|
Name |
Accession |
Description |
Interval |
E-value |
| recG |
TIGR00643 |
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair] |
238-942 |
0e+00 |
|
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273192 [Multi-domain] Cd Length: 630 Bit Score: 859.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 238 CGFHTMKKLLHHFPRTYadlqnaqvdiEDGQYLIFVGKVLSskGVRASSSFSFLEVIvscevsgrdrtpedlSHNAEDKA 317
Cdd:TIGR00643 1 LGIHTVQDLLFYFPRRY----------EDRTLLQTIGELLP--GERATIVGEVLSHC---------------IFGFKRRK 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 318 GKSIFLHLKkFFRGTRFTWQPfLNSIQEKHKVGDLVCISGKVKSLRAEDhfemreynidVLKDEEESSHRAQG----RPY 393
Cdd:TIGR00643 54 VLKLRLKDG-GYKKLELRFFN-RAFLKKKFKVGSKVVVYGKVKSSKFKA----------YLIHPEFISEKDGVefelKIL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 394 PIYPSKGGLNPKFLSDVISRALRVLPA-NMDPIPKEITKVFGLPSLNDAYVGIHEPKTLDEADLARKRLIFDEFFYLQLA 472
Cdd:TIGR00643 122 PVYPLTEGLTQKKLRKLIQQALDQLDKsLEDPLPEELREKYGLLSLEDALRAIHFPKTLSLLELARRRLIFDEFFYLQLA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 473 RLYQMLQslgtkiekdvlleKFRKPVLNSVYIEEwSTLTKsFLKALPYSLTPSQLSAVSEIIWDLKRPVPMNRLLQGDVG 552
Cdd:TIGR00643 202 MLARRLG-------------EKQQFSAPPANPSE-ELLTK-FLASLPFKLTRAQKRVVKEILQDLKSDVPMNRLLQGDVG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 553 CGKTVVAFLACMEVIGSGYQAAFMAPTELLAIQHYEQCRDLLENMeGVSskptIGLLTGSTPAKQSRMIRQDLQSGAISF 632
Cdd:TIGR00643 267 SGKTLVAALAMLAAIEAGYQVALMAPTEILAEQHYNSLRNLLAPL-GIE----VALLTGSLKGKRRKELLETIASGQIHL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 633 IIGTHSLIAEKIEYSALRIAVVDEQQRFGVIQRGKFNSKLYGTsmisksgssdsddtskadlsMAPHVLAMSATPIPRSL 712
Cdd:TIGR00643 342 VVGTHALIQEKVEFKRLALVIIDEQHRFGVEQRKKLREKGQGG--------------------FTPHVLVMSATPIPRTL 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 713 ALALYGDISLTQITGMPLGRIPVETHIFEGNETgiKEVYSMMLEDLKSGGRVYVVYPVIDQSEQLpQLRAASAELEIVTK 792
Cdd:TIGR00643 402 ALTVYGDLDTSIIDELPPGRKPITTVLIKHDEK--DIVYEFIEEEIAKGRQAYVVYPLIEESEKL-DLKAAEALYERLKK 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 793 KFPKYNCGLLHGRMKSDDKEEALNKFRSGETQILLSTQVIEIGVDVPDASMMVVMNAERFGIAQLHQLRGRVGRGTRKSK 872
Cdd:TIGR00643 479 AFPKYNVGLLHGRMKSDEKEAVMEEFREGEVDILVATTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSY 558
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186498546 873 CLLVG---SSTNSLKRLNMLGKSSDGFYLANIDLLLRGPGDLLGKKQSGhLPEFPVARLEIDGNMLQEAHIAA 942
Cdd:TIGR00643 559 CLLVYknpKSESAKKRLRVMADTLDGFVIAEEDLELRGPGDLLGTKQSG-YPEFRVADLVRDREILVEAREDA 630
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
217-965 |
0e+00 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 729.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 217 LATSIDSMPGLSKRHSNQLDSCGFHTMKKLLHHFPRTYADLQNaQVDI---EDGQYLIFVGKVLSSKGVRASSSFSFLEV 293
Cdd:COG1200 4 LDTPLTYLKGVGPKRAKLLAKLGIRTVGDLLFHLPRRYEDRTR-LTPIaelRPGETVTVEGTVVSVEVVRRRRRRRILEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 294 IVScevsgrdrtpedlshnaeDKAGksiFLHLKkFFRgtrftwQPFLnsiQEKHKVGDLVCISGKVKSLRAEdhFEMreY 373
Cdd:COG1200 83 TLS------------------DGTG---SLTLV-FFN------QPYL---KKQLKPGTRVLVSGKVERFRGG--LQM--V 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 374 NIDVLKDEEESSHRAqGRPYPIYPSKGGLNPKFLSDVISRALRVLPANM-DPIPKEITKVFGLPSLNDAYVGIHEPKTLD 452
Cdd:COG1200 128 HPEYELLDEEEAELA-GRLTPVYPLTEGLSQKTLRKLIRQALDLLAPDLpEPLPEELRARYGLPSLAEALRNIHFPPSDE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 453 EADLARKRLIFDEFFYLQLARLYQMLQslgtkiekdvlLEKFRKPVLNSVyieewSTLTKSFLKALPYSLTPSQLSAVSE 532
Cdd:COG1200 207 DLHPARRRLAFEELLALQLALLLRRAR-----------RRKRKGPALPGD-----GELLEAFLAALPFELTGAQKRVIAE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 533 IIWDLKRPVPMNRLLQGDVGCGKTVVAFLACMEVIGSGYQAAFMAPTELLAIQHYEQCRDLLENMeGVSskptIGLLTGS 612
