|
Name |
Accession |
Description |
Interval |
E-value |
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
5-588 |
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: 773.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 5 ARKVLQQVYGYPEFREGQKNIITNLLEGRDTLGIMPTGGGKSICYQVPAMLMEGVTLVISPLISLMKDQVDALHVLGVPA 84
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 85 TFINSTLEAKEVEQRMQGAMQGKYKLLYIAPERLESERFRARMSALNLPLVAIDEAHCVSQWGHDFRPSYVSIAPFIREL 164
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 165 PNRPIVAAFTATATAEVTaDIARLLDLDQAGIFVNGFSRDNLELTILRGENKRDYIQNYVKEHTHQPGIIYAATRKDVEE 244
Cdd:TIGR01389 161 PQVPRIALTATADAETRQ-DIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 245 LYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDG 324
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 325 EPSECILLFSAQDIMTQKFLIEQNQLSPDRKANEYKKLQTMIDFCYSPRCLRNVILHYFDETNIKDtCGNCSSCKDDRDT 404
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEP-CGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 405 VDITVEAQKIFSCIRRMGERFGISMVASVLKGSKAKKIVDYRFDRLPTHGIMRDLPEKEISDLINVLISEGFLQLSDGQY 484
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 485 PVVRLMQPAAEVLQGKLQV---------NQKVRKQQVKVAAIDNTLFEQLRLLRREIAAREKVPPYIIFSDSTLREMSEI 555
Cdd:TIGR01389 479 IGLQLTEAARKVLKNEVEVllrpfkvvaKEKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEK 558
|
570 580 590
....*....|....*....|....*....|...
gi 1844954634 556 CPTSESAMLRIKGVGEVKYRNYGKPFLDLLRTY 588
Cdd:TIGR01389 559 RPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-476 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 738.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 1 MLDGARKVLQQVYGYPEFREGQKNIITNLLEGRDTLGIMPTGGGKSICYQVPAMLMEGVTLVISPLISLMKDQVDALHVL 80
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 81 GVPATFINSTLEAKEVEQRMQGAMQGKYKLLYIAPERLESERFRARMSALNLPLVAIDEAHCVSQWGHDFRPSYVSIAPF 160
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 161 IRELPNRPI----------VaaftatataevTADIARLLDLDQAGIFVNGFSRDNLELTILRG--ENKRDYIQNYVKEHT 228
Cdd:COG0514 161 RERLPNVPVlaltatatprV-----------RADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 229 HQPGIIYAATRKDVEELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIHYNMPK 308
Cdd:COG0514 230 GGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 309 NMEAYYQEAGRAGRDGEPSECILLFSAQDIMTQKFLIEQNQLSPDRKANEYKKLQTMIDFCYSPRCLRNVILHYFDETnI 388
Cdd:COG0514 310 SIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEE-L 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 389 KDTCGNCSSCKDDRDTVDITVEAQKIFSCIRRMGERFGISMVASVLKGSKAKKIVDYRFDRLPTHGIMRDLPEKEISDLI 468
Cdd:COG0514 389 AEPCGNCDNCLGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVI 468
|
....*...
gi 1844954634 469 NVLISEGF 476
Cdd:COG0514 469 RQLLAQLF 476
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
5-586 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 569.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 5 ARKVLQQVYGYPEFREGQKNIITNLLEGRDTLGIMPTGGGKSICYQVPAMLMEGVTLVISPLISLMKDQVDALHVLGVPA 84
Cdd:PRK11057 13 AKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 85 TFINSTLEAKEVEQRMQGAMQGKYKLLYIAPERLESERFRARMSALNLPLVAIDEAHCVSQWGHDFRPSYVSIAPFIREL 164
Cdd:PRK11057 93 ACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 165 PNRPIVaAFTATATAEVTADIARLLDLDQAGIFVNGFSRDNLELTILRGENKRDYIQNYVKEHTHQPGIIYAATRKDVEE 244
Cdd:PRK11057 173 PTLPFM-ALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 245 LYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDG 324
Cdd:PRK11057 252 TAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 325 EPSECILLFSAQDIMTQKFLIEQNQLSPdRKANEYKKLQTMIDFCYSPRCLRNVILHYFDETNIKDtCGNCSSCKDDRDT 404
Cdd:PRK11057 332 LPAEAMLFYDPADMAWLRRCLEEKPAGQ-QQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEP-CGNCDICLDPPKQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 405 VDITVEAQKIFSCIRRMGERFGISMVASVLKGSKAKKIVDYRFDRLPTHGIMRDLPEKEISDLINVLISEGFLQLSDGQY 484
Cdd:PRK11057 410 YDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 485 PVVRLMQPAAEVLQGKLQVNQKV-RKQQVKVAA--------IDNTLFEQLRLLRREIAAREKVPPYIIFSDSTLREMSEI 555
Cdd:PRK11057 490 SALQLTEAARPVLRGEVSLQLAVpRIVALKPRAmqksfggnYDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQ 569
|
570 580 590
....*....|....*....|....*....|.
