|
Name |
Accession |
Description |
Interval |
E-value |
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
104-776 |
0e+00 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 961.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 104 MKQPSCEIKYAKRVGPRKEAILKKLGISTLGDLIFYFPRDYEDRRKIIPISEISFEGKLTTRGKVVNVETKKI-GSMTIT 182
Cdd:COG1200 1 MAPLDTPLTYLKGVGPKRAKLLAKLGIRTVGDLLFHLPRRYEDRTRLTPIAELRPGETVTVEGTVVSVEVVRRrRRRRIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 183 AAVLADGVSQLLLKWFNQEYLHKGLQVlkNKTIYATGLVKHSqFGGIEMVNPEIEPEDGTQVLE---ILPIYPLTHGISQ 259
Cdd:COG1200 81 EVTLSDGTGSLTLVFFNQPYLKKQLKP--GTRVLVSGKVERF-RGGLQMVHPEYELLDEEEAELagrLTPVYPLTEGLSQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 260 KEIRRIVRENISCVCHYTDE-LPEELMKKRKLMDISRALLGIHFPKSNYHLKKSIERLAYEELFLMQFALLLSRKSFEEI 338
Cdd:COG1200 158 KTLRKLIRQALDLLAPDLPEpLPEELRARYGLPSLAEALRNIHFPPSDEDLHPARRRLAFEELLALQLALLLRRARRRKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 339 GGLPKKIPGKLAEEFLRKLPFKLTDSQKEAHRQIRADLMSNKPMSRLLQGDVGCGKTVVAQLAIVDNFEAGFQSAVMAPT 418
Cdd:COG1200 238 KGPALPGDGELLEAFLAALPFELTGAQKRVIAEIAADLASPHPMNRLLQGDVGSGKTVVALLAMLAAVEAGYQAALMAPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 419 SILAMQHYRRMSPAFEEMGIRTALLLGETSSREKEKIKRMLSDGEISVVIGTHTLIQEDVSFSNLGLVIIDEQHRFGVKQ 498
Cdd:COG1200 318 EILAEQHYRSLSKLLEPLGIRVALLTGSTKAKERREILAALASGEADIVVGTHALIQDDVEFKNLGLVVIDEQHRFGVEQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 499 REALVSKGKALDTLVMTATPIPRTLALTIYGDLDITVIDEMPPGRKDVKTMLVSVSKLEQVYEFVKKEIAEGGQVFIVYP 578
Cdd:COG1200 398 RLALREKGEAPHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPIKTRVVPEERRDEVYERIREEIAKGRQAYVVCP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 579 LIEESDKIQAKAAIRMHEYLsKKIFGEFRVGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVMIIENP 658
Cdd:COG1200 478 LIEESEKLDLQAAEETYEEL-REAFPGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVMVIENA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 659 ERFGLAQLHQLRGRIGRGDKQGYCFLVVGN-VDDDALERLRYFSMTKNGFEVAEYDMKLRGPGEILGLKQHGLPELKIAD 737
Cdd:COG1200 557 ERFGLSQLHQLRGRVGRGSAQSYCLLLYDApLSETARERLEVMRETNDGFEIAEEDLELRGPGEFLGTRQSGLPDLRIAD 636
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 157313485 738 LIRDRELLFRARNDAEEIVRKK---EQYPDIVKKVKTIYGER 776
Cdd:COG1200 637 LVRDADLLEAAREDAEELLEEDpelASHPALRRWLGLRFRDE 678
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
111-783 |
0e+00 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 934.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 111 IKYAKRVGPRKEAILKKLGISTLGDLIFYFPRDYEDRRKIIPISEISFEGKLTTRGKVVNVETKKiGSMTITAAVLADGV 190
Cdd:PRK10917 11 LTSLKGVGPKTAEKLAKLGIHTVQDLLLHLPRRYEDRTRLKPIAELRPGEKVTVEGEVLSAEVVF-GKRRRLTVTVSDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 191 SQLLLKWF--NQEYLHKGLQVlkNKTIYATGLVKHSQFGgIEMVNPEIEPEDGTQVL---EILPIYPLTHGISQKEIRRI 265
Cdd:PRK10917 90 GNLTLRFFnfNQPYLKKQLKV--GKRVAVYGKVKRGKYG-LEMVHPEYEVLEEESPElegRLTPVYPLTEGLKQKTLRKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 266 VRENISCVCHYTDELPEELMKKRKLMDISRALLGIHFPKSNYHLKKSIERLAYEELFLMQFALLLSRKSFEEIGGLPKKI 345
Cdd:PRK10917 167 IKQALELLDALPELLPEELLEKYGLLSLAEALRAIHFPPSDEDLHPARRRLKFEELFALQLSLLLLRAGRRSKKAGPLPY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 346 PGKLAEEFLRKLPFKLTDSQKEAHRQIRADLMSNKPMSRLLQGDVGCGKTVVAQLAIVDNFEAGFQSAVMAPTSILAMQH 425
Cdd:PRK10917 247 DGELLKKFLASLPFELTGAQKRVVAEILADLASPKPMNRLLQGDVGSGKTVVAALAALAAIEAGYQAALMAPTEILAEQH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 426 YRRMSPAFEEMGIRTALLLGETSSREKEKIKRMLSDGEISVVIGTHTLIQEDVSFSNLGLVIIDEQHRFGVKQREALVSK 505
Cdd:PRK10917 327 YENLKKLLEPLGIRVALLTGSLKGKERREILEAIASGEADIVIGTHALIQDDVEFHNLGLVIIDEQHRFGVEQRLALREK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 506 GKALDTLVMTATPIPRTLALTIYGDLDITVIDEMPPGRKDVKTMLVSVSKLEQVYEFVKKEIAEGGQVFIVYPLIEESDK 585
Cdd:PRK10917 407 GENPHVLVMTATPIPRTLAMTAYGDLDVSVIDELPPGRKPITTVVIPDSRRDEVYERIREEIAKGRQAYVVCPLIEESEK 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 586 IQAKAAIRMHEYLsKKIFGEFRVGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVMIIENPERFGLAQ 665
Cdd:PRK10917 487 LDLQSAEETYEEL-QEAFPELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVMVIENAERFGLAQ 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 666 LHQLRGRIGRGDKQGYCFLVVGN-VDDDALERLRYFSMTKNGFEVAEYDMKLRGPGEILGLKQHGLPELKIADLIRDREL 744
Cdd:PRK10917 566 LHQLRGRVGRGAAQSYCVLLYKDpLSETARERLKIMRETNDGFVIAEKDLELRGPGELLGTRQSGLPEFKVADLVRDEEL 645
|
650 660 670
....*....|....*....|....*....|....*....
