|
Name |
Accession |
Description |
Interval |
E-value |
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
1-488 |
0e+00 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 674.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 1 MAALEeIELTQLKGVGAKLAETLSKLDIHNMQDLLFHLPFRYEDRTRIHSAASLRPGMQGLFEVEVLGSRVVH--GRRRS 78
Cdd:COG1200 1 MAPLD-TPLTYLKGVGPKRAKLLAKLGIRTVGDLLFHLPRRYEDRTRLTPIAELRPGETVTVEGTVVSVEVVRrrRRRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 79 LEVKVKDASGTVTLRFYHFsAAQARQLQKGTYLRCYGEARLGKLGIEFYHPEYNIITGDEKNTAPeTLTPVYPLTEGIQQ 158
Cdd:COG1200 80 LEVTLSDGTGSLTLVFFNQ-PYLKKQLKPGTRVLVSGKVERFRGGLQMVHPEYELLDEEEAELAG-RLTPVYPLTEGLSQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 159 ARLRAICRQALGWLDRcDVRDLLPPSIRKAYQLPELKHALSYLHAPPTEADqlallegRHLCQQRLIVEELLGHHLSLLK 238
Cdd:COG1200 158 KTLRKLIRQALDLLAP-DLPEPLPEELRARYGLPSLAEALRNIHFPPSDED-------LHPARRRLAFEELLALQLALLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 239 LRKGVQSHQALPCQNNSQLGTQLLEQLPFELTGAQKKVCSDVDHDLGQAFPMLRLVQGDVGSGKTIVAALAALKVVESGA 318
Cdd:COG1200 230 RRARRRKRKGPALPGDGELLEAFLAALPFELTGAQKRVIAEIAADLASPHPMNRLLQGDVGSGKTVVALLAMLAAVEAGY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 319 QVALMAPTEILAEQHLLNFSQWFAELklpdgnSIEIAWLSGKSKGKTRAAALGKIASGNAQVVIGTHALFQDEVKFSRLA 398
Cdd:COG1200 310 QAALMAPTEILAEQHYRSLSKLLEPL------GIRVALLTGSTKAKERREILAALASGEADIVVGTHALIQDDVEFKNLG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 399 LAIIDEQHRFGVHQRLSLKNKGQdsglVPHQLIMTATPIPRTLAMSAYADLDTSVIDELPPGRQKIETFAIPDSRRSEMV 478
Cdd:COG1200 384 LVVIDEQHRFGVEQRLALREKGE----APHVLVMTATPIPRTLAMTLYGDLDVSVIDELPPGRKPIKTRVVPEERRDEVY 459
|
490
....*....|
gi 1024592031 479 ERVRKSCEAG 488
Cdd:COG1200 460 ERIREEIAKG 469
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
1-488 |
0e+00 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 648.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 1 MAALEEIELTQLKGVGAKLAETLSKLDIHNMQDLLFHLPFRYEDRTRIHSAASLRPGMQGLFEVEVLGSRVVHGRRRSLE 80
Cdd:PRK10917 3 LLLLLDAPLTSLKGVGPKTAEKLAKLGIHTVQDLLLHLPRRYEDRTRLKPIAELRPGEKVTVEGEVLSAEVVFGKRRRLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 81 VKVKDASGTVTLRFYHFSAAQ-ARQLQKGTYLRCYGEARLGKLGIEFYHPEYNIITGDEKNTAPeTLTPVYPLTEGIQQA 159
Cdd:PRK10917 83 VTVSDGTGNLTLRFFNFNQPYlKKQLKVGKRVAVYGKVKRGKYGLEMVHPEYEVLEEESPELEG-RLTPVYPLTEGLKQK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 160 RLRAICRQALGWLDrcDVRDLLPPSIRKAYQLPELKHALSYLHAPPTEADqlallegRHLCQQRLIVEELLGHHLSLLKL 239
Cdd:PRK10917 162 TLRKLIKQALELLD--ALPELLPEELLEKYGLLSLAEALRAIHFPPSDED-------LHPARRRLKFEELFALQLSLLLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 240 RKGVQSHQALPCQNNSQLGTQLLEQLPFELTGAQKKVCSDVDHDLGQAFPMLRLVQGDVGSGKTIVAALAALKVVESGAQ 319
Cdd:PRK10917 233 RAGRRSKKAGPLPYDGELLKKFLASLPFELTGAQKRVVAEILADLASPKPMNRLLQGDVGSGKTVVAALAALAAIEAGYQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 320 VALMAPTEILAEQHLLNFSQWFAELklpdgnSIEIAWLSGKSKGKTRAAALGKIASGNAQVVIGTHALFQDEVKFSRLAL 399
Cdd:PRK10917 313 AALMAPTEILAEQHYENLKKLLEPL------GIRVALLTGSLKGKERREILEAIASGEADIVIGTHALIQDDVEFHNLGL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 400 AIIDEQHRFGVHQRLSLKNKGQDsglvPHQLIMTATPIPRTLAMSAYADLDTSVIDELPPGRQKIETFAIPDSRRSEMVE 479
Cdd:PRK10917 387 VIIDEQHRFGVEQRLALREKGEN----PHVLVMTATPIPRTLAMTAYGDLDVSVIDELPPGRKPITTVVIPDSRRDEVYE 462
|
....*....
