|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-469 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 778.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 1 MPTAHEILKSVFGYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPALMFKGITVVISPLISLMKDQVDALNANG 80
Cdd:COG0514 2 RDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 81 IGADALNSNNEEGENAAIRQRCKAGQTKILYISPERLQRE--IPWLQQhLSISLFAIDEAHCISQWGHDFRPEYTQLGML 158
Cdd:COG0514 82 IRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPrfLELLRR-LKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 159 HQAFPSATIMALTATADKLTKEDIVRQLNLRDFRLFVSSFDRPNLSLDVRRGYSAsEKLKAILSIISKHKHESGIIYCLS 238
Cdd:COG0514 161 RERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPD-DKLAQLLDFLKEHPGGSGIVYCLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 239 RKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIG 318
Cdd:COG0514 240 RKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 319 RAGRDGLPSETVLFYNFQDIITLRKFVNDS----GQRDINSEKLDRMQEYAESQVCRRRILLNYFGENNSSNCGNCDICK 394
Cdd:COG0514 320 RAGRDGLPAEALLLYGPEDVAIQRFFIEQSppdeERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCL 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504358324 395 HPPQRFNGTILVQKALSAIKRTGEHIGFSMTADILKGTLSDEIVQKGYNKLKTFGVGSKTTLKHWHDYLLQMLQL 469
Cdd:COG0514 400 GPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
4-611 |
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: 713.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 4 AHEILKSVFGYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPALMFKGITVVISPLISLMKDQVDALNANGIGA 83
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 84 DALNSNNEEGENAAIRQRCKAGQTKILYISPERLqrEIPWLQQHLS---ISLFAIDEAHCISQWGHDFRPEYTQLGMLHQ 160
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERL--EQDYFLNMLQripIALVAVDEAHCVSQWGHDFRPEYQRLGSLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 161 AFPSATIMALTATADKLTKEDIVRQLNLRDFRLFVSSFDRPNLSLDVRRGYSaseKLKAILSIISKHKHESGIIYCLSRK 240
Cdd:TIGR01389 159 RFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNN---KQKFLLDYLKKHRGQSGIIYASSRK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 241 STEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRA 320
Cdd:TIGR01389 236 KVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 321 GRDGLPSETVLFYNFQDIITLRKFVNDS----GQRDINSEKLDRMQEYAESQVCRRRILLNYFGENNSSNCGNCDICKHP 396
Cdd:TIGR01389 316 GRDGLPAEAILLYSPADIALLKRRIEQSeaddDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 397 PQRFNGTILVQKALSAIKRTGEHIGFSMTADILKGTLSDEIVQKGYNKLKTFGVGSKTTLKHWHDYLLQMLQLGYIEIAY 476
Cdd:TIGR01389 396 PKSYDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTEND 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 477 NENNHLKITESGNEVLFGKktaelaiaakaEAKEDAKPRSSRTSFNRSGNSHTTyahssaddAEDNSLFEALRKVRRQIA 556
Cdd:TIGR01389 476 EIYIGLQLTEAARKVLKNE-----------VEVLLRPFKVVAKEKTRVQKNLSV--------GVDNALFEALRELRKEQA 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 504358324 557 DENNWPAYVVLSDRTLRDLAYKAPTSINELQDVSGFGEMKIRKFGQQFVDAIRDY 611
Cdd:TIGR01389 537 DEQNVPPYVIFSDSTLREMAEKRPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
1-612 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 662.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 1 MPTAHEILKSVFGYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPALMFKGITVVISPLISLMKDQVDALNANG 80
Cdd:PRK11057 10 ESLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 81 IGADALNSNNEEGENAAIRQRCKAGQTKILYISPERLQREiPWLQQ--HLSISLFAIDEAHCISQWGHDFRPEYTQLGML 158
Cdd:PRK11057 90 VAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMD-NFLEHlaHWNPALLAVDEAHCISQWGHDFRPEYAALGQL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 159 HQAFPSATIMALTATADKLTKEDIVRQLNLRDFRLFVSSFDRPNLSldvrrgYSASEKLK---AILSIISKHKHESGIIY 235
Cdd:PRK11057 169 RQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIR------YTLVEKFKpldQLMRYVQEQRGKSGIIY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 236 CLSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQ 315
Cdd:PRK11057 243 CNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 316 EIGRAGRDGLPSETVLFYNFQDIITLRKFVN---DSGQRDINSEKLDRMQEYAESQVCRRRILLNYFGENNSSNCGNCDI 392
Cdd:PRK11057 323 ETGRAGRDGLPAEAMLFYDPADMAWLRRCLEekpAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 393 CKHPPQRFNGTILVQKALSAIKRTGEHIGFSMTADILKGTLSDEIVQKGYNKLKTFGVGSKTTLKHWHDYLLQMLQLGYI 472
Cdd:PRK11057 403 CLDPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 473 EIAYNENNHLKITESGNEVLFGKktaeLAIAAKAEAKEDAKPRSSRTSFNRSgnshttYahssaddaeDNSLFEALRKVR 552
Cdd:PRK11057 483 TQNIAQHSALQLTEAARPVLRGE----VSLQLAVPRIVALKPRAMQKSFGGN------Y---------DRKLFAKLRKLR 543
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 553 RQIADENNWPAYVVLSDRTLRDLAYKAPTSINELQDVSGFGEMKIRKFGQQFVDAIRDYM 612
Cdd:PRK11057 544 KSIADEENIPPYVVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAHV 603
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
7-451 |
0e+00 |
|
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: 575.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 7 ILKSVFGYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPALMFKGITVVISPLISLMKDQVDALNANGIGADAL 86
Cdd:TIGR00614 2 ILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 87 NSNNEEGENAAIRQRCKAGQTKILYISPERLQREIPWLQQ---HLSISLFAIDEAHCISQWGHDFRPEYTQLGMLHQAFP 163
Cdd:TIGR00614 82 NSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNRLLQTleeRKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 164 SATIMALTATADKLTKEDIVRQLNLRDFRLFVSSFDRPNLSLDVRRGYS-ASEKLKAIlsIISKHKHESGIIYCLSRKST 242
Cdd:TIGR00614 162 NVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPkILEDLLRF--IRKEFEGKSGIIYCPSRKKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 243 EKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAGR 322
