|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-500 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 751.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 1 MSLSAQEILQKYFGYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALLRDGVCIVISPLISLMKDQVDALKTN 80
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 81 GIAAAFLNSTQSFEEQQKILESCYKKEIALLYVSPERLISD-----ISSItsmtNPSMFVIDEAHCISAWGHDFRPEYRH 155
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPrflelLRRL----KISLFAIDEAHCISQWGHDFRPDYRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 156 IGLLRQRFSHLPFIALTATADKVTRKDIIKQLHLKDPKIFVSSFDRKNLSLDVRIGIKtKQKLEEITTFIKQNNSLCGII 235
Cdd:COG0514 157 LGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPP-DDKLAQLLDFLKEHPGGSGIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 236 YCLSRTTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYY 315
Cdd:COG0514 236 YCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 316 QEIGRAGRDGLPAATILYYNYSDLTMLNRFAAQS----GQADINLEKLKRIQHYAEADICRRKILLSYFSETLEKNCGNC 391
Cdd:COG0514 316 QEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSppdeERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNC 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 392 DVCRHPRKHFDGTLLIQKALSAMARMREKEGATMVIDVLRGSLRTDLREAGYDKLKTHGIGSDLCTSDWQRYLMQMLNLg 471
Cdd:COG0514 396 DNCLGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ- 474
|
490 500
....*....|....*....|....*....
gi 510821755 472 iiemaydenfalkstaygkeiLFGKKKAE 500
Cdd:COG0514 475 ---------------------LFGERKLE 482
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
5-595 |
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: 726.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 5 AQEILQKYFGYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALLRDGVCIVISPLISLMKDQVDALKTNGIAA 84
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 85 AFLNSTQSFEEQQKILESCYKKEIALLYVSPERLISD-ISSITSMTNPSMFVIDEAHCISAWGHDFRPEYRHIGLLRQRF 163
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDyFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 164 SHLPFIALTATADKVTRKDIIKQLHLKDPKIFVSSFDRKNLSLDVrigIKTKQKLEEITTFIKQNNSLCGIIYCLSRTTC 243
Cdd:TIGR01389 161 PQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSV---VKKNNKQKFLLDYLKKHRGQSGIIYASSRKKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 244 EEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGRAGR 323
Cdd:TIGR01389 238 EELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 324 DGLPAATILYYNYSDLTMLNRFAAQS----GQADINLEKLKRIQHYAEADICRRKILLSYFSETLEKNCGNCDVCRHPRK 399
Cdd:TIGR01389 318 DGLPAEAILLYSPADIALLKRRIEQSeaddDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 400 HFDGTLLIQKALSAMARMREKEGATMVIDVLRGSLRTDLREAGYDKLKTHGIGSDLCTSDWQRYLMQMLNLGIIEMAYDE 479
Cdd:TIGR01389 398 SYDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 480 NFALKSTAYGKEILfgKKKAELIVLPPLIKPAKTSLTTHARPVNYEDELLEQLKKVRRKFSLEEKVPAYIIFSDATLHEM 559
Cdd:TIGR01389 478 YIGLQLTEAARKVL--KNEVEVLLRPFKVVAKEKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREM 555
|
570 580 590
....*....|....*....|....*....|....*.
