|
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 ... |
6-586 |
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: 773.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 6 INEILKKYYGYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIPAMYFGGVTIVISPLISLMKDQVDTLNSLGIKS 85
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 86 AYINSSLSNEELNTIIHRASMGDYKLIYVAPERLESHLFRNILMILPVDQIAIDEAHCVSQWGHDFRASYRMISSLIEDL 165
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 166 NPRPVIsAFTATATELVKDDIVRLLELQEPNIYVSGFNRDNLSFKVVKSRDRKSYIVDYLKSNIESSGIIYAATRKDVER 245
Cdd:TIGR01389 161 PQVPRI-ALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 246 LYIFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFVIHYNIPRNIESYYQEAGRAGRDG 325
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 326 EEGECILLYDSRDINTQQYLINTSIANSDRAAIEYDKLQSIDNYCHTNKCLRKYILEYFGEDiTWDNCHNCSNCTQDYEL 405
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGEN-EVEPCGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 406 KDITVESQKIISCVYRMKESYGVGLIAEVLRGSKNQKILALAMDKLSTYGIIKNYTIGEIKEIINYLISEKYLALTKDMF 485
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 486 SIVKLTNKAVQFIKESETIYMR---IEATSKNTKG-------ESGLFNELKALRKVIAENEKIPPYIIFSDATLKELSAK 555
Cdd:TIGR01389 479 IGLQLTEAARKVLKNEVEVLLRpfkVVAKEKTRVQknlsvgvDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEK 558
|
570 580 590
....*....|....*....|....*....|.
gi 1119951532 556 KPINKEDMLLIKGIGEVKFERYGEDFMEVIK 586
Cdd:TIGR01389 559 RPATLNALLKIKGVGQNKLDRYGEAFLEVIR 589
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
5-475 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 740.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 5 SINEILKKYYGYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIPAMYFGGVTIVISPLISLMKDQVDTLNSLGIK 84
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 85 SAYINSSLSNEELNTIIHRASMGDYKLIYVAPERLESHLFRNILMILPVDQIAIDEAHCVSQWGHDFRASYRMISSLIED 164
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 165 LNPRPVIsAFTATATELVKDDIVRLLELQEPNIYVSGFNRDNLSFKVVK--SRDRKSYIVDYLKSNIESSGIIYAATRKD 242
Cdd:COG0514 164 LPNVPVL-ALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPkpPDDKLAQLLDFLKEHPGGSGIVYCLSRKK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 243 VERLYIFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFVIHYNIPRNIESYYQEAGRAG 322
Cdd:COG0514 243 VEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 323 RDGEEGECILLYDSRDINTQQYLINTSIANSDRAAIEYDKLQSIDNYCHTNKCLRKYILEYFGEDiTWDNCHNCSNCTQD 402
Cdd:COG0514 323 RDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEE-LAEPCGNCDNCLGP 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119951532 403 YELKDITVESQKIISCVYRMKESYGVGLIAEVLRGSKNQKILALAMDKLSTYGIIKNYTIGEIKEIINYLISE 475
Cdd:COG0514 402 PETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
8-586 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 548.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 8 EILKKYYGYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIPAMYFGGVTIVISPLISLMKDQVDTLNSLGIKSAY 87
Cdd:PRK11057 15 QVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAAC 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 88 INSSLSNEELNTIIHRASMGDYKLIYVAPERLESHLFRNILMILPVDQIAIDEAHCVSQWGHDFRASYRMISSLIEDLNP 167
Cdd:PRK11057 95 LNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRFPT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 168 RPVIsAFTATATELVKDDIVRLLELQEPNIYVSGFNRDNLSFKVVKSRDRKSYIVDYLKSNIESSGIIYAATRKDVERLY 247
Cdd:PRK11057 175 LPFM-ALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 248 IFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFVIHYNIPRNIESYYQEAGRAGRDGEE 327
Cdd:PRK11057 254 ARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 328 GECILLYDSRDINTQQYLINTSIAnSDRAAIEYDKLQSIDNYCHTNKCLRKYILEYFGEDiTWDNCHNCSNCTQDYELKD 407
Cdd:PRK11057 334 AEAMLFYDPADMAWLRRCLEEKPA-GQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEG-RQEPCGNCDICLDPPKQYD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 408 ITVESQKIISCVYRMKESYGVGLIAEVLRGSKNQKILALAMDKLSTYGIIKNYTIGEIKEIINYLISEKYLALTKDMFSI 487
Cdd:PRK11057 412 GLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQHSA 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 488 VKLTNKAVQFIKESETIYM---RIEA--TSKNTKGESG-----LFNELKALRKVIAENEKIPPYIIFSDATLKELSAKKP 557
Cdd:PRK11057 492 LQLTEAARPVLRGEVSLQLavpRIVAlkPRAMQKSFGGnydrkLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQMP 571
|
570 580
....*....|....*....|....*....
