|
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 ... |
5-587 |
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: 762.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 5 AEKVLKEYYGFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLMLEGTAIIVSPLISLMKDQVDALENLGISA 84
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 85 TYINSSLSTTEQRERLISLQNGKYQFIYVAPERFDHPQFLAIIKHIKLSFLAFDEAHCISQWGHDFRPSYRSIVSTIGTL 164
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 165 SNLPfVMGLTATATKEVIQDIQTLLNIDDQTVVNTGFARKNLSFHVIKGQDKQSFLKKYIAEHNNESGIIYAPTRKQVDS 244
Cdd:TIGR01389 161 PQVP-RIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 245 LSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGRDG 324
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 325 EPSDCILLFSGQDIHLQKFLIEQSLMDEEKKVNEYKKLQSMINYCHTATCLQQFMLRYFQDDSLQDgCANCSNCQQSGEQ 404
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEP-CGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 405 TDKTREAQMILSCVKRMGERFGAGLTAKVLKGSKDKKIKQFGFESLSTYGLMAKETEKTITSFIHYLVAEGYLSTGDQRF 484
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 485 PTLQLTKEAEAILKGKQKIWMKQTNV-------QQQQQSDDYDTGLFEALRILRKKIADQQGVPPYILFSDVALKEMSIY 557
Cdd:TIGR01389 479 IGLQLTEAARKVLKNEVEVLLRPFKVvakektrVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEK 558
|
570 580 590
....*....|....*....|....*....|
gi 1887651538 558 FPKTKQDMLRIKGVGEKKYEQYGEAFMDEI 587
Cdd:TIGR01389 559 RPATLNALLKIKGVGQNKLDRYGEAFLEVI 588
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-474 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 754.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 1 MLEQAEKVLKEYYGFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLMLEGTAIIVSPLISLMKDQVDALENL 80
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 81 GISATYINSSLSTTEQRERLISLQNGKYQFIYVAPERFDHPQFLAIIKHIKLSFLAFDEAHCISQWGHDFRPSYRSIVST 160
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 161 IGTLSNLPfVMGLTATATKEVIQDIQTLLNIDDQTVVNTGFARKNLSFHVIKG--QDKQSFLKKYIAEHNNESGIIYAPT 238
Cdd:COG0514 161 RERLPNVP-VLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGGSGIVYCLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 239 RKQVDSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAG 318
Cdd:COG0514 240 RKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 319 RAGRDGEPSDCILLFSGQDIHLQKFLIEQSLMDEEKKVNEYKKLQSMINYCHTATCLQQFMLRYFqDDSLQDGCANCSNC 398
Cdd:COG0514 320 RAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYF-GEELAEPCGNCDNC 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887651538 399 QQSGEQTDKTREAQMILSCVKRMGERFGAGLTAKVLKGSKDKKIKQFGFESLSTYGLMAKETEKTITSFIHYLVAE 474
Cdd:COG0514 399 LGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
4-587 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 531.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 4 QAEKVLKEYYGFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLMLEGTAIIVSPLISLMKDQVDALENLGIS 83
Cdd:PRK11057 12 LAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 84 ATYINSSLSTTEQRERLISLQNGKYQFIYVAPERFDHPQFLAIIKHIKLSFLAFDEAHCISQWGHDFRPSYRSIVSTIGT 163
Cdd:PRK11057 92 AACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 164 LSNLPFvMGLTATATKEVIQDIQTLLNIDDQTVVNTGFARKNLSFHVIKGQDKQSFLKKYIAEHNNESGIIYAPTRKQVD 243
Cdd:PRK11057 172 FPTLPF-MALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 244 SLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGRD 323
Cdd:PRK11057 251 DTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 324 GEPSDCILLFSGQDIHLQKFLIEQSLMDEEKKVnEYKKLQSMINYCHTATCLQQFMLRYFqDDSLQDGCANCSNCQQSGE 403
Cdd:PRK11057 331 GLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDI-ERHKLNAMGAFAEAQTCRRLVLLNYF-GEGRQEPCGNCDICLDPPK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 404 QTDKTREAQMILSCVKRMGERFGAGLTAKVLKGSKDKKIKQFGFESLSTYGLMAKETEKTITSFIHYLVAEGYLSTGDQR 483
Cdd:PRK11057 409 QYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQ 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 484 FPTLQLTKEAEAILKGKQ-------KIWMKQTNVQQQQQSDDYDTGLFEALRILRKKIADQQGVPPYILFSDVALKEMSI 556
Cdd:PRK11057 489 HSALQLTEAARPVLRGEVslqlavpRIVALKPRAMQKSFGGNYDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAE 568
|
570 580 590
....*....|....*....|....*....|.