Cdd:COG1200 271 IAADLASPHPMNRLLQGDVGSGKTVVALLAMLAAVEAGYQAALMAPTEILAEQHYRSLSKLLEPL-GIR----VALLTGS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 613 TPAKQSRMIRQDLQSGAISFIIGTHSLIAEKIEYSALRIAVVDEQQRFGVIQRGKFNSKlygtsmisksgssdsddtska 692
Cdd:COG1200 346 TKAKERREILAALASGEADIVVGTHALIQDDVEFKNLGLVVIDEQHRFGVEQRLALREK--------------------- 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 693 dlSMAPHVLAMSATPIPRSLALALYGDISLTQITGMPLGRIPVETHIFegNETGIKEVYSMMLEDLKSGGRVYVVYPVID 772
Cdd:COG1200 405 --GEAPHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPIKTRVV--PEERRDEVYERIREEIAKGRQAYVVCPLIE 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 773 QSEQLpQLRAASAELEIVTKKFPKYNCGLLHGRMKSDDKEEALNKFRSGETQILLSTQVIEIGVDVPDASMMVVMNAERF 852
Cdd:COG1200 481 ESEKL-DLQAAEETYEELREAFPGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVMVIENAERF 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 853 GIAQLHQLRGRVGRGTRKSKCLLVGS---STNSLKRLNMLGKSSDGFYLANIDLLLRGPGDLLGKKQSGhLPEFPVARLE 929
Cdd:COG1200 560 GLSQLHQLRGRVGRGSAQSYCLLLYDaplSETARERLEVMRETNDGFEIAEEDLELRGPGEFLGTRQSG-LPDLRIADLV 638
|
730 740 750
....*....|....*....|....*....|....*.
gi 186498546 930 IDGNMLQEAHIAALNVLGDSHDLEKFPALKAELSMR 965
Cdd:COG1200 639 RDADLLEAAREDAEELLEEDPELASHPALRRWLGLR 674
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
212-954 |
0e+00 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 686.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 212 AAQRFLATSIDSMPGLSKRHSNQLDSCGFHTMKKLLHHFPRTYADLQNAQ--VDIEDGQYLIFVGKVLSSKGVRASSSFs 289
Cdd:PRK10917 2 SLLLLLDAPLTSLKGVGPKTAEKLAKLGIHTVQDLLLHLPRRYEDRTRLKpiAELRPGEKVTVEGEVLSAEVVFGKRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 290 fLEVIVScevsgrdrtpedlshnaeDKAGKsifLHLKKFFRGTRFtwqpflnsIQEKHKVGDLVCISGKVKslRAEDHFE 369
Cdd:PRK10917 81 -LTVTVS------------------DGTGN---LTLRFFNFNQPY--------LKKQLKVGKRVAVYGKVK--RGKYGLE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 370 MREYNIDVLKDEEESShraQGRPYPIYPSKGGLNPKFLSDVISRALRVLPANMDPIPKEITKVFGLPSLNDAYVGIHEPK 449
Cdd:PRK10917 129 MVHPEYEVLEEESPEL---EGRLTPVYPLTEGLKQKTLRKLIKQALELLDALPELLPEELLEKYGLLSLAEALRAIHFPP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 450 TLDEADLARKRLIFDEFFYLQLArlyqMLQslgtkieKDVLLEKFRKPVLNsvyieEWSTLTKSFLKALPYSLTPSQLSA 529
Cdd:PRK10917 206 SDEDLHPARRRLKFEELFALQLS----LLL-------LRAGRRSKKAGPLP-----YDGELLKKFLASLPFELTGAQKRV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 530 VSEIIWDLKRPVPMNRLLQGDVGCGKTVVAFLACMEVIGSGYQAAFMAPTELLAIQHYEQCRDLLENMeGVSskptIGLL 609
Cdd:PRK10917 270 VAEILADLASPKPMNRLLQGDVGSGKTVVAALAALAAIEAGYQAALMAPTEILAEQHYENLKKLLEPL-GIR----VALL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 610 TGSTPAKQSRMIRQDLQSGAISFIIGTHSLIAEKIEYSALRIAVVDEQQRFGVIQRGKFNSKlygtsmisksgssdsddt 689
Cdd:PRK10917 345 TGSLKGKERREILEAIASGEADIVIGTHALIQDDVEFHNLGLVIIDEQHRFGVEQRLALREK------------------ 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 690 skadlSMAPHVLAMSATPIPRSLALALYGDISLTQITGMPLGRIPVETHIFegNETGIKEVYSMMLEDLKSGGRVYVVYP 769
Cdd:PRK10917 407 -----GENPHVLVMTATPIPRTLAMTAYGDLDVSVIDELPPGRKPITTVVI--PDSRRDEVYERIREEIAKGRQAYVVCP 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 770 VIDQSEQLpQLRAASAELEIVTKKFPKYNCGLLHGRMKSDDKEEALNKFRSGETQILLSTQVIEIGVDVPDASMMVVMNA 849
Cdd:PRK10917 480 LIEESEKL-DLQSAEETYEELQEAFPELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVMVIENA 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 850 ERFGIAQLHQLRGRVGRGTRKSKCLLVGS---STNSLKRLNMLGKSSDGFYLANIDLLLRGPGDLLGKKQSGhLPEFPVA 926
Cdd:PRK10917 559 ERFGLAQLHQLRGRVGRGAAQSYCVLLYKdplSETARERLKIMRETNDGFVIAEKDLELRGPGELLGTRQSG-LPEFKVA 637
|
730 740
....*....|....*....|....*...