gi 1119951532 558 INKEDMLLIKGIGEVKFERYGEDFMEVIK 586
Cdd:PRK11057 572 ITASEMLSVNGVGQRKLERFGKPFMALIR 600
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
9-456 |
3.47e-155 |
|
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: 453.46 E-value: 3.47e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 9 ILKKYYGYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIPAMYFGGVTIVISPLISLMKDQVDTLNSLGIKSAYI 88
Cdd:TIGR00614 2 ILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 89 NSSLSNEELNTIIHRASMGDYKLIYVAPE------RLESHLFRNILMILpvdqIAIDEAHCVSQWGHDFRASYRMISSLI 162
Cdd:TIGR00614 82 NSAQTKEQQLNVLTDLKDGKIKLLYVTPEkisasnRLLQTLEERKGITL----IAVDEAHCISQWGHDFRPDYKALGSLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 163 EDLNPRPVIsAFTATATELVKDDIVRLLELQEPNIYVSGFNRDNLSFKVvksRDRKSYIVDYLKSNIES-----SGIIYA 237
Cdd:TIGR00614 158 QKFPNVPVM-ALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEV---RRKTPKILEDLLRFIRKefegkSGIIYC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 238 ATRKDVERLYIFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFVIHYNIPRNIESYYQE 317
Cdd:TIGR00614 234 PSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 318 AGRAGRDGEEGECILLYDSRDINTQQYLInTSIANSDRAAIEYDKLQSIDNYCHTNKCLRKYILEYFGE----------- 386
Cdd:TIGR00614 314 SGRAGRDGLPSECHLFYAPADMNRLRRLL-MEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEkgfnksfcimg 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119951532 387 -DITWDNCHNCSN-CTQDYE--LKDITVESQKIISCVYRMKESYGVGLIAEVLRGSKNQKILALAMDKLSTYGI 456
Cdd:TIGR00614 393 tEKCCDNCCKRLDyKTKDVTdkVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGR 466
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
11-585 |
7.80e-111 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 358.44 E-value: 7.80e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 11 KKYYGYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIPAMYFGGVTIVISPLISLMKDQVDTLNSLGIKSAYINS 90
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 91 SLSNEELNTIIHRAS--MGDYKLIYVAPERLESH--LFRNiLMILP----VDQIAIDEAHCVSQWGHDFRASYRMISSLI 162
Cdd:PLN03137 533 GMEWAEQLEILQELSseYSKYKLLYVTPEKVAKSdsLLRH-LENLNsrglLARFVIDEAHCVSQWGHDFRPDYQGLGILK 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 163 EDLNPRPVIsAFTATATELVKDDIVRLLELQEPNIYVSGFNRDNLSFKVV-KSRDRKSYIVDYLKSN-IESSGIIYAATR 240
Cdd:PLN03137 612 QKFPNIPVL-ALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVpKTKKCLEDIDKFIKENhFDECGIIYCLSR 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 241 KDVERLYIFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFVIHYNIPRNIESYYQEAGR 320
Cdd:PLN03137 691 MDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGR 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 321 AGRDGEEGECILLYDSRDINTQQYLINTSIANSDRAAIEYDKLQSIDNYCHTN---------------KCLRKYILEYFG 385
Cdd:PLN03137 771 AGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSPMAMGYNRMASSGRILETNtenllrmvsycenevDCRRFLQLVHFG 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 386 EDITWDNCHN-CSNCTQDYEL--KDITVESQKIISCVYRMKESYGVGLIAEVLRGSKNQKILALAMDKLSTYGIIKNYTI 462
Cdd:PLN03137 851 EKFDSTNCKKtCDNCSSSKSLidKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLSK 930
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 463 GEIKEIINYLISEKYLA---LTKDMF----SIVKLTN-KAVQFIKESETIYMRIEATSKNTK-GESG------------- 520
Cdd:PLN03137 931 GEASRILHYLVTEDILAedvKKSDLYgsvsSLLKVNEsKAYKLFSGGQTIIMRFPSSVKASKpSKFEatpakgpltsgkq 1010
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 521 --------------------LFNELKALRKVIAEN--EKIPPYIIFSDATLKELSAKKPINKEDMLLIKGIGEVKFERYG 578
Cdd:PLN03137 1011 stlpmatpaqppvdlnlsaiLYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKYG 1090
|
....*..
gi 1119951532 579 EDFMEVI 585
Cdd:PLN03137 1091 DRLLETI 1097
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
8-203 |
9.87e-102 |
|
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: 306.38 E-value: 9.87e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 8 EILKKYYGYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIPAMYFGGVTIVISPLISLMKDQVDTLNSLGIKSAY 87
Cdd:cd17920 2 QILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 88 INSSLSNEELNTIIHRASMGDYKLIYVAPERLESHLFRNIL----MILPVDQIAIDEAHCVSQWGHDFRASYRMISSLIE 163
Cdd:cd17920 82 LNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLqrlpERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLRR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1119951532 164 DLnPRPVISAFTATATELVKDDIVRLLELQEPNIYVSGFN 203
Cdd:cd17920 162 AL-PGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
7-197 |
9.59e-72 |
|
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: 229.06 E-value: 9.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 7 NEILKKYYGYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIPAMYF----GGVTIVISPLISLMKDQVDTLNSLg 82
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLrrrgPGLTLVVSPLIALMKDQVDALPRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 83 IKSAYINSSLSNEELNTIIHRASMGDYKLIYVAPERLESHLFRNIL-MILPVDQIAIDEAHCVSQWGHDFRASYRMISSL 161
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLrQTPPISLLVVDEAHCISEWSHNFRPDYLRLCRV 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1119951532 162 IEDLNPRPVISAFTATATELVKDDIVRLLELQEPNI 197
Cdd:cd18018 160 LRELLGAPPVLALTATATKRVVEDIASHLGIPESGV 195
