlkKGQVGALIISPTRELATQIYEVLQSFLehHLPKLKCQLLIG---GTNVEEDVKKFK 113
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 492427108 369 TGDVQILIGTHAVLED-------TVGFSSLGMVIIDEQHRF 402
Cdd:cd17960 114 RNGPNILVGTPGRLEEllsrkadKVKVKSLEVLVLDEADRL 154
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
394-607 |
1.49e-06 |
|
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: 50.89 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 394 VIIDEQHRFGVAQRAKLWS-----KNVCPPHvLVMTATpIPRTLaMTLYGDLDVsVIDELPPGRKPI--QTIHQFDNRRA 466
Cdd:cd09639 127 LIFDEVHFYDEYTLALILAvlevlKDNDVPI-LLMSAT-LPKFL-KEYAEKIGY-VEENEPLDLKPNerAPFIKIESDKV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 467 SLYASIRKQIE---EGRQIYIVYPLIKESEkmdiknleEGYELICAEFPDCQVSKVHGKMKP---AEKDAE-MQRFVSGE 539
Cdd:cd09639 203 GEISSLERLLEfikKGGSVAIIVNTVDRAQ--------EFYQQLKEKGPEEEIMLIHSRFTEkdrAKKEAElLLEFKKSE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 540 TQIMVATTVIEVGVNVpNASVMVIENAErfgLSQLHQLRGRVGR-GADQSYCILVTT------------YKLTEETRKRL 606
Cdd:cd09639 275 KFVIVATQVIEASLDI-SVDVMITELAP---IDSLIQRLGRLHRyGEKNGEEVYIITdapdgkgqkpypYDLVERTIELL 350
|
.
gi 492427108 607 E 607
Cdd:cd09639 351 E 351
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
394-607 |
1.98e-06 |
|
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: 50.53 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 394 VIIDEQHRFGVAQRAKLWS-----KNVCPPHvLVMTATpIPRTLaMTLYGDLDVSVIDELPP----GRKPIQTIHQFDNR 464
Cdd:TIGR01587 128 LIFDEVHFYDEYTLALILAvlevlKDNDVPI-LLMSAT-LPKFL-KEYAEKIGYVEFNEPLDlkeeRRFENHRFILIESD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 465 RASLYASIRKQIE---EGRQIYIVYPLIKESEkmdiknleEGYELICAEFPDCQVSKVHGKMKP---AEKDAEMQR--FV 536
Cdd:TIGR01587 205 KVGEISSLERLLEfikKGGSIAIIVNTVDRAQ--------EFYQQLKEKAPEEEIILYHSRFTEkdrAKKEAELLRemKK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 537 SGETQIMVATTVIEVGVNVpNASVMVIENA------ERFGlsQLHQLRGRVGRGAD-------QSYCILVTTYKLTEETR 603
Cdd:TIGR01587 277 SNEKFVIVATQVIEASLDI-SADVMITELApidsliQRLG--RLHRYGRKIGENFEvyiitiaPEGKLFPYPYELVERTI 353
|
....
gi 492427108 604 KRLE 607
Cdd:TIGR01587 354 QKLE 357
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
263-398 |
5.80e-06 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 47.96 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 263 QNLPFE-LTGAQKRVIKEIrkdMGSGRQMnrLLQGDVGSGKTLVALMSMLIALDNGY--------QACMMAPTEILAAQH 333
Cdd:cd17964 10 TRMGFEtMTPVQQKTLKPI---LSTGDDV--LARAKTGTGKTLAFLLPAIQSLLNTKpagrrsgvSALIISPTRELALQI 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492427108 334 YETIRKFLFGM-DVRVELLMGsvkGKKREKILKDLLTGDVQILIGTH----AVLEDTVG---FSSLGMVIIDE 398
Cdd:cd17964 85 AAEAKKLLQGLrKLRVQSAVG---GTSRRAELNRLRRGRPDILVATPgrliDHLENPGVakaFTDLDYLVLDE 154
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
280-407 |
6.25e-06 |
|
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: 46.94 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 280 IRKDMGSGRqmNRLLQGDVGSGKTLVALMSMLIALDNGYQACMMAPTEILAAQHYETIRKFlFGMDVRVELlmgSVkGKK 359
Cdd:cd18028 10 VRAGLLKGE--NLLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKKL-EEIGLKVGI---ST-GDY 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 492427108 360 REkilKDLLTGDVQILIGTHAVLEDTVGFSS-----LGMVIIDEQHRFGVAQR 407
Cdd:cd18028 83 DE---DDEWLGDYDIIVATYEKFDSLLRHSPswlrdVGVVVVDEIHLISDEER 132
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
297-429 |
1.97e-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: 45.63 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 297 DVGSGKTL--VALMSMLIALDNG-YQACMMAPTEILaaQHYET-IRKFLfgMDVRVELLMGSVKGKKREKILKDLLTGDV 372
Cdd:cd17919 27 EMGLGKTLqaIAFLAYLLKEGKErGPVLVVCPLSVL--ENWEReFEKWT--PDLRVVVYHGSQRERAQIRAKEKLDKFDV 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492427108 373 qILIGTHAVLEDTVGFSSL--GMVIIDEQHRF--GVAQRAKlWSKNVCPPHVLVMTATPIP 429
Cdd:cd17919 103 -VLTTYETLRRDKASLRKFrwDLVVVDEAHRLknPKSQLSK-ALKALRAKRRLLLTGTPLQ 161
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
294-401 |
4.23e-05 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 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: 350699 [Multi-domain] Cd Length: 198 Bit Score: 44.97 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 294 LQG-DV------GSGKTLVALMSMLIAL-------DNGYQACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGsvkGK- 358