gi 510821755 560 ADKKPLTTSEMLSITGVGEYKFDRYGEEFLDLIGNY 595
Cdd:TIGR01389 556 AEKRPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
5-592 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 686.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 5 AQEILQKYFGYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALLRDGVCIVISPLISLMKDQVDALKTNGIAA 84
Cdd:PRK11057 13 AKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 85 AFLNSTQSFEEQQKILESCYKKEIALLYVSPERLISD--ISSITSmTNPSMFVIDEAHCISAWGHDFRPEYRHIGLLRQR 162
Cdd:PRK11057 93 ACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDnfLEHLAH-WNPALLAVDEAHCISQWGHDFRPEYAALGQLRQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 163 FSHLPFIALTATADKVTRKDIIKQLHLKDPKIFVSSFDRKNlsldVRIGIKTKQK-LEEITTFIKQNNSLCGIIYCLSRT 241
Cdd:PRK11057 172 FPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPN----IRYTLVEKFKpLDQLMRYVQEQRGKSGIIYCNSRA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 242 TCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGRA 321
Cdd:PRK11057 248 KVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 322 GRDGLPAATILYYNYSDLTMLNRF---AAQSGQADINLEKLKRIQHYAEADICRRKILLSYFSETLEKNCGNCDVCRHPR 398
Cdd:PRK11057 328 GRDGLPAEAMLFYDPADMAWLRRCleeKPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 399 KHFDGTLLIQKALSAMARMREKEGATMVIDVLRGSLRTDLREAGYDKLKTHGIGSDLCTSDWQRYLMQMLNLGIIEMAYD 478
Cdd:PRK11057 408 KQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIA 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 479 ENFALKSTAYGKEILFGKKKAELIVlpPLIKPAKTSLTTHARPVNYEDELLEQLKKVRRKFSLEEKVPAYIIFSDATLHE 558
Cdd:PRK11057 488 QHSALQLTEAARPVLRGEVSLQLAV--PRIVALKPRAMQKSFGGNYDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIE 565
|
570 580 590
....*....|....*....|....*....|....
gi 510821755 559 MADKKPLTTSEMLSITGVGEYKFDRYGEEFLDLI 592
Cdd:PRK11057 566 MAEQMPITASEMLSVNGVGQRKLERFGKPFMALI 599
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
8-454 |
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: 549.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 8 ILQKYFGYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALLRDGVCIVISPLISLMKDQVDALKTNGIAAAFL 87
Cdd:TIGR00614 2 ILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 88 NSTQSFEEQQKILESCYKKEIALLYVSPERLISD---ISSITSMTNPSMFVIDEAHCISAWGHDFRPEYRHIGLLRQRFS 164
Cdd:TIGR00614 82 NSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASnrlLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 165 HLPFIALTATADKVTRKDIIKQLHLKDPKIFVSSFDRKNLSLDVRIgiKTKQKLEEITTFI-KQNNSLCGIIYCLSRTTC 243
Cdd:TIGR00614 162 NVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRR--KTPKILEDLLRFIrKEFEGKSGIIYCPSRKKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 244 EEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGRAGR 323
Cdd:TIGR00614 240 EQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 324 DGLPAATILYYNYSDLTMLNRFAA---QSGQADINLEKLKRIQHYAEADICRRKILLSYFSETL----------EKNCGN 390
Cdd:TIGR00614 320 DGLPSECHLFYAPADMNRLRRLLMeepDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGfnksfcimgtEKCCDN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 391 CDVC------RHPRKHFDGTLLIQKALSAMARMREKEGATMVIDVLRGSLRTDLREAGYDKLKTHGIGSD 454
Cdd:TIGR00614 400 CCKRldyktkDVTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKD 469
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
10-592 |
5.80e-139 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 433.94 E-value: 5.80e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 10 QKYFGYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALLRDGVCIVISPLISLMKDQVDALKTNGIAAAFLNS 89
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 90 TQSFEEQQKILE--SCYKKEIALLYVSPER------LISDISSITSMTNPSMFVIDEAHCISAWGHDFRPEYRHIGLLRQ 161
Cdd:PLN03137 533 GMEWAEQLEILQelSSEYSKYKLLYVTPEKvaksdsLLRHLENLNSRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 162 RFSHLPFIALTATADKVTRKDIIKQLHLKDPKIFVSSFDRKNLSLDVRIgiKTKQKLEEITTFIKQNN-SLCGIIYCLSR 240
Cdd:PLN03137 613 KFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVP--KTKKCLEDIDKFIKENHfDECGIIYCLSR 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 241 TTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGR 320
Cdd:PLN03137 691 MDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGR 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 321 AGRDGLPAATILYYNYSD-----------------LTM-LNRFAAQSGQADINLEKLKRIQHYAEADI-CRRKILLSYFS 381
Cdd:PLN03137 771 AGRDGQRSSCVLYYSYSDyirvkhmisqggveqspMAMgYNRMASSGRILETNTENLLRMVSYCENEVdCRRFLQLVHFG 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 382 ETLEK-NCGN-CDVCRHPRKHFDGTL-LIQKALSAMARM-REKEGATMVIDVLRGSLRTDLREAGYDKLKTHGIGSDLCT 457
Cdd:PLN03137 851 EKFDStNCKKtCDNCSSSKSLIDKDVtEIARQLVELVKLtGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLSK 930
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 458 SDWQRYLMQMlnlgIIEMAYDENFAlKSTAYGK------------EILFGKKKAELIVLPPLIK----------PAKTSL 515
Cdd:PLN03137 931 GEASRILHYL----VTEDILAEDVK-KSDLYGSvssllkvneskaYKLFSGGQTIIMRFPSSVKaskpskfeatPAKGPL 1005
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 516 T----------THARP---VNYEDELLEQLKKVRRKFSLE--EKVPAYIIFSDATLHEMADKKPLTTSEMLSITGVGEYK 580
Cdd:PLN03137 1006 TsgkqstlpmaTPAQPpvdLNLSAILYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAK 1085
|
650
....*....|..
