|
Name |
Accession |
Description |
Interval |
E-value |
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
106-787 |
0e+00 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 987.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 106 SSLNFDIKYAKGVGERRAKILKKLGIETVKDLLWWLPRDYEDRRRIVPLSSIVADRKVTIRAKLQNFSVKKV-KEYVIIS 184
Cdd:COG1200 2 APLDTPLTYLKGVGPKRAKLLAKLGIRTVGDLLFHLPRRYEDRTRLTPIAELRPGETVTVEGTVVSVEVVRRrRRRRILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 185 AVVSDGFGQIILKWFNQEYITDRLIKEREYLITGIPKKTpFGPYEMNSPEIEEITG---RVPREILPLYSLSAGISQKVM 261
Cdd:COG1200 82 VTLSDGTGSLTLVFFNQPYLKKQLKPGTRVLVSGKVERF-RGGLQMVHPEYELLDEeeaELAGRLTPVYPLTEGLSQKTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 262 RKIVRKNITNVR-LLKEFIPAEVIKERNLLPRHHAMYTVHFPKSLYELKESRRRLAYEELFLFEVAVLYNREKLKTTKGg 340
Cdd:COG1200 161 RKLIRQALDLLApDLPEPLPEELRARYGLPSLAEALRNIHFPPSDEDLHPARRRLAFEELLALQLALLLRRARRRKRKG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 341 ISKSISGKLAERFIDSLNFVLTGDQMRAFEEIREDMKAPTPMNRLLQGDVGSGKTVVAELAIIDNFEAGYQSAMMVPTTV 420
Cdd:COG1200 240 PALPGDGELLEAFLAALPFELTGAQKRVIAEIAADLASPHPMNRLLQGDVGSGKTVVALLAMLAAVEAGYQAALMAPTEI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 421 LATQQHQKLVKDLEPLGIKVELLVGSQKKSQQEEIKKRIAIGEVDVVVGTHALIQENVKFKDLGLVIIDEQHRFGVKQRE 500
Cdd:COG1200 320 LAEQHYRSLSKLLEPLGIRVALLTGSTKAKERREILAALASGEADIVVGTHALIQDDVEFKNLGLVVIDEQHRFGVEQRL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 501 ALMNKGALVDTLVMTATPIPRTLALTAYGDLDISTITEMPPGRAPIRTMLISEKRLPELYAFIRDEVNHGHQAFFIYPLI 580
Cdd:COG1200 400 ALREKGEAPHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPIKTRVVPEERRDEVYERIREEIAKGRQAYVVCPLI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 581 EESEQMDLKAATDEAERLQkEVFPDIGVELLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVMVIEHPER 660
Cdd:COG1200 480 EESEKLDLQAAEETYEELR-EAFPGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVMVIENAER 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 661 FGLAQLHQLRGRVGRSSLKSYCMLVLNSNISGEALDRLRKFAGTQNGFKLAEIDLSLRGPGEFMGTRQHGLPDFLVADIV 740
Cdd:COG1200 559 FGLSQLHQLRGRVGRGSAQSYCLLLYDAPLSETARERLEVMRETNDGFEIAEEDLELRGPGEFLGTRQSGLPDLRIADLV 638
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 239505248 741 KDSELLIMARNDAMELLKRDPNLEKHNRIIEEIKERFGEnISLIEVG 787
Cdd:COG1200 639 RDADLLEAAREDAEELLEEDPELASHPALRRWLGLRFRD-EDYLEVG 684
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
102-787 |
0e+00 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 946.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 102 PVKVSSLNFDIKYAKGVGERRAKILKKLGIETVKDLLWWLPRDYEDRRRIVPLSSIVADRKVTIRAKLQNFSVKKVKEyV 181
Cdd:PRK10917 1 PSLLLLLDAPLTSLKGVGPKTAEKLAKLGIHTVQDLLLHLPRRYEDRTRLKPIAELRPGEKVTVEGEVLSAEVVFGKR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 182 IISAVVSDGFGQIILKWF--NQEYITDRLIKEREYLITGIPKKTPFGpYEMNSPEIEEITG---RVPREILPLYSLSAGI 256
Cdd:PRK10917 80 RLTVTVSDGTGNLTLRFFnfNQPYLKKQLKVGKRVAVYGKVKRGKYG-LEMVHPEYEVLEEespELEGRLTPVYPLTEGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 257 SQKVMRKIVRKNITNVRLLKEFIPAEVIKERNLLPRHHAMYTVHFPKSLYELKESRRRLAYEELFLFEVAVLYNREKLKT 336
Cdd:PRK10917 159 KQKTLRKLIKQALELLDALPELLPEELLEKYGLLSLAEALRAIHFPPSDEDLHPARRRLKFEELFALQLSLLLLRAGRRS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 337 TKGGISKsISGKLAERFIDSLNFVLTGDQMRAFEEIREDMKAPTPMNRLLQGDVGSGKTVVAELAIIDNFEAGYQSAMMV 416
Cdd:PRK10917 239 KKAGPLP-YDGELLKKFLASLPFELTGAQKRVVAEILADLASPKPMNRLLQGDVGSGKTVVAALAALAAIEAGYQAALMA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 417 PTTVLATQQHQKLVKDLEPLGIKVELLVGSQKKSQQEEIKKRIAIGEVDVVVGTHALIQENVKFKDLGLVIIDEQHRFGV 496
Cdd:PRK10917 318 PTEILAEQHYENLKKLLEPLGIRVALLTGSLKGKERREILEAIASGEADIVIGTHALIQDDVEFHNLGLVIIDEQHRFGV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 497 KQREALMNKGALVDTLVMTATPIPRTLALTAYGDLDISTITEMPPGRAPIRTMLISEKRLPELYAFIRDEVNHGHQAFFI 576
Cdd:PRK10917 398 EQRLALREKGENPHVLVMTATPIPRTLAMTAYGDLDVSVIDELPPGRKPITTVVIPDSRRDEVYERIREEIAKGRQAYVV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 577 YPLIEESEQMDLKAATDEAERLQKEvFPDIGVELLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVMVIE 656
Cdd:PRK10917 478 CPLIEESEKLDLQSAEETYEELQEA-FPELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVMVIE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 657 HPERFGLAQLHQLRGRVGRSSLKSYCMLVLNSNISGEALDRLRKFAGTQNGFKLAEIDLSLRGPGEFMGTRQHGLPDFLV 736
Cdd:PRK10917 557 NAERFGLAQLHQLRGRVGRGAAQSYCVLLYKDPLSETARERLKIMRETNDGFVIAEKDLELRGPGELLGTRQSGLPEFKV 636
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 239505248 737 ADIVKDSELLIMARNDAMELLKRDPNLEkhnriiEEIKERFGENISLIEVG 787
Cdd:PRK10917 637 ADLVRDEELLEEARKDARELLERDPELA------EALLERWLGERERYDKA 681
|
|
| recG |
TIGR00643 |
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair] |
129-753 |
0e+00 |
|
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273192 [Multi-domain] Cd Length: 630 Bit Score: 717.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 129 LGIETVKDLLWWLPRDYEDRRRIVPLSSIVADRKVTIRAKLQNFSVKKVKEYVIISAVVSDGFGQII-LKWFNQEYITDR 207
Cdd:TIGR00643 1 LGIHTVQDLLFYFPRRYEDRTLLQTIGELLPGERATIVGEVLSHCIFGFKRRKVLKLRLKDGGYKKLeLRFFNRAFLKKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 208 LIKEREYLITGIPKKTPFGPYEMNSP-EIEEITGRVPREILPLYSLSAGISQKVMRKIVRKNITNV-RLLKEFIPAEVIK 285
Cdd:TIGR00643 81 FKVGSKVVVYGKVKSSKFKAYLIHPEfISEKDGVEFELKILPVYPLTEGLTQKKLRKLIQQALDQLdKSLEDPLPEELRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 286 ERNLLPRHHAMYTVHFPKSLYELKESRRRLAYEELFLFEVAVLYNREKLKTTKGGISKSISGKLAERFIDSLNFVLTGDQ 365
Cdd:TIGR00643 161 KYGLLSLEDALRAIHFPKTLSLLELARRRLIFDEFFYLQLAMLARRLGEKQQFSAPPANPSEELLTKFLASLPFKLTRAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 366 MRAFEEIREDMKAPTPMNRLLQGDVGSGKTVVAELAIIDNFEAGYQSAMMVPTTVLATQQHQKLVKDLEPLGIKVELLVG 445
