|
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 ... |
1-588 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273594 [Multi-domain] Cd Length: 591 Bit Score: 855.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 1 MEAILSHYFGYQSFRPGQKEIITKILAHHNVLGVLPTGGGKSICYQIPGLKLGGTTVVISPLISLMKDQVDQLKAMGIHA 80
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 81 AYLNSSLSQKQQKQIEQELASGKIQFLYVAPERFENQYFLSILRKLEIHLIAFDEAHCISKWGHDFRPSYQNVIQKVMTL 160
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 161 PQDFVvIALTATATTEVQRDIMDKLYISADNRVKTSTKRRNLIFKVNPTYQRQKFVLDYVQAHRDEAGIIYCSTRKQVEE 240
Cdd:TIGR01389 161 PQVPR-IALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 241 LQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDG 320
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 321 LKSECILLYSERDKGLHEYFISVSQADDDYKDKMGEKLTKMLQYTKTKKCLEATIVHYFEPNEkLEECQQCSNCVQENKT 400
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENE-VEPCGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 401 YDMTKEAKMIVSCVARMRQQENYSVIIQVLRGEQSDYIKYNHYDQLSTYGIMKAYTTSELSHLIDELRFKGFLNEHNEIL 480
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 481 I---CDQSVQSLLKEDVTIFTTPFRQKSKEK--VYINTVEGVDRALYNELVDVRKQLSNKLGIAPVSIFSDYTLEEFAKR 555
Cdd:TIGR01389 479 IglqLTEAARKVLKNEVEVLLRPFKVVAKEKtrVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEK 558
|
570 580 590
....*....|....*....|....*....|...
gi 488390370 556 KPASKQEMIAIEGVGSYKLKHYCPNFLERIQSY 588
Cdd:TIGR01389 559 RPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-467 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 666.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 1 MEAILSHYFGYQSFRPGQKEIITKILAHHNVLGVLPTGGGKSICYQIPGLKLGGTTVVISPLISLMKDQVDQLKAMGIHA 80
Cdd:COG0514 5 ALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 81 AYLNSSLSQKQQKQIEQELASGKIQFLYVAPERFENQYFLSILRKLEIHLIAFDEAHCISKWGHDFRPSYQNVIQKVMTL 160
Cdd:COG0514 85 AFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRERL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 161 PqDFVVIALTATATTEVQRDIMDKLYISADNRVKTSTKRRNLIFKVNPTYQRQK--FVLDYVQAHRDEAGIIYCSTRKQV 238
Cdd:COG0514 165 P-NVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKlaQLLDFLKEHPGGSGIVYCLSRKKV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 239 EELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGR 318
Cdd:COG0514 244 EELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 319 DGLKSECILLYSERDKGLHEYFISVSQADDDYKDKMGEKLTKMLQYTKTKKCLEATIVHYF-EPNEklEECQQCSNCVQE 397
Cdd:COG0514 324 DGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFgEELA--EPCGNCDNCLGP 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 398 NKTYDMTKEAKMIVSCVARMRQQENYSVIIQVLRGEQSDYIKYNHYDQLSTYGIMKAYTTSELSHLIDEL 467
Cdd:COG0514 402 PETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQL 471
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
2-586 |
1.33e-161 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 474.97 E-value: 1.33e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 2 EAILSHYFGYQSFRPGQKEIITKILAHHNVLGVLPTGGGKSICYQIPGLKLGGTTVVISPLISLMKDQVDQLKAMGIHAA 81
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 82 YLNSSLSQKQQKQIEQELASGKIQFLYVAPERFENQYFLSILRKLEIHLIAFDEAHCISKWGHDFRPSYQNVIQKVMTLP 161
Cdd:PRK11057 94 CLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRFP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 162 qDFVVIALTATATTEVQRDIMDKL-------YISADNRVKTstkRRNLIFKVNPTYQrqkfVLDYVQAHRDEAGIIYCST 234
Cdd:PRK11057 174 -TLPFMALTATADDTTRQDIVRLLglndpliQISSFDRPNI---RYTLVEKFKPLDQ----LMRYVQEQRGKSGIIYCNS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 235 RKQVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAG 314
Cdd:PRK11057 246 RAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 315 RAGRDGLKSECILLYSERD-----KGLHEyfisvsQADDDYKDKMGEKLTKMLQYTKTKKCLEATIVHYFEPNEKlEECQ 389
Cdd:PRK11057 326 RAGRDGLPAEAMLFYDPADmawlrRCLEE------KPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQ-EPCG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 390 QCSNCVQENKTYDMTKEAKMIVSCVARMRQQENYSVIIQVLRGEQSDYIKYNHYDQLSTYGIMKAYTTSELSHLIDELRF 469
Cdd:PRK11057 399 NCDICLDPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 470 KGFLNE---HNEILICDQSVQSLLKEDVTI-FTTP----FRQKSKEKVYINTvegVDRALYNELVDVRKQLSNKLGIAPV 541
Cdd:PRK11057 479 LGLVTQniaQHSALQLTEAARPVLRGEVSLqLAVPrivaLKPRAMQKSFGGN---YDRKLFAKLRKLRKSIADEENIPPY 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 488390370 542 SIFSDYTLEEFAKRKPASKQEMIAIEGVGSYKLKHYCPNFLERIQ 586
Cdd:PRK11057 556 VVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIR 600
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
4-454 |
1.08e-136 |
|
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: 406.46 E-value: 1.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 4 ILSHYFGYQSFRPGQKEIITKILAHHNVLGVLPTGGGKSICYQIPGLKLGGTTVVISPLISLMKDQVDQLKAMGIHAAYL 83
Cdd:TIGR00614 2 ILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 84 NSSLSQKQQKQIEQELASGKIQFLYVAPERF-ENQYFLSILR-KLEIHLIAFDEAHCISKWGHDFRPSYQNVIQKVMTLP 161