gi 157313485 745 LFRARNDAEEIVrkkEQYPDIVKKVKTIYGERLKLVKIA 783
Cdd:PRK10917 646 LEEARKDARELL---ERDPELAEALLERWLGERERYDKA 681
|
|
| recG |
TIGR00643 |
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair] |
128-752 |
0e+00 |
|
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273192 [Multi-domain] Cd Length: 630 Bit Score: 733.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 128 LGISTLGDLIFYFPRDYEDRRKIIPISEISFEGKLTTRGKVVNVETKKIGSMTITAAVLADGVSQLL-LKWFNQEYLHKG 206
Cdd:TIGR00643 1 LGIHTVQDLLFYFPRRYEDRTLLQTIGELLPGERATIVGEVLSHCIFGFKRRKVLKLRLKDGGYKKLeLRFFNRAFLKKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 207 LQVlkNKTIYATGLVKHSQFGGiEMVNPE--IEPEDGTQVLEILPIYPLTHGISQKEIRRIVREN----ISCVchyTDEL 280
Cdd:TIGR00643 81 FKV--GSKVVVYGKVKSSKFKA-YLIHPEfiSEKDGVEFELKILPVYPLTEGLTQKKLRKLIQQAldqlDKSL---EDPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 281 PEELMKKRKLMDISRALLGIHFPKSNYHLKKSIERLAYEELFLMQFALL-LSRKSFEEIGGLPKKIPGKLAEEFLRKLPF 359
Cdd:TIGR00643 155 PEELREKYGLLSLEDALRAIHFPKTLSLLELARRRLIFDEFFYLQLAMLaRRLGEKQQFSAPPANPSEELLTKFLASLPF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 360 KLTDSQKEAHRQIRADLMSNKPMSRLLQGDVGCGKTVVAQLAIVDNFEAGFQSAVMAPTSILAMQHYRRMSPAFEEMGIR 439
Cdd:TIGR00643 235 KLTRAQKRVVKEILQDLKSDVPMNRLLQGDVGSGKTLVAALAMLAAIEAGYQVALMAPTEILAEQHYNSLRNLLAPLGIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 440 TALLLGETSSREKEKIKRMLSDGEISVVIGTHTLIQEDVSFSNLGLVIIDEQHRFGVKQREALVSKGKAL---DTLVMTA 516
Cdd:TIGR00643 315 VALLTGSLKGKRRKELLETIASGQIHLVVGTHALIQEKVEFKRLALVIIDEQHRFGVEQRKKLREKGQGGftpHVLVMSA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 517 TPIPRTLALTIYGDLDITVIDEMPPGRKDVKTMLVSVSKLEQVYEFVKKEIAEGGQVFIVYPLIEESDKIQAKAAIRMHE 596
Cdd:TIGR00643 395 TPIPRTLALTVYGDLDTSIIDELPPGRKPITTVLIKHDEKDIVYEFIEEEIAKGRQAYVVYPLIEESEKLDLKAAEALYE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 597 YLsKKIFGEFRVGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVMIIENPERFGLAQLHQLRGRIGRG 676
Cdd:TIGR00643 475 RL-KKAFPKYNVGLLHGRMKSDEKEAVMEEFREGEVDILVATTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRG 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157313485 677 DKQGYCFLVVGN-VDDDALERLRYFSMTKNGFEVAEYDMKLRGPGEILGLKQHGLPELKIADLIRDRELLFRARNDA 752
Cdd:TIGR00643 554 DHQSYCLLVYKNpKSESAKKRLRVMADTLDGFVIAEEDLELRGPGDLLGTKQSGYPEFRVADLVRDREILVEAREDA 630
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
309-729 |
3.05e-115 |
|
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: 370.92 E-value: 3.05e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 309 LKKSIERLAYEelfLMQFALLlsRKSfeeIGGLPKKIPGKLAEEFLRKLPFKLTDSQKEAHRQIRADLMSNKPMSRLLQG 388
Cdd:TIGR00580 408 VKKSVREIAAK---LIELYAK--RKA---IKGHAFPPDLEWQQEFEDSFPFEETPDQLKAIEEIKADMESPRPMDRLVCG 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 389 DVGCGKTVVAQLAIVDNFEAGFQSAVMAPTSILAMQHYRRMSPAFEEMGIRTALLLGETSSREKEKIKRMLSDGEISVVI 468
Cdd:TIGR00580 480 DVGFGKTEVAMRAAFKAVLDGKQVAVLVPTTLLAQQHFETFKERFANFPVTIELLSRFRSAKEQNEILKELASGKIDILI 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 469 GTHTLIQEDVSFSNLGLVIIDEQHRFGVKQREALVSKGKALDTLVMTATPIPRTLALTIYGDLDITVIDEMPPGRKDVKT 548
Cdd:TIGR00580 560 GTHKLLQKDVKFKDLGLLIIDEEQRFGVKQKEKLKELRTSVDVLTLSATPIPRTLHMSMSGIRDLSIIATPPEDRLPVRT 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 549 MLVSVSKlEQVYEFVKKEIAEGGQVFIVYPLIEESDKIqaKAAIRMheylskkIFGEFRVGLLHGKMSQQEKDKIMERFA 628
Cdd:TIGR00580 640 FVMEYDP-ELVREAIRRELLRGGQVFYVHNRIESIEKL--ATQLRE-------LVPEARIAIAHGQMTENELEEVMLEFY 709
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 629 TGEFDILISTTVIEVGIDVPRATVMIIENPERFGLAQLHQLRGRIGRGDKQGYCFLVVGN---VDDDALERLRY---FSM 702
Cdd:TIGR00580 710 KGEFQVLVCTTIIETGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKKKAYAYLLYPHqkaLTEDAQKRLEAiqeFSE 789
|
410 420
....*....|....*....|....*..
gi 157313485 703 TKNGFEVAEYDMKLRGPGEILGLKQHG 729
Cdd:TIGR00580 790 LGAGFKIALHDLEIRGAGNLLGEEQSG 816
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
316-540 |
5.00e-115 |
|
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: 347.21 E-value: 5.00e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 316 LAYEELFLMQFALLLSRKSFEEIGGLPKKIPGKLAEEFLRKLPFKLTDSQKEAHRQIRADLMSNKPMSRLLQGDVGCGKT 395
Cdd:cd17992 1 LAFEELFALQLALLLRRRKIEELKGIILEISGELLKKFLEALPFELTGAQKRVIDEILRDLASEKPMNRLLQGDVGSGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 396 VVAQLAIVDNFEAGFQSAVMAPTSILAMQHYRRMSPAFEEMGIRTALLLGETSSREKEKIKRMLSDGEISVVIGTHTLIQ 475
Cdd:cd17992 81 VVAALAMLAAVENGYQVALMAPTEILAEQHYDSLKKLLEPLGIRVALLTGSTKAKEKREILEKIASGEIDIVIGTHALIQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157313485 476 EDVSFSNLGLVIIDEQHRFGVKQREALVSKGKALDTLVMTATPIPRTLALTIYGDLDITVIDEMP 540
Cdd:cd17992 161 EDVEFHNLGLVIIDEQHRFGVEQRLKLREKGETPHVLVMTATPIPRTLALTLYGDLDVSIIDELP 225
|
|
| Mfd |
COG1197 |
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ... |
349-729 |
9.16e-99 |
|
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription];
Pssm-ID: 440810 [Multi-domain] Cd Length: 1130 Bit Score: 330.88 E-value: 9.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 349 LAEEFlrklPFKLTDSQKEAHRQIRADLMSNKPMSRLLQGDVGCGKTVVAQ----LAIVDnfeaGFQSAVMAPTSILAMQ 424
Cdd:COG1197 579 FEAAF----PYEETPDQLRAIEEVKADMESPRPMDRLVCGDVGFGKTEVALraafKAVMD----GKQVAVLVPTTLLAQQ 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 425 HYRRMSPAFEEMGIRTALLlgetsSR-----EKEKIKRMLSDGEISVVIGTHTLIQEDVSFSNLGLVIIDEQHRFGVKQR 499
Cdd:COG1197 651 HYETFKERFAGFPVRVEVL-----SRfrtakEQKETLEGLADGKVDIVIGTHRLLSKDVKFKDLGLLIIDEEQRFGVRHK 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 500 EALvskgKAL----DTLVMTATPIPRTL--ALTiyGDLDITVIDEMPPGRKDVKTmlvSVSKL--EQVYEFVKKEIAEGG 571
Cdd:COG1197 726 EKL----KALranvDVLTLTATPIPRTLqmSLS--GIRDLSIIATPPEDRLPVKT---FVGEYddALIREAILRELLRGG 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 572 QVFIVYPLIEEsdkIQakaaiRMHEYLsKKIFGEFRVGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRAT 651
Cdd:COG1197 797 QVFYVHNRVED---IE-----KVAARL-QELVPEARIAVAHGQMSERELERVMLDFYEGEFDVLVCTTIIETGIDIPNAN 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 652 VMIIENPERFGLAQLHQLRGRIGRGDKQGYCFLVVGNVD---DDALERLRyfSMTKN-----GFEVAEYDMKLRGPGEIL 723
Cdd:COG1197 868 TIIIERADRFGLAQLYQLRGRVGRSHRRAYAYLLYPPDKvltEDAEKRLE--AIQEFtelgaGFKLAMHDLEIRGAGNLL 945
|
....*.
gi 157313485 724 GLKQHG 729
Cdd:COG1197 946 GEEQSG 951
|
|
| RecG_wedge |
pfam17191 |
RecG wedge domain; This DNA-binding domain has an OB-fold with large elaborations. |
110-273 |
2.92e-91 |
|
RecG wedge domain; This DNA-binding domain has an OB-fold with large elaborations.