Cdd:TIGR00643 241 KRVVKEILQDLKSDVPMNRLLQGDVGSGKTLVAALAMLAAIEAGYQVALMAPTEILAEQHYNSLRNLLAPLGIEVALLTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 446 SQKKSQQEEIKKRIAIGEVDVVVGTHALIQENVKFKDLGLVIIDEQHRFGVKQREALMNKG---ALVDTLVMTATPIPRT 522
Cdd:TIGR00643 321 SLKGKRRKELLETIASGQIHLVVGTHALIQEKVEFKRLALVIIDEQHRFGVEQRKKLREKGqggFTPHVLVMSATPIPRT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 523 LALTAYGDLDISTITEMPPGRAPIRTMLISEKRLPELYAFIRDEVNHGHQAFFIYPLIEESEQMDLKAATDEAERLqKEV 602
Cdd:TIGR00643 401 LALTVYGDLDTSIIDELPPGRKPITTVLIKHDEKDIVYEFIEEEIAKGRQAYVVYPLIEESEKLDLKAAEALYERL-KKA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 603 FPDIGVELLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVMVIEHPERFGLAQLHQLRGRVGRSSLKSYC 682
Cdd:TIGR00643 480 FPKYNVGLLHGRMKSDEKEAVMEEFREGEVDILVATTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYC 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239505248 683 MLVLNSNISGEALDRLRKFAGTQNGFKLAEIDLSLRGPGEFMGTRQHGLPDFLVADIVKDSELLIMARNDA 753
Cdd:TIGR00643 560 LLVYKNPKSESAKKRLRVMADTLDGFVIAEEDLELRGPGDLLGTKQSGYPEFRVADLVRDREILVEAREDA 630
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
315-540 |
4.88e-118 |
|
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: 355.30 E-value: 4.88e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 315 LAYEELFLFEVAVLYNREKLKTTKGgISKSISGKLAERFIDSLNFVLTGDQMRAFEEIREDMKAPTPMNRLLQGDVGSGK 394
Cdd:cd17992 1 LAFEELFALQLALLLRRRKIEELKG-IILEISGELLKKFLEALPFELTGAQKRVIDEILRDLASEKPMNRLLQGDVGSGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 395 TVVAELAIIDNFEAGYQSAMMVPTTVLATQQHQKLVKDLEPLGIKVELLVGSQKKSQQEEIKKRIAIGEVDVVVGTHALI 474
Cdd:cd17992 80 TVVAALAMLAAVENGYQVALMAPTEILAEQHYDSLKKLLEPLGIRVALLTGSTKAKEKREILEKIASGEIDIVIGTHALI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239505248 475 QENVKFKDLGLVIIDEQHRFGVKQREALMNKGALVDTLVMTATPIPRTLALTAYGDLDISTITEMP 540
Cdd:cd17992 160 QEDVEFHNLGLVIIDEQHRFGVEQRLKLREKGETPHVLVMTATPIPRTLALTLYGDLDVSIIDELP 225
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
351-730 |
1.48e-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: 358.59 E-value: 1.48e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 351 ERFIDSLNFVLTGDQMRAFEEIREDMKAPTPMNRLLQGDVGSGKTVVAELAIIDNFEAGYQSAMMVPTTVLATQQHQKLV 430
Cdd:TIGR00580 442 QEFEDSFPFEETPDQLKAIEEIKADMESPRPMDRLVCGDVGFGKTEVAMRAAFKAVLDGKQVAVLVPTTLLAQQHFETFK 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 431 KDLEPLGIKVELLVGSQKKSQQEEIKKRIAIGEVDVVVGTHALIQENVKFKDLGLVIIDEQHRFGVKQREALMNKGALVD 510
Cdd:TIGR00580 522 ERFANFPVTIELLSRFRSAKEQNEILKELASGKIDILIGTHKLLQKDVKFKDLGLLIIDEEQRFGVKQKEKLKELRTSVD 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 511 TLVMTATPIPRTLALTAYGDLDISTITEMPPGRAPIRTMLiSEKRLPELYAFIRDEVNHGHQAFFIYPLIEESEQMdlka 590
Cdd:TIGR00580 602 VLTLSATPIPRTLHMSMSGIRDLSIIATPPEDRLPVRTFV-MEYDPELVREAIRRELLRGGQVFYVHNRIESIEKL---- 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 591 atdeAERLQKEVfPDIGVELLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVMVIEHPERFGLAQLHQLR 670
Cdd:TIGR00580 677 ----ATQLRELV-PEARIAIAHGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIERADKFGLAQLYQLR 751
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239505248 671 GRVGRSSLKSYCMLVLNSN--ISGEALDRLR---KFAGTQNGFKLAEIDLSLRGPGEFMGTRQHG 730
Cdd:TIGR00580 752 GRVGRSKKKAYAYLLYPHQkaLTEDAQKRLEaiqEFSELGAGFKIALHDLEIRGAGNLLGEEQSG 816
|
|
| Mfd |
COG1197 |
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ... |
359-730 |
2.94e-106 |
|
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription];
Pssm-ID: 440810 [Multi-domain] Cd Length: 1130 Bit Score: 351.29 E-value: 2.94e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 359 FVLTGDQMRAFEEIREDMKAPTPMNRLLQGDVGSGKTVVAE----LAIIDnfeaGYQSAMMVPTTVLAtQQHQKLVKD-L 433
Cdd:COG1197 585 YEETPDQLRAIEEVKADMESPRPMDRLVCGDVGFGKTEVALraafKAVMD----GKQVAVLVPTTLLA-QQHYETFKErF 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 434 EPLGIKVELLvgS--QKKSQQEEIKKRIAIGEVDVVVGTHALIQENVKFKDLGLVIIDEQHRFGVKQREALMNKGALVDT 511
Cdd:COG1197 660 AGFPVRVEVL--SrfRTAKEQKETLEGLADGKVDIVIGTHRLLSKDVKFKDLGLLIIDEEQRFGVRHKEKLKALRANVDV 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 512 LVMTATPIPRTL--ALTayGDLDISTITEMPPGRAPIRT-------MLISEkrlpelyAfIRDEVNHGHQAFFIYPLIEE 582
Cdd:COG1197 738 LTLTATPIPRTLqmSLS--GIRDLSIIATPPEDRLPVKTfvgeyddALIRE-------A-ILRELLRGGQVFYVHNRVED 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 583 SEQMdlkaatdeAERLQKEVfPDIGVELLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVMVIEHPERFG 662
Cdd:COG1197 808 IEKV--------AARLQELV-PEARIAVAHGQMSERELERVMLDFYEGEFDVLVCTTIIETGIDIPNANTIIIERADRFG 878
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239505248 663 LAQLHQLRGRVGRSSLKSYCMLVL--NSNISGEALDRLRkfAGTQN-----GFKLAEIDLSLRGPGEFMGTRQHG 730
Cdd:COG1197 879 LAQLYQLRGRVGRSHRRAYAYLLYppDKVLTEDAEKRLE--AIQEFtelgaGFKLAMHDLEIRGAGNLLGEEQSG 951
|
|
| RecG_wedge |
pfam17191 |
RecG wedge domain; This DNA-binding domain has an OB-fold with large elaborations. |
111-272 |
9.70e-93 |
|
RecG wedge domain; This DNA-binding domain has an OB-fold with large elaborations.
Pssm-ID: 407316 [Multi-domain] Cd Length: 162 Bit Score: 287.03 E-value: 9.70e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 111 DIKYAKGVGERRAKILKKLGIETVKDLLWWLPRDYEDRRRIVPLSSIVADRKVTIRAKLQNFSVKKVKEYVIISAVVSDG 190
Cdd:pfam17191 1 PIKYAKGVGPKREKILKKLGIETIGDLIWYFPRDYEDRRKIIPISDIRHDEKVTTKGKIVNFETKKIGSLVIISAVLSDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 191 FGQIILKWFNQEYITDRLIKEREYLITGIPKKTPFGPYEMNSPEIEEITGRVPREILPLYSLSAGISQKVMRKIVRKNIT 270
Cdd:pfam17191 81 IGQVLLKWFNQEYIKKFLQKGKEVYITGTVKEGPFGPIEMNNPEIEEITGEQEREILPVYPLTEGISQKNMRKIVKENIS 160
|
..