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
6-203 |
3.47e-61 |
|
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: 201.44 E-value: 3.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 6 INEILKKYYGYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIPAMYFGGVTIVISPLISLMKDQVDTLNSLGIKS 85
Cdd:cd18015 6 VKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 86 AYINSSLSNEELNTIIhrASMGD----YKLIYVAPERL-ESHLFRNIL----MILPVDQIAIDEAHCVSQWGHDFRASYR 156
Cdd:cd18015 86 TMLNASSSKEHVKWVH--AALTDknseLKLLYVTPEKIaKSKRFMSKLekayNAGRLARIAIDEVHCCSQWGHDFRPDYK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1119951532 157 MISSLiEDLNPRPVISAFTATATELVKDDIVRLLELQEPNIYVSGFN 203
Cdd:cd18015 164 KLGIL-KRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
10-203 |
3.68e-58 |
|
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: 193.07 E-value: 3.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 10 LKKYYGYDDFREGQREIIESIISHR-DTFGIMPTGGGKSICYQIPAMYFGGVTIVISPLISLMKDQVDTLNSLGIKSAYI 88
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLEERrDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 89 NSSLSNEELNTIihraSMGDYKLIYVAPERLEshlfRNILMILPVDQ----IAIDEAHCVSQWGHDFRASYRMISSlIED 164
Cdd:cd18017 84 GSAQSQNVLDDI----KMGKIRVIYVTPEFVS----KGLELLQQLRNgitlIAIDEAHCVSQWGHDFRSSYRHLGS-IRN 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1119951532 165 LNPRPVISAFTATATELVKDDIVRLLELQEPNIYVSGFN 203
Cdd:cd18017 155 RLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
8-203 |
6.03e-54 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 182.33 E-value: 6.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 8 EILKKYYGYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIPAMYFGGVTIVISPLISLMKDQVDTLNSLGIKSAY 87
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 88 INSSLSNEELNTIIHRASMGD--YKLIYVAPE------RLESHLF----RNILMilpvdQIAIDEAHCVSQWGHDFRASY 155
Cdd:cd18016 87 LTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEkisasnRLISTLEnlyeRKLLA-----RFVIDEAHCVSQWGHDFRPDY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1119951532 156 RMISSLIEDLNPRPVIsAFTATATELVKDDIVRLLELQEPNIYVSGFN 203
Cdd:cd18016 162 KRLNMLRQKFPSVPMM-ALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
204-334 |
8.92e-49 |
|
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: 165.84 E-value: 8.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 204 RDNLSFKVVKSRDRKSYIVD---YLKSNIESSGIIYAATRKDVERLYIFLKKLDFSVTKYHGGLEDEERKENQDLFLYDD 280
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLlkrIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1119951532 281 AKVMIATNAFGMGIDKSNVRFVIHYNIPRNIESYYQEAGRAGRDGEEGECILLY 334
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 ... |
8-195 |
1.80e-47 |
|
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: 164.95 E-value: 1.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 8 EILKKYYGYDDFR-EGQREIIESIISHR-DTFGIMPTGGGKSICYQIPAMYFGGVTIVISPLISLMKDQVDTLNSLGIKS 85
Cdd:cd18014 2 STLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 86 AYINSSLSNEELNTIIH--RASMGDYKLIYVAPERLESHLFRNILMIL----PVDQIAIDEAHCVSQWGHDFRASYRMIS 159
Cdd:cd18014 82 DSLNSKLSAQERKRIIAdlESEKPQTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLRLG 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1119951532 160 SLIEDLNPRPVIsAFTATATELVKDDIVRLLELQEP 195
Cdd:cd18014 162 ALRSRYGHVPWV-ALTATATPQVQEDIFAQLRLKKP 196
|
|
| DpdF |
NF041063 |
protein DpdF; |
9-345 |
3.84e-47 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 177.03 E-value: 3.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 9 ILKKYYGYDDFR-EGQREIIES----------IIShrdtfgiMPTGGGKSICYQIPAMYF---GGVTIVISPLISLMKDQ 74
Cdd:NF041063 130 FLAEALGFTHYRsPGQREAVRAallappgstlIVN-------LPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQ 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 75 ----VDTLNSLGIKS----AYInSSLSNEELNTIIHRASMGDYKLIYVAPE----RLESHLF----RNILmilpvDQIAI 138
Cdd:NF041063 203 erraRELLRRAGPDLggplAWH-GGLSAEERAAIRQRIRDGTQRILFTSPEsltgSLRPALFdaaeAGLL-----RYLVV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 139 DEAHCVSQWGHDFRASYRMISSLIEDL------NPRPVISAFTATATELVKDDIVRLLELQEPNIYVSG-FNRDNLSFKV 211
Cdd:NF041063 277 DEAHLVDQWGDGFRPEFQLLAGLRRSLlrlapsGRPFRTLLLSATLTESTLDTLETLFGPPGPFIVVSAvQLRPEPAYWV 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 212 VKSRDRKSYI------VDYLKSNIessgIIYAATRKDVERLYIFLKKLDFS-VTKYHGGLEDEERK-------ENQdlfl 277
Cdd:NF041063 357 AKCDSEEERRervleaLRHLPRPL----ILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERErlieqwrENE---- 428
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119951532 278 YDdakVMIATNAFGMGIDKSNVRFVIHYNIPRNIESYYQEAGRAGRDGEEGECILLYDSRDINTQQYL 345
Cdd:NF041063 429 LD---IVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKSL 493
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
403-509 |
1.10e-35 |
|
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure. The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 462780 [Multi-domain] Cd Length: 108 Bit Score: 129.58 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 403 YELKDITVESQKIISCVYRMKESYGVGLIAEVLRGSKNQKILALAMDKLSTYGIIKNYTIGEIKEIINYLISEKYLALTK 482
Cdd:pfam09382 2 PETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDI 81
|
90 100
....*....|....*....|....*..