Cdd:cd17941 25 LQGrDIlgaaktGSGKTLAFLVPLLEKLyrerwtpEDGLGALIISPTRELAMQIFEVLRKVGKYHSFSAGLIIG---GKd 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 492427108 359 ---KREKIlkdlltGDVQILIGT------HavLEDTVGF--SSLGMVIIDEQHR 401
Cdd:cd17941 102 vkeEKERI------NRMNILVCTpgrllqH--MDETPGFdtSNLQMLVLDEADR 147
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
293-398 |
7.13e-05 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 45.91 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 293 LLQG-DV------GSGKT---LVALMSMLIALDNGY-QACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGSVKGKKRE 361
Cdd:COG0513 36 ILAGrDVlgqaqtGTGKTaafLLPLLQRLDPSRPRApQALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQI 115
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 492427108 362 KILKDlltGdVQILIGTHAVLED-----TVGFSSLGMVIIDE 398
Cdd:COG0513 116 RALKR---G-VDIVVATPGRLLDliergALDLSGVETLVLDE 153
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
296-402 |
7.65e-05 |
|
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: 44.23 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 296 GDV------GSGKTLVALMSMLIALdngyQACMMAPTEILAAQHYETIRKFLFGMD---VRVELLMGSVKGKKREKILKD 366
Cdd:cd17938 37 GDVlmaaetGSGKTGAFCLPVLQIV----VALILEPSRELAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLES 112
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 492427108 367 lltgDVQILIGTHAVLEDTVG-----FSSLGMVIIDEQHRF 402
Cdd:cd17938 113 ----GVDIVVGTPGRLEDLIKtgkldLSSVRFFVLDEADRL 149
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
299-384 |
1.18e-04 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 43.85 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSMLIAL-----------DNGYQACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGsvkGKKREKILKDL 367
Cdd:cd17945 37 GSGKTAAFLIPLLVYIsrlppldeetkDDGPYALILAPTRELAQQIEEETQKFAKPLGIRVVSIVG---GHSIEEQAFSL 113
|
90
....*....|....*..
gi 492427108 368 LTGdVQILIGTHAVLED 384
Cdd:cd17945 114 RNG-CEILIATPGRLLD 129
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
299-427 |
1.87e-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: 42.29 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVAlmsMLIALDNGYQACM-MAPTEILAAQHYETIRKflFGMDVRVELLMGsvkGKKREKILKDLLTGDVQILIG 377
Cdd:cd17926 28 GSGKTLTA---LALIAYLKELRTLiVVPTDALLDQWKERFED--FLGDSSIGLIGG---GKKKDFDDANVVVATYQSLSN 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 492427108 378 THAVLEDtvGFSSLGMVIIDEQHRFGvaqrAKLWS---KNVCPPHVLVMTATP 427
Cdd:cd17926 100 LAEEEKD--LFDQFGLLIVDEAHHLP----AKTFSeilKELNAKYRLGLTATP 146
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
520-592 |
1.92e-04 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 41.81 E-value: 1.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492427108 520 HGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPNASvMVIEnaerFGLSQ----LHQLRGRVGRGADQSYCIL 592
Cdd:cd18794 61 HAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVR-FVIH----YSLPKsmesYYQESGRAGRDGLPSECIL 132
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
273-402 |
2.13e-04 |
|
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: 43.39 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 273 QKRVIKEIRKDMGSGRQmnrLLQGDV------GSGKTLVALMSMLIALDNG----YQACMMAPTEILAAQHYETIRKFLF 342
Cdd:cd17956 17 QAAVIPWLLPSSKSTPP---YRPGDLcvsaptGSGKTLAYVLPIVQALSKRvvprLRALIVVPTKELVQQVYKVFESLCK 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492427108 343 GMDVRVELLMGSVKGKKREKILKDLLTGD----VQILIGT------HavLEDTVGFS--SLGMVIIDEQHRF 402
Cdd:cd17956 94 GTGLKVVSLSGQKSFKKEQKLLLVDTSGRylsrVDILVATpgrlvdH--LNSTPGFTlkHLRFLVIDEADRL 163
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
290-398 |
2.94e-04 |
|
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: 42.56 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 290 MNRLLQGDVGSGKTLVALMSML--IALDNGY-QACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGSVKGKKREKIlkd 366
Cdd:cd17963 34 ENLIAQSQSGTGKTAAFVLAMLsrVDPTLKSpQALCLAPTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKI--- 110
|
90 100 110
....*....|....*....|....*....|....*..