gi 186498546 927 RLEIDGNMLQEAHIAALNVLGDSHDLEK 954
Cdd:PRK10917 638 DLVRDEELLEEARKDARELLERDPELAE 665
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
461-729 |
2.04e-108 |
|
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: 334.89 E-value: 2.04e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 461 LIFDEFFYLQLARLYQMLQslgtkIEKdvllekfrkpvLNSVYIEEWSTLTKSFLKALPYSLTPSQLSAVSEIIWDLKRP 540
Cdd:cd17992 1 LAFEELFALQLALLLRRRK-----IEE-----------LKGIILEISGELLKKFLEALPFELTGAQKRVIDEILRDLASE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 541 VPMNRLLQGDVGCGKTVVAFLACMEVIGSGYQAAFMAPTELLAIQHYEQCRDLLENMegvssKPTIGLLTGSTPAKQSRM 620
Cdd:cd17992 65 KPMNRLLQGDVGSGKTVVAALAMLAAVENGYQVALMAPTEILAEQHYDSLKKLLEPL-----GIRVALLTGSTKAKEKRE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 621 IRQDLQSGAISFIIGTHSLIAEKIEYSALRIAVVDEQQRFGVIQRGKFNSKLYgtsmisksgssdsddtskadlsmAPHV 700
Cdd:cd17992 140 ILEKIASGEIDIVIGTHALIQEDVEFHNLGLVIIDEQHRFGVEQRLKLREKGE-----------------------TPHV 196
|
250 260
....*....|....*....|....*....
gi 186498546 701 LAMSATPIPRSLALALYGDISLTQITGMP 729
Cdd:cd17992 197 LVMTATPIPRTLALTLYGDLDVSIIDELP 225
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
514-943 |
5.67e-94 |
|
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: 318.53 E-value: 5.67e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 514 FLKALPYSLTPSQLSAVSEIIWDLKRPVPMNRLLQGDVGCGKTVVAFLACMEVIGSGYQAAFMAPTELLAIQHYEQCRDL 593
Cdd:TIGR00580 444 FEDSFPFEETPDQLKAIEEIKADMESPRPMDRLVCGDVGFGKTEVAMRAAFKAVLDGKQVAVLVPTTLLAQQHFETFKER 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 594 LENMeGVsskpTIGLLTGSTPAKQSRMIRQDLQSGAISFIIGTHSLIAEKIEYSALRIAVVDEQQRFGVIQRGKFNSkly 673
Cdd:TIGR00580 524 FANF-PV----TIELLSRFRSAKEQNEILKELASGKIDILIGTHKLLQKDVKFKDLGLLIIDEEQRFGVKQKEKLKE--- 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 674 gtsmisksgssdsddtskadLSMAPHVLAMSATPIPRSLALALYG--DISLtqITGMPLGRIPVETHIFEGNETGIKEVy 751
Cdd:TIGR00580 596 --------------------LRTSVDVLTLSATPIPRTLHMSMSGirDLSI--IATPPEDRLPVRTFVMEYDPELVREA- 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 752 smMLEDLKSGGRVYVVYPVIDQSEQLP-QLRAASAELEIvtkkfpkyncGLLHGRMKSDDKEEALNKFRSGETQILLSTQ 830
Cdd:TIGR00580 653 --IRRELLRGGQVFYVHNRIESIEKLAtQLRELVPEARI----------AIAHGQMTENELEEVMLEFYKGEFQVLVCTT 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 831 VIEIGVDVPDASMMVVMNAERFGIAQLHQLRGRVGRGTRKSKC-LLVGS----STNSLKRLNMLGKSSD---GFYLANID 902
Cdd:TIGR00580 721 IIETGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKKKAYAyLLYPHqkalTEDAQKRLEAIQEFSElgaGFKIALHD 800
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 186498546 903 LLLRGPGDLLGKKQSGHLPEFPvarLEIDGNMLQEAhIAAL 943
Cdd:TIGR00580 801 LEIRGAGNLLGEEQSGHIESIG---FDLYMELLEEA-IEEL 837
|
|
| Mfd |
COG1197 |
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ... |
519-943 |
9.94e-76 |
|
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription];
Pssm-ID: 440810 [Multi-domain] Cd Length: 1130 Bit Score: 270.40 E-value: 9.94e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 519 PYSLTPSQLSAVSEIIWDLKRPVPMNRLLQGDVGCGKTVVA----FLACMevigSGYQAAFMAPTELLAIQHYEQCRDLL 594
Cdd:COG1197 584 PYEETPDQLRAIEEVKADMESPRPMDRLVCGDVGFGKTEVAlraaFKAVM----DGKQVAVLVPTTLLAQQHYETFKERF 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 595 ENMegvsskP-TIGLLTGSTPAKQSRMIRQDLQSGAISFIIGTHSLIAEKIEYSALRIAVVDEQQRFGVIQRGKFnsKLY 673