gi 1119951532 483 DMFSIVKLTNKAVQFIKESETIYMRIE 509
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 ... |
407-498 |
1.43e-30 |
|
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure; The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 214936 [Multi-domain] Cd Length: 92 Bit Score: 114.49 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 407 DITVESQKIISCVYRMKESYGVGLIAEVLRGSKNQKILALAMDKLSTYGIIKNYTIGEIKEIINYLISEKYLALTKDMFS 486
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 1119951532 487 IVKLTNKAVQFI 498
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
20-184 |
1.94e-27 |
|
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: 108.48 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 20 REGQREIIESIISHRDTFGIMPTGGGKSICYQIPAMYF------GGVTIVISPLISLMKDQVDTLNSLGIKSAY-INSSL 92
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAldkldnGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 93 SNEELNTIihRASMGDYKLIYVAPERLESHL-----FRNILMilpvdqIAIDEAHCVSQWGhdFRASYRMIsslIEDLNP 167
Cdd:pfam00270 81 GGDSRKEQ--LEKLKGPDILVGTPGRLLDLLqerklLKNLKL------LVLDEAHRLLDMG--FGPDLEEI---LRRLPK 147
|
170
....*....|....*..
gi 1119951532 168 RPVISAFTATATELVKD 184
Cdd:pfam00270 148 KRQILLLSATLPRNLED 164
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
208-334 |
4.77e-25 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 100.66 E-value: 4.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 208 SFKVVKSRDRKSY-IVDYLKSNIESSGIIYAATRKDVERLYIFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIA 286
Cdd:cd18787 4 LYVVVEEEEKKLLlLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1119951532 287 TNAFGMGIDKSNVRFVIHYNIPRNIESYYQEAGRAGRDGEEGECILLY 334
Cdd:cd18787 84 TDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
244-325 |
2.41e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 96.90 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 244 ERLYIFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFVIHYNIPRNIESYYQEAGRAGR 323
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1119951532 324 DG 325
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
216-325 |
4.03e-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: 94.20 E-value: 4.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 216 DRKSYIVDYLKSNIESSGIIYAATRKDVERLYiFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGID 295
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 1119951532 296 KSNVRFVIHYNIPRNIESYYQEAGRAGRDG 325
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
12-192 |
1.25e-22 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 96.02 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 12 KYYGYDDFREGQREIIESIISH-RDTFGIMPTGGGKSICYQIPAMYF-----GGVTIVISPLISLMKDQVDTLNSLGIKS 85
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 86 AYINSSL-SNEELNTIIHRASMGDYKLIYVAPERLESHLFRNILMILPVDQIAIDEAHCVSQWGHdfrasYRMISSLIED 164
Cdd:smart00487 82 GLKVVGLyGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGF-----GDQLEKLLKL 156
|
170 180
....*....|....*....|....*...
gi 1119951532 165 LNPRPVISAFTATATELVKDDIVRLLEL 192
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLND 184
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
520-585 |
4.87e-20 |
|
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: 84.12 E-value: 4.87e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119951532 520 GLFNELKALRKVIAENEKIPPYIIFSDATLKELSAKKPINKEDMLLIKGIGEVKFERYGEDFMEVI 585
Cdd:pfam00570 3 ALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
337-400 |
7.90e-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: 83.49 E-value: 7.90e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119951532 337 RDINTQQYLINTSIANSDRAAIEYDKLQSIDNYC-HTNKCLRKYILEYFGEDITWDNCHNCSNCT 400
Cdd:pfam16124 2 QDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCeNTTDCRRKQLLRYFGEEFDSEPCGNCDNCL 66
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
23-340 |
1.91e-19 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 90.98 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 23 QREIIESIISHRDTFGIMPTGGGKSICYQIPAM------YFGGV-TIVISP---LIslmkDQV-DTLNSLG----IKSAy 87
Cdd:COG0513 29 QAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrldpsRPRAPqALILAPtreLA----LQVaEELRKLAkylgLRVA- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 88 insslsneelnTIIHRASMGD--YKL-----IYVA-PERLESHLFRNILMILPVDQIAIDEAhcvsqwghDfrasyRMIS 159
Cdd:COG0513 104 -----------TVYGGVSIGRqiRALkrgvdIVVAtPGRLLDLIERGALDLSGVETLVLDEA--------D-----RMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 160 -SLIEDLnpRPVISA---------FTATatelVKDDIVRLLE--LQEP-NIYVSGFNRDN----LSFKVVKSRDRKSYIV 222
Cdd:COG0513 160 mGFIEDI--ERILKLlpkerqtllFSAT----MPPEIRKLAKryLKNPvRIEVAPENATAetieQRYYLVDKRDKLELLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 223 DYLKSNIESSGIIYAATRKDVERLYIFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFV 302
Cdd:COG0513 234 RLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHV 313
|
330 340 350
....*....|....*....|....*....|....*...
gi 1119951532 303 IHYNIPRNIESYYQEAGRAGRDGEEGECILLYDSRDIN 340
Cdd:COG0513 314 INYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERR 351
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
521-587 |
1.01e-16 |
|
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: 75.03 E-value: 1.01e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119951532 521 LFNELKALRKVIAENEKIPPYIIFSDATLKELSAKKPINKEDMLLIKGIGEVKFERYGEDFMEVIKK 587
Cdd:smart00341 7 LLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQE 73
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
23-387 |
4.08e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.53 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 23 QREIIESIISHRDTFG-----IMPTGGGKSI----CYQipAMYFGGVTIVISPLISLMKDQVDTLNSLGIKSAYINSSLS 93
Cdd:COG1061 85 QQEALEALLAALERGGgrglvVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAGGGKKD 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 94 NEELNTIIHRASMGdykliyvapERLESHLFRNilmilPVDQIAIDEAHcvsqwgHDFRASYRMIsslIEDLNPRPVIsA 173
Cdd:COG1061 163 SDAPITVATYQSLA---------RRAHLDELGD-----RFGLVIIDEAH------HAGAPSYRRI---LEAFPAAYRL-G 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 174 FTAT----------------------ATELVKDDIVRLLELQEPNIYVSGFNRD------NLSFKVVKSRDRKSYIVDYL 225
Cdd:COG1061 219 LTATpfrsdgreillflfdgivyeysLKEAIEDGYLAPPEYYGIRVDLTDERAEydalseRLREALAADAERKDKILREL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 226 KSNI--ESSGIIYAATRKDVERLYIFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFVI 303
Cdd:COG1061 299 LREHpdDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 304 HYnipRNIES---YYQEAGRAGRDGEEGECILLYD--SRDINTQQYLINtsiANSDRAAIEYDKLQSIDNYCHTNKCLRK 378
Cdd:COG1061 379 LL---RPTGSpreFIQRLGRGLRPAPGKEDALVYDfvGNDVPVLEELAK---DLRDLAGYRVEFLDEEESEELALLIAVK 452
|
....*....