gi 510821755 581 FDRYGEEFLDLI 592
Cdd:PLN03137 1086 VSKYGDRLLETI 1097
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
6-200 |
7.42e-109 |
|
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: 325.26 E-value: 7.42e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 6 QEILQKYFGYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALLRDGVCIVISPLISLMKDQVDALKTNGIAAA 85
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 86 FLNSTQSFEEQQKILESCYKKEIALLYVSPERLISD-----ISSITSMTNPSMFVIDEAHCISAWGHDFRPEYRHIGLLR 160
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPdflelLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 510821755 161 QRFSHLPFIALTATADKVTRKDIIKQLHLKDPKIFVSSFD 200
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
7-201 |
5.19e-71 |
|
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: 227.52 E-value: 5.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 7 EILQKYFGYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALL----RDGVCIVISPLISLMKDQVDALKtNGI 82
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALP-RAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 83 AAAFLNSTQSFEEQQKILESCYKKEIALLYVSPERLIS-DISSITSMTNP-SMFVIDEAHCISAWGHDFRPEYRHIG-LL 159
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNeSFRELLRQTPPiSLLVVDEAHCISEWSHNFRPDYLRLCrVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510821755 160 RQRFSHLPFIALTATADKVTRKDIIKqlHLKDPKIFVSSFDR 201
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVEDIAS--HLGIPESGVVRGPL 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
5-200 |
9.41e-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: 221.86 E-value: 9.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 5 AQEILQKYFGYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALLRDGVCIVISPLISLMKDQVDALKTNGIAA 84
Cdd:cd18015 6 VKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 85 AFLNSTQSFEEQQKILESCYKK--EIALLYVSPE------RLISDISSITSMTNPSMFVIDEAHCISAWGHDFRPEYRHI 156
Cdd:cd18015 86 TMLNASSSKEHVKWVHAALTDKnsELKLLYVTPEkiakskRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRPDYKKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 510821755 157 GLLRQRFSHLPFIALTATADKVTRKDIIKQLHLKDPKIFVSSFD 200
Cdd:cd18015 166 GILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
1-200 |
6.25e-68 |
|
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: 219.70 E-value: 6.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 1 MSLSAQEILQKYFGYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALLRDGVCIVISPLISLMKDQVDALKTN 80
Cdd:cd18016 1 HSKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 81 GIAAAFLNSTQSFEEQQKILESCYKKE--IALLYVSPE------RLISDISSITSMTNPSMFVIDEAHCISAWGHDFRPE 152
Cdd:cd18016 81 DIPATYLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEkisasnRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510821755 153 YRHIGLLRQRFSHLPFIALTATADKVTRKDIIKQLHLKDPKIFVSSFD 200
Cdd:cd18016 161 YKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
201-334 |
4.73e-64 |
|
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: 206.68 E-value: 4.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 201 RKNLSLDVRIGIKTKQKLEEITTFIKQNNSLCGIIYCLSRTTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDD 280
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 510821755 281 LMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGRAGRDGLPAATILYY 334
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
9-200 |
5.27e-63 |
|
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: 206.16 E-value: 5.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 9 LQKYFGYDEFRPQQEEIINEVI-SGNDVLVLMPTGGGKSVCFQIPALLRDGVCIVISPLISLMKDQVDALKTNGIAAAFL 87
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 88 NSTQSFEEQQKILESCYKkeiaLLYVSPERLISDISSITSMTNP-SMFVIDEAHCISAWGHDFRPEYRHIGLLRQRFSHL 166
Cdd:cd18017 84 GSAQSQNVLDDIKMGKIR----VIYVTPEFVSKGLELLQQLRNGiTLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLPNV 159
|
170 180 190
....*....|....*....|....*....|....
