|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
6-488 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 772.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 6 NLTDQLKKYFGFDNFKGNQEPIIQNLLDGNDTFVLMPTGGGKSLCYQLPSLLMEGTAIVISPLIALMKNQVDAMRNFSEE 85
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 86 dgvAHFINSSLNKGAIDQVRSDILAGKTKLLYVAPESLTKEENVEFLRSVKISFYAVDEAHCISEWGHDFRPEYRRIRPI 165
Cdd:COG0514 84 ---AAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 166 INEIGKAPLIALTATATPKVQHDIQKNLGMVDAHVFKSSFNRPNLYYEVRPKT-QNVDKDIIKFIKNNPEKSGIIYCLSR 244
Cdd:COG0514 161 RERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPpDDKLAQLLDFLKEHPGGSGIVYCLSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 245 KKVEELAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGR 324
Cdd:COG0514 241 KKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 325 AGRDGGEGQCITFYTNKDLQKLEKFMQGKPVAE--QEIGKQLLLETAAYAESSVCRRKTLLHYFGEEYtEENCGNCDNCL 402
Cdd:COG0514 321 AGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEerKRVERAKLDAMLAYAETTGCRRQFLLRYFGEEL-AEPCGNCDNCL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 403 NPKKQVEAQELLCAVIETIIAVKENFKADYIIDVLQGRETSEVQAHLHEDLEVFGSGMGEEDKTWNAVIRQALIAGYLSK 482
Cdd:COG0514 400 GPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQLFGER 479
|
....*.
gi 492255599 483 DVENYG 488
Cdd:COG0514 480 KLERYG 485
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
11-602 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273594 [Multi-domain] Cd Length: 591 Bit Score: 655.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 11 LKKYFGFDNFKGNQEPIIQNLLDGNDTFVLMPTGGGKSLCYQLPSLLMEGTAIVISPLIALMKNQVDAMRnfseEDGV-A 89
Cdd:TIGR01389 5 LKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLR----AAGVaA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 90 HFINSSLNKGAIDQVRSDILAGKTKLLYVAPESLTKEENVEFLRSVKISFYAVDEAHCISEWGHDFRPEYRRIRPIINEI 169
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 170 GKAPLIALTATATPKVQHDIQKNLGMVDAHVFKSSFNRPNLYYEVRPKtQNVDKDIIKFIKNNPEKSGIIYCLSRKKVEE 249
Cdd:TIGR01389 161 PQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKK-NNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 250 LAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGRDG 329
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 330 GEGQCITFYTNKDLQKLEKFM-QGKPVAE-QEIGKQLLLETAAYAESSVCRRKTLLHYFGEEYTeENCGNCDNCLNPKKQ 407
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIeQSEADDDyKQIEREKLRAMIAYCETQTCRRAYILRYFGENEV-EPCGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 408 VEAQELLCAVIETIIAVKENFKADYIIDVLQGRETSEVQAHLHEDLEVFGSGMGEEDKTWNAVIRQALIAGYLSKDVENY 487
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 488 GLLKVTDAGKKFLKHPKSFKITEDNDFEevEEETPARGGGSCAVDPVLYSMLKDLRKKLSKKLEVPPYVIFQDPSLEAMA 567
Cdd:TIGR01389 479 IGLQLTEAARKVLKNEVEVLLRPFKVVA--KEKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMA 556
|
570 580 590
....*....|....*....|....*....|....*
gi 492255599 568 TIYPVTLEELQNIPGVGAGKAKRYGEEFCKLIKRH 602
Cdd:TIGR01389 557 EKRPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
11-607 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 543.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 11 LKKYFGFDNFKGNQEPIIQNLLDGNDTFVLMPTGGGKSLCYQLPSLLMEGTAIVISPLIALMKNQVDAMRnfseEDGV-A 89
Cdd:PRK11057 17 LQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLL----ANGVaA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 90 HFINSSLNKGAIDQVRSDILAGKTKLLYVAPESLTKEENVEFLRSVKISFYAVDEAHCISEWGHDFRPEYRRIRPIINEI 169
Cdd:PRK11057 93 ACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 170 GKAPLIALTATATPKVQHDIQKNLGMVDAHVFKSSFNRPNLYYEVRPKTQNVDKdIIKFIKNNPEKSGIIYCLSRKKVEE 249
Cdd:PRK11057 173 PTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQ-LMRYVQEQRGKSGIIYCNSRAKVED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 250 LAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGRDG 329
Cdd:PRK11057 252 TAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 330 GEGQCITFYTNKDLQKLEKFMQGKPV-AEQEIGKQLLLETAAYAESSVCRRKTLLHYFGeEYTEENCGNCDNCLNPKKQ- 407
Cdd:PRK11057 332 LPAEAMLFYDPADMAWLRRCLEEKPAgQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFG-EGRQEPCGNCDICLDPPKQy 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 408 ---VEAQELLcaviETIIAVKENFKADYIIDVLQGRETSEVQAHLHEDLEVFGSGMGEEDKTWNAVIRQALIAGYLSKDV 484
Cdd:PRK11057 411 dglEDAQKAL----SCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNI 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 485 ENYGLLKVTDAGKKFLKHPKSFKITedndfeeVEEETPARGGGSCAV-----DPVLYSMLKDLRKKLSKKLEVPPYVIFQ 559
Cdd:PRK11057 487 AQHSALQLTEAARPVLRGEVSLQLA-------VPRIVALKPRAMQKSfggnyDRKLFAKLRKLRKSIADEENIPPYVVFN 559
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 492255599 560 DPSLEAMATIYPVTLEELQNIPGVGAGKAKRYGEEFCKLIKRHCEENE 607
Cdd:PRK11057 560 DATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAHVDGDD 607
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
11-459 |
3.07e-168 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129701 [Multi-domain] Cd Length: 470 Bit Score: 491.59 E-value: 3.07e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 11 LKKYFGFDNFKGNQEPIIQNLLDGNDTFVLMPTGGGKSLCYQLPSLLMEGTAIVISPLIALMKNQVDAMRNFSEEdgvAH 90
Cdd:TIGR00614 3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIP---AT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 91 FINSSLNKGAIDQVRSDILAGKTKLLYVAPESLTKeeNVEFLR----SVKISFYAVDEAHCISEWGHDFRPEYRRIRPII 166
Cdd:TIGR00614 80 FLNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISA--SNRLLQtleeRKGITLIAVDEAHCISQWGHDFRPDYKALGSLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 167 NEIGKAPLIALTATATPKVQHDIQKNLGMVDAHVFKSSFNRPNLYYEVRPKTQNVDKDIIKFI-KNNPEKSGIIYCLSRK 245
Cdd:TIGR00614 158 QKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPKILEDLLRFIrKEFEGKSGIIYCPSRK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 246 KVEELAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRA 325