Cdd:TIGR00614 82 NSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsASNRLLQTLEeRKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 162 qDFVVIALTATATTEVQRDIMDKLYISADNRVKTSTKRRNLIFKV-----NPTYQRQKFVldyVQAHRDEAGIIYCSTRK 236
Cdd:TIGR00614 162 -NVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVrrktpKILEDLLRFI---RKEFEGKSGIIYCPSRK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 237 QVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRA 316
Cdd:TIGR00614 238 KVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 317 GRDGLKSECILLYSERDKGLHEYFIsVSQADDDYKDKMGEKLTKMLQYTKTKKCLEATIVHYFE------------PNEK 384
Cdd:TIGR00614 318 GRDGLPSECHLFYAPADMNRLRRLL-MEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGekgfnksfcimgTEKC 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488390370 385 LEECQQCSNCVQENKT---YDMTKEAKMIVSCVARMRQQENYSVIIQVLRGEQSDYIKYNHYDQLSTYGIMKA 454
Cdd:TIGR00614 397 CDNCCKRLDYKTKDVTdkvYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKD 469
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
9-587 |
1.33e-96 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 319.92 E-value: 1.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 9 FGYQSFRPGQKEIITKILAHHNVLGVLPTGGGKSICYQIPGLKLGGTTVVISPLISLMKDQVDQLKAMGIHAAYLNSSLS 88
Cdd:PLN03137 456 FGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGME 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 89 QKQQKQIEQELASG--KIQFLYVAPERFENQYflSILRKLEI-------HLIAFDEAHCISKWGHDFRPSYQNV---IQK 156
Cdd:PLN03137 536 WAEQLEILQELSSEysKYKLLYVTPEKVAKSD--SLLRHLENlnsrgllARFVIDEAHCVSQWGHDFRPDYQGLgilKQK 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 157 VMTLPqdfvVIALTATATTEVQRDIMDKLYISADNRVKTSTKRRNLIFKVNPTYQR-----QKFVLdyvQAHRDEAGIIY 231
Cdd:PLN03137 614 FPNIP----VLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKclediDKFIK---ENHFDECGIIY 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 232 CSTRKQVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLESYYQ 311
Cdd:PLN03137 687 CLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQ 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 312 EAGRAGRDGLKSECILLYSERDKGLHEYFISVSQAD--------------DDYKDKMGEKLTKMLQYTKT----KKCLEa 373
Cdd:PLN03137 767 ECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEqspmamgynrmassGRILETNTENLLRMVSYCENevdcRRFLQ- 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 374 tIVHYFEPNEKLEECQQCSNCVQeNKTY---DMTKEAKMIVSCVARMRQQENYSVIIQVLRGEQSDYIKYNHYDQLSTYG 450
Cdd:PLN03137 846 -LVHFGEKFDSTNCKKTCDNCSS-SKSLidkDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHG 923
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 451 IMKAYTTSELSHLIDELRFKGFLNEHNEILICDQSVQSLLKED--------------VTIFTTPFRQKSKEKVYINTVEG 516
Cdd:PLN03137 924 AGKHLSKGEASRILHYLVTEDILAEDVKKSDLYGSVSSLLKVNeskayklfsggqtiIMRFPSSVKASKPSKFEATPAKG 1003
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 517 -------------------VDRALYNELVDVRKQLSNKL------GIAPVSIFSDYTLEEFAKRKPASKQEMIAIEGVGS 571
Cdd:PLN03137 1004 pltsgkqstlpmatpaqppVDLNLSAILYTALRKLRTALvkeagdGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGK 1083
|
650
....*....|....*.
gi 488390370 572 YKLKHYCPNFLERIQS 587
Cdd:PLN03137 1084 AKVSKYGDRLLETIES 1099
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
2-197 |
1.47e-90 |
|
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: 277.49 E-value: 1.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 2 EAILSHYFGYQSFRPGQKEIITKILAHHNVLGVLPTGGGKSICYQIPGLKLGGTTVVISPLISLMKDQVDQLKAMGIHAA 81
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 82 YLNSSLSQKQQKQIEQELASGKIQFLYVAPERFENQYFLSILRKL----EIHLIAFDEAHCISKWGHDFRPSYQNVIQKV 157
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLperkRLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488390370 158 MTLPqDFVVIALTATATTEVQRDIMDKLYISADNRVKTST 197
Cdd:cd17920 161 RALP-GVPILALTATATPEVREDILKRLGLRNPVIFRASF 199
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
2-197 |
4.01e-74 |
|
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: 235.23 E-value: 4.01e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 2 EAILSHYFGYQSFRPGQKEIITKILAHHNVLGVLPTGGGKSICYQIPGL----KLGGTTVVISPLISLMKDQVDQLKAmG 77
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALllrrRGPGLTLVVSPLIALMKDQVDALPR-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 78 IHAAYLNSSLSQKQQKQIEQELASGKIQFLYVAPERFENQYFLSILRKLE-IHLIAFDEAHCISKWGHDFRPSY---QNV 153
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPpISLLVVDEAHCISEWSHNFRPDYlrlCRV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488390370 154 IQKVMTLPQdfvVIALTATATTEVQRDIMDKLYISADNRVKTST 197
Cdd:cd18018 160 LRELLGAPP---VLALTATATKRVVEDIASHLGIPESGVVRGPL 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
3-189 |
1.41e-55 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 186.80 E-value: 1.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 3 AILSHYFGYQSFRPGQKEIITKILAHHNVLGVLPTGGGKSICYQIPGLKLGGTTVVISPLISLMKDQVDQLKAMGIHAAY 82