gi 1024592031 480 RVRKSCEAG 488
Cdd:PRK10917 463 RIREEIAKG 471
|
|
| recG |
TIGR00643 |
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair] |
26-488 |
9.80e-162 |
|
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273192 [Multi-domain] Cd Length: 630 Bit Score: 472.21 E-value: 9.80e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 26 LDIHNMQDLLFHLPFRYEDRTRIHSAASLRPGMQGLFEVEVLG-SRVVHGRRRSLEVKVKDASG-TVTLRFYHfSAAQAR 103
Cdd:TIGR00643 1 LGIHTVQDLLFYFPRRYEDRTLLQTIGELLPGERATIVGEVLShCIFGFKRRKVLKLRLKDGGYkKLELRFFN-RAFLKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 104 QLQKGTYLRCYGEARLGKLGIEFYHPEYNIitGDEKNTAPETLTPVYPLTEGIQQARLRAICRQALGWLDRCdVRDLLPP 183
Cdd:TIGR00643 80 KFKVGSKVVVYGKVKSSKFKAYLIHPEFIS--EKDGVEFELKILPVYPLTEGLTQKKLRKLIQQALDQLDKS-LEDPLPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 184 SIRKAYQLPELKHALSYLHAPPTeadqlalLEGRHLCQQRLIVEELLGHHLSLLKLRKGVQSHQALPCQN-NSQLGTQLL 262
Cdd:TIGR00643 157 ELREKYGLLSLEDALRAIHFPKT-------LSLLELARRRLIFDEFFYLQLAMLARRLGEKQQFSAPPANpSEELLTKFL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 263 EQLPFELTGAQKKVCSDVDHDLGQAFPMLRLVQGDVGSGKTIVAALAALKVVESGAQVALMAPTEILAEQHLLNFSQWFA 342
Cdd:TIGR00643 230 ASLPFKLTRAQKRVVKEILQDLKSDVPMNRLLQGDVGSGKTLVAALAMLAAIEAGYQVALMAPTEILAEQHYNSLRNLLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 343 ELklpdgnSIEIAWLSGKSKGKTRAAALGKIASGNAQVVIGTHALFQDEVKFSRLALAIIDEQHRFGVHQRLSLKNKGQd 422
Cdd:TIGR00643 310 PL------GIEVALLTGSLKGKRRKELLETIASGQIHLVVGTHALIQEKVEFKRLALVIIDEQHRFGVEQRKKLREKGQ- 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024592031 423 SGLVPHQLIMTATPIPRTLAMSAYADLDTSVIDELPPGRQKIETFAIPDSRRSEMVERVRKSCEAG 488
Cdd:TIGR00643 383 GGFTPHVLVMSATPIPRTLALTVYGDLDTSIIDELPPGRKPITTVLIKHDEKDIVYEFIEEEIAKG 448
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
224-458 |
8.60e-114 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350750 [Multi-domain] Cd Length: 225 Bit Score: 334.89 E-value: 8.60e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 224 LIVEELLGHHLSLLKLRKGVQSHQALPCQNNSQLGTQLLEQLPFELTGAQKKVCSDVDHDLGQAFPMLRLVQGDVGSGKT 303
Cdd:cd17992 1 LAFEELFALQLALLLRRRKIEELKGIILEISGELLKKFLEALPFELTGAQKRVIDEILRDLASEKPMNRLLQGDVGSGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 304 IVAALAALKVVESGAQVALMAPTEILAEQHLLNFSQWFAELKlpdgnsIEIAWLSGKSKGKTRAAALGKIASGNAQVVIG 383
Cdd:cd17992 81 VVAALAMLAAVENGYQVALMAPTEILAEQHYDSLKKLLEPLG------IRVALLTGSTKAKEKREILEKIASGEIDIVIG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024592031 384 THALFQDEVKFSRLALAIIDEQHRFGVHQRLSLKNKGQDsglvPHQLIMTATPIPRTLAMSAYADLDTSVIDELP 458
Cdd:cd17992 155 THALIQEDVEFHNLGLVIIDEQHRFGVEQRLKLREKGET----PHVLVMTATPIPRTLALTLYGDLDVSIIDELP 225
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
260-455 |
6.96e-60 |
|