Cdd:TIGR00614 238 KVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 326 GRDGGEGQCITFYTNKDLQKLEKFMQGKPVAEQEIGKQLLLE-TAAYAESSVCRRKTLLHYFGE---------EYTEENC 395
Cdd:TIGR00614 318 GRDGLPSECHLFYAPADMNRLRRLLMEEPDGNFRTYKLKLYEmMEYCLNSSTCRRLILLSYFGEkgfnksfciMGTEKCC 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492255599 396 GNCDNCLN-------PKKQ---VEAQELLcaviETIIAVKENFKADYIIDVLQGRETSEVQAHLHEDLEVFGSG 459
Cdd:TIGR00614 398 DNCCKRLDyktkdvtDKVYdfgPQAQKAL----SAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRG 467
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
12-599 |
4.55e-129 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 411.98 E-value: 4.55e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 12 KKYFGFDNFKGNQEPIIQNLLDGNDTFVLMPTGGGKSLCYQLPSLLMEGTAIVISPLIALMKNQVdamRNFSEEDGVAHF 91
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQI---MNLLQANIPAAS 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 92 INSSL----NKGAIDQVRSDilAGKTKLLYVAPESLTKEE----NVEFLRSVKI-SFYAVDEAHCISEWGHDFRPEYRRI 162
Cdd:PLN03137 530 LSAGMewaeQLEILQELSSE--YSKYKLLYVTPEKVAKSDsllrHLENLNSRGLlARFVIDEAHCVSQWGHDFRPDYQGL 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 163 RPIINEIGKAPLIALTATATPKVQHDIQKNLGMVDAHVFKSSFNRPNLYYEVRPKTQNVDKDIIKFIKNNP-EKSGIIYC 241
Cdd:PLN03137 608 GILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKCLEDIDKFIKENHfDECGIIYC 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 242 LSRKKVEELAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQE 321
Cdd:PLN03137 688 LSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQE 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 322 TGRAGRDGGEGQCITFYTNKDLQKLeKFMQGKPVAEQ-----------------EIGKQLLLETAAYAESSV-CRRKTLL 383
Cdd:PLN03137 768 CGRAGRDGQRSSCVLYYSYSDYIRV-KHMISQGGVEQspmamgynrmassgrilETNTENLLRMVSYCENEVdCRRFLQL 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 384 HYFGEEYTEENCGN-CDNCLNPKKQVEAQELLCA--VIETIIAVKENFKADYIIDVLQGRETSEVQAHLHEDLEVFGSGM 460
Cdd:PLN03137 847 VHFGEKFDSTNCKKtCDNCSSSKSLIDKDVTEIArqLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGK 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 461 GEEDKTWNAVIRQALIAGYLSKDVEN---YG----LLKVTDA--------GKKF-LKHPKSFKITEDNDFeeveEETPAR 524
Cdd:PLN03137 927 HLSKGEASRILHYLVTEDILAEDVKKsdlYGsvssLLKVNESkayklfsgGQTIiMRFPSSVKASKPSKF----EATPAK 1002
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 525 GG-----------GSCAVDPV-------LYSMLKDLRKKLSKKLE--VPPYVIFQDPSLEAMATIYPVTLEELQNIPGVG 584
Cdd:PLN03137 1003 GPltsgkqstlpmATPAQPPVdlnlsaiLYTALRKLRTALVKEAGdgVMAYHIFGNATLQQISKRIPRTKEELLEINGLG 1082
|
650
....*....|....*
gi 492255599 585 AGKAKRYGEEFCKLI 599
Cdd:PLN03137 1083 KAKVSKYGDRLLETI 1097
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
11-206 |
6.86e-93 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 287.51 E-value: 6.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 11 LKKYFGFDNFKGNQEPIIQNLLDGNDTFVLMPTGGGKSLCYQLPSLLMEGTAIVISPLIALMKNQVDAMRNFseedGV-A 89
Cdd:cd17920 4 LKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQL----GIrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 90 HFINSSLNKGAIDQVRSDILAGKTKLLYVAPESLTKEENVEFLRSVK----ISFYAVDEAHCISEWGHDFRPEYRRIRPI 165
Cdd:cd17920 80 AALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492255599 166 INEIGKAPLIALTATATPKVQHDIQKNLGMVDAHVFKSSFN 206
Cdd:cd17920 160 RRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
11-206 |
3.74e-66 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 217.12 E-value: 3.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 11 LKKYFGFDNFKGNQEPIIQNLLDGNDTFVLMPTGGGKSLCYQLPSLLME----GTAIVISPLIALMKNQVDAMRNFSEed 86
Cdd:cd18018 4 LRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPRAIK-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 87 gvAHFINSSLNKG----AIDQVRsdilAGKTKLLYVAPESLTKEENVEFLRSVK-ISFYAVDEAHCISEWGHDFRPEYRR 161
Cdd:cd18018 82 --AAALNSSLTREerrrILEKLR----AGEVKILYVSPERLVNESFRELLRQTPpISLLVVDEAHCISEWSHNFRPDYLR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492255599 162 IRPIINEIGKA-PLIALTATATPKVQHDIQKNLGMVDAHVFKSSFN 206
Cdd:cd18018 156 LCRVLRELLGApPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
207-338 |
8.73e-66 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. 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: 350181 [Multi-domain] Cd Length: 134 Bit Score: 213.61 E-value: 8.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 207 RPNLYYEVRPKTQNVDKDI-IKFIK-NNPEKSGIIYCLSRKKVEELAEILQANGINARAYHAGMDSATRTQNQDDFLMEK 284
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDlLKRIKvEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 492255599 285 IDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGRDGGEGQCITFY 338
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
9-206 |
7.80e-57 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 191.91 E-value: 7.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 9 DQLKKYFGFDNFKGNQEPIIQNLL-DGNDTFVLMPTGGGKSLCYQLPSLLMEGTAIVISPLIALMKNQVDAMrnfseedg 87
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQL-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 88 VAHFINSSLNKGAIDQ-VRSDILAGKTKLLYVAPESLTKeeNVEFLRSVK--ISFYAVDEAHCISEWGHDFRPEYRRIRP 164
Cdd:cd18017 74 VMSNIPACFLGSAQSQnVLDDIKMGKIRVIYVTPEFVSK--GLELLQQLRngITLIAIDEAHCVSQWGHDFRSSYRHLGS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492255599 165 IINEIGKAPLIALTATATPKVQHDIQKNLGMVDAHVFKSSFN 206
Cdd:cd18017 152 IRNRLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
7-206 |
9.54e-56 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350773 [Multi-domain] Cd Length: 209 Bit Score: 189.50 E-value: 9.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 7 LTDQLKKYFGFDNFKGNQEPIIQNLLDGNDTFVLMPTGGGKSLCYQLPSLLMEGTAIVISPLIALMKNQVDAMRNFseed 86
Cdd:cd18015 6 VKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 87 GV-AHFINSSLNKGAIDQVRSDILAGKT--KLLYVAPE----------SLTKEENVEFLRSVkisfyAVDEAHCISEWGH 153
Cdd:cd18015 82 GIsATMLNASSSKEHVKWVHAALTDKNSelKLLYVTPEkiakskrfmsKLEKAYNAGRLARI-----AIDEVHCCSQWGH 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492255599 154 DFRPEYRRIRPIINEIGKAPLIALTATATPKVQHDIQKNLGMVDAHVFKSSFN 206