Pssm-ID: 407316 [Multi-domain] Cd Length: 162 Bit Score: 283.17 E-value: 2.92e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 110 EIKYAKRVGPRKEAILKKLGISTLGDLIFYFPRDYEDRRKIIPISEISFEGKLTTRGKVVNVETKKIGSMTITAAVLADG 189
Cdd:pfam17191 1 PIKYAKGVGPKREKILKKLGIETIGDLIWYFPRDYEDRRKIIPISDIRHDEKVTTKGKIVNFETKKIGSLVIISAVLSDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 190 VSQLLLKWFNQEYLHKGLQvlKNKTIYATGLVKHSQFGGIEMVNPEIEPEDGTQVLEILPIYPLTHGISQKEIRRIVREN 269
Cdd:pfam17191 81 IGQVLLKWFNQEYIKKFLQ--KGKEVYITGTVKEGPFGPIEMNNPEIEEITGEQEREILPVYPLTEGISQKNMRKIVKEN 158
|
....
gi 157313485 270 ISCV 273
Cdd:pfam17191 159 ISYV 162
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
546-701 |
1.39e-77 |
|
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: 246.87 E-value: 1.39e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 546 VKTMLVSVSKLEQVYEFVKKEIAEGGQVFIVYPLIEESDKIQAKAAIRMHEYLSKKIFGEFRVGLLHGKMSQQEKDKIME 625
Cdd:cd18811 2 ITTYLIFHTRLDKVYEFVREEIAKGRQAYVIYPLIEESEKLDLKAAVAMYEYLKERFRPELNVGLLHGRLKSDEKDAVMA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157313485 626 RFATGEFDILISTTVIEVGIDVPRATVMIIENPERFGLAQLHQLRGRIGRGDKQGYCFLVVGNV-DDDALERLRYFS 701
Cdd:cd18811 82 EFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYKDPlTETAKQRLRVMT 158
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
353-729 |
7.31e-77 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 269.69 E-value: 7.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 353 FLRKLPFKLTDSQKEAHRQIRADLMSNKPMSRLLQGDVGCGKTVVAQLAIVDNFEAGFQSAVMAPTSILAMQHYRRMSPA 432
Cdd:PRK10689 593 FCDSFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQHYDNFRDR 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 433 FEEMGIRTALLLGETSSREKEKIKRMLSDGEISVVIGTHTLIQEDVSFSNLGLVIIDEQHRFGVKQREALVSKGKALDTL 512
Cdd:PRK10689 673 FANWPVRIEMLSRFRSAKEQTQILAEAAEGKIDILIGTHKLLQSDVKWKDLGLLIVDEEHRFGVRHKERIKAMRADVDIL 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 513 VMTATPIPRTLALTIYGDLDITVIDEMPPGRKDVKTMLVSVSKLeQVYEFVKKEIAEGGQVFIVYPLIEesdKIQaKAAI 592
Cdd:PRK10689 753 TLTATPIPRTLNMAMSGMRDLSIIATPPARRLAVKTFVREYDSL-VVREAILREILRGGQVYYLYNDVE---NIQ-KAAE 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 593 RMHEYLSkkifgEFRVGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVMIIENPERFGLAQLHQLRGR 672
Cdd:PRK10689 828 RLAELVP-----EARIAIGHGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLRGR 902
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157313485 673 IGRGDKQGYCFLVVGN---VDDDALERLRYFSMTKN---GFEVAEYDMKLRGPGEILGLKQHG 729
Cdd:PRK10689 903 VGRSHHQAYAWLLTPHpkaMTTDAQKRLEAIASLEDlgaGFALATHDLEIRGAGELLGEEQSG 965
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
546-698 |
5.77e-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: 229.46 E-value: 5.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 546 VKTMLVSVSKLEQVYEFVKKEIAEGGQVFIVYPLIEESDKIQAKAAIRMHEYLsKKIFGEFRVGLLHGKMSQQEKDKIME 625
Cdd:cd18792 2 IRTYVIPHDDLDLVYEAIERELARGGQVYYVYPRIEESEKLDLKSIEALAEEL-KELVPEARVALLHGKMTEDEKEAVML 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157313485 626 RFATGEFDILISTTVIEVGIDVPRATVMIIENPERFGLAQLHQLRGRIGRGDKQGYCFLVVGN---VDDDALERLR 698
Cdd:cd18792 81 EFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYPDpkkLTETAKKRLR 156
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
347-537 |
1.80e-69 |
|
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: 226.14 E-value: 1.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 347 GKLAEEFLRKLPFKLTDSQKEAHRQIRADLMSNKPMSRLLQGDVGCGKTVVAQLAIVDNFEAGFQSAVMAPTSILAMQHY 426
Cdd:cd17918 2 RALIQELCKSLPFSLTKDQAQAIKDIEKDLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 427 RRMSPAFEEmgIRTALLLGETssreKEKIKRmlsdgEISVVIGTHTLIQEDVSFSNLGLVIIDEQHRFGVKQREALVSKG 506
Cdd:cd17918 82 EEARKFLPF--INVELVTGGT----KAQILS-----GISLLVGTHALLHLDVKFKNLDLVIVDEQHRFGVAQREALYNLG 150
|
170 180 190
....*....|....*....|....*....|.
gi 157313485 507 kALDTLVMTATPIPRTLALTIYGDLDITVID 537
Cdd:cd17918 151 -ATHFLEATATPIPRTLALALSGLLDLSVID 180
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
346-537 |
1.85e-65 |
|
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350749 [Multi-domain] Cd Length: 193 Bit Score: 215.90 E-value: 1.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 346 PGKLAEEFLRKLPFKLTDSQKEAHRQIRADLMSNKPMSRLLQGDVGCGKTVVAQLAIVDNFEAGFQSAVMAPTSILAMQH 425
Cdd:cd17991 1 DGEEQEEFEASFPYEETPDQLKAIEEILKDMESGKPMDRLICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 426 YRRMSPAFEEMGIRTALLLGETSSREKEKIKRMLSDGEISVVIGTHTLIQEDVSFSNLGLVIIDEQHRFGVKQREALVSK 505
Cdd:cd17991 81 YETFKERFANFPVNVELLSRFTTAAEQREILEGLKEGKVDIVIGTHRLLSKDVEFKNLGLLIIDEEQRFGVKQKEKLKEL 160
|
170 180 190
....*....|....*....|....*....|..
gi 157313485 506 GKALDTLVMTATPIPRTLALTIYGDLDITVID 537
Cdd:cd17991 161 RPNVDVLTLSATPIPRTLHMALSGIRDLSVIA 192
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
546-698 |
2.95e-40 |
|
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: 145.18 E-value: 2.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 546 VKTMLVSVSKlEQVYEFVKKEIAEGGQVFIVYPLIEESDKIQAKAairmheylsKKIFGEFRVGLLHGKMSQQEKDKIME 625
Cdd:cd18810 2 VRTYVMPYDD-ELIREAIERELLRGGQVFYVHNRIESIEKLATQL---------RQLVPEARIAIAHGQMTENELEEVML 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157313485 626 RFATGEFDILISTTVIEVGIDVPRATVMIIENPERFGLAQLHQLRGRIGRGDKQGYCFLVVGN---VDDDALERLR 698
Cdd:cd18810 72 EFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKERAYAYFLYPDqkkLTEDALKRLE 147
|
|
| RecG_N |
pfam17190 |
RecG N-terminal helical domain; This four helical bundle domain is found at the N-terminus of ... |
8-95 |
3.62e-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: 122.52 E-value: 3.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 8 LVEEFLDFLEQSLLEVLHGKKGTNELVEEVQDRYELVADHVLQNSEIL-EKFKQLFEYIEPVADMQPERAIKRVKNSLGM 86
Cdd:pfam17190 1 LLEEFLDECEQLLKKVLNGKLKTNELIEEIKDNLSLLDDPLLENEEGLkEKLGQFLEYYKPIANLPPERAIKRLKNGLEM 80
|
....*....
gi 157313485 87 IERFRDWYL 95
Cdd:pfam17190 81 IEKLRYWFL 89
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
353-544 |
3.55e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 103.73 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 353 FLRKLPFKLTDSQKEAHRQIRADLMSnkpmsRLLQGDVGCGKTVVAQLAIVDNF--EAGFQSAVMAPTSILAMQHYRRMS 430
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRD-----VILAAPTGSGKTLAALLPALEALkrGKGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 431 PAFEEMGIRTALLLGETSsreKEKIKRMLSDGEISVVIGT-----HTLIQEDVSFSNLGLVIIDEQHRFGVKQREALVSK 505
Cdd:smart00487 76 KLGPSLGLKVVGLYGGDS---KREQLRKLESGKTDILVTTpgrllDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 157313485 506 -----GKALDTLVMTATP---IPRTLALTIYGDLDITVIDEMPPGRK 544
Cdd:smart00487 153 llkllPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIE 199
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
371-524 |
8.43e-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: 98.47 E-value: 8.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 371 QIRA--DLMSNKPMsrLLQGDVGCGKTVVAQLAIVDNFE---AGFQSAVMAPTSILAMQHYRRMSPAFEEMGIRTALLL- 444
Cdd:pfam00270 4 QAEAipAILEGRDV--LVQAPTGSGKTLAFLLPALEALDkldNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 445 GETSSREKEKIKRmlsdgeISVVIGTH----TLIQEDVSFSNLGLVIIDEQHRFGVKQREALVSK-----GKALDTLVMT 515
Cdd:pfam00270 82 GDSRKEQLEKLKG------PDILVGTPgrllDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEilrrlPKKRQILLLS 155
|
....*....