Cdd:COG1197 660 AGF------PvRVEVLSRFRTAKEQKETLEGLADGKVDIVIGTHRLLSKDVKFKDLGLLIIDEEQRFGVRHKEKL--KAL 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 674 GTSMisksgssdsddtskadlsmapHVLAMSATPIPRSLALALYG--DISLtqITGMPLGRIPVETHIFEGNETGIKEVy 751
Cdd:COG1197 732 RANV---------------------DVLTLTATPIPRTLQMSLSGirDLSI--IATPPEDRLPVKTFVGEYDDALIREA- 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 752 smMLEDLKSGGRVYVVYP-V--IDQ-----SEQLPQLRAASAeleivtkkfpkyncgllHGRMKSDDKEEALNKFRSGET 823
Cdd:COG1197 788 --ILRELLRGGQVFYVHNrVedIEKvaarlQELVPEARIAVA-----------------HGQMSERELERVMLDFYEGEF 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 824 QILLSTQVIEIGVDVPDASMMVVMNAERFGIAQLHQLRGRVGRGTRKSKCLLV-----GSSTNSLKRLNMLGKSSD---G 895
Cdd:COG1197 849 DVLVCTTIIETGIDIPNANTIIIERADRFGLAQLYQLRGRVGRSHRRAYAYLLyppdkVLTEDAEKRLEAIQEFTElgaG 928
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 186498546 896 FYLANIDLLLRGPGDLLGKKQSGHlpefpvarleIDG-------NMLQEAhIAAL 943
Cdd:COG1197 929 FKLAMHDLEIRGAGNLLGEEQSGH----------IAEvgfdlylQMLEEA-VAAL 972
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
514-920 |
1.83e-58 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 218.85 E-value: 1.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 514 FLKALPYSLTPSQLSAVSEIIWDLKRPVPMNRLLQGDVGCGKTVVAFLACMEVIGSGYQAAFMAPTELLAIQHYEQCRDL 593
Cdd:PRK10689 593 FCDSFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQHYDNFRDR 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 594 LENMegvsskPT-IGLLTGSTPAKQSRMIRQDLQSGAISFIIGTHSLIAEKIEYSALRIAVVDEQQRFGViqRGKFNSKl 672
Cdd:PRK10689 673 FANW------PVrIEMLSRFRSAKEQTQILAEAAEGKIDILIGTHKLLQSDVKWKDLGLLIVDEEHRFGV--RHKERIK- 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 673 ygtsmisksgssdsddtskadlSMAPHV--LAMSATPIPRSLALALYGDISLTQITGMPLGRIPVETHIFEGNETGIKEV 750
Cdd:PRK10689 744 ----------------------AMRADVdiLTLTATPIPRTLNMAMSGMRDLSIIATPPARRLAVKTFVREYDSLVVREA 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 751 ysmMLEDLKSGGRVYVVYPVIDQSEqlpqlRAASAELEIVtkkfPKYNCGLLHGRMKSDDKEEALNKFRSGETQILLSTQ 830
Cdd:PRK10689 802 ---ILREILRGGQVYYLYNDVENIQ-----KAAERLAELV----PEARIAIGHGQMRERELERVMNDFHHQRFNVLVCTT 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 831 VIEIGVDVPDASMMVVMNAERFGIAQLHQLRGRVGRGTRKSKCLLV-----GSSTNSLKRLNMLGKSSD---GFYLANID 902
Cdd:PRK10689 870 IIETGIDIPTANTIIIERADHFGLAQLHQLRGRVGRSHHQAYAWLLtphpkAMTTDAQKRLEAIASLEDlgaGFALATHD 949
|
410
....*....|....*...
gi 186498546 903 LLLRGPGDLLGKKQSGHL 920
Cdd:PRK10689 950 LEIRGAGELLGEEQSGQM 967
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
734-891 |
1.13e-54 |
|
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: 186.78 E-value: 1.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 734 PVETH-IFEGNEtgiKEVYSMMLEDLKSGGRVYVVYPVIDQSEQLpQLRAASAELEIVTKKF-PKYNCGLLHGRMKSDDK 811
Cdd:cd18811 1 PITTYlIFHTRL---DKVYEFVREEIAKGRQAYVIYPLIEESEKL-DLKAAVAMYEYLKERFrPELNVGLLHGRLKSDEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 812 EEALNKFRSGETQILLSTQVIEIGVDVPDASMMVVMNAERFGIAQLHQLRGRVGRGTRKSKCLLVG---SSTNSLKRLNM 888
Cdd:cd18811 77 DAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYkdpLTETAKQRLRV 156
|
...
