|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
6-477 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 758.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 6 LDQARELLRKFYGYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPALVFPGITLVISPLISLMKDQVDSLLEQG 85
Cdd:COG0514 2 RDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 86 VPATYINSQLSLDESQQRLAAIAAGRYKLIYVAPERLDTDYFRYIIEQQEISMVAVDEAHCLSQWGHDFRPSYRQIAPFI 165
Cdd:COG0514 82 IRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 166 ASLPQRPLVsAFTATATPEVKEDIVTLLHLRQPRIHVTGFDRPNLYFEVRRG--EDKKKYITGFIKKHPEESGIIYAATR 243
Cdd:COG0514 162 ERLPNVPVL-ALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGGSGIVYCLSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 244 KEVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKNIEAYYQEAGR 323
Cdd:COG0514 241 KKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 324 AGRDGEPGSCILLFSPQDVMTQKYLIDVSIENEERKAHNLGTLQKMVDYCHTPECLRHFIIHYFGGASTDvTCDNCGNCK 403
Cdd:COG0514 321 AGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAE-PCGNCDNCL 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654668938 404 AGLERIDVTIDAQKVFSCVYRMHESFGLTLVAQVLKGSKDKRVRELHFDKLSTFGLFKERTLADIKLLIQRFIA 477
Cdd:COG0514 400 GPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLA 473
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
9-592 |
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: 749.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 9 ARELLRKFYGYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPALVFPGITLVISPLISLMKDQVDSLLEQGVPA 88
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 89 TYINSQLSLDESQQRLAAIAAGRYKLIYVAPERLDTDYFRYIIEQQEISMVAVDEAHCLSQWGHDFRPSYRQIAPFIASL 168
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 169 PQRPlVSAFTATATPEVKEDIVTLLHLRQPRIHVTGFDRPNLYFEVRRGEDKKKYITGFIKKHPEESGIIYAATRKEVDS 248
Cdd:TIGR01389 161 PQVP-RIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 249 LYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKNIEAYYQEAGRAGRDG 328
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 329 EPGSCILLFSPQDVMTQKYLIDVSIENEERKAHNLGTLQKMVDYCHTPECLRHFIIHYFGGASTDvTCDNCGNCKAGLER 408
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVE-PCGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 409 IDVTIDAQKVFSCVYRMHESFGLTLVAQVLKGSKDKRVRELHFDKLSTFGLFKERTLADIKLLIQRFIATDYLALTESKY 488
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 489 PVVTLRPSAYPVLKGQEKVYQAVPQPEREK---------EPAAPELFDHLRHLRKEIATREHVPPYVVFSDATLRDMCRV 559
Cdd:TIGR01389 479 IGLQLTEAARKVLKNEVEVLLRPFKVVAKEktrvqknlsVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEK 558
|
570 580 590
....*....|....*....|....*....|...
gi 654668938 560 QPQSLDEMLTVKGIGEQKLRKYGQEFLECLQKN 592
Cdd:TIGR01389 559 RPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
8-590 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 550.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 8 QARELLRKFYGYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPALVFPGITLVISPLISLMKDQVDSLLEQGVP 87
Cdd:PRK11057 12 LAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 88 ATYINSQLSLDESQQRLAAIAAGRYKLIYVAPERLDTDYFRYIIEQQEISMVAVDEAHCLSQWGHDFRPSYRQIAPFIAS 167
Cdd:PRK11057 92 AACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 168 LPQRPLVsAFTATATPEVKEDIVTLLHLRQPRIHVTGFDRPNLYFEVRRGEDKKKYITGFIKKHPEESGIIYAATRKEVD 247
Cdd:PRK11057 172 FPTLPFM-ALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 248 SLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKNIEAYYQEAGRAGRD 327
Cdd:PRK11057 251 DTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 328 GEPGSCILLFSPQDVMTQKYLIDVSIENEER--KAHNLGTlqkMVDYCHTPECLRHFIIHYFgGASTDVTCDNCGNCKAG 405
Cdd:PRK11057 331 GLPAEAMLFYDPADMAWLRRCLEEKPAGQQQdiERHKLNA---MGAFAEAQTCRRLVLLNYF-GEGRQEPCGNCDICLDP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 406 LERIDVTIDAQKVFSCVYRMHESFGLTLVAQVLKGSKDKRVRELHFDKLSTFGLFKE----------RTLADIKLLIQRF 475
Cdd:PRK11057 407 PKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDkshehwvsviRQLIHLGLVTQNI 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 476 IATDYLALTEskypvvtlrpSAYPVLKGQEKVYQAVPQPEREKEPAAP---------ELFDHLRHLRKEIATREHVPPYV 546
Cdd:PRK11057 487 AQHSALQLTE----------AARPVLRGEVSLQLAVPRIVALKPRAMQksfggnydrKLFAKLRKLRKSIADEENIPPYV 556
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 654668938 547 VFSDATLRDMCRVQPQSLDEMLTVKGIGEQKLRKYGQEFLECLQ 590
Cdd:PRK11057 557 VFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIR 600
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
13-463 |
1.84e-170 |
|
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: 492.36 E-value: 1.84e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 13 LRKFYGYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPALVFPGITLVISPLISLMKDQVDSLLEQGVPATYIN 92
Cdd:TIGR00614 3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 93 SQLSLDESQQRLAAIAAGRYKLIYVAPERL--DTDYFRYIIEQQEISMVAVDEAHCLSQWGHDFRPSYRQIAPFIASLPQ 170
Cdd:TIGR00614 83 SAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsaSNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFPN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 171 RPLVsAFTATATPEVKEDIVTLLHLRQPRIHVTGFDRPNLYFEVRRG-----EDKKKYItgfIKKHPEESGIIYAATRKE 245
Cdd:TIGR00614 163 VPVM-ALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKtpkilEDLLRFI---RKEFEGKSGIIYCPSRKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 246 VDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKNIEAYYQEAGRAG 325
Cdd:TIGR00614 239 VEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 326 RDGEPGSCILLFSPQDVMTQKYLIdVSIENEERKAHNLGTLQKMVDYCHTPECLRHFIIHYFG---------GASTDVTC 396
Cdd:TIGR00614 319 RDGLPSECHLFYAPADMNRLRRLL-MEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGekgfnksfcIMGTEKCC 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654668938 397 DNCGNCKAgLERIDVT-------IDAQKVFSCVYRMHESFGLTLVAQVLKGSKDKRVRELHFDKLSTFGLFKER 463
Cdd:TIGR00614 398 DNCCKRLD-YKTKDVTdkvydfgPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKDE 470
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
14-590 |
4.04e-110 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 356.51 E-value: 4.04e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 14 RKFYGYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPALVFPGITLVISPLISLMKDQVDSLLEQGVPATYINS 93
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 94 QLSLDESQQRLAAIAAG--RYKLIYVAPERL-DTDYFRYIIE----QQEISMVAVDEAHCLSQWGHDFRPSYRQIAPFIA 166