gi 510821755 167 PFIALTATADKVTRKDIIKQLHLKDPKIFVSSFD 200
Cdd:cd18017 160 PIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
6-192 |
6.07e-60 |
|
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: 198.46 E-value: 6.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 6 QEILQKYFGYDEFR-PQQEEIINEVISGN-DVLVLMPTGGGKSVCFQIPALLRDGVCIVISPLISLMKDQVDALKTNGIA 83
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 84 AAFLNSTQSFEEQQKILES--CYKKEIALLYVSPERLISD-----ISSITSMTNPSMFVIDEAHCISAWGHDFRPEYRHI 156
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADleSEKPQTKFLYITPEMAATSsfqplLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 510821755 157 GLLRQRFSHLPFIALTATADKVTRKDIIKQLHLKDP 192
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| DpdF |
NF041063 |
protein DpdF; |
8-339 |
6.46e-42 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 162.00 E-value: 6.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 8 ILQKYFGYDEFR-PQQEEIINEVIS---GNDVLVLMPTGGGKSVCFQIPALL---RDGVCIVISPLISLMKDQVDALKtN 80
Cdd:NF041063 130 FLAEALGFTHYRsPGQREAVRAALLappGSTLIVNLPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQERRAR-E 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 81 GIAAAFLNSTQSF--------EEQQKILESCYKKEIALLYVSPErlisdiSSITSMTNP----------SMFVIDEAHCI 142
Cdd:NF041063 209 LLRRAGPDLGGPLawhgglsaEERAAIRQRIRDGTQRILFTSPE------SLTGSLRPAlfdaaeagllRYLVVDEAHLV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 143 SAWGHDFRPE------YRHiGLLRQRFSHLPF--IALTATADKVTRKDIIKQLHLKDPKIFVSS----------FDRKNl 204
Cdd:NF041063 283 DQWGDGFRPEfqllagLRR-SLLRLAPSGRPFrtLLLSATLTESTLDTLETLFGPPGPFIVVSAvqlrpepaywVAKCD- 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 205 SLDVRigiktKQKLEEittfikqnnSLCG-----IIYCLSRTTCEEVAYELKIKGIN-AGYYHAGMNARERERVQENFIN 278
Cdd:NF041063 361 SEEER-----RERVLE---------ALRHlprplILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRE 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510821755 279 DDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGRAGRDGLPAATILYYNYSDL 339
Cdd:NF041063 427 NELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDL 487
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
19-181 |
8.35e-32 |
|
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: 120.81 E-value: 8.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 19 RPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPAL------LRDGVCIVISPLISLMKDQVDALK----TNGIAAAFLN 88
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKklgkGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 89 STQSFEEQQKILescykKEIALLYVSPERLISDISSITSMTNPSMFVIDEAHCISAWGhdFRPEYRHIglLRQRFSHLPF 168
Cdd:pfam00270 81 GGDSRKEQLEKL-----KGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEI--LRRLPKKRQI 151
|
170
....*....|...