gi 157313485 516 ATPiPRTLA 524
Cdd:pfam00270 156 ATL-PRNLE 163
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
554-675 |
1.28e-23 |
|
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: 96.13 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 554 SKLEQVYEFVKKEiaEGGQVFIVYPLIEESDKiqakaairmhEYLSKKIfgEFRVGLLHGKMSQQEKDKIMERFATGEFD 633
Cdd:pfam00271 1 EKLEALLELLKKE--RGGKVLIFSQTKKTLEA----------ELLLEKE--GIKVARLHGDLSQEEREEILEDFRKGKID 66
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 157313485 634 ILISTTVIEVGIDVPRATVMIIENPErFGLAQLHQLRGRIGR 675
Cdd:pfam00271 67 VLVATDVAERGLDLPDVDLVINYDLP-WNPASYIQRIGRAGR 107
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
358-783 |
1.68e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 96.25 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 358 PFKLTDSQKEAHRQIRADLMSNKPMSrLLQGDVGCGKTVVAqLAIVDNFEAGFQSAVMAPTSILAMQhyrrmspAFEEmg 437
Cdd:COG1061 78 SFELRPYQQEALEALLAALERGGGRG-LVVAPTGTGKTVLA-LALAAELLRGKRVLVLVPRRELLEQ-------WAEE-- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 438 IRTALLLGETSSREKEKIKRmlsdgeisVVIGTHTLIQEDVSFSNL----GLVIIDEQHRFGVKQREALVSKGKALDTLV 513
Cdd:COG1061 147 LRRFLGDPLAGGGKKDSDAP--------ITVATYQSLARRAHLDELgdrfGLVIIDEAHHAGAPSYRRILEAFPAAYRLG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 514 MTATPIpRTLALTIYGDLDITVIDEMPPGRK---------DVKTMLVSVSKLEQVY----EFVKKEIAEGGQ--VFIVYP 578
Cdd:COG1061 219 LTATPF-RSDGREILLFLFDGIVYEYSLKEAiedgylappEYYGIRVDLTDERAEYdalsERLREALAADAErkDKILRE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 579 LIEE-----------SDKIQAKAairMHEYLSKKifgEFRVGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDV 647
Cdd:COG1061 298 LLREhpddrktlvfcSSVDHAEA---LAELLNEA---GIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 648 PRATVMII----ENPerfglAQLHQLRGRIGRGDKQGYCFLVVgNVDDDALERLRYFSMTKNGFEVAEYDMKLRGPGEIL 723
Cdd:COG1061 372 PRLDVAILlrptGSP-----REFIQRLGRGLRPAPGKEDALVY-DFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEEL 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 724 GLKQHGLPELKIADLIRDRELLFRARNDAEEIVRKKEQYPDIVKKVKTIYGERLKLVKIA 783
Cdd:COG1061 446 ALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKA 505
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
382-517 |
3.32e-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: 87.84 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 382 MSRLLQGDVGCGKTVVAQLAIVDNF-EAGFQSAVMAPTSILAMQHYRRMSPAFeEMGIRTALLLGETSSREKEKIKRmls 460
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLlKKGKKVLVLVPTKALALQTAERLRELF-GPGIRVAVLVGGSSAEEREKNKL--- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 461 dGEISVVIGTHTLIQEDV------SFSNLGLVIIDEQHRFGVKQREALVSK-------GKALDTLVMTAT 517
Cdd:cd00046 78 -GDADIIIATPDMLLNLLlredrlFLKDLKLIIVDEAHALLIDSRGALILDlavrkagLKNAQVILLSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
593-675 |
8.47e-20 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 84.19 E-value: 8.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 593 RMHEYLSKKifgEFRVGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVMIIENPeRFGLAQLHQLRGR 672
Cdd:smart00490 2 ELAELLKEL---GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL-PWSPASYIQRIGR 77
|
...
gi 157313485 673 IGR 675
Cdd:smart00490 78 AGR 80
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
344-699 |
6.45e-17 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 84.56 E-value: 6.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 344 KIPGKLAEEFLRKLPFK-LTDSQKEAhrqIRADLMSNKpmSRLLQGDVGCGKTVVAQLAIVDNFEAGFQSAVMAPTSILA 422
Cdd:COG1204 5 ELPLEKVIEFLKERGIEeLYPPQAEA---LEAGLLEGK--NLVVSAPTASGKTLIAELAILKALLNGGKALYIVPLRALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 423 MQHYRRMSPAFEEMGIRTALLLGETSSREKEKIKRmlsdgeiSVVIGT----HTLIQEDVSF-SNLGLVIIDEQHRFGVK 497
Cdd:COG1204 80 SEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRY-------DILVATpeklDSLLRNGPSWlRDVDLVVVDEAHLIDDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 498 QR----EALVSKgkaldtlVMTATPIPRTLALT--------IYGDLDITVIDE-----------MPPGRKDVKTmlVSVS 554
Cdd:COG1204 153 SRgptlEVLLAR-------LRRLNPEAQIVALSatignaeeIAEWLDAELVKSdwrpvplnegvLYDGVLRFDD--GSRR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 555 KLEQVYEFVKKEIAEGGQVfIVY--------------------PLIEESDKIQAKAAIRMHEY---------LSKKIfgE 605
Cdd:COG1204 224 SKDPTLALALDLLEEGGQV-LVFvssrrdaeslakkladelkrRLTPEEREELEELAEELLEVseethtnekLADCL--E 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 606 FRVGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVmIIENPERFGLAQL-----HQLRGRIGR-G-DK 678
Cdd:COG1204 301 KGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRV-IIRDTKRGGMVPIpvlefKQMAGRAGRpGyDP 379
|
410 420
....*....|....*....|.
gi 157313485 679 QGYCFLVVGNvdDDALERLRY 699
Cdd:COG1204 380 YGEAILVAKS--SDEADELFE 398
|
|
| RecG_dom3_C |
pfam19833 |
ATP-dependent DNA helicase RecG, domain 3, C-terminal; This domain is found in ATP-dependent ... |
703-761 |
1.44e-13 |
|
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: 66.73 E-value: 1.44e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 703 TKNGFEVAEYDMKLRGPGEILGLKQHGLP-ELKIADLIRDRELLFRARNDAEEIVRKKEQ 761
Cdd:pfam19833 1 TNDGFEIAEADLKLRGPGDLEGTQQSGIAfDLKIADIARDGQLLQLARTEAEEIIDNDPE 60
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
556-686 |
2.81e-12 |
|
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: 64.45 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 556 LEQVYEFVKKEiaegGQVFIVYPLIEESDKIQ--------AKAAIRMHEYLSKKifgEFRVGLLHGKMSQQEKDKIMERF 627
Cdd:cd18787 1 IKQLYVVVEEE----EKKLLLLLLLLEKLKPGkaiifvntKKRVDRLAELLEEL---GIKVAALHGDLSQEERERALKKF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157313485 628 ATGEFDILISTTVIEVGIDVPRATVMII----ENPERFglaqLHqlR-GRIGRGDKQGYCFLVV 686
Cdd:cd18787 74 RSGKVRVLVATDVAARGLDIPGVDHVINydlpRDAEDY----VH--RiGRTGRAGRKGTAITFV 131
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
385-697 |
5.66e-11 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 65.17 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 385 LLQG-DV------GCGKTVVAQLAIVDNFEAGFQSA----VMAPTSILAMQHYRRMSPAFEEMGIRTALLLGETS-SREK 452
Cdd:COG0513 36 ILAGrDVlgqaqtGTGKTAAFLLPLLQRLDPSRPRApqalILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSiGRQI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 453 EKIKRmlsdGeISVVIGT------HtLIQEDVSFSNLGLVIIDEqhrfgvkqrealvskgkAlDtlvmtatpipRTLALT 526
Cdd:COG0513 116 RALKR----G-VDIVVATpgrlldL-IERGALDLSGVETLVLDE-----------------A-D----------RMLDMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 527 IYGDLDiTVIDEMPPGRKdvkTMLVS------VSKLeqVYEFVKK----EIAEGG-------QVFIvypLIEESDKIQA- 588
Cdd:COG0513 162 FIEDIE-RILKLLPKERQ---TLLFSatmppeIRKL--AKRYLKNpvriEVAPENataetieQRYY---LVDKRDKLELl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 589 -------------------KAAIRMHEYLSKKifgEFRVGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPR 649
Cdd:COG0513 233 rrllrdedperaivfcntkRGADRLAEKLQKR---GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDD 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 157313485 650 ATvMII-----ENPERFglaqLHqlR-GRIGRGDKQGYCFLVVGNVDDDALERL 697
Cdd:COG0513 310 VS-HVInydlpEDPEDY----VH--RiGRTGRAGAEGTAISLVTPDERRLLRAI 356
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
365-518 |
4.35e-10 |
|
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: 59.53 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 365 QKEAHRQIRADLMSNKPMsrLLQGDVGCGKTVVAQLAIVDNFEAGFQSAVMAPTSILAMQHYRRMSPAFeemGIRTALLL 444
Cdd:cd17929 1 QRKAYEAIVSSLGGFKTF--LLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTPQLIKRFKKRF---GDKVAVLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 445 GETSSREKEKIKRMLSDGEISVVIGTHTLIQedVSFSNLGLVIIDEQHRFGVKQ--------REALVSKGKALD-TLVM- 514
Cdd:cd17929 76 SKLSDKERADEWRKIKRGEAKVVIGARSALF--APFKNLGLIIVDEEHDSSYKQdsgpryhaRDVAIYRAKLENaPVVLg 153
|
....