gi 239505248 271 NV 272
Cdd:pfam17191 161 YV 162
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
353-730 |
8.23e-74 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 261.22 E-value: 8.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 353 FIDSLNFVLTGDQMRAFEEIREDMKAPTPMNRLLQGDVGSGKTVVAELAIIDNFEAGYQSAMMVPTTVLAtQQHQKLVKD 432
Cdd:PRK10689 593 FCDSFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLA-QQHYDNFRD 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 433 -LEPLGIKVELLVGSQKKSQQEEIKKRIAIGEVDVVVGTHALIQENVKFKDLGLVIIDEQHRFGVKQREALMNKGALVDT 511
Cdd:PRK10689 672 rFANWPVRIEMLSRFRSAKEQTQILAEAAEGKIDILIGTHKLLQSDVKWKDLGLLIVDEEHRFGVRHKERIKAMRADVDI 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 512 LVMTATPIPRTLALTAYGDLDISTITEMPPGRAPIRTMLISEKRLPELYAFIRdEVNHGHQAFFIYPLIEESEqmdlKAa 591
Cdd:PRK10689 752 LTLTATPIPRTLNMAMSGMRDLSIIATPPARRLAVKTFVREYDSLVVREAILR-EILRGGQVYYLYNDVENIQ----KA- 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 592 tdeAERLQkEVFPDIGVELLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVMVIEHPERFGLAQLHQLRG 671
Cdd:PRK10689 826 ---AERLA-ELVPEARIAIGHGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLRG 901
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239505248 672 RVGRSSLKSYCMLvLNSN---ISGEALDRLRKFAGTQN---GFKLAEIDLSLRGPGEFMGTRQHG 730
Cdd:PRK10689 902 RVGRSHHQAYAWL-LTPHpkaMTTDAQKRLEAIASLEDlgaGFALATHDLEIRGAGELLGEEQSG 965
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
347-537 |
1.40e-71 |
|
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: 232.46 E-value: 1.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 347 GKLAERFIDSLNFVLTGDQMRAFEEIREDMKAPTPMNRLLQGDVGSGKTVVAELAIIDNFEAGYQSAMMVPTTVLATQQH 426
Cdd:cd17991 2 GEEQEEFEASFPYEETPDQLKAIEEILKDMESGKPMDRLICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQHY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 427 QKLVKDLEPLGIKVELLVGSQKKSQQEEIKKRIAIGEVDVVVGTHALIQENVKFKDLGLVIIDEQHRFGVKQREALMNKG 506
Cdd:cd17991 82 ETFKERFANFPVNVELLSRFTTAAEQREILEGLKEGKVDIVIGTHRLLSKDVEFKNLGLLIIDEEQRFGVKQKEKLKELR 161
|
170 180 190
....*....|....*....|....*....|.
gi 239505248 507 ALVDTLVMTATPIPRTLALTAYGDLDISTIT 537
Cdd:cd17991 162 PNVDVLTLSATPIPRTLHMALSGIRDLSVIA 192
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
545-703 |
2.12e-71 |
|
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: 230.69 E-value: 2.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 545 PIRTMLISEKRLPELYAFIRDEVNHGHQAFFIYPLIEESEQMDLKAATDEAERLQKEVFPDIGVELLHGRMSDEEKNRIM 624
Cdd:cd18811 1 PITTYLIFHTRLDKVYEFVREEIAKGRQAYVIYPLIEESEKLDLKAAVAMYEYLKERFRPELNVGLLHGRLKSDEKDAVM 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239505248 625 HRFKNKEAMILVSTSVVEVGIDIPTATVMVIEHPERFGLAQLHQLRGRVGRSSLKSYCMLVLNSNISGEALDRLRKFAG 703
Cdd:cd18811 81 AEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYKDPLTETAKQRLRVMTE 159
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
347-537 |
1.51e-67 |
|
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: 221.14 E-value: 1.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 347 GKLAERFIDSLNFVLTGDQMRAFEEIREDMKAPTPMNRLLQGDVGSGKTVVAELAIIDNFEAGYQSAMMVPTTVLATQQH 426
Cdd:cd17918 2 RALIQELCKSLPFSLTKDQAQAIKDIEKDLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 427 QKLVKDLEPlgIKVELLVGSQKKSQQEEIkkriaigevDVVVGTHALIQENVKFKDLGLVIIDEQHRFGVKQREALMNKG 506
Cdd:cd17918 82 EEARKFLPF--INVELVTGGTKAQILSGI---------SLLVGTHALLHLDVKFKNLDLVIVDEQHRFGVAQREALYNLG 150
|
170 180 190
....*....|....*....|....*....|.
gi 239505248 507 AlVDTLVMTATPIPRTLALTAYGDLDISTIT 537
Cdd:cd17918 151 A-THFLEATATPIPRTLALALSGLLDLSVID 180
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
545-703 |
1.74e-63 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 209.43 E-value: 1.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 545 PIRTMLISEKRLPELYAFIRDEVNHGHQAFFIYPLIEESEQMDLKAATDEAERLqKEVFPDIGVELLHGRMSDEEKNRIM 624
Cdd:cd18792 1 PIRTYVIPHDDLDLVYEAIERELARGGQVYYVYPRIEESEKLDLKSIEALAEEL-KELVPEARVALLHGKMTEDEKEAVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 625 HRFKNKEAMILVSTSVVEVGIDIPTATVMVIEHPERFGLAQLHQLRGRVGRSSLKSYCMLVLNSNISG--EALDRLRKFA 702
Cdd:cd18792 80 LEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYPDPKKLteTAKKRLRAIA 159
|
.
gi 239505248 703 G 703
Cdd:cd18792 160 E 160
|
|
| RecG_N |
pfam17190 |
RecG N-terminal helical domain; This four helical bundle domain is found at the N-terminus of ... |
2-90 |
2.09e-33 |
|
RecG N-terminal helical domain; This four helical bundle domain is found at the N-terminus of bacterial RecG proteins.
Pssm-ID: 407315 Cd Length: 89 Bit Score: 123.29 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 2 LLEDYLDRCEKLLEKFLSGKVDTIELIQEIKRGAELLEPEELSANEGLKDYIGKFVSYYLPLASLPNERQHLRVKNGFTM 81
Cdd:pfam17190 1 LLEEFLDECEQLLKKVLNGKLKTNELIEEIKDNLSLLDDPLLENEEGLKEKLGQFLEYYKPIANLPPERAIKRLKNGLEM 80
|
....*....
gi 239505248 82 INKLRGKFL 90
Cdd:pfam17190 81 IEKLRYWFL 89
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
545-699 |
8.26e-33 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 123.99 E-value: 8.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 545 PIRTMLiSEKRLPELYAFIRDEVNHGHQAFFIYPLIEESEqmdlkaatdEAERLQKEVFPDIGVELLHGRMSDEEKNRIM 624
Cdd:cd18810 1 PVRTYV-MPYDDELIREAIERELLRGGQVFYVHNRIESIE---------KLATQLRQLVPEARIAIAHGQMTENELEEVM 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239505248 625 HRFKNKEAMILVSTSVVEVGIDIPTATVMVIEHPERFGLAQLHQLRGRVGRSSLKSYCMLVLNSN--ISGEALDRLR 699
Cdd:cd18810 71 LEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKERAYAYFLYPDQkkLTEDALKRLE 147
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
362-524 |
8.39e-28 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 110.02 E-value: 8.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 362 TGDQMRAFEEIREDMkaptpmNRLLQGDVGSGKTVVAELAIIDNFE---AGYQSAMMVPTTVLATQQHQKLVKDLEPLGI 438
Cdd:pfam00270 1 TPIQAEAIPAILEGR------DVLVQAPTGSGKTLAFLLPALEALDkldNGPQALVLAPTRELAEQIYEELKKLGKGLGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 439 KVELLVGSQKKSQQEEikkriAIGEVDVVVGTH----ALIQENVKFKDLGLVIIDEQHRFGVKQREALMNK-----GALV 509
Cdd:pfam00270 75 KVASLLGGDSRKEQLE-----KLKGPDILVGTPgrllDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEilrrlPKKR 149
|
170
....*....|....*
gi 239505248 510 DTLVMTATPiPRTLA 524
Cdd:pfam00270 150 QILLLSATL-PRNLE 163
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
353-546 |
3.70e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 101.03 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 353 FIDSLNFVLTGDQMRAFEEIREDMKaptpmNRLLQGDVGSGKTVVAELAIIDNF--EAGYQSAMMVPTTVLATQQHQKLV 430