gi 1887651538 557 YFPKTKQDMLRIKGVGEKKYEQYGEAFMDEI 587
Cdd:PRK11057 569 QMPITASEMLSVNGVGQRKLERFGKPFMALI 599
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
7-454 |
2.33e-150 |
|
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: 444.98 E-value: 2.33e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 7 KVLKEYYGFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLMLEGTAIIVSPLISLMKDQVDALENLGISATY 86
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 87 INSSLSTTEQRERLISLQNGKYQFIYVAPERF--DHPQFLAIIKHIKLSFLAFDEAHCISQWGHDFRPSYRSIVSTIGTL 164
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsaSNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 165 SNLPfVMGLTATATKEVIQDIQTLLNIDDQTVVNTGFARKNLSFHVIKGQDKQSF-LKKYI-AEHNNESGIIYAPTRKQV 242
Cdd:TIGR00614 161 PNVP-VMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPKILEdLLRFIrKEFEGKSGIIYCPSRKKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 243 DSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGR 322
Cdd:TIGR00614 240 EQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 323 DGEPSDCILLFSGQDIHLQKFLIeqsLMDEEKKVNEYK-KLQSMINYC-HTATCLQQFMLRYFQDDSLQDG--------- 391
Cdd:TIGR00614 320 DGLPSECHLFYAPADMNRLRRLL---MEEPDGNFRTYKlKLYEMMEYClNSSTCRRLILLSYFGEKGFNKSfcimgtekc 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1887651538 392 CANCSNC--QQSGEQTDKTRE----AQMILSCVKRMGERFGAGLTAKVLKGSKDKKIKQFGFESLSTYG 454
Cdd:TIGR00614 397 CDNCCKRldYKTKDVTDKVYDfgpqAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYG 465
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
10-587 |
2.06e-99 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 331.09 E-value: 2.06e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 10 KEYYGFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLMLEGTAIIVSPLISLMKDQVDALENLGISATYINS 89
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 90 SLSTTEQRE--RLISLQNGKYQFIYVAPERFDHPQFLaiIKHIK-------LSFLAFDEAHCISQWGHDFRPSYRSIVST 160
Cdd:PLN03137 533 GMEWAEQLEilQELSSEYSKYKLLYVTPEKVAKSDSL--LRHLEnlnsrglLARFVIDEAHCVSQWGHDFRPDYQGLGIL 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 161 IGTLSNLPfVMGLTATATKEVIQDIQTLLNIDDQTVVNTGFARKNLSFHVIKGQDK-QSFLKKYIAE-HNNESGIIYAPT 238
Cdd:PLN03137 611 KQKFPNIP-VLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKcLEDIDKFIKEnHFDECGIIYCLS 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 239 RKQVDSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAG 318
Cdd:PLN03137 690 RMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECG 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 319 RAGRDGEPSDCILLFSGQDIHLQKFLIEQSLMDEEKKVNEYKKLQS--------------MINYCHT-ATCLQQFMLRYF 383
Cdd:PLN03137 770 RAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSPMAMGYNRMASsgriletntenllrMVSYCENeVDCRRFLQLVHF 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 384 QDDSLQDGCAN-CSNCQQSGEQTDK--TREAQMILSCVKRMGERFGAGLTAKVLKGSKDKKIKQFGFESLSTYGLMAKET 460
Cdd:PLN03137 850 GEKFDSTNCKKtCDNCSSSKSLIDKdvTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLS 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 461 EKTITSFIHYLVAEGYLSTGDQR------FPTLQLTKEAEA--ILKGKQKIWM---------KQTNVQQQQQSDDYDTG- 522
Cdd:PLN03137 930 KGEASRILHYLVTEDILAEDVKKsdlygsVSSLLKVNESKAykLFSGGQTIIMrfpssvkasKPSKFEATPAKGPLTSGk 1009
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 523 ---------------------LFEALRILRKKIADQ--QGVPPYILFSDVALKEMSIYFPKTKQDMLRIKGVGEKKYEQY 579
Cdd:PLN03137 1010 qstlpmatpaqppvdlnlsaiLYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKY 1089
|
....*...
gi 1887651538 580 GEAFMDEI 587
Cdd:PLN03137 1090 GDRLLETI 1097
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
6-201 |
2.61e-97 |
|
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: 298.29 E-value: 2.61e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 6 EKVLKEYYGFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLMLEGTAIIVSPLISLMKDQVDALENLGISAT 85
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 86 YINSSLSTTEQRERLISLQNGKYQFIYVAPERFDHPQFLAIIKHIK----LSFLAFDEAHCISQWGHDFRPSYRSIVSTI 161
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1887651538 162 GTLSNLPfVMGLTATATKEVIQDIQTLLNIDDQTVVNTGF 201
Cdd:cd17920 161 RALPGVP-ILALTATATPEVREDILKRLGLRNPVIFRASF 199
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
6-202 |
4.79e-76 |
|
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: 242.93 E-value: 4.79e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 6 EKVLKEYYGFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLMLE----GTAIIVSPLISLMKDQVDALENLg 81
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 82 ISATYINSSLSTTEQRERLISLQNGKYQFIYVAPERFDHPQFLAIIKHIK-LSFLAFDEAHCISQWGHDFRPSYRSIVST 160
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPpISLLVVDEAHCISEWSHNFRPDYLRLCRV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1887651538 161 IGTLSNLPFVMGLTATATKEVIQDIQTLLNIDDQTVVNTGFA 202
Cdd:cd18018 160 LRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
3-192 |
1.15e-57 |
|
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: 194.12 E-value: 1.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 3 EQAEKVLKEYYGFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLMLEGTAIIVSPLISLMKDQVDALENLGI 82
Cdd:cd18015 4 GKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 83 SATYINSSLSTTEQRERLISLQNGKYQF--IYVAPERFDHPQ-FLAIIKHI----KLSFLAFDEAHCISQWGHDFRPSYR 155
Cdd:cd18015 84 SATMLNASSSKEHVKWVHAALTDKNSELklLYVTPEKIAKSKrFMSKLEKAynagRLARIAIDEVHCCSQWGHDFRPDYK 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1887651538 156 SIVSTIGTLSNLPfVMGLTATATKEVIQDIQTLLNID 192
Cdd:cd18015 164 KLGILKRQFPNVP-ILGLTATATSKVLKDVQKILCIQ 199
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
9-201 |
8.22e-54 |
|
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: 183.44 E-value: 8.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 9 LKEYYGFDSFRPGQKEVISHIL-DKKNTLAIMPTGGGKSICYQIPGLMLEGTAIIVSPLISLMKDQVDALENLGISATYI 87
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 88 NSSlsttEQRERLISLQNGKYQFIYVAPERFDHPQFL--AIIKHIKLsfLAFDEAHCISQWGHDFRPSYRSIVSTIGTLS 165
Cdd:cd18017 84 GSA----QSQNVLDDIKMGKIRVIYVTPEFVSKGLELlqQLRNGITL--IAIDEAHCVSQWGHDFRSSYRHLGSIRNRLP 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1887651538 166 NLPfVMGLTATATKEVIQDIQTLLNIDDQTVVNTGF 201
Cdd:cd18017 158 NVP-IVALTATATPSVRDDIIKNLNLRNPQITCTSF 192