Cdd:cd18015 8 DTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 83 LNSSLSQKQQKQIEQELASGKIQF--LYVAPERF-ENQYFLSILRKLE----IHLIAFDEAHCISKWGHDFRPSYQNV-I 154
Cdd:cd18015 88 LNASSSKEHVKWVHAALTDKNSELklLYVTPEKIaKSKRFMSKLEKAYnagrLARIAIDEVHCCSQWGHDFRPDYKKLgI 167
|
170 180 190
....*....|....*....|....*....|....*
gi 488390370 155 QKvmTLPQDFVVIALTATATTEVQRDIMDKLYISA 189
Cdd:cd18015 168 LK--RQFPNVPILGLTATATSKVLKDVQKILCIQK 200
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
199-329 |
8.03e-53 |
|
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: 176.63 E-value: 8.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 199 RRNLIFKV---NPTYQRQKFVLDYVQAHRDEAGIIYCSTRKQVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDR 275
Cdd:cd18794 1 RPNLFYSVrpkDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 488390370 276 IKVVVATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLY 329
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
5-185 |
4.10e-49 |
|
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: 169.19 E-value: 4.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 5 LSHYFGYQSFRPGQKEIItkilahHNVLG-------VLPTGGGKSICYQIPGLKLGGTTVVISPLISLMKDQVDQLKAMG 77
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVI------RSVLEerrdnlvVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 78 IHAAYLNSSLSQKQQKQIEQelasGKIQFLYVAPERFENQyfLSILRKLEIH--LIAFDEAHCISKWGHDFRPSYQNVIQ 155
Cdd:cd18017 78 IPACFLGSAQSQNVLDDIKM----GKIRVIYVTPEFVSKG--LELLQQLRNGitLIAIDEAHCVSQWGHDFRSSYRHLGS 151
|
170 180 190
....*....|....*....|....*....|
gi 488390370 156 KVMTLPqDFVVIALTATATTEVQRDIMDKL 185
Cdd:cd18017 152 IRNRLP-NVPIVALTATATPSVRDDIIKNL 180
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
1-185 |
4.86e-47 |
|
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: 163.84 E-value: 4.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 1 MEAILSHYFGYQSFRPGQKEIITKILAHHNVLGVLPTGGGKSICYQIPGLKLGGTTVVISPLISLMKDQVDQLKAMGIHA 80
Cdd:cd18016 5 MMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 81 AYLNSSLSQKQQKQIEQELASGK--IQFLYVAPERF-ENQYFLSILRKL-EIHLIA---FDEAHCISKWGHDFRPSYQ-- 151
Cdd:cd18016 85 TYLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKIsASNRLISTLENLyERKLLArfvIDEAHCVSQWGHDFRPDYKrl 164
|
170 180 190
....*....|....*....|....*....|....*
gi 488390370 152 NVI-QKVMTLPqdfvVIALTATATTEVQRDIMDKL 185
Cdd:cd18016 165 NMLrQKFPSVP----MMALTATATPRVQKDILNQL 195
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
5-187 |
3.61e-43 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 153.40 E-value: 3.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 5 LSHYFGYQSFR-PGQKEIITKIL-AHHNVLGVLPTGGGKSICYQIPGLKLGGTTVVISPLISLMKDQVDQLKAMGIHAAY 82
Cdd:cd18014 4 LKKVFGHSDFKsPLQEKATMAVVkGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 83 LNSSLSQKQQKQIEQEL--ASGKIQFLYVAPERFENQYFLSILRKLEIH----LIAFDEAHCISKWGHDFRPSYQNvIQK 156
Cdd:cd18014 84 LNSKLSAQERKRIIADLesEKPQTKFLYITPEMAATSSFQPLLSSLVSRnllsYLVVDEAHCVSQWGHDFRPDYLR-LGA 162
|
170 180 190
....*....|....*....|....*....|.
gi 488390370 157 VMTLPQDFVVIALTATATTEVQRDIMDKLYI 187
Cdd:cd18014 163 LRSRYGHVPWVALTATATPQVQEDIFAQLRL 193
|
|
| DpdF |
NF041063 |
protein DpdF; |
1-333 |
2.76e-41 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 159.69 E-value: 2.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 1 MEAILSHYFGYQSFR-PGQKEiitkilAHHNVL----G-----VLPTGGGKSICYQIPGL---KLGGTTVVISPLISLMK 67
Cdd:NF041063 127 GDPFLAEALGFTHYRsPGQRE------AVRAALlappGstlivNLPTGSGKSLVAQAPALlasRQGGLTLVVVPTVALAI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 68 DQVDQLKAMGIHA--------AYlNSSLSQKQQKQIEQELASGKIQFLYVAPErfenqyflSILRKL-----------EI 128
Cdd:NF041063 201 DQERRARELLRRAgpdlggplAW-HGGLSAEERAAIRQRIRDGTQRILFTSPE--------SLTGSLrpalfdaaeagLL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 129 HLIAFDEAHCISKWGHDFRPSYQnviqkvmTLP-------------QDFVVIALTATATTEvQRDIMDKLYiSADNRVKT 195
Cdd:NF041063 272 RYLVVDEAHLVDQWGDGFRPEFQ-------LLAglrrsllrlapsgRPFRTLLLSATLTES-TLDTLETLF-GPPGPFIV 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 196 stkrrnlifkVN-------PTY---------QRQKFVLDYVqAHRDEAGIIYCSTRKQVEELQEAIQSIDLE-AAIYHAG 258
Cdd:NF041063 343 ----------VSavqlrpePAYwvakcdseeERRERVLEAL-RHLPRPLILYVTKVEDAEAWLQRLRAAGFRrVALFHGD 411
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488390370 259 LSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLYSERD 333
Cdd:NF041063 412 TPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDD 486
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
15-179 |
1.84e-28 |
|
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: 111.18 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 15 RPGQKEIITKILAHHNVLGVLPTGGGKSICYQIPGLKL------GGTTVVISPLISLMKDQVDQLKAMGIHAAY-LNSSL 87
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAldkldnGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 88 SQKQQKQIEQELAsgKIQFLYVAPERFenQYFLSILRKLE-IHLIAFDEAHCISKWGhdFRPSYQNVIQKvmtLPQDFVV 166
Cdd:pfam00270 81 GGDSRKEQLEKLK--GPDILVGTPGRL--LDLLQERKLLKnLKLLVLDEAHRLLDMG--FGPDLEEILRR---LPKKRQI 151
|
170
....*....|...