Cdd:cd18015 157 DFRPDYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
7-206 |
4.91e-53 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 182.33 E-value: 4.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 7 LTDQLKKYFGFDNFKGNQEPIIQNLLDGNDTFVLMPTGGGKSLCYQLPSLLMEGTAIVISPLIALMKNQVDAMRNFseeD 86
Cdd:cd18016 5 MMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL---D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 87 GVAHFINSSLNKGAIDQVRSDILAGK--TKLLYVAPESLTKE----ENVEFLRSVK-ISFYAVDEAHCISEWGHDFRPEY 159
Cdd:cd18016 82 IPATYLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKISASnrliSTLENLYERKlLARFVIDEAHCVSQWGHDFRPDY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492255599 160 RRIRPIINEIGKAPLIALTATATPKVQHDIQKNLGMVDAHVFKSSFN 206
Cdd:cd18016 162 KRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
11-193 |
6.06e-49 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350772 [Multi-domain] Cd Length: 205 Bit Score: 170.73 E-value: 6.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 11 LKKYFGFDNFKGN-QEPIIQNLLDGN-DTFVLMPTGGGKSLCYQLPSLLMEGTAIVISPLIALMKNQVDAMRNFSEEdgv 88
Cdd:cd18014 4 LKKVFGHSDFKSPlQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 89 AHFINSSLNKGAIDQVRSDILAG--KTKLLYVAPESLTKEENVEFLRSV----KISFYAVDEAHCISEWGHDFRPEYRRI 162
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEkpQTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|.
gi 492255599 163 RPIINEIGKAPLIALTATATPKVQHDIQKNL 193
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQL 191
|
|
| DpdF |
NF041063 |
protein DpdF; |
11-344 |
1.53e-47 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 180.49 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 11 LKKYFGFDNFK--GNQEPIIQNLL--DGNDTFVLMPTGGGKSLCYQLPSLL---MEGTAIVISPLIALMKNQVDAMRNFS 83
Cdd:NF041063 131 LAEALGFTHYRspGQREAVRAALLapPGSTLIVNLPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQERRARELL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 84 EEDGVAHFIN----SSLNKGAIDQVRSDILAGKTKLLYVAPESLTKEenvefLRSV--------KISFYAVDEAHCISEW 151
Cdd:NF041063 211 RRAGPDLGGPlawhGGLSAEERAAIRQRIRDGTQRILFTSPESLTGS-----LRPAlfdaaeagLLRYLVVDEAHLVDQW 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 152 GHDFRPEYRRIRPIINE-IGKAP------LIALTATATPKVQHDIQK------NLGMVDAhvfksSFNRPNLYYEVRPKT 218
Cdd:NF041063 286 GDGFRPEFQLLAGLRRSlLRLAPsgrpfrTLLLSATLTESTLDTLETlfgppgPFIVVSA-----VQLRPEPAYWVAKCD 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 219 QNVDKD--IIKFIKNNPeKSGIIYCLSRKKVEELAEILQANGIN-ARAYHAGMDSATRTQnqddfLME-----KIDVIVA 290
Cdd:NF041063 361 SEEERRerVLEALRHLP-RPLILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERER-----LIEqwrenELDIVVA 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 492255599 291 TIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGRDGGEGQCITFYTNKDLQ 344
Cdd:NF041063 435 TSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLD 488
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
404-511 |
1.09e-26 |
|
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure. The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 462780 [Multi-domain] Cd Length: 108 Bit Score: 104.54 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 404 PKKQVEAQELLCAVIETIIAVKENFKADYIIDVLQGRETSEVQAHLHEDLEVFGSGMGEEDKTWNAVIRQALIAGYLSKD 483
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*...
gi 492255599 484 VENYGLLKVTDAGKKFLKHPKSFKITED 511
Cdd:pfam09382 81 IEFYSVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
211-338 |
3.44e-26 |
|
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: 104.13 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 211 YYEVRPKTQNVDKDIIKFIKNNPEKSGIIYCLSRKKVEELAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVA 290
Cdd:cd18787 4 LYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 492255599 291 TIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGRDGGEGQCITFY 338
Cdd:cd18787 84 TDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
211-360 |
3.32e-25 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 109.08 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 211 YYEVRPKtqnvDKD--IIKFIKNNPEKSGIIYCLSRKKVEELAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVI 288
Cdd:COG0513 220 YYLVDKR----DKLelLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVL 295
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492255599 289 VAT-IAfGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGRDGGEGQCITFYTNKD---LQKLEKFMqGKPVAEQEI 360
Cdd:COG0513 296 VATdVA-ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDErrlLRAIEKLI-GQKIEEEEL 369
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
248-329 |
6.84e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 98.82 E-value: 6.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 248 EELAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGR 327
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 492255599 328 DG 329
Cdd:smart00490 81 AG 82
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
24-186 |
2.28e-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: 100.01 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 24 QEPIIQNLLDGNDTFVLMPTGGGKSLCYQLPSL------LMEGTAIVISPLIALMKNQVDAMRNFSEEDGVAhfINSSLN 97
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK--VASLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 98 KGAIDQVRSDIlaGKTKLLYVAPESLTKE-ENVEFLRSVKisFYAVDEAHCISEWGhdFRPEYRRIRPIINEigKAPLIA 176
Cdd:pfam00270 82 GDSRKEQLEKL--KGPDILVGTPGRLLDLlQERKLLKNLK--LLVLDEAHRLLDMG--FGPDLEEILRRLPK--KRQILL 153
|
170
....*....|
gi 492255599 177 LTATATPKVQ 186
Cdd:pfam00270 154 LSATLPRNLE 163
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
223-329 |
1.44e-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: 95.74 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 223 KDIIKFIKNNPEKSGIIYCLSRKKVEElAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPD 302
Cdd:pfam00271 4 EALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
|
90 100
....*....|....*....|....*..