gi 186498546 889 LGK 891
Cdd:cd18811 157 MTE 159
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
514-722 |
2.78e-54 |
|
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: 187.01 E-value: 2.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 514 FLKALPYSLTPSQLSAVSEIIWDLKRPVPMNRLLQGDVGCGKTVVAFLACMEVIGSGYQAAFMAPTELLAIQHYEQCRDL 593
Cdd:cd17991 8 FEASFPYEETPDQLKAIEEILKDMESGKPMDRLICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQHYETFKER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 594 LENMeGVsskpTIGLLTGSTPAKQSRMIRQDLQSGAISFIIGTHSLIAEKIEYSALRIAVVDEQQRFGVIQRGKFnSKLY 673
Cdd:cd17991 88 FANF-PV----NVELLSRFTTAAEQREILEGLKEGKVDIVIGTHRLLSKDVEFKNLGLLIIDEEQRFGVKQKEKL-KELR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 186498546 674 GTSmisksgssdsddtskadlsmapHVLAMSATPIPRSLALALYG--DISL 722
Cdd:cd17991 162 PNV----------------------DVLTLSATPIPRTLHMALSGirDLSV 190
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
514-726 |
5.72e-54 |
|
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: 185.70 E-value: 5.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 514 FLKALPYSLTPSQLSAVSEIIWDLKRPVPMNRLLQGDVGCGKTVVAFLACMEVIGSGYQAAFMAPTELLAIQHYEQCRDL 593
Cdd:cd17918 8 LCKSLPFSLTKDQAQAIKDIEKDLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARKF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 594 LENMEgvsskptIGLLTGSTpakqsrmiRQDLQSGaISFIIGTHSLIAEKIEYSALRIAVVDEQQRFGVIQRGKFNSKly 673
Cdd:cd17918 88 LPFIN-------VELVTGGT--------KAQILSG-ISLLVGTHALLHLDVKFKNLDLVIVDEQHRFGVAQREALYNL-- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 186498546 674 gtsmisksgssdsddtskadlsMAPHVLAMSATPIPRSLALALYGDISLTQIT 726
Cdd:cd17918 150 ----------------------GATHFLEATATPIPRTLALALSGLLDLSVID 180
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
734-891 |
5.41e-51 |
|
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: 176.30 E-value: 5.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 734 PVETHIFEGNETgiKEVYSMMLEDLKSGGRVYVVYPVIDQSEQLpQLRAASAELEIVTKKFPKYNCGLLHGRMKSDDKEE 813
Cdd:cd18792 1 PIRTYVIPHDDL--DLVYEAIERELARGGQVYYVYPRIEESEKL-DLKSIEALAEELKELVPEARVALLHGKMTEDEKEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 814 ALNKFRSGETQILLSTQVIEIGVDVPDASMMVVMNAERFGIAQLHQLRGRVGRGTRKSKCLLV-----GSSTNSLKRLNM 888
Cdd:cd18792 78 VMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLypdpkKLTETAKKRLRA 157
|
...
gi 186498546 889 LGK 891
Cdd:cd18792 158 IAE 160
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
734-886 |
6.15e-30 |
|
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: 115.90 E-value: 6.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 734 PVETHIFEGNETGIKEVysmMLEDLKSGGRVYVVYPVIdqsEQLPQLRAASAELeivtkkFPKYNCGLLHGRMKSDDKEE 813
Cdd:cd18810 1 PVRTYVMPYDDELIREA---IERELLRGGQVFYVHNRI---ESIEKLATQLRQL------VPEARIAIAHGQMTENELEE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186498546 814 ALNKFRSGETQILLSTQVIEIGVDVPDASMMVVMNAERFGIAQLHQLRGRVGRGTRKSKC-LLVGSS----TNSLKRL 886
Cdd:cd18810 69 VMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKERAYAyFLYPDQkkltEDALKRL 146
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
755-866 |
4.64e-20 |
|
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: 86.11 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 755 LEDLKSGGRVYVVYPVIDQseqlpqlraasAELEIVTKKFpKYNCGLLHGRMKSDDKEEALNKFRSGETQILLSTQVIEI 834
Cdd:pfam00271 9 LLKKERGGKVLIFSQTKKT-----------LEAELLLEKE-GIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
|
90 100 110
....*....|....*....|....*....|..
gi 186498546 835 GVDVPDASMMVVMNAErFGIAQLHQLRGRVGR 866
Cdd:pfam00271 77 GLDLPDVDLVINYDLP-WNPASYIQRIGRAGR 107
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
788-866 |
8.68e-19 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 81.49 E-value: 8.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 788 EIVTKKFPK--YNCGLLHGRMKSDDKEEALNKFRSGETQILLSTQVIEIGVDVPDASMMVVMNAeRFGIAQLHQLRGRVG 865
Cdd:smart00490 1 EELAELLKElgIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL-PWSPASYIQRIGRAG 79
|
.