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
203-333 |
1.48e-50 |
|
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: 172.39 E-value: 1.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 203 RKNLSFHVIKGQDKQSFL---KKYIAEHNNESGIIYAPTRKQVDSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEE 279
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLdllKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1887651538 280 ATIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGRDGEPSDCILLF 333
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
7-197 |
6.64e-48 |
|
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: 167.65 E-value: 6.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 7 KVLKEYYGFDSFR-PGQKEVISHILDKK-NTLAIMPTGGGKSICYQIPGLMLEGTAIIVSPLISLMKDQVDALENLGISA 84
Cdd:cd18014 2 STLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 85 TYINSSLSTTEQRERLISLQNGKYQ--FIYVAPERFDHPQFLAIIKHI----KLSFLAFDEAHCISQWGHDFRPSYRSIV 158
Cdd:cd18014 82 DSLNSKLSAQERKRIIADLESEKPQtkFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLRLG 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1887651538 159 STIGTLSNLPFVmGLTATATKEVIQDIQTLLNIdDQTVV 197
Cdd:cd18014 162 ALRSRYGHVPWV-ALTATATPQVQEDIFAQLRL-KKPVA 198
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
7-201 |
5.87e-45 |
|
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: 159.61 E-value: 5.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 7 KVLKEYYGFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLMLEGTAIIVSPLISLMKDQVDALENLGISATY 86
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 87 INSSLSTTEQRE--RLISLQNGKYQFIYVAPERFDHP-QFLAIIKHIK----LSFLAFDEAHCISQWGHDFRPSYRSIVS 159
Cdd:cd18016 87 LTGDKTDAEATKiyLQLSKKDPIIKLLYVTPEKISASnRLISTLENLYerklLARFVIDEAHCVSQWGHDFRPDYKRLNM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1887651538 160 TIGTLSNLPfVMGLTATATKEVIQDIQTLLNIDDQTVVNTGF 201
Cdd:cd18016 167 LRQKFPSVP-MMALTATATPRVQKDILNQLKMLRPQVFTMSF 207
|
|
| DpdF |
NF041063 |
protein DpdF; |
8-354 |
2.31e-43 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 167.78 E-value: 2.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 8 VLKEYYGFDSFR-PGQKEVISHIL--DKKNTLAI-MPTGGGKSICYQIPGLML---EGTAIIVSPLISLMKDQVDALENL 80
Cdd:NF041063 130 FLAEALGFTHYRsPGQREAVRAALlaPPGSTLIVnLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQERRAREL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 81 GISATYINSSL------STTEQRERLIS-LQNGKYQFIYVAPER---------FDhpqfLAiiKHIKLSFLAFDEAHCIS 144
Cdd:NF041063 210 LRRAGPDLGGPlawhggLSAEERAAIRQrIRDGTQRILFTSPESltgslrpalFD----AA--EAGLLRYLVVDEAHLVD 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 145 QWGHDFRPSYRSIVSTIGTL-----SNLPFV-MGLTATATKEVIQDIQTLLNIDDQT-VVNTGFARKNLSFhvikgqdkq 217
Cdd:NF041063 284 QWGDGFRPEFQLLAGLRRSLlrlapSGRPFRtLLLSATLTESTLDTLETLFGPPGPFiVVSAVQLRPEPAY--------- 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 218 sflkkYIAEHNNESG----------------IIYAPTRKQVDSLSTLLKQKGYA-VASYHAGLSEQFRQQ--EQ---NRF 275
Cdd:NF041063 355 -----WVAKCDSEEErrervlealrhlprplILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERliEQwreNEL 429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1887651538 276 iqeeaTIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGRDGEPSDCILLFSGQDIHLQKFLIEQSLMDEEK 354
Cdd:NF041063 430 -----DIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKSLNRPKLISVEK 503
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
403-507 |
4.70e-37 |
|
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: 134.20 E-value: 4.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 403 EQTDKTREAQMILSCVKRMGERFGAGLTAKVLKGSKDKKIKQFGFESLSTYGLMAKETEKTITSFIHYLVAEGYLSTGDQ 482
Cdd:pfam09382 3 ETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDIE 82
|
90 100
....*....|....*....|....*
gi 1887651538 483 RFPTLQLTKEAEAILKGKQKIWMKQ 507
Cdd:pfam09382 83 FYSVLKLTPKAREVLKGEEKVMLRV 107
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
406-497 |
1.63e-33 |
|
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: 123.35 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 406 DKTREAQMILSCVKRMGERFGAGLTAKVLKGSKDKKIKQFGFESLSTYGLMAKETEKTITSFIHYLVAEGYLSTGDQRFP 485
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 1887651538 486 TLQLTKEAEAIL 497
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
19-181 |
6.96e-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: 115.80 E-value: 6.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 19 RPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPglMLE--------GTAIIVSPLISLMKDQVDALENLGISATYINSS 90
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLP--ALEaldkldngPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 91 L----STTEQRERLislqnGKYQFIYVAPERFDHpqFLAIIKHIK-LSFLAFDEAHCISQWGhdFRPSYRSIvstIGTLS 165
Cdd:pfam00270 79 LlggdSRKEQLEKL-----KGPDILVGTPGRLLD--LLQERKLLKnLKLLVLDEAHRLLDMG--FGPDLEEI---LRRLP 146
|
170
....*....|....*.
gi 1887651538 166 NLPFVMGLTATATKEV 181
Cdd:pfam00270 147 KKRQILLLSATLPRNL 162
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
215-324 |
2.45e-25 |
|
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: 100.75 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 215 DKQSFLKKYIAEHNNESGIIYAPTRKQVDsLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGID 294
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 1887651538 295 KSNVRYVIHYALPMNIESYYQEAGRAGRDG 324
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
11-209 |
1.29e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 101.80 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 11 EYYGFDSFRPGQKEVISHILD-KKNTLAIMPTGGGKSICYQIPGLML-----EGTAIIVSPLISLMKDQVDALENLGISA 84
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 85 TYINSSLSTTEQRERLIS-LQNGKYQFIYVAPERFDHPQFLAIIKHIKLSFLAFDEAHCISQWGhdFRPSYRSIVStigT 163
Cdd:smart00487 82 GLKVVGLYGGDSKREQLRkLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLK---L 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1887651538 164 LSNLPFVMGLTATATKEvIQDIQTLLNIDDQTVVNTGFARKNLSFH 209
Cdd:smart00487 157 LPKNVQLLLLSATPPEE-IENLLELFLNDPVFIDVGFTPLEPIEQF 201
|
|
| HTH_40 |
pfam14493 |
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of ... |
604-692 |
5.59e-24 |
|
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of helicase proteins.