Cdd:PLN03137 533 GMEWAEQLEILQELSSEysKYKLLYVTPEKVaKSDSLLRHLEnlnsRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 167 SLPQRPlVSAFTATATPEVKEDIVTLLHLRQPRIHVTGFDRPNLYFEVRRGEDK-KKYITGFIKK-HPEESGIIYAATRK 244
Cdd:PLN03137 613 KFPNIP-VLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKcLEDIDKFIKEnHFDECGIIYCLSRM 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 245 EVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKNIEAYYQEAGRA 324
Cdd:PLN03137 692 DCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRA 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 325 GRDGEPGSCILLFSPQDVMTQKYLIDVSIENE-------ERKAH-------NLGTLQKMVDYCHTP-ECLRHF-IIHY-- 386
Cdd:PLN03137 772 GRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQspmamgyNRMASsgriletNTENLLRMVSYCENEvDCRRFLqLVHFge 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 387 -FGGASTDVTCDNCGNCKAGLERiDVTIDAQKVFSCVYRMHESFGLTLVAQVLKGSKDKRVRELHFDKLSTFGLFKERTL 465
Cdd:PLN03137 852 kFDSTNCKKTCDNCSSSKSLIDK-DVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLSK 930
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 466 ADIKLLIQRFIATDYLA-----------------LTESKYPV-------VTLR-PSAYPVLKgQEKvYQAVP-------- 512
Cdd:PLN03137 931 GEASRILHYLVTEDILAedvkksdlygsvssllkVNESKAYKlfsggqtIIMRfPSSVKASK-PSK-FEATPakgpltsg 1008
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 513 --QPEREKEPAAPE--------LFDHLRHLRKEIATR--EHVPPYVVFSDATLRDMCRVQPQSLDEMLTVKGIGEQKLRK 580
Cdd:PLN03137 1009 kqSTLPMATPAQPPvdlnlsaiLYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSK 1088
|
650
....*....|
gi 654668938 581 YGQEFLECLQ 590
Cdd:PLN03137 1089 YGDRLLETIE 1098
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
10-206 |
4.76e-103 |
|
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: 309.85 E-value: 4.76e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 10 RELLRKFYGYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPALVFPGITLVISPLISLMKDQVDSLLEQGVPAT 89
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 90 YINSQLSLDESQQRLAAIAAGRYKLIYVAPERLDTDYFRYII----EQQEISMVAVDEAHCLSQWGHDFRPSYRQIAPFI 165
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLqrlpERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 654668938 166 ASLPQRPLVsAFTATATPEVKEDIVTLLHLRQPRIHVTGFD 206
Cdd:cd17920 161 RALPGVPIL-ALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
11-193 |
3.52e-73 |
|
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: 232.53 E-value: 3.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 11 ELLRKFYGYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPALVF----PGITLVISPLISLMKDQVDSLlEQGV 86
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLrrrgPGLTLVVSPLIALMKDQVDAL-PRAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 87 PATYINSQLSLDESQQRLAAIAAGRYKLIYVAPERLDTDYFRYIIEQQE-ISMVAVDEAHCLSQWGHDFRPSYRQIAPFI 165
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPpISLLVVDEAHCISEWSHNFRPDYLRLCRVL 160
|
170 180
....*....|....*....|....*...
gi 654668938 166 ASLPQRPLVSAFTATATPEVKEDIVTLL 193
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVEDIASHL 188
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
13-206 |
2.05e-64 |
|
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: 209.63 E-value: 2.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 13 LRKFYGYQDFRPAQRPVVESLL-SGQDTVAIMPTGAGKSICFQLPALVFPGITLVISPLISLMKDQVDSLLEQGVPATYI 91
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 92 NSQlsldESQQRLAAIAAGRYKLIYVAPERLDTDyfRYIIEQQE--ISMVAVDEAHCLSQWGHDFRPSYRQIAPFIASLP 169
Cdd:cd18017 84 GSA----QSQNVLDDIKMGKIRVIYVTPEFVSKG--LELLQQLRngITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLP 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 654668938 170 QRPLVsAFTATATPEVKEDIVTLLHLRQPRIHVTGFD 206
Cdd:cd18017 158 NVPIV-ALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
207-337 |
5.51e-58 |
|
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: 190.50 E-value: 5.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 207 RPNLYFEVRRGEDKKKYIT--GFIK-KHPEESGIIYAATRKEVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDN 283
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDllKRIKvEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 654668938 284 VQVIVATNAFGMGIDKSNVRYVIHYNMPKNIEAYYQEAGRAGRDGEPGSCILLF 337
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
4-206 |
6.45e-58 |
|
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: 192.97 E-value: 6.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 4 PYLDQARELLRKFYGYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPALVFPGITLVISPLISLMKDQVDSLLE 83
Cdd:cd18015 1 PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 84 QGVPATYINSQLSLDESQQRLAAI--AAGRYKLIYVAPERL-DTDYFRYIIEQQE----ISMVAVDEAHCLSQWGHDFRP 156
Cdd:cd18015 81 LGISATMLNASSSKEHVKWVHAALtdKNSELKLLYVTPEKIaKSKRFMSKLEKAYnagrLARIAIDEVHCCSQWGHDFRP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 654668938 157 SYRQIAPFIASLPQRPLVsAFTATATPEVKEDIVTLLHLRQPRIHVTGFD 206
Cdd:cd18015 161 DYKKLGILKRQFPNVPIL-GLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DpdF |
NF041063 |
protein DpdF; |
4-354 |
4.72e-55 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 199.75 E-value: 4.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 4 PYLDQARELLRKFY-------------GYQDFR-PAQRPVVESLLS---GQDTVAIMPTGAGKSICFQLPALVFP---GI 63
Cdd:NF041063 109 PFEDVFAERLRRTLepvpgdpflaealGFTHYRsPGQREAVRAALLappGSTLIVNLPTGSGKSLVAQAPALLASrqgGL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 64 TLVISPLISLMKDQ----VDSLLEQGVPAT----YInSQLSLDESQQRLAAIAAGRYKLIYVAPERLDTDYFRYII---E 132
Cdd:NF041063 189 TLVVVPTVALAIDQerraRELLRRAGPDLGgplaWH-GGLSAEERAAIRQRIRDGTQRILFTSPESLTGSLRPALFdaaE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 133 QQEISMVAVDEAHCLSQWGHDFRPSYRQIAPFIASL-----PQRPLVSAF-TATATPEVKEDIVTLL------------H 194
Cdd:NF041063 268 AGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSLlrlapSGRPFRTLLlSATLTESTLDTLETLFgppgpfivvsavQ 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 195 LRQ-PRIHVTGFDRPnlyfevrrgEDKKKYITGFIKKHPEESgIIYAATRKEVDSLYEYLKKKKFA-VGRYHAGMSDKAR 272
Cdd:NF041063 348 LRPePAYWVAKCDSE---------EERRERVLEALRHLPRPL-ILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAER 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 273 NQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKNIEAYYQEAGRAGRDGEPGSCILLFSPQDV-----MTQKY 347
Cdd:NF041063 418 ERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLdiaksLNRPK 497
|
....*..