Cdd:TIGR00614 240 EQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 323 DGLPSETVLFYNFQDIITLRKFV---NDSGQRDINSEKLDRMQEYAESQVCRRRILLNYFGE--NNSSN--------CGN 389
Cdd:TIGR00614 320 DGLPSECHLFYAPADMNRLRRLLmeePDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEkgFNKSFcimgtekcCDN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504358324 390 CDICK------HPPQRFNGTILVQKALSAIKRTGEHIGFSMTADILKGTLSDEIVQKGYNKLKTFGVG 451
Cdd:TIGR00614 400 CCKRLdyktkdVTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRG 467
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
9-614 |
2.68e-126 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 400.81 E-value: 2.68e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 9 KSVFGYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPALMFKGITVVISPLISLMKDQVDALNANGIGADALNS 88
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 89 NNEEGENAAIRQRCKAGQTK--ILYISPER------LQREIPWLQQHLSISLFAIDEAHCISQWGHDFRPEYTQLGMLHQ 160
Cdd:PLN03137 533 GMEWAEQLEILQELSSEYSKykLLYVTPEKvaksdsLLRHLENLNSRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 161 AFPSATIMALTATADKLTKEDIVRQLNLRDFRLFVSSFDRPNLsldvrrGYSASEKLKAILSIISK-----HKHESGIIY 235
Cdd:PLN03137 613 KFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNL------WYSVVPKTKKCLEDIDKfikenHFDECGIIY 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 236 CLSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQ 315
Cdd:PLN03137 687 CLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQ 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 316 EIGRAGRDGLPSETVLFYNFQDIITLRKFV----------------NDSGQR--DINSEKLDRMQEYAESQV-CRRRILL 376
Cdd:PLN03137 767 ECGRAGRDGQRSSCVLYYSYSDYIRVKHMIsqggveqspmamgynrMASSGRilETNTENLLRMVSYCENEVdCRRFLQL 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 377 NYFGEN-NSSNCGN-CDICKhppqrfNGTILVQKALSAI--------KRTGEHIGFSMTADILKGTLSDEIVQKGYNKLK 446
Cdd:PLN03137 847 VHFGEKfDSTNCKKtCDNCS------SSKSLIDKDVTEIarqlvelvKLTGERFSSAHILEVYRGSLNQYVKKHRHETLS 920
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 447 TFGVGSKTT-------LKHW--HDYLLQMLQLGyiEIAYNENNHLKITESGNEVLF-GKKTA-----ELAIAAKAEAKED 511
Cdd:PLN03137 921 LHGAGKHLSkgeasriLHYLvtEDILAEDVKKS--DLYGSVSSLLKVNESKAYKLFsGGQTIimrfpSSVKASKPSKFEA 998
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 512 AKPRSSRTSFNRSGNSHTTYAHSSADDAEDNSLFEALRKVRRQIADE--NNWPAYVVLSDRTLRDLAYKAPTSINELQDV 589
Cdd:PLN03137 999 TPAKGPLTSGKQSTLPMATPAQPPVDLNLSAILYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEI 1078
|
650 660
....*....|....*....|....*
gi 504358324 590 SGFGEMKIRKFGQQFVDAIRDYMNQ 614
Cdd:PLN03137 1079 NGLGKAKVSKYGDRLLETIESTINE 1103
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
5-199 |
8.73e-108 |
|
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: 322.56 E-value: 8.73e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 5 HEILKSVFGYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPALMFKGITVVISPLISLMKDQVDALNANGIGAD 84
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 85 ALNSNNEEGENAAIRQRCKAGQTKILYISPERLQREIPW-----LQQHLSISLFAIDEAHCISQWGHDFRPEYTQLGMLH 159
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLellqrLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504358324 160 QAFPSATIMALTATADKLTKEDIVRQLNLRDFRLFVSSFD 199
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
5-190 |
4.57e-76 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 240.62 E-value: 4.57e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 5 HEILKSVFGYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPALMFK----GITVVISPLISLMKDQVDALNAnG 80
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPR-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 81 IGADALNSNNEEGENAAIRQRCKAGQTKILYISPERLQRE--IPWLQQHLSISLFAIDEAHCISQWGHDFRPEYTQLG-M 157
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNEsfRELLRQTPPISLLVVDEAHCISEWSHNFRPDYLRLCrV 159
|
170 180 190
....*....|....*....|....*....|...
gi 504358324 158 LHQAFPSATIMALTATADKLTKEDIVRQLNLRD 190
Cdd:cd18018 160 LRELLGAPPVLALTATATKRVVEDIASHLGIPE 192
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
6-199 |
8.18e-69 |
|
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: 222.24 E-value: 8.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 6 EILKSVFGYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPALMFKGITVVISPLISLMKDQVDALNANGIGADA 85
Cdd:cd18015 8 DTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 86 LNSNNEEGENAAIRQRC--KAGQTKILYISPERL---QREIPWLQQHLSI---SLFAIDEAHCISQWGHDFRPEYTQLGM 157
Cdd:cd18015 88 LNASSSKEHVKWVHAALtdKNSELKLLYVTPEKIaksKRFMSKLEKAYNAgrlARIAIDEVHCCSQWGHDFRPDYKKLGI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504358324 158 LHQAFPSATIMALTATADKLTKEDIVRQLNLRDFRLFVSSFD 199
Cdd:cd18015 168 LKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
200-333 |
2.47e-66 |
|
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: 212.84 E-value: 2.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 200 RPNLSLDVRRGYSASEKLKAILSIISKHKHESGIIYCLSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDN 279
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504358324 280 INVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAGRDGLPSETVLFY 333
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
8-199 |
2.09e-64 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 210.02 E-value: 2.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 8 LKSVFGYDAFRPMQEEIIEHVV-SGKDALVLMPTGGGKSICYQIPALMFKGITVVISPLISLMKDQVDALNANGIGADAL 86
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 87 NSNNEEGEnaaiRQRCKAGQTKILYISPERLQREIPWLQQ-HLSISLFAIDEAHCISQWGHDFRPEYTQLGMLHQAFPSA 165
Cdd:cd18017 84 GSAQSQNV----LDDIKMGKIRVIYVTPEFVSKGLELLQQlRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLPNV 159
|
170 180 190
....*....|....*....|....*....|....