Pssm-ID: 464189 Cd Length: 89 Bit Score: 96.42 E-value: 5.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 604 SHLVSYEFYQAGYTLEEIAQMREVKDQTIINHLYQCFQEGYQLEWNVFFSEAEEKDVLKAQAELPEPKLKALKEKLGEAY 683
Cdd:pfam14493 1 SAEITLELYKEGLSIEEIAEERGLKESTIEGHLAELIEAGEPVDIERLVSEEEQKEILDAIEKLGSESLKPIKEALPEEI 80
|
....*....
gi 1887651538 684 SYAMIRGVL 692
Cdd:pfam14493 81 SYFEIRLVL 89
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
14-349 |
5.98e-24 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 105.23 E-value: 5.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 14 GFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLM-LEGT------AIIVSP---LIslmkDQV-DALENLGI 82
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQrLDPSrprapqALILAPtreLA----LQVaEELRKLAK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 83 satyiNSSLSTT---------EQRERLislQNGkYQFIyVA-PER-FDHpqflaiI--KHIKLS---FLAFDEAhcisqw 146
Cdd:COG0513 97 -----YLGLRVAtvyggvsigRQIRAL---KRG-VDIV-VAtPGRlLDL------IerGALDLSgveTLVLDEA------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 147 ghD------FRPSYRSIvstigtLSNLP-------FvmglTATATKEVIQDIQTLLN------IDDQTVVNtgfARKNLS 207
Cdd:COG0513 155 --DrmldmgFIEDIERI------LKLLPkerqtllF----SATMPPEIRKLAKRYLKnpvrieVAPENATA---ETIEQR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 208 FHVIKGQDKQSFLKKYIAEHNNESGIIYAPTRKQVDSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATN 287
Cdd:COG0513 220 YYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATD 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1887651538 288 AFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGRDGEPSDCILLFSGQDIHLQKfLIEQSL 349
Cdd:COG0513 300 VAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLR-AIEKLI 360
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
243-324 |
3.35e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 93.82 E-value: 3.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 243 DSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGR 322
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1887651538 323 DG 324
Cdd:smart00490 81 AG 82
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
207-333 |
1.01e-21 |
|
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: 91.41 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 207 SFHVIKGQDKQSFLKKY-IAEHNNESGIIYAPTRKQVDSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVA 285
Cdd:cd18787 4 LYVVVEEEEKKLLLLLLlLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1887651538 286 TNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGRDGEPSDCILLF 333
Cdd:cd18787 84 TDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
520-587 |
2.68e-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: 87.98 E-value: 2.68e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887651538 520 DTGLFEALRILRKKIADQQGVPPYILFSDVALKEMSIYFPKTKQDMLRIKGVGEKKYEQYGEAFMDEI 587
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
336-398 |
5.65e-19 |
|
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: 81.18 E-value: 5.65e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887651538 336 QDIHLQKFLIEQSLMDEEKKVNEYKKLQSMINYC-HTATCLQQFMLRYFQDDSLQDGCANCSNC 398
Cdd:pfam16124 2 QDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCeNTTDCRRKQLLRYFGEEFDSEPCGNCDNC 65
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
517-587 |
1.99e-17 |
|
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: 77.34 E-value: 1.99e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887651538 517 DDYDTGLFEALRILRKKIADQQGVPPYILFSDVALKEMSIYFPKTKQDMLRIKGVGEKKYEQYGEAFMDEI 587
Cdd:smart00341 1 RERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVI 71
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
22-327 |
7.15e-17 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 84.89 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 22 QKEVISHILDKKNTLAIMPTGGGKSICYQIPGL--MLEG---TAIIVSPLISLMKDQVDALENLgISATYINSSLST--- 93
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLEDpgaTALYLYPTKALARDQLRRLREL-AEALGLGVRVATydg 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 94 -TEQRERlislqngkyQFIYvaperfDHPQFL---------AIIKHIK--------LSFLAFDEAHcisqwghdfrpSYR 155
Cdd:COG1205 140 dTPPEER---------RWIR------EHPDIVltnpdmlhyGLLPHHTrwarffrnLRYVVIDEAH-----------TYR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 156 SI----VSTI-----------GtlSNLPFVMgltATATkevIQD----IQTLLNIDDQTVVNTGFAR--KNLSF---HVI 211
Cdd:COG1205 194 GVfgshVANVlrrlrricrhyG--SDPQFIL---ASAT---IGNpaehAERLTGRPVTVVDEDGSPRgeRTFVLwnpPLV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 212 KGQDKQSFLK--KYIAEHNNESG---IIYAPTRKQVDSLSTLLKQK------GYAVASYHAGLSEQFRQQEQNRFIQEEA 280
Cdd:COG1205 266 DDGIRRSALAeaARLLADLVREGlrtLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGEL 345
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1887651538 281 TIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGRDGEPS 327
Cdd:COG1205 346 LGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS 392
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
19-358 |
1.62e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 80.07 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 19 RPGQKEVISHIL-----DKKNTLAIMPTGGGKSIcyqipgLMLE--------GTAIIVSPLISLMKDQVDALENL----- 80
Cdd:COG1061 82 RPYQQEALEALLaalerGGGRGLVVAPTGTGKTV------LALAlaaellrgKRVLVLVPRRELLEQWAEELRRFlgdpl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 81 -----------GISATYinSSLSTTEQRERLislqngkyqfiyvaPERFDHpqflaIIkhiklsflaFDEAHcisqwgHD 149
Cdd:COG1061 156 agggkkdsdapITVATY--QSLARRAHLDEL--------------GDRFGL-----VI---------IDEAH------HA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 150 FRPSYRSIVSTIgtlsNLPFVMGLTAT---------------------ATKEVIQD-----IQTLLNIDDQTVVNTGFAR 203
Cdd:COG1061 200 GAPSYRRILEAF----PAAYRLGLTATpfrsdgreillflfdgivyeySLKEAIEDgylapPEYYGIRVDLTDERAEYDA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 204 --KNLSFHVIKGQD-KQSFLKKYIAEH-NNESGIIYAPTRKQVDSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEE 279
Cdd:COG1061 276 lsERLREALAADAErKDKILRELLREHpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 280 ATIMVATNAFGMGIDKSNVRYVIHYAlpmNIES---YYQEAGRA--GRDGEPSDCILLFSGQDIHLQKFLIEQSLMDEEK 354
Cdd:COG1061 356 LRILVTVDVLNEGVDVPRLDVAILLR---PTGSpreFIQRLGRGlrPAPGKEDALVYDFVGNDVPVLEELAKDLRDLAGY 432
|
....