gi 510821755 169 IALTATADKVTRK 181
Cdd:pfam00270 152 LLLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
11-209 |
2.63e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 109.50 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 11 KYFGYDEFRPQQEEIINEVISGN-DVLVLMPTGGGKSVCFQIPALLR-----DGVCIVISPLISLMKDQVDALK-----T 79
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKklgpsL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 80 NGIAAAFLNSTQSFEEQQKILESCYKkeiaLLYVSPERLISDISS-ITSMTNPSMFVIDEAHCISAWGhdFRPEYRHIgl 158
Cdd:smart00487 82 GLKVVGLYGGDSKREQLRKLESGKTD----ILVTTPGRLLDLLENdKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL-- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510821755 159 LRQRFSHLPFIALTATADKVTRKdiIKQLHLKDPkIFVSSFDRKNLSLDVR 209
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIEN--LLELFLNDP-VFIDVGFTPLEPIEQF 201
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
397-501 |
1.10e-26 |
|
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: 104.54 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 397 PRKHFDGTLLIQKALSAMARMREKEGATMVIDVLRGSLRTDLREAGYDKLKTHGIGSDLCTSDWQRYLMQMLNLGIIEMA 476
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*
gi 510821755 477 YDENFALKSTAYGKEILFGKKKAEL 501
Cdd:pfam09382 81 IEFYSVLKLTPKAREVLKGEEKVML 105
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
244-325 |
5.27e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 98.82 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 244 EEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGRAGR 323
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 510821755 324 DG 325
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 ... |
402-493 |
1.63e-24 |
|
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: 97.55 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 402 DGTLLIQKALSAMARMREKEGATMVIDVLRGSLRTDLREAGYDKLKTHGIGSDLCTSDWQRYLMQMLNLGIIEMAYDENF 481
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 510821755 482 ALKSTAYGKEIL 493
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
14-375 |
8.74e-23 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 100.99 E-value: 8.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 14 GYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALLR------DGV-CIVISP---LIslmkDQV-DALKTngi 82
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRldpsrpRAPqALILAPtreLA----LQVaEELRK--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 83 AAAFLNST-------QSFEEQQKILescyKKEIALLYVSPERLIS-------DISSItsmtnpSMFVIDEAhcisawghD 148
Cdd:COG0513 94 LAKYLGLRvatvyggVSIGRQIRAL----KRGVDIVVATPGRLLDliergalDLSGV------ETLVLDEA--------D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 149 ------FRPEYRHIgllrqrFSHLPFIALT----ATADKVTRKdIIKQlHLKDPKIFvsSFDRKNLSLD----VRIGIKT 214
Cdd:COG0513 156 rmldmgFIEDIERI------LKLLPKERQTllfsATMPPEIRK-LAKR-YLKNPVRI--EVAPENATAEtieqRYYLVDK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 215 KQKLEEITTFIKQNNSLCGIIYCLSRTTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCAT-IAfGMG 293
Cdd:COG0513 226 RDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 294 IDKSNVRWVIHYNLPKSMESYYQEIG---RAGRDGLpaaTILYYNYSDLTMLNRFAAQSGQadinleKLKRIQHYAEADI 370
Cdd:COG0513 305 IDIDDVSHVINYDLPEDPEDYVHRIGrtgRAGAEGT---AISLVTPDERRLLRAIEKLIGQ------KIEEEELPGFEPV 375
|
....*
gi 510821755 371 CRRKI 375
Cdd:COG0513 376 EEKRL 380
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
216-325 |
2.09e-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: 92.27 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 216 QKLEEITTFIKQNNSLCGIIYCLSRTTCEEvAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGID 295
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 510821755 296 KSNVRWVIHYNLPKSMESYYQEIGRAGRDG 325
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
17-321 |
7.49e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 93.55 E-value: 7.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 17 EFRPQQEEIINEVIS-----GNDVLVLMPTGGGKSVCFQ--IPALLRDGVCIVISPLISLMKDQVDALKTngIAAAFLNS 89
Cdd:COG1061 80 ELRPYQQEALEALLAalergGGRGLVVAPTGTGKTVLALalAAELLRGKRVLVLVPRRELLEQWAEELRR--FLGDPLAG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 90 TQSFEEQQKILescykkeIAllyvSPERLISDISSITSMTNPSMFVIDEAHCISAwghdfrPEYRHIgllRQRFSHLPFI 169
Cdd:COG1061 158 GGKKDSDAPIT-------VA----TYQSLARRAHLDELGDRFGLVIIDEAHHAGA------PSYRRI---LEAFPAAYRL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 170 ALTAT-----------------ADKVTRKDIIKQLHLKDPKIFV---------SSFDRKNLSLDVRIGIKTKQKLEEITT 223
Cdd:COG1061 218 GLTATpfrsdgreillflfdgiVYEYSLKEAIEDGYLAPPEYYGirvdltderAEYDALSERLREALAADAERKDKILRE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 224 FIKQNNSLC-GIIYCLSRTTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWV 302
Cdd:COG1061 298 LLREHPDDRkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVA 377
|
330
....*....|....*....