gi 157313485 515 TATP 518
Cdd:cd17929 154 SATP 157
|
|
| RecG_wedge_OBF |
cd04488 |
RecG_wedge_OBF: A subfamily of OB folds corresponding to the OB fold found in the N-terminal ... |
163-237 |
7.76e-10 |
|
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: 55.66 E-value: 7.76e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157313485 163 TTRGKVVNVETKKIGSMTITAAVLADGVSQLLLKWFN-QEYLHKGLQVlkNKTIYATGLVKHSqFGGIEMVNPEIE 237
Cdd:cd04488 1 TVEGTVVSVEVVPRRGRRRLKVTLSDGTGTLTLVFFNfQPYLKKQLPP--GTRVRVSGKVKRF-RGGLQIVHPEYE 73
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
391-517 |
1.71e-09 |
|
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: 57.66 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 391 GCGKTVVAQLAIVDNFEAGFQSAV-MAPTSILAMQHYRRMSPAFEEMGIRTALLLGETSSREKEKIKRmlsdgeiSVVIG 469
Cdd:cd17921 27 SSGKTLIAELAILRALATSGGKAVyIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSVNKLLLAEA-------DILVA 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157313485 470 ThtliQE----------DVSFSNLGLVIIDEQHRFGVKQR----EALVSK----GKALDTLVMTAT 517
Cdd:cd17921 100 T----PEkldlllrnggERLIQDVRLVVVDEAHLIGDGERgvvlELLLSRllriNKNARFVGLSAT 161
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
616-686 |
4.03e-09 |
|
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: 53.86 E-value: 4.03e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157313485 616 SQQEKDKIMERFAtgefdILISTTVIEVGIDVPRATVMIIENPERFgLAQLHQLRGRIGR-GDKQGYCFLVV 686
Cdd:cd18785 12 SIEHAEEIASSLE-----ILVATNVLGEGIDVPSLDTVIFFDPPSS-AASYIQRVGRAGRgGKDEGEVILFV 77
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
387-698 |
7.25e-09 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 58.68 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 387 QGDVGCGKT---VVAQLAIVDNFEAGFQSAVMAPTSILAMQHYRRMSPAFEEMGIRTALLLGETSSREK-EKIKRmlsdg 462
Cdd:PTZ00424 71 QAQSGTGKTatfVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDiNKLKA----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 463 EISVVIGT----HTLIQED-VSFSNLGLVIIDEQhrfgvkqrEALVSKG-KALDTLVMTATPIPRTLAL---TIYGD-LD 532
Cdd:PTZ00424 146 GVHMVVGTpgrvYDMIDKRhLRVDDLKLFILDEA--------DEMLSRGfKGQIYDVFKKLPPDVQVALfsaTMPNEiLE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 533 ITVIDEMPPGRKDVKTMLVSVSKLEQVYEFVKKEIAEGGQVFIVYPLIEESDKIQAKAAIRMHEYLSKKIF-GEFRVGLL 611
Cdd:PTZ00424 218 LTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHeRDFTVSCM 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 612 HGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVMI----IENPERFglaqLHqlrgRIGRGDKQGYCFLVVG 687
Cdd:PTZ00424 298 HGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVInydlPASPENY----IH----RIGRSGRFGRKGVAIN 369
|
330
....*....|.
gi 157313485 688 NVDDDALERLR 698
Cdd:PTZ00424 370 FVTPDDIEQLK 380
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
359-681 |
9.81e-09 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 58.74 E-value: 9.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 359 FKLTDSQKEAHRQIR--ADLMSNKPMSrllqgdvgCGKTVVAQLAIVDNFEAGFQSAVMAPTSILAMQHYRRMSpAFEEM 436
Cdd:PRK01172 21 FELYDHQRMAIEQLRkgENVIVSVPTA--------AGKTLIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELS-RLRSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 437 GIRTALLLGETSSrEKEKIKRMlsdgeiSVVIGTH----TLIQEDVSFSN-LGLVIIDEQHRFGVKQRealvskGKALDT 511
Cdd:PRK01172 92 GMRVKISIGDYDD-PPDFIKRY------DVVILTSekadSLIHHDPYIINdVGLIVADEIHIIGDEDR------GPTLET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 512 LVMTA---TPIPRTLAL--TIYGDLDI-------TVIDEMPPGRKDV-----KTMLVSVSKLEQVYE--FVKKEIAEGGQ 572
Cdd:PRK01172 159 VLSSAryvNPDARILALsaTVSNANELaqwlnasLIKSNFRPVPLKLgilyrKRLILDGYERSQVDInsLIKETVNDGGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 573 VfivypLIEESDKiqaKAAIRMHEYLSkKIFGEFR-----------------------VGLLHGKMSQQEKDKIMERFAT 629
Cdd:PRK01172 239 V-----LVFVSSR---KNAEDYAEMLI-QHFPEFNdfkvssennnvyddslnemlphgVAFHHAGLSNEQRRFIEEMFRN 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157313485 630 GEFDILISTTVIEVGIDVPrATVMIIENPERFGLA--------QLHQLRGRIGRG--DKQGY 681
Cdd:PRK01172 310 RYIKVIVATPTLAAGVNLP-ARLVIVRDITRYGNGgirylsnmEIKQMIGRAGRPgyDQYGI 370
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
358-518 |
6.29e-08 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 56.32 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 358 PFKLTDSQKEAHRQIRADLmSNKPMsrLLQGDVGCGKTVVAQLAIVDNFEAGFQSAVMAP----TSilAMQhyRRmspaF 433
Cdd:PRK05580 142 PPTLNPEQAAAVEAIRAAA-GFSPF--LLDGVTGSGKTEVYLQAIAEVLAQGKQALVLVPeialTP--QML--AR----F 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 434 EE-MGIRTALLLGETSSREKEKIKRMLSDGEISVVIGTHtliqedvS-----FSNLGLVIIDEQHRFGVKQRE------- 500
Cdd:PRK05580 211 RArFGAPVAVLHSGLSDGERLDEWRKAKRGEAKVVIGAR-------SalflpFKNLGLIIVDEEHDSSYKQQEgpryhar 283
|
170 180
....*....|....*....|..
gi 157313485 501 --ALVsKGKALD-TLVM-TATP 518
Cdd:PRK05580 284 dlAVV-RAKLENiPVVLgSATP 304
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
486-647 |
2.54e-07 |
|
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: 53.93 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 486 VIIDEQHRFGVKQREALVskgKALDTL--------VMTATpIPRTLALTIYGDLDItVIDEMPPGRKDVKTML---VSVS 554
Cdd:COG1203 272 IILDEVQAYPPYMLALLL---RLLEWLknlggsviLMTAT-LPPLLREELLEAYEL-IPDEPEELPEYFRAFVrkrVELK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 555 K----LEQVYEFVKKEIAEGGQVFIVYPLIeesdkiqaKAAIRMHEYLsKKIFGEFRVGLLHGKMSQQEK----DKIMER 626
Cdd:COG1203 347 EgplsDEELAELILEALHKGKSVLVIVNTV--------KDAQELYEAL-KEKLPDEEVYLLHSRFCPADRseieKEIKER 417
|
170 180
....*....|....*....|.