gi 654668938 348 LIdvSIE 354
Cdd:NF041063 498 LI--SVE 502
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
10-198 |
2.99e-53 |
|
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: 180.36 E-value: 2.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 10 RELLRKFYGYQDFR-PAQRPVVESLLSG-QDTVAIMPTGAGKSICFQLPALVFPGITLVISPLISLMKDQVDSLLEQGVP 87
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 88 ATYINSQLSLDESQQRLAAIAAGR--YKLIYVAPERLDTDYFRYIIEQ----QEISMVAVDEAHCLSQWGHDFRPSYRQI 161
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEKpqTKFLYITPEMAATSSFQPLLSSlvsrNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 654668938 162 APFIASLPQRPLVsAFTATATPEVKEDIVTLLHLRQP 198
Cdd:cd18014 161 GALRSRYGHVPWV-ALTATATPQVQEDIFAQLRLKKP 196
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
11-206 |
1.74e-50 |
|
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: 173.09 E-value: 1.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 11 ELLRKFYGYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPALVFPGITLVISPLISLMKDQVDSLLEQGVPATY 90
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 91 INSQLSLDESQQRLAAIAAGR--YKLIYVAPERLDT-----DYFRYIIEQQEISMVAVDEAHCLSQWGHDFRPSYRQIAP 163
Cdd:cd18016 87 LTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKISAsnrliSTLENLYERKLLARFVIDEAHCVSQWGHDFRPDYKRLNM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 654668938 164 FIASLPQRPLVsAFTATATPEVKEDIVTLLHLRQPRIHVTGFD 206
Cdd:cd18016 167 LRQKFPSVPMM-ALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
407-512 |
7.38e-35 |
|
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: 127.27 E-value: 7.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 407 ERIDVTIDAQKVFSCVYRMHESFGLTLVAQVLKGSKDKRVRELHFDKLSTFGLFKERTLADIKLLIQRFIATDYLALTES 486
Cdd:pfam09382 3 ETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDIE 82
|
90 100
....*....|....*....|....*.
gi 654668938 487 KYPVVTLRPSAYPVLKGQEKVYQAVP 512
Cdd:pfam09382 83 FYSVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
23-187 |
2.56e-30 |
|
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: 116.57 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 23 RPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPAL-----VFPGI-TLVISPLISLMKDQVDSLLEQGVPATY-INSQL 95
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdkLDNGPqALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 96 SLDESQQRLAAIAagRYKLIYVAPERLDtDYFRYIIEQQEISMVAVDEAHCLSQWGhdFRPSYRQIapfIASLPQRPLVS 175
Cdd:pfam00270 81 GGDSRKEQLEKLK--GPDILVGTPGRLL-DLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEI---LRRLPKKRQIL 152
|
170
....*....|..
gi 654668938 176 AFTATATPEVKE 187
Cdd:pfam00270 153 LLSATLPRNLED 164
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
410-501 |
3.99e-30 |
|
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: 113.34 E-value: 3.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 410 DVTIDAQKVFSCVYRMHESFGLTLVAQVLKGSKDKRVRELHFDKLSTFGLFKERTLADIKLLIQRFIATDYLALTESKYP 489
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 654668938 490 VVTLRPSAYPVL 501
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
18-341 |
1.57e-26 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 112.16 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 18 GYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPAL--VFPGI-----TLVISP---LIslmkDQVDSLLEQ--- 84
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPtreLA----LQVAEELRKlak 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 85 -----------GVPatyINSQLsldesqQRLAAIAAgryklIYVA-PERLdTDYfryiIEQ-----QEISMVAVDEA-HC 146
Cdd:COG0513 97 ylglrvatvygGVS---IGRQI------RALKRGVD-----IVVAtPGRL-LDL----IERgaldlSGVETLVLDEAdRM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 147 LSQwGhdFRPSYRQIapfIASLPQRPLVSAFTATATPEVKEdivtLL--HLRQP-RIHVTGFDRPN-----LYFEVRRgE 218
Cdd:COG0513 158 LDM-G--FIEDIERI---LKLLPKERQTLLFSATMPPEIRK----LAkrYLKNPvRIEVAPENATAetieqRYYLVDK-R 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 219 DKKKYITGFIKKHPEESGIIYAATRKEVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGID 298
Cdd:COG0513 227 DKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGID 306
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 654668938 299 KSNVRYVIHYNMPKNIEAYYQEAGRAGRDGEPGSCILLFSPQD 341
Cdd:COG0513 307 IDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDE 349
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
219-328 |
2.01e-26 |
|
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: 103.83 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 219 DKKKYITGFIKKHPEESGIIYAATRKEVDslYEYL-KKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGI 297
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLlEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 654668938 298 DKSNVRYVIHYNMPKNIEAYYQEAGRAGRDG 328
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
247-328 |
1.13e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 100.75 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 247 DSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKNIEAYYQEAGRAGR 326
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 654668938 327 DG 328
Cdd:smart00490 81 AG 82
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
210-337 |
1.36e-25 |
|
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: 102.20 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 210 LYFEVRRGEDKKKYITGFIKKHPEESGIIYAATRKEVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVA 289