gi 492255599 303 VRYVIHYDIPKSLEGYYQETGRAGRDG 329
Cdd:pfam00271 83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
13-215 |
9.98e-22 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 93.71 E-value: 9.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 13 KYFGFDNFKGNQEPIIQNLLDGN-DTFVLMPTGGGKSLCYQLPSLL-----MEGTAIVISPLIALMKNQVDAMRNFSEED 86
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 87 GVahfINSSLNKGA-IDQVRSDILAGKTKLLYVAPESLTKEENVEFLRSVKISFYAVDEAHCISEWGhdFRPEYRRIRPI 165
Cdd:smart00487 82 GL---KVVGLYGGDsKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492255599 166 INEigKAPLIALTATATPKVQHDIQKNLGMVdahVFKSSFNRPNLYYEVR 215
Cdd:smart00487 157 LPK--NVQLLLLSATPPEEIENLLELFLNDP---VFIDVGFTPLEPIEQF 201
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
408-500 |
7.94e-21 |
|
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure; The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 214936 [Multi-domain] Cd Length: 92 Bit Score: 87.53 E-value: 7.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 408 VEAQELLCAVIETiiavKENFKADYIIDVLQGRETSEVQAHLHEDLEVFGSGMGEEDKTWNAVIRQALIAGYLSKDVENY 487
Cdd:smart00956 4 EEAQKLLSCVYRT----GQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRY 79
|
90
....*....|...
gi 492255599 488 GLLKVTDAGKKFL 500
Cdd:smart00956 80 PYLKLTEKARPVL 92
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
341-402 |
2.41e-20 |
|
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
Pssm-ID: 465031 [Multi-domain] Cd Length: 66 Bit Score: 85.03 E-value: 2.41e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492255599 341 KDLQKLEKFMQGKPVAE--QEIGKQLLLETAAYAESSV-CRRKTLLHYFGEEYTEENCGNCDNCL 402
Cdd:pfam16124 2 QDVVRLRFLIEQSEADEerKEVELQKLQAMVAYCENTTdCRRKQLLRYFGEEFDSEPCGNCDNCL 66
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
532-599 |
3.64e-17 |
|
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.
Pssm-ID: 425755 [Multi-domain] Cd Length: 68 Bit Score: 76.04 E-value: 3.64e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492255599 532 DPVLYSMLKDLRKKLSKKLEVPPYVIFQDPSLEAMATIYPVTLEELQNIPGVGAGKAKRYGEEFCKLI 599
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
28-332 |
1.38e-16 |
|
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: 84.12 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 28 IQNLLDGNDTFVLMPTGGGKSLCYQLPSL--LMEG---TAIVISPLIALMKNQVDAMRNFSEEDGVahfinsSLNKGAID 102
Cdd:COG1205 65 IEAARAGKNVVIATPTASGKSLAYLLPVLeaLLEDpgaTALYLYPTKALARDQLRRLRELAEALGL------GVRVATYD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 103 ---------QVRSD--------------ILAGKTKLlyvapesltkeenVEFLRSVKisFYAVDEAHcisewghdfrpEY 159
Cdd:COG1205 139 gdtppeerrWIREHpdivltnpdmlhygLLPHHTRW-------------ARFFRNLR--YVVIDEAH-----------TY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 160 ------------RRIRPIINEIGKAPL-IALTAT-ATPKvQHdIQKNLGmVDAHVFKSS----------FNRPNLYYEVR 215
Cdd:COG1205 193 rgvfgshvanvlRRLRRICRHYGSDPQfILASATiGNPA-EH-AERLTG-RPVTVVDEDgsprgertfvLWNPPLVDDGI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 216 PKTQNVD-KDIIK-FIKNNpeKSGIIYCLSRKKVEELAEILQAN------GINARAYHAGMDSATRTQNQDDFLMEKIDV 287
Cdd:COG1205 270 RRSALAEaARLLAdLVREG--LRTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGELLG 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 492255599 288 IVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGRDGGEG 332
Cdd:COG1205 348 VVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS 392
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
24-338 |
2.65e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 79.68 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 24 QEPIIQNLLD----GNDTFVL-MPTGGGKSL----CYQlpSLLMEGTAIVISPLIALMKNQVDAMRNFseedgvahfINS 94
Cdd:COG1061 85 QQEALEALLAalerGGGRGLVvAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRF---------LGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 95 SLNKGAIDQVRSDILagktkllyVA-PESLTKEENVEFLRSvKISFYAVDEAHcisewgHDFRPEYRRIrpiINEIGKAP 173
Cdd:COG1061 154 PLAGGGKKDSDAPIT--------VAtYQSLARRAHLDELGD-RFGLVIIDEAH------HAGAPSYRRI---LEAFPAAY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 174 LIALTATATPKVQHDI-------------------QKNLGMVDAHVFKSSFNRPNLYYE---------VRPKTQNVDKDI 225
Cdd:COG1061 216 RLGLTATPFRSDGREIllflfdgivyeyslkeaieDGYLAPPEYYGIRVDLTDERAEYDalserlreaLAADAERKDKIL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 226 IKFIKNNPE-KSGIIYCLSRKKVEELAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVR 304
Cdd:COG1061 296 RELLREHPDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLD 375
|
330 340 350
....*....|....*....|....*....|....
gi 492255599 305 YVIHYDIPKSLEGYYQETGRAGRDGGEGQCITFY 338
Cdd:COG1061 376 VAILLRPTGSPREFIQRLGRGLRPAPGKEDALVY 409
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
24-351 |
4.76e-15 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 78.74 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 24 QEPIIQNLLDGNDTFVLMPTGGGKSLCYQLPSL------LMEGTAIVISPLIALMKNQVDAMRNFSEEdgvAHFINS-SL 96
Cdd:PRK11634 33 QAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTRELAVQVAEAMTDFSKH---MRGVNVvAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 97 NKGAIDQVRSDILAGKTKLLYVAPESLTKEENVEFLRSVKISFYAVDEAHCISEWGHdfrpeYRRIRPIINEIGKAPLIA 176
Cdd:PRK11634 110 YGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGF-----IEDVETIMAQIPEGHQTA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 177 LTATATPKVQHDIQKNLgMVDAH---VFKSSFNRPNL---YYEVRPKTQNvdKDIIKFIKNNPEKSGIIYCLSRKKVEEL 250
Cdd:PRK11634 185 LFSATMPEAIRRITRRF-MKEPQevrIQSSVTTRPDIsqsYWTVWGMRKN--EALVRFLEAEDFDAAIIFVRTKNATLEV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 251 AEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGRDGG 330
Cdd:PRK11634 262 AEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGR 341
|
330 340
....*....|....*....|....