gi 1887651538 355 KVNE 358
Cdd:COG1061 433 RVEF 436
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
14-349 |
2.34e-13 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 73.02 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 14 GFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGL-------------MLEGTAIIVSP----LISLMKDQVDA 76
Cdd:PRK01297 106 GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIInqllqtpppkeryMGEPRALIIAPtrelVVQIAKDAAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 77 LENLGISATYINSSLSTTEQRERLislqNGKYQFIYVA-PERF-DHPQFLAIikHI-KLSFLAFDEAHCISQWGhdFRPS 153
Cdd:PRK01297 186 TKYTGLNVMTFVGGMDFDKQLKQL----EARFCDILVAtPGRLlDFNQRGEV--HLdMVEVMVLDEADRMLDMG--FIPQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 154 YRSIVSTIGTLSNLPFVMgLTATATKEViqdiqtlLNIDDQTVVN--------TGFARKNLSFHV--IKGQDKQSFLKKY 223
Cdd:PRK01297 258 VRQIIRQTPRKEERQTLL-FSATFTDDV-------MNLAKQWTTDpaiveiepENVASDTVEQHVyaVAGSDKYKLLYNL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 224 IAEHNNESGIIYAPTRKQVDSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIH 303
Cdd:PRK01297 330 VTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVIN 409
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1887651538 304 YALPMNIESYYQEAGRAGRDGEPSDCIlLFSGQDIHLQKFLIEQSL 349
Cdd:PRK01297 410 FTLPEDPDDYVHRIGRTGRAGASGVSI-SFAGEDDAFQLPEIEELL 454
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
233-332 |
4.88e-13 |
|
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: 66.90 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 233 IIYAPTRKQVDSLSTLLKQ-------KGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIHYA 305
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKArlveegpLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*..
gi 1887651538 306 LPMNIESYYQEAGRAGRDGEPSDCILL 332
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
33-176 |
1.25e-12 |
|
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: 65.89 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 33 KNTLAIMPTGGGKSICYQIPGLML----EGTAIIVSPLISLMKDQ---VDALENLGISATYINSSlSTTEQRERLIslqN 105
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGG-SSAEEREKNK---L 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887651538 106 GKYQFIYVAPERFD---HPQFLAIIKHIKLsfLAFDEAHCISQWGHDFRPSYRSIVSTIGTLSNlpfVMGLTAT 176
Cdd:cd00046 78 GDADIIIATPDMLLnllLREDRLFLKDLKL--IIVDEAHALLIDSRGALILDLAVRKAGLKNAQ---VILLSAT 146
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
131-324 |
2.74e-12 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 69.80 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 131 KLSFLAFDEAHCISQWGhdFRPSYRSIVSTI----GTLSnlpfvmgLTATATKEVIQDIQTLLNidDQTV-VNTGF---- 201
Cdd:PTZ00110 277 RVTYLVLDEADRMLDMG--FEPQIRKIVSQIrpdrQTLM-------WSATWPKEVQSLARDLCK--EEPVhVNVGSldlt 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 202 ARKNLS--FHVIKGQDKQSFLKKYIAEHNNESG--IIYAPTRKQVDSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQ 277
Cdd:PTZ00110 346 ACHNIKqeVFVVEEHEKRGKLKMLLQRIMRDGDkiLIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKT 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1887651538 278 EEATIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGRDG 324
Cdd:PTZ00110 426 GKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
14-331 |
4.87e-12 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 69.11 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 14 GFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGL-----MLEGTAIIV-SPLISLMKDQVDALENLGISATYI 87
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpELKAPQILVlAPTRELAVQVAEAMTDFSKHMRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 88 NSSLSTTEQRE--RLISLQNGKyQFIYVAPERF-DHPQfLAIIKHIKLSFLAFDEAHCIsqwghdFRPSYRSIVSTIgtL 164
Cdd:PRK11634 105 NVVALYGGQRYdvQLRALRQGP-QIVVGTPGRLlDHLK-RGTLDLSKLSGLVLDEADEM------LRMGFIEDVETI--M 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 165 SNLP--FVMGLTATATKEVIQDIQTLLNIDDQTV-----VNTgfaRKNLS--FHVIKGQDKQSFLKKYIAEHNNESGIIY 235
Cdd:PRK11634 175 AQIPegHQTALFSATMPEAIRRITRRFMKEPQEVriqssVTT---RPDISqsYWTVWGMRKNEALVRFLEAEDFDAAIIF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 236 APTRKQVDSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQ 315
Cdd:PRK11634 252 VRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVH 331
|
330
....*....|....*.
gi 1887651538 316 EAGRAGRDGEPSDCIL 331
Cdd:PRK11634 332 RIGRTGRAGRAGRALL 347
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
11-346 |
1.27e-11 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 67.51 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 11 EYYGFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLM------LEGT-------AIIVSP---LISLMKDQV 74
Cdd:PLN00206 137 ETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctirSGHPseqrnplAMVLTPtreLCVQVEDQA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 75 DAL-ENLGISATYINSSLSTTEQRERLislQNGkYQFIYVAPERFdhpqFLAIIKH----IKLSFLAFDEAHCISQWGhd 149
Cdd:PLN00206 217 KVLgKGLPFKTALVVGGDAMPQQLYRI---QQG-VELIVGTPGRL----IDLLSKHdielDNVSVLVLDEVDCMLERG-- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 150 FRPSYRSIVSTIGTlsnlPFVMGLTATATKEVIQDIQTLLNidDQTVVNTG------FARKNLSFHVIKGQDKQSFLKKY 223
Cdd:PLN00206 287 FRDQVMQIFQALSQ----PQVLLFSATVSPEVEKFASSLAK--DIILISIGnpnrpnKAVKQLAIWVETKQKKQKLFDIL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 224 IA-EHNNESGIIYAPTRKQVDSLS-TLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYV 301
Cdd:PLN00206 361 KSkQHFKPPAVVFVSSRLGADLLAnAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQV 440
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1887651538 302 IHYALPMNIESYYQEAGRAGRDGEPSDCILLFSGQDIHLQKFLIE 346
Cdd:PLN00206 441 IIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
233-338 |
2.60e-11 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 66.00 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 233 IIYAPTRKQVDSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIHYALPMNIES 312
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100
....*....|....*....|....*.