gi 492427108 367 lltgDVQILIGTHAVLEDTVGF-----SSLGMVIIDE 398
Cdd:cd17963 111 ----TAQIVIGTPGTVLDWLKKrqldlKKIKILVLDE 143
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
273-398 |
3.66e-04 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins 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: 350697 [Multi-domain] Cd Length: 199 Bit Score: 42.31 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 273 QKRVIKEIRKdmgsGRQMnrLLQGDVGSGKTLVALMSMLIALDNGY---QACMMAPTEILAAQHYETIRKFLFGMDVRVE 349
Cdd:cd17939 24 QQRAIVPIIK----GRDV--IAQAQSGTGKTATFSIGALQRIDTTVretQALVLAPTRELAQQIQKVVKALGDYMGVKVH 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 492427108 350 LLMGSVKGKKREKILKDlltgDVQILIGTHAVLEDTVGFSSLG-----MVIIDE 398
Cdd:cd17939 98 ACIGGTSVREDRRKLQY----GPHIVVGTPGRVFDMLQRRSLRtdkikMFVLDE 147
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
299-624 |
3.72e-04 |
|
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: 43.53 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSMLiALDNGYQACMM---APTEILAAQHYETIRKfLFGMDVRV----------ELLMGSVKGKKREKILK 365
Cdd:COG1203 157 GGGKTEAALLFAL-RLAAKHGGRRIiyaLPFTSIINQTYDRLRD-LFGEDVLLhhsladldllEEEEEYESEARWLKLLK 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 366 DLLtgDVQILIGTH----AVLEDTVGFSSLGM-------VIIDE------------------QHRFGVaqraklwsknvc 416
Cdd:COG1203 235 ELW--DAPVVVTTIdqlfESLFSNRKGQERRLhnlansvIILDEvqayppymlalllrllewLKNLGG------------ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 417 ppHVLVMTATpIPRTLAMTLYGDLDVsvIDELPPgrKPIQTIHQFDNRR----------ASLYASIRKQIEEGRQIYIVY 486
Cdd:COG1203 301 --SVILMTAT-LPPLLREELLEAYEL--IPDEPE--ELPEYFRAFVRKRvelkegplsdEELAELILEALHKGKSVLVIV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 487 PLIKESEKMdiknleegYELICAEFPDCQVSKVHGKMKPA---EKDAEM-QRFVSGETQIMVATTVIEVGVNVpNASVMV 562
Cdd:COG1203 374 NTVKDAQEL--------YEALKEKLPDEEVYLLHSRFCPAdrsEIEKEIkERLERGKPCILVSTQVVEAGVDI-DFDVVI 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492427108 563 IENAerfGLSQLHQLRGRV---GRGADQSYCILvttYKLTEETRKRleimVQTNDGFEIAEADLK 624
Cdd:COG1203 445 RDLA---PLDSLIQRAGRCnrhGRKEEEGNVYV---FDPEDEGGGY----VYDKPLLERTRELLR 499
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
288-428 |
5.40e-04 |
|
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: 41.89 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 288 RQMNRLLQGD-VGSGKTLVALMSM--LIALDNGYQACMMAPTeILAAQ-HYETIRKFLfgmdVRVELLMGSVKGKKREKI 363
Cdd:cd18011 15 KPPVRLLLADeVGLGKTIEAGLIIkeLLLRGDAKRVLILCPA-SLVEQwQDELQDKFG----LPFLILDRETAAQLRRLI 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492427108 364 LKDLLTGDVQI----LIGTHAVLEDTVGFSSLGMVIIDEQHRFGVA------QRAKLwSKNVCP--PHVLVMTATPI 428
Cdd:cd18011 90 GNPFEEFPIVIvsldLLKRSEERRGLLLSEEWDLVVVDEAHKLRNSgggketKRYKL-GRLLAKraRHVLLLTATPH 165
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
297-429 |
6.48e-04 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 42.90 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 297 DVGSGKTLVALMSMLIALDNGYQACMM--APTeILAAQHYETIRKFLFGMDVRVelLMGSvkgKKREKILKDLltGDVQI 374
Cdd:COG0553 268 DMGLGKTIQALALLLELKERGLARPVLivAPT-SLVGNWQRELAKFAPGLRVLV--LDGT---RERAKGANPF--EDADL 339
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492427108 375 LIGTHAVL---EDTVGFSSLGMVIIDEqhrfgvAQRAKLWS-------KNVCPPHVLVMTATPIP 429
Cdd:COG0553 340 VITSYGLLrrdIELLAAVDWDLVILDE------AQHIKNPAtkrakavRALKARHRLALTGTPVE 398
|
|
| DEAD-like_helicase_N |
cd17912 |
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ... |
291-340 |