gi 492255599 331 EGQCITFYTNKD---LQKLEKFMQ 351
Cdd:PRK11634 342 AGRALLFVENRErrlLRNIERTMK 365
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
136-342 |
5.86e-15 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 78.29 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 136 KISFYAVDEAHCISEWGhdFRPEyrrIRPIINEIGKAPLIALTATATP---KVQHDIQKNLGMVDAhvfkSSFNRPN--- 209
Cdd:PLN00206 270 NVSVLVLDEVDCMLERG--FRDQ---VMQIFQALSQPQVLLFSATVSPeveKFASSLAKDIILISI----GNPNRPNkav 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 210 ----LYYEVRPKTQNVdKDIIKFiKNNPEKSGIIYCLSRKKVEELAE-ILQANGINARAYHAGMDSATRTQNQDDFLMEK 284
Cdd:PLN00206 341 kqlaIWVETKQKKQKL-FDILKS-KQHFKPPAVVFVSSRLGADLLANaITVVTGLKALSIHGEKSMKERREVMKSFLVGE 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492255599 285 IDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGRDGGEGQCITFYTNKD 342
Cdd:PLN00206 419 VPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEED 476
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
32-380 |
3.86e-14 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 75.58 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 32 LDGNDTFVLMPTGGGKSLCYQLPS--------LLMEGTA-IVIspLIALMKNQVDAMRNFSEEDGVAHFINSSLNKGAID 102
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGDGpIVL--VLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 103 QvRSDILAGK--TKLLYVAPESLTK--EENVEFLRSVkiSFYAVDEAHCISEWGhdFRPEyrrIRPIINEIgKAPLIALT 178
Cdd:PTZ00110 243 K-RGQIYALRrgVEILIACPGRLIDflESNVTNLRRV--TYLVLDEADRMLDMG--FEPQ---IRKIVSQI-RPDRQTLM 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 179 ATAT-PK-VQ---HD------IQKNLGMVDahvFKSSFN-RPNLYY-EVRPKTQNVdKDIIKFIKNNPEKSgIIYCLSRK 245
Cdd:PTZ00110 314 WSATwPKeVQslaRDlckeepVHVNVGSLD---LTACHNiKQEVFVvEEHEKRGKL-KMLLQRIMRDGDKI-LIFVETKK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 246 KVEELAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRA 325
Cdd:PTZ00110 389 GADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRT 468
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 492255599 326 GRDGGEGQCITFYT---NKDLQKLEKFMQGkpvAEQEIGKQllLETAAYAESSVCRRK 380
Cdd:PTZ00110 469 GRAGAKGASYTFLTpdkYRLARDLVKVLRE---AKQPVPPE--LEKLSNERSNGTERR 521
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
34-180 |
1.55e-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: 68.58 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 34 GNDTFVLMPTGGGKSLCYQLP----SLLMEGTAIVISPLIALMKNQVDAMRNFSEEDGVAHFINSSLNKGAidqvRSDIL 109
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAalllLLKKGKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVGGSSAEE----REKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492255599 110 AGKTKLLYVAPESLTKEENVEFLRSVK-ISFYAVDEAHCISEWGHDFRPEYRRIRPIINeiGKAPLIALTAT 180
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALILDLAVRKAGL--KNAQVILLSAT 146
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
238-348 |
2.18e-13 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 72.55 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 238 IIYCLSRKKVEELAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEG 317
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100 110
....*....|....*....|....*....|.
gi 492255599 318 YYQETGRAGRDGGEGQCITFYTNKDLQKLEK 348
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIEQLKE 381
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
535-609 |
5.72e-13 |
|
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.
Pssm-ID: 128635 [Multi-domain] Cd Length: 81 Bit Score: 64.63 E-value: 5.72e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492255599 535 LYSMLKDLRKKLSKKLEVPPYVIFQDPSLEAMATIYPVTLEELQNIPGVGAGKAKRYGEEFCKLIKRHCEENEIE 609
Cdd:smart00341 7 LLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDSPSEA 81
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
238-338 |
1.68e-12 |
|
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: 63.11 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 238 IIYCLSRKKVEELAEILQanginarayhagmdsatrtqnqddflmekidVIVATIAFGMGIDKPDVRYVIHYDIPKSLEG 317
Cdd:cd18785 7 IVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSAAS 55
|
90 100
....*....|....*....|..
gi 492255599 318 YYQETGRAGRDGG-EGQCITFY 338
Cdd:cd18785 56 YIQRVGRAGRGGKdEGEVILFV 77
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
228-329 |
2.06e-11 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 66.50 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 228 FIKNNPEKSGIIYCLSRKKVEELAEILQANGINArAYHAG-MDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYV 306
Cdd:PRK11192 239 LLKQPEVTRSIVFVRTRERVHELAGWLRKAGINC-CYLEGeMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHV 317
|
90 100
....*....|....*....|....*.
gi 492255599 307 IHYDIPKSLEGYYQE---TGRAGRDG 329
Cdd:PRK11192 318 INFDMPRSADTYLHRigrTGRAGRKG 343
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
238-331 |
2.93e-11 |
|
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: 61.89 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 238 IIYCLSRKKVE----ELAEILQANGINA---RAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIHYD 310
Cdd:cd18797 39 IVFCRSRKLAElllrYLKARLVEEGPLAskvASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|.