gi 510821755 303 IHYNLPKSMESYYQEIGRA 321
Cdd:COG1061 378 ILLRPTGSPREFIQRLGRG 396
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
525-592 |
2.42e-19 |
|
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: 82.20 E-value: 2.42e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510821755 525 EDELLEQLKKVRRKFSLEEKVPAYIIFSDATLHEMADKKPLTTSEMLSITGVGEYKFDRYGEEFLDLI 592
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
194-323 |
1.79e-18 |
|
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: 81.78 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 194 IFVSSFDRKNLSLDVRIGIKTKQKleeittfikqnnslcGIIYCLSRTTCEEVAYELKIKGINAGYYHAGMNARERERVQ 273
Cdd:cd18787 6 VVVEEEEKKLLLLLLLLEKLKPGK---------------AIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERAL 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 510821755 274 ENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGRAGR 323
Cdd:cd18787 71 KKFRSGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
22-332 |
1.88e-16 |
|
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: 82.96 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 22 QEEIINEVISGNDVLVLMPTGGGKSVCFQIPAL---LRDGVC--IVISPLISLMKDQVDALKT------NGIAAAFLNST 90
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLealLEDPGAtaLYLYPTKALARDQLRRLRElaealgLGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 91 QSFEEQQKILESCykkeiallyvspeRLIsdissitsMTNPSM---------------------FVIDEAHcisawghdf 149
Cdd:COG1205 141 TPPEERRWIREHP-------------DIV--------LTNPDMlhygllphhtrwarffrnlryVVIDEAH--------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 150 rpEYR-----HIGLLRQRFSHL-------P-FIALTAT-------ADKVT---------------RKDIIkqlhLKDPKI 194
Cdd:COG1205 191 --TYRgvfgsHVANVLRRLRRIcrhygsdPqFILASATignpaehAERLTgrpvtvvdedgsprgERTFV----LWNPPL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 195 FVSSFDRKNLSLDVRIgiktkqkleeITTFIKQNnsLCGIIYCLSRTTCEEVAYELKIKGINAGY------YHAGMNARE 268
Cdd:COG1205 265 VDDGIRRSALAEAARL----------LADLVREG--LRTLVFTRSRRGAELLARYARRALREPDLadrvaaYRAGYLPEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510821755 269 RERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGRAGRDGLPAATIL 332
Cdd:COG1205 333 RREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
14-347 |
5.80e-15 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 77.91 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 14 GYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALLRdgvCIVISPLISlmKDQVDALktngiaAAFLNSTQSF 93
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISR---CCTIRSGHP--SEQRNPL------AMVLTPTREL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 94 ----EEQQKIL------------------ESCY--KKEIALLYVSPERLISDISSIT-SMTNPSMFVIDEAHCISAWGhd 148
Cdd:PLN00206 209 cvqvEDQAKVLgkglpfktalvvggdampQQLYriQQGVELIVGTPGRLIDLLSKHDiELDNVSVLVLDEVDCMLERG-- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 149 FRPEYRHIgllRQRFSHLPFIALTATADKVTRKdiIKQLHLKDPkIFVS--SFDRKNLSLD-VRIGIKTKQKLEEITTFI 225
Cdd:PLN00206 287 FRDQVMQI---FQALSQPQVLLFSATVSPEVEK--FASSLAKDI-ILISigNPNRPNKAVKqLAIWVETKQKKQKLFDIL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 226 KQNNSLC--GIIYCLSRTTCEEVAYEL-KIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWV 302
Cdd:PLN00206 361 KSKQHFKppAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQV 440
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 510821755 303 IHYNLPKSMESYYQEIGRAGRDGLPAATILYYNYSDLTMLNRFAA 347
Cdd:PLN00206 441 IIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
14-333 |