gi 504358324 166 TIMALTATADKLTKEDIVRQLNLRDFRLFVSSFD 199
Cdd:cd18017 160 PIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
6-199 |
1.13e-62 |
|
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: 205.83 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 6 EILKSVFGYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPALMFKGITVVISPLISLMKDQVDALNANGIGADA 85
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 86 LNSNNEEGENAAIRQRCKAGQ--TKILYISPE------RLQREIPWLQQHLSISLFAIDEAHCISQWGHDFRPEYTQLGM 157
Cdd:cd18016 87 LTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEkisasnRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPDYKRLNM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504358324 158 LHQAFPSATIMALTATADKLTKEDIVRQLNLRDFRLFVSSFD 199
Cdd:cd18016 167 LRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
5-189 |
2.88e-61 |
|
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: 202.32 E-value: 2.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 5 HEILKSVFGYDAFR-PMQEEIIEHVVSGK-DALVLMPTGGGKSICYQIPALMFKGITVVISPLISLMKDQVDALNANGIG 82
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 83 ADALNSNNEEGENAAIRQ--RCKAGQTKILYISPER-----LQREIPWLQQHLSISLFAIDEAHCISQWGHDFRPEYTQL 155
Cdd:cd18014 81 VDSLNSKLSAQERKRIIAdlESEKPQTKFLYITPEMaatssFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....
gi 504358324 156 GMLHQAFPSATIMALTATADKLTKEDIVRQLNLR 189
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLK 194
|
|
| DpdF |
NF041063 |
protein DpdF; |
7-358 |
7.16e-50 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 185.50 E-value: 7.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 7 ILKSVFGYDAFR-PMQEEIIEHVVS---GKDALVLMPTGGGKSICYQIPALMFK---GITVVISPLISLMKDQVDAL--- 76
Cdd:NF041063 130 FLAEALGFTHYRsPGQREAVRAALLappGSTLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALAIDQERRArel 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 77 ----NANGIGADALNSNNEEGENAAIRQRCKAGQTKILYISPERLQREipwLQQHL-------SISLFAIDEAHCISQWG 145
Cdd:NF041063 210 lrraGPDLGGPLAWHGGLSAEERAAIRQRIRDGTQRILFTSPESLTGS---LRPALfdaaeagLLRYLVVDEAHLVDQWG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 146 HDFRPEYTQLGMLHQAFPSA-------TIMALTATadkLTKEdivrQLN-LRD-------FRLFVSSFDRPNLSLDVRRG 210
Cdd:NF041063 287 DGFRPEFQLLAGLRRSLLRLapsgrpfRTLLLSAT---LTES----TLDtLETlfgppgpFIVVSAVQLRPEPAYWVAKC 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 211 YSASEKLKAILSIISkHKHESGIIYCLSRKSTEKVAEELINAGvYAK--AYHAGLTAEERNNVQEDFINDNINVVCATIA 288
Cdd:NF041063 360 DSEEERRERVLEALR-HLPRPLILYVTKVEDAEAWLQRLRAAG-FRRvaLFHGDTPDAERERLIEQWRENELDIVVATSA 437
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 289 FGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAGRDGLPSETVLFYNFQDIITlrkfvndsgQRDINSEKL 358
Cdd:NF041063 438 FGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDI---------AKSLNRPKL 498
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
18-176 |
1.63e-30 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 117.34 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 18 RPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPAL------MFKGITVVISPLISLMKDQVDALNANGIGADaLNSNNE 91
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLG-LKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 92 EGENAAIRQRCKAGQTKILYISPERLQREIPWLQQHLSISLFAIDEAHCISQWGhdFRPEYTQlgMLHQAFPSATIMALT 171
Cdd:pfam00270 80 LGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEE--ILRRLPKKRQILLLS 155
|
....*
gi 504358324 172 ATADK 176
Cdd:pfam00270 156 ATLPR 160
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
396-496 |
2.06e-27 |
|
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: 106.47 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 396 PPQRFNGTILVQKALSAIKRTGEHIGFSMTADILKGTLSDEIVQKGYNKLKTFGVGSKTTLKHWHDYLLQMLQLGYIEIA 475
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|.
gi 504358324 476 YNENNHLKITESGNEVLFGKK 496
Cdd:pfam09382 81 IEFYSVLKLTPKAREVLKGEE 101
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
401-492 |
1.17e-26 |
|
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: 103.71 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 401 NGTILVQKALSAIKRTGEHIGFSMTADILKGTLSDEIVQKGYNKLKTFGVGSKTTLKHWHDYLLQMLQLGYIEIAYNENN 480
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 504358324 481 HLKITESGNEVL 492
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
12-208 |
1.06e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 104.88 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 12 FGYDAFRPMQEEIIEHVVSG-KDALVLMPTGGGKSICYQIPALMF-----KGITVVISPLISLMKDQVDALNANGIGADA 85
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 86 LNSNNEEGEN-AAIRQRCKAGQTKILYISPERLQREIPWLQQHLS-ISLFAIDEAHCISQWGhdFRPEYTQLgmLHQAFP 163
Cdd:smart00487 84 KVVGLYGGDSkREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSnVDLVILDEAHRLLDGG--FGDQLEKL--LKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504358324 164 SATIMALTATADKLTKEDIVRQLNLrdfRLFVSSFDRPNLSLDVR 208
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLND---PVFIDVGFTPLEPIEQF 201
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
243-324 |
5.67e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 93.05 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 243 EKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAGR 322
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 504358324 323 DG 324
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
215-324 |
2.92e-22 |
|
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: 91.89 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 215 EKLKAILSIISKHKHESGIIYCLSRKSTEkvAEELINAGVY-AKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGI 293
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKEGIkVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 504358324 294 DKSNVRYVIHYNLPKSIESFYQEIGRAGRDG 324
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
335-394 |
1.60e-20 |
|
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
Pssm-ID: 465031 [Multi-domain] Cd Length: 66 Bit Score: 85.42 E-value: 1.60e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504358324 335 FQDIITLRKFVNDSG----QRDINSEKLDRMQEYAESQV-CRRRILLNYFGEN-NSSNCGNCDICK 394
Cdd:pfam16124 1 YQDVVRLRFLIEQSEadeeRKEVELQKLQAMVAYCENTTdCRRKQLLRYFGEEfDSEPCGNCDNCL 66
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
541-608 |
3.79e-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: 84.51 E-value: 3.79e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504358324 541 DNSLFEALRKVRRQIADENNWPAYVVLSDRTLRDLAYKAPTSINELQDVSGFGEMKIRKFGQQFVDAI 608
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
216-322 |
1.46e-19 |
|
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: 84.87 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 216 KLKAILSIISKHKHESGIIYCLSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDK 295
Cdd:cd18787 14 KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDI 93
|
90 100
....*....|....*....|....*..