gi 488390370 167 IALTATATTEVQR 179
Cdd:pfam00270 152 LLLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
7-203 |
7.60e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 102.18 E-value: 7.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 7 HYFGYQSFRPGQKEIITKILAH-HNVLGVLPTGGGKSICYQIPGLKL-----GGTTVVISPLISLMKDQVDQLKAMGIHA 80
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 81 AYLNSSL-SQKQQKQIEQELASGKIQFLYVAPERFENQYFLSILRKLEIHLIAFDEAHCISKWGhdFRPSYQNVIQKvmt 159
Cdd:smart00487 82 GLKVVGLyGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKL--- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488390370 160 LPQDFVVIALTATATTEVQRDImdKLYISADNRVKTSTKRRNLI 203
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLL--ELFLNDPVFIDVGFTPLEPI 198
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
214-320 |
9.25e-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: 98.82 E-value: 9.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 214 KFVLDYVQAHRDEAGIIYCSTRKQVEElQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSN 293
Cdd:pfam00271 4 EALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
|
90 100
....*....|....*....|....*..
gi 488390370 294 VRYVIHYNMPGDLESYYQEAGRAGRDG 320
Cdd:pfam00271 83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
239-320 |
9.62e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 94.97 E-value: 9.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 239 EELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGR 318
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 488390370 319 DG 320
Cdd:smart00490 81 AG 82
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
402-478 |
6.08e-22 |
|
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: 90.23 E-value: 6.08e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488390370 402 DMTKEAKMIVSCVARMRQQENYSVIIQVLRGEQSDYIKYNHYDQLSTYGIMKAYTTSELSHLIDELRFKGFLNEHNE 478
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGG 77
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
171-336 |
2.62e-20 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 93.67 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 171 ATATTEVQR---DIMDK-LYISADNRVKTSTKRRNLIFKVNPtYQRQKFVLDYVQAHRDEAGIIYCSTRKQVEELQEAIQ 246
Cdd:COG0513 184 ATMPPEIRKlakRYLKNpVRIEVAPENATAETIEQRYYLVDK-RDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQ 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 247 SIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECI 326
Cdd:COG0513 263 KRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAI 342
|
170
....*....|
gi 488390370 327 LLYSERDKGL 336
Cdd:COG0513 343 SLVTPDERRL 352
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
200-329 |
3.07e-20 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 86.79 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 200 RNLIFKVNPTYQRQKFVLDYVQAHRDEAGIIYCSTRKQVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVV 279
Cdd:cd18787 2 KQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488390370 280 VATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLY 329
Cdd:cd18787 82 VATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
15-316 |
8.04e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 83.92 E-value: 8.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 15 RPGQKEIITKILA-----HHNVLGVLPTGGGKSI----CYQipGLKLGGTTVVISPLISLMKDQVDQLKAmgihaaYLNS 85
Cdd:COG1061 82 RPYQQEALEALLAalergGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRR------FLGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 86 SLSQKQQKQIEQELASGKIQFLYVAP--ERFENQYflsilrkleiHLIAFDEAHciskwgHDFRPSYQNVIQKvmtLPQD 163
Cdd:COG1061 154 PLAGGGKKDSDAPITVATYQSLARRAhlDELGDRF----------GLVIIDEAH------HAGAPSYRRILEA---FPAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 164 FVvIALTATATTEVQRDIMDKLYI-----------SADNRVK---------TSTKRRNLIFKVNPTYQR---------QK 214
Cdd:COG1061 215 YR-LGLTATPFRSDGREILLFLFDgivyeyslkeaIEDGYLAppeyygirvDLTDERAEYDALSERLREalaadaerkDK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 215 FVLDYVQAHRD-EAGIIYCSTRKQVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSN 293
Cdd:COG1061 294 ILRELLREHPDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPR 373
|
330 340
....*....|....*....|....
gi 488390370 294 VRYVIhYNMP-GDLESYYQEAGRA 316
Cdd:COG1061 374 LDVAI-LLRPtGSPREFIQRLGRG 396
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
28-172 |
1.25e-16 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 77.06 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 28 HHNVLGVLPTGGGKSICYQIP----GLKLGGTTVVISPLISLMKDQVDQLKA---MGIHAAYLNSSLSQKQQKQIEQELA 100
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAalllLLKKGKKVLVLVPTKALALQTAERLRElfgPGIRVAVLVGGSSAEEREKNKLGDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488390370 101 sgkiQFLYVAPERFENQY-FLSILRKLEIHLIAFDEAHCISKWGHDFRPSYQNVIQKVMTLPQdfvVIALTAT 172
Cdd:cd00046 81 ----DIIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQ---VILLSAT 146
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
399-473 |
1.38e-16 |
|
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: 75.65 E-value: 1.38e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488390370 399 KTYDMTKEAKMIVSCVARMRQQENYSVIIQVLRGEQSDYIKYNHYDQLSTYGIMKAYTTSELSHLIDELRFKGFL 473
Cdd:pfam09382 3 ETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYL 77
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
120-346 |
1.76e-16 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 82.53 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 120 LSILRKLEIHL-----IAFDEAHCISKWGhdFRpsyQNVIQKVMTLPQDFVVIaLTATATTEVQR--DIMDK--LYISAD 190
Cdd:PLN00206 258 IDLLSKHDIELdnvsvLVLDEVDCMLERG--FR---DQVMQIFQALSQPQVLL-FSATVSPEVEKfaSSLAKdiILISIG 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 191 NRVKTSTKRRNLIFKVNPTYQRQK-FVLDYVQAHRDEAGIIYCSTRKQVEELQEAIQSID-LEAAIYHAGLSNKEREQAQ 268
Cdd:PLN00206 332 NPNRPNKAVKQLAIWVETKQKKQKlFDILKSKQHFKPPAVVFVSSRLGADLLANAITVVTgLKALSIHGEKSMKERREVM 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488390370 269 NDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLYSERDKGLHEYFISVSQA 346
Cdd:PLN00206 412 KSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKS 489
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
518-585 |
7.30e-16 |
|
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: 72.18 E-value: 7.30e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488390370 518 DRALYNELVDVRKQLSNKLGIAPVSIFSDYTLEEFAKRKPASKQEMIAIEGVGSYKLKHYCPNFLERI 585
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
229-328 |
1.18e-15 |
|
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: 74.22 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 229 IIYCSTRKQVEELQEAIQSIDLEA-------AIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYN 301
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEgplaskvASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*..