gi 186498546 866 R 866
Cdd:smart00490 80 R 80
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
514-736 |
1.84e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 84.85 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 514 FLKALPYSLTPSQLSAVSEIIWDLKrpvpmNRLLQGDVGCGKTVVAFLACMEVI--GSGYQAAFMAPTELLAIQHYEQCR 591
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLR-----DVILAAPTGSGKTLAALLPALEALkrGKGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 592 DLLENMEGVsskpTIGLLTGSTPAKQsrmiRQDLQSGAISFIIGT-----HSLIAEKIEYSALRIAVVDEQQRFGviqRG 666
Cdd:smart00487 76 KLGPSLGLK----VVGLYGGDSKREQ----LRKLESGKTDILVTTpgrllDLLENDKLSLSNVDLVILDEAHRLL---DG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186498546 667 KFNSKLYGtsmisksgssdsddtSKADLSMAPHVLAMSATP---IPRSLALALYGDISLTQITGmPLGRIPVE 736
Cdd:smart00487 145 GFGDQLEK---------------LLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFT-PLEPIEQF 201
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
523-666 |
3.16e-15 |
|
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: 74.20 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 523 TPSQLSAVSEIIwdLKRPVpmnrLLQGDVGCGKTVVAFLACMEVIG---SGYQAAFMAPTELLAIQHYEQCRDLLENMEg 599
Cdd:pfam00270 1 TPIQAEAIPAIL--EGRDV----LVQAPTGSGKTLAFLLPALEALDkldNGPQALVLAPTRELAEQIYEELKKLGKGLG- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186498546 600 vssKPTIGLLTGSTPAKQSRMIRQdlqsgaISFIIGTH----SLIAEKIEYSALRIAVVDEQQRFGVIQRG 666
Cdd:pfam00270 74 ---LKVASLLGGDSRKEQLEKLKG------PDILVGTPgrllDLLQERKLLKNLKLLVLDEAHRLLDMGFG 135
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
516-872 |
4.17e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 73.14 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 516 KALPYSLTPSQLSAVSEIIWDLKRPVPMNrLLQGDVGCGKTVVAfLACMEVIGSGYQAAFMAPTELLAIQHYEQCRDLLE 595
Cdd:COG1061 75 SGTSFELRPYQQEALEALLAALERGGGRG-LVVAPTGTGKTVLA-LALAAELLRGKRVLVLVPRRELLEQWAEELRRFLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 596 NMEGVSSKPTIGlltgstpakqsRMIrqdlqsgaisfIIGTHSLIAEKIEYSALR----IAVVDEQQRFGviqrgkfnSK 671
Cdd:COG1061 153 DPLAGGGKKDSD-----------API-----------TVATYQSLARRAHLDELGdrfgLVIIDEAHHAG--------AP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 672 LYGTSMisksgssdsddtskaDLSMAPHVLAMSATPI---PRSLALALYGDIsltqITGMPLGRI-------PVETHIFE 741
Cdd:COG1061 203 SYRRIL---------------EAFPAAYRLGLTATPFrsdGREILLFLFDGI----VYEYSLKEAiedgylaPPEYYGIR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 742 GNETGIKEVYSMMLEDLKS---GGRVYVVYPVIDQSEQLPQLRAA------SAELEIVTKKFPK--YNCGLLHGRMKSDD 810
Cdd:COG1061 264 VDLTDERAEYDALSERLREalaADAERKDKILRELLREHPDDRKTlvfcssVDHAEALAELLNEagIRAAVVTGDTPKKE 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186498546 811 KEEALNKFRSGETQILLSTQVIEIGVDVPDASMMVVM---NAERFgIAQlhqlrgRVGRGTRKSK 872
Cdd:COG1061 344 REEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLrptGSPRE-FIQ------RLGRGLRPAP 401
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
543-673 |
1.51e-11 |
|
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: 63.19 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 543 MNRLLQGDVGCGKTVVAFLACMEVIGS-GYQAAFMAPTELLAIQHYEQCRDLLenmegvSSKPTIGLLTGSTPAK-QSRM 620
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKkGKKVLVLVPTKALALQTAERLRELF------GPGIRVAVLVGGSSAEeREKN 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 186498546 621 IRQDLQsgaisFIIGTHSLI------AEKIEYSALRIAVVDEQQRFGVIQRGKFNSKLY 673
Cdd:cd00046 76 KLGDAD-----IIIATPDMLlnlllrEDRLFLKDLKLIIVDEAHALLIDSRGALILDLA 129
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
796-870 |
2.58e-08 |
|
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: 53.28 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 796 KYNCGLLHGRMKSDDKEEALNKFRSGETQILLSTQVIEIGVDVPDASmMVV-----MNAERFgiaqLHqlR-GRVGRGTR 869
Cdd:cd18787 51 GIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVD-HVInydlpRDAEDY----VH--RiGRTGRAGR 123
|
.