gi 504358324 296 SNVRYVIHYNLPKSIESFYQEIGRAGR 322
Cdd:cd18787 94 PGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
2-325 |
1.96e-19 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 91.88 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 2 PTAHEILKSvFGYDAFRPMQEEIIE-HVVSGKDALVLMPTGGGKSICYQIPAL--MFKGITVV-ISPLISL----MKDQV 73
Cdd:COG1204 9 EKVIEFLKE-RGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLRALasekYREFK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 74 DALNANGIGADALNSNNEEGENAAIRQRckagqtkILYISPERLQ----REIPWLQQhlsISLFAIDEAHCIsqwGHDFR 149
Cdd:COG1204 88 RDFEELGIKVGVSTGDYDSDDEWLGRYD-------ILVATPEKLDsllrNGPSWLRD---VDLVVVDEAHLI---DDESR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 150 peytqlGM--------LHQAFPSATIMALTATADKLtkEDIVRQLNLrdfRLFVSSFdRPN-LSLDVRRGYS------AS 214
Cdd:COG1204 155 ------GPtlevllarLRRLNPEAQIVALSATIGNA--EEIAEWLDA---ELVKSDW-RPVpLNEGVLYDGVlrfddgSR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 215 EKLKAILSIISKHKHESG--IIYCLSRKSTEKVAEELINA---------------------------------------G 253
Cdd:COG1204 223 RSKDPTLALALDLLEEGGqvLVFVSSRRDAESLAKKLADElkrrltpeereeleelaeellevseethtnekladclekG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 254 VyakAYH-AGLTAEERNNVQEDFINDNINVVCAT--IAFGMgidksN--VRYVI------HYNLPKSIESFYQEIGRAGR 322
Cdd:COG1204 303 V---AFHhAGLPSELRRLVEDAFREGLIKVLVATptLAAGV-----NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAGR 374
|
...
gi 504358324 323 DGL 325
Cdd:COG1204 375 PGY 377
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
18-367 |
4.52e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 90.85 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 18 RPMQEEIIEHVVS-----GKDALVLMPTGGGKSI----CYQipALMFKGITVVISPLISLMKDQVDALnangigADALNs 88
Cdd:COG1061 82 RPYQQEALEALLAalergGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEEL------RRFLG- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 89 nneegeNAAIRQRCKAGQTKILYISPERLQR--EIPWLQQHlsISLFAIDEAHcisqwgHDFRPEYTQLGmlhQAFPSAT 166
Cdd:COG1061 153 ------DPLAGGGKKDSDAPITVATYQSLARraHLDELGDR--FGLVIIDEAH------HAGAPSYRRIL---EAFPAAY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 167 IMALTAT---ADKLTKE--------------DIVRQLNLRDFRLFV---------SSFDRPNLSLDVRRGYSASEKLKAI 220
Cdd:COG1061 216 RLGLTATpfrSDGREILlflfdgivyeyslkEAIEDGYLAPPEYYGirvdltderAEYDALSERLREALAADAERKDKIL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 221 LSIISKH-KHESGIIYCLSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVR 299
Cdd:COG1061 296 RELLREHpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLD 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 300 YVIHYNLPKSIESFYQEIGRAGRDGLPSETVLFYNF--QDIITLRKFVNDSGQRDINSEKLDRMQEYAES 367
Cdd:COG1061 376 VAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDFvgNDVPVLEELAKDLRDLAGYRVEFLDEEESEEL 445
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
13-343 |
2.44e-18 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 88.31 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 13 GYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPALMF-------------KGITVVISP---LISLMKDQVDAL 76
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcctirsghpseqrNPLAMVLTPtreLCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 77 -------NANGIGADALNsnneegenaaiRQ--RCKAGQTKILYiSPERLqreIPWLQQH----LSISLFAIDEAHCISQ 143
Cdd:PLN00206 220 gkglpfkTALVVGGDAMP-----------QQlyRIQQGVELIVG-TPGRL---IDLLSKHdielDNVSVLVLDEVDCMLE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 144 WGhdFRPEYTQLgmlHQAFPSATIMALTAT--------ADKLTKEDIVrqlnlrdfrLFVSSFDRPNLSLD-VRRGYSAS 214
Cdd:PLN00206 285 RG--FRDQVMQI---FQALSQPQVLLFSATvspevekfASSLAKDIIL---------ISIGNPNRPNKAVKqLAIWVETK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 215 EKLKAILSIISKHKH--ESGIIYCLSRKSTEKVAEEL-INAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGM 291
Cdd:PLN00206 351 QKKQKLFDILKSKQHfkPPAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGR 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 504358324 292 GIDKSNVRYVIHYNLPKSIESFYQEIGRAGRDGLPSETVLFYN------FQDIITLRK 343
Cdd:PLN00206 431 GVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNeedrnlFPELVALLK 488
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
21-331 |
4.03e-18 |
|
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: 88.35 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 21 QEEIIEHVVSGKDALVLMPTGGGKSICYQIPAL--MFKGIT---VVISPLISLMKDQVDALNA------NGIGADALNSN 89
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLEDPGataLYLYPTKALARDQLRRLRElaealgLGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 90 NEEGENAAIRQRCKagqtkILYISPERLQREIpwLQQHLSISLF-------AIDEAHcisqwghdfrpEYT-----QLGM 157
Cdd:COG1205 141 TPPEERRWIREHPD-----IVLTNPDMLHYGL--LPHHTRWARFfrnlryvVIDEAH-----------TYRgvfgsHVAN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 158 L----------HQAFP-----SATIMALTATADKLTKedivrqlnlRDFRL------------FVssFDRPNLSLDVRRG 210
Cdd:COG1205 203 VlrrlrricrhYGSDPqfilaSATIGNPAEHAERLTG---------RPVTVvdedgsprgertFV--LWNPPLVDDGIRR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 211 YSASEkLKAILSIISKHKHeSGIIYCLSRKSTEKVA----EELINAGVYAK--AYHAGLTAEERNNVQEDFINDNINVVC 284
Cdd:COG1205 272 SALAE-AARLLADLVREGL-RTLVFTRSRRGAELLAryarRALREPDLADRvaAYRAGYLPEERREIERGLRSGELLGVV 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 504358324 285 ATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAGRDGLPSETVL 331
Cdd:COG1205 350 STNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
212-373 |
9.24e-18 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 85.97 E-value: 9.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 212 SASEKLKAILSIISKHKHESGIIYCLSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCAT-IAfG 290
Cdd:COG0513 224 DKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-A 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 291 MGIDKSNVRYVIHYNLPKSIESFYQEIG---RAGRDGlpsETVLFYNFQDIITLRKFVNDSGQRdINSEKLDRMQEYAES 367
Cdd:COG0513 303 RGIDIDDVSHVINYDLPEDPEDYVHRIGrtgRAGAEG---TAISLVTPDERRLLRAIEKLIGQK-IEEEELPGFEPVEEK 378
|
....*.