8.96e-15 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 77.58 E-value: 8.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 14 GYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPAL------LRDGVCIVISPLISLMKDQVDALKT-----NGI 82
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTRELAVQVAEAMTDfskhmRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 83 AAAFLNSTQSFEEQQKILescyKKEIALLYVSPERLISDISSIT-SMTNPSMFVIDEAHCISAWGhdFRPEYRHIgllrq 161
Cdd:PRK11634 105 NVVALYGGQRYDVQLRAL----RQGPQIVVGTPGRLLDHLKRGTlDLSKLSGLVLDEADEMLRMG--FIEDVETI----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 162 rFSHLPF---IAL-TATADKVTRKdiIKQLHLKDP---KIFVSSFDRKNLSLDVRIgIKTKQKLEEITTFIKQNNSLCGI 234
Cdd:PRK11634 174 -MAQIPEghqTALfSATMPEAIRR--ITRRFMKEPqevRIQSSVTTRPDISQSYWT-VWGMRKNEALVRFLEAEDFDAAI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 235 IYCLSRTTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESY 314
Cdd:PRK11634 250 IFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESY 329
|
330
....*....|....*....
gi 510821755 315 YQEIGRAGRDGLPAATILY 333
Cdd:PRK11634 330 VHRIGRTGRAGRAGRALLF 348
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
7-326 |
2.10e-14 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 76.09 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 7 EILQKyFGYDEFRPQQEEII-NEVISGNDVLVLMPTGGGKSVCFQIP---ALLRDGVCIVISPLISL----MKDQVDALK 78
Cdd:COG1204 13 EFLKE-RGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTLIAELAilkALLNGGKALYIVPLRALasekYREFKRDFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 79 TNGIAAAFlnSTQSFEEQQKILESCYkkeiaLLYVSPERLISDISSITS-MTNPSMFVIDEAHCIsawgHDfrpEYRHIG 157
Cdd:COG1204 92 ELGIKVGV--STGDYDSDDEWLGRYD-----ILVATPEKLDSLLRNGPSwLRDVDLVVVDEAHLI----DD---ESRGPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 158 L------LRQRFSHLPFIALTAT------------ADKVT--------RKDIIKQ--LHLKDPK---------------- 193
Cdd:COG1204 158 LevllarLRRLNPEAQIVALSATignaeeiaewldAELVKsdwrpvplNEGVLYDgvLRFDDGSrrskdptlalaldlle 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 194 ------IFVSSfdRKN-------LS--LDVRIGIKTKQKLEEITTFIKQNNSLCGiiyclsrtTCEEVAYELKiKGInaG 258
Cdd:COG1204 238 eggqvlVFVSS--RRDaeslakkLAdeLKRRLTPEEREELEELAEELLEVSEETH--------TNEKLADCLE-KGV--A 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 259 YYHAGMNARERERVQENFINDDLMVVCAT--IAFGMgidksnvrwvihyNLP-----------------KSMEsYYQEIG 319
Cdd:COG1204 305 FHHAGLPSELRRLVEDAFREGLIKVLVATptLAAGV-------------NLParrviirdtkrggmvpiPVLE-FKQMAG 370
|
....*..
gi 510821755 320 RAGRDGL 326
Cdd:COG1204 371 RAGRPGY 377
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
523-592 |
5.97e-14 |
|
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: 67.32 E-value: 5.97e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 523 NYEDELLEQLKKVRRKFSLEEKVPAYIIFSDATLHEMADKKPLTTSEMLSITGVGEYKFDRYGEEFLDLI 592
Cdd:smart00341 2 ERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVI 71
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
336-395 |
6.28e-14 |
|
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: 66.54 E-value: 6.28e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510821755 336 YSDLTMLNRFAAQSGQAD----INLEKLKRIQHYAEADI-CRRKILLSYFSETL-EKNCGNCDVCR 395
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEerkeVELQKLQAMVAYCENTTdCRRKQLLRYFGEEFdSEPCGNCDNCL 66
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
234-332 |
2.22e-13 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 67.67 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 234 IIYCLSRTTCE----EVAYELKIKGINAGY---YHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYN 306
Cdd:cd18797 39 IVFCRSRKLAElllrYLKARLVEEGPLASKvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*.