7.68e-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: 38.65 E-value: 7.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 492427108 291 NRLLQGDVGSGKTLVALMSMLIALDNGYQACMMAPTEILAAQHYETIRKF 340
Cdd:cd17912 1 NILHLGPTGSGKTLVAIQKIASAMSSGKSVLVVTPTKLLAHEILIVIDEI 50
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
266-432 |
7.82e-04 |
|
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: 41.10 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 266 PFELTGAQKRVIKEIRkdmgsgRQMNRLLQGDVGSGKTLVALMSMLIALDNGYQACMMAPTEILAAQHYETIRKfLFGmD 345
Cdd:cd18027 6 PFELDVFQKQAILHLE------AGDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFKN-TFG-D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 346 VrvellmgsvkgkkrekilkDLLTGDVQI------LIGTHAVLEDTVGFSS-----LGMVIIDEQHRFGVAQRAKLWSKN 414
Cdd:cd18027 78 V-------------------GLITGDVQLnpeascLIMTTEILRSMLYNGSdvirdLEWVIFDEVHYINDAERGVVWEEV 138
|
170 180
....*....|....*....|.
gi 492427108 415 VC--PPHV-LVMTATPIPRTL 432
Cdd:cd18027 139 LImlPDHVsIILLSATVPNTV 159
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
299-401 |
7.86e-04 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 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: 350712 [Multi-domain] Cd Length: 203 Bit Score: 41.15 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSMLIALDN---GYQACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGSVkgkkrekilkDLLTGDVQ-- 373
Cdd:cd17954 47 GSGKTAAFALPILQALLEnpqRFFALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGM----------DMMAQAIAla 116
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 492427108 374 ----ILIGT------HavLEDTVGFS--SLGMVIIDEQHR 401
Cdd:cd17954 117 kkphVIVATpgrlvdH--LENTKGFSlkSLKFLVMDEADR 154
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
532-594 |
8.07e-04 |
|
C-terminal helicase domain of the 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. Dicer exists throughout eukaryotes, and a subset has 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 helicase domains 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: 350189 [Multi-domain] Cd Length: 142 Bit Score: 40.27 E-value: 8.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492427108 532 MQRFVSGETQIMVATTVIEVGVNVPNASVMVienaeRFGLS----QLHQLRGRvGRgADQSYCILVT 594
Cdd:cd18802 83 LDKFRDGELNLLIATSVLEEGIDVPACNLVI-----RFDLPktlrSYIQSRGR-AR-APNSKYILMV 142
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
299-427 |
8.79e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 41.26 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSMLIALD-----NGYQACMMAPTEILAAQHYETIRKFLFGMDVRVellmGSVKGKKREKILKDLLTGDVQ 373
Cdd:cd17927 27 GSGKTFVAVLICEHHLKkfpagRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKV----TGLSGDTSENVSVEQIVESSD 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492427108 374 ILIGTHAVLED------TVGFSSLGMVIIDEQHRfgvAQ-------------RAKLWSKNVCpPHVLVMTATP 427
Cdd:cd17927 103 VIIVTPQILVNdlksgtIVSLSDFSLLVFDECHN---TTknhpyneimfrylDQKLGSSGPL-PQILGLTASP 171
|
|
| DEXHc_UvrB |
cd17916 |
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ... |
266-341 |
1.37e-03 |
|
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II) and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA, but its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a member of the DEAD-like 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: 350674 [Multi-domain] Cd Length: 299 Bit Score: 41.43 E-value: 1.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492427108 266 PFELTGAQKRVIKEIRKDMGSGRQMNRLLqGDVGSGKTLValMSMLIAlDNGYQACMMAPTEILAAQHYETIRKFL 341