gi 504358324 368 QVCRRR 373
Cdd:COG0513 379 RLERLK 384
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
233-331 |
7.94e-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: 71.90 E-value: 7.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 233 IIYCLSRKSTEKVA----EELINAGVYAK---AYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRYVIHYN 305
Cdd:cd18797 39 IVFCRSRKLAELLLrylkARLVEEGPLASkvaSYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*.
gi 504358324 306 LPKSIESFYQEIGRAGRDGLPSETVL 331
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
192-325 |
1.27e-14 |
|
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: 71.43 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 192 RLFVSSFDRPNLSLDVRRGYSASEKLKAILSIISKHKHESGIIYCLSRKSTEKVAEELINAGVYakayHAGLTAEERNNV 271
Cdd:cd18795 6 EEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLAGIAFH----HAGLTREDRELV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504358324 272 QEDFINDNINVVCATIAFGMGID--------KSNVRYVIHYNLPKSIESFYQEIGRAGRDGL 325
Cdd:cd18795 82 EELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKGYRELSPLEYLQMIGRAGRPGF 143
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
31-173 |
5.67e-14 |
|
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: 69.35 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 31 GKDALVLMPTGGGKSICYQIPA----LMFKGITVVISPLISLMKDQ---VDALNANGIGADALNSnneeGENAAIRQRCK 103
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAAllllLKKGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVG----GSSAEEREKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504358324 104 AGQTKILYISPERLQREIPWLQQH--LSISLFAIDEAHCISQWGHDFRPEYtqLGMLHQAFPSATIMALTAT 173
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLREDRLflKDLKLIIVDEAHALLIDSRGALILD--LAVRKAGLKNAQVILLSAT 146
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
540-611 |
2.40e-12 |
|
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: 62.70 E-value: 2.40e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504358324 540 EDNSLFEALRKVRRQIADENNWPAYVVLSDRTLRDLAYKAPTSINELQDVSGFGEMKIRKFGQQFVDAIRDY 611
Cdd:smart00341 3 RQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEA 74
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
13-332 |
6.55e-12 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 68.34 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 13 GYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPAL-----MFKGITV-VISPLISLMKDQVDALN-----ANGI 81
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpELKAPQIlVLAPTRELAVQVAEAMTdfskhMRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 82 GADALNSnneeGENAAIRQRCKAGQTKILYISPERLQREIPWLQQHLS-ISLFAIDEAHCISQWG--HDFRPEYTQLGML 158
Cdd:PRK11634 105 NVVALYG----GQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSkLSGLVLDEADEMLRMGfiEDVETIMAQIPEG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 159 HQ-AFPSATI-MALTATADKLTKEDivrqlnlRDFRLFVSSFDRPNLSLDVRRGYSAsEKLKAILSIISKHKHESGIIYC 236
Cdd:PRK11634 181 HQtALFSATMpEAIRRITRRFMKEP-------QEVRIQSSVTTRPDISQSYWTVWGM-RKNEALVRFLEAEDFDAAIIFV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 237 LSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQE 316
Cdd:PRK11634 253 RTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHR 332
|
330
....*....|....*.