Cdd:cd18787 4 LYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 654668938 290 TNAFGMGIDKSNVRYVIHYNMPKNIEAYYQEAGRAGRDGEPGSCILLF 337
Cdd:cd18787 84 TDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
15-215 |
1.40e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 101.41 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 15 KFYGYQDFRPAQRPVVESLLSG-QDTVAIMPTGAGKSICFQLPAL-----VFPGITLVISPLISLMKDQVDSLLEQGVPA 88
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALealkrGKGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 89 TYIN-SQLSLDESQQRLAAIAAGRYKLIYVAPERLDTDYFRYIIEQQEISMVAVDEAHCLSQWGhdFRPSYRQIapfIAS 167
Cdd:smart00487 82 GLKVvGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL---LKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 654668938 168 LPQRPLVSAFTATATPEVKEDivTLLHLRQPrIHVTGFDRPNLYFEVR 215
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENL--LELFLNDP-VFIDVGFTPLEPIEQF 201
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
524-589 |
3.35e-22 |
|
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: 90.29 E-value: 3.35e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654668938 524 ELFDHLRHLRKEIATREHVPPYVVFSDATLRDMCRVQPQSLDEMLTVKGIGEQKLRKYGQEFLECL 589
Cdd:pfam00570 3 ALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
18-341 |
6.94e-22 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 99.48 E-value: 6.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 18 GYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLP-----ALVFPG--------ITLVISP---LISLMKDQVdSL 81
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrcCTIRSGhpseqrnpLAMVLTPtreLCVQVEDQA-KV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 82 LEQGVPatyINSQLSL--DESQQRLAAIAAGrYKLIYVAPERLDTDYFRYIIEQQEISMVAVDEAHCLSQWGhdFRPSYR 159
Cdd:PLN00206 219 LGKGLP---FKTALVVggDAMPQQLYRIQQG-VELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG--FRDQVM 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 160 QIapfIASLPQrPLVSAFTATATPEVkEDIVTLLHLRQPRIHVTGFDRPN-------LYFEVRRgedKKKYITGFI--KK 230
Cdd:PLN00206 293 QI---FQALSQ-PQVLLFSATVSPEV-EKFASSLAKDIILISIGNPNRPNkavkqlaIWVETKQ---KKQKLFDILksKQ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 231 HPEESGIIYAATRKEVDSLYEYLKK-KKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYN 309
Cdd:PLN00206 365 HFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFD 444
|
330 340 350
....*....|....*....|....*....|..
gi 654668938 310 MPKNIEAYYQEAGRAGRDGEPGSCILLFSPQD 341
Cdd:PLN00206 445 MPNTIKEYIHQIGRASRMGEKGTAIVFVNEED 476
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
524-592 |
3.44e-19 |
|
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: 81.96 E-value: 3.44e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654668938 524 ELFDHLRHLRKEIATREHVPPYVVFSDATLRDMCRVQPQSLDEMLTVKGIGEQKLRKYGQEFLECLQKN 592
Cdd:smart00341 6 RLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEA 74
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
339-403 |
1.11e-18 |
|
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: 80.03 E-value: 1.11e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654668938 339 PQDVMTQKYLIDVSIENEERKAHNLGTLQKMVDYC-HTPECLRHFIIHYFGGASTDVTCDNCGNCK 403
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCeNTTDCRRKQLLRYFGEEFDSEPCGNCDNCL 66
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
23-363 |
2.02e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 85.85 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 23 RPAQRPVVESLLS-----GQDTVAIMPTGAGKSICFQLPA--LVFPGITLVISPLISLMKDQVDSLLEqgvpatYINSQL 95
Cdd:COG1061 82 RPYQQEALEALLAalergGGRGLVVAPTGTGKTVLALALAaeLLRGKRVLVLVPRRELLEQWAEELRR------FLGDPL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 96 SLDESQQRLAAIAAGRYKLIYVAPERLDT-DYFRYIIeqqeismvaVDEAHclsqwgHDFRPSYRQIapfIASLPQRPLV 174
Cdd:COG1061 156 AGGGKKDSDAPITVATYQSLARRAHLDELgDRFGLVI---------IDEAH------HAGAPSYRRI---LEAFPAAYRL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 175 SaftATATPE----------------VKEDIVTLL---HLRQPRIHV--TGFDRPNLYFEVRRGEDKKKYITG------- 226
Cdd:COG1061 218 G---LTATPFrsdgreillflfdgivYEYSLKEAIedgYLAPPEYYGirVDLTDERAEYDALSERLREALAADaerkdki 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 227 ---FIKKHPEES-GIIYAATRKEVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNV 302
Cdd:COG1061 295 lreLLREHPDDRkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRL 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654668938 303 RYVIhYNMP-KNIEAYYQEAGRAGRDGEPGSCILLFSpqdvmtqkyLIDVSIENEERKAHNL 363
Cdd:COG1061 375 DVAI-LLRPtGSPREFIQRLGRGLRPAPGKEDALVYD---------FVGNDVPVLEELAKDL 426
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
6-346 |
5.47e-17 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 83.34 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 6 LDQARELLRKFYGYQDFRPA--QRPVVESLLSGQDTVAIMPTGAGKSICFQLPAL------VFPGITLVISPLISL---- 73
Cdd:PTZ00424 33 LKLNEDLLRGIYSYGFEKPSaiQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALqlidydLNACQALILAPTRELaqqi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 74 ------MKDQVDSLLEQGVPATYINSQLSLDESQQRLAAIAAGRyklIYvapERLDTDYFRYiieqQEISMVAVDEAHCL 147
Cdd:PTZ00424 113 qkvvlaLGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGR---VY---DMIDKRHLRV----DDLKLFILDEADEM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 148 SQWG-----HD-FR--PSYRQIAPFIASLPQRPLVSAFTATATPE---VKEDIVTLLHLRQprihvtgfdrpnLYFEVRR 216