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: 194.56 E-value: 6.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 260 QLLEQLPFELTGAQKKVCSDVDHDLGQAFPMLRLVQGDVGSGKTIVAALAALKVVESGAQVALMAPTEILAEQHLLNFSQ 339
Cdd:cd17918 7 ELCKSLPFSLTKDQAQAIKDIEKDLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 340 WFAElklpdgnsIEIAWLSGKSKgktraaalGKIASGnAQVVIGTHALFQDEVKFSRLALAIIDEQHRFGVHQRLSLKNK 419
Cdd:cd17918 87 FLPF--------INVELVTGGTK--------AQILSG-ISLLVGTHALLHLDVKFKNLDLVIVDEQHRFGVAQREALYNL 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1024592031 420 GQdsglvPHQLIMTATPIPRTLAMSAYADLDTSVID 455
Cdd:cd17918 150 GA-----THFLEATATPIPRTLALALSGLLDLSVID 180
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
260-455 |
2.84e-59 |
|
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: 193.56 E-value: 2.84e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 260 QLLEQLPFELTGAQKKVCSDVDHDLGQAFPMLRLVQGDVGSGKTIVAALAALKVVESGAQVALMAPTEILAEQHLLNFSQ 339
Cdd:cd17991 7 EFEASFPYEETPDQLKAIEEILKDMESGKPMDRLICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQHYETFKE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 340 WFAELKlpdgnsIEIAWLSGKSKGKTRAAALGKIASGNAQVVIGTHALFQDEVKFSRLALAIIDEQHRFGVHQRLSLKNK 419
Cdd:cd17991 87 RFANFP------VNVELLSRFTTAAEQREILEGLKEGKVDIVIGTHRLLSKDVEFKNLGLLIIDEEQRFGVKQKEKLKEL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1024592031 420 GQDSglvpHQLIMTATPIPRTLAMSAYADLDTSVID 455
Cdd:cd17991 161 RPNV----DVLTLSATPIPRTLHMALSGIRDLSVIA 192
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
226-470 |
7.78e-51 |
|
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: 186.02 E-value: 7.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 226 VEELLGHHLSLLKLRKGVQSHqALPCQNNSQLgtQLLEQLPFELTGAQKKVCSDVDHDLGQAFPMLRLVQGDVGSGKTIV 305
Cdd:TIGR00580 412 VREIAAKLIELYAKRKAIKGH-AFPPDLEWQQ--EFEDSFPFEETPDQLKAIEEIKADMESPRPMDRLVCGDVGFGKTEV 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 306 AALAALKVVESGAQVALMAPTEILAEQHLLNFSQWFAelklpdGNSIEIAWLSGKSKGKTRAAALGKIASGNAQVVIGTH 385
Cdd:TIGR00580 489 AMRAAFKAVLDGKQVAVLVPTTLLAQQHFETFKERFA------NFPVTIELLSRFRSAKEQNEILKELASGKIDILIGTH 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 386 ALFQDEVKFSRLALAIIDEQHRFGVHQRLSLKnkgQDSGLVpHQLIMTATPIPRTLAMSAYADLDTSVIDELPPGRQKIE 465
Cdd:TIGR00580 563 KLLQKDVKFKDLGLLIIDEEQRFGVKQKEKLK---ELRTSV-DVLTLSATPIPRTLHMSMSGIRDLSIIATPPEDRLPVR 638
|
....*
gi 1024592031 466 TFAIP 470
Cdd:TIGR00580 639 TFVME 643
|
|
| Mfd |
COG1197 |
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ... |
266-470 |
1.01e-47 |
|
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription];
Pssm-ID: 440810 [Multi-domain] Cd Length: 1130 Bit Score: 177.18 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 266 PFELTGAQKKVCSDVDHDLGQAFPMLRLVQGDVGSGKTIVAALAALKVVESGAQVALMAPTEILAEQHLLNFSQWFAElk 345