gi 1844954634 556 CPTSESAMLRIKGVGEVKYRNYGKPFLDLLR 586
Cdd:PRK11057 570 MPITASEMLSVNGVGQRKLERFGKPFMALIR 600
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
7-458 |
2.50e-154 |
|
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: 451.92 E-value: 2.50e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 7 KVLQQVYGYPEFREGQKNIITNLLEGRDTLGIMPTGGGKSICYQVPAMLMEGVTLVISPLISLMKDQVDALHVLGVPATF 86
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 87 INSTLEAKEVEQRMQGAMQGKYKLLYIAPERL-ESERFRARM-SALNLPLVAIDEAHCVSQWGHDFRPSYVSIAPFIREL 164
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsASNRLLQTLeERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 165 PNRPIVAAFTATATAEVTaDIARLLDLDQAGIFVNGFSRDNLELTILRGENK--RDYIQNYVKEHTHQPGIIYAATRKDV 242
Cdd:TIGR00614 161 PNVPVMALTATASPSVRE-DILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPKilEDLLRFIRKEFEGKSGIIYCPSRKKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 243 EELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGR 322
Cdd:TIGR00614 240 EQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 323 DGEPSECILLFSAQDIMTQKFLIEQnqlSPDRKANEYK-KLQTMIDFC-YSPRCLRNVILHYFDETNIKDT--------- 391
Cdd:TIGR00614 320 DGLPSECHLFYAPADMNRLRRLLME---EPDGNFRTYKlKLYEMMEYClNSSTCRRLILLSYFGEKGFNKSfcimgtekc 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844954634 392 CGNCSSCKDDR------DTVDITVEAQKIFSCIRRMGERFGISMVASVLKGSKAKKIVDYRFDRLPTHGIMRD 458
Cdd:TIGR00614 397 CDNCCKRLDYKtkdvtdKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKD 469
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
10-587 |
3.55e-110 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 357.28 E-value: 3.55e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 10 QQVYGYPEFREGQKNIITNLLEGRDTLGIMPTGGGKSICYQVPAMLMEGVTLVISPLISLMKDQVDALHVLGVPATFINS 89
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 90 TLEAKEVEQRMQ--GAMQGKYKLLYIAPERL-ESERFRARMSALN----LPLVAIDEAHCVSQWGHDFRPSYVSIAPFIR 162
Cdd:PLN03137 533 GMEWAEQLEILQelSSEYSKYKLLYVTPEKVaKSDSLLRHLENLNsrglLARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 163 ELPNRPiVAAFTATATAEVTADIARLLDLDQAGIFVNGFSRDNLELTILRGENK-RDYIQNYVKE-HTHQPGIIYAATRK 240
Cdd:PLN03137 613 KFPNIP-VLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKcLEDIDKFIKEnHFDECGIIYCLSRM 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 241 DVEELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRA 320
Cdd:PLN03137 692 DCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRA 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 321 GRDGEPSECILLFSAQDIMTQKFLIEQNQL--SP-----DRKANEYKKLQT-------MIDFCYSP-RCLRNV-ILHY-- 382
Cdd:PLN03137 772 GRDGQRSSCVLYYSYSDYIRVKHMISQGGVeqSPmamgyNRMASSGRILETntenllrMVSYCENEvDCRRFLqLVHFge 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 383 -FDETNIKDTCGNCSSCKDDRDTvDITVEAQKIFSCIRRMGERFGISMVASVLKGSKAKKIVDYRFDRLPTHGIMRDLPE 461
Cdd:PLN03137 852 kFDSTNCKKTCDNCSSSKSLIDK-DVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLSK 930
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 462 KEISDLINVLISEGFLQ--------------------------LSDGQYPVVRLMQPAAEVLQGKLQVN--------QKV 507
Cdd:PLN03137 931 GEASRILHYLVTEDILAedvkksdlygsvssllkvneskayklFSGGQTIIMRFPSSVKASKPSKFEATpakgpltsGKQ 1010
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 508 RKQQVKVAA-------IDNTLFEQLRLLRREIA--AREKVPPYIIFSDSTLREMSEICPTSESAMLRIKGVGEVKYRNYG 578
Cdd:PLN03137 1011 STLPMATPAqppvdlnLSAILYTALRKLRTALVkeAGDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKYG 1090
|
....*....