gi 492255599 311 IPKSLEGYYQETGRAGRDGGE 331
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKD 139
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-146 |
3.24e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; 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. Hrq1 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: 350681 [Multi-domain] Cd Length: 182 Bit Score: 56.82 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 28 IQNLLDGNDTFVLMPTGGGKSLCYQLPSL--LME---GTAIVISPLIALMKNQVDAMRNFSEEDGvahfinSSLNKGAID 102
Cdd:cd17923 9 IEAARAGRSVVVTTGTASGKSLCYQLPILeaLLRdpgSRALYLYPTKALAQDQLRSLRELLEQLG------LGIRVATYD 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 492255599 103 -----QVRSDILAGKTKLLYVAPESL------TKEENVEFLRSVKisFYAVDEAH 146
Cdd:cd17923 83 gdtprEERRAIIRNPPRILLTNPDMLhyallpHHDRWARFLRNLR--YVVLDEAH 135
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
229-368 |
4.46e-09 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 59.54 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 229 IKNNPEKSGIIYCLSRKKVEELAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIH 308
Cdd:PRK01297 330 VTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVIN 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 309 YDIPKSLEGYYQETGRAGRDGGEGQCITFYTNKDLQKLekfmqgkPVAEQEIGKQLLLET 368
Cdd:PRK01297 410 FTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQL-------PEIEELLGRKISCEM 462
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
199-332 |
1.70e-08 |
|
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: 54.10 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 199 HVFKSSFNRPNLYYEVRPKTQNVDKDIIKFIKNNPEKSGIIYCLSRKKVEELAEILqaNGInarAY-HAGMDSATRTQNQ 277
Cdd:cd18795 8 YVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDL--AGI---AFhHAGLTREDRELVE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492255599 278 DDFLMEKIDVIVATIAFGMGIDKPDVRYVI----HYD------IPkSLEgYYQETGRAGRDG----GEG 332
Cdd:cd18795 83 ELFREGLIKVLVATSTLAAGVNLPARTVIIkgtqRYDgkgyreLS-PLE-YLQMIGRAGRPGfdtrGEA 149
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
31-301 |
2.02e-08 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 57.59 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 31 LLDGNDTFVLMPTGGGKSLCYQL---PSLLM-EGTAIVISPLIALmKNQvdAMRNFSEEDGvaHFINSSLNKGA----ID 102
Cdd:COG1202 222 LLEGKDQLVVSATATGKTLIGELagiKNALEgKGKMLFLVPLVAL-ANQ--KYEDFKDRYG--DGLDVSIRVGAsrirDD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 103 QVR----SDILAGKtkllYvapesltkeENVEF-LRSVK----ISFYAVDEAHCI--SEWGHDFRPEYRRIRPIINEigk 171
Cdd:COG1202 297 GTRfdpnADIIVGT----Y---------EGIDHaLRTGRdlgdIGTVVIDEVHMLedPERGHRLDGLIARLKYYCPG--- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 172 APLIALTAT-ATPKVqhdIQKNLGMvdahvfkssfnrpNLY-YEVRPK--------TQNVDK-DII-KFIK---NNPEKS 236
Cdd:COG1202 361 AQWIYLSATvGNPEE---LAKKLGA-------------KLVeYEERPVplerhltfADGREKiRIInKLVKrefDTKSSK 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 237 G-----IIYCLSRKKVEELAEILqanGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKP 301
Cdd:COG1202 425 GyrgqtIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFP 491
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
539-672 |
2.25e-08 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 56.80 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 539 LKDL---RKKLSKKLEVPPYVIFQDPSLEAMATIYPVTLEELQNIPGVGAGKAKRYGEEFCKLIKRHCEENEIERPEDLR 615
Cdd:COG0349 213 LRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAEALALPEEELPEPPR 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 616 VRTVANKSKmkvAIIQAIdrKVALDDIALSKGIEfSELL---DEVEAIVYSGTKLNIDYF 672
Cdd:COG0349 293 RLPLSPGYK---ALLKLL--KALLKEVAEELGVA-PELLasrKDLEALARWGELADPPLL 346
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
250-336 |
2.84e-08 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 56.74 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 250 LAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGRDG 329
Cdd:PRK10590 261 LAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAA 340
|
....*..
gi 492255599 330 GEGQCIT 336
Cdd:PRK10590 341 ATGEALS 347
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
213-341 |
1.81e-07 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 51.48 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 213 EVRPKTQNVDkDIIKFIKNNPEKSG--IIYCLSRKKVEELAEILQANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVA 290
Cdd:cd18790 5 EVRPTEGQVD-DLLGEIRKRVARGErvLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 492255599 291 TIAFGMGIDKPDVRYVIHYDIPKslEGYY-------QETGRAGRDgGEGQCItFYTNK 341
Cdd:cd18790 84 INLLREGLDLPEVSLVAILDADK--EGFLrsetsliQTIGRAARN-VNGKVI-LYADK 137
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
216-329 |
2.67e-07 |
|
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: 50.28 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 216 PKTQNVDKDIIKFIKNNPEKSGIIYCLSRKKVEELAEILQAN-------------GINARAYHAGMDSATRTQNQ--DDF 280
Cdd:cd18802 7 PKLQKLIEILREYFPKTPDFRGIIFVERRATAVVLSRLLKEHpstlafircgfliGRGNSSQRKRSLMTQRKQKEtlDKF 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 492255599 281 LMEKIDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGRDG 329
Cdd:cd18802 87 RDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
31-371 |
5.19e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 52.98 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 31 LLDGNDTFVLMPTGGGKSLCYQLP---SLLMEGTAIVISPLIALMkNQV-DAMRNFSEEDGVAHFINSslnkGAIDqvRS 106
Cdd:COG1204 35 LLEGKNLVVSAPTASGKTLIAELAilkALLNGGKALYIVPLRALA-SEKyREFKRDFEELGIKVGVST----GDYD--SD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 107 DILAGKTKLLYVAPE---SLTKeENVEFLRsvKISFYAVDEAHCIsewGHDFR-PEY-------RRIRPiineigKAPLI 175
Cdd:COG1204 108 DEWLGRYDILVATPEkldSLLR-NGPSWLR--DVDLVVVDEAHLI---DDESRgPTLevllarlRRLNP------EAQIV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 176 ALTATatpkVQ--HDIQKNLgmvDAHVFKSSFnRPN-----LYY----EVRPKTQNVDKDIIKFIKNNPEKSG--IIYCL 242
Cdd:COG1204 176 ALSAT----IGnaEEIAEWL---DAELVKSDW-RPVplnegVLYdgvlRFDDGSRRSKDPTLALALDLLEEGGqvLVFVS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 243 SRKKVEELAEILqANGINAR-------------------------------------AYH-AGMDSATRTqnqddfLME- 283
Cdd:COG1204 248 SRRDAESLAKKL-ADELKRRltpeereeleelaeellevseethtnekladclekgvAFHhAGLPSELRR------LVEd 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 284 -----KIDVIVAT--IAfgMGIDKPdVRYVI--------HYDIPkSLEgYYQETGRAGRDG----GEGQCITFYTNKDLQ 344
Cdd:COG1204 321 afregLIKVLVATptLA--AGVNLP-ARRVIirdtkrggMVPIP-VLE-FKQMAGRAGRPGydpyGEAILVAKSSDEADE 395
|
410 420
....*....|....*....|....*..