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLR-----DVILAAPTGSGKTLAALLPALEALkrGKGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 431 KDLEPLGIKVELLVGSQKKsqqEEIKKRIAIGEVDVVVGT-----HALIQENVKFKDLGLVIIDEQHRFGVK-QREALMN 504
Cdd:smart00487 76 KLGPSLGLKVVGLYGGDSK---REQLRKLESGKTDILVTTpgrllDLLENDKLSLSNVDLVILDEAHRLLDGgFGDQLEK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 239505248 505 KGALVD----TLVMTATPIPRTLALTAYGDLDISTITEMPPGRAPI 546
Cdd:smart00487 153 LLKLLPknvqLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPI 198
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
382-517 |
8.21e-20 |
|
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: 86.69 E-value: 8.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 382 MNRLLQGDVGSGKTVVAELAIIDNF-EAGYQSAMMVPTTVLATQQHQKLvKDLEPLGIKVELLVGSQKKSQQEEIKKRIA 460
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLlKKGKKVLVLVPTKALALQTAERL-RELFGPGIRVAVLVGGSSAEEREKNKLGDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 461 igevDVVVGTHALIQENVK------FKDLGLVIIDEQHRFGVKQREALMNKGAL-------VDTLVMTAT 517
Cdd:cd00046 81 ----DIIIATPDMLLNLLLredrlfLKDLKLIIVDEAHALLIDSRGALILDLAVrkaglknAQVILLSAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
365-786 |
1.05e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 93.55 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 365 QMRAFEEIREDMKAPTPMNrLLQGDVGSGKTVVAeLAIIDNFEAGYQSAMMVPTTVLATQQHQKLVKDLeplgiKVELLV 444
Cdd:COG1061 85 QQEALEALLAALERGGGRG-LVVAPTGTGKTVLA-LALAAELLRGKRVLVLVPRRELLEQWAEELRRFL-----GDPLAG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 445 GSQKKSQQeeikkriaigevDVVVGTHALIQENVKFKDL----GLVIIDEQHRFGVKQREALMNKGALVDTLVMTATPIp 520
Cdd:COG1061 158 GGKKDSDA------------PITVATYQSLARRAHLDELgdrfGLVIIDEAHHAGAPSYRRILEAFPAAYRLGLTATPF- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 521 RTLALTAYGDLDISTITEMPPGRApirtmlISEKRLPELYAF-IRDEVNHGHQAFFIYP------LIEESEQMDLKAA-- 591
Cdd:COG1061 225 RSDGREILLFLFDGIVYEYSLKEA------IEDGYLAPPEYYgIRVDLTDERAEYDALSerlreaLAADAERKDKILRel 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 592 ----------------TDEAERLQKEvFPDIG--VELLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVM 653
Cdd:COG1061 299 lrehpddrktlvfcssVDHAEALAEL-LNEAGirAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 654 VIehperfgLA------QLHQLRGRVGRSSL-KSYCMLVlnsNISGEALDRLRKFAGTQ-----NGFKLAEIDLSLRGPG 721
Cdd:COG1061 378 IL-------LRptgsprEFIQRLGRGLRPAPgKEDALVY---DFVGNDVPVLEELAKDLrdlagYRVEFLDEEESEELAL 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239505248 722 EFMGTRQHGLPDFLVADIVKDSELLIMARNDAMELLKRDPNLEKHNRIIEEIKERFGENISLIEV 786
Cdd:COG1061 448 LIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEK 512
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
595-675 |
1.48e-17 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 78.02 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 595 AERLQKEvfpDIGVELLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVMVIEHPeRFGLAQLHQLRGRVG 674
Cdd:smart00490 4 AELLKEL---GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL-PWSPASYIQRIGRAG 79
|
.
gi 239505248 675 R 675
Cdd:smart00490 80 R 80
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
605-675 |
2.26e-17 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 78.41 E-value: 2.26e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239505248 605 DIGVELLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVMVIEHPErFGLAQLHQLRGRVGR 675
Cdd:pfam00271 38 GIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLP-WNPASYIQRIGRAGR 107
|
|
| RecG_dom3_C |
pfam19833 |
ATP-dependent DNA helicase RecG, domain 3, C-terminal; This domain is found in ATP-dependent ... |
704-781 |
1.25e-14 |
|
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: 69.81 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 704 TQNGFKLAEIDLSLRGPGEFMGTRQHGLP-DFLVADIVKDSELLIMARNDAMELLKRDPNLEK-HNRII-EEIKERFGEN 780
Cdd:pfam19833 1 TNDGFEIAEADLKLRGPGDLEGTQQSGIAfDLKIADIARDGQLLQLARTEAEEIIDNDPECSLpENAVLwRQLKELRKTN 80
|
.
gi 239505248 781 I 781
Cdd:pfam19833 81 I 81
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
357-676 |
4.01e-14 |
|
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: 75.30 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 357 LNFVLTGDQMRAFEEIREDMKAPTPMnrLLQGDVGSGKTvvaelaiidnfEagyqsaMMVPTTVLATQQHQKL------- 429
Cdd:COG4098 107 WEGTLTPAQQKASDELLEAIKKKEEH--LVWAVCGAGKT-----------E------MLFPAIAEALKQGGRVciatprv 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 430 --VKDLEP------LGIKVELLVG-SQKKSQQEEIkkriaigevdVVVGTHALIqenvKFKD-LGLVIIDE--------- 490
Cdd:COG4098 168 dvVLELAPrlqqafPGVDIAALYGgSEEKYRYAQL----------VIATTHQLL----RFYQaFDLLIIDEvdafpysgd 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 491 -QHRFGVKQreALMNKGALVdtlVMTATPiPRTL-ALTAYGDLDISTItempPGR-------APIRTML------ISEKR 555
Cdd:COG4098 234 pMLQYAVKR--ARKPDGKLI---YLTATP-SKALqRQVKRGKLKVVKL----PARyhghplpVPKFKWLgnwkkrLRRGK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 556 LPE-LYAFIRDEVNHGHQAFFIYPLIEESEQmdlkaatdeAERLQKEVFPDIGVELLHGrmSDEEKNRIMHRFKNKEAMI 634
Cdd:COG4098 304 LPRkLLKWLKKRLKEGRQLLIFVPTIELLEQ---------LVALLQKLFPEERIAGVHA--EDPERKEKVQAFRDGEIPI 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 239505248 635 LVSTSVVEVGIDIPTATVMVI--EHPeRFGLAQLHQLRGRVGRS 676
Cdd:COG4098 373 LVTTTILERGVTFPNVDVAVLgaDHP-VFTEAALVQIAGRVGRS 415
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
391-681 |
1.30e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 74.16 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 391 GSGKTVVAELAIIDNFEAGYQSAMMVPTTVLATQQHQKLVKDLEPLGIKVELLVGsqkksqqEEIKKRIAIGEVDVVVGT 470
Cdd:COG1204 48 ASGKTLIAELAILKALLNGGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTG-------DYDSDDEWLGRYDILVAT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 471 ----HALIQENVKF-KDLGLVIIDEQHRFGVKQRealmnkGALVDTLV---MTATPIPRTLALTAY------------GD 530
Cdd:COG1204 121 peklDSLLRNGPSWlRDVDLVVVDEAHLIDDESR------GPTLEVLLarlRRLNPEAQIVALSATignaeeiaewldAE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 531 LDISTITemppgraPIRTML------------ISEKRLPELYAFIRDEVNHGHQA--FF----------------IYPLI 580
Cdd:COG1204 195 LVKSDWR-------PVPLNEgvlydgvlrfddGSRRSKDPTLALALDLLEEGGQVlvFVssrrdaeslakkladeLKRRL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 581 EESEQMDLKAATDEAERLQKEVFP-DIGVELL-------HGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATV 652
Cdd:COG1204 268 TPEEREELEELAEELLEVSEETHTnEKLADCLekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRV 347
|
330 340 350
....*....|....*....|....*....|....
gi 239505248 653 mVIEHPERFGLAQL-----HQLRGRVGRSSLKSY 681
Cdd:COG1204 348 -IIRDTKRGGMVPIpvlefKQMAGRAGRPGYDPY 380
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
358-681 |
1.73e-13 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 74.15 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 358 NFVLTGDQMRAFEEIREDMkaptpmNRLLQGDVGSGKTVVAELAIIDNFEAGYQSAMMVPTTVLATQQHQKLVKdLEPLG 437
Cdd:PRK01172 20 DFELYDHQRMAIEQLRKGE------NVIVSVPTAAGKTLIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELSR-LRSLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 438 IKVELLVGSQKKSQQeeikkriAIGEVDVVVGTH----ALIQENVK-FKDLGLVIIDEQHRFGVKQRealmnkGALVDTL 512
Cdd:PRK01172 93 MRVKISIGDYDDPPD-------FIKRYDVVILTSekadSLIHHDPYiINDVGLIVADEIHIIGDEDR------GPTLETV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 513 VMTA---TPIPRTLALTAYGD--------LDISTI-TEMPPgrAPIRTMLISEKRL---------PELYAFIRDEVNHGH 571
Cdd:PRK01172 160 LSSAryvNPDARILALSATVSnanelaqwLNASLIkSNFRP--VPLKLGILYRKRLildgyersqVDINSLIKETVNDGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 572 QAFFIYPLIEESEQM------------DLKAATDEAErlqkeVFPDIGVELL-------HGRMSDEEKNRIMHRFKNKEA 632
Cdd:PRK01172 238 QVLVFVSSRKNAEDYaemliqhfpefnDFKVSSENNN-----VYDDSLNEMLphgvafhHAGLSNEQRRFIEEMFRNRYI 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 239505248 633 MILVSTSVVEVGIDIPTATVmVIEHPERFGLA--------QLHQLRGRVGRSSLKSY 681
Cdd:PRK01172 313 KVIVATPTLAAGVNLPARLV-IVRDITRYGNGgirylsnmEIKQMIGRAGRPGYDQY 368
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
365-527 |
1.94e-12 |
|
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: 66.52 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 365 QMRAFEEIRED-----MKAPTpmnrllqgdvGSGKTVVAELAIIDNFEAGYQSAM-MVPTTVLATQQHQKLVKDLEPLGI 438
Cdd:cd17921 6 QREALRALYLSgdsvlVSAPT----------SSGKTLIAELAILRALATSGGKAVyIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 439 KVELLVGSQKKSQQEEIKKriaigevDVVVGT----HALIQ--ENVKFKDLGLVIIDEQHRFGVKQRealmnkGALVDTL 512
Cdd:cd17921 76 NVGLLTGDPSVNKLLLAEA-------DILVATpeklDLLLRngGERLIQDVRLVVVDEAHLIGDGER------GVVLELL 142
|
170
....*....|....*...
gi 239505248 513 V---MTATPIPRTLALTA 527
Cdd:cd17921 143 LsrlLRINKNARFVGLSA 160
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
365-518 |
1.03e-11 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350687 [Multi-domain] Cd Length: 178 Bit Score: 64.15 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 365 QMRAFEEIRE--DMKAPTpmnrLLQGDVGSGKTVVAELAIIDNFEAGYQSAMMVPTTVLATQqhqkLVKDLEP-LGIKVE 441
Cdd:cd17929 1 QRKAYEAIVSslGGFKTF----LLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTPQ----LIKRFKKrFGDKVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 442 LLVGSQKKSQQEEIKKRIAIGEVDVVVGTH-ALIqenVKFKDLGLVIIDEQHRFGVKQ--------REALMNKGALVD-T 511
Cdd:cd17929 73 VLHSKLSDKERADEWRKIKRGEAKVVIGARsALF---APFKNLGLIIVDEEHDSSYKQdsgpryhaRDVAIYRAKLENaP 149
|
....*...
gi 239505248 512 LVM-TATP 518
Cdd:cd17929 150 VVLgSATP 157
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
377-675 |
2.82e-11 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 66.32 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 377 KAPTPMN-----RLLQG-DV------GSGKTVVAELAIIDNFEAGYQSA----MMVPTTVLATQQHQKLVKDLEPLGIKV 440
Cdd:COG0513 23 TTPTPIQaqaipLILAGrDVlgqaqtGTGKTAAFLLPLLQRLDPSRPRApqalILAPTRELALQVAEELRKLAKYLGLRV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 441 ELLVGSQK-KSQQEEIKKRiaigeVDVVVGT----HALI-QENVKFKDLGLVIIDEqhrfgvkqrealmnkgalVDtlvm 514
Cdd:COG0513 103 ATVYGGVSiGRQIRALKRG-----VDIVVATpgrlLDLIeRGALDLSGVETLVLDE------------------AD---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 515 tatpipRTLaltaygDL----DISTI-TEMPPGRapiRTMLISE---KRLPEL-YAFIRD-------------------- 565
Cdd:COG0513 156 ------RML------DMgfieDIERIlKLLPKER---QTLLFSAtmpPEIRKLaKRYLKNpvrievapenataetieqry 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 566 -EVNHGHQAFFIYPLIEEsEQMDL-------KAATDE-AERLQKEvfpDIGVELLHGRMSDEEKNRIMHRFKNKEAMILV 636
Cdd:COG0513 221 yLVDKRDKLELLRRLLRD-EDPERaivfcntKRGADRlAEKLQKR---GISAAALHGDLSQGQRERALDAFRNGKIRVLV 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 239505248 637 STSVVEVGIDIPTATvMVI-----EHPERFglaqLHqlR-GRVGR 675
Cdd:COG0513 297 ATDVAARGIDIDDVS-HVInydlpEDPEDY----VH--RiGRTGR 334
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
365-527 |
9.42e-11 |
|
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: 61.90 E-value: 9.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 365 QMRAFEEIREDmkaptpmNRLLQGDVGSGKTVVAELAI-------IDNFEAGYQSAMMVPTTVLATQQHQKLVKDLeplG 437
Cdd:cd18034 7 QLELFEAALKR-------NTIVVLPTGSGKTLIAVMLIkemgelnRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHT---D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 438 IKVELLVGSQKKSQQEEIKKRIAIGEVDVVVGT-----HALIQENVKFKDLGLVIIDEQHRfGVKqrEALMNKGALVDTL 512
Cdd:cd18034 77 LKVGEYSGEMGVDKWTKERWKEELEKYDVLVMTaqillDALRHGFLSLSDINLLIFDECHH-ATG--DHPYARIMKEFYH 153
|
170
....*....|....*
gi 239505248 513 VMTATPIPRTLALTA 527
Cdd:cd18034 154 LEGRTSRPRILGLTA 168
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
332-647 |
2.31e-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: 63.95 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 332 EKLKTTKGGISKSISGKLAERFIDSLNFVLTGDQMR--AFEEIREDMK---------APTpmnrllqgdvGSGKTVVAeL 400
Cdd:COG1203 97 ANFDMARQALDHLLAERLERLLPKKSKPRTPINPLQneALELALEAAEeepglfiltAPT----------GGGKTEAA-L 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 401 AIIDNFEAGYQSAMMV---PTTVLATQQHQKLVKDLEP-LGI---KVELLVGSQKKSQQEEIKKRIAIGEV---DVVVGT 470
Cdd:COG1203 166 LFALRLAAKHGGRRIIyalPFTSIINQTYDRLRDLFGEdVLLhhsLADLDLLEEEEEYESEARWLKLLKELwdaPVVVTT 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 471 -----HALIqENVKFKDLGL-------VIIDEQHRFGVKQREALMnkgALVDTL--------VMTAT--PIPRTLALTAY 528
Cdd:COG1203 246 idqlfESLF-SNRKGQERRLhnlansvIILDEVQAYPPYMLALLL---RLLEWLknlggsviLMTATlpPLLREELLEAY 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 529 GDLDISTITEMPPGRAPI--RTMLISEKR-LPELYAFIRDEVNHGHQAFFIYPLIeeseqmdlKAATDEAERLqKEVFPD 605
Cdd:COG1203 322 ELIPDEPEELPEYFRAFVrkRVELKEGPLsDEELAELILEALHKGKSVLVIVNTV--------KDAQELYEAL-KEKLPD 392
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 239505248 606 IGVELLHGRMSDEEK----NRIMHRFKNKEAMILVSTSVVEVGIDI 647
Cdd:COG1203 393 EEVYLLHSRFCPADRseieKEIKERLERGKPCILVSTQVVEAGVDI 438
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
360-500 |
8.58e-09 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 59.01 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 360 VLTGDQMRAFEEIREDMK-APTpmnrLLQGDVGSGKT-----VVAELaiidnFEAGYQSAMMVPTTVLaTQQHQKLVKdl 433
Cdd:PRK05580 144 TLNPEQAAAVEAIRAAAGfSPF----LLDGVTGSGKTevylqAIAEV-----LAQGKQALVLVPEIAL-TPQMLARFR-- 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239505248 434 EPLGIKVELLVGSQKKSQQEEIKKRIAIGEVDVVVGTH-ALIqenVKFKDLGLVIIDEQHRFGVKQRE 500
Cdd:PRK05580 212 ARFGAPVAVLHSGLSDGERLDEWRKAKRGEAKVVIGARsALF---LPFKNLGLIIVDEEHDSSYKQQE 276
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
384-542 |
9.52e-09 |
|
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: 55.80 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 384 RLLQGD-------VGSGKTVVaeLAIIDNFEA--GYQSAMMVPTTVLATQQHQKLVKDLEPLGIKVELLV--GSQKKSQQ 452
Cdd:cd17924 28 RLLRGKsfaiiapTGVGKTTF--GLATSLYLAskGKRSYLIFPTKSLVKQAYERLSKYAEKAGVEVKILVyhSRLKKKEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 453 EEIKKRIAIGEVDVVVGTHALIQENV---KFKDLGLVIIDEqhrfgvkqrealmnkgalVDTLVMTATPIPRTLALTAYG 529
Cdd:cd17924 106 EELLEKIEKGDFDILVTTNQFLSKNFdllSNKKFDFVFVDD------------------VDAVLKSSKNIDRLLKLLGFG 167
|
170
....*....|...
gi 239505248 530 DLDISTITEMPPG 542
Cdd:cd17924 168 QLVVSSATGRPRG 180
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
589-675 |
3.95e-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: 52.51 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 589 KAATDE-AERLQKEVFPdigVELLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVmVI-----EHPERFg 662
Cdd:cd18787 37 KKRVDRlAELLEELGIK---VAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVDH-VInydlpRDAEDY- 111
|
90
....*....|....
gi 239505248 663 laqLHqlR-GRVGR 675
Cdd:cd18787 112 ---VH--RiGRTGR 120
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
383-527 |
1.71e-07 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 51.95 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 383 NRLLQGDVGSGKTVVAELAIIDNFEAGYQSAMMVPTTVLATQQHQKLvKDLEPLGIKVELLVGSQKKSQQeeikkriAIG 462
Cdd:cd18028 19 NLLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEF-KKLEEIGLKVGISTGDYDEDDE-------WLG 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239505248 463 EVDVVVGTHALIQENVKFK-----DLGLVIIDEQHRFGVKQRealmnkGALVDTLV---MTATPIPRTLALTA 527
Cdd:cd18028 91 DYDIIVATYEKFDSLLRHSpswlrDVGVVVVDEIHLISDEER------GPTLESIVarlRRLNPNTQIIGLSA 157
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
365-490 |
6.17e-07 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 50.52 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 365 QMRAFEEIRED----MKAPTpmnrllqgdvGSGKT---VVAELAIIDNFEAGYQSAM----MVPTTVLATQQHQKLVKDL 433
Cdd:cd00268 17 QAQAIPLILSGrdviGQAQT----------GSGKTlafLLPILEKLLPEPKKKGRGPqalvLAPTRELAMQIAEVARKLG 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239505248 434 EPLGIKVELLVGSQKKSQQEEIKKRIaigeVDVVVGT----HALIQE-NVKFKDLGLVIIDE 490
Cdd:cd00268 87 KGTGLKVAAIYGGAPIKKQIEALKKG----PDIVVGTpgrlLDLIERgKLDLSNVKYLVLDE 144
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
359-492 |
7.51e-07 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 52.81 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 359 FVLTGDQMRAFEEIREDMKAPTPMnrLLQGDVGSGKTVVAeLAIIDNF-EAGYQSAMMVPTTVLATQqhqkLVKDLEP-L 436
Cdd:COG1198 194 PTLNEEQQAAVEAIRAAAGGFSVF--LLHGVTGSGKTEVY-LQAIAEVlAQGKQALVLVPEIALTPQ----TVERFRArF 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 437 GIKVELLVGSQKKSQQEEIKKRIAIGEVDVVVGTH-ALiqenvkF---KDLGLVIIDEQH 492
Cdd:COG1198 267 GARVAVLHSGLSDGERLDEWRRARRGEARIVIGTRsAL------FapfPNLGLIIVDEEH 320
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
391-527 |
1.44e-06 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 49.74 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 391 GSGKTVVAELAI---IDNFEAGYQS--AMMVPTTVLATQQHQKLVKDLEPLGIKVELLVG--SQKKSQQEEIKKRiaige 463
Cdd:cd17927 27 GSGKTFVAVLICehhLKKFPAGRKGkvVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGdtSENVSVEQIVESS----- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239505248 464 vDVVVGTHALIQ------ENVKFKDLGLVIIDEQHRfgvKQREALMNKGA--LVDTLVMTATPIPRTLALTA 527
Cdd:cd17927 102 -DVIIVTPQILVndlksgTIVSLSDFSLLVFDECHN---TTKNHPYNEIMfrYLDQKLGSSGPLPQILGLTA 169
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
391-518 |
2.26e-06 |
|
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: 48.07 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 391 GSGKTVVAELAIIDNFEAGyqSAMMVPTTVLATQQHQKLVKDLEPlgikvellvgSQKKSQQEEIKKRIAIGEVDVvvgt 470
Cdd:cd17926 28 GSGKTLTALALIAYLKELR--TLIVVPTDALLDQWKERFEDFLGD----------SSIGLIGGGKKKDFDDANVVV---- 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 239505248 471 hALIQ------ENVK--FKDLGLVIIDEQHRFGVKQ-REALMNKGALVdTLVMTATP 518
Cdd:cd17926 92 -ATYQslsnlaEEEKdlFDQFGLLIVDEAHHLPAKTfSEILKELNAKY-RLGLTATP 146
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
620-675 |
3.33e-06 |
|
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: 45.39 E-value: 3.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 239505248 620 KNRIMHRFKNKEAM-ILVSTSVVEVGIDIPTATVMVIEHPERFgLAQLHQLRGRVGR 675
Cdd:cd18785 10 TNSIEHAEEIASSLeILVATNVLGEGIDVPSLDTVIFFDPPSS-AASYIQRVGRAGR 65
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
385-679 |
4.32e-06 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 49.74 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 385 LLQGDVGSGKTVVA---ELAIIDNFEAGyQSAMMVPTTVLATQQHQKLVKDL--EPLGIKVELLVGSQKKSQQEEIKK-- 457
Cdd:cd09639 3 VIEAPTGYGKTEAAllwALHSLKSQKAD-RVIIALPTRATINAMYRRAKEAFgeTGLYHSSILSSRIKEMGDSEEFEHlf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 458 --------------------RIAIGEVDVVVGTHALIQENVKfkdLGLVIIDEQHRFG-------VKQREALMNKGALVd 510
Cdd:cd09639 82 plyihsndtlfldpitvctiDQVLKSVFGEFGHYEFTLASIA---NSLLIFDEVHFYDeytlaliLAVLEVLKDNDVPI- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 511 tLVMTATpIPRTLALTAYG-DLDISTITEMPPGRAPIRTMLISEKRLPELYAFIR--DEVNHGHQAFFIYPLIEESEQMD 587
Cdd:cd09639 158 -LLMSAT-LPKFLKEYAEKiGYVEENEPLDLKPNERAPFIKIESDKVGEISSLERllEFIKKGGSVAIIVNTVDRAQEFY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 588 LKAatdeaerlqKEVFPDIGVELLHGRMS--DEEK--NRIMHRFKNKEAMILVSTSVVEVGIDIpTATVMVIEHPErfgL 663
Cdd:cd09639 236 QQL---------KEKGPEEEIMLIHSRFTekDRAKkeAELLLEFKKSEKFVIVATQVIEASLDI-SVDVMITELAP---I 302
|
330
....*....|....*.
gi 239505248 664 AQLHQLRGRVGRSSLK 679
Cdd:cd09639 303 DSLIQRLGRLHRYGEK 318
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
392-492 |
8.05e-06 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 49.50 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 392 SGKTVVAELAIIDNFEAGyQSAM--MVPTTVLATQQHQKLVKDLEPlGIKVELLVGSQkksqqeeikkRIAIGE------ 463
Cdd:COG1202 236 TGKTLIGELAGIKNALEG-KGKMlfLVPLVALANQKYEDFKDRYGD-GLDVSIRVGAS----------RIRDDGtrfdpn 303
|
90 100 110
....*....|....*....|....*....|....
gi 239505248 464 VDVVVGT-----HALIQENvKFKDLGLVIIDEQH 492
Cdd:COG1202 304 ADIIVGTyegidHALRTGR-DLGDIGTVVIDEVH 336
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
163-238 |
1.01e-05 |
|
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Pssm-ID: 460164 [Multi-domain] Cd Length: 75 Bit Score: 44.15 E-value: 1.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239505248 163 VTIRAKLQNFSVKKVKeyvIISAVVSDGFGQIILKWFNQEY--ITDRLIKEREYLITGIPKKTPFGPYEMNSPEIEEI 238
Cdd:pfam01336 1 VTVAGRVTSIRRSGGK---LLFLTLRDGTGSIQVVVFKEEAekLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIELL 75
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
391-503 |
1.03e-05 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 47.21 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 391 GSGKTVVAELAIIDNFEAGYQSAMMV-PTTVLATQQHQKLVKDLEPLGIKVELLVGSQKKSQQEEIKKRiaigevDVVVG 469
Cdd:cd18026 43 SGGKTLVAEILMLKRLLERRKKALFVlPYVSIVQEKVDALSPLFEELGFRVEGYAGNKGRSPPKRRKSL------SVAVC 116
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 239505248 470 T----HALIQ---ENVKFKDLGLVIIDEQHRFGVKQREALM 503
Cdd:cd18026 117 TiekaNSLVNsliEEGRLDELGLVVVDELHMLGDGHRGALL 157
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
340-696 |
1.04e-05 |
|
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: 49.06 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 340 GISKSISGKLAERFIDSL-NFvltgdQMRAFEEIRED----MKAPTpmnrllqgdvGSGKTVVAELAIIDNFEAGYQS-A 413
Cdd:COG1205 40 WLPPELRAALKKRGIERLySH-----QAEAIEAARAGknvvIATPT----------ASGKSLAYLLPVLEALLEDPGAtA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 414 MMV-PTTVLATQQHQKLVK--DLEPLGIKVELLVGSQKKSQQEEIKKRiaigeVDVVVGT-----------HALIQENvk 479
Cdd:COG1205 105 LYLyPTKALARDQLRRLRElaEALGLGVRVATYDGDTPPEERRWIREH-----PDIVLTNpdmlhygllphHTRWARF-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 480 FKDLGLVIIDEQHR----FG--VKQ-----REALMNKGALVDTLVMTATpI--PRTLA--LTaygDLDISTITE------ 538
Cdd:COG1205 178 FRNLRYVVIDEAHTyrgvFGshVANvlrrlRRICRHYGSDPQFILASAT-IgnPAEHAerLT---GRPVTVVDEdgsprg 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 539 -------MPP-GRAPIRTMLISE-KRLpelyafIRDEVNHGHQ--AFFiyplieESEQMDLKAATDEAERLQKEVFPDiG 607
Cdd:COG1205 254 ertfvlwNPPlVDDGIRRSALAEaARL------LADLVREGLRtlVFT------RSRRGAELLARYARRALREPDLAD-R 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 608 VELLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPT--ATVMViehperfG----LAQLHQLRGRVGRSSLKSY 681
Cdd:COG1205 321 VAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGldAVVLA-------GypgtRASFWQQAGRAGRRGQDSL 393
|
410
....*....|....*
gi 239505248 682 CMLVLNSNisgeALD 696
Cdd:COG1205 394 VVLVAGDD----PLD 404
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
383-501 |
2.47e-05 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 47.89 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 383 NRLLQGDVGSGKTVVAELAIIDN-FEAGYQSAMMVPTTVLATQQHQKLvKDLEPLGIKVELLVGSQKKSQQeeikkriAI 461
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMVNKlLREGGKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYDSTDE-------WL 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 239505248 462 GEVDVVVGT----HALIQENVKF-KDLGLVIIDEQHRFGVKQREA 501
Cdd:PRK00254 113 GKYDIIIATaekfDSLLRHGSSWiKDVKLVVADEIHLIGSYDRGA 157
|
|
| RecG_wedge_OBF |
cd04488 |
RecG_wedge_OBF: A subfamily of OB folds corresponding to the OB fold found in the N-terminal ... |
164-236 |
2.65e-05 |
|
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: 42.95 E-value: 2.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239505248 164 TIRAKLQNFSVKKVKEYVIISAVVSDGFGQIILKWFN-QEYITDRLIKEREYLITGIPKKTPFGPyEMNSPEIE 236
Cdd:cd04488 1 TVEGTVVSVEVVPRRGRRRLKVTLSDGTGTLTLVFFNfQPYLKKQLPPGTRVRVSGKVKRFRGGL-QIVHPEYE 73
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
618-686 |
1.19e-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: 43.01 E-value: 1.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239505248 618 EEKNRIMHRFKNKEAMILVSTSVVEVGIDIPT--ATVMViEHPerFGLAQLHQLRGRVGRSSLKSYCMLVL 686
Cdd:cd18797 79 EDRREIEAELFNGELLGVVATNALELGIDIGGldAVVLA-GYP--GSLASLWQQAGRAGRRGKDSLVILVA 146
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
365-492 |
1.98e-04 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 43.50 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 365 QMRAFEEIRED-----MKAPTpmnrllqgdvGSGKTVVAELAIIDNF-------EAGYQSAMMVPTTVLATQQHQKLVKD 432
Cdd:cd18023 6 QSEVFPDLLYSdknfvVSAPT----------GSGKTVLFELAILRLLkernplpWGNRKVVYIAPIKALCSEKYDDWKEK 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239505248 433 LEPLGIKVELLVGSQKKSQQEEIKKriaigeVDVVVGTHA-------LIQENVKF-KDLGLVIIDEQH 492
Cdd:cd18023 76 FGPLGLSCAELTGDTEMDDTFEIQD------ADIILTTPEkwdsmtrRWRDNGNLvQLVALVLIDEVH 137
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
391-527 |
3.77e-04 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 42.46 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 391 GSGKTVVAELAIIDNFE----AGYQS--AMMVPTTVLATQQHQKLVKDLEPlGIKVELLVGSQ--KKSQQEEIKKRiaig 462
Cdd:cd18036 27 GSGKTRVAVYICRHHLEkrrsAGEKGrvVVLVNKVPLVEQQLEKFFKYFRK-GYKVTGLSGDSshKVSFGQIVKAS---- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239505248 463 evDVVVGT---------HALIQENVKFKDLGLVIIDEQHRfgvKQREALMNK--GALVDTLVMTATPIPRTLALTA 527
Cdd:cd18036 102 --DVIICTpqilinnllSGREEERVYLSDFSLLIFDECHH---TQKEHPYNKimRMYLDKKLSSQGPLPQILGLTA 172
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
365-519 |
4.00e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 41.89 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 365 QMRAFEEIREDMKaPTPMNRLLQGDVGSGKTVVAeLAIIDNF--EAGYQSAMM-VPTTVLATQQHQKLVKDLEPLGIKVE 441
Cdd:pfam04851 8 QIEAIENLLESIK-NGQKRGLIVMATGSGKTLTA-AKLIARLfkKGPIKKVLFlVPRKDLLEQALEEFKKFLPNYVEIGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 442 LLVGsqkksqqeeIKKRIAIGEVDVVVGT-HALIQENVKFKDL------GLVIIDEQHRFGVKQREALMNKGALVDTLVM 514
Cdd:pfam04851 86 IISG---------DKKDESVDDNKIVVTTiQSLYKALELASLEllpdffDVIIIDEAHRSGASSYRNILEYFKPAFLLGL 156
|
....*
gi 239505248 515 TATPI 519
Cdd:pfam04851 157 TATPE 161
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
387-647 |
5.69e-04 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 43.40 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 387 QGDVGSGKT------VVAEL----AIIDNFEAGYQSAMMVPTTVLATQQHQKLVKDLEPLGIKVELLVGSQKKSQQEEIK 456
Cdd:PRK04537 52 QAQTGTGKTlaflvaVMNRLlsrpALADRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 457 KRiaigEVDVVVGT----------------HA----LIQENVKFKDLGLViidEQHRFGVKQrealMNKGALVDTLVMTA 516
Cdd:PRK04537 132 QQ----GVDVIIATpgrlidyvkqhkvvslHAceicVLDEADRMFDLGFI---KDIRFLLRR----MPERGTRQTLLFSA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 517 TPIPRTLALtAYGDLDistitemPPGRAPIRTMLISEKRLPELYAFIRDEvnhgHQAFFIYPLIEESEQM------DLKA 590
Cdd:PRK04537 201 TLSHRVLEL-AYEHMN-------EPEKLVVETETITAARVRQRIYFPADE----EKQTLLLGLLSRSEGArtmvfvNTKA 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 239505248 591 ATDEAERLQKEVFPDIGVelLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDI 647
Cdd:PRK04537 269 FVERVARTLERHGYRVGV--LSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHI 323
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
594-676 |
6.32e-04 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 40.71 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 594 EAERLQ---KEVFPDIGVELL----HGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDI-PTATVMVIEHPerFGLAQ 665
Cdd:cd18796 50 QAERLAqrlRELCPDRVPPDFialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIgDVDLVIQIGSP--KSVAR 127
|
90
....*....|.
gi 239505248 666 LHQlrgRVGRS 676
Cdd:cd18796 128 LLQ---RLGRS 135
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
380-513 |
7.19e-04 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350778 [Multi-domain] Cd Length: 199 Bit Score: 41.65 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 380 TPMNRLLQGDVGSGKTVVAELAII---------------DNFEAGYqsamMVPTTVLATQQHQKLVKDLEPLGIKVELLV 444
Cdd:cd18020 16 TNENMLICAPTGAGKTNIAMLTILheirqhvnqggvikkDDFKIVY----IAPMKALAAEMVEKFSKRLAPLGIKVKELT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239505248 445 GSQKKSQQEEIKKRIAIG---EVDVVvgTHALIQENVKFKDLGLVIIDEQHrfgvkqreaLMN--KGALVDTLV 513
Cdd:cd18020 92 GDMQLTKKEIAETQIIVTtpeKWDVV--TRKSSGDVALSQLVRLLIIDEVH---------LLHddRGPVIESLV 154
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
615-672 |
1.20e-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: 39.88 E-value: 1.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239505248 615 MSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVMViehpeRFGLA----QLHQLRGR 672
Cdd:cd18802 74 MTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVI-----RFDLPktlrSYIQSRGR 130
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
615-675 |
1.29e-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: 40.03 E-value: 1.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239505248 615 MSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVMVIEHPERFGLAQLhQLRGRVGR 675
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMI-QRMGRTGR 133
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
365-470 |
1.71e-03 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 40.77 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 365 QMRAFEEIRedMKAPTPMNR-----LLQG-DV------GSGKTV---------VAELAIID--NFEAGYQSAMMVPTTVL 421
Cdd:cd17945 1 LLRVIRKLG--YKEPTPIQRqaipiGLQNrDIigiaetGSGKTAaflipllvyISRLPPLDeeTKDDGPYALILAPTREL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 239505248 422 ATQQHQKLVKDLEPLGIKVELLVGSQKKsqqEEIKKRIAIGeVDVVVGT 470
Cdd:cd17945 79 AQQIEEETQKFAKPLGIRVVSIVGGHSI---EEQAFSLRNG-CEILIAT 123
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
615-655 |
1.88e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 41.78 E-value: 1.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 239505248 615 MSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPtATVMVI 655
Cdd:PRK13766 407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIP-SVDLVI 446
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
382-492 |
1.99e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 40.21 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 382 MNRLLQG-DV------GSGKTVVAELAiidnfeagyqsAMMVP-TTV-----LATQQHQklVKDLEPLGIKVELLVGSQK 448
Cdd:cd17920 21 INAVLAGrDVlvvmptGGGKSLCYQLP-----------ALLLDgVTLvvsplISLMQDQ--VDRLQQLGIRAAALNSTLS 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 239505248 449 KSQQEEIKKRIAIGEVDVV---------VGTHALIQENVKFKDLGLVIIDEQH 492
Cdd:cd17920 88 PEEKREVLLRIKNGQYKLLyvtperllsPDFLELLQRLPERKRLALIVVDEAH 140
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
586-679 |
2.14e-03 |
|
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: 40.69 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 586 MDLKAATDEAERLQKEV---FPD-----IGVELLHGRMSDEEknrIMHRFKNKEAMILVSTSVVEVGIDIPTATVMVI-- 655
Cdd:cd18804 94 EDLVFKGIGTERVEEELktlFPEariarIDRDTTRKKGALEK---LLDQFERGEIDILIGTQMIAKGLDFPNVTLVGIln 170
|
90 100 110
....*....|....*....|....*....|....*
gi 239505248 656 -----EHP-----ER-FGLaqLHQLRGRVGRSSLK 679
Cdd:cd18804 171 adsglNSPdfrasERaFQL--LTQVSGRAGRGDKP 203
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
605-655 |
2.99e-03 |
|
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: 39.15 E-value: 2.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 239505248 605 DIGVELLHGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATVMVI 655
Cdd:cd18789 68 RLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQ 118
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
387-490 |
3.17e-03 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 39.61 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 387 QGDVGSGKT---VVAELAIIDNFEAGYQSAMMVPTTVLAtQQHQKLVKDL-EPLGIKVELLVGSQkkSQQEEIKKRIAig 462
Cdd:cd17939 40 QAQSGTGKTatfSIGALQRIDTTVRETQALVLAPTRELA-QQIQKVVKALgDYMGVKVHACIGGT--SVREDRRKLQY-- 114
|
90 100 110
....*....|....*....|....*....|...
gi 239505248 463 EVDVVVGT-----HALIQENVKFKDLGLVIIDE 490
Cdd:cd17939 115 GPHIVVGTpgrvfDMLQRRSLRTDKIKMFVLDE 147
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
391-494 |
4.58e-03 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 39.10 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 391 GSGKT---VVAELAIIDNFEAGYQSAMM-----VPTTVLATQQHQKLVKDLEPLG--IKVELLVGSQKKSQQEEIKKRia 460
Cdd:cd17960 37 GSGKTlafLIPVLEILLKRKANLKKGQVgaliiSPTRELATQIYEVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKR-- 114
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 239505248 461 iGEVDVVVGTHA-------LIQENVKFKDLGLVIIDEQHRF 494
Cdd:cd17960 115 -NGPNILVGTPGrleellsRKADKVKVKSLEVLVLDEADRL 154
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
552-684 |
5.02e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 40.65 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 552 SEKRLPELYAFIRDevNHGHQAFFIYPLieesEQMDLKAAtdeAERLQ----KEVFpdigvelLHGRMSDEEKNRIMHRF 627
Cdd:PLN03137 663 TKKCLEDIDKFIKE--NHFDECGIIYCL----SRMDCEKV---AERLQefghKAAF-------YHGSMDPAQRAFVQKQW 726
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 239505248 628 KNKEAMILVSTSVVEVGIDIPTATvMVIEHPERFGLAQLHQLRGRVGRSSLKSYCML 684
Cdd:PLN03137 727 SKDEINIICATVAFGMGINKPDVR-FVIHHSLPKSIEGYHQECGRAGRDGQRSSCVL 782
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
615-650 |
5.10e-03 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 40.48 E-value: 5.10e-03
10 20 30
....*....|....*....|....*....|....*.
gi 239505248 615 MSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTA 650
Cdd:COG1111 395 LTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEV 430
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
595-655 |
7.69e-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: 37.46 E-value: 7.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239505248 595 AERLQKEvfpDIGVELLHGRMSDEEKNRIMHRFKNKEA--MILVSTSVVEVGIDIPTATVMVI 655
Cdd:cd18793 44 EEALRER---GIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGVGLNLTAANRVIL 103
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
387-705 |
7.71e-03 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 39.42 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 387 QGDVGSGKT---VVAELAIIDNFEAGYQSAMMVPTTVLAtQQHQKLVKDL-EPLGIKVELLVGSQkkSQQEEIKKRIAig 462
Cdd:PTZ00424 71 QAQSGTGKTatfVIAALQLIDYDLNACQALILAPTRELA-QQIQKVVLALgDYLKVRCHACVGGT--VVRDDINKLKA-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 463 EVDVVVGTHALI-----QENVKFKDLGLVIIDEQHR-----FGVKQREALMNKGALVDTLVMTATpIPRTLaltaygdLD 532
Cdd:PTZ00424 146 GVHMVVGTPGRVydmidKRHLRVDDLKLFILDEADEmlsrgFKGQIYDVFKKLPPDVQVALFSAT-MPNEI-------LE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 533 ISTITEMPPGRAPIRTMLISEKRLPELYAFIRDEVNHGHQAFFIYPLIEESEQMDLKAATDEAERLQKEVFP-DIGVELL 611
Cdd:PTZ00424 218 LTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHErDFTVSCM 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 612 HGRMSDEEKNRIMHRFKNKEAMILVSTSVVEVGIDIPTATvMVIEH-----PERFglaqLHQLrGRVGRSSLKSYCM-LV 685
Cdd:PTZ00424 298 HGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVS-LVINYdlpasPENY----IHRI-GRSGRFGRKGVAInFV 371
|
330 340
....*....|....*....|
gi 239505248 686 LNSNIsgEALDRLRKFAGTQ 705
Cdd:PTZ00424 372 TPDDI--EQLKEIERHYNTQ 389
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
377-490 |
8.17e-03 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 38.34 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239505248 377 KAPTPMNR-----LLQG-DV------GSGKTVVAELAIIDNF-----EAGYQSAMMVPTTVLATQQHQKLVKDLEPLGIK 439
Cdd:cd17957 11 REPTPIQMqaipiLLHGrDLlacaptGSGKTLAFLIPILQKLgkprkKKGLRALILAPTRELASQIYRELLKLSKGTGLR 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 239505248 440 VELLVGSQKKSQQeeiKKRIAIGEVDVVVGT-----HALIQENVKFKDLGLVIIDE 490
Cdd:cd17957 91 IVLLSKSLEAKAK---DGPKSITKYDILVSTplrlvFLLKQGPIDLSSVEYLVLDE 143
|
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