Cdd:COG1197 584 PYEETPDQLRAIEEVKADMESPRPMDRLVCGDVGFGKTEVALRAAFKAVMDGKQVAVLVPTTLLAQQHYETFKERFAG-- 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 346 LPdgnsIEIAWLSG-KSKGKTRaAALGKIASGNAQVVIGTHALFQDEVKFSRLALAIIDEQHRFGVHQ--RL-SLKNKgq 421
Cdd:COG1197 662 FP----VRVEVLSRfRTAKEQK-ETLEGLADGKVDIVIGTHRLLSKDVKFKDLGLLIIDEEQRFGVRHkeKLkALRAN-- 734
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1024592031 422 dsglVpHQLIMTATPIPRTLAMSayadL----DTSVIDELPPGRQKIETFAIP 470
Cdd:COG1197 735 ----V-DVLTLTATPIPRTLQMS----LsgirDLSIIATPPEDRLPVKTFVGE 778
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
263-467 |
1.57e-35 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 141.04 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 263 EQLPFELTGAQKKVCSDVDHDLGQAFPMLRLVQGDVGSGKTIVAALAALKVVESGAQVALMAPTEILAEQHLLNFSQWFA 342
Cdd:PRK10689 595 DSFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQHYDNFRDRFA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 343 ELklpdgnSIEIAWLSGKSKGKTRAAALGKIASGNAQVVIGTHALFQDEVKFSRLALAIIDEQHRFGVHQRLSLKNKGQD 422
Cdd:PRK10689 675 NW------PVRIEMLSRFRSAKEQTQILAEAAEGKIDILIGTHKLLQSDVKWKDLGLLIVDEEHRFGVRHKERIKAMRAD 748
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024592031 423 SGLvphqLIMTATPIPRTLAMSAYADLDTSVIDELPPGRQKIETF 467
Cdd:PRK10689 749 VDI----LTLTATPIPRTLNMAMSGMRDLSIIATPPARRLAVKTF 789
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
261-462 |
6.65e-22 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 93.33 E-value: 6.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 261 LLEQLPFELTGAQKKVCSDVDHDLgqafpMLRLVQGDVGSGKTIVAALAALKVV--ESGAQVALMAPTEILAEQHLLNFS 338
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGL-----RDVILAAPTGSGKTLAALLPALEALkrGKGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 339 QWFAELKLpdgnsIEIAWLSGKSKGKTRAaalgKIASGNAQVVIGT-----HALFQDEVKFSRLALAIIDEQHRFGVHQR 413
Cdd:smart00487 76 KLGPSLGL-----KVVGLYGGDSKREQLR----KLESGKTDILVTTpgrllDLLENDKLSLSNVDLVILDEAHRLLDGGF 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1024592031 414 LS-LKNKGQDSGLVPHQLIMTATP---IPRTLAMSAYADLDTSVIDELPPGRQ 462
Cdd:smart00487 147 GDqLEKLLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIE 199
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
286-445 |
2.55e-20 |
|
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: 87.68 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 286 QAFPMLR-----LVQGDVGSGKTIVAALAALKVVE---SGAQVALMAPTEILAEQHLLNFSQWFAELKlpdgnsIEIAWL 357
Cdd:pfam00270 6 EAIPAILegrdvLVQAPTGSGKTLAFLLPALEALDkldNGPQALVLAPTRELAEQIYEELKKLGKGLG------LKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 358 SGkskGKTRAAALGKIAsgNAQVVIGTH----ALFQDEVKFSRLALAIIDEQHRFGvhqrlslknkgqDSGLVPH-QLIM 432
Cdd:pfam00270 80 LG---GDSRKEQLEKLK--GPDILVGTPgrllDLLQERKLLKNLKLLVLDEAHRLL------------DMGFGPDlEEIL 142
|
170
....*....|....