gi 492255599 345 KLEKFMQGKPvaeQEIGKQLLLETAAY 371
Cdd:COG1204 396 LFERYILGEP---EPIRSKLANESALR 419
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
247-356 |
2.60e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 50.72 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 247 VEELAEILQANGinaraYHAGMDSATRTQNQDDFLMEK-----IDVIVAT--IAFGMGIDkpDVRYVIHYDIPKSLEGYY 319
Cdd:PRK04537 270 VERVARTLERHG-----YRVGVLSGDVPQKKRESLLNRfqkgqLEILVATdvAARGLHID--GVKYVYNYDLPFDAEDYV 342
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 492255599 320 QETGRAGRDGGEGQCITFYTNK---DLQKLEKFMQGK-PVA 356
Cdd:PRK04537 343 HRIGRTARLGEEGDAISFACERyamSLPDIEAYIEQKiPVE 383
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
212-327 |
2.91e-06 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain] Cd Length: 174 Bit Score: 48.07 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 212 YEVRPKTQNVDKDIIKFIKnnpeKSGIIYCLSRK---KVEELAEILQANGINARAYHAGmdsatRTQNQDDFLMEKIDVI 288
Cdd:cd18798 6 YIEDSDSLEKLLELVKKLG----DGGLIFVSIDYgkeYAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEIDVL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 492255599 289 VATIAF-GM---GIDKPD-VRYVIHYDIPksLEGYYQETGRAGR 327
Cdd:cd18798 77 IGVASYyGVlvrGIDLPErIKYAIFYGVP--VTTYIQASGRTSR 118
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
233-337 |
7.50e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 48.81 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 233 PEKSgIIYCLSRKKVEELAEILQANGinaraYHAGMDSATRTQNQ-----DDFLMEKIDVIVATIAFGMGIDKPDVRYVI 307
Cdd:PRK04837 255 PDRA-IIFANTKHRCEEIWGHLAADG-----HRVGLLTGDVAQKKrlrilEEFTRGDLDILVATDVAARGLHIPAVTHVF 328
|
90 100 110
....*....|....*....|....*....|
gi 492255599 308 HYDIPKSLEGYYQETGRAGRDGGEGQCITF 337
Cdd:PRK04837 329 NYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
25-354 |
1.36e-05 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 48.66 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 25 EPIIQNLLDGNDTFVLMPTGGGKSLCYQLP---SLLMEG-TAIVISPLIALMKNQvdaMRNFSEEDGVAhfINSSLNKGA 100
Cdd:PRK00254 30 EALKSGVLEGKNLVLAIPTASGKTLVAEIVmvnKLLREGgKAVYLVPLKALAEEK---YREFKDWEKLG--LRVAMTTGD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 101 IDQvrSDILAGKTKLLYVAPE---SLTKEENvEFLRSVKIsfYAVDEAHCISEWGHDFRPEYrrirpIINEI-GKAPLIA 176
Cdd:PRK00254 105 YDS--TDEWLGKYDIIIATAEkfdSLLRHGS-SWIKDVKL--VVADEIHLIGSYDRGATLEM-----ILTHMlGRAQILG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 177 LTATA--TPKVQHDIQKNLGMVD---AHVFKSSFNRPNLYYE---VRPKTQNVDKDIIKFIKNNpeKSGIIYCLSRKKVE 248
Cdd:PRK00254 175 LSATVgnAEELAEWLNAELVVSDwrpVKLRKGVFYQGFLFWEdgkIERFPNSWESLVYDAVKKG--KGALVFVNTRRSAE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 249 -----------------------ELAEILQANGIN---ARA-------YHAGMDSATRTQNQDDFLMEKIDVIVATIAFG 295
Cdd:PRK00254 253 kealelakkikrfltkpelralkELADSLEENPTNeklKKAlrggvafHHAGLGRTERVLIEDAFREGLIKVITATPTLS 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492255599 296 MGIDKPDVRYVIH----------YDIPkSLEgYYQETGRAGRD--GGEGQCITFYTNKDLQKL-EKFMQGKP 354
Cdd:PRK00254 333 AGINLPAFRVIIRdtkrysnfgwEDIP-VLE-IQQMMGRAGRPkyDEVGEAIIVATTEEPSKLmERYIFGKP 402
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
235-331 |
2.99e-05 |
|
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: 44.56 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 235 KSGIIYCLSRKKVEELAEIL------QANGINARAYHAGMDSATRTQNQDDFLMEKIDVIVATIAFGMGIDKPDVRYVIH 308
Cdd:cd18796 39 KSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQ 118
|
90 100
....*....|....*....|...
gi 492255599 309 YDIPKSLEGYYQETGRAGRDGGE 331
Cdd:cd18796 119 IGSPKSVARLLQRLGRSGHRPGA 141
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
227-335 |
3.10e-05 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 47.42 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 227 KFIKNNPEKSGIIYCLSRKKVEELAEILQANGINARAY--------HAGMdsatrTQNQ-----DDFLMEKIDVIVATIA 293
Cdd:COG1111 346 EQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskegDKGL-----TQKEqieilERFRAGEFNVLVATSV 420
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 492255599 294 FGMGIDKPDVRYVIHYD-IPKSLEgYYQETGRAGRdGGEGQCI 335
Cdd:COG1111 421 AEEGLDIPEVDLVIFYEpVPSEIR-SIQRKGRTGR-KREGRVV 461
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
216-341 |
4.89e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 46.79 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 216 PKTQNVdKDIIKFI-KNNPEKSGIIYCLSRKKVEELAEILQANGINARAY--------HAGMdsatrTQNQ-----DDFL 281
Cdd:PRK13766 347 PKLEKL-REIVKEQlGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFvgqaskdgDKGM-----SQKEqieilDKFR 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492255599 282 MEKIDVIVATIAFGMGIDKPDVRYVIHYD-IP---KSLegyyQETGRAGRdGGEGQCITFYTNK 341
Cdd:PRK13766 421 AGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPseiRSI----QRKGRTGR-QEEGRVVVLIAKG 479
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
223-329 |
9.64e-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: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 223 KDIIKFIKNNPEKSgIIYCLSRKKVEELAEILQANGINARAYHAGMDSATRTQNQDDF-LMEKIDVIVATI-AFGMGIDK 300
Cdd:cd18793 17 LELLEELREPGEKV-LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnEDPDIRVFLLSTkAGGVGLNL 95
|
90 100 110
....*....|....*....|....*....|..