Cdd:PTZ00424 183 LSRGfkgqiYDvFKklPPDVQVALFSATMPNEILELTTKFMRDPKrilVKKDELTLEGIRQ------------FYVAVEK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 217 GEDKKKYITGFIKKHPEESGIIYAATRKEVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMG 296
Cdd:PTZ00424 251 EEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARG 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 654668938 297 IDKSNVRYVIHYNMPKNIEAYYQEAGRAGRDGEPGSCILLFSPQDVMTQK 346
Cdd:PTZ00424 331 IDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLK 380
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
36-176 |
5.80e-16 |
|
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: 75.13 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 36 GQDTVAIMPTGAGKSICFQLPAL----VFPGITLVISPLISLMKDQ---VDSLLEQGVPATYINSqlslDESQQRLAAIA 108
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALllllKKGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVG----GSSAEEREKNK 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654668938 109 AGRYKLIYVAPERLDTDYFRYI-IEQQEISMVAVDEAHCLSQWGHDFRPSYRQIAPFIASLPQRPLVSA 176
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSA 145
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
18-341 |
1.36e-14 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 76.49 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 18 GYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICF------QL-----PALVFPG--ITLVISP----LISLMKDQVDS 80
Cdd:PRK01297 106 GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFlisiinQLlqtppPKERYMGepRALIIAPtrelVVQIAKDAAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 81 LLEQGVPATYINSQLSLDESQQRLAAiaagRYKLIYVA-PERLDTDYFRYIIEQQEISMVAVDEAHCLSQWGhdFRPSYR 159
Cdd:PRK01297 186 TKYTGLNVMTFVGGMDFDKQLKQLEA----RFCDILVAtPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMG--FIPQVR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 160 QIAPFIASLPQRPLVsAFTATATpevkEDIVTLLH--LRQPRI------HVTGFDRPNLYFEVRrGEDKKKYITGFIKKH 231
Cdd:PRK01297 260 QIIRQTPRKEERQTL-LFSATFT----DDVMNLAKqwTTDPAIveiepeNVASDTVEQHVYAVA-GSDKYKLLYNLVTQN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 232 PEESGIIYAATRKEVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMP 311
Cdd:PRK01297 334 PWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLP 413
|
330 340 350
....*....|....*....|....*....|
gi 654668938 312 KNIEAYYQEAGRAGRDGEPGSCILLFSPQD 341
Cdd:PRK01297 414 EDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
26-336 |
3.89e-13 |
|
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: 72.56 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 26 QRPVVESLLSGQDTVAIMPTGAGKSICFQLPALV----FPGIT-LVISPLISLMKDQVDSL------LEQGV-PATYins 93
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEalleDPGATaLYLYPTKALARDQLRRLrelaeaLGLGVrVATY--- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 94 qlslD---ESQQRLAAIAAGRYklIYVAPERLDT----------DYF---RYIIeqqeismvaVDEAHclsqwghdfrpS 157
Cdd:COG1205 138 ----DgdtPPEERRWIREHPDI--VLTNPDMLHYgllphhtrwaRFFrnlRYVV---------IDEAH-----------T 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 158 YR---------------QIAPFIASLPQrpLVSAfTAT-ATPE-------------VKEDivtlLHLRQPRIHVtgFDRP 208
Cdd:COG1205 192 YRgvfgshvanvlrrlrRICRHYGSDPQ--FILA-SATiGNPAehaerltgrpvtvVDED----GSPRGERTFV--LWNP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 209 NLYFEVRR---GEDKKKYITGFIKKhpEESGIIYAATRKEVDSLYEYLKK---KKFAVGR---YHAGMSDKARNQAQEDF 279
Cdd:COG1205 263 PLVDDGIRrsaLAEAARLLADLVRE--GLRTLVFTRSRRGAELLARYARRalrEPDLADRvaaYRAGYLPEERREIERGL 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 654668938 280 LYDNVQVIVATNAFGMGIDKSNVRYVI--HYnmPKNIEAYYQEAGRAGRDGEPGSCILL 336
Cdd:COG1205 341 RSGELLGVVSTNALELGIDIGGLDAVVlaGY--PGTRASFWQQAGRAGRRGQDSLVVLV 397
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
34-358 |
3.97e-12 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 69.03 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 34 LSGQDTVAIMPTGAGKSICFQLPALVF--------PG---ITLVISP---LISLMKDQV----------DSLLEQGVPat 89
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAIVHinaqpllrYGdgpIVLVLAPtreLAEQIREQCnkfgasskirNTVAYGGVP-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 90 yinsqlsldeSQQRLAAIAAGRYKLIyVAPERLdTDYfryiIEQ-----QEISMVAVDEAHCLSQWGhdFRPSYRQIAPF 164
Cdd:PTZ00110 243 ----------KRGQIYALRRGVEILI-ACPGRL-IDF----LESnvtnlRRVTYLVLDEADRMLDMG--FEPQIRKIVSQ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 165 IAslPQRPLVsAFTATATPEVKEDIVTLLhlRQPRIHV-------TGFDRPNLYFEVRRGEDKKKYITGFIKKHPEESG- 236
Cdd:PTZ00110 305 IR--PDRQTL-MWSATWPKEVQSLARDLC--KEEPVHVnvgsldlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGDk 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 237 -IIYAATRKEVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKNIE 315
Cdd:PTZ00110 380 iLIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIE 459
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 654668938 316 AYYQEAGRAGRDGEPGSCILLFSPQDVMTQKYLIDVSIENEER 358
Cdd:PTZ00110 460 DYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQP 502
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
237-336 |
5.68e-12 |
|
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: 63.82 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 237 IIYAATRKEVDSLYEYLK----KKKFAVGR---YHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYN 309
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKarlvEEGPLASKvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*..