gi 186498546 870 K 870
Cdd:cd18787 124 K 124
|
|
| RecG_dom3_C |
pfam19833 |
ATP-dependent DNA helicase RecG, domain 3, C-terminal; This domain is found in ATP-dependent ... |
892-946 |
1.09e-07 |
|
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: 50.16 E-value: 1.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 186498546 892 SSDGFYLANIDLLLRGPGDLLGKKQSGHLPEFPVARLEIDGNMLQEAHIAALNVL 946
Cdd:pfam19833 1 TNDGFEIAEADLKLRGPGDLEGTQQSGIAFDLKIADIARDGQLLQLARTEAEEII 55
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
697-870 |
3.26e-07 |
|
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: 53.59 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 697 APHVLaMSATpIPRSLalalygdISLTQITGMP-----LGRIPVETHIFEGNETGIKEVYSMM---LEDLKSGGRVYVVY 768
Cdd:cd09639 155 VPILL-MSAT-LPKFL-------KEYAEKIGYVeenepLDLKPNERAPFIKIESDKVGEISSLerlLEFIKKGGSVAIIV 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 769 PVIDQSEQLPQ-LRAASAELEIVtkkfpkyncgLLHGRMKSDDKE----EALNKFRSGETQILLSTQVIEIGVDVpDASM 843
Cdd:cd09639 226 NTVDRAQEFYQqLKEKGPEEEIM----------LIHSRFTEKDRAkkeaELLLEFKKSEKFVIVATQVIEASLDI-SVDV 294
|
170 180
....*....|....*....|....*..
gi 186498546 844 MVvmnAERFGIAQLHQLRGRVGRGTRK 870
Cdd:cd09639 295 MI---TELAPIDSLIQRLGRLHRYGEK 318
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
822-876 |
4.00e-07 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 48.47 E-value: 4.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 186498546 822 ETQILLSTQVIEIGVDVPDASMMVVMNAERFgIAQLHQLRGRVGR-GTRKSKCLLV 876
Cdd:cd18785 22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSS-AASYIQRVGRAGRgGKDEGEVILF 76
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
805-875 |
5.85e-06 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' 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 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: 350191 [Multi-domain] Cd Length: 238 Bit Score: 48.78 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 805 RMKSD------DKEEALNKFRSGETQILLSTQVIEIGVDVPDASMMVVMNA------------ERfgIAQL-HQLRGRVG 865
Cdd:cd18804 121 RIDRDttrkkgALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGILNAdsglnspdfrasER--AFQLlTQVSGRAG 198
|
90
....*....|
gi 186498546 866 RGTRKSKCLL 875
Cdd:cd18804 199 RGDKPGKVII 208
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
792-876 |
1.12e-05 |
|
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: 46.05 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 792 KKFPKYNCGLLHGR----------MKSDDKEEALNKFRSGETQILLSTQVIEIGVDVPDASMMVvmnaeRFGIA----QL 857
Cdd:cd18802 50 STLAFIRCGFLIGRgnssqrkrslMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVI-----RFDLPktlrSY 124
|
90
....*....|....*....
gi 186498546 858 HQLRGRvGRgTRKSKCLLV 876
Cdd:cd18802 125 IQSRGR-AR-APNSKYILM 141
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
700-876 |
1.17e-05 |
|
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: 48.92 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 700 VLAMSATpIPRSLALALYGDISLtqITGMPlGRIPVETHIFEGNETGIK-------EVYSMMLEDLKSGGRVYVVypV-- 770
Cdd:COG1203 302 VILMTAT-LPPLLREELLEAYEL--IPDEP-EELPEYFRAFVRKRVELKegplsdeELAELILEALHKGKSVLVI--Vnt 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 771 IDQSEQLpqlraasaeLEIVTKKFPKYNCGLLHGRMKSDDK----EEALNKFRSGETQILLSTQVIEIGVDVpDASMMVV 846
Cdd:COG1203 376 VKDAQEL---------YEALKEKLPDEEVYLLHSRFCPADRseieKEIKERLERGKPCILVSTQVVEAGVDI-DFDVVIR 445
|
170 180 190
....*....|....*....|....*....|...
gi 186498546 847 MNAerfGIAQLHQLRGRV---GRGTRKSKCLLV 876
Cdd:COG1203 446 DLA---PLDSLIQRAGRCnrhGRKEEEGNVYVF 475
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
788-875 |
2.17e-05 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 48.58 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 788 EIVTKKFPKYNCGllhgRMKSD---DK---EEALNKFRSGETQILLSTQVIEIGVDVPDASMMVVMNA------------ 849
Cdd:COG1198 495 EELAELFPDARVL----RMDRDttrRKgalEKLLEAFARGEADILVGTQMLAKGHDFPNVTLVGVLDAdlglnspdfraa 570
|
90 100
....*....|....*....|....*..
gi 186498546 850 ERFgiAQL-HQLRGRVGRGTRKSKCLL 875
Cdd:COG1198 571 ERT--FQLlTQVAGRAGRAEKPGEVLI 595
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
788-875 |
4.15e-05 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 47.46 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 788 EIVTKKFPKYNCGllhgRMKSD-----DK-EEALNKFRSGETQILLSTQVIEIGVDVPDASMMVVMNA------------ 849
Cdd:PRK05580 444 EELAELFPEARIL----RIDRDttrrkGAlEQLLAQFARGEADILIGTQMLAKGHDFPNVTLVGVLDAdlglfspdfras 519
|
90 100
....*....|....*....|....*.
gi 186498546 850 ERFgIAQLHQLRGRVGRGTRKSKCLL 875
Cdd:PRK05580 520 ERT-FQLLTQVAGRAGRAEKPGEVLI 544
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
806-870 |
5.86e-05 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 47.03 E-value: 5.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186498546 806 MKSDDKEEALNKFRSGETQILLSTQVIEIGVDVPDASMMV----VMNAERFgIaqlhQLRGRVGRGTRK 870
Cdd:COG1111 395 LTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIfyepVPSEIRS-I----QRKGRTGRKREG 458
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
797-870 |
1.68e-04 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 45.14 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 797 YNCGLLHGRMKSDDKEEALNKFRSGETQILLSTQVIEIGVDVPDASmMVV-----MNAERFgiaqLHqlR-GRVGRGTRK 870
Cdd:COG0513 266 ISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVS-HVInydlpEDPEDY----VH--RiGRTGRAGAE 338
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
780-875 |
1.69e-04 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 45.61 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 780 LRAASAELEIV-TKKFPKYNCGLLHGRMKSDDKEEALNKFRSGETQILLSTQVIEIGVDVPDASMMV----VMNAERFgi 854
Cdd:PRK11634 252 VRTKNATLEVAeALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVnydiPMDSESY-- 329
|
90 100
....*....|....*....|.
gi 186498546 855 aqLHQLrGRVGRGTRKSKCLL 875
Cdd:PRK11634 330 --VHRI-GRTGRAGRAGRALL 347
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
552-659 |
1.92e-04 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 45.49 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 552 GCGKTVVAFLACMEVIGS-GYQAAFMAPTELLAIQHYEQCRDLLENMEGvsskpTIGLLTGST-PAKqsrmiRQDLQSGA 629
Cdd:COG1111 27 GLGKTAVALLVIAERLHKkGGKVLFLAPTKPLVEQHAEFFKEALNIPED-----EIVVFTGEVsPEK-----RKELWEKA 96
|
90 100 110
....*....|....*....|....*....|....*
gi 186498546 630 iSFIIGT-----HSLIAEKIEYSALRIAVVDEQQR 659
Cdd:COG1111 97 -RIIVATpqvieNDLIAGRIDLDDVSLLIFDEAHR 130
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
797-870 |
2.04e-04 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 44.82 E-value: 2.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186498546 797 YNCGLLHGRMKSDDKEEALNKFRSGETQILLSTQVIEIGVDVPDASMMV----VMNAERFgiaqLHQLrGRVGRGTRK 870
Cdd:PTZ00424 292 FTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVInydlPASPENY----IHRI-GRSGRFGRK 364
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
774-847 |
2.74e-04 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350176 [Multi-domain] Cd Length: 153 Bit Score: 42.24 E-value: 2.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186498546 774 SEQLPQLRAASaeleivtKKFPKYncgLLHGRMKSDDKEEALNKFRSGETQILLSTQVIEIGVDVPDASMMVVM 847
Cdd:cd18789 56 TDNVEALYRYA-------KRLLKP---FITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQI 119
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
780-877 |
3.19e-04 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 41.86 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 780 LRAASAELEIVTKKFPKYNCGLLhgrmkSDDKEEALNKFRSGETQILLSTQVIEIGVDVP--DAsmmVVMNAERFGIAQL 857
Cdd:cd18797 55 LKARLVEEGPLASKVASYRAGYL-----AEDRREIEAELFNGELLGVVATNALELGIDIGglDA---VVLAGYPGSLASL 126
|
90 100
....*....|....*....|
gi 186498546 858 HQLRGRVGRGTRKSKCLLVG 877
Cdd:cd18797 127 WQQAGRAGRRGKDSLVILVA 146
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
813-868 |
3.67e-04 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 44.48 E-value: 3.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 813 EALNKFRSGETQILLSTQVIEIGVDVPDASMMV----VMNAERFgIaqlhQLRGRVGRGT 868
Cdd:PRK13766 414 EILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIfyepVPSEIRS-I----QRKGRTGRQE 468
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
806-867 |
3.73e-04 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain] Cd Length: 143 Bit Score: 41.57 E-value: 3.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186498546 806 MKSDDKEEALNKFRSGETQILLSTQVIEIGVDVPDASMMVVMNAERFGIAQLhQLRGRVGRG 867
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMI-QRMGRTGRK 134
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
816-908 |
4.88e-04 |
|
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: 44.06 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186498546 816 NKFRSGETQILLSTQVIEIGVDVP--DAsmmVVMNaerfG----IAQLHQLRGRVGRGTRKSKCLLVGSStNSLkrlnml 889
Cdd:COG1205 338 RGLRSGELLGVVSTNALELGIDIGglDA---VVLA----GypgtRASFWQQAGRAGRRGQDSLVVLVAGD-DPL------ 403
|
90
....*....|....*....
gi 186498546 890 gkssDGFYLANIDLLLRGP 908
Cdd:COG1205 404 ----DQYYVRHPEELFERP 418
|
|
| |