gi 492255599 301 PDVRYVIHYDI---PKSLEgyyQETGRAGRDG 329
Cdd:cd18793 96 TAANRVILYDPwwnPAVEE---QAIDRAHRIG 124
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
41-180 |
1.17e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 42.68 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 41 MPTGGGKSLC-YQLPSLLMEGTAIVISPLIALMKNQVDAMRNFSEEDgvahfinsslnkgAIDQVRSDILAGKT-KLLYV 118
Cdd:cd17926 25 LPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDS-------------SIGLIGGGKKKDFDdANVVV 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492255599 119 A-PESLTKEENVEFLRSVKISFYAVDEAHCISEwghdfrPEYRRIRPIINeigKAPLIALTAT 180
Cdd:cd17926 92 AtYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPA------KTFSEILKELN---AKYRLGLTAT 145
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
27-180 |
1.27e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 43.04 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 27 IIQNLLDGNDTFVL-MPTGGGKS-----LCYQLPSLLMEGTAIVISPLIALMKNQVDAMRNFSEEdgvAHFINSSLNKGA 100
Cdd:pfam04851 15 LLESIKNGQKRGLIvMATGSGKTltaakLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPN---YVEIGEIISGDK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 101 IDQVRSDIlagktKLLYVAPESLTKEENVEFLRSVKISF--YAVDEAHcisewgHDFRPEYRRirpIINEIGKAPLIALT 178
Cdd:pfam04851 92 KDESVDDN-----KIVVTTIQSLYKALELASLELLPDFFdvIIIDEAH------RSGASSYRN---ILEYFKPAFLLGLT 157
|
..
gi 492255599 179 AT 180
Cdd:pfam04851 158 AT 159
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
34-180 |
1.51e-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: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 34 GNDTFVLMPTGGGKSLCYQLPSL--LME----GTAIV-ISPLIALMKNQVDAMRNFSEEDGVAhfINSSLNKGAIDQ-VR 105
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALssLADepekGVQVLyISPLKALINDQERRLEEPLDEIDLE--IPVAVRHGDTSQsEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 106 SDILAGKTKLLYVAPESL----TKEENVEFLRSVKisFYAVDEAHCI--SEWGHDFRPEYRRIRPIIneIGKAPLIALTA 179
Cdd:cd17922 79 AKQLKNPPGILITTPESLelllVNKKLRELFAGLR--YVVVDEIHALlgSKRGVQLELLLERLRKLT--GRPLRRIGLSA 154
|
.
gi 492255599 180 T 180
Cdd:cd17922 155 T 155
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
23-329 |
2.08e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 44.87 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 23 NQEPIIQNLLDGNDTFVLMPTGGGKSLC-----YQlpSLLMEGTAIVISPLIALmknqvdAMRNFSEedgvahfinssln 97
Cdd:PRK01172 26 HQRMAIEQLRKGENVIVSVPTAAGKTLIaysaiYE--TFLAGLKSIYIVPLRSL------AMEKYEE------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 98 kgaIDQVRSdiLAGKTKLL---YVAPESLTKEENVEFLRSVK--------------ISFYAVDEAHCIsewGHDFR-PEY 159
Cdd:PRK01172 85 ---LSRLRS--LGMRVKISigdYDDPPDFIKRYDVVILTSEKadslihhdpyiindVGLIVADEIHII---GDEDRgPTL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 160 RRIRPIINEIG-KAPLIALTATATpkvqhDIQKNLGMVDAHVFKSSFnRP-----NLYYEVRPKT---QNVDKDIIKFIK 230
Cdd:PRK01172 157 ETVLSSARYVNpDARILALSATVS-----NANELAQWLNASLIKSNF-RPvplklGILYRKRLILdgyERSQVDINSLIK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 231 NNPEKSG--IIYCLSRKKVEELAEIL----------QANGINARAY---------------HAGMDSATRTQNQDDFLME 283
Cdd:PRK01172 231 ETVNDGGqvLVFVSSRKNAEDYAEMLiqhfpefndfKVSSENNNVYddslnemlphgvafhHAGLSNEQRRFIEEMFRNR 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 492255599 284 KIDVIVATIAFGMGIDKPdVRYVIHYDIPKSLEGYY---------QETGRAGRDG 329
Cdd:PRK01172 311 YIKVIVATPTLAAGVNLP-ARLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPG 364
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
214-327 |
2.58e-04 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 41.96 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 214 VRPKTQNVDKDIIKFIKNNPEKSG---IIYCLSRKKVEELAEILQANGINARA----------YHAGMDSATRTQNQDDF 280
Cdd:cd18801 7 IHPKLEKLEEIVKEHFKKKQEGSDtrvIIFSEFRDSAEEIVNFLSKIRPGIRAtrfigqasgkSSKGMSQKEQKEVIEQF 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 492255599 281 LMEKIDVIVATIAFGMGIDKPDVRYVIHYDIPKSLEGYYQETGRAGR 327
Cdd:cd18801 87 RKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
7-67 |
1.51e-03 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 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: 350707 [Multi-domain] Cd Length: 214 Bit Score: 40.65 E-value: 1.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492255599 7 LTDQLKKYFGFDNFKGNQEPIIQNLLDGNDTFVLMPTGGGKSLCYQLP--SLLM---------EGT-AIVISP 67
Cdd:cd17949 1 LVSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPiiQRLLsleprvdrsDGTlALVLVP 73
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
31-181 |
6.61e-03 |
|
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: 38.40 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 31 LLDGNDTFVLMPTGGGKSLCYQLPSLL----MEGTAIVISPLIALMkNQVdaMRNFSEEdgvahFINSSLNKGAI--DQV 104
Cdd:cd17921 14 YLSGDSVLVSAPTSSGKTLIAELAILRalatSGGKAVYIAPTRALV-NQK--EADLRER-----FGPLGKNVGLLtgDPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 105 RSDILAGKTKLLYVAPE---SLTKEENVEFLRSVKIsfYAVDEAHCISewghdfrpEYRR-------IRPIINEIGKAPL 174
Cdd:cd17921 86 VNKLLLAEADILVATPEkldLLLRNGGERLIQDVRL--VVVDEAHLIG--------DGERgvvlellLSRLLRINKNARF 155
|
....*..
gi 492255599 175 IALTATA 181
Cdd:cd17921 156 VGLSATL 162
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
234-327 |
7.05e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 37.15 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255599 234 EKSGIIYCLSRKKVEELAEILQANGINARAYHAGMDSATRTQN---QDDFLMEKIDVIVATIAFGMGIDKPDVRYVIhYD 310
Cdd:cd18799 6 EIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV-FL 84
|
90
....*....|....*...
gi 492255599 311 IP-KSLEGYYQETGRAGR 327
Cdd:cd18799 85 RPtESRTLFLQMLGRGLR 102
|
|
| |