gi 488390370 302 MPGDLESYYQEAGRAGRDGLKSECILL 328
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
2-341 |
4.46e-14 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 74.93 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 2 EAILSHY--FGYQSFRPGQKEIITK-ILAHHNVLGVLPTGGGKS------ICYQipgLKLGGTTVVISPLISL----MKD 68
Cdd:COG1204 9 EKVIEFLkeRGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTliaelaILKA---LLNGGKALYIVPLRALasekYRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 69 QVDQLKAMGIHAAylnssLSQKQQKQIEQELASGKIqflYVA-PERFenqyfLSILRK-----LEIHLIAFDEAHCIskw 142
Cdd:COG1204 86 FKRDFEELGIKVG-----VSTGDYDSDDEWLGRYDI---LVAtPEKL-----DSLLRNgpswlRDVDLVVVDEAHLI--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 143 GHDFR-PSYQNVIQKVMTLPQDFVVIALTATAT-TEVQRDIMD-KLYISADNRVKTST---KRRNLIFKvnPTYQRQKFV 216
Cdd:COG1204 150 DDESRgPTLEVLLARLRRLNPEAQIVALSATIGnAEEIAEWLDaELVKSDWRPVPLNEgvlYDGVLRFD--DGSRRSKDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 217 -LDYVQAHRDEAG--IIYCSTRK-----------------------QVEELQEAIQSIDLE--------------AAIYH 256
Cdd:COG1204 228 tLALALDLLEEGGqvLVFVSSRRdaeslakkladelkrrltpeereELEELAEELLEVSEEthtnekladclekgVAFHH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 257 AGLSNKER---EQAqndFVYDRIKVVVATNAFGMGIdksN--VRYVI------HYNMPGDLESYYQEAGRAGRDGLKSE- 324
Cdd:COG1204 308 AGLPSELRrlvEDA---FREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAGRPGYDPYg 381
|
410 420
....*....|....*....|
gi 488390370 325 ---CILLYSERDKGLHEYFI 341
Cdd:COG1204 382 eaiLVAKSSDEADELFERYI 401
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
229-334 |
2.33e-12 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 69.08 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 229 IIYCSTRKQVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLES 308
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100
....*....|....*....|....*.
gi 488390370 309 YYQEAGRAGRDGLKSECILLYSERDK 334
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDI 376
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
229-328 |
3.32e-12 |
|
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: 64.50 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 229 IIYCSTRKQVEELQEAIQSIdleaAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGID--------KSNVRYVIHY 300
Cdd:cd18795 47 LVFCSSRKECEKTAKDLAGI----AFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKG 122
|
90 100 110
....*....|....*....|....*....|
gi 488390370 301 NMPGDLESYYQEAGRAGRDGL--KSECILL 328
Cdd:cd18795 123 YRELSPLEYLQMIGRAGRPGFdtRGEAIIM 152
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
18-320 |
1.96e-11 |
|
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: 66.78 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 18 QKEIITKILAHHNVLGVLPTGGGKSICYQIPGL-----KLGGTTVVISPLISLMKDQVDQLKAM---------------- 76
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLealleDPGATALYLYPTKALARDQLRRLRELaealglgvrvatydgd 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 77 ---------------------GIHAAYLNSSlsqkqqkqieqelasgkiqflyvapERFenQYFLSILRkleihLIAFDE 135
Cdd:COG1205 141 tppeerrwirehpdivltnpdMLHYGLLPHH-------------------------TRW--ARFFRNLR-----YVVIDE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 136 AHciskwghdfrpSYQ--------NVI---QKVMT-LPQDFVVIALTAT-------AT-------TEVQRDimdklyisa 189
Cdd:COG1205 189 AH-----------TYRgvfgshvaNVLrrlRRICRhYGSDPQFILASATignpaehAErltgrpvTVVDED--------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 190 dnrvkTSTK-RRNLIFkVNP----TYQRQ-------KFVLDYVQAHRdeAGIIYCSTRKQVE----ELQEAIQSIDLEAA 253
Cdd:COG1205 249 -----GSPRgERTFVL-WNPplvdDGIRRsalaeaaRLLADLVREGL--RTLVFTRSRRGAEllarYARRALREPDLADR 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488390370 254 I--YHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVI--HYnmPGDLESYYQEAGRAGRDG 320
Cdd:COG1205 321 VaaYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVlaGY--PGTRASFWQQAGRAGRRG 389
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
517-588 |
2.08e-11 |
|
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: 60.00 E-value: 2.08e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488390370 517 VDRALYNELVDVRKQLSNKLGIAPVSIFSDYTLEEFAKRKPASKQEMIAIEGVGSYKLKHYCPNFLERIQSY 588
Cdd:smart00341 3 RQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEA 74
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
272-329 |
6.36e-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: 58.48 E-value: 6.36e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488390370 272 VYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDG-LKSECILLY 329
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
332-394 |
1.43e-09 |
|
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: 54.22 E-value: 1.43e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488390370 332 RDKGLHEYFISVSQADDDYKDKMGEKLTKMLQY-TKTKKCLEATIVHYFEPNEKLEECQQCSNC 394
Cdd:pfam16124 2 QDVVRLRFLIEQSEADEERKEVELQKLQAMVAYcENTTDCRRKQLLRYFGEEFDSEPCGNCDNC 65
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
10-336 |
4.01e-09 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 59.48 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 10 GYQSFRPGQKEIITKILAHHNVLGVLPTGGGKSICYQIPGLKlggttvVISPliSLMKDQVDQL---KAMGIHAAYLNSS 86
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLH------NLDP--ELKAPQILVLaptRELAVQVAEAMTD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 87 LSQKQQKQIEQELASGkiqflyvapERFENQyfLSILR-----------KLEIHL------------IAFDEAHCISKWG 143
Cdd:PRK11634 97 FSKHMRGVNVVALYGG---------QRYDVQ--LRALRqgpqivvgtpgRLLDHLkrgtldlsklsgLVLDEADEMLRMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 144 hdFRPSYQNVIQKVMTLPQDFVVIALTATATTEVQRDIMDKlyiSADNRVKTSTKRRNLIFKVNPT---YQRQKFVLDYV 220
Cdd:PRK11634 166 --FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKE---PQEVRIQSSVTTRPDISQSYWTvwgMRKNEALVRFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 221 QAHRDEAGIIYCSTRKQVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHY 300
Cdd:PRK11634 241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 488390370 301 NMPGDLESYYQEAGRAGRDGLKSECILLYSERDKGL 336
Cdd:PRK11634 321 DIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRL 356
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
216-318 |
6.71e-09 |
|
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: 54.96 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 216 VLDYVQAHRDEagIIYCSTRKQVE----ELQEA--IQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGI 289
Cdd:cd18796 31 VIFLLERHKST--LVFTNTRSQAErlaqRLRELcpDRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGI 108
|
90 100
....*....|....*....|....*....