gi 1024592031 433 TATPIPR-TLAMSA 445
Cdd:pfam00270 143 RRLPKKRqILLLSA 156
|
|
| RecG_wedge_OBF |
cd04488 |
RecG_wedge_OBF: A subfamily of OB folds corresponding to the OB fold found in the N-terminal ... |
62-131 |
5.46e-19 |
|
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: 81.09 E-value: 5.46e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024592031 62 FEVEVLGSRVVHGRRRS-LEVKVKDASGTVTLRFYHFSAAQARQLQKGTYLRCYGEARLGKLGIEFYHPEY 131
Cdd:cd04488 2 VEGTVVSVEVVPRRGRRrLKVTLSDGTGTLTLVFFNFQPYLKKQLPPGTRVRVSGKVKRFRGGLQIVHPEY 72
|
|
| RecG_wedge |
pfam17191 |
RecG wedge domain; This DNA-binding domain has an OB-fold with large elaborations. |
13-170 |
2.56e-17 |
|
RecG wedge domain; This DNA-binding domain has an OB-fold with large elaborations.
Pssm-ID: 407316 [Multi-domain] Cd Length: 162 Bit Score: 79.02 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 13 KGVGAKLAETLSKLDIHNMQDLLFHLPFRYEDRTRIHSAASLRPGMQGL-------FEVEVLGSRVVhgrrrsLEVKVKD 85
Cdd:pfam17191 6 KGVGPKREKILKKLGIETIGDLIWYFPRDYEDRRKIIPISDIRHDEKVTtkgkivnFETKKIGSLVI------ISAVLSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 86 ASGTVTLRFYHFSAAQARqLQKGTYLRCYGEARLGKLG-IEFYHPEYNIITGdeknTAPETLTPVYPLTEGIQQARLRAI 164
Cdd:pfam17191 80 GIGQVLLKWFNQEYIKKF-LQKGKEVYITGTVKEGPFGpIEMNNPEIEEITG----EQEREILPVYPLTEGISQKNMRKI 154
|
....*.
gi 1024592031 165 CRQALG 170
Cdd:pfam17191 155 VKENIS 160
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
290-435 |
1.51e-13 |
|
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: 67.81 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 290 MLRLVQGDVGSGKTIVAALAALKVVES-GAQVALMAPTEILAEQHLLNFSQWFAElklpdGNSIEIawLSGKSKGKTRAa 368
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKkGKKVLVLVPTKALALQTAERLRELFGP-----GIRVAV--LVGGSSAEERE- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024592031 369 algKIASGNAQVVIGTHA------LFQDEVKFSRLALAIIDEQHRFGV--HQRLSLKNKGQDSGLVPHQLI-MTAT 435
Cdd:cd00046 74 ---KNKLGDADIIIATPDmllnllLREDRLFLKDLKLIIVDEAHALLIdsRGALILDLAVRKAGLKNAQVIlLSAT 146
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
153-406 |
1.98e-11 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 66.33 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 153 TEGIQQARLRAIcrqalgwLDRCDVRDLLPPSIRkayQLpeLKHALSYLHAPPTEADQLALLEGRHLCQQRLIVEELLGH 232
Cdd:PRK05580 52 GSEVPADKLKPI-------LEVLDLEPLLPPELL---RL--LDWAADYYLSPLGEVLRLALLAELALAASSAVLKGLVKK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 233 HLsllkLRKGVQSHQALPCQNNSqlgtqllEQLPFELTGAQKKVCSDVDHDLG-QAFpmlrLVQGDVGSGKTIV--AALA 309
Cdd:PRK05580 120 GL----IELEEVEVLRLRPPPDP-------AFEPPTLNPEQAAAVEAIRAAAGfSPF----LLDGVTGSGKTEVylQAIA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 310 AlkVVESGAQVALMAPtEI-LAEQHLLNFSQWFaelklpdGNSIEIaWLSGKSKGKtRAAALGKIASGNAQVVIGTH-AL 387
Cdd:PRK05580 185 E--VLAQGKQALVLVP-EIaLTPQMLARFRARF-------GAPVAV-LHSGLSDGE-RLDEWRKAKRGEAKVVIGARsAL 252
|
250
....*....|....*....