gi 504358324 317 IGRAGRDGLPSETVLF 332
Cdd:PRK11634 333 IGRTGRAGRAGRALLF 348
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
130-343 |
8.43e-12 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 67.16 E-value: 8.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 130 ISLFAIDEAHCISQWG-----HD-FR--PEYTQLGMLHQAFPSaTIMALTATADKLTKEDIVRQ--LNLRDFRLFVSSFD 199
Cdd:PTZ00424 171 LKLFILDEADEMLSRGfkgqiYDvFKklPPDVQVALFSATMPN-EILELTTKFMRDPKRILVKKdeLTLEGIRQFYVAVE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 200 RPNLSLDVRRgysaseKLKAILSIISkhkhesGIIYCLSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDN 279
Cdd:PTZ00424 250 KEEWKFDTLC------DLYETLTITQ------AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504358324 280 INVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAGRDGLPSETVLFYNFQDIITLRK 343
Cdd:PTZ00424 318 TRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKE 381
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
227-335 |
2.87e-10 |
|
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: 58.81 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 227 HKHESGIIYCLSRKSTEKVAEELINAGVYAK------AYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRY 300
Cdd:cd18796 36 ERHKSTLVFTNTRSQAERLAQRLRELCPDRVppdfiaLHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDL 115
|
90 100 110
....*....|....*....|....*....|....*
gi 504358324 301 VIHYNLPKSIESFYQEIGRAGRDglPSETVLFYNF 335
Cdd:cd18796 116 VIQIGSPKSVARLLQRLGRSGHR--PGAASKGRLV 148
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
14-332 |
1.01e-09 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 61.66 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 14 YDAFRPMQEEIIEHVVSGKDALVLMPTGGGKS-----------ICYQIPALMFKGITVV-ISPLISLMKDQVDALNA--N 79
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlaaflpaldelARRPRPGELPDGLRVLyISPLKALANDIERNLRAplE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 80 GIGADAlnsnneeGEN--------------AAIRQRckagQTK----ILYISPERLqreipwlqqHLSIS------LFA- 134
Cdd:COG1201 102 EIGEAA-------GLPlpeirvgvrtgdtpASERQR----QRRrpphILITTPESL---------ALLLTspdareLLRg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 135 -----IDEAH--CISQWGhdfrpeyTQLgMLH----QAF--PSATIMALTATADKLtkEDI----VRQLNLRDFRLFVSS 197
Cdd:COG1201 162 vrtviVDEIHalAGSKRG-------VHL-ALSlerlRALapRPLQRIGLSATVGPL--EEVarflVGYEDPRPVTIVDAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 198 FDRPnLSLDV------------RRGYSASEKLKAILSIISKHKheSGIIYCLSRKSTEKVAEEL--INAGVY--AKAYHA 261
Cdd:COG1201 232 AGKK-PDLEVlvpvedlierfpWAGHLWPHLYPRVLDLIEAHR--TTLVFTNTRSQAERLFQRLneLNPEDAlpIAAHHG 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504358324 262 GLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAG-RDGLPSETVLF 332
Cdd:COG1201 309 SLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEVSKGRLV 380
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
233-322 |
9.67e-09 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 58.36 E-value: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 233 IIYCLSRKSTEKVAEELinaGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGID--KSNvryVIHYNLPKSI 310
Cdd:COG1202 431 IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDfpASQ---VIFDSLAMGI 504
|
90
....*....|....*..
gi 504358324 311 E-----SFYQEIGRAGR 322
Cdd:COG1202 505 EwlsvqEFHQMLGRAGR 521
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
7-324 |
1.27e-08 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 57.86 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 7 ILKSVF--GYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPA--------LMFKG---ITVVISPLISLmkdqv 73
Cdd:PTZ00110 141 ILKSLKnaGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPTREL----- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 74 dalnANGIGADAlnsnNEEGENAAIRQRC------KAGQT-------KILYISPERLqreIPWLQQHLS----ISLFAID 136
Cdd:PTZ00110 216 ----AEQIREQC----NKFGASSKIRNTVayggvpKRGQIyalrrgvEILIACPGRL---IDFLESNVTnlrrVTYLVLD 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 137 EAHCISQWGhdFRPEYTQLgmLHQAFPSATIMALTAT--------ADKLTKEDIVrQLNLRDFRLFVSSFDRPNLslDVR 208
Cdd:PTZ00110 285 EADRMLDMG--FEPQIRKI--VSQIRPDRQTLMWSATwpkevqslARDLCKEEPV-HVNVGSLDLTACHNIKQEV--FVV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 209 RGYSASEKLKAILSIISKHKHESgIIYCLSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIA 288
Cdd:PTZ00110 358 EEHEKRGKLKMLLQRIMRDGDKI-LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDV 436
|
330 340 350
....*....|....*....|....*....|....*.
gi 504358324 289 FGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAGRDG 324
Cdd:PTZ00110 437 ASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
21-324 |
1.33e-08 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 57.97 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 21 QEEIIEHVVSGKDALVLMPTGGGKSIC--YQIPALMFKGI-TVVISPLISL-MKDQVDALNANGIGADALNSNNEEGENA 96
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIaySAIYETFLAGLkSIYIVPLRSLaMEKYEELSRLRSLGMRVKISIGDYDDPP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 97 AIRQRckagqTKILYISPER---LQREIPWLQQhlSISLFAIDEAHCISQWGHDFRPEyTQLGMLHQAFPSATIMALTAT 173
Cdd:PRK01172 107 DFIKR-----YDVVILTSEKadsLIHHDPYIIN--DVGLIVADEIHIIGDEDRGPTLE-TVLSSARYVNPDARILALSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 174 ADKLTkeDIVRQLN----LRDFR---LFVSSFDRPNLSLDvrrGYSASEKlkAILSIISKHKHESG--IIYCLSRKSTEK 244
Cdd:PRK01172 179 VSNAN--ELAQWLNasliKSNFRpvpLKLGILYRKRLILD---GYERSQV--DINSLIKETVNDGGqvLVFVSSRKNAED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 245 VAEELI--------------NAGVYAKA-----------YHAGLTAEERNNVQEDFINDNINVVCATIAFGMGID----- 294
Cdd:PRK01172 252 YAEMLIqhfpefndfkvsseNNNVYDDSlnemlphgvafHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNlparl 331
|
330 340 350
....*....|....*....|....*....|...
gi 504358324 295 ---KSNVRYVIHYNLPKSIESFYQEIGRAGRDG 324
Cdd:PRK01172 332 vivRDITRYGNGGIRYLSNMEIKQMIGRAGRPG 364
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
13-332 |
2.24e-08 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 56.84 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 13 GYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQI-----------PALMFKG--ITVVISP----LISLMKDQVDA 75
Cdd:PRK01297 106 GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLIsiinqllqtppPKERYMGepRALIIAPtrelVVQIAKDAAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 76 LNANGIGADALNSNNEEGENaaiRQRCKAGQTKILYISPERL----QREIPWLQQhlsISLFAIDEAHCISQWGhdFRPE 151
Cdd:PRK01297 186 TKYTGLNVMTFVGGMDFDKQ---LKQLEARFCDILVATPGRLldfnQRGEVHLDM---VEVMVLDEADRMLDMG--FIPQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 152 YTQLgmLHQAFPSA---TIM-ALTATADKLtkeDIVRQLNLRDFRLFVSSFDRPNLSLDVR-RGYSASEKLKAILSIISK 226
Cdd:PRK01297 258 VRQI--IRQTPRKEerqTLLfSATFTDDVM---NLAKQWTTDPAIVEIEPENVASDTVEQHvYAVAGSDKYKLLYNLVTQ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 227 HKHESGIIYCLSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRYVIHYNL 306
Cdd:PRK01297 333 NPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTL 412
|
330 340
....*....|....*....|....*.