gi 488390370 290 DKSNVRYVIHYNMPGDLESYYQEAGRAGR 318
Cdd:cd18796 109 DIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
229-322 |
7.25e-09 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 58.63 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 229 IIYCSTRKQVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLES 308
Cdd:PTZ00110 381 LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIED 460
|
90
....*....|....
gi 488390370 309 YYQEAGRAGRDGLK 322
Cdd:PTZ00110 461 YVHRIGRTGRAGAK 474
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
226-336 |
3.42e-08 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 56.10 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 226 EAGIIYCSTRKQVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGD 305
Cdd:PRK11192 246 TRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRS 325
|
90 100 110
....*....|....*....|....*....|.
gi 488390370 306 LESYYQEAGRAGRDGLKSECILLYSERDKGL 336
Cdd:PRK11192 326 ADTYLHRIGRTGRAGRKGTAISLVEAHDHLL 356
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
1-333 |
5.68e-08 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 55.30 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 1 MEAIlsHYFGYQSFRPGQKEIITKILAHHNVLGVLPTGGGKSICYQI-----------PGLKLGGT--TVVISP----LI 63
Cdd:PRK01297 99 MHAI--HDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLIsiinqllqtppPKERYMGEprALIIAPtrelVV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 64 SLMKDQVDQLKAMGIHaayLNSSLSQKQQKQIEQELASGKIQFLYVAPERFenqyfLSILRKLEIHL-----IAFDEAHC 138
Cdd:PRK01297 177 QIAKDAAALTKYTGLN---VMTFVGGMDFDKQLKQLEARFCDILVATPGRL-----LDFNQRGEVHLdmvevMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 139 ISKWGhdFRPSYQNVIQKvmTLPQ-DFVVIALTATATTEV----QRDIMDKLYISADNRVKTSTKRRNLIFKVNPTyQRQ 213
Cdd:PRK01297 249 MLDMG--FIPQVRQIIRQ--TPRKeERQTLLFSATFTDDVmnlaKQWTTDPAIVEIEPENVASDTVEQHVYAVAGS-DKY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 214 KFVLDYVQAHRDEAGIIYCSTRKQVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSN 293
Cdd:PRK01297 324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 488390370 294 VRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLYSERD 333
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
233-341 |
8.40e-07 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 51.88 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 233 STRKQVEELQEAIQSidlEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMG--------IDKSNVRYVIHYNM-P 303
Cdd:PRK02362 290 SDTETSKDLADCVAK---GAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGlnlparrvIIRDYRRYDGGAGMqP 366
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 488390370 304 GDLESYYQEAGRAGRDGLK--SECILL---YSERDKgLHEYFI 341
Cdd:PRK02362 367 IPVLEYHQMAGRAGRPGLDpyGEAVLLaksYDELDE-LFERYI 408
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
229-318 |
1.02e-06 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 51.82 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 229 IIYCSTRKQVEELQEAIQsidLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFG----------------MGIDKS 292
Cdd:COG1202 431 IIFTNSRRRCHEIARALG---YKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAagvdfpasqvifdslaMGIEWL 507
|
90 100
....*....|....*....|....*.
gi 488390370 293 NVRyvihynmpgdleSYYQEAGRAGR 318
Cdd:COG1202 508 SVQ------------EFHQMLGRAGR 521
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
229-328 |
6.80e-06 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 48.65 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 229 IIYCSTRKQVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLES 308
Cdd:PRK10590 249 LVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPED 328
|
90 100
....*....|....*....|
gi 488390370 309 YYQEAGRAGRDGLKSECILL 328
Cdd:PRK10590 329 YVHRIGRTGRAAATGEALSL 348
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
10-341 |
2.78e-05 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 47.12 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 10 GYQSFRPGQKEIITK-ILAHHNVLGVLPTGGGKSICYQIPG----LKLGGTTVVISPLISLMKDQVDQLK---AMGIHAA 81
Cdd:PRK00254 20 GIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMvnklLREGGKAVYLVPLKALAEEKYREFKdweKLGLRVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 82 YLNSSLSQKQQKQieqelasGKIQFLYVAPERFEnqyflSILRK-----LEIHLIAFDEAHCISKwgHDFRPSYQNVIQK 156
Cdd:PRK00254 100 MTTGDYDSTDEWL-------GKYDIIIATAEKFD-----SLLRHgsswiKDVKLVVADEIHLIGS--YDRGATLEMILTH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 157 VMTLPQdfvVIALTATA--TTEVQRDIMDKLYISADNRVKTstkRRNLIFKVNPTYQRQK----------FVLDYVQahR 224
Cdd:PRK00254 166 MLGRAQ---ILGLSATVgnAEELAEWLNAELVVSDWRPVKL---RKGVFYQGFLFWEDGKierfpnswesLVYDAVK--K 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 225 DEAGIIYCSTRKQVE----ELQEAIQSI--------------DLE---------------AAIYHAGLSNKEREQAQNDF 271
Cdd:PRK00254 238 GKGALVFVNTRRSAEkealELAKKIKRFltkpelralkeladSLEenptneklkkalrggVAFHHAGLGRTERVLIEDAF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 272 VYDRIKVVVATNAFGMGIDKSNVRYVIHynmpgDLESY-------------YQEAGRAGR---DGLKSECILLYSERDKG 335
Cdd:PRK00254 318 REGLIKVITATPTLSAGINLPAFRVIIR-----DTKRYsnfgwedipvleiQQMMGRAGRpkyDEVGEAIIVATTEEPSK 392
|
....*.