gi 654668938 310 MPKNIEAYYQEAGRAGRDGEPGSCILL 336
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
6-336 |
1.08e-11 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 67.27 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 6 LDQARELLR--KFYGYQdfRPA--QRPVVESLLSGQDTVAIMPTGAGKSICFQLPALV--------FPGIT--LVISP-- 69
Cdd:PRK11192 6 LELDESLLEalQDKGYT--RPTaiQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQhlldfprrKSGPPriLILTPtr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 70 -LISLMKDQVDSLLEQ----------GVPatYINSQLSLDESQQrlaaiaagryklIYVA-PERLdtdyFRYIIEQQ--- 134
Cdd:PRK11192 84 eLAMQVADQARELAKHthldiatitgGVA--YMNHAEVFSENQD------------IVVAtPGRL----LQYIKEENfdc 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 135 -EISMVAVDEAHCLSQWGhdFRPSYRQIAP----------FIASLpQRPLVSAFTAT---------ATPEVKEdivtllh 194
Cdd:PRK11192 146 rAVETLILDEADRMLDMG--FAQDIETIAAetrwrkqtllFSATL-EGDAVQDFAERllndpveveAEPSRRE------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 195 lrQPRIHvtgfdrpNLYFEVRRGEDKKKYITGFIKKHPEESGIIYAATRKEVDSLYEYLKKKKFAVGRYHAGMSDKARNQ 274
Cdd:PRK11192 216 --RKKIH-------QWYYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNE 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654668938 275 AQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKNIEAYYQEAGRAGRDGEPGSCILL 336
Cdd:PRK11192 287 AIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
18-359 |
1.43e-11 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 67.18 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 18 GYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLP-------ALVFPGItLVISPLISL-------MKDQVDSLLE 83
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPllhnldpELKAPQI-LVLAPTRELavqvaeaMTDFSKHMRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 84 QGVPATYINSQLSLdesqqRLAAIAAGRyKLIYVAPERLDTDYFRYIIEQQEISMVAVDEAHCLSQWGhdFRPSYRQIap 163
Cdd:PRK11634 104 VNVVALYGGQRYDV-----QLRALRQGP-QIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG--FIEDVETI-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 164 fIASLPQRPLVSAFTATaTPEVKEDIvTLLHLRQP---RIHVTGFDRPNL---YFEVRrGEDKKKYITGFIKKHPEESGI 237
Cdd:PRK11634 174 -MAQIPEGHQTALFSAT-MPEAIRRI-TRRFMKEPqevRIQSSVTTRPDIsqsYWTVW-GMRKNEALVRFLEAEDFDAAI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 238 IYAATRKEVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKNIEAY 317
Cdd:PRK11634 250 IFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESY 329
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 654668938 318 YQEAGRAGRDGEPGSCILLfspqdvmtqkylidvsIENEERK 359
Cdd:PRK11634 330 VHRIGRTGRAGRAGRALLF----------------VENRERR 355
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
280-336 |
5.46e-10 |
|
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: 55.79 E-value: 5.46e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 654668938 280 LYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKNIEAYYQEAGRAGRDG-EPGSCILL 336
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
6-326 |
7.59e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 61.45 E-value: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 6 LDQARELLRKFyGYQDFRPAQRPVVES-LLSGQDTVAIMPTGAGKSICFQLP---ALVFPGITLVISPLISL---MKDQV 78
Cdd:COG1204 8 LEKVIEFLKER-GIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAilkALLNGGKALYIVPLRALaseKYREF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 79 DSLLEQGVPATYINSqLSLDESQQRLaaiaaGRYKLIYVAPERLDTdYFRYIIE-QQEISMVAVDEAH------------ 145
Cdd:COG1204 87 KRDFEELGIKVGVST-GDYDSDDEWL-----GRYDILVATPEKLDS-LLRNGPSwLRDVDLVVVDEAHliddesrgptle 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 146 ----------------CLS----------QW------GHDFRPSYRQIA---PFIASLPQRPLVSaftatatpevKEDIV 190
Cdd:COG1204 160 vllarlrrlnpeaqivALSatignaeeiaEWldaelvKSDWRPVPLNEGvlyDGVLRFDDGSRRS----------KDPTL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 191 TLLhlrqprIHVTGFDRPNLYFE--VRRGEDKKKYITGFIKKH--PEESGII---------YAATRKEVDSLYEYLKKKk 257
Cdd:COG1204 230 ALA------LDLLEEGGQVLVFVssRRDAESLAKKLADELKRRltPEEREELeelaeelleVSEETHTNEKLADCLEKG- 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654668938 258 faVGRYHAGMSDKARNqAQED-FLYDNVQVIVATNAFGMGIdksN--VRYVI----HYNMPKNIEA--YYQEAGRAGR 326
Cdd:COG1204 303 --VAFHHAGLPSELRR-LVEDaFREGLIKVLVATPTLAAGV---NlpARRVIirdtKRGGMVPIPVleFKQMAGRAGR 374
|
|
| RQC_minor_1 |
NF041107 |
RQC-minor-1 family DNA-binding protein; The DNA-binding RQC domain (PF09382) appears primarily ... |
430-483 |
1.61e-09 |
|
RQC-minor-1 family DNA-binding protein; The DNA-binding RQC domain (PF09382) appears primarily in RecQ, a DNA helicase involved in recombination, replication, and repair. However, it appears also in this uncharacterized protein family, to which we give the name "RQC-minor-1 family DNA-binding protein." A majority of members contain an additional C-terminal predicted zinc-ribbon domain. Members appear not to show any conserved gene neighborhood.
Pssm-ID: 469031 [Multi-domain] Cd Length: 173 Bit Score: 57.20 E-value: 1.61e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 654668938 430 GLTLVAQVLKGSKDKRVRELHFDKLSTFGLFKERTLADIKLLIQRFIATDYLAL 483
Cdd:NF041107 22 GRTMLAKILKGSKDKKVLELGLDQCPAYGYYKSLTLEEITAKIDWMIKHDYLEI 75
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
212-336 |
8.39e-09 |
|
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: 54.87 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 212 FEVRRGEDKKKYITGFIKKHPEESG-IIYAATRKEVDSLYEYLKkkkfAVGRYHAGMSDKARNQAQEDFLYDNVQVIVAT 290
Cdd:cd18795 21 VDVMNKFDSDIIVLLKIETVSEGKPvLVFCSSRKECEKTAKDLA----GIAFHHAGLTREDRELVEELFREGLIKVLVAT 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 654668938 291 NAFGMGID--------KSNVRYVIHYNMPKNIEAYYQEAGRAGRDG--EPGSCILL 336
Cdd:cd18795 97 STLAAGVNlpartviiKGTQRYDGKGYRELSPLEYLQMIGRAGRPGfdTRGEAIIM 152
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
18-336 |
1.47e-08 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 57.13 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 18 GYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPALVF------------PGITLVISPLISLMKdQVDSLLEQg 85
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHlitrqphakgrrPVRALILTPTRELAA-QIGENVRD- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 86 vPATYINSQ-------LSLDESQQRLAaiaaGRYKLIYVAPERL-DTDYFRYI-IEQQEIsmVAVDEAHCLSQWG--HDF 154
Cdd:PRK10590 98 -YSKYLNIRslvvfggVSINPQMMKLR----GGVDVLVATPGRLlDLEHQNAVkLDQVEI--LVLDEADRMLDMGfiHDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 155 RPsyrqiapFIASLPQRPLVSAFTATATPEVKEDIVTLLHlrQPrihvtgfdrpnLYFEVRRGEDKKKYITGFI----KK 230
Cdd:PRK10590 171 RR-------VLAKLPAKRQNLLFSATFSDDIKALAEKLLH--NP-----------LEIEVARRNTASEQVTQHVhfvdKK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 231 HPEE-------SG-----IIYAATRKEVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGID 298
Cdd:PRK10590 231 RKREllsqmigKGnwqqvLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLD 310
|
330 340 350
....*....|....*....|....*....|....*...