gi 1844954634 579 KPFLDLLRT 587
Cdd:PLN03137 1091 DRLLETIES 1099
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
6-202 |
3.84e-85 |
|
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: 264.01 E-value: 3.84e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 6 RKVLQQVYGYPEFREGQKNIITNLLEGRDTLGIMPTGGGKSICYQVPAMLMEGVTLVISPLISLMKDQVDALHVLGVPAT 85
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 86 FINSTLEAKEVEQRMQGAMQGKYKLLYIAPERLESERFRARMSALN----LPLVAIDEAHCVSQWGHDFRPSYVSIAPFI 161
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1844954634 162 RELPNRPI----------VaaftatataevTADIARLLDLDQAGIFVNGFS 202
Cdd:cd17920 161 RALPGVPIlaltatatpeV-----------REDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
7-201 |
5.35e-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: 214.04 E-value: 5.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 7 KVLQQVYGYPEFREGQKNIITNLLEGRDTLGIMPTGGGKSICYQVPAMLME----GVTLVISPLISLMKDQVDALHVLgV 82
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPRA-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 83 PATFINSTLEAKEVEQRMQGAMQGKYKLLYIAPERLESERFRARM-SALNLPLVAIDEAHCVSQWGHDFRPSYVSIAPFI 161
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLrQTPPISLLVVDEAHCISEWSHNFRPDYLRLCRVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1844954634 162 RELPNRPIVAAFTATATAEVTADIARLLDLDQAGIFVNGF 201
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPL 200
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
203-333 |
2.37e-59 |
|
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: 194.35 E-value: 2.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 203 RDNLELTILRGENKR---DYIQNYVKEHTHQPGIIYAATRKDVEELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDD 279
Cdd:cd18794 1 RPNLFYSVRPKDKKDeklDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1844954634 280 IRVMIATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEPSECILLF 333
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 ... |
5-170 |
1.40e-55 |
|
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: 187.19 E-value: 1.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 5 ARKVLQQVYGYPEFREGQKNIITNLLEGRDTLGIMPTGGGKSICYQVPAMLMEGVTLVISPLISLMKDQVDALHVLGVPA 84
Cdd:cd18015 6 VKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 85 TFINSTLEAKEVEQRMQGAMQGK--YKLLYIAPERL-ESERFrarMSALN-------LPLVAIDEAHCVSQWGHDFRPSY 154
Cdd:cd18015 86 TMLNASSSKEHVKWVHAALTDKNseLKLLYVTPEKIaKSKRF---MSKLEkaynagrLARIAIDEVHCCSQWGHDFRPDY 162
|
170
....*....|....*.
gi 1844954634 155 VSIAPFIRELPNRPIV 170
Cdd:cd18015 163 KKLGILKRQFPNVPIL 178
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
9-201 |
1.56e-46 |
|
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: 162.25 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 9 LQQVYGYPEFREGQKNIITNLLE-GRDTLGIMPTGGGKSICYQVPAMLMEGVTLVISPLISLMKDQVDALHVLGVPATFI 87
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLEeRRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 88 NSTLEAKEVeqrmQGAMQGKYKLLYIAPERLESERFRARMSALNLPLVAIDEAHCVSQWGHDFRPSYVSIAPFIRELPNR 167
Cdd:cd18017 84 GSAQSQNVL----DDIKMGKIRVIYVTPEFVSKGLELLQQLRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLPNV 159
|
170 180 190
....*....|....*....|....*....|....
gi 1844954634 168 PIVaAFTATATAEVTADIARLLDLDQAGIFVNGF 201
Cdd:cd18017 160 PIV-ALTATATPSVRDDIIKNLNLRNPQITCTSF 192
|
|
| DpdF |
NF041063 |
protein DpdF; |
8-338 |
6.20e-46 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 173.56 E-value: 6.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 8 VLQQVYGYPEFR-EGQKNIITNLL---EGrDTLGI-MPTGGGKSICYQVPAML---MEGVTLVISPLISLMKDQVDALHV 79
Cdd:NF041063 130 FLAEALGFTHYRsPGQREAVRAALlapPG-STLIVnLPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQERRARE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 80 L---------GVPATFINSTLEAKE-VEQRMqgaMQGKYKLLYIAPErleserfrARMSALNLPL-----------VAID 138
Cdd:NF041063 209 LlrragpdlgGPLAWHGGLSAEERAaIRQRI---RDGTQRILFTSPE--------SLTGSLRPALfdaaeagllryLVVD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 139 EAHCVSQWGHDFRPSYVSIAPFIREL-----PNRPIVAaftatataevtadiarLL---DLDQAGI------FVngfSRD 204
Cdd:NF041063 278 EAHLVDQWGDGFRPEFQLLAGLRRSLlrlapSGRPFRT----------------LLlsaTLTESTLdtletlFG---PPG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 205 NLEL---TILRGENkrDYIQNY-VKEHTHQ------------PGIIYAATRKDVEELYETLRKKGFA-AGKYHAGLTDEE 267
Cdd:NF041063 339 PFIVvsaVQLRPEP--AYWVAKcDSEEERRervlealrhlprPLILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAE 416
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844954634 268 RSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEPSECILLFSAQDI 338
Cdd:NF041063 417 RERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDL 487
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
7-170 |
4.07e-43 |
|
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: 153.44 E-value: 4.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 7 KVLQQVYGYPEFREGQKNIITNLLEGRDTLGIMPTGGGKSICYQVPAMLMEGVTLVISPLISLMKDQVDALHVLGVPATF 86
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 87 INSTLEAKEVEQ--RMQGAMQGKYKLLYIAPERL-ESERFRARMSALN----LPLVAIDEAHCVSQWGHDFRPSYVSIAP 159
Cdd:cd18016 87 LTGDKTDAEATKiyLQLSKKDPIIKLLYVTPEKIsASNRLISTLENLYerklLARFVIDEAHCVSQWGHDFRPDYKRLNM 166
|
170
....*....|.
gi 1844954634 160 FIRELPNRPIV 170
Cdd:cd18016 167 LRQKFPSVPMM 177
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
6-170 |
9.85e-43 |
|
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: 152.24 E-value: 9.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 6 RKVLQQVYGYPEFR-EGQKNIITNLLEGR-DTLGIMPTGGGKSICYQVPAMLMEGVTLVISPLISLMKDQVDALHVLGVP 83
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 84 ATFINSTLEAKEvEQRMQGAMQG---KYKLLYIAPERLESERFRARMSAL----NLPLVAIDEAHCVSQWGHDFRPSYVS 156
Cdd:cd18014 81 VDSLNSKLSAQE-RKRIIADLESekpQTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLR 159
|
170
....*....|....
gi 1844954634 157 IAPFIRELPNRPIV 170
Cdd:cd18014 160 LGALRSRYGHVPWV 173
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
402-508 |
8.88e-38 |
|
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: 135.36 E-value: 8.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 402 RDTVDITVEAQKIFSCIRRMGERFGISMVASVLKGSKAKKIVDYRFDRLPTHGIMRDLPEKEISDLINVLISEGFLQLSD 481
Cdd:pfam09382 2 PETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDI 81
|
90 100
....*....|....*....|....*..
gi 1844954634 482 GQYPVVRLMQPAAEVLQGKLQVNQKVR 508
Cdd:pfam09382 82 EFYSVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
406-497 |
3.04e-34 |
|
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: 124.90 E-value: 3.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 406 DITVEAQKIFSCIRRMGERFGISMVASVLKGSKAKKIVDYRFDRLPTHGIMRDLPEKEISDLINVLISEGFLQLSDGQYP 485
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 1844954634 486 VVRLMQPAAEVL 497
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
243-324 |
7.48e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 95.36 E-value: 7.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 243 EELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGR 322
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1844954634 323 DG 324
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
215-324 |
3.24e-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: 94.58 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 215 NKRDYIQNYVKEHTHQPGIIYAATRKDVEELYeTLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGID 294
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 1844954634 295 KSNVRYVIHYNMPKNMEAYYQEAGRAGRDG 324
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
518-585 |
7.29e-21 |
|
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: 86.44 E-value: 7.29e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844954634 518 DNTLFEQLRLLRREIAAREKVPPYIIFSDSTLREMSEICPTSESAMLRIKGVGEVKYRNYGKPFLDLL 585
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
19-170 |
8.34e-21 |
|
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: 89.61 E-value: 8.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 19 REGQKNIITNLLEGRDTLGIMPTGGGKSICYQVPAM------LMEGVTLVISPLISLMKDQVDALHVLGVPaTFINSTLE 92
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKG-LGLKVASL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844954634 93 AKEVEQRMQGAMQGKYKLLYIAPERLESErFRARMSALNLPLVAIDEAHCVSQWGhdFRPSYVSIapfIRELP-NRPIV 170
Cdd:pfam00270 80 LGGDSRKEQLEKLKGPDILVGTPGRLLDL-LQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEI---LRRLPkKRQIL 152
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
210-333 |
1.59e-20 |
|
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: 87.56 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 210 ILRGENKRDY-IQNYVKEHTHQPGIIYAATRKDVEELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNA 288
Cdd:cd18787 7 VVEEEEKKLLlLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDV 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1844954634 289 FGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEPSECILLF 333
Cdd:cd18787 87 AARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
336-399 |
2.23e-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: 2.23e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844954634 336 QDIMTQKFLIEQNQLSPDRKANEYKKLQTMIDFCYSP-RCLRNVILHYFDETNIKDTCGNCSSCK 399
Cdd:pfam16124 2 QDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCENTtDCRRKQLLRYFGEEFDSEPCGNCDNCL 66
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
517-589 |
7.26e-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: 81.19 E-value: 7.26e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844954634 517 IDNTLFEQLRLLRREIAAREKVPPYIIFSDSTLREMSEICPTSESAMLRIKGVGEVKYRNYGKPFLDLLRTYA 589
Cdd:smart00341 3 RQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEAS 75
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
212-337 |
6.08e-17 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 83.27 E-value: 6.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 212 RGENKRDYIQNYVKEHTHQPGIIYAATRKDVEELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGM 291
Cdd:COG0513 224 DKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1844954634 292 GIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEPSECILLFSAQD 337
Cdd:COG0513 304 GIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDE 349
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
13-170 |
1.77e-16 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 78.30 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 13 YGYPEFREGQKNIITNLLEG-RDTLGIMPTGGGKSICYQVPAML-----MEGVTLVISPLISLMKDQVDALHVLGVPATF 86
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 87 INSTLE-AKEVEQRMQGAMQGKYKLLYIAPERLESERFRARMSALNLPLVAIDEAHCVSQWGhdFRPSYVSIAPFIRelP 165
Cdd:smart00487 84 KVVGLYgGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLLP--K 159
|
....*
gi 1844954634 166 NRPIV 170
Cdd:smart00487 160 NVQLL 164
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
233-332 |
1.26e-14 |
|
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: 71.13 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 233 IIYAATRKDVEELY----ETLRKKGFAAGK---YHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIHYN 305
Cdd:cd18797 39 IVFCRSRKLAELLLrylkARLVEEGPLASKvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*..
gi 1844954634 306 MPKNMEAYYQEAGRAGRDGEPSECILL 332
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
233-342 |
1.06e-11 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 67.16 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 233 IIYAATRKDVEELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIHYNMPKNMEA 312
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100 110
....*....|....*....|....*....|
gi 1844954634 313 YYQEAGRAGRDGEPSECILLFSAQDIMTQK 342
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIEQLK 380
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
16-360 |
1.37e-11 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 67.36 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 16 PEFREGQKNIITNLL-----EGRDTLGIMPTGGGKSIcyqVPAMLME-----GVTLVISPLISLMKDQVDAL-HVLGVPa 84
Cdd:COG1061 79 FELRPYQQEALEALLaalerGGGRGLVVAPTGTGKTV---LALALAAellrgKRVLVLVPRRELLEQWAEELrRFLGDP- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 85 tfiNSTLEAKEVEQRMQGAMqgkYKLLYIapeRLESERFRARMSalnlpLVAIDEAHcvsqwgHDFRPSYVSIapfIREL 164
Cdd:COG1061 155 ---LAGGGKKDSDAPITVAT---YQSLAR---RAHLDELGDRFG-----LVIIDEAH------HAGAPSYRRI---LEAF 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 165 PNRPIV-------AAFTATATAEVTADIA---RLLDLDQAGIFV--------NGFSRDNLELTILR----------GENK 216
Cdd:COG1061 212 PAAYRLgltatpfRSDGREILLFLFDGIVyeySLKEAIEDGYLAppeyygirVDLTDERAEYDALSerlrealaadAERK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 217 RDYIQNYVKEHTHQ-PGIIYAATRKDVEELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDK 295
Cdd:COG1061 292 DKILRELLREHPDDrKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844954634 296 SNVRYVIhYNMP-KNMEAYYQEAGRAGRDGEPSECILLFsaqDIMTQKFLIEQNQLSPDRKANEYK 360
Cdd:COG1061 372 PRLDVAI-LLRPtGSPREFIQRLGRGLRPAPGKEDALVY---DFVGNDVPVLEELAKDLRDLAGYR 433
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
213-324 |
2.69e-11 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 66.09 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 213 GENKRDYIQNYVKEHTHQPGIIYAATRKDVEELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMG 292
Cdd:PRK01297 319 GSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRG 398
|
90 100 110
....*....|....*....|....*....|..
gi 1844954634 293 IDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDG 324
Cdd:PRK01297 399 IHIDGISHVINFTLPEDPDDYVHRIGRTGRAG 430
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
233-332 |
4.41e-10 |
|
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: 62.55 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 233 IIYAATRKDVEELYETLRK---KGFAAGK---YHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVI--HY 304
Cdd:COG1205 292 LVFTRSRRGAELLARYARRalrEPDLADRvaaYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVlaGY 371
|
90 100
....*....|....*....|....*...
gi 1844954634 305 nmPKNMEAYYQEAGRAGRDGEPSECILL 332
Cdd:COG1205 372 --PGTRASFWQQAGRAGRRGQDSLVVLV 397
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
233-324 |
5.73e-10 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 62.10 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 233 IIYAATRKDVEELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIHYNMPKNMEA 312
Cdd:PTZ00110 381 LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIED 460
|
90
....*....|..
gi 1844954634 313 YYQEAGRAGRDG 324
Cdd:PTZ00110 461 YVHRIGRTGRAG 472
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
225-337 |
9.17e-10 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 61.34 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 225 KEHTHQPGIIYAATRKDVEELYETLRK-KGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIH 303
Cdd:PLN00206 363 KQHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVII 442
|
90 100 110
....*....|....*....|....*....|....
gi 1844954634 304 YNMPKNMEAYYQEAGRAGRDGEPSECILLFSAQD 337
Cdd:PLN00206 443 FDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEED 476
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
212-332 |
1.08e-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: 57.18 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 212 RGENKRDYIQnYVKEHTHQPG---IIYAATRKDVEELYETLRkkGFAAgkYHAGLTDEERSYMQEAFLYDDIRVMIATNA 288
Cdd:cd18795 24 MNKFDSDIIV-LLKIETVSEGkpvLVFCSSRKECEKTAKDLA--GIAF--HHAGLTREDRELVEELFREGLIKVLVATST 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1844954634 289 FGMGID--------KSNVRYVIHYNMPKNMEAYYQEAGRAGRDG--EPSECILL 332
Cdd:cd18795 99 LAAGVNlpartviiKGTQRYDGKGYRELSPLEYLQMIGRAGRPGfdTRGEAIIM 152
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
276-332 |
1.58e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 54.63 E-value: 1.58e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844954634 276 LYDDIRVMIATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDG-EPSECILL 332
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
32-162 |
3.10e-08 |
|
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: 52.79 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 32 GRDTLGIMPTGGGKSICYQVPAMLM----EGVTLVISPLISLMKDQVDALHVL---GVPATFINSTLEAKEVEqrmqGAM 104
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEERE----KNK 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844954634 105 QGKYKLLYIAPERLE-SERFRARMSALNLPLVAIDEAHCVSQWGHDFRPSYVSIAPFIR 162
Cdd:cd00046 77 LGDADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGL 135
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
214-338 |
8.62e-08 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 54.95 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 214 ENKRDYIQNYVKEHTHQPGIIYAATRKDVEELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGI 293
Cdd:PRK11192 230 EHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGI 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1844954634 294 DKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEPSECILLFSAQDI 338
Cdd:PRK11192 310 DIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDH 354
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
211-334 |
1.14e-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: 51.50 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 211 LRGENKRDYIQNYVKEHT-HQPGIIYAATRKDVEELYETLRKK------GFAAGKYHAGLTDEERSYMQEAFLYDDIRVM 283
Cdd:cd18796 19 WAGESGADAYAEVIFLLErHKSTLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVV 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1844954634 284 IATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEPSECILLFS 334
Cdd:cd18796 99 VATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLVP 149
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
243-322 |
3.90e-06 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 49.89 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 243 EELYETLRKK-GFaagkYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIdksN--VRYVI----HYNMPKNMEA--Y 313
Cdd:COG1204 293 EKLADCLEKGvAF----HHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV---NlpARRVIirdtKRGGMVPIPVleF 365
|
....*....
gi 1844954634 314 YQEAGRAGR 322
Cdd:COG1204 366 KQMAGRAGR 374
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
216-332 |
7.58e-06 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 48.65 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 216 KRDYIQNYVKEHTHQPGIIYAATRKDVEELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDK 295
Cdd:PRK10590 232 KRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDI 311
|
90 100 110
....*....|....*....|....*....|....*..
gi 1844954634 296 SNVRYVIHYNMPKNMEAYYQEAGRAGRDGEPSECILL 332
Cdd:PRK10590 312 EELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSL 348
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
523-586 |
1.38e-05 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 47.56 E-value: 1.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 523 EQLRLLR-----REIAAREK-VPPYIIFSDSTLREMSEICPTSESAMLRIKGVGEVKYRNYGKPFLDLLR 586
Cdd:COG0349 208 RQLAVLRelaawREREARKRdVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVA 277
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
26-141 |
6.01e-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: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 26 ITNLLEGRDTLGIMPTGGGKSICYQVPAM--LME--GVT-LVISPLISLMKDQVDALHVLGVP-------ATFINST-LE 92
Cdd:cd17923 9 IEAARAGRSVVVTTGTASGKSLCYQLPILeaLLRdpGSRaLYLYPTKALAQDQLRSLRELLEQlglgirvATYDGDTpRE 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1844954634 93 AKEVEQRmqgamqGKYKLLYIAPERLE------SERFRARMSalNLPLVAIDEAH 141
Cdd:cd17923 89 ERRAIIR------NPPRILLTNPDMLHyallphHDRWARFLR--NLRYVVLDEAH 135
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
14-331 |
6.55e-05 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 45.99 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 14 GYPEFREGQKNIITNLLEGRDTLGIMPTGGGKSICYQVP------AMLMEGVTLVISPLISLMKDQVDAL-----HVLGV 82
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPllhnldPELKAPQILVLAPTRELAVQVAEAMtdfskHMRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 83 PATFINSTlEAKEVEQRmqgAMQGKYKLLYIAPERLESERFRARMSALNLPLVAIDEAHCVSQWGhdfrpsyvsiapFIR 162
Cdd:PRK11634 105 NVVALYGG-QRYDVQLR---ALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG------------FIE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 163 ELPNRpivaaftatataevtadIARLLDLDQAGIF-----------VNGFSRDNLELTI----------------LRGEN 215
Cdd:PRK11634 169 DVETI-----------------MAQIPEGHQTALFsatmpeairriTRRFMKEPQEVRIqssvttrpdisqsywtVWGMR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 216 KRDYIQNYVKEHTHQPGIIYAATRKDVEELYETLRKKGFAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDK 295
Cdd:PRK11634 232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311
|
330 340 350
....*....|....*....|....*....|....*.