gi 1887651538 313 YYQEAGRAGRDGEPSDCILLFSGQDI 338
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDI 376
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
9-322 |
3.46e-11 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 66.07 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 9 LKEYY---GFDSFRPGQKEVI-SHILDKKNTLAIMPTGGGKS------ICYQipgLMLEGTAIIVSPLISL----MKDQV 74
Cdd:COG1204 11 VIEFLkerGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTliaelaILKA---LLNGGKALYIVPLRALasekYREFK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 75 DALENLGISaTYInSSLSTTEQRERLislqnGKYQfIYVA-PERFDhpqflAIIKHI-----KLSFLAFDEAHCIsqwGH 148
Cdd:COG1204 88 RDFEELGIK-VGV-STGDYDSDDEWL-----GRYD-ILVAtPEKLD-----SLLRNGpswlrDVDLVVVDEAHLI---DD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 149 DFR-PSYRSIVSTIGTLSNLPFVMGLTATATKevIQDI-----QTLLNIDDQTVV-NTGFARKNlsfhVIKGQDKQSFLK 221
Cdd:COG1204 152 ESRgPTLEVLLARLRRLNPEAQIVALSATIGN--AEEIaewldAELVKSDWRPVPlNEGVLYDG----VLRFDDGSRRSK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 222 KYI---AEH---NNESGIIYAPTRKQV----------------------------------------DSLSTLLKqKGya 255
Cdd:COG1204 226 DPTlalALDlleEGGQVLVFVSSRRDAeslakkladelkrrltpeereeleelaeellevseethtnEKLADCLE-KG-- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 256 VASYHAGLSeqfrqQEQnRFIQEEAT------IMVATNAFGMGIdksN--VRYVI------HYALPMNIESYYQEAGRAG 321
Cdd:COG1204 303 VAFHHAGLP-----SEL-RRLVEDAFreglikVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAG 373
|
.
gi 1887651538 322 R 322
Cdd:COG1204 374 R 374
|
|
| YpbB |
COG4955 |
Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown]; |
608-694 |
1.43e-10 |
|
Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown];
Pssm-ID: 443982 [Multi-domain] Cd Length: 346 Bit Score: 63.49 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 608 SYEFYQAGYTLEEIAQMREVKDQTIINHLYQCFQEGYQLEWNVFFSEAEEKDVLKAQAELPEPKLKALKEKLGEaYSYAM 687
Cdd:COG4955 255 TYQLLQQGLSLEEIAQIRRLKLSTIEDHLVEIAIKDPDFPIEPFVNKEDQQEIIQAIEKLGTWKLKEIKEQLPD-LSYFQ 333
|
....*..
gi 1887651538 688 IRGVLIK 694
Cdd:COG4955 334 IRLVLAK 340
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
41-330 |
1.99e-10 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 63.82 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 41 TGGGKSICYQI---------PGLM----LEGTAIIVSPL----ISLMKDQVDALENLGISATYINSSLSTTEQRERLisl 103
Cdd:PRK04537 55 TGTGKTLAFLVavmnrllsrPALAdrkpEDPRALILAPTrelaIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELL--- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 104 QNGkYQFIYVAPERF-DHPQFLAIIKHIKLSFLAFDEAHCISQWG--HDFRPSYRSIVSTiGTLSNLPFvmglTATATKE 180
Cdd:PRK04537 132 QQG-VDVIIATPGRLiDYVKQHKVVSLHACEICVLDEADRMFDLGfiKDIRFLLRRMPER-GTRQTLLF----SATLSHR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 181 VIQDIQTLLNIDDQTVVNT---GFARKNLSFHVIKGQDKQSFLKKYIAEHNNESGIIYAPTRKQVDSLSTLLKQKGYAVA 257
Cdd:PRK04537 206 VLELAYEHMNEPEKLVVETetiTAARVRQRIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVG 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887651538 258 SYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGRDGEPSDCI 330
Cdd:PRK04537 286 VLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAI 358
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
276-332 |
4.05e-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: 56.56 E-value: 4.05e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1887651538 276 IQEEATIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGRDG-EPSDCILL 332
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
18-176 |
4.15e-09 |
|
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: 55.77 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 18 FRPGQKEVISHILDKKNT---LAIMPTGGGKSIC-YQIPGLMLEGTAIIVSPLISLMKDQVDALENLGISAT-YINSSLS 92
Cdd:cd17926 1 LRPYQEEALEAWLAHKNNrrgILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSiGLIGGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 93 TTEQRERLISLqnGKYQ--FIYVAPERFDHPQFLAIIkhiklsflaFDEAHCISQwghdfrPSYRSIVstigTLSNLPFV 170
Cdd:cd17926 81 KKDFDDANVVV--ATYQslSNLAEEEKDLFDQFGLLI---------VDEAHHLPA------KTFSEIL----KELNAKYR 139
|
....*.
gi 1887651538 171 MGLTAT 176
Cdd:cd17926 140 LGLTAT 145
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
227-327 |
1.98e-08 |
|
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: 53.81 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 227 HNNESGIIYAPTRKQVDSLSTLLKQKGYA------VASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRY 300
Cdd:cd18796 36 ERHKSTLVFTNTRSQAERLAQRLRELCPDrvppdfIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDL 115
|
90 100
....*....|....*....|....*...
gi 1887651538 301 VIHYALPMNIESYYQEAGRAG-RDGEPS 327
Cdd:cd18796 116 VIQIGSPKSVARLLQRLGRSGhRPGAAS 143
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
17-176 |
7.63e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 52.29 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 17 SFRPGQKEVISHIL-----DKKNTLAIMPTGGGKSICY--QIPGLMLEGT---AIIVSPLISLMKDQVDALENLGISATY 86
Cdd:pfam04851 3 ELRPYQIEAIENLLesiknGQKRGLIVMATGSGKTLTAakLIARLFKKGPikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 87 INSSLStteQRERLISLQNGKYQFI---------YVAPERFDHPQFLAIIkhiklsflaFDEAHcisqwgHDFRPSYRSI 157
Cdd:pfam04851 83 IGEIIS---GDKKDESVDDNKIVVTtiqslykalELASLELLPDFFDVII---------IDEAH------RSGASSYRNI 144
|
170
....*....|....*....