gi 654668938 299 KSNVRYVIHYNMPKNIEAYYQEAGRAGRDGEPGSCILL 336
Cdd:PRK10590 311 IEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSL 348
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
529-593 |
2.48e-07 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 52.95 E-value: 2.48e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654668938 529 LRHLRKEIATREHVPPYVVFSDATLRDMCRVQPQSLDEMLTVKGIGEQKLRKYGQEFLECLQKNK 593
Cdd:COG0349 216 LAAWREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAEAL 280
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
234-338 |
3.60e-07 |
|
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: 49.96 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 234 ESGIIYAATRKEVDSLYEYLKK---KKFAVGRY--HAGMSDKARNQAQEDFLYD-NVQVIVATNAFGMGIDKSNVRYVIH 307
Cdd:cd18796 39 KSTLVFTNTRSQAERLAQRLRElcpDRVPPDFIalHHGSLSRELREEVEAALKRgDLKVVVATSSLELGIDIGDVDLVIQ 118
|
90 100 110
....*....|....*....|....*....|.
gi 654668938 308 YNMPKNIEAYYQEAGRAGRDGEPGSCILLFS 338
Cdd:cd18796 119 IGSPKSVARLLQRLGRSGHRPGAASKGRLVP 149
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
228-371 |
4.98e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 52.81 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 228 IKKHPEESGIIYAATRKEVDSLYEYLKKKKFAVGRY--------HAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDK 299
Cdd:COG1111 348 LGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskegDKGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDI 427
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654668938 300 SNVRYVIHY-NMPKNIEaYYQEAGRAGRDGEpGSCILLFSpQDVMTQKYLIdVSIENEERKAHNLGTLQKMVD 371
Cdd:COG1111 428 PEVDLVIFYePVPSEIR-SIQRKGRTGRKRE-GRVVVLIA-KGTRDEAYYW-SSRRKEKKMKSILKKLKKLLD 496
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
212-339 |
8.54e-07 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 48.88 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 212 FEVRRGEDKKKYITGFIKKHPEESGIIYAatrKEVDSLYEYLKKK---KFAVGRYHAGMSDKARNQAQEDFLYDNVQVIV 288
Cdd:cd18811 16 YEFVREEIAKGRQAYVIYPLIEESEKLDL---KAAVAMYEYLKERfrpELNVGLLHGRLKSDEKDAVMAEFREGEVDILV 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 654668938 289 ATNAFGMGIDKSNVRYVIHYNMPK-NIEAYYQEAGRAGRDGEPGSCILLFSP 339
Cdd:cd18811 93 STTVIEVGVDVPNATVMVIEDAERfGLSQLHQLRGRVGRGDHQSYCLLVYKD 144
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
21-149 |
1.70e-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: 48.80 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 21 DFRPAQRPVVESLLSGQDTVAI-MPTGAGKSICFQLpALV-----FPGITLVISPLISLMKDQVDSLLEQGVPAtYINSQ 94
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVsAPTSSGKTLIAEL-AILralatSGGKAVYIAPTRALVNQKEADLRERFGPL-GKNVG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 654668938 95 LSLDESQQRLAAIAAGRyklIYVA-PERLDTdYFRYIIEQ--QEISMVAVDEAHCLSQ 149
Cdd:cd17921 79 LLTGDPSVNKLLLAEAD---ILVAtPEKLDL-LLRNGGERliQDVRLVVVDEAHLIGD 132
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
199-344 |
2.12e-06 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 48.03 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 199 RIHVTGFDRPNLYFEVRRGEDKKKYITGFIKKHPEESGIIYAatrKEVDSLYEYLKKK--KFAVGRYHAGMSDKARNQAQ 276
Cdd:cd18792 3 RTYVIPHDDLDLVYEAIERELARGGQVYYVYPRIEESEKLDL---KSIEALAEELKELvpEARVALLHGKMTEDEKEAVM 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654668938 277 EDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPK-NIEAYYQEAGRAGRDGEPGSCILLFSPQDVMT 344
Cdd:cd18792 80 LEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRfGLSQLHQLRGRVGRGKHQSYCYLLYPDPKKLT 148
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
218-334 |
3.58e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 49.58 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 218 EDKKKYITGFIKKHPEESGIIYAATRKEVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGI 297
Cdd:PRK04837 240 EEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGL 319
|
90 100 110
....*....|....*....|....*....|....*..
gi 654668938 298 DKSNVRYVIHYNMPKNIEAYYQEAGRAGRDGEPGSCI 334
Cdd:PRK04837 320 HIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSI 356
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
22-180 |
7.03e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.51 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 22 FRPAQ----RPVVESLLSGQDTVAI-MPTGAGKSIC-FQLPALVFP----GITLVISPLISL---MKDQVDSLLEQGVPA 88
Cdd:pfam04851 4 LRPYQieaiENLLESIKNGQKRGLIvMATGSGKTLTaAKLIARLFKkgpiKKVLFLVPRKDLleqALEEFKKFLPNYVEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 89 TYINSQLSLDESQ----------QRLaaiaagrYKLIYVAPERLDTDYFRYIIeqqeismvaVDEAHclsqwgHDFRPSY 158
Cdd:pfam04851 84 GEIISGDKKDESVddnkivvttiQSL-------YKALELASLELLPDFFDVII---------IDEAH------RSGASSY 141
|
170 180
....*....|....*....|..