gi 157313485 627 FATGEFDILISTTVIEVGIDV 647
Cdd:COG1203 418 LERGKPCILVSTQVVEAGVDI 438
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
595-678 |
7.81e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 52.81 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 595 HEYLSKKifgEFRVGLLHGK--------MSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVMI----IENPERFg 662
Cdd:COG1111 370 VEFLSEP---GIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIfyepVPSEIRS- 445
|
90
....*....|....*.
gi 157313485 663 laqlHQLRGRIGRGDK 678
Cdd:COG1111 446 ----IQRKGRTGRKRE 457
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
365-509 |
1.09e-06 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 49.64 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 365 QKEAhrqIRADLMSNKpmSRLLQGDVGCGKTVVAQLAIVDNFEAGFQSAVMAPTSILAMQHYRRMSpAFEEMGIRTALLL 444
Cdd:cd18028 6 QAEA---VRAGLLKGE--NLLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFK-KLEEIGLKVGIST 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157313485 445 GETSSREKEKikrmlsdGEISVVIGTH----TLIQEDVSF-SNLGLVIIDEQHRFGVKQR----EALVSKGKAL 509
Cdd:cd18028 80 GDYDEDDEWL-------GDYDIIVATYekfdSLLRHSPSWlRDVGVVVVDEIHLISDEERgptlESIVARLRRL 146
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
359-519 |
1.33e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 48.82 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 359 FKLTDSQKEAHRQIRAdLMSNKPMSRLLQGDVGCGKTVVAqLAIVDNF--EAGFQSAVM-APTSILAMQHYRRMSPAFEE 435
Cdd:pfam04851 2 LELRPYQIEAIENLLE-SIKNGQKRGLIVMATGSGKTLTA-AKLIARLfkKGPIKKVLFlVPRKDLLEQALEEFKKFLPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 436 MGIRTALLLGETSSREKEKIKrmlsdgeisVVIGT-HTL------IQEDVSFSNLGLVIIDEQHRFGVKQREALVSKGKA 508
Cdd:pfam04851 80 YVEIGEIISGDKKDESVDDNK---------IVVTTiQSLykalelASLELLPDFFDVIIIDEAHRSGASSYRNILEYFKP 150
|
170
....*....|.
gi 157313485 509 LDTLVMTATPI 519
Cdd:pfam04851 151 AFLLGLTATPE 161
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
358-492 |
1.49e-06 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 51.66 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 358 PFKLTDSQKEAHRQIRADLMSNKPMsrLLQGDVGCGKTVV----AQLAIvdnfEAGFQSAVMAPTSILAMQHYRRMSPAF 433
Cdd:COG1198 193 PPTLNEEQQAAVEAIRAAAGGFSVF--LLHGVTGSGKTEVylqaIAEVL----AQGKQALVLVPEIALTPQTVERFRARF 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157313485 434 eemGIRTALLLGETSSREKEKIKRMLSDGEISVVIGTHtliqedvS-----FSNLGLVIIDEQH 492
Cdd:COG1198 267 ---GARVAVLHSGLSDGERLDEWRRARRGEARIVIGTR-------SalfapFPNLGLIIVDEEH 320
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
597-655 |
1.59e-06 |
|
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: 48.40 E-value: 1.59e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 157313485 597 YLSKKIFGEFRVGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVMII 655
Cdd:cd18789 60 EALYRYAKRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQ 118
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
387-490 |
2.54e-06 |
|
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: 48.86 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 387 QGDVGCGKT---VVAQLAIVDNFEAGFQSAVMAPTSILAMQHYRRMSPAFEEMGIRTALLLGETSSREkekIKRMLSDGe 463
Cdd:cd17939 40 QAQSGTGKTatfSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALGDYMGVKVHACIGGTSVRE---DRRKLQYG- 115
|
90 100 110
....*....|....*....|....*....|..
gi 157313485 464 ISVVIGT-----HTLIQEDVSFSNLGLVIIDE 490
Cdd:cd17939 116 PHIVVGTpgrvfDMLQRRSLRTDKIKMFVLDE 147
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
600-701 |
3.73e-06 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 48.78 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 600 KKIFGEFRVG-----LLHGKMSQQekdKIMERFATGEFDILISTTVIEVGIDVPRATVMIIEN------------PER-F 661
Cdd:cd18804 111 KTLFPEARIAridrdTTRKKGALE---KLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGILNadsglnspdfraSERaF 187
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 157313485 662 GLaqLHQLRGRIGRGDKQGYCFLVVGNVDDDALERLRYFS 701
Cdd:cd18804 188 QL--LTQVSGRAGRGDKPGKVIIQTYNPEHPLIQAAKEED 225
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
341-694 |
4.03e-06 |
|
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: 50.60 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 341 LPKKIPGKLAEEFLRKLPFKLTDSQKEAHRQIRAdlmsnkpmsrllqG-DV------GCGKTVVAQLAIVDNFEAGFQSA 413
Cdd:COG1205 37 WPDWLPPELRAALKKRGIERLYSHQAEAIEAARA-------------GkNVviatptASGKSLAYLLPVLEALLEDPGAT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 414 VM--APTSILAMQHYRRMSPAFEEMG--IRTALLLGETSSREKEKIKR----------MLSDGeisvVIGTHTLIQEdvS 479
Cdd:COG1205 104 ALylYPTKALARDQLRRLRELAEALGlgVRVATYDGDTPPEERRWIREhpdivltnpdMLHYG----LLPHHTRWAR--F 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 480 FSNLGLVIIDEQHR----FG--VkqreALVSK---------GKALDTLVMTATpI--PRTLALTIYGdLDITVIDE--MP 540
Cdd:COG1205 178 FRNLRYVVIDEAHTyrgvFGshV----ANVLRrlrricrhyGSDPQFILASAT-IgnPAEHAERLTG-RPVTVVDEdgSP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 541 PGRKDV-------KTMLVSVSKLEQVYEFVKKEIAEGGQVfIVYplieeSDKIQA--KAAIRMHEYLSKKIFGE----FR 607
Cdd:COG1205 252 RGERTFvlwnpplVDDGIRRSALAEAARLLADLVREGLRT-LVF-----TRSRRGaeLLARYARRALREPDLADrvaaYR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 608 VGLLHgkmsqQEKDKIMERFATGEFDILISTTVIEVGIDVPR--ATVMiIENPerFGLAQLHQLRGRIGRGDKQGYCFLV 685
Cdd:COG1205 326 AGYLP-----EERREIERGLRSGELLGVVSTNALELGIDIGGldAVVL-AGYP--GTRASFWQQAGRAGRRGQDSLVVLV 397
|
....*....
gi 157313485 686 VGnvdDDAL 694
Cdd:COG1205 398 AG---DDPL 403
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
385-675 |
9.38e-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: 48.58 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 385 LLQGDVGCGKTVVAQLAIVDNFEAGFQSAVM--APTSILAMQHYRRMSPAFEEMGIRTALLLG-----ETSSREKEKIKR 457
Cdd:cd09639 3 VIEAPTGYGKTEAALLWALHSLKSQKADRVIiaLPTRATINAMYRRAKEAFGETGLYHSSILSsrikeMGDSEEFEHLFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 458 MLSDGEISVVIG--------------THTLIQEDVSFSNLG--LVIIDEQHRFGVKQREALVSKGKAL-----DTLVMTA 516
Cdd:cd09639 83 LYIHSNDTLFLDpitvctidqvlksvFGEFGHYEFTLASIAnsLLIFDEVHFYDEYTLALILAVLEVLkdndvPILLMSA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 517 TpIPRTLaLTIYGDLDItVIDEMPPGRKDVKT---------MLVSVSKLEQVYEFVKKeiaeGGQVFIVYPLIEESDKIQ 587
Cdd:cd09639 163 T-LPKFL-KEYAEKIGY-VEENEPLDLKPNERapfikiesdKVGEISSLERLLEFIKK----GGSVAIIVNTVDRAQEFY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 588 AKAairmheylsKKIFGEFRVGLLHGKMSQQEKDK----IMERFATGEFDILISTTVIEVGIDVPrATVMIIEnperfgL 663
Cdd:cd09639 236 QQL---------KEKGPEEEIMLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLDIS-VDVMITE------L 299
|
330
....*....|..