Cdd:cd17916 6 PFKPAGDQPQAIAKLVEGLKRGVKFQTLL-GVTGSGKTFT--IANVIA-QVNKPTLVIAHNKTLAAQLYSEFKEFF 77
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
299-432 |
1.69e-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: 40.44 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSML--------IALDNGYQACMMAPTEILAAQHYETIRKFLFGMDVRVELLMGsvkGKKREKILKDLLTG 370
Cdd:cd17953 59 GSGKTLAFLLPMFrhikdqrpVKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYG---GSGISEQIAELKRG 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492427108 371 dVQILIGTHAVLEDTVGFSS--------LGMVIIDEQHR---FGVAQRAKLWSKNVCPPHVLVMTATPIPRTL 432
Cdd:cd17953 136 -AEIVVCTPGRMIDILTANNgrvtnlrrVTYVVLDEADRmfdMGFEPQIMKIVNNIRPDRQTVLFSATFPRKV 207
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
520-596 |
1.71e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 41.81 E-value: 1.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492427108 520 HGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPNASvMVIENAERFGLSQLHQLRGRVGRGADQSYCILVTTY 596
Cdd:PLN03137 711 HGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVR-FVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSY 786
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
299-426 |
2.50e-03 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350810 [Multi-domain] Cd Length: 264 Bit Score: 40.34 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSMLIAL-DNGY-----------QACMMAPTEILAAQHYETIRKFLFGMDVRVELLMG--SVKGKKREkil 364
Cdd:cd18052 90 GSGKTAAFLLPVLTGMmKEGLtassfsevqepQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGgvSVGHQIRQ--- 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492427108 365 kdlLTGDVQILIGTHAVLED-----TVGFSSLGMVIIDEQHR-----FGVAQRaKLWSKNVCPP----HVLVMTAT 426
Cdd:cd18052 167 ---IEKGCHILVATPGRLLDfigrgKISLSKLKYLILDEADRmldmgFGPEIR-KLVSEPGMPSkedrQTLMFSAT 238
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
516-583 |
2.92e-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: 38.26 E-value: 2.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492427108 516 VSKVHGKMKPAEKDAEMQRFVSGETQIMVATTVIEVGVNVPNASVmVI-----ENAERFglsqLHqlR-GRVGR 583
Cdd:cd18787 54 VAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVDH-VInydlpRDAEDY----VH--RiGRTGR 120
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
262-401 |
3.47e-03 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 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: 350707 [Multi-domain] Cd Length: 214 Bit Score: 39.49 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 262 SQNLPFE-LTGAQKRVIKEIRKdmgsGRqmNRLLQGDVGSGKTL---VALMSMLIALDN------GYQACMMAPTEILAA 331
Cdd:cd17949 6 KSKMGIEkPTAIQKLAIPVLLQ----GR--DVLVRSQTGSGKTLaylLPIIQRLLSLEPrvdrsdGTLALVLVPTRELAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 332 QHYETIRKFL--FGMDVrVELLMGSVKgKKREKilKDLLTGdVQILIGT------HavLEDTVGF--SSLGMVIIDEQHR 401
Cdd:cd17949 80 QIYEVLEKLLkpFHWIV-PGYLIGGEK-RKSEK--ARLRKG-VNILIATpgrlldH--LKNTQSFdvSNLRWLVLDEADR 152
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
299-402 |
5.16e-03 |
|
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: 38.33 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492427108 299 GSGKTLVALMSMLIAL----DNGYQACMMAPTEILAAQHYETIRKFL--FGMDVRVELLMGSVKGKKREKILKDLltgdV 372
Cdd:cd17922 11 GSGKTEAAFLPALSSLadepEKGVQVLYISPLKALINDQERRLEEPLdeIDLEIPVAVRHGDTSQSEKAKQLKNP----P 86
|
90 100 110
....*....|....*....|....*....|....*..
gi 492427108 373 QILIGT----HAVLEDTVG---FSSLGMVIIDEQHRF 402
Cdd:cd17922 87 GILITTpeslELLLVNKKLrelFAGLRYVVVDEIHAL 123
|
|
| |