gi 1024592031 388 FqdeVKFSRLALAIIDEQH 406
Cdd:PRK05580 253 F---LPFKNLGLIIVDEEH 268
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
293-406 |
5.16e-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: 61.46 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 293 LVQGDVGSGKTIVAALAALKVVESGAQVALMAPtEI-LAEQHLLNFSQWFaelklpdGNSIEIaWLSGKSKGKtRAAALG 371
Cdd:cd17929 19 LLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVP-EIsLTPQLIKRFKKRF-------GDKVAV-LHSKLSDKE-RADEWR 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 1024592031 372 KIASGNAQVVIGTH-ALFqdeVKFSRLALAIIDEQH 406
Cdd:cd17929 89 KIKRGEAKVVIGARsALF---APFKNLGLIIVDEEH 121
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
299-437 |
3.02e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 53.06 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 299 GSGKTIVAALAALKVVESGAQ--VALMAPTEILAEQHLLNFSQWFaelklPDGNSIEIAWlSGKSKgktraaalgKIASG 376
Cdd:pfam04851 33 GSGKTLTAAKLIARLFKKGPIkkVLFLVPRKDLLEQALEEFKKFL-----PNYVEIGEII-SGDKK---------DESVD 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 377 NAQVVIGT-HALFQDEVKFSRLALA------IIDEQHRFG--VHQRLSLKNKGqdsglvPHQLIMTATPI 437
Cdd:pfam04851 98 DNKIVVTTiQSLYKALELASLELLPdffdviIIDEAHRSGasSYRNILEYFKP------AFLLGLTATPE 161
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
299-436 |
7.21e-08 |
|
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: 52.52 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 299 GSGKTIVAALAALKVVES-GAQVALMAPTEILAEQHLLNFSQWfaeLKLPDgnsiEIAWLSGKSKGKTRAAAL--GKIAS 375
Cdd:cd18035 26 GLGKTIIAILVAADRLTKkGGKVLILAPSRPLVEQHAENLKRV---LNIPD----KITSLTGEVKPEERAERWdaSKIIV 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024592031 376 GNAQVVigTHALFQDEVKFSRLALAIIDEQHR-FGVHQRLSLKNKGQDSGLVPHQLIMTATP 436
Cdd:cd18035 99 ATPQVI--ENDLLAGRITLDDVSLLIFDEAHHaVGNYAYVYIAHRYKREANNPLILGLTASP 158
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
299-436 |
1.58e-07 |
|
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: 51.66 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 299 GSGKTIVAALAA---LKVVESG--AQVALMAPTEILAEQHLLNFSQWFAELKLpdgnsiEIAWLSGKSKGKTRAAALGKi 373
Cdd:cd17927 27 GSGKTFVAVLICehhLKKFPAGrkGKVVFLANKVPLVEQQKEVFRKHFERPGY------KVTGLSGDTSENVSVEQIVE- 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024592031 374 asgNAQVVIGTHALFQD------EVKFSRLALAIIDEQHR------FGVHQRLSLKNKGQDSGLVPHQLIMTATP 436
Cdd:cd17927 100 ---SSDVIIVTPQILVNdlksgtIVSLSDFSLLVFDECHNttknhpYNEIMFRYLDQKLGSSGPLPQILGLTASP 171
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
266-406 |
3.45e-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: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 266 PFELTGAQKKVCSDVDHDLG--QAFpmlrLVQGDVGSGKTIV--AALAalKVVESGAQVALMAPtEI-LAEQHLLNFSQW 340
Cdd:COG1198 193 PPTLNEEQQAAVEAIRAAAGgfSVF----LLHGVTGSGKTEVylQAIA--EVLAQGKQALVLVP-EIaLTPQTVERFRAR 265
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024592031 341 FaelklpdGNSIEIaWLSGKSKGKtRAAALGKIASGNAQVVIGTH-ALFqdeVKFSRLALAIIDEQH 406
Cdd:COG1198 266 F-------GARVAV-LHSGLSDGE-RLDEWRRARRGEARIVIGTRsALF---APFPNLGLIIVDEEH 320