gi 157313485 664 AQLHQLRGRIGR 675
Cdd:cd09639 300 APIDSLIQRLGR 311
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
615-648 |
1.14e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 49.10 E-value: 1.14e-05
10 20 30
....*....|....*....|....*....|....
gi 157313485 615 MSQQEKDKIMERFATGEFDILISTTVIEVGIDVP 648
Cdd:PRK13766 407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIP 440
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
615-685 |
1.53e-05 |
|
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: 45.42 E-value: 1.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157313485 615 MSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVMIIENPERFGLAQLhQLRGRIGRGdKQGYCFLV 685
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMI-QRMGRTGRK-RQGRVVVL 142
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
391-526 |
1.90e-05 |
|
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: 46.27 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 391 GCGKTVVAQLAI---VDNFEAGFQS--AVMAPTSILAMQHYRRMSPAFEEMGIRTALLLGETSS--REKEKIKRmlSDge 463
Cdd:cd17927 27 GSGKTFVAVLICehhLKKFPAGRKGkvVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSEnvSVEQIVES--SD-- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157313485 464 isVVIGTHTLIQED------VSFSNLGLVIIDEQHR------FGVKQREALVSKGKALDtlvmtatPIPRTLALT 526
Cdd:cd17927 103 --VIIVTPQILVNDlksgtiVSLSDFSLLVFDECHNttknhpYNEIMFRYLDQKLGSSG-------PLPQILGLT 168
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
544-686 |
3.73e-05 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 44.47 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 544 KDVKTMLVSVSklEQVYEFVKKEIAEGGQVfivypLIEESDKiqakaaiRMHEYLSKKIFGefrVGLLHGKMSQQEKDKI 623
Cdd:cd18795 19 LRVDVMNKFDS--DIIVLLKIETVSEGKPV-----LVFCSSR-------KECEKTAKDLAG---IAFHHAGLTREDRELV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157313485 624 MERFATGEFDILISTTVIEVGIDVPRATVmIIENPERFG--------LAQLHQLRGRIGR-G-DKQGYCFLVV 686
Cdd:cd18795 82 EELFREGLIKVLVATSTLAAGVNLPARTV-IIKGTQRYDgkgyrelsPLEYLQMIGRAGRpGfDTRGEAIIMT 153
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
615-672 |
4.65e-05 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 44.12 E-value: 4.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157313485 615 MSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVMIienpeRFGLA----QLHQLRGR 672
Cdd:cd18802 74 MTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVI-----RFDLPktlrSYIQSRGR 130
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
391-518 |
4.88e-05 |
|
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: 45.04 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 391 GCGKTVVAQLAIVDNFEA------GFQSAV-MAPTSILAMQHYRRMSPAFEEMGIRTALLLGETSsrekekikrMLSDGE 463
Cdd:cd18023 27 GSGKTVLFELAILRLLKErnplpwGNRKVVyIAPIKALCSEKYDDWKEKFGPLGLSCAELTGDTE---------MDDTFE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157313485 464 ISvviGTHTLI-------------QEDVSF-SNLGLVIIDEQHRFGvKQR----EALVSKGKALDTLVMTATP 518
Cdd:cd18023 98 IQ---DADIILttpekwdsmtrrwRDNGNLvQLVALVLIDEVHIIK-ENRgatlEVVVSRMKTLSSSSELRGS 166
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
391-688 |
6.78e-05 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 46.38 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 391 GCGKTVVAQLAIVDNFEAGF---QSAVMAPTSILAMQHYRRMSPAFEEM-GIRTALLLGetSSREKEKIkRMLSDGEiSV 466
Cdd:PRK11634 53 GSGKTAAFSLPLLHNLDPELkapQILVLAPTRELAVQVAEAMTDFSKHMrGVNVVALYG--GQRYDVQL-RALRQGP-QI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 467 VIGT------HtLIQEDVSFSNL-GLVI--IDEQHRFG-VKQREALVSKGKALDTLVMTATPIP---RTLALTIYGDLDI 533
Cdd:PRK11634 129 VVGTpgrlldH-LKRGTLDLSKLsGLVLdeADEMLRMGfIEDVETIMAQIPEGHQTALFSATMPeaiRRITRRFMKEPQE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 534 TVIDEMPPGRKDVKTMLVSV---SKLEQVYEFVKKEIAEGGQVFIVypliEESDKIQAKAAIRMHEYLSkkifgefrvGL 610
Cdd:PRK11634 208 VRIQSSVTTRPDISQSYWTVwgmRKNEALVRFLEAEDFDAAIIFVR----TKNATLEVAEALERNGYNS---------AA 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157313485 611 LHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVMIIENPERFGLAQLHQLrGRIGRGDKQGYCFLVVGN 688
Cdd:PRK11634 275 LNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRI-GRTGRAGRAGRALLFVEN 351
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
391-518 |
8.35e-05 |
|
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: 43.45 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 391 GCGKTVVAQLAIVDNFEAGFqsAVMAPTSILAMQHYRRmspaFEEmgirtallLGETSSREKEKIKRMLSDGEISVVIGT 470
Cdd:cd17926 28 GSGKTLTALALIAYLKELRT--LIVVPTDALLDQWKER----FED--------FLGDSSIGLIGGGKKKDFDDANVVVAT 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 157313485 471 H---TLIQEDVS--FSNLGLVIIDEQHRFGVKQREALVSKGKALDTLVMTATP 518
Cdd:cd17926 94 YqslSNLAEEEKdlFDQFGLLIVDEAHHLPAKTFSEILKELNAKYRLGLTATP 146
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
594-655 |
8.73e-05 |
|
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: 42.85 E-value: 8.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157313485 594 MHEYLSKKifgEFRVGLLHGKMSQQEKDKIMERFAT--GEFDILISTTVIEVGIDVPRATVMII 655
Cdd:cd18793 43 LEEALRER---GIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGVGLNLTAANRVIL 103
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
568-639 |
9.51e-05 |
|
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: 43.86 E-value: 9.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157313485 568 AEGGQVFIVYPliEESDKIQAKAAIRMheyLSKKIFGEFRVGLLHGKMSQQEKDKIMERFATGEFDILISTT 639
Cdd:cd17924 58 SKGKRSYLIFP--TKSLVKQAYERLSK---YAEKAGVEVKILVYHSRLKKKEKEELLEKIEKGDFDILVTTN 124
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
391-532 |
1.40e-04 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 42.96 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 391 GCGKTVVAQLAIVDNF----EAGFQSAVMAPTSILAMQHYRRMSPAFEEM--GIRTALLLGETSSREKEKIKRMLSDgei 464
Cdd:cd17922 11 GSGKTEAAFLPALSSLadepEKGVQVLYISPLKALINDQERRLEEPLDEIdlEIPVAVRHGDTSQSEKAKQLKNPPG--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 465 sVVIGT-----HTLIQE--DVSFSNLGLVIIDEQHRF-----GVkQREALVSKgkaLDTLvmTATPIPRT-LALTIyGDL 531
Cdd:cd17922 88 -ILITTpesleLLLVNKklRELFAGLRYVVVDEIHALlgskrGV-QLELLLER---LRKL--TGRPLRRIgLSATL-GNL 159
|
.
gi 157313485 532 D 532
Cdd:cd17922 160 E 160
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
607-651 |
1.83e-04 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 44.58 E-value: 1.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 157313485 607 RVGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRAT 651
Cdd:PRK04837 281 RVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVT 325
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
389-654 |
4.81e-04 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 43.68 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 389 DVGCGKTVVAQLAIVDNFEAGFQSAVM--APTSILA--MQHYRRMSPafeemGIRTALLlgeTSSREKEKIKRMLSDGEi 464
Cdd:COG0553 268 DMGLGKTIQALALLLELKERGLARPVLivAPTSLVGnwQRELAKFAP-----GLRVLVL---DGTRERAKGANPFEDAD- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 465 sVVIGTHTLIQEDV-SFSNL--GLVIIDEQHRfgVKQREALVSK-GKALDT---LVMTATPIP----------RTLALTI 527
Cdd:COG0553 339 -LVITSYGLLRRDIeLLAAVdwDLVILDEAQH--IKNPATKRAKaVRALKArhrLALTGTPVEnrleelwsllDFLNPGL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 528 YGDLD---------IT-------------------------VIDEMPPgrKDVKTMLVSVSKLEQ-----VYEFVKKEIA 568
Cdd:COG0553 416 LGSLKafrerfarpIEkgdeealerlrrllrpfllrrtkedVLKDLPE--KTEETLYVELTPEQRalyeaVLEYLRRELE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 569 E------GGQVF--------------IVYPLIEESDKIQAKAA----------------------IRMHEYLSKKIFGE- 605
Cdd:COG0553 494 GaegirrRGLILaaltrlrqicshpaLLLEEGAELSGRSAKLEallelleellaegekvlvfsqfTDTLDLLEERLEERg 573
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 157313485 606 FRVGLLHGKMSQQEKDKIMERFATGE--FDILISTTVIEVGIDVPRATVMI 654
Cdd:COG0553 574 IEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVI 624
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
391-493 |
4.85e-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: 41.73 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 391 GCGKTVVAQLAIVDNFEA-GFQSAVMAPTSILAMQHYRRMSPAFeEMGIRTALLLGETSSREKEKIKRmlsdgEISVVIG 469
Cdd:cd18035 26 GLGKTIIAILVAADRLTKkGGKVLILAPSRPLVEQHAENLKRVL-NIPDKITSLTGEVKPEERAERWD-----ASKIIVA 99
|
90 100
....*....|....*....|....*....