gi 654668938 159 RQIAPFIaslpQRPLVSAFTAT 180
Cdd:pfam04851 142 RNILEYF----KPAFLLGLTAT 159
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
228-336 |
2.60e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 47.18 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 228 IKKHPEESGIIYAATRKEVDSLYEYLKKKKFAVGRY--------HAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDK 299
Cdd:PRK13766 360 LGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFvgqaskdgDKGMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDI 439
|
90 100 110
....*....|....*....|....*....|....*...
gi 654668938 300 SNVRYVIHYN-MPKNIEAyYQEAGRAGRdGEPGSCILL 336
Cdd:PRK13766 440 PSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEGRVVVL 475
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
26-145 |
5.37e-05 |
|
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: 44.11 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 26 QRPVVESLLSGQDTVAIMPTGAGKSICFQLPALV----FPGIT-LVISPLISLMKDQVDSL---LEQG----VPATYINs 93
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEallrDPGSRaLYLYPTKALAQDQLRSLrelLEQLglgiRVATYDG- 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 654668938 94 qlslDESQQRLAAIAAGRYKLIYVAPERLDTDYFRYIIEQQEISM----VAVDEAH 145
Cdd:cd17923 84 ----DTPREERRAIIRNPPRILLTNPDMLHYALLPHHDRWARFLRnlryVVLDEAH 135
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
237-328 |
6.46e-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: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 237 IIYAATRKEVDSLYEYLKKKKFAVGRYHAGMSDKARNQAQEDF--LYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKN- 313
Cdd:cd18793 31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFneDPDIRVFLLSTKAGGVGLNLTAANRVILYDPWWNp 110
|
90
....*....|....*.
gi 654668938 314 -IEAyyQEAGRAGRDG 328
Cdd:cd18793 111 aVEE--QAIDRAHRIG 124
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
232-328 |
1.04e-04 |
|
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: 42.58 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 232 PEESGIIYAATRKEVDSLYEYLK---------KKKFAVGR------YHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMG 296
Cdd:cd18802 24 PDFRGIIFVERRATAVVLSRLLKehpstlafiRCGFLIGRgnssqrKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEG 103
|
90 100 110
....*....|....*....|....*....|..
gi 654668938 297 IDKSNVRYVIHYNMPKNIEAYYQEAGRAGRDG 328
Cdd:cd18802 104 IDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
22-180 |
1.09e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 42.68 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 22 FRPAQRPVVESLL---SGQDTVAIMPTGAGKSIC-FQLPALVFPGITLVISPLISLMKDQVDSLLEQGVPAT-YINSQLS 96
Cdd:cd17926 1 LRPYQEEALEAWLahkNNRRGILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSiGLIGGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 97 LDESQQRLAAIAagRYKLIYVAPERLdtdyfRYIIEQQeiSMVAVDEAHCLS--QWGHdfrpsyrqiapfIASLPQRPLV 174
Cdd:cd17926 81 KKDFDDANVVVA--TYQSLSNLAEEE-----KDLFDQF--GLLIVDEAHHLPakTFSE------------ILKELNAKYR 139
|
....*.
gi 654668938 175 SAFTAT 180
Cdd:cd17926 140 LGLTAT 145
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
244-337 |
1.20e-03 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 39.65 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 244 KEVDSLYEYLKKKKF---AVGRYHAGMSDKARNQAQEDFLYDNVQVIVATNAFGMGIDKSNVRYVIHYNMPKNIEAYYQE 320
Cdd:cd18801 48 NFLSKIRPGIRATRFigqASGKSSKGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQR 127
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90
....*....|....*..
gi 654668938 321 AGRAGRdGEPGSCILLF 337
Cdd:cd18801 128 MGRTGR-KRQGRVVVLL 143
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| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
10-56 |
1.73e-03 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 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: 350717 [Multi-domain] Cd Length: 205 Bit Score: 39.98 E-value: 1.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 654668938 10 RELLRKfyGYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLP 56
Cdd:cd17959 14 RAIKKK--GYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIP 58
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| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
18-198 |
2.86e-03 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 39.48 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 18 GYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPAL----------VFPGIT-LVISPLISLmKDQVDSLLEQ-- 84
Cdd:cd17960 9 GFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeillkrkanlKKGQVGaLIISPTREL-ATQIYEVLQSfl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654668938 85 GVPATYINSQLSL--DESQQRLAAIAAGRYKLIYVAPERLDtDYFRYIIEQQEISMVAV---DEAHCLSQWGhdFRPSYR 159
Cdd:cd17960 88 EHHLPKLKCQLLIggTNVEEDVKKFKRNGPNILVGTPGRLE-ELLSRKADKVKVKSLEVlvlDEADRLLDLG--FEADLN 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 654668938 160 QIapfIASLP-QR--PLvsaFTATATPEVKEDIVTllHLRQP 198
Cdd:cd17960 165 RI---LSKLPkQRrtGL---FSATQTDAVEELIKA--GLRNP 198
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| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
18-58 |
2.89e-03 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 39.11 E-value: 2.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 654668938 18 GYQDFRPAQRPVVESLLSGQDTVAIMPTGAGKSICFQLPAL 58
Cdd:cd17957 9 GYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPIL 49
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| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
34-69 |
5.63e-03 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350724 [Multi-domain] Cd Length: 197 Bit Score: 38.50 E-value: 5.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 654668938 34 LSGQDTVAIMPTGAGKSICFQLPALVF--------PG---ITLVISP 69
Cdd:cd17966 25 LSGRDMVGIAQTGSGKTLAFLLPAIVHinaqppleRGdgpIVLVLAP 71
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|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
28-60 |
9.17e-03 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 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: 350709 [Multi-domain] Cd Length: 206 Bit Score: 37.70 E-value: 9.17e-03
10 20 30
....*....|....*....|....*....|...
gi 654668938 28 PVVeslLSGQDTVAIMPTGAGKSICFQLPALVF 60
Cdd:cd17951 22 PTI---LSGRDMIGIAFTGSGKTLVFTLPLIMF 51
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