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
299-407 |
6.71e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 52.04 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 299 GSGKTIVAALAALKVVES-GAQVALMAPTEILAEQHLLNFSQwfaELKLPDGnsiEIAWLSGKSKGKTRAAALGKiasgn 377
Cdd:COG1111 27 GLGKTAVALLVIAERLHKkGGKVLFLAPTKPLVEQHAEFFKE---ALNIPED---EIVVFTGEVSPEKRKELWEK----- 95
|
90 100 110
....*....|....*....|....*....|....*
gi 1024592031 378 AQVVIGT-HALFQD----EVKFSRLALAIIDEQHR 407
Cdd:COG1111 96 ARIIVATpQVIENDliagRIDLDDVSLLIFDEAHR 130
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
299-445 |
2.20e-06 |
|
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: 48.03 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 299 GSGKTIVAALAALKVVESGAQVAL-MAPTEILAEQHLLNFSQWFAELKLPDGnsieiawlsgkskGKTRAAALGKIASGN 377
Cdd:cd17921 27 SSGKTLIAELAILRALATSGGKAVyIAPTRALVNQKEADLRERFGPLGKNVG-------------LLTGDPSVNKLLLAE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024592031 378 AQVVIGTHALFQ------DEVKFSRLALAIIDEQHRFGVHQRlslknkgqdsGLVPHQLI---MTATPIPRTLAMSA 445
Cdd:cd17921 94 ADILVATPEKLDlllrngGERLIQDVRLVVVDEAHLIGDGER----------GVVLELLLsrlLRINKNARFVGLSA 160
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
299-436 |
5.81e-06 |
|
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: 47.09 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 299 GSGKTIVAALAALKVVE------SGAQVALMAPTEILAEQHLLNFSQWFAELklpdgnsIEIAWLSGKSKGKTRAAALGK 372
Cdd:cd18036 27 GSGKTRVAVYICRHHLEkrrsagEKGRVVVLVNKVPLVEQQLEKFFKYFRKG-------YKVTGLSGDSSHKVSFGQIVK 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024592031 373 iasgNAQVVIGTHALFQ---------DEVKFSRLALAIIDE------QHRFGVHQRLSLKNKGQDSGLVPHQLIMTATP 436
Cdd:cd18036 100 ----ASDVIICTPQILInnllsgreeERVYLSDFSLLIFDEchhtqkEHPYNKIMRMYLDKKLSSQGPLPQILGLTASP 174
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
299-407 |
2.32e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 47.18 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 299 GSGKTIVAAL-AALKVVESGAQVALMAPTEILAEQHLLNFSQWfaeLKLPDGnsiEIAWLSGKSKGKTRAAALGKiasgn 377
Cdd:PRK13766 39 GLGKTAIALLvIAERLHKKGGKVLILAPTKPLVEQHAEFFRKF---LNIPEE---KIVVFTGEVSPEKRAELWEK----- 107
|
90 100 110
....*....|....*....|....*....|....*
gi 1024592031 378 AQVVIGT-----HALFQDEVKFSRLALAIIDEQHR 407
Cdd:PRK13766 108 AKVIVATpqvieNDLIAGRISLEDVSLLIFDEAHR 142
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
297-437 |
2.33e-04 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350769 [Multi-domain] Cd Length: 207 Bit Score: 42.28 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 297 DVGSGKTIVAALAAlkvvesgAQVALMAPTE---ILAEQHLLNfsQWFAELKLPDGNSIEIAwlsgksKGKTRAAALGKI 373
Cdd:cd18011 25 EVGLGKTIEAGLII-------KELLLRGDAKrvlILCPASLVE--QWQDELQDKFGLPFLIL------DRETAAQLRRLI 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024592031 374 ASGNAQ---VVIGTHALFQDE-----VKFSRLALAIIDEQHRFGV------HQRLSLknkGQD-SGLVPHQLIMTATPI 437
Cdd:cd18011 90 GNPFEEfpiVIVSLDLLKRSEerrglLLSEEWDLVVVDEAHKLRNsgggkeTKRYKL---GRLlAKRARHVLLLTATPH 165