gi 1119951532 379 YILEYFGED 387
Cdd:COG1061 453 PALEVKGEL 461
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
15-358 |
2.13e-14 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 75.98 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 15 GYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIP------AMYFGGVT-------IVISP---LISLMKDQVDTL 78
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrccTIRSGHPSeqrnplaMVLTPtreLCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 79 -NSLGIKSAYInssLSNEELNTIIHRASMGdYKLIYVAPERLESHLFRNILMILPVDQIAIDEAHCVSQWGhdFRASYRM 157
Cdd:PLN00206 220 gKGLPFKTALV---VGGDAMPQQLYRIQQG-VELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG--FRDQVMQ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 158 ISSLIedlnPRPVISAFTAT--------ATELVKDDIVrllelqepnIYVSGFNRDNLSFKV----VKSRDRKSYIVDYL 225
Cdd:PLN00206 294 IFQAL----SQPQVLLFSATvspevekfASSLAKDIIL---------ISIGNPNRPNKAVKQlaiwVETKQKKQKLFDIL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 226 KS--NIESSGIIYAATRKDVERLYIFLKKLD-FSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFV 302
Cdd:PLN00206 361 KSkqHFKPPAVVFVSSRLGADLLANAITVVTgLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQV 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1119951532 303 IHYNIPRNIESYYQEAGRAGRDGEEGECILLYDSRDINTQQYLIntSIANSDRAAI 358
Cdd:PLN00206 441 IIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELV--ALLKSSGAAI 494
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
23-347 |
1.53e-13 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 73.72 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 23 QREIIESIISHRDTFGIMPTGGGKSICYQIPA----MYFGGVT-IVISPLISLMKDQVDTLNSL------GIKSA----- 86
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVlealLEDPGATaLYLYPTKALARDQLRRLRELaealglGVRVAtydgd 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 87 ---------YINSS--LSNEElntIIHRAsmgdykliYVAPERLESHLFRNilmilpVDQIAIDEAHcvsqwghdfraSY 155
Cdd:COG1205 141 tppeerrwiREHPDivLTNPD---MLHYG--------LLPHHTRWARFFRN------LRYVVIDEAH-----------TY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 156 RMI--SS----------LIEDLNPRPVISAFTAT-------ATELVKDDiVRLlelqepnIYVSGFNRDNLSF-----KV 211
Cdd:COG1205 193 RGVfgSHvanvlrrlrrICRHYGSDPQFILASATignpaehAERLTGRP-VTV-------VDEDGSPRGERTFvlwnpPL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 212 VKSRDRKSY-------IVDYLKSNIesSGIIYAATRKDVERLYIFLKK------LDFSVTKYHGGLEDEERKENQDLFLY 278
Cdd:COG1205 265 VDDGIRRSAlaeaarlLADLVREGL--RTLVFTRSRRGAELLARYARRalrepdLADRVAAYRAGYLPEERREIERGLRS 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119951532 279 DDAKVMIATNAFGMGIDKSNVRFVIHYNIPRNIESYYQEAGRAGRDGEEGECILL--YDSRDintqQYLIN 347
Cdd:COG1205 343 GELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVagDDPLD----QYYVR 409
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
234-327 |
3.91e-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: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 234 IIYAATRKDVERLYIFLK-------KLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFVIHYN 306
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKarlveegPLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|.
gi 1119951532 307 IPRNIESYYQEAGRAGRDGEE 327
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKD 139
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
216-341 |
9.42e-13 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 70.24 E-value: 9.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 216 DRKSYIVDYLKSNIES----SGIIYAATRKDVERLYIFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFG 291
Cdd:PTZ00424 249 EKEEWKFDTLCDLYETltitQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLA 328
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1119951532 292 MGIDKSNVRFVIHYNIPRNIESYYQEAGRAGRDGEEGECILLYDSRDINT 341
Cdd:PTZ00424 329 RGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQ 378
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
192-333 |
3.27e-11 |
|
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: 61.80 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 192 LQEpniYVSGFNRDNLSFKVVKSRDRKSYIVDYLKSNIESSG---IIYAATRKDVERLYIFLKKLDFsvtkYHGGLEDEE 268
Cdd:cd18795 5 LEE---YVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGkpvLVFCSSRKECEKTAKDLAGIAF----HHAGLTRED 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119951532 269 RKENQDLFLYDDAKVMIATNAFGMGID--------KSNVRFVIHYNIPRNIESYYQEAGRAGRDG--EEGECILL 333
Cdd:cd18795 78 RELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKGYRELSPLEYLQMIGRAGRPGfdTRGEAIIM 152
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
277-334 |
4.59e-11 |
|
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: 58.87 E-value: 4.59e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119951532 277 LYDDAKVMIATNAFGMGIDKSNVRFVIHYNIPRNIESYYQEAGRAGRDG-EEGECILLY 334
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
40-173 |
8.97e-11 |
|
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: 60.11 E-value: 8.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 40 MPTGGGKSICYQIPAMY----FGGVTIVISPLISLMKDQ---VDTLNSLGIKSAYINSSLSNEELntiiHRASMGDYKLI 112
Cdd:cd00046 8 APTGSGKTLAALLAALLlllkKGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEER----EKNKLGDADII 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119951532 113 YVAPERLESHLFRNILM-ILPVDQIAIDEAHCVSQWGHDFRASYRMISSLIEDLNPRPVISA 173
Cdd:cd00046 84 IATPDMLLNLLLREDRLfLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSA 145
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
2-338 |
5.95e-10 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 62.17 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 2 ILLSINEIlkkyyGYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIPAMYFGGVTI------VISPLISLMKDQV 75
Cdd:PRK11634 17 ILEALNDL-----GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELkapqilVLAPTRELAVQVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 76 DTLNSLGIKSAYINS-SLSNEELNTIIHRASMGDYKLIYVAPERLESHLFRNILMILPVDQIAIDEAHcvsqwghdfrAS 154
Cdd:PRK11634 92 EAMTDFSKHMRGVNVvALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEAD----------EM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 155 YRMisSLIEDL-NPRPVISA------FTATATELVKDDIVRLL-ELQEPNIYVSGFNRDNLS--FKVVKSRDRKSYIVDY 224
Cdd:PRK11634 162 LRM--GFIEDVeTIMAQIPEghqtalFSATMPEAIRRITRRFMkEPQEVRIQSSVTTRPDISqsYWTVWGMRKNEALVRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 225 LKSNIESSGIIYAATRKDVERLYIFLKKLDFSVTKYHGGLEDEERKenQDLFLYDDAK--VMIATNAFGMGIDKSNVRFV 302
Cdd:PRK11634 240 LEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALRE--QTLERLKDGRldILIATDVAARGLDVERISLV 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 1119951532 303 IHYNIPRNIESYYQEAGRAGRDGEEGECILLYDSRD 338
Cdd:PRK11634 318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRE 353
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
31-328 |
2.50e-09 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 59.79 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 31 ISHRDTFGIMPTGGGKSICYQIPAMYF-----------GGVTIVISPLISLMKDQVDTLNSLGIKSAYINS--------S 91
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAIVHinaqpllrygdGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTvayggvpkR 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 92 LSNEELNTIIHrasmgdyklIYVA-PERLESHLFRNILMILPVDQIAIDEAHCVSQWGhdFRASYRMISSLIedlnpRPV 170
Cdd:PTZ00110 245 GQIYALRRGVE---------ILIAcPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMG--FEPQIRKIVSQI-----RPD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 171 ISAFTATAT---ELVKddIVRLLELQEPnIYVsgfNRDNLSFK----------VVKSRDRKSYIVDYLKSNIESSG--II 235
Cdd:PTZ00110 309 RQTLMWSATwpkEVQS--LARDLCKEEP-VHV---NVGSLDLTachnikqevfVVEEHEKRGKLKMLLQRIMRDGDkiLI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 236 YAATRKDVERLYIFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFVIHYNIPRNIESYY 315
Cdd:PTZ00110 383 FVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYV 462
|
330
....*....|...
gi 1119951532 316 QEAGRAGRDGEEG 328
Cdd:PTZ00110 463 HRIGRTGRAGAKG 475
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
3-338 |
2.62e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 59.91 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 3 LLSINEILKKYyGYDDFREGQREIIESIISHRDTFGI-MPTGGGKS------ICYQIPAmyfGGVTIVISPLISLMKDQV 75
Cdd:COG1204 8 LEKVIEFLKER-GIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTliaelaILKALLN---GGKALYIVPLRALASEKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 76 DTLNSLgiksayinssLSNEELNTIIhraSMGDYKL---------IYVA-PERLESHLFRNILMILPVDQIAIDEAHCVs 145
Cdd:COG1204 84 REFKRD----------FEELGIKVGV---STGDYDSddewlgrydILVAtPEKLDSLLRNGPSWLRDVDLVVVDEAHLI- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 146 qwGHDFR-ASYRMISSLIEDLNPRPVISAFTATAT-----------ELVKDDI--VRLLElqepNIYVSGfnrdNLSFKv 211
Cdd:COG1204 150 --DDESRgPTLEVLLARLRRLNPEAQIVALSATIGnaeeiaewldaELVKSDWrpVPLNE----GVLYDG----VLRFD- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 212 VKSRDRKSYIVDYLKSNIESSG--IIYAATRKDVERL------------------------YIFLKKLDFSVTKY----- 260
Cdd:COG1204 219 DGSRRSKDPTLALALDLLEEGGqvLVFVSSRRDAESLakkladelkrrltpeereeleelaEELLEVSEETHTNEkladc 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 261 --------HGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIdksN--VRFVI------HYNIPRNIESYYQEAGRAGRD 324
Cdd:COG1204 299 lekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAGRP 375
|
410
....*....|....*.
gi 1119951532 325 G--EEGECILLYDSRD 338
Cdd:COG1204 376 GydPYGEAILVAKSSD 391
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
231-323 |
1.11e-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: 54.19 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 231 SSGIIYAATRKDVERLYIFLKKL---DFSVTKY---HGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFVIH 304
Cdd:cd18796 39 KSTLVFTNTRSQAERLAQRLRELcpdRVPPDFIalhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQ 118
|
90
....*....|....*....