gi 504358324 307 PKSIESFYQEIGRAGRDGLPSETVLF 332
Cdd:PRK01297 413 PEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
17-173 |
2.97e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 53.44 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 17 FRPMQEE----IIEHVVSG-KDALVLMPTGGGKSICY-QIPALMFK----GITVVISPLISLMKDQVDALNANGIGADAL 86
Cdd:pfam04851 4 LRPYQIEaienLLESIKNGqKRGLIVMATGSGKTLTAaKLIARLFKkgpiKKVLFLVPRKDLLEQALEEFKKFLPNYVEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 87 NSNNEEGENAAIRQrckagQTKILYISPERLQREIPWLQQHLSIS---LFAIDEAHcisqwgHDFRPEYTQlgmLHQAFP 163
Cdd:pfam04851 84 GEIISGDKKDESVD-----DNKIVVTTIQSLYKALELASLELLPDffdVIIIDEAH------RSGASSYRN---ILEYFK 149
|
170
....*....|
gi 504358324 164 SATIMALTAT 173
Cdd:pfam04851 150 PAFLLGLTAT 159
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
280-333 |
1.16e-07 |
|
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: 49.24 E-value: 1.16e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 504358324 280 INVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAGRDG-LPSETVLFY 333
Cdd:cd18785 23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
6-322 |
1.00e-06 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 51.35 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 6 EILKSVF--GYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPALMFkgitvvisplisLMKDQVDALNANGIGA 83
Cdd:PRK10590 11 DILRAVAeqGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQH------------LITRQPHAKGRRPVRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 84 DALNSNNEE----GENAA-------IR------------QRCK-AGQTKILYISPERL-----QREIPWLQqhlsISLFA 134
Cdd:PRK10590 79 LILTPTRELaaqiGENVRdyskylnIRslvvfggvsinpQMMKlRGGVDVLVATPGRLldlehQNAVKLDQ----VEILV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 135 IDEAHCISQWG--HDFRPEYTQL-----GMLHQAFPSATIMALtatADKLtkedivrqlnlrdfrlfvssFDRPnLSLDV 207
Cdd:PRK10590 155 LDEADRMLDMGfiHDIRRVLAKLpakrqNLLFSATFSDDIKAL---AEKL--------------------LHNP-LEIEV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 208 RRGYSASEKLKAILSIISKHKHESGIIYCLSRKSTEKV-------------AEELINAGVYAKAYHAGLTAEERNNVQED 274
Cdd:PRK10590 211 ARRNTASEQVTQHVHFVDKKRKRELLSQMIGKGNWQQVlvftrtkhganhlAEQLNKDGIRSAAIHGNKSQGARTRALAD 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504358324 275 FINDNINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAGR 322
Cdd:PRK10590 291 FKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
216-324 |
1.05e-06 |
|
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: 48.24 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 216 KLKAILSIISKHKHESG--IIYCLSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFIND-NINVV-CATIAFGM 291
Cdd:cd18793 12 KLEALLELLEELREPGEkvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVFlLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|....*
gi 504358324 292 GIDKSNVRYVIHYNLP--KSIESfyQEIGRAGRDG 324
Cdd:cd18793 92 GLNLTAANRVILYDPWwnPAVEE--QAIDRAHRIG 124
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
21-139 |
1.97e-06 |
|
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: 48.35 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 21 QEEIIEHVVSGKDALVLMPTGGGKSICYQIPAL----MFKGIT-VVISPLISLMKDQVDALNA------NGIGADALNSN 89
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeallRDPGSRaLYLYPTKALAQDQLRSLRElleqlgLGIRVATYDGD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 504358324 90 NEEGENAAIRQRckagQTKILYISPERL--------QREIPWLQqhlSISLFAIDEAH 139
Cdd:cd17923 85 TPREERRAIIRN----PPRILLTNPDMLhyallphhDRWARFLR---NLRYVVLDEAH 135
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
216-324 |
3.95e-06 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 49.56 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 216 KLKAILSIISKHKHESGIIYCLSRKSTEKVAEELINAGVYAkAYHAG-LTAEERNNVQEDFINDNINVVCATIAFGMGID 294
Cdd:PRK11192 232 KTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINC-CYLEGeMVQAKRNEAIKRLTDGRVNVLVATDVAARGID 310
|
90 100 110
....*....|....*....|....*....|
gi 504358324 295 KSNVRYVIHYNLPKSIESFYQEIGRAGRDG 324
Cdd:PRK11192 311 IDDVSHVINFDMPRSADTYLHRIGRTGRAG 340
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
552-610 |
1.95e-05 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 47.17 E-value: 1.95e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 504358324 552 RRQIADENNWPAYVVLSDRTLRDLAYKAPTSINELQDVSGFGEMKIRKFGQQFVDAIRD 610
Cdd:COG0349 220 REREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAE 278
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
14-321 |
2.47e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 47.57 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 14 YDAFRPMQEEIIEHVVSGKDALVLMPTGGGK------SICYQIPALMFKG-----ITVV-ISPLISLMKDQVDALNA--N 79
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKtlaaflAIIDELFRLGREGeledkVYCLyVSPLRALNNDIHRNLEEplT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 80 GIGADALNSNNEEGEnaaIRQRCKAGQTK-------------ILYISPERLQ------------REIPWL---------- 124
Cdd:PRK13767 110 EIREIAKERGEELPE---IRVAIRTGDTSsyekqkmlkkpphILITTPESLAillnspkfreklRTVKWVivdeihslae 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 125 ---QQHLSISLFAIDEAHcisqwGHDFrpeyTQLGMlhqafpSATIMALTATADKLT-KEDIVRQlnlRDFRLFVSSFDR 200
Cdd:PRK13767 187 nkrGVHLSLSLERLEELA-----GGEF----VRIGL------SATIEPLEEVAKFLVgYEDDGEP---RDCEIVDARFVK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 201 PnlsLDVRRG-------YSASEKL-KAILSIISKH--KHESGIIYCLSRKSTEKVA------------EELInagvyaKA 258
Cdd:PRK13767 249 P---FDIKVIspvddliHTPAEEIsEALYETLHELikEHRTTLIFTNTRSGAERVLynlrkrfpeeydEDNI------GA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504358324 259 YHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAG 321
Cdd:PRK13767 320 HHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
6-53 |
9.00e-05 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, 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: 350698 [Multi-domain] Cd Length: 201 Bit Score: 43.83 E-value: 9.00e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 504358324 6 EILKSVF--GYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPAL 53
Cdd:cd17940 9 ELLMGIFekGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPIL 58
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
256-333 |
1.13e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 45.30 E-value: 1.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504358324 256 AKAYHAGLTAEERNNVQEDFINDNINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAGRDGLPSETVLFY 333
Cdd:PRK09751 304 ARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVGGVSKGLFF 381
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
216-322 |
1.68e-04 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 41.96 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 216 KLKAILSIISKH-------KHESGIIYCLSRKSTEKVAEELIN----------AGVYAKAYHAGLTAEERNNVQEDFIND 278
Cdd:cd18801 10 KLEKLEEIVKEHfkkkqegSDTRVIIFSEFRDSAEEIVNFLSKirpgiratrfIGQASGKSSKGMSQKEQKEVIEQFRKG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 504358324 279 NINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAGR 322
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
230-322 |
4.71e-04 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 40.24 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 230 ESGIIYCLSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNV---QEDFINDNINVVCATIAFGMGIDKSNVRYVIhynL 306
Cdd:cd18799 7 IKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV---F 83
|
90
....*....|....*....