gi 1887651538 158 VStigtLSNLPFVMGLTAT 176
Cdd:pfam04851 145 LE----YFKPAFLLGLTAT 159
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
216-340 |
7.82e-08 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 55.33 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 216 KQSFLKKYIAEHNNESGIIYAPTRKQVDSLSTLLKQKGYAvASYHAGLSEQF-RQQEQNRFIQEEATIMVATNAFGMGID 294
Cdd:PRK11192 232 KTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGIN-CCYLEGEMVQAkRNEAIKRLTDGRVNVLVATDVAARGID 310
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1887651538 295 KSNVRYVIHYALPMNIESYYQEAGRAGRDGEPSDCILLFSGQDIHL 340
Cdd:PRK11192 311 IDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLL 356
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
22-141 |
1.50e-07 |
|
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: 51.82 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 22 QKEVISHILDKKNTLAIMPTGGGKSICYQIPglMLE-------GTAIIVSPLISLMKDQVDALENLgISATYINSSLST- 93
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLP--ILEallrdpgSRALYLYPTKALAQDQLRSLREL-LEQLGLGIRVATy 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887651538 94 ---TEQRERlislqngkyQFIYVAPER--FDHPQFL--AIIKH--------IKLSFLAFDEAH 141
Cdd:cd17923 82 dgdTPREER---------RAIIRNPPRilLTNPDMLhyALLPHhdrwarflRNLRYVVLDEAH 135
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
209-322 |
4.92e-07 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 53.36 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 209 HVI--KGQDKQSFLKKYIA-EHNNESG-------IIYAPTRKQVDSLSTLLkqkGYAVASYHAGLSEQFRQQEQNRFIQE 278
Cdd:COG1202 397 HLTfaDGREKIRIINKLVKrEFDTKSSkgyrgqtIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQ 473
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1887651538 279 EATIMVATNAFGMGID--KSNvryVIHYALPMNIE-----SYYQEAGRAGR 322
Cdd:COG1202 474 ELAAVVTTAALAAGVDfpASQ---VIFDSLAMGIEwlsvqEFHQMLGRAGR 521
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
14-322 |
6.38e-07 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 52.50 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 14 GFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLMLEGT------------AIIVSPLISLMKdQVDalENLG 81
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITrqphakgrrpvrALILTPTRELAA-QIG--ENVR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 82 ISATYIN-SSL------STTEQRERLislqNGKYQFIYVAPERFDHPQFLAIIKHIKLSFLAFDEAHCISQWG--HDFRp 152
Cdd:PRK10590 97 DYSKYLNiRSLvvfggvSINPQMMKL----RGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGfiHDIR- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 153 syRSIVSTIGTLSNLPFvmglTATATKEVIQDIQTLLNIDDQTVV---NTGFARKNLSFHVIKGQDKQSFLKKYIAEHNN 229
Cdd:PRK10590 172 --RVLAKLPAKRQNLLF----SATFSDDIKALAEKLLHNPLEIEVarrNTASEQVTQHVHFVDKKRKRELLSQMIGKGNW 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 230 ESGIIYAPTRKQVDSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIHYALPMN 309
Cdd:PRK10590 246 QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNV 325
|
330
....*....|...
gi 1887651538 310 IESYYQEAGRAGR 322
Cdd:PRK10590 326 PEDYVHRIGRTGR 338
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
196-324 |
5.46e-06 |
|
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: 46.78 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 196 VVNTGFARKNLSFHVIKGQDKQSFLKkyIAEHNNESG-IIYAPTRKQVDSLSTLLKqkgyAVASYHAGLSEQFRQ--QE- 271
Cdd:cd18795 11 GFNGLGIKLRVDVMNKFDSDIIVLLK--IETVSEGKPvLVFCSSRKECEKTAKDLA----GIAFHHAGLTREDRElvEEl 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1887651538 272 -QNRFIQeeatIMVATNAFGMGID--------KSNVRYVIHYALPMNIESYYQEAGRAGRDG 324
Cdd:cd18795 85 fREGLIK----VLVATSTLAAGVNlpartviiKGTQRYDGKGYRELSPLEYLQMIGRAGRPG 142
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
219-332 |
1.18e-05 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 45.66 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 219 FLKKYIAEHNNESGIIYAPTRKQVDSLSTLLKQKGYAVASYHAG--------------LSEQFRQQEQ-NRFIQEEATIM 283
Cdd:cd18802 15 ILREYFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrsLMTQRKQKETlDKFRDGELNLL 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1887651538 284 VATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRAGRDGepSDCILL 332
Cdd:cd18802 95 IATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYILM 141
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
17-177 |
2.37e-05 |
|
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: 45.33 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 17 SFRPGQKEVISHILDK-KNTLAIMPTGGGKSICYQipgLML-------EGTAIIVSPLISLMKDQVDALENLgISATYIN 88
Cdd:cd17921 1 LLNPIQREALRALYLSgDSVLVSAPTSSGKTLIAE---LAIlralatsGGKAVYIAPTRALVNQKEADLRER-FGPLGKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 89 SSLSTTEQRERLISLqnGKYQFIYVAPERFD-----HPQFLaiIKHIKLsfLAFDEAHCISQwGHdfR-PSYRSIVSTIG 162
Cdd:cd17921 77 VGLLTGDPSVNKLLL--AEADILVATPEKLDlllrnGGERL--IQDVRL--VVVDEAHLIGD-GE--RgVVLELLLSRLL 147
|
170
....*....|....*.
gi 1887651538 163 TLS-NLPFVmGLTATA 177
Cdd:cd17921 148 RINkNARFV-GLSATL 162
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
238-324 |
4.16e-05 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 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: 350192 [Multi-domain] Cd Length: 135 Bit Score: 43.70 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 238 TRKQVDSLSTLL-KQKGYAVASYHAGLSEQFRQQEQNRFIQEE--ATIMVATNAFGMGIDkSNVRYVIHYAL-------- 306
Cdd:cd18805 26 SRKDIFSLKREIeKRTGLKCAVIYGALPPETRRQQARLFNDPEsgYDVLVASDAIGMGLN-LNIRRVIFSSLskfdgnem 104
|
90
....*....|....*....
gi 1887651538 307 -PMNIESYYQEAGRAGRDG 324
Cdd:cd18805 105 rPLSPSEVKQIAGRAGRFG 123
|
|
| RQC_minor_1 |
NF041107 |
RQC-minor-1 family DNA-binding protein; The DNA-binding RQC domain (PF09382) appears primarily ... |
426-491 |
5.88e-05 |
|
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: 44.10 E-value: 5.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1887651538 426 GAGLTAKVLKGSKDKKIKQFGFESLSTYGLMAKETEKTITSFIHYLVAEGYLSTG-DQRFPTLQLTK 491
Cdd:NF041107 22 GRTMLAKILKGSKDKKVLELGLDQCPAYGYYKSLTLEEITAKIDWMIKHDYLEIEyDGRLPLLVFTE 88
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
6-82 |
3.42e-04 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 42.20 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 6 EKVLKEY--YGFDSFRPGQKEVISH--ILDKKNTLAIMPTGGGKSICYQIpgLML------EGTAIIVSPLISLMKDQVD 75
Cdd:cd18026 3 DAVREAYakKGIKKLYDWQKECLSLpgLLEGRNLVYSLPTSGGKTLVAEI--LMLkrllerRKKALFVLPYVSIVQEKVD 80
|
....*..