gi 510821755 307 LPKSMESYYQEIGRAGRDGLPAATIL 332
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
32-174 |
5.38e-13 |
|
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: 66.66 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 32 GNDVLVLMPTGGGKSVCFQIPALLR-----DGVCiVISPLISLMKDQVDALK---TNGIAAAFLNSTQSFEEQQKILEsc 103
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLllkkgKKVL-VLVPTKALALQTAERLRelfGPGIRVAVLVGGSSAEEREKNKL-- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510821755 104 ykKEIALLYVSPERLISDISSITSMTNP--SMFVIDEAHCISAWGHDFRPEYrhIGLLRQRFSHLPFIALTAT 174
Cdd:cd00046 78 --GDADIIIATPDMLLNLLLREDRLFLKdlKLIIVDEAHALLIDSRGALILD--LAVRKAGLKNAQVILLSAT 146
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
234-326 |
5.09e-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: 64.11 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 234 IIYCLSRTTCEEVAyeLKIKGInaGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGID--------KSNVRWVIHY 305
Cdd:cd18795 47 LVFCSSRKECEKTA--KDLAGI--AFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKG 122
|
90 100
....*....|....*....|.
gi 510821755 306 NLPKSMESYYQEIGRAGRDGL 326
Cdd:cd18795 123 YRELSPLEYLQMIGRAGRPGF 143
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
135-323 |
2.55e-11 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 66.84 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 135 VIDEAHCISawghdfRPEYRH-----IGLLRQRFSHLPFIALTATadkvtrkdiikqlhLKDPKIFVSSFDRKNLSLDVR 209
Cdd:COG1202 331 VIDEVHMLE------DPERGHrldglIARLKYYCPGAQWIYLSAT--------------VGNPEELAKKLGAKLVEYEER 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 210 --------IGIKTKQKLEEITTFIKQ---NNSLCG-----IIYCLSRTTCEEVAYELkikGINAGYYHAGMNARERERVQ 273
Cdd:COG1202 391 pvplerhlTFADGREKIRIINKLVKRefdTKSSKGyrgqtIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510821755 274 ENFINDDLMVVCATIAFGMGID--KSNV---------RWVihynlpkSMESYYQEIGRAGR 323
Cdd:COG1202 468 RRFADQELAAVVTTAALAAGVDfpASQVifdslamgiEWL-------SVQEFHQMLGRAGR 521
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
30-325 |
3.69e-11 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 65.95 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 30 ISGNDVLVLMPTGGGKSVCFQIPA--------LLRDG---VCIVISP---LISLMKDQ------VDALKTNGIAAAFLNS 89
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPtreLAEQIREQcnkfgaSSKIRNTVAYGGVPKR 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 90 TQSFEEQQ--KILESCykkeiallyvsPERLISDI-SSITSMTNPSMFVIDEAHCISAWGhdFRPEYRHI-GLLRQRFSH 165
Cdd:PTZ00110 245 GQIYALRRgvEILIAC-----------PGRLIDFLeSNVTNLRRVTYLVLDEADRMLDMG--FEPQIRKIvSQIRPDRQT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 166 LPFIALTATADKVTRKDIIKQ--LHlkdpkIFVSSFDRK---NLSLDVRIgIKTKQKLEEITTFIKQ--NNSLCGIIYCL 238
Cdd:PTZ00110 312 LMWSATWPKEVQSLARDLCKEepVH-----VNVGSLDLTachNIKQEVFV-VEEHEKRGKLKMLLQRimRDGDKILIFVE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 239 SRTTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEI 318
Cdd:PTZ00110 386 TKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRI 465
|
....*..
gi 510821755 319 GRAGRDG 325
Cdd:PTