|
Name |
Accession |
Description |
Interval |
E-value |
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
5-672 |
0e+00 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 966.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 5 MKLSDSIQYLKGVGPKALENYQKLGISTLEDLLFYFPFRYEDFSGKSAL-ELMDGEKATVVGVVVTPvSSRYYGFKKNRL 83
Cdd:COG1200 2 APLDTPLTYLKGVGPKRAKLLAKLGIRTVGDLLFHLPRRYEDRTRLTPIaELRPGETVTVEGTVVSV-EVVRRRRRRRIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 84 NFKIKQDELVISVSFFNQAYLAQKIEVGANLAIYGKWDARRAALSG----IKLL---AQIDNGR-EPVYRLKEGVKQGKL 155
Cdd:COG1200 81 EVTLSDGTGSLTLVFFNQPYLKKQLKPGTRVLVSGKVERFRGGLQMvhpeYELLdeeEAELAGRlTPVYPLTEGLSQKTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 156 VSLIKQVMDLgALNLIEETLPAYLLEKYRLLPRSLAVFNMHFPEDDEAHRQALRRVKFEELFYFQLKMQALKYRDKKLtK 235
Cdd:COG1200 161 RKLIRQALDL-LAPDLPEPLPEELRARYGLPSLAEALRNIHFPPSDEDLHPARRRLAFEELLALQLALLLRRARRRKR-K 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 236 GLSLPYDDKLLLEKINQLPFDLTQAQERALDEICRDLRSNNHMNRLLQGDVGSGKTAVASLAMYAAHTAGFQSAMMVPTE 315
Cdd:COG1200 239 GPALPGDGELLEAFLAALPFELTGAQKRVIAEIAADLASPHPMNRLLQGDVGSGKTVVALLAMLAAVEAGYQAALMAPTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 316 ILANQHLLSLKELFPEL--RVGLLTSGMKPADKREVLAGLVAGSVDMVVGTHALIQDGVEFKNLGLVITDEQHRFGVKQR 393
Cdd:COG1200 319 ILAEQHYRSLSKLLEPLgiRVALLTGSTKAKERREILAALASGEADIVVGTHALIQDDVEFKNLGLVVIDEQHRFGVEQR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 394 KFLREKGENSDVLMMTATPIPRTLAITSYGDMDVSIIDELPKGRVPITTRWTRQEQFSQVLAWIKDELKKGAQVYFISPL 473
Cdd:COG1200 399 LALREKGEAPHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPIKTRVVPEERRDEVYERIREEIAKGRQAYVVCPL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 474 IEESETLDLKNAQDLYQDLKDYFGDqAKIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNAD 553
Cdd:COG1200 479 IEESEKLDLQAAEETYEELREAFPG-LRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVMVIENAE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 554 RFGLSQLHQLRGRVGRGSKKSYAILVANPK-SDQGKERMKIMTETNNGFVLAEADLRMRGSGEIFGLRQSGLPEFTVSDI 632
Cdd:COG1200 558 RFGLSQLHQLRGRVGRGSAQSYCLLLYDAPlSETARERLEVMRETNDGFEIAEEDLELRGPGEFLGTRQSGLPDLRIADL 637
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2467961996 633 VVDYNILEAARLEAEAIFEDD-NLRSNPQ-YRLLFENLSDLD 672
Cdd:COG1200 638 VRDADLLEAAREDAEELLEEDpELASHPAlRRWLGLRFRDED 679
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
5-667 |
0e+00 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 961.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 5 MKLSDSIQYLKGVGPKALENYQKLGISTLEDLLFYFPFRYEDFSG-KSALELMDGEKATVVGVVVtpvSSRYYGFKKNRL 83
Cdd:PRK10917 5 LLLDAPLTSLKGVGPKTAEKLAKLGIHTVQDLLLHLPRRYEDRTRlKPIAELRPGEKVTVEGEVL---SAEVVFGKRRRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 84 NFKIKQDELVISVSFF--NQAYLAQKIEVGANLAIYGKWDARRAALS----GIKLLAQIDNGR----EPVYRLKEGVKQG 153
Cdd:PRK10917 82 TVTVSDGTGNLTLRFFnfNQPYLKKQLKVGKRVAVYGKVKRGKYGLEmvhpEYEVLEEESPELegrlTPVYPLTEGLKQK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 154 KLVSLIKQVMDLgaLNLIEETLPAYLLEKYRLLPRSLAVFNMHFPEDDEAHRQALRRVKFEELFYFQLKMQALKYRDKKL 233
Cdd:PRK10917 162 TLRKLIKQALEL--LDALPELLPEELLEKYGLLSLAEALRAIHFPPSDEDLHPARRRLKFEELFALQLSLLLLRAGRRSK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 234 tKGLSLPYDDKLLLEKINQLPFDLTQAQERALDEICRDLRSNNHMNRLLQGDVGSGKTAVASLAMYAAHTAGFQSAMMVP 313
Cdd:PRK10917 240 -KAGPLPYDGELLKKFLASLPFELTGAQKRVVAEILADLASPKPMNRLLQGDVGSGKTVVAALAALAAIEAGYQAALMAP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 314 TEILANQHLLSLKELFPEL--RVGLLTSGMKPADKREVLAGLVAGSVDMVVGTHALIQDGVEFKNLGLVITDEQHRFGVK 391
Cdd:PRK10917 319 TEILAEQHYENLKKLLEPLgiRVALLTGSLKGKERREILEAIASGEADIVIGTHALIQDDVEFHNLGLVIIDEQHRFGVE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 392 QRKFLREKGENSDVLMMTATPIPRTLAITSYGDMDVSIIDELPKGRVPITTRWTRQEQFSQVLAWIKDELKKGAQVYFIS 471
Cdd:PRK10917 399 QRLALREKGENPHVLVMTATPIPRTLAMTAYGDLDVSVIDELPPGRKPITTVVIPDSRRDEVYERIREEIAKGRQAYVVC 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 472 PLIEESETLDLKNAQDLYQDLKDYFGDqAKIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMN 551
Cdd:PRK10917 479 PLIEESEKLDLQSAEETYEELQEAFPE-LRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVMVIEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 552 ADRFGLSQLHQLRGRVGRGSKKSYAILVA-NPKSDQGKERMKIMTETNNGFVLAEADLRMRGSGEIFGLRQSGLPEFTVS 630
Cdd:PRK10917 558 AERFGLAQLHQLRGRVGRGAAQSYCVLLYkDPLSETARERLKIMRETNDGFVIAEKDLELRGPGELLGTRQSGLPEFKVA 637
|
650 660 670
....*....|....*....|....*....|....*...
gi 2467961996 631 DIVVDYNILEAARLEAEAIFEDD-NLRSNPQYRLLFEN 667
Cdd:PRK10917 638 DLVRDEELLEEARKDARELLERDpELAEALLERWLGER 675
|
|
| recG |
TIGR00643 |
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair] |
28-646 |
0e+00 |
|
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273192 [Multi-domain] Cd Length: 630 Bit Score: 783.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 28 LGISTLEDLLFYFPFRYEDFSG-KSALELMDGEKATVVGVVVtpvSSRYYGFKKNR-LNFKIKQD-ELVISVSFFNQAYL 104
Cdd:TIGR00643 1 LGIHTVQDLLFYFPRRYEDRTLlQTIGELLPGERATIVGEVL---SHCIFGFKRRKvLKLRLKDGgYKKLELRFFNRAFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 105 AQKIEVGANLAIYG--KWDARRAALSGIKLLAQIDNGR-----EPVYRLKEGVKQGKLVSLIKQVMDLGAlNLIEETLPA 177
Cdd:TIGR00643 78 KKKFKVGSKVVVYGkvKSSKFKAYLIHPEFISEKDGVEfelkiLPVYPLTEGLTQKKLRKLIQQALDQLD-KSLEDPLPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 178 YLLEKYRLLPRSLAVFNMHFPEDDEAHRQALRRVKFEELFYFQLKMQALKYRDKKLTKGLSLPYDDKLLLEKINQLPFDL 257
Cdd:TIGR00643 157 ELREKYGLLSLEDALRAIHFPKTLSLLELARRRLIFDEFFYLQLAMLARRLGEKQQFSAPPANPSEELLTKFLASLPFKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 258 TQAQERALDEICRDLRSNNHMNRLLQGDVGSGKTAVASLAMYAAHTAGFQSAMMVPTEILANQHLLSLKELFPEL--RVG 335
Cdd:TIGR00643 237 TRAQKRVVKEILQDLKSDVPMNRLLQGDVGSGKTLVAALAMLAAIEAGYQVALMAPTEILAEQHYNSLRNLLAPLgiEVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 336 LLTSGMKPADKREVLAGLVAGSVDMVVGTHALIQDGVEFKNLGLVITDEQHRFGVKQRKFLREKGE---NSDVLMMTATP 412
Cdd:TIGR00643 317 LLTGSLKGKRRKELLETIASGQIHLVVGTHALIQEKVEFKRLALVIIDEQHRFGVEQRKKLREKGQggfTPHVLVMSATP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 413 IPRTLAITSYGDMDVSIIDELPKGRVPITTRWTRQEQFSQVLAWIKDELKKGAQVYFISPLIEESETLDLKNAQDLYQDL 492
Cdd:TIGR00643 397 IPRTLALTVYGDLDTSIIDELPPGRKPITTVLIKHDEKDIVYEFIEEEIAKGRQAYVVYPLIEESEKLDLKAAEALYERL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 493 KDYFGDqAKIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNADRFGLSQLHQLRGRVGRGSK 572
Cdd:TIGR00643 477 KKAFPK-YNVGLLHGRMKSDEKEAVMEEFREGEVDILVATTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDH 555
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2467961996 573 KSYAILVA-NPKSDQGKERMKIMTETNNGFVLAEADLRMRGSGEIFGLRQSGLPEFTVSDIVVDYNILEAARLEA 646
Cdd:TIGR00643 556 QSYCLLVYkNPKSESAKKRLRVMADTLDGFVIAEEDLELRGPGDLLGTKQSGYPEFRVADLVRDREILVEAREDA 630
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
212-434 |
1.28e-121 |
|
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: 361.08 E-value: 1.28e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 212 KFEELFYFQLKMQALKYRDKKLtKGLSLPYDDKLLLEKINQLPFDLTQAQERALDEICRDLRSNNHMNRLLQGDVGSGKT 291
Cdd:cd17992 2 AFEELFALQLALLLRRRKIEEL-KGIILEISGELLKKFLEALPFELTGAQKRVIDEILRDLASEKPMNRLLQGDVGSGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 292 AVASLAMYAAHTAGFQSAMMVPTEILANQHLLSLKELFPEL--RVGLLTSGMKPADKREVLAGLVAGSVDMVVGTHALIQ 369
Cdd:cd17992 81 VVAALAMLAAVENGYQVALMAPTEILAEQHYDSLKKLLEPLgiRVALLTGSTKAKEKREILEKIASGEIDIVIGTHALIQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2467961996 370 DGVEFKNLGLVITDEQHRFGVKQRKFLREKGENSDVLMMTATPIPRTLAITSYGDMDVSIIDELP 434
Cdd:cd17992 161 EDVEFHNLGLVIIDEQHRFGVEQRLKLREKGETPHVLVMTATPIPRTLALTLYGDLDVSIIDELP 225
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
228-623 |
4.16e-110 |
|
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: 353.97 E-value: 4.16e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 228 YRDKKLTKGLSLPYDDKLLLEKINQLPFDLTQAQERALDEICRDLRSNNHMNRLLQGDVGSGKTAVASLAMYAAHTAGFQ 307
Cdd:TIGR00580 423 YAKRKAIKGHAFPPDLEWQQEFEDSFPFEETPDQLKAIEEIKADMESPRPMDRLVCGDVGFGKTEVAMRAAFKAVLDGKQ 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 308 SAMMVPTEILANQHLLSLKELFPE--LRVGLLTSGMKPADKREVLAGLVAGSVDMVVGTHALIQDGVEFKNLGLVITDEQ 385
Cdd:TIGR00580 503 VAVLVPTTLLAQQHFETFKERFANfpVTIELLSRFRSAKEQNEILKELASGKIDILIGTHKLLQKDVKFKDLGLLIIDEE 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 386 HRFGVKQRKFLREKGENSDVLMMTATPIPRTLAITSYGDMDVSIIDELPKGRVPITTrWTRQEQFSQVLAWIKDELKKGA 465
Cdd:TIGR00580 583 QRFGVKQKEKLKELRTSVDVLTLSATPIPRTLHMSMSGIRDLSIIATPPEDRLPVRT-FVMEYDPELVREAIRRELLRGG 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 466 QVYFISPLIEesetlDLKNAQDLYQDLKDYfgdqAKIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDAT 545
Cdd:TIGR00580 662 QVFYVHNRIE-----SIEKLATQLRELVPE----ARIAIAHGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNAN 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 546 IMVIMNADRFGLSQLHQLRGRVGRGSKKSYA-ILVANPK--SDQGKERMKIMTETNN---GFVLAEADLRMRGSGEIFGL 619
Cdd:TIGR00580 733 TIIIERADKFGLAQLYQLRGRVGRSKKKAYAyLLYPHQKalTEDAQKRLEAIQEFSElgaGFKIALHDLEIRGAGNLLGE 812
|
....
gi 2467961996 620 RQSG 623
Cdd:TIGR00580 813 EQSG 816
|
|
| Mfd |
COG1197 |
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ... |
254-623 |
1.36e-95 |
|
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription];
Pssm-ID: 440810 [Multi-domain] Cd Length: 1130 Bit Score: 318.93 E-value: 1.36e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 254 PFDLTQAQERALDEICRDLRSNNHMNRLLQGDVGSGKTAVASLAMYAAHTAGFQSAMMVPTEILANQHLLSLKELF---P 330
Cdd:COG1197 584 PYEETPDQLRAIEEVKADMESPRPMDRLVCGDVGFGKTEVALRAAFKAVMDGKQVAVLVPTTLLAQQHYETFKERFagfP 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 331 eLRVGLLtSGMK-PADKREVLAGLVAGSVDMVVGTHALIQDGVEFKNLGLVITDEQHRFGVKQRKFLREKGENSDVLMMT 409
Cdd:COG1197 664 -VRVEVL-SRFRtAKEQKETLEGLADGKVDIVIGTHRLLSKDVKFKDLGLLIIDEEQRFGVRHKEKLKALRANVDVLTLT 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 410 ATPIPRTL--AITSYGDMdvSIIDELPKGRVPITTrwtrqeqFsqVLAW----IKD----ELKKGAQVYFISPLIEeseT 479
Cdd:COG1197 742 ATPIPRTLqmSLSGIRDL--SIIATPPEDRLPVKT-------F--VGEYddalIREailrELLRGGQVFYVHNRVE---D 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 480 LDlknaqDLYQDLKDYFGDqAKIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNADRFGLSQ 559
Cdd:COG1197 808 IE-----KVAARLQELVPE-ARIAVAHGQMSERELERVMLDFYEGEFDVLVCTTIIETGIDIPNANTIIIERADRFGLAQ 881
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 560 LHQLRGRVGRGSKKSYA-ILVANPK--SDQGKERMKIMTETNN---GFVLAEADLRMRGSGEIFGLRQSG 623
Cdd:COG1197 882 LYQLRGRVGRSHRRAYAyLLYPPDKvlTEDAEKRLEAIQEFTElgaGFKLAMHDLEIRGAGNLLGEEQSG 951
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
439-596 |
5.02e-81 |
|
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: 253.81 E-value: 5.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 439 PITTRWTRQEQFSQVLAWIKDELKKGAQVYFISPLIEESETLDLKNAQDLYQDLKDYFGDQAKIALLHGRMKAQEKDEIM 518
Cdd:cd18811 1 PITTYLIFHTRLDKVYEFVREEIAKGRQAYVIYPLIEESEKLDLKAAVAMYEYLKERFRPELNVGLLHGRLKSDEKDAVM 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2467961996 519 TSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNADRFGLSQLHQLRGRVGRGSKKSYAILVANPK-SDQGKERMKIMTE 596
Cdd:cd18811 81 AEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYKDPlTETAKQRLRVMTE 159
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
254-623 |
3.68e-72 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 253.51 E-value: 3.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 254 PFDLTQAQERALDEICRDLRSNNHMNRLLQGDVGSGKTAVASLAMYAAHTAGFQSAMMVPTEILANQHLLSLKELFPE-- 331
Cdd:PRK10689 598 PFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQHYDNFRDRFANwp 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 332 LRVGLLTSGMKPADKREVLAGLVAGSVDMVVGTHALIQDGVEFKNLGLVITDEQHRFGVKQRKFLREKGENSDVLMMTAT 411
Cdd:PRK10689 678 VRIEMLSRFRSAKEQTQILAEAAEGKIDILIGTHKLLQSDVKWKDLGLLIVDEEHRFGVRHKERIKAMRADVDILTLTAT 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 412 PIPRTLAITSYGDMDVSIIDELPKGRVPITTrWTRQEQFSQVLAWIKDELKKGAQVYFISPLIEESEtldlKNAQDLYQD 491
Cdd:PRK10689 758 PIPRTLNMAMSGMRDLSIIATPPARRLAVKT-FVREYDSLVVREAILREILRGGQVYYLYNDVENIQ----KAAERLAEL 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 492 LKdyfgdQAKIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNADRFGLSQLHQLRGRVGRGS 571
Cdd:PRK10689 833 VP-----EARIAIGHGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLRGRVGRSH 907
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2467961996 572 KKSYA-ILVANPK---SDQGK--ERMKIMTETNNGFVLAEADLRMRGSGEIFGLRQSG 623
Cdd:PRK10689 908 HQAYAwLLTPHPKamtTDAQKrlEAIASLEDLGAGFALATHDLEIRGAGELLGEEQSG 965
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
439-596 |
1.08e-71 |
|
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: 229.08 E-value: 1.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 439 PITTRWTRQEQFSQVLAWIKDELKKGAQVYFISPLIEESETLDLKNAQDLYQDLKDYFGDqAKIALLHGRMKAQEKDEIM 518
Cdd:cd18792 1 PIRTYVIPHDDLDLVYEAIERELARGGQVYYVYPRIEESEKLDLKSIEALAEELKELVPE-ARVALLHGKMTEDEKEAVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 519 TSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNADRFGLSQLHQLRGRVGRGSKKSYAILVANPK---SDQGKERMKIMT 595
Cdd:cd18792 80 LEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYPDPkklTETAKKRLRAIA 159
|
.
gi 2467961996 596 E 596
Cdd:cd18792 160 E 160
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
242-431 |
3.58e-66 |
|
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: 215.90 E-value: 3.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 242 DDKLLLEKINQLPFDLTQAQERALDEICRDLRSNNHMNRLLQGDVGSGKTAVASLAMYAAHTAGFQSAMMVPTEILANQH 321
Cdd:cd17991 1 DGEEQEEFEASFPYEETPDQLKAIEEILKDMESGKPMDRLICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 322 LLSLKELFPEL--RVGLLTSGMKPADKREVLAGLVAGSVDMVVGTHALIQDGVEFKNLGLVITDEQHRFGVKQRKFLREK 399
Cdd:cd17991 81 YETFKERFANFpvNVELLSRFTTAAEQREILEGLKEGKVDIVIGTHRLLSKDVEFKNLGLLIIDEEQRFGVKQKEKLKEL 160
|
170 180 190
....*....|....*....|....*....|..
gi 2467961996 400 GENSDVLMMTATPIPRTLAITSYGDMDVSIID 431
Cdd:cd17991 161 RPNVDVLTLSATPIPRTLHMALSGIRDLSVIA 192
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
242-431 |
4.52e-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: 209.96 E-value: 4.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 242 DDKLLLEKINQLPFDLTQAQERALDEICRDLRSNNHMNRLLQGDVGSGKTAVASLAMYAAHTAGFQSAMMVPTEILANQH 321
Cdd:cd17918 1 DRALIQELCKSLPFSLTKDQAQAIKDIEKDLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 322 LLSLKELFPELRVGLLTSGMKPADKREvlaglvagsVDMVVGTHALIQDGVEFKNLGLVITDEQHRFGVKQRKFLREKGe 401
Cdd:cd17918 81 YEEARKFLPFINVELVTGGTKAQILSG---------ISLLVGTHALLHLDVKFKNLDLVIVDEQHRFGVAQREALYNLG- 150
|
170 180 190
....*....|....*....|....*....|
gi 2467961996 402 NSDVLMMTATPIPRTLAITSYGDMDVSIID 431
Cdd:cd17918 151 ATHFLEATATPIPRTLALALSGLLDLSVID 180
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
457-596 |
1.47e-35 |
|
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: 131.31 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 457 IKDELKKGAQVYFISPLIEesetlDLKNAQDLYQDLKDYfgdqAKIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIE 536
Cdd:cd18810 18 IERELLRGGQVFYVHNRIE-----SIEKLATQLRQLVPE----ARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIE 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2467961996 537 VGVNVPDATIMVIMNADRFGLSQLHQLRGRVGRGSKKSYA-ILVANPKS--DQGKERMKIMTE 596
Cdd:cd18810 89 SGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKERAYAyFLYPDQKKltEDALKRLEAIQE 151
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
258-418 |
5.93e-24 |
|
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: 98.85 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 258 TQAQERALDEIC--RDLrsnnhmnrLLQGDVGSGKTAVASLAMYAA---HTAGFQSAMMVPTEILANQHLLSLKELF--P 330
Cdd:pfam00270 1 TPIQAEAIPAILegRDV--------LVQAPTGSGKTLAFLLPALEAldkLDNGPQALVLAPTRELAEQIYEELKKLGkgL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 331 ELRVGLLTSGMKPADKREVLAGlvagsVDMVVGTH----ALIQDGVEFKNLGLVITDEQHR-----FGVKQRKFLREKGE 401
Cdd:pfam00270 73 GLKVASLLGGDSRKEQLEKLKG-----PDILVGTPgrllDLLQERKLLKNLKLLVLDEAHRlldmgFGPDLEEILRRLPK 147
|
170
....*....|....*..
gi 2467961996 402 NSDVLMMTATPiPRTLA 418
Cdd:pfam00270 148 KRQILLLSATL-PRNLE 163
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
253-441 |
1.07e-21 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 93.33 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 253 LPFDLTQAQERALDEICrdlrsNNHMNRLLQGDVGSGKTAVASLAM--YAAHTAGFQSAMMVPTEILANQHLLSLKELFP 330
Cdd:smart00487 5 GFEPLRPYQKEAIEALL-----SGLRDVILAAPTGSGKTLAALLPAleALKRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 331 E--LRVGLLTSGmkpADKREVLAGLVAGSVDMVVGT-----HALIQDGVEFKNLGLVITDEQHRFGVKQR-----KFLRE 398
Cdd:smart00487 80 SlgLKVVGLYGG---DSKREQLRKLESGKTDILVTTpgrllDLLENDKLSLSNVDLVILDEAHRLLDGGFgdqleKLLKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2467961996 399 KGENSDVLMMTATPIPRTLAITSYGDMDVSIIDELPKGRVPIT 441
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIE 199
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
177-579 |
3.60e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 94.71 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 177 AYLLEKYRLLPRSLAVFNMHFPEDDEAHRQALRRVKFEELFYFQLKMQALKYRDKKLTKGLSL-PYddklllekinqlpf 255
Cdd:COG1061 19 LLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELrPY-------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 256 dltqaQERALDEICRDLRSNNHMNrLLQGDVGSGKTAVASLAMYAAHTAG---FqsamMVPTEILANQHLLSLKELFPEL 332
Cdd:COG1061 85 -----QQEALEALLAALERGGGRG-LVVAPTGTGKTVLALALAAELLRGKrvlV----LVPRRELLEQWAEELRRFLGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 333 RVGlltSGMKPADKrevlaglvagsvDMVVGTHALIQDGVEFKNL----GLVITDEQHRFGVKQRKFLREKGENSDVLMM 408
Cdd:COG1061 155 LAG---GGKKDSDA------------PITVATYQSLARRAHLDELgdrfGLVIIDEAHHAGAPSYRRILEAFPAAYRLGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 409 TATPI---PRTLAITSYGDM--DVSIIDELPKGRV------PITTRWTRQ----EQFSQVLAW---------------IK 458
Cdd:COG1061 220 TATPFrsdGREILLFLFDGIvyEYSLKEAIEDGYLappeyyGIRVDLTDEraeyDALSERLREalaadaerkdkilreLL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 459 DELKKGAQVYFISPLIEESEtldlknaqdlyqDLKDYFGDQ-AKIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEV 537
Cdd:COG1061 300 REHPDDRKTLVFCSSVDHAE------------ALAELLNEAgIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNE 367
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2467961996 538 GVNVPDATIMVIMNADRFgLSQLHQLRGRVGRGSK-KSYAILV 579
Cdd:COG1061 368 GVDVPRLDVAILLRPTGS-PREFIQRLGRGLRPAPgKEDALVY 409
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
501-569 |
7.37e-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: 85.34 E-value: 7.37e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2467961996 501 KIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNADrFGLSQLHQLRGRVGR 569
Cdd:pfam00271 40 KVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLP-WNPASYIQRIGRAGR 107
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
501-569 |
1.75e-18 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 80.33 E-value: 1.75e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2467961996 501 KIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNADrFGLSQLHQLRGRVGR 569
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-WSPASYIQRIGRAGR 80
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
277-411 |
2.72e-18 |
|
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: 82.07 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 277 HMNRLLQGDVGSGKTAVASLAMY-AAHTAGFQSAMMVPTEILANQHLLSLKELFPE-LRVGLLTSGMKPADKREvlagLV 354
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALlLLLKKGKKVLVLVPTKALALQTAERLRELFGPgIRVAVLVGGSSAEEREK----NK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 355 AGSVDMVVGTHALIQ------DGVEFKNLGLVITDEQHRFGVKQRKFLREK-------GENSDVLMMTAT 411
Cdd:cd00046 77 LGDADIIIATPDMLLnlllreDRLFLKDLKLIIVDEAHALLIDSRGALILDlavrkagLKNAQVILLSAT 146
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
252-569 |
1.15e-15 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 79.92 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 252 QLPFDLTQAQERALDEICRDLRSNNhmNRLLQGDVGSGKTAVASLAMYAAHTAGFQSAMMVP-TEI---LANQhllsLKE 327
Cdd:COG4098 106 TWEGTLTPAQQKASDELLEAIKKKE--EHLVWAVCGAGKTEMLFPAIAEALKQGGRVCIATPrVDVvleLAPR----LQQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 328 LFPELRVGLLTSGMKPADKRevlAGLVagsvdmVVGTHALIQdgveFKN-LGLVITDE----------QHRFGVKQ-RKf 395
Cdd:COG4098 180 AFPGVDIAALYGGSEEKYRY---AQLV------IATTHQLLR----FYQaFDLLIIDEvdafpysgdpMLQYAVKRaRK- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 396 lrekgENSDVLMMTATPiPRTL--AITSyGDMDVSIID------ELPkgrVPITT-------RWTRQEQFSQVLAWIKDE 460
Cdd:COG4098 246 -----PDGKLIYLTATP-SKALqrQVKR-GKLKVVKLParyhghPLP---VPKFKwlgnwkkRLRRGKLPRKLLKWLKKR 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 461 LKKGAQVYFISPLIEESETLdlknaqdlYQDLKDYFGDqAKIALLHGrmKAQEKDEIMTSFKAKEYDILVSTTVIEVGVN 540
Cdd:COG4098 316 LKEGRQLLIFVPTIELLEQL--------VALLQKLFPE-ERIAGVHA--EDPERKEKVQAFRDGEIPILVTTTILERGVT 384
|
330 340 350
....*....|....*....|....*....|
gi 2467961996 541 VPDATIMVIMNADR-FGLSQLHQLRGRVGR 569
Cdd:COG4098 385 FPNVDVAVLGADHPvFTEAALVQIAGRVGR 414
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
254-578 |
3.87e-15 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 79.04 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 254 PFDLTQAQERALDEICRDLRSNNHmnrLLQGDVGSGKT-----AVAslamyAAHTAGFQSAMMVPtEI-LANQHLLSLKE 327
Cdd:PRK05580 142 PPTLNPEQAAAVEAIRAAAGFSPF---LLDGVTGSGKTevylqAIA-----EVLAQGKQALVLVP-EIaLTPQMLARFRA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 328 LFPElRVGLLTSGMKPADKREVLAGLVAGSVDMVVGTH-ALIqdgVEFKNLGLVITDEQHRFGVKQ--------RKF--L 396
Cdd:PRK05580 213 RFGA-PVAVLHSGLSDGERLDEWRKAKRGEAKVVIGARsALF---LPFKNLGLIIVDEEHDSSYKQqegpryhaRDLavV 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 397 REKGENSDVLMMTATPiprtlAITSY-------------------GDM-DVSIID--ELPKGRvpiTTRWtrqeqFSQVL 454
Cdd:PRK05580 289 RAKLENIPVVLGSATP-----SLESLanaqqgryrllrltkraggARLpEVEIIDmrELLRGE---NGSF-----LSPPL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 455 -AWIKDELKKGAQV-YFI-----SPLI------------------------------------------EESETLDLKN- 484
Cdd:PRK05580 356 lEAIKQRLERGEQVlLFLnrrgyAPFLlcrdcgwvaecphcdasltlhrfqrrlrchhcgyqepipkacPECGSTDLVPv 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 485 ---AQDLYQDLKDYFgDQAKIALL-------HGRMKaqekdEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNAD- 553
Cdd:PRK05580 436 gpgTERLEEELAELF-PEARILRIdrdttrrKGALE-----QLLAQFARGEADILIGTQMLAKGHDFPNVTLVGVLDADl 509
|
410 420 430
....*....|....*....|....*....|....*.
gi 2467961996 554 -----------RFgLSQLHQLRGRVGRGSKKSYAIL 578
Cdd:PRK05580 510 glfspdfraseRT-FQLLTQVAGRAGRAEKPGEVLI 544
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
243-585 |
3.99e-14 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 75.32 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 243 DKLLLEKINQL-----PFDLTQAQERALDeicRDLRSNNHMnrLLQGDVGSGKTAVASLAMYAAHTAGFQSAMMVPTEIL 317
Cdd:COG1204 4 AELPLEKVIEFlkergIEELYPPQAEALE---AGLLEGKNL--VVSAPTASGKTLIAELAILKALLNGGKALYIVPLRAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 318 ANQHLLSLKELFPEL--RVGLLTSGMKPADKRevlaglvAGSVDMVVGT----HALIQDGVEF-KNLGLVITDEQHRFGV 390
Cdd:COG1204 79 ASEKYREFKRDFEELgiKVGVSTGDYDSDDEW-------LGRYDILVATpeklDSLLRNGPSWlRDVDLVVVDEAHLIDD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 391 KQRKF--------LREKGENSDVLMMTAT---------------------PIPRTLAITSYGDMDVSiiDELPKGRVPIt 441
Cdd:COG1204 152 ESRGPtlevllarLRRLNPEAQIVALSATignaeeiaewldaelvksdwrPVPLNEGVLYDGVLRFD--DGSRRSKDPT- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 442 trwtrqeqfsqvLAWIKDELKKGAQ--VYF----------------ISPLIEESETLDLKNAQDLYQDLKDYFGDQAKIA 503
Cdd:COG1204 229 ------------LALALDLLEEGGQvlVFVssrrdaeslakkladeLKRRLTPEEREELEELAEELLEVSEETHTNEKLA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 504 LL--------HGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATImVIMNADRFGLSQL-----HQLRGRVGRG 570
Cdd:COG1204 297 DClekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRV-IIRDTKRGGMVPIpvlefKQMAGRAGRP 375
|
410
....*....|....*..
gi 2467961996 571 SKKSY--AILVANPKSD 585
Cdd:COG1204 376 GYDPYgeAILVAKSSDE 392
|
|
| RecG_dom3_C |
pfam19833 |
ATP-dependent DNA helicase RecG, domain 3, C-terminal; This domain is found in ATP-dependent ... |
597-671 |
1.30e-12 |
|
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: 63.65 E-value: 1.30e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2467961996 597 TNNGFVLAEADLRMRGSGEIFGLRQSGLP-EFTVSDIVVDYNILEAARLEAEAIFEDDNLRSNPQYRLLFENLSDL 671
Cdd:pfam19833 1 TNDGFEIAEADLKLRGPGDLEGTQQSGIAfDLKIADIARDGQLLQLARTEAEEIIDNDPECSLPENAVLWRQLKEL 76
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
261-412 |
6.36e-12 |
|
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: 64.54 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 261 QERALDEICRDLRSNNhmNRLLQGDVGSGKTAVASLAMYAAHTAGFQSAMMVPtEI-LANQHLLSLKELFPeLRVGLLTS 339
Cdd:cd17929 1 QRKAYEAIVSSLGGFK--TFLLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVP-EIsLTPQLIKRFKKRFG-DKVAVLHS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 340 GMKPADKREVLAGLVAGSVDMVVGTH-ALIqdgVEFKNLGLVITDEQHRFGVKQRK----------FLREKGENSDVLMM 408
Cdd:cd17929 77 KLSDKERADEWRKIKRGEAKVVIGARsALF---APFKNLGLIIVDEEHDSSYKQDSgpryhardvaIYRAKLENAPVVLG 153
|
....
gi 2467961996 409 TATP 412
Cdd:cd17929 154 SATP 157
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
281-589 |
1.64e-11 |
|
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: 66.30 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 281 LLQGDVGSGKT-AVASLAMYAAHTAGFQSAMMV-PTEILANQHLLSLKELFPELRVG---LLTSGMKPADKREVLAGLVA 355
Cdd:cd09639 3 VIEAPTGYGKTeAALLWALHSLKSQKADRVIIAlPTRATINAMYRRAKEAFGETGLYhssILSSRIKEMGDSEEFEHLFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 356 -----------------------GSVDMVVGTHALIQDGVEfknLGLVITDEQHRFG-------VKQRKFLREKGenSDV 405
Cdd:cd09639 83 lyihsndtlfldpitvctidqvlKSVFGEFGHYEFTLASIA---NSLLIFDEVHFYDeytlaliLAVLEVLKDND--VPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 406 LMMTATpIPRTLA--ITSYG-DMDVSIIDELPKGRVPITTRWTRQEQFSQVLAWIKDELKKGAQVYFISPLIEEsetldl 482
Cdd:cd09639 158 LLMSAT-LPKFLKeyAEKIGyVEENEPLDLKPNERAPFIKIESDKVGEISSLERLLEFIKKGGSVAIIVNTVDR------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 483 knAQDLYQDLKDYfGDQAKIALLHGRM----KAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVpDATIMVimnADRFGLS 558
Cdd:cd09639 231 --AQEFYQQLKEK-GPEEEIMLIHSRFtekdRAKKEAELLLEFKKSEKFVIVATQVIEASLDI-SVDVMI---TELAPID 303
|
330 340 350
....*....|....*....|....*....|.
gi 2467961996 559 QLHQLRGRVGRGSKKSYAILVANPKSDQGKE 589
Cdd:cd09639 304 SLIQRLGRLHRYGEKNGEEVYIITDAPDGKG 334
|
|
| RecG_wedge |
pfam17191 |
RecG wedge domain; This DNA-binding domain has an OB-fold with large elaborations. |
11-161 |
4.11e-11 |
|
RecG wedge domain; This DNA-binding domain has an OB-fold with large elaborations.
Pssm-ID: 407316 [Multi-domain] Cd Length: 162 Bit Score: 61.69 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 11 IQYLKGVGPKALENYQKLGISTLEDLLFYFPFRYEDFSG-KSALELMDGEKATVvgvvvtpvssryygfKKNRLNFKIKQ 89
Cdd:pfam17191 2 IKYAKGVGPKREKILKKLGIETIGDLIWYFPRDYEDRRKiIPISDIRHDEKVTT---------------KGKIVNFETKK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 90 -DELVISVS------------FFNQAYLAQKIEVGANLAIYGKwdARRAALSGIKL----LAQIDNGRE----PVYRLKE 148
Cdd:pfam17191 67 iGSLVIISAvlsdgigqvllkWFNQEYIKKFLQKGKEVYITGT--VKEGPFGPIEMnnpeIEEITGEQEreilPVYPLTE 144
|
170
....*....|...
gi 2467961996 149 GVKQGKLVSLIKQ 161
Cdd:pfam17191 145 GISQKNMRKIVKE 157
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
246-588 |
2.20e-10 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 63.56 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 246 LLEKINQLPFDLTQAQERALDEiCRDLRSNNHMNRLLQGDVGSGKTaVASLAMYAAHTAGFQSAMMV---PTEILANQHL 322
Cdd:COG1203 117 LLPKKSKPRTPINPLQNEALEL-ALEAAEEEPGLFILTAPTGGGKT-EAALLFALRLAAKHGGRRIIyalPFTSIINQTY 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 323 LSLKELFPElRVGLLTS--GMKPADKREVLAGLVAGSVD--------MVVGT-----HALI--QDGVEFKNLGL----VI 381
Cdd:COG1203 195 DRLRDLFGE-DVLLHHSlaDLDLLEEEEEYESEARWLKLlkelwdapVVVTTidqlfESLFsnRKGQERRLHNLansvII 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 382 TDEQHRFGVKQ----RKFLREKGE-NSDVLMMTAT--PIPRTL------AITSYGDMDVSIIDELPKGRVPIT-TRWTRQ 447
Cdd:COG1203 274 LDEVQAYPPYMlallLRLLEWLKNlGGSVILMTATlpPLLREElleayeLIPDEPEELPEYFRAFVRKRVELKeGPLSDE 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 448 EqfsqVLAWIKDELKKGAQVYFISPLIeesetldlKNAQDLYQDLKDYFGDQaKIALLHGRMKAQEK----DEIMTSFKA 523
Cdd:COG1203 354 E----LAELILEALHKGKSVLVIVNTV--------KDAQELYEALKEKLPDE-EVYLLHSRFCPADRseieKEIKERLER 420
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2467961996 524 KEYDILVSTTVIEVGVNVpDATIMVImnaDRFGLSQLHQLRGRVGRGSKKSYA--ILVANPKSDQGK 588
Cdd:COG1203 421 GKPCILVSTQVVEAGVDI-DFDVVIR---DLAPLDSLIQRAGRCNRHGRKEEEgnVYVFDPEDEGGG 483
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
254-578 |
9.41e-10 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 61.67 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 254 PFDLTQAQERALDEICRDLRSNNHMnrLLQGDVGSGKTAVaslamY---AAHT--AGFQSAMMVPtEI-LANQHLLSLKE 327
Cdd:COG1198 193 PPTLNEEQQAAVEAIRAAAGGFSVF--LLHGVTGSGKTEV-----YlqaIAEVlaQGKQALVLVP-EIaLTPQTVERFRA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 328 LFPElRVGLLTSGMKPADKREVLAGLVAGSVDMVVGTH-ALIqdgVEFKNLGLVITDEQH--RFgvKQ--------RKF- 395
Cdd:COG1198 265 RFGA-RVAVLHSGLSDGERLDEWRRARRGEARIVIGTRsALF---APFPNLGLIIVDEEHdsSY--KQedgpryhaRDVa 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 396 -LREKGENSDVLMMTATPiprtlAITSY-----GDM---------------DVSIID---ELPKGRvpittRWtrqeqFS 451
Cdd:COG1198 339 vVRAKLEGAPVVLGSATP-----SLESLynaqkGRYrllelperaggaplpEVELVDmreEPLEGG-----RI-----LS 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 452 QVL-AWIKDELKKGAQV-YFI-----SPLIE--------------------------------------------ESETL 480
Cdd:COG1198 404 PPLlEAIEETLERGEQVlLFLnrrgyAPFLLcrdcgwvakcpncdvsltyhrsrrrlrchycgyeepvpkqcpecGSDSL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 481 DLKNA--QDLYQDLKDYFGDqAKIAllhgRM------KAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNA 552
Cdd:COG1198 484 RPFGPgtERVEEELAELFPD-ARVL----RMdrdttrRKGALEKLLEAFARGEADILVGTQMLAKGHDFPNVTLVGVLDA 558
|
410 420 430
....*....|....*....|....*....|....*...
gi 2467961996 553 DRfGLS------------QLHQLRGRVGRGSKKSYAIL 578
Cdd:COG1198 559 DL-GLNspdfraaertfqLLTQVAGRAGRAEKPGEVLI 595
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
287-580 |
1.59e-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: 57.92 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 287 GSGKTAVASL----AMYAAHTAgfqSAMMV-PTEILANQHLLSLKELF----PELRVGLLTSGMKPADKREVLAglvAGS 357
Cdd:COG1205 81 ASGKSLAYLLpvleALLEDPGA---TALYLyPTKALARDQLRRLRELAealgLGVRVATYDGDTPPEERRWIRE---HPD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 358 V-----DMVvgtHALIQDGVE-----FKNLGLVITDEQHR----FG--VKQ-----RKFLREKGENSDVLMMTATpI--P 414
Cdd:COG1205 155 IvltnpDML---HYGLLPHHTrwarfFRNLRYVVIDEAHTyrgvFGshVANvlrrlRRICRHYGSDPQFILASAT-IgnP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 415 RTLA--ITsygDMDVSIIDEL--PKGRV-------PITTRWTRQEQFSQVLAWIKDELKKGAQ--VYFISplieesetld 481
Cdd:COG1205 231 AEHAerLT---GRPVTVVDEDgsPRGERtfvlwnpPLVDDGIRRSALAEAARLLADLVREGLRtlVFTRS---------- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 482 LKNAQDLYQDLKDYFGDQA---KIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVP--DATIMVimnadrfG 556
Cdd:COG1205 298 RRGAELLARYARRALREPDladRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGglDAVVLA-------G 370
|
330 340
....*....|....*....|....*...
gi 2467961996 557 ----LSQLHQLRGRVGRGSKKSYAILVA 580
Cdd:COG1205 371 ypgtRASFWQQAGRAGRRGQDSLVVLVA 398
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
256-393 |
4.27e-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: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 256 DLTQAQERALDEIcrdLRSNNHMnrLLQGDVGSGKTAVASLAMYAAHTAGFQSAM-MVPTEILANQHLLSLKELF--PEL 332
Cdd:cd17921 1 LLNPIQREALRAL---YLSGDSV--LVSAPTSSGKTLIAELAILRALATSGGKAVyIAPTRALVNQKEADLRERFgpLGK 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2467961996 333 RVGLLTSGMKPADKREVLAglvagsvDMVVGT----HALIQDGVE--FKNLGLVITDEQHRFGVKQR 393
Cdd:cd17921 76 NVGLLTGDPSVNKLLLAEA-------DILVATpeklDLLLRNGGErlIQDVRLVVVDEAHLIGDGER 135
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
492-585 |
1.04e-07 |
|
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: 53.40 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 492 LKDYFGDqAKIAllhgRM------KAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNADrFGL-------- 557
Cdd:cd18804 110 LKTLFPE-ARIA----RIdrdttrKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGILNAD-SGLnspdfras 183
|
90 100 110
....*....|....*....|....*....|...
gi 2467961996 558 ----SQLHQLRGRVGRGSKKSYAIL-VANPKSD 585
Cdd:cd18804 184 erafQLLTQVSGRAGRGDKPGKVIIqTYNPEHP 216
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
523-577 |
1.33e-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: 1.33e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2467961996 523 AKEYDILVSTTVIEVGVNVPDATIMVIMNADRFgLSQLHQLRGRVGRGSKKSYAI 577
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSS-AASYIQRVGRAGRGGKDEGEV 73
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
487-580 |
3.85e-07 |
|
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: 49.95 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 487 DLYQDLKDYFGDQAKIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVP--DATIMViMNAdrFGLSQLHQLR 564
Cdd:cd18797 54 YLKARLVEEGPLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGglDAVVLA-GYP--GSLASLWQQA 130
|
90
....*....|....*.
gi 2467961996 565 GRVGRGSKKSYAILVA 580
Cdd:cd18797 131 GRAGRRGKDSLVILVA 146
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
483-578 |
8.46e-07 |
|
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: 48.66 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 483 KNAQDLYQDLKDyfgDQAKIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATiMVI-----MNADRFgl 557
Cdd:cd18787 38 KRVDRLAELLEE---LGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVD-HVInydlpRDAEDY-- 111
|
90 100
....*....|....*....|..
gi 2467961996 558 sqLHqlR-GRVGRGSKKSYAIL 578
Cdd:cd18787 112 --VH--RiGRTGRAGRKGTAIT 129
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
287-627 |
1.29e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 51.65 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 287 GSGKTAVASLAMYAA-HTAGFQSAMMVPTEILANQHLLSLKELF--PELRVGLLTSGMKPaDKREVLAGlvagSVDMVVG 363
Cdd:COG1111 27 GLGKTAVALLVIAERlHKKGGKVLFLAPTKPLVEQHAEFFKEALniPEDEIVVFTGEVSP-EKRKELWE----KARIIVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 364 T-----HALIQDGVEFKNLGLVITDEQHRfGVKQ-------RKFLrEKGENSDVLMMTATP---------IPRTLAITS- 421
Cdd:COG1111 102 TpqvieNDLIAGRIDLDDVSLLIFDEAHR-AVGNyayvyiaERYH-EDAKDPLILGMTASPgsdeekieeVCENLGIENv 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 422 ----YGDMDVS---------------------IID-----------ELPKGRVPITTRWTRQEqfSQVLAW---IKDELK 462
Cdd:COG1111 180 evrtEEDPDVApyvhdtevewirvelpeelkeIRDllnevlddrlkKLKELGVIVSTSPDLSK--KDLLALqkkLQRRIR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 463 KGAQVYF--ISPLIE--------------------------ESETLDL---KNAQDLYQD---------LKDYFGDQAKI 502
Cdd:COG1111 258 EDDSEGYraISILAEalklrhalelletqgveallrylerlEEEARSSggsKASKRLVSDprfrkamrlAEEADIEHPKL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 503 ALLH---------------------------------------GR------------MKAQEKDEIMTSFKAKEYDILVS 531
Cdd:COG1111 338 SKLReilkeqlgtnpdsriivftqyrdtaemiveflsepgikaGRfvgqaskegdkgLTQKEQIEILERFRAGEFNVLVA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 532 TTVIEVGVNVPdATIMVIM-----NADRFglsqlHQLRGRVGRGSKKSYAILVANPKSDQG-------KER-MKIMTETN 598
Cdd:COG1111 418 TSVAEEGLDIP-EVDLVIFyepvpSEIRS-----IQRKGRTGRKREGRVVVLIAKGTRDEAyywssrrKEKkMKSILKKL 491
|
490 500
....*....|....*....|....*....
gi 2467961996 599 NgfvlaeADLRMRGSGEIFGLRQSGLPEF 627
Cdd:COG1111 492 K------KLLDKQEKEKLKESAQATLDEF 514
|
|
| RecG_wedge_OBF |
cd04488 |
RecG_wedge_OBF: A subfamily of OB folds corresponding to the OB fold found in the N-terminal ... |
76-128 |
1.60e-06 |
|
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: 46.03 E-value: 1.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2467961996 76 YGFKKNRLNFKIKQDELVISVSFFN-QAYLAQKIEVGANLAIYGKWDARRAALS 128
Cdd:cd04488 13 PRRGRRRLKVTLSDGTGTLTLVFFNfQPYLKKQLPPGTRVRVSGKVKRFRGGLQ 66
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
490-598 |
1.97e-05 |
|
C-terminal helicase domain of the UvrB family helicases; 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. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB 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: 350177 [Multi-domain] Cd Length: 171 Bit Score: 45.31 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 490 QDLKDYFGDQA-KIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNADRFGL----SQLHQLR 564
Cdd:cd18790 41 EDLTEYLQELGvKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFlrseTSLIQTI 120
|
90 100 110
....*....|....*....|....*....|....
gi 2467961996 565 GRVGRGSkKSYAILVANPKSDQGKermKIMTETN 598
Cdd:cd18790 121 GRAARNV-NGKVILYADKITDSMQ---KAIEETE 150
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
261-413 |
3.05e-05 |
|
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: 45.34 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 261 QERALDEICRDlrsnnhmNRLLQGDVGSGKTAVASLAMYAAH-------TAGFQSAMMVPTEILANQHLLSLKELFPeLR 333
Cdd:cd18034 7 QLELFEAALKR-------NTIVVLPTGSGKTLIAVMLIKEMGelnrkekNPKKRAVFLVPTVPLVAQQAEAIRSHTD-LK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 334 VGLLTSGMKPADKREVLAGLVAGSVDMVVGT-----HALIQDGVEFKNLGLVITDEQHRfGVKQ-------RKFLREKGE 401
Cdd:cd18034 79 VGEYSGEMGVDKWTKERWKEELEKYDVLVMTaqillDALRHGFLSLSDINLLIFDECHH-ATGDhpyarimKEFYHLEGR 157
|
170
....*....|....
gi 2467961996 402 NS--DVLMMTATPI 413
Cdd:cd18034 158 TSrpRILGLTASPV 171
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
509-592 |
3.58e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 47.18 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 509 MKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPdATIMVIM-----NADRFglsqlHQLRGRVGRGSKKSYAILVANPK 583
Cdd:PRK13766 407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIP-SVDLVIFyepvpSEIRS-----IQRKGRTGRQEEGRVVVLIAKGT 480
|
90
....*....|....*..
gi 2467961996 584 SDQG-------KER-MK 592
Cdd:PRK13766 481 RDEAyywssrrKEKkMK 497
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
502-589 |
1.53e-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: 42.62 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 502 IALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMnADRFGLSQlhQLRGRVGRgskksyaILvaN 581
Cdd:cd18789 71 KPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQI-SGHGGSRR--QEAQRLGR-------IL--R 138
|
....*...
gi 2467961996 582 PKSDQGKE 589
Cdd:cd18789 139 PKKGGGKN 146
|
|
| PRK09694 |
PRK09694 |
CRISPR-associated helicase/endonuclease Cas3; |
447-582 |
1.86e-04 |
|
CRISPR-associated helicase/endonuclease Cas3;
Pssm-ID: 182031 [Multi-domain] Cd Length: 878 Bit Score: 44.80 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 447 QEQFSQVLAWIKdelkKGAQVYFISPLIeesetldlKNAQDLYQDLKDYFGDQAKIALLHGRMKAQEK----DEIMTSF- 521
Cdd:PRK09694 547 LTLLQRMIAAAN----AGAQVCLICNLV--------DDAQKLYQRLKELNNTQVDIDLFHARFTLNDRrekeQRVIENFg 614
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2467961996 522 ---KAKEYDILVSTTVIEVGVNVP-DATIMVIMNADRfglsqLHQLRGRVGRGSKKSYAILVANP 582
Cdd:PRK09694 615 kngKRNQGRILVATQVVEQSLDLDfDWLITQLCPVDL-----LFQRLGRLHRHHRKYRPAGFEIP 674
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
279-418 |
3.15e-04 |
|
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: 41.94 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 279 NRLLQGDVGSGKTAVASLAMYAAHTAGFQSAMMVPTEILANQHLLSLKELF-PELRVGlLTSGMKPADKREVlaglvaGS 357
Cdd:cd18028 19 NLLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKKLEeIGLKVG-ISTGDYDEDDEWL------GD 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2467961996 358 VDMVVGTH----ALIQDGVEF-KNLGLVITDEQHRFGVKQR--------KFLREKGENSDVLMMTAT-PIPRTLA 418
Cdd:cd18028 92 YDIIVATYekfdSLLRHSPSWlRDVGVVVVDEIHLISDEERgptlesivARLRRLNPNTQIIGLSATiGNPDELA 166
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
287-412 |
4.09e-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: 41.14 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 287 GSGKTAVASLAMYAAHTAGFqsAMMVPTEILANQHLLSLKELFPELRVGLLTSGmkpADKREVLAGLVAGSVDMVVGTHA 366
Cdd:cd17926 28 GSGKTLTALALIAYLKELRT--LIVVPTDALLDQWKERFEDFLGDSSIGLIGGG---KKKDFDDANVVVATYQSLSNLAE 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2467961996 367 LIQDGVEFKnlGLVITDEQHRFGVKQ-RKFLREKGENSdVLMMTATP 412
Cdd:cd17926 103 EEKDLFDQF--GLLIVDEAHHLPAKTfSEILKELNAKY-RLGLTATP 146
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
287-412 |
6.05e-04 |
|
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: 41.35 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 287 GSGKTAVASLAMYAAHTA-GFQSAMMVPTEILANQHLLSLKELF-PELRVGLLTSGMKPaDKREVL--AGLVAGSVDMVV 362
Cdd:cd18035 26 GLGKTIIAILVAADRLTKkGGKVLILAPSRPLVEQHAENLKRVLnIPDKITSLTGEVKP-EERAERwdASKIIVATPQVI 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2467961996 363 gTHALIQDGVEFKNLGLVITDEQHR------FGVKQRKFLREkGENSDVLMMTATP 412
Cdd:cd18035 105 -ENDLLAGRITLDDVSLLIFDEAHHavgnyaYVYIAHRYKRE-ANNPLILGLTASP 158
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
287-412 |
1.61e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 41.78 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 287 GSGKTAVASL-AMYAAHTAGFQSAMMVPTEILANQHLLSLKELF--PELRVGLLTsGMKPADKREVLaglvAGSVDMVVG 363
Cdd:PRK13766 39 GLGKTAIALLvIAERLHKKGGKVLILAPTKPLVEQHAEFFRKFLniPEEKIVVFT-GEVSPEKRAEL----WEKAKVIVA 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 364 T-----HALIQDGVEFKNLGLVITDEQHR------FGVKQRKFlREKGENSDVLMMTATP 412
Cdd:PRK13766 114 TpqvieNDLIAGRISLEDVSLLIFDEAHRavgnyaYVYIAERY-HEDAKNPLVLGLTASP 172
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
462-533 |
1.63e-03 |
|
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: 40.00 E-value: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2467961996 462 KKGAQVYFISPlieeSETLdLKNAQDLYQDLKDYFGDQAKIALLHGRMKAQEKDEIMTSFKAKEYDILVSTT 533
Cdd:cd17924 58 SKGKRSYLIFP----TKSL-VKQAYERLSKYAEKAGVEVKILVYHSRLKKKEKEELLEKIEKGDFDILVTTN 124
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
281-413 |
1.63e-03 |
|
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: 40.35 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 281 LLQGDVGSGKTAVASLAM--YAAHTAGFQSAMMVPTeILANQHLLSLKELF----PELRVGLLTSGMKPADKREVLAGLV 354
Cdd:cd18011 21 LLADEVGLGKTIEAGLIIkeLLLRGDAKRVLILCPA-SLVEQWQDELQDKFglpfLILDRETAAQLRRLIGNPFEEFPIV 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2467961996 355 AGSVDMVvGTHALIQDGVEFKNLGLVITDEQHRFGVKQR-------KFLREKGENSD-VLMMTATPI 413
Cdd:cd18011 100 IVSLDLL-KRSEERRGLLLSEEWDLVVVDEAHKLRNSGGgketkryKLGRLLAKRARhVLLLTATPH 165
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
509-579 |
2.35e-03 |
|
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: 38.73 E-value: 2.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2467961996 509 MKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVimnadRFGLS----QLHQLRGRvGRGSKKSYAILV 579
Cdd:cd18802 74 MTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVI-----RFDLPktlrSYIQSRGR-ARAPNSKYILMV 142
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
256-307 |
2.55e-03 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 39.14 E-value: 2.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2467961996 256 DLTQAQERALDEICRDLRSNNHMnRLLqgDVGSGKtavASLAMYAAHTAGFQ 307
Cdd:COG2230 31 TLEEAQEAKLDLILRKLGLKPGM-RVL--DIGCGW---GGLALYLARRYGVR 76
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
478-550 |
4.06e-03 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. 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: 350180 [Multi-domain] Cd Length: 135 Bit Score: 37.84 E-value: 4.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2467961996 478 ETLDLknaqdLYQDLKDYFGdqaKIALLHGRMKAQEKDEIMTSFKAKEYD--ILVSTTVIEVGVNVPDATIMVIM 550
Cdd:cd18793 38 DTLDI-----LEEALRERGI---KYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILY 104
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
509-570 |
5.41e-03 |
|
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: 37.72 E-value: 5.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2467961996 509 MKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNADRFGLSQLhQLRGRVGRG 570
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMI-QRMGRTGRK 134
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
501-584 |
6.26e-03 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 39.77 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467961996 501 KIALLHGRMKAQEKDEIMTSFKAKEYDILVSTTVIEVGVNVPDATIMVIMNADRFGLSQLHQLrGRVGRGSKKSYAILVA 580
Cdd:PLN00206 394 KALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQI-GRASRMGEKGTAIVFV 472
|
....
gi 2467961996 581 NPKS 584
Cdd:PLN00206 473 NEED 476
|
|
| |