gi 1844954634 296 SNVRYVIHYNMPKNMEAYYQEAGRAGRDGEPSECIL 331
Cdd:PRK11634 312 ERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALL 347
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
254-321 |
3.39e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 43.76 E-value: 3.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844954634 254 FAAGKYHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAG 321
Cdd:PRK09751 302 FIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
233-332 |
4.63e-04 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 43.18 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 233 IIYAATRKDVEELYETLRKKGFAAGKY--------HAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGIDKSNVRYVIHY 304
Cdd:COG1111 357 IVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskegDKGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFY 436
|
90 100
....*....|....*....|....*....
gi 1844954634 305 -NMPKNMEaYYQEAGRAGRDGEPSECILL 332
Cdd:COG1111 437 ePVPSEIR-SIQRKGRTGRKREGRVVVLI 464
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
208-322 |
5.69e-04 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 42.96 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 208 LTILRGENKRDYIQNYVKE---HTHQPG-----IIYAATRKDVEELYETLrkkGFAAGKYHAGLTDEERSYMQEAFLYDD 279
Cdd:COG1202 398 LTFADGREKIRIINKLVKRefdTKSSKGyrgqtIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQE 474
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844954634 280 IRVMIATNAFG----------------MGIDKSNVRyvihynmpknmeAYYQEAGRAGR 322
Cdd:COG1202 475 LAAVVTTAALAagvdfpasqvifdslaMGIEWLSVQ------------EFHQMLGRAGR 521
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
273-332 |
8.91e-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: 39.88 E-value: 8.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 273 EAFLYDDIRVMIATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGepSECILL 332
Cdd:cd18802 84 DKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYILM 141
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
259-324 |
1.24e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 41.79 E-value: 1.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844954634 259 YHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMGID--------KSNVRYVIHYNMP-KNMEAyYQEAGRAGRDG 324
Cdd:PRK01172 291 HHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNlparlvivRDITRYGNGGIRYlSNMEI-KQMIGRAGRPG 364
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
32-141 |
2.41e-03 |
|
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: 39.10 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844954634 32 GRDTLGIMPTGGGK------SICYQVPAMLMEGV-TLVISPLISLMKDQVDAL------HVLGVPATFINSTLEAKEvEQ 98
Cdd:cd17922 1 GRNVLIAAPTGSGKteaaflPALSSLADEPEKGVqVLYISPLKALINDQERRLeepldeIDLEIPVAVRHGDTSQSE-KA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1844954634 99 RMQGAMQGkykLLYIAPERLE----SERFRARMSalNLPLVAIDEAH 141
Cdd:cd17922 80 KQLKNPPG---ILITTPESLElllvNKKLRELFA--GLRYVVVDEIH 121
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
259-324 |
3.17e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 40.71 E-value: 3.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844954634 259 YHAGLTDEERSYMQEAFLYDDIRVMIATNAFGMG--------IDKSNVRYVIHYNM-PKNMEAYYQEAGRAGRDG 324
Cdd:PRK02362 309 HHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGlnlparrvIIRDYRRYDGGAGMqPIPVLEYHQMAGRAGRPG 383
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
14-54 |
5.56e-03 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 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: 350700 [Multi-domain] Cd Length: 198 Bit Score: 38.50 E-value: 5.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1844954634 14 GYPEFREGQKNIITNLLEGRDTLGIMPTGGGKSICYQVPAM 54
Cdd:cd17942 9 GFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI 49
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