gi 1887651538 76 ALENLGI 82
Cdd:cd18026 81 ALSPLFE 87
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
247-324 |
3.74e-04 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 43.77 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 247 TLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIdksNV--RYVIHYAL---------PMNIESYYQ 315
Cdd:COG4581 293 TLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGI---NMpaRTVVFTKLskfdgerhrPLTAREFHQ 369
|
....*....
gi 1887651538 316 EAGRAGRDG 324
Cdd:COG4581 370 IAGRAGRRG 378
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
17-176 |
5.23e-04 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 41.55 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 17 SFRPGQKEVI-SHILDKKNTLAIMPTGGGKSICYQ---IPGLMLEGTAIIVSPLISLMKDQVD---ALENLGISAtyins 89
Cdd:cd18028 1 ELYPPQAEAVrAGLLKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRALASEKYEefkKLEEIGLKV----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 90 SLSTTEQRERLISLqnGKYQFIYVAPERFDhpqflAIIKHIK-----LSFLAFDEAHCISQWGHDfrPSYRSIVSTIGTL 164
Cdd:cd18028 76 GISTGDYDEDDEWL--GDYDIIVATYEKFD-----SLLRHSPswlrdVGVVVVDEIHLISDEERG--PTLESIVARLRRL 146
|
170
....*....|..
gi 1887651538 165 SNLPFVMGLTAT 176
Cdd:cd18028 147 NPNTQIIGLSAT 158
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
3-143 |
6.76e-04 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 42.88 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 3 EQAEKVLKEYyGFDSFRPGQKEVI-SHILDKKNTLAIMPTGGGKSICYQIP---GLMLE-GTAIIVSPLISLMKDQVDAL 77
Cdd:PRK00254 10 ERIKRVLKER-GIEELYPPQAEALkSGVLEGKNLVLAIPTASGKTLVAEIVmvnKLLREgGKAVYLVPLKALAEEKYREF 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887651538 78 ---ENLGISATYINSSLSTTEqrERLislqnGKYQFIYVAPERFD----HPQflAIIKHIKLsfLAFDEAHCI 143
Cdd:PRK00254 89 kdwEKLGLRVAMTTGDYDSTD--EWL-----GKYDIIIATAEKFDsllrHGS--SWIKDVKL--VVADEIHLI 150
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
238-321 |
6.96e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 42.99 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 238 TRKQVDSLSTLLKQkgyavaSYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEA 317
Cdd:PRK09751 292 TSNRVQSSDVFIAR------SHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRI 365
|
....
gi 1887651538 318 GRAG 321
Cdd:PRK09751 366 GRAG 369
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
216-330 |
1.10e-03 |
|
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: 39.77 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 216 KQSFLKKYIAE--HNNESGIIYAPTRKQVDSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEAT--IMVATNAFGM 291
Cdd:cd18793 12 KLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGV 91
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1887651538 292 GIDKSNVRYVIHYAL---PMNIEsyyQEAGRAGRDGEPSDCI 330
Cdd:cd18793 92 GLNLTAANRVILYDPwwnPAVEE---QAIDRAHRIGQKKPVV 130
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
2-140 |
3.27e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 39.23 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 2 LEQAEKVLKEYYGFDSFRPgQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLML---EGTAIIVSPLISLMKDQVDALE 78
Cdd:cd17924 3 YEDFEEFFKKKTGFPPWGA-QRTWAKRLLRGKSFAIIAPTGVGKTTFGLATSLYLaskGKRSYLIFPTKSLVKQAYERLS 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1887651538 79 NLGISA------TYINSSLSTTEQRERLISLQNGKYQfIYVAPERFDHPQFlAIIKHIKLSFLAFDEA 140
Cdd:cd17924 82 KYAEKAgvevkiLVYHSRLKKKEKEELLEKIEKGDFD-ILVTTNQFLSKNF-DLLSNKKFDFVFVDDV 147
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
240-332 |
4.00e-03 |
|
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: 38.40 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 240 KQVDSLSTLLKQK--GYAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVR-YVIHYALPMNIESYYQE 316
Cdd:cd18792 45 KSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANtMIIEDADRFGLSQLHQL 124
|
90
....*....|....*.
gi 1887651538 317 AGRAGRDGEPSDCILL 332
Cdd:cd18792 125 RGRVGRGKHQSYCYLL 140
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
7-55 |
5.57e-03 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 38.58 E-value: 5.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1887651538 7 KVLKEYyGFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPGLM 55
Cdd:cd00268 3 KALKKL-GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILE 50
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
33-78 |
5.73e-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: 38.33 E-value: 5.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1887651538 33 KNTLAIMPTGGGK------SICYQIPGLMLEGTAII-VSPLISLMKDQVDALE 78
Cdd:cd17922 2 RNVLIAAPTGSGKteaaflPALSSLADEPEKGVQVLyISPLKALINDQERRLE 54
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
14-77 |
5.86e-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: 38.71 E-value: 5.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887651538 14 GFDSFRPGQKEVISHILDKKNTLAIMPTGGGKSICYQIPglMLEgtaIIVSPLISLMKDQVDAL 77
Cdd:cd17960 9 GFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIP--VLE---ILLKRKANLKKGQVGAL 67
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
243-354 |
6.11e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 39.82 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 243 DSLSTLLKQKGYAVASYHAGLSEQFRQQEQNRFIQEEAT--IMVATNAFGMGIDKSNVRYVIHYALPMNIESYYQEAGRA 320
Cdd:COG0553 563 DLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRA 642
|
90 100 110
....*....|....*....|....*....|....*.
gi 1887651538 321 GRdgepsdcIllfsGQ--DIHLQKFLIEQSLmdEEK 354
Cdd:COG0553 643 HR-------I----GQtrDVQVYKLVAEGTI--EEK 665
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
254-332 |
6.90e-03 |
|
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: 37.71 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887651538 254 YAVASYHAGLSEQFRQQEQNRFIQEEATIMVATNAFGMGIDKSNVR-YVIHYALPMNIESYYQEAGRAGRDGEPSDCILL 332
Cdd:cd18811 62 LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATvMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLV 141
|
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| |