gi 488390370 336 LHEYFI 341
Cdd:PRK00254 393 LMERYI 398
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
127-320 |
6.09e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 46.03 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 127 EIHLIAFDEAHCIskwGHDFR-PSYQNVIQKVMTLPQDFVVIALTATATTEVQ--------------RDIMDKLYISADN 191
Cdd:PRK01172 135 DVGLIVADEIHII---GDEDRgPTLETVLSSARYVNPDARILALSATVSNANElaqwlnasliksnfRPVPLKLGILYRK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 192 RVKTSTKRR-----NLIFK------------VNPTYQRQKFVLDYVQAHRDEAGIIYCSTRKQV--EELQEAIQSidlEA 252
Cdd:PRK01172 212 RLILDGYERsqvdiNSLIKetvndggqvlvfVSSRKNAEDYAEMLIQHFPEFNDFKVSSENNNVydDSLNEMLPH---GV 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488390370 253 AIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSnVRYVIHYNMP--GDLESYY-------QEAGRAGRDG 320
Cdd:PRK01172 289 AFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP-ARLVIVRDITryGNGGIRYlsnmeikQMIGRAGRPG 364
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
12-188 |
6.72e-05 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 43.85 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 12 QSFRPGQKEIITKILaHHNVLGVLPTGGGKSICYQIPGLKL-----GGTTVVISPLISLMKDQVDQ-LKAMGI---HAAY 82
Cdd:cd18033 1 VPLRDYQFTIVQKAL-FQNTLVALPTGLGKTFIAAVVMLNYyrwfpKGKIVFMAPTKPLVSQQIEAcYKITGIpssQTAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 83 LNSSLSQKQQKQIeqeLASGKIQFLyvAPERFENQYFLSILRKLEIHLIAFDEAHCISKwghdfRPSYQNVIQKVMTLPQ 162
Cdd:cd18033 80 LTGSVPPTKRAEL---WASKRVFFL--TPQTLENDLKEGDCDPKSIVCLVIDEAHRATG-----NYAYCQVVRELMRYNS 149
|
170 180
....*....|....*....|....*...
gi 488390370 163 DFVVIALTAT--ATTEVQRDIMDKLYIS 188
Cdd:cd18033 150 HFRILALTATpgSKLEAVQQVIDNLLIS 177
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
18-75 |
9.17e-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: 43.34 E-value: 9.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488390370 18 QKEIITKILAHHNVLGVLPTGGGKSICYQIPGL-----KLGGTTVVISPLISLMKDQVDQLKA 75
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeallrDPGSRALYLYPTKALAQDQLRSLRE 67
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
13-172 |
1.08e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 43.04 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 13 SFRPGQKEIITKILA-----HHNVLGVLPTGGGKS-----ICYQIPGLKLGGTTVVISPLISLMKDQVDQLKAMGIHAAY 82
Cdd:pfam04851 3 ELRPYQIEAIENLLEsikngQKRGLIVMATGSGKTltaakLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 83 LNSSLS----QKQQKQIEQELASgkIQFLYVAPERFENQYFlsilrKLEIHLIAFDEAHciskwgHDFRPSYQNVIQKVm 158
Cdd:pfam04851 83 IGEIISgdkkDESVDDNKIVVTT--IQSLYKALELASLELL-----PDFFDVIIIDEAH------RSGASSYRNILEYF- 148
|
170
....*....|....
gi 488390370 159 tlpQDFVVIALTAT 172
Cdd:pfam04851 149 ---KPAFLLGLTAT 159
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
13-185 |
3.01e-04 |
|
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: 42.42 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 13 SFRPGQKEIITKILAHHNVLGVLPTGGGKS-----IC----YQIPGlKLGGTTVVISPLISLMKDQVDQLKAMGIHAAYL 83
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPA-GRKGKVVFLANKVPLVEQQKEVFRKHFERPGYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 84 NSSLSQKQQKQIEQELASGKIQFLYVAPERFENQYFLSILRKLE-IHLIAFDEAHCISKWGhdfrpSYQNVI-----QKV 157
Cdd:cd17927 81 VTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSdFSLLVFDECHNTTKNH-----PYNEIMfryldQKL 155
|
170 180
....*....|....*....|....*...
gi 488390370 158 MTLPQDFVVIALTATATTEVQRDIMDKL 185
Cdd:cd17927 156 GSSGPLPQILGLTASPGVGGAKNTEEAL 183
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
13-173 |
5.18e-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: 41.09 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 13 SFRPGQKEIITKI-LAHHNVLGVLPTGGGKSICYQIPGLKL----GGTTVVISPLISLMKDQVDQLKAMGIHaayLNSSL 87
Cdd:cd17921 1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRAlatsGGKAVYIAPTRALVNQKEADLRERFGP---LGKNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 88 SQKQQKQIEQELASGKIQFLYVAPERFENQ-YFLSILRKLEIHLIAFDEAHCIskwGHDFR-PSYQNVIQKVMTLPQDFV 165
Cdd:cd17921 78 GLLTGDPSVNKLLLAEADILVATPEKLDLLlRNGGERLIQDVRLVVVDEAHLI---GDGERgVVLELLLSRLLRINKNAR 154
|
....*...
gi 488390370 166 VIALTATA 173
Cdd:cd17921 155 FVGLSATL 162
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
239-329 |
5.72e-04 |
|
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: 40.79 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 239 EELQEAIQSiDLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGID--KSNVRYVIHYNMPGdLESYYQEAGRA 316
Cdd:cd18811 52 EYLKERFRP-ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDvpNATVMVIEDAERFG-LSQLHQLRGRV 129
|
90
....*....|...
gi 488390370 317 GRDGLKSECILLY 329
Cdd:cd18811 130 GRGDHQSYCLLVY 142
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
14-137 |
9.14e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 39.98 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 14 FRPGQKEIITKILAHHN----VLgVLPTGGGKSICyqipGLKL-----GGTTVVISPLISLMKDQVDQLKAMGIHAA-YL 83
Cdd:cd17926 1 LRPYQEEALEAWLAHKNnrrgIL-VLPTGSGKTLT----ALALiaylkELRTLIVVPTDALLDQWKERFEDFLGDSSiGL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 488390370 84 NSSLSQKQQKQIEQELASGKIQFLYVAPERFENQYFLsilrkleihLIAFDEAH 137
Cdd:cd17926 76 IGGGKKKDFDDANVVVATYQSLSNLAEEEKDLFDQFG---------LLIVDEAH 120
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
133-321 |
2.76e-03 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 40.69 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 133 FDEAHCISkwghD-FR-PSYQNVIqkvMTLPQDFVVIALTATA--TTEVQRDIMDklyISADNRVKTSTKR--------- 199
Cdd:COG4581 139 MDEFHYLA----DpDRgWVWEEPI---IHLPARVQLVLLSATVgnAEEFAEWLTR---VRGETAVVVSEERpvplefhyl 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 200 ----RNLIFKVNPTYQRQKFVLDYVQA--HRDEAGIIY-------C------------STRKQVEELQEAIQ--SIDLEA 252
Cdd:COG4581 209 vtprLFPLFRVNPELLRPPSRHEVIEEldRGGLLPAIVfifsrrgCdeaaqqllsarlTTKEERAEIREAIDefAEDFSV 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 253 AIY--------------HAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIdksnvryvihyNMP-------------G- 304
Cdd:COG4581 289 LFGktlsrllrrgiavhHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGI-----------NMPartvvftklskfdGe 357
|
250 260
....*....|....*....|..
gi 488390370 305 ---DLES--YYQEAGRAGRDGL 321
Cdd:COG4581 358 rhrPLTAreFHQIAGRAGRRGI 379
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
236-329 |
3.04e-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: 38.79 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 236 KQVEELQEAIQSI--DLEAAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVI--HYNMPGdLESYYQ 311
Cdd:cd18792 45 KSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIieDADRFG-LSQLHQ 123
|
90
....*....|....*...
gi 488390370 312 EAGRAGRDGLKSECILLY 329
Cdd:cd18792 124 LRGRVGRGKHQSYCYLLY 141
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
194-318 |
3.20e-03 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350176 [Multi-domain] Cd Length: 153 Bit Score: 38.38 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 194 KTSTKRRNLIFKVNPT-YQRQKFVLDYvqaHRD-EAGIIYCSTRKQVEELQEAIqsidLEAAIYHAgLSNKEREQAQNDF 271
Cdd:cd18789 19 LGAHRKRRLLAAMNPNkLRALEELLKR---HEQgDKIIVFTDNVEALYRYAKRL----LKPFITGE-TPQSEREEILQNF 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488390370 272 VYDRIKVVVATNAFGMGID--KSNVRYVI--HYNmpgdleSYYQEAGRAGR 318
Cdd:cd18789 91 REGEYNTLVVSKVGDEGIDlpEANVAIQIsgHGG------SRRQEAQRLGR 135
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
252-333 |
3.55e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 40.68 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 252 AAIYHAGLSNKEREQAQNDFVYDRIKVVVATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRD--GLKSECILLY 329
Cdd:PRK09751 304 ARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQvgGVSKGLFFPR 383
|
....
gi 488390370 330 SERD 333
Cdd:PRK09751 384 TRRD 387
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
214-326 |
3.72e-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: 37.84 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 214 KFVLDYVQAHRDEAG--IIYCSTRKQVEELQEAIQSIDLEAAIYHAGLSNKEREQAQNDF--VYDRIKVVVATNAFGMGI 289
Cdd:cd18793 14 EALLELLEELREPGEkvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFneDPDIRVFLLSTKAGGVGL 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488390370 290 DKSNVRYVIHY----NmPGDLEsyyQEAGRAGRDGLKSECI 326
Cdd:cd18793 94 NLTAANRVILYdpwwN-PAVEE---QAIDRAHRIGQKKPVV 130
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
2-60 |
4.11e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 39.91 E-value: 4.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488390370 2 EAILSHYFGYQSFRPGQKEIITKI---LAHHNVLgVL--PTGGGKSICYQIPGLKL---GGTTVVIS 60
Cdd:COG1199 3 DGLLALAFPGFEPRPGQREMAEAVaraLAEGRHL-LIeaGTGTGKTLAYLVPALLAareTGKKVVIS 68
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
230-321 |
4.34e-03 |
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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: 37.92 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390370 230 IYCSTRKQVEELQEAI-QSIDLEAAIYHAGLSNKER-EQAQ--NDFVYDrIKVVVATNAFGMGIDkSNVRYVIHY----- 300
Cdd:cd18805 22 VVAFSRKDIFSLKREIeKRTGLKCAVIYGALPPETRrQQARlfNDPESG-YDVLVASDAIGMGLN-LNIRRVIFSslskf 99
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90 100
....*....|....*....|....*
gi 488390370 301 --NMPGDLESYY--QEAGRAGRDGL 321
Cdd:cd18805 100 dgNEMRPLSPSEvkQIAGRAGRFGS 124
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