gi 1119951532 305 YNIPRNIESYYQEAGRAGR 323
Cdd:cd18796 119 IGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
19-177 |
1.81e-07 |
|
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: 50.77 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 19 FREGQREIIESIISH-RDTFGI--MPTGGGKSIC-YQIPAMYFGGVTIVISPLISLMKDQVDTLNSLGIKSA-YINSSLS 93
Cdd:cd17926 1 LRPYQEEALEAWLAHkNNRRGIlvLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSiGLIGGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 94 NEELNTIihrasmgdykLIYVA-PERLESHLFRNILMILPVDQIAIDEAHcvsqwghdfRASYRMISSLIEDLNPRPVIs 172
Cdd:cd17926 81 KKDFDDA----------NVVVAtYQSLSNLAEEEKDLFDQFGLLIVDEAH---------HLPAKTFSEILKELNAKYRL- 140
|
....*
gi 1119951532 173 AFTAT 177
Cdd:cd17926 141 GLTAT 145
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
211-331 |
2.02e-07 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 53.76 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 211 VVKSRDRKSYIVDYLKSNIESSGIIYAATRKDVERLYIFLKKLDFSVTKYHGGLEDEERKENQDLFLYDDAKVMIATNAF 290
Cdd:PRK01297 316 AVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVA 395
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1119951532 291 GMGIDKSNVRFVIHYNIPRNIESYYQEAGRAGRDGEEGECI 331
Cdd:PRK01297 396 GRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSI 436
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
472-587 |
4.77e-06 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 49.10 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 472 LISEKYLALTKDMFSIvkLTNKAVQFIkESETIYMRIEATSKNTKGESGLFNELKALRKVIAENEKIPPYIIFSDATLKE 551
Cdd:COG0349 166 LEREGRLEWAEEECAR--LLDPATYRE-DPEEAWLRLKGAWKLNPRQLAVLRELAAWREREARKRDVPRNRVLKDEALLE 242
|
90 100 110
....*....|....*....|....*....|....*.
gi 1119951532 552 LSAKKPINKEDMLLIKGIGEVKFERYGEDFMEVIKK 587
Cdd:COG0349 243 LARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAE 278
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
19-177 |
1.17e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 45.74 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 19 FREGQREIIESI---ISHRDTFGI--MPTGGGKSICY-QIPAMYF--GGV--TIVISPLISLMKDQVDTLNSLGIKSAYI 88
Cdd:pfam04851 4 LRPYQIEAIENLlesIKNGQKRGLivMATGSGKTLTAaKLIARLFkkGPIkkVLFLVPRKDLLEQALEEFKKFLPNYVEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 89 NSSLSNEELNTIIHrasmgDYKLIYVAPERLESHLFRNILMILP--VDQIAIDEAHcvsqwgHDFRASYRmissLIEDLN 166
Cdd:pfam04851 84 GEIISGDKKDESVD-----DNKIVVTTIQSLYKALELASLELLPdfFDVIIIDEAH------RSGASSYR----NILEYF 148
|
170
....*....|.
gi 1119951532 167 PRPVISAFTAT 177
Cdd:pfam04851 149 KPAFLLGLTAT 159
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
23-360 |
1.64e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 47.96 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 23 QREIIESIISHRDTFGIMPTGGGKSIC--YQIPAMYFGGV-TIVISPLISLMKDQVDTLNSLGIKSAYINSSLSN-EELN 98
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIaySAIYETFLAGLkSIYIVPLRSLAMEKYEELSRLRSLGMRVKISIGDyDDPP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 99 TIIHRasmgdYKLIYVAPERLESHLFRNILMILPVDQIAIDEAHCVsqwGHDFRA-SYRMISSLIEDLNPRPVISAFTAT 177
Cdd:PRK01172 107 DFIKR-----YDVVILTSEKADSLIHHDPYIINDVGLIVADEIHII---GDEDRGpTLETVLSSARYVNPDARILALSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 178 AT-----------ELVKDDI----VRLLELQEPNIYVSGFNRDNLSfkvvksrdrksyIVDYLKSNIESSG--IIYAATR 240
Cdd:PRK01172 179 VSnanelaqwlnaSLIKSNFrpvpLKLGILYRKRLILDGYERSQVD------------INSLIKETVNDGGqvLVFVSSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 241 KDVERLYIFLKKL-----DFSVTK--------------------YHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGID 295
Cdd:PRK01172 247 KNAEDYAEMLIQHfpefnDFKVSSennnvyddslnemlphgvafHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVN 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1119951532 296 KSnVRFVIHYNIPR----------NIEsYYQEAGRAGRDGeegecillYDSRDINtqqyLINTSIANSDRAAIEY 360
Cdd:PRK01172 327 LP-ARLVIVRDITRygnggirylsNME-IKQMIGRAGRPG--------YDQYGIG----YIYAASPASYDAAKKY 387
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
23-142 |
6.34e-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: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 23 QREIIESIISHRDTFGIMPTGGGKSICYQIPAMY-----FGGVTIVISPLISLMKDQVDTLNSL------GIKSAYINSS 91
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEallrdPGSRALYLYPTKALAQDQLRSLRELleqlglGIRVATYDGD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119951532 92 LSNEELNTIIHRAS--------MGDYKLIYvaPERLESHLFRNilmilpVDQIAIDEAH 142
Cdd:cd17923 85 TPREERRAIIRNPPrilltnpdMLHYALLP--HHDRWARFLRN------LRYVVLDEAH 135
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
23-146 |
1.84e-04 |
|
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: 42.63 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 23 QREIIESIISHRDTFGI-MPTGGGKSICYQIpAMY-----FGGVTIVISPLISLMKDQVDTLNSLgiksayinssLSNEE 96
Cdd:cd17921 6 QREALRALYLSGDSVLVsAPTSSGKTLIAEL-AILralatSGGKAVYIAPTRALVNQKEADLRER----------FGPLG 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119951532 97 LNTIIhraSMGDYKL---------IYVA-PERLESHLFRN-ILMILPVDQIAIDEAHCVSQ 146
Cdd:cd17921 75 KNVGL---LTGDPSVnklllaeadILVAtPEKLDLLLRNGgERLIQDVRLVVVDEAHLIGD 132
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
207-325 |
8.57e-04 |
|
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: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 207 LSFKVVKSRDRK-SYIVDYLKSNIESSG--IIYAATRKDVERLYIFLKKLDFSVTKYHGGLEDEERKENQDLF--LYDDA 281
Cdd:cd18793 1 LPPKIEEVVSGKlEALLELLEELREPGEkvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFneDPDIR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1119951532 282 KVMIATNAFGMGIDKSNVRFVIHYNIPRN--IESyyQEAGRAGRDG 325
Cdd:cd18793 81 VFLLSTKAGGVGLNLTAANRVILYDPWWNpaVEE--QAIDRAHRIG 124
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
225-329 |
9.90e-04 |
|
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: 39.46 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 225 LKSNIESSGIIYAATRKDVERLYIFL-KKLDFSVTKYHGGLEDEERKENQDLFL--YDDAKVMIATNAFGMGIDkSNVRF 301
Cdd:cd18805 12 SLRNLRPGDCVVAFSRKDIFSLKREIeKRTGLKCAVIYGALPPETRRQQARLFNdpESGYDVLVASDAIGMGLN-LNIRR 90
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1119951532 302 VIHYNIP-------RNIESYY--QEAGRAGRDG---EEGE 329
Cdd:cd18805 91 VIFSSLSkfdgnemRPLSPSEvkQIAGRAGRFGshfPEGE 130
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
260-322 |
1.16e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 42.22 E-value: 1.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119951532 260 YHGGLEDEERKENQDLFLYDDAKVMIATNAFGMGIDKSNVRFVIHYNIPRNIESYYQEAGRAG 322
Cdd:PRK09751 307 HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
19-177 |
5.21e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 38.57 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 19 FREGQREIIESIISHRDTFGIMPTGGGKS-----IC----YQIPAMYfGGVTIVISPLISLMKDQVDTLNSLGIKSAYIN 89
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPAGR-KGKVVFLANKVPLVEQQKEVFRKHFERPGYKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 90 SSLSNEELNTIIHRASMGDYKLIYVAPERLESHLFRNILMILP-VDQIAIDEAHCVSQwghdfRASYRMI-----SSLIE 163
Cdd:cd17927 82 TGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSdFSLLVFDECHNTTK-----NHPYNEImfrylDQKLG 156
|
170
....*....|....
gi 1119951532 164 DLNPRPVISAFTAT 177
Cdd:cd17927 157 SSGPLPQILGLTAS 170
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
15-200 |
5.92e-03 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 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: 350699 [Multi-domain] Cd Length: 198 Bit Score: 38.43 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 15 GYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIPAM----------YFGGVTIVISPLISLMKDQVDTLNSLG-- 82
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLeklyrerwtpEDGLGALIISPTRELAMQIFEVLRKVGky 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 83 --IKSAYINSSLSNEELNTIIHRASMgdyklIYVAPERLESHLFRNILMILPVDQIAI-DEAHCVSQWGhdFRASyrmIS 159
Cdd:cd17941 89 hsFSAGLIIGGKDVKEEKERINRMNI-----LVCTPGRLLQHMDETPGFDTSNLQMLVlDEADRILDMG--FKET---LD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1119951532 160 SLIEDLNPRPVISAFTATATELVKdDIVRlLELQEPnIYVS 200
Cdd:cd17941 159 AIVENLPKSRQTLLFSATQTKSVK-DLAR-LSLKNP-EYIS 196
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
15-200 |
8.07e-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: 38.11 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 15 GYDDFREGQREIIESIISHRDTFGIMPTGGGKSICYQIPAMYF----------GGVTIVISP-----------LISLMKD 73
Cdd:cd17942 9 GFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELlyklkfkprnGTGVIIISPtrelalqiygvAKELLKY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 74 QVDTlnsLGIKSAYINSSLSNEELNTIIHrasmgdykLIYVAPERLESHL-------FRNiLMILpvdqiAIDEAHCVSQ 146
Cdd:cd17942 89 HSQT---FGIVIGGANRKAEAEKLGKGVN--------ILVATPGRLLDHLqntkgflYKN-LQCL-----IIDEADRILE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1119951532 147 WGhdFRASYRMISSLiedLNPRPVISAFTATATELVkDDIVRlLELQEPNIYVS 200
Cdd:cd17942 152 IG--FEEEMRQIIKL---LPKRRQTMLFSATQTRKV-EDLAR-ISLKKKPLYVG 198
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
221-325 |
8.83e-03 |
|
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: 36.80 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119951532 221 IVDYLKSNIESSGIIYAATRKDVERLYIFLKK----LDF-----------SVTKYHGGLEDEERKENQDLFLYDDAKVMI 285
Cdd:cd18802 16 LREYFPKTPDFRGIIFVERRATAVVLSRLLKEhpstLAFircgfligrgnSSQRKRSLMTQRKQKETLDKFRDGELNLLI 95
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1119951532 286 ATNAFGMGIDKSNVRFVIHYNIPRNIESYYQEAGRAGRDG 325
Cdd:cd18802 96 ATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
|
|
| |