gi 157313485 470 THTLIQED-----VSFSNLGLVIIDEQHR 493
Cdd:cd18035 100 TPQVIENDllagrITLDDVSLLIFDEAHH 128
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
393-705 |
4.97e-04 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 43.65 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 393 GKTVVAQLAIVDN-FEAGFQSAVMAPTSILAMQHYRRMSpAFEEMGIRTALLLGETSSREKEKikrmlsdGEISVVIGT- 470
Cdd:PRK00254 51 GKTLVAEIVMVNKlLREGGKAVYLVPLKALAEEKYREFK-DWEKLGLRVAMTTGDYDSTDEWL-------GKYDIIIATa 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 471 ---HTLIQEDVSF-SNLGLVIIDEQHRFGVKQREALVSK------GKAlDTLVMTATpIPRTLALTIYGDLDITVIDEMP 540
Cdd:PRK00254 123 ekfDSLLRHGSSWiKDVKLVVADEIHLIGSYDRGATLEMilthmlGRA-QILGLSAT-VGNAEELAEWLNAELVVSDWRP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 541 PG-RKDV-----------KTMLVSVSKLEQVYEFVKKeiaeGGQVFIVYPLIEESDKIQAKAAIRMHEYLSKKIFGEFR- 607
Cdd:PRK00254 201 VKlRKGVfyqgflfwedgKIERFPNSWESLVYDAVKK----GKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKe 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 608 ---------------------VGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPrATVMIIENPER---FGL 663
Cdd:PRK00254 277 ladsleenptneklkkalrggVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLP-AFRVIIRDTKRysnFGW 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 157313485 664 A-----QLHQLRGRIGRG--DKQGYCfLVVGNVDDDALERLRY--------FSMTKN 705
Cdd:PRK00254 356 EdipvlEIQQMMGRAGRPkyDEVGEA-IIVATTEEPSKLMERYifgkpeklFSMLSN 411
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
611-694 |
5.06e-04 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 43.24 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 611 LHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDVPRATVMIIENPERFGLAQLHQLrGRIGRGDKQGYCFLVVgNVD 690
Cdd:PLN00206 398 IHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQI-GRASRMGEKGTAIVFV-NEE 475
|
....
gi 157313485 691 DDAL 694
Cdd:PLN00206 476 DRNL 479
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
163-238 |
5.10e-04 |
|
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: 39.14 E-value: 5.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157313485 163 TTRGKVVNVETKKIGSMTITaavLADGVSQLLLKWFNQEYLHKGLQVLKNKTIYATGLVKHSQFGGIEMVNPEIEP 238
Cdd:pfam01336 2 TVAGRVTSIRRSGGKLLFLT---LRDGTGSIQVVVFKEEAEKLAKKLKEGDVVRVTGKVKKRKGGELELVVEEIEL 74
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
588-687 |
6.16e-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: 40.70 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 588 AKAAIRMHEYLSKKIFGeFRVGLLhgkmsQQEKDKIMERFATGEFDILISTTVIEVGIDVPR--ATVMiIENPerFGLAQ 665
Cdd:cd18797 55 LKARLVEEGPLASKVAS-YRAGYL-----AEDRREIEAELFNGELLGVVATNALELGIDIGGldAVVL-AGYP--GSLAS 125
|
90 100
....*....|....*....|..
gi 157313485 666 LHQLRGRIGRGDKqGYCFLVVG 687
Cdd:cd18797 126 LWQQAGRAGRRGK-DSLVILVA 146
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
391-495 |
1.82e-03 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 40.32 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 391 GCGKTVVAQLAIVDNFEAGFQS-AV-MAPTSILAMQHYRRMSPAFEE-MGIRTALLLGETSSREKekikrMLSDGEisVV 467
Cdd:cd18021 29 GSGKTVCAELALLRHWRQNPKGrAVyIAPMQELVDARYKDWRAKFGPlLGKKVVKLTGETSTDLK-----LLAKSD--VI 101
|
90 100 110
....*....|....*....|....*....|....*..
gi 157313485 468 IGTHTliQEDV---------SFSNLGLVIIDEQHRFG 495
Cdd:cd18021 102 LATPE--QWDVlsrrwkqrkNVQSVELFIADELHLIG 136
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
389-520 |
2.57e-03 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350677 [Multi-domain] Cd Length: 182 Bit Score: 39.47 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 389 DVGCGKTVVAqLAIVD----NFEAGFQSAVMAPTSILamQHYRRmspAFEE--MGIRTALLLGETSSREKEKIKRMLSDG 462
Cdd:cd17919 27 EMGLGKTLQA-IAFLAyllkEGKERGPVLVVCPLSVL--ENWER---EFEKwtPDLRVVVYHGSQRERAQIRAKEKLDKF 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157313485 463 EisVVIGTHTLIQEDVSFS---NLGLVIIDEQHRfgVKQREALVSK-GKALDT---LVMTATPIP 520
Cdd:cd17919 101 D--VVLTTYETLRRDKASLrkfRWDLVVVDEAHR--LKNPKSQLSKaLKALRAkrrLLLTGTPLQ 161
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
411-490 |
3.21e-03 |
|
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: 39.35 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 411 QSAVMAPTSILAMQHYRRMSPAFEEMGIRTALLLGETSsreKEKIKRMLSDGeISVVIGT----HTLIQE-DVSFSNLGL 485
Cdd:cd00268 64 QALVLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAP---IKKQIEALKKG-PDIVVGTpgrlLDLIERgKLDLSNVKY 139
|
....*
gi 157313485 486 VIIDE 490
Cdd:cd00268 140 LVLDE 144
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
388-517 |
4.55e-03 |
|
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA polymerase I transcription of the 47S precursor rRNA. DHX33 belongs to 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: 438710 [Multi-domain] Cd Length: 178 Bit Score: 38.87 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 388 GDVGCGKTV-VAQLAivdnFEAGFQS----AVMAPTSILAMQHYRRMSpafEEMGIRTALLLG-----ETSSREKEKIKR 457
Cdd:cd17978 24 GETGSGKTTqIPQYL----YEAGFARggmiGITQPRRVAAVSVAKRVA---EEMGVELGQLVGysvrfDDVTSEETRIKY 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157313485 458 MlSDGeisvvigthTLIQE---DVSFSNLGLVIIDEQHR--------FGV---KQREALVSKGKALDTLVMTAT 517
Cdd:cd17978 97 M-TDG---------MLLREaigDPLLSKYSVIILDEAHErtvhtdvlFGLvksAQRRRKEQKLSPLKVIIMSAT 160
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
391-493 |
5.42e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 40.24 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157313485 391 GCGKTVVAQLAIVDNFEA-GFQSAVMAPTSILAMQHYRRMSPAFEEMGIRTALLLGETSSREKEKIKRmlsdgEISVVIG 469
Cdd:PRK13766 39 GLGKTAIALLVIAERLHKkGGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKRAELWE-----KAKVIVA 113
|
90 100
....*....|....*....|....*....
gi 157313485 470 THTLIQED-----VSFSNLGLVIIDEQHR 493
Cdd:PRK13766 114 TPQVIENDliagrISLEDVSLLIFDEAHR 142
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
605-675 |
6.80e-03 |
|
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: 38.01 E-value: 6.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157313485 605 EFRVGLLHGKMSQQEKDKIMERFATGEFDILISTTVIEVGIDV-PRATVMIIENPerFGLAQLHQlrgRIGR 675
Cdd:cd18796 68 PDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIgDVDLVIQIGSP--KSVARLLQ---RLGR 134
|
|
| |