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
293-409 |
8.69e-04 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 41.93 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 293 LVQGDVGSGKTIVAALAALKVVEsGAQVALMAPTEILAEqhllnfsQWFAELKlpdgnsieiawlsgksKGKTRAAALGK 372
Cdd:COG1061 104 LVVAPTGTGKTVLALALAAELLR-GKRVLVLVPRRELLE-------QWAEELR----------------RFLGDPLAGGG 159
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1024592031 373 IASGNAQVVIGTHALFQDEVKFSRLA----LAIIDEQHRFG 409
Cdd:COG1061 160 KKDSDAPITVATYQSLARRAHLDELGdrfgLVIIDEAHHAG 200
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
267-403 |
1.00e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 40.39 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 267 FELTGAQ----KKVCSdvdhdlGQAFPMLrlvqGDVGSGKTIVAALAALKVVESGAQVALMAPTEILAEQHLLNFSQwFA 342
Cdd:cd17924 16 FPPWGAQrtwaKRLLR------GKSFAII----APTGVGKTTFGLATSLYLASKGKRSYLIFPTKSLVKQAYERLSK-YA 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024592031 343 ElklPDGNSIEIAWLSGKSKGKTRAAALGKIASGNAQVVIGTHALFQ---DEVKFSRLALAIID 403
Cdd:cd17924 85 E---KAGVEVKILVYHSRLKKKEKEELLEKIEKGDFDILVTTNQFLSknfDLLSNKKFDFVFVD 145
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
299-406 |
3.73e-03 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 39.88 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 299 GSGKTIVAALAALKVVESGAQVALMAPTEILAEQHLLNFSQWFAELKLpdgnSIEIAwlsgkskgkTRAAALGKIASGNA 378
Cdd:COG1204 48 ASGKTLIAELAILKALLNGGKALYIVPLRALASEKYREFKRDFEELGI----KVGVS---------TGDYDSDDEWLGRY 114
|
90 100 110
....*....|....*....|....*....|...
gi 1024592031 379 QVVIGT----HALFQDEVKF-SRLALAIIDEQH 406
Cdd:COG1204 115 DILVATpeklDSLLRNGPSWlRDVDLVVVDEAH 147
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
286-408 |
5.31e-03 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 38.07 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 286 QAFPMLrLVQGDV------GSGKTIVAALAALKVVesgaQVALMAPTEILAEQHLLNFSQWFAELKLPdgnSIEIAWLSg 359
Cdd:cd17938 28 EAIPLI-LGGGDVlmaaetGSGKTGAFCLPVLQIV----VALILEPSRELAEQTYNCIENFKKYLDNP---KLRVALLI- 98
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1024592031 360 kskGKTRAAALGKIASGNAQVVIGTHALFQDEVK-----FSRLALAIIDEQHRF 408
Cdd:cd17938 99 ---GGVKAREQLKRLESGVDIVVGTPGRLEDLIKtgkldLSSVRFFVLDEADRL 149
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| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
297-438 |
5.53e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 39.44 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024592031 297 DVGSGKTIVAALAALKVVESGAQvalmAPTEILAEQHLLnfSQWFAELK--LPDgnsIEIAWLSGKSKGKTRAAALgkia 374
Cdd:COG0553 268 DMGLGKTIQALALLLELKERGLA----RPVLIVAPTSLV--GNWQRELAkfAPG---LRVLVLDGTRERAKGANPF---- 334
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024592031 375 sGNAQVVIGTHALF---QDEVKFSRLALAIIDEQHRfgvhqrlsLKNKG-QDSGLV-----PHQLIMTATPIP 438
Cdd:COG0553 335 -EDADLVITSYGLLrrdIELLAAVDWDLVILDEAQH--------IKNPAtKRAKAVralkaRHRLALTGTPVE 398
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