gi 504358324 307 PKSIES---FYQEIGRAGR 322
Cdd:cd18799 84 LRPTESrtlFLQMLGRGLR 102
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
13-54 |
7.20e-04 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 41.27 E-value: 7.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 504358324 13 GYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPALM 54
Cdd:cd00268 9 GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILE 50
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
31-118 |
7.90e-04 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 40.64 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 31 GKDALVLMPTGGGK------SICYQIPALMFKGITVV-ISPLISLMKDQVDALN--ANGIGAD---ALNSnneeGE-NAA 97
Cdd:cd17922 1 GRNVLIAAPTGSGKteaaflPALSSLADEPEKGVQVLyISPLKALINDQERRLEepLDEIDLEipvAVRH----GDtSQS 76
|
90 100
....*....|....*....|.
gi 504358324 98 IRQRCKAGQTKILYISPERLQ 118
Cdd:cd17922 77 EKAKQLKNPPGILITTPESLE 97
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
214-332 |
1.01e-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: 39.88 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 214 SEKLKAILSIISKHKHESGIIYCL---SRKSTEKVAEEL----------INAGVY------AKAYHAGLTAEERNNVQED 274
Cdd:cd18802 6 IPKLQKLIEILREYFPKTPDFRGIifvERRATAVVLSRLlkehpstlafIRCGFLigrgnsSQRKRSLMTQRKQKETLDK 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 504358324 275 FINDNINVVCATIAFGMGIDKSNVRYVIHYNLPKSIESFYQEIGRAGRDGlpSETVLF 332
Cdd:cd18802 86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYILM 141
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
10-53 |
1.54e-03 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 40.25 E-value: 1.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 504358324 10 SVFGYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPAL 53
Cdd:cd17960 6 AELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVL 49
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
201-335 |
5.69e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 39.82 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 201 PNLSLDVRRGYSA-SEKLKAILSIISKHKHESG--IIYCLSRKSTEKVAEELINAGVYAKAYHAGLTAEERNNVQEDFIN 277
Cdd:COG0553 518 PALLLEEGAELSGrSAKLEALLELLEELLAEGEkvLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE 597
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504358324 278 D-NINVV-CATIAFGMGIDKSNVRYVIHYNL---PKSIEsfyQEIGRAGRDGLPsETVLFYNF 335
Cdd:COG0553 598 GpEAPVFlISLKAGGEGLNLTAADHVIHYDLwwnPAVEE---QAIDRAHRIGQT-RDVQVYKL 656
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
8-53 |
7.89e-03 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 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: 350707 [Multi-domain] Cd Length: 214 Bit Score: 38.34 E-value: 7.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 504358324 8 LKSVFGYDAFRPMQEEIIEHVVSGKDALVLMPTGGGKSICYQIPAL 53
Cdd:cd17949 5 LKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPII 50
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
259-331 |
8.36e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 39.17 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 259 YHAGLTAEERNNVQEDFINDNINVVCA--TIAFGMG------IDKSNVRYVIHYNL-PKSIESFYQEIGRAGRDGL-P-S 327
Cdd:PRK02362 309 HHAGLSREHRELVEDAFRDRLIKVISStpTLAAGLNlparrvIIRDYRRYDGGAGMqPIPVLEYHQMAGRAGRPGLdPyG 388
|
....
gi 504358324 328 ETVL 331
Cdd:PRK02362 389 EAVL 392
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
17-184 |
8.56e-03 |
|
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: 37.63 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 17 FRPMQEEIIEHVV-SGKDALVLMPTGGGKSICYQIPALM----FKGITVVISPLISL----MKDQVDALNANGIGADALN 87
Cdd:cd17921 2 LNPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRalatSGGKAVYIAPTRALvnqkEADLRERFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504358324 88 SNNEEgenaairQRCKAGQTKILYISPERLQ-----REIPWLQQhlsISLFAIDEAHCISQwghdfrPEY-----TQLGM 157
Cdd:cd17921 82 GDPSV-------NKLLLAEADILVATPEKLDlllrnGGERLIQD---VRLVVVDEAHLIGD------GERgvvleLLLSR 145
|
170 180 190
....*....|....*....|....*....|....
gi 504358324 158 LHQAFPSATIMALTAT-------ADKLTKEDIVR 184
Cdd:cd17921 146 LLRINKNARFVGLSATlpnaedlAEWLGVEDLIR 179
|
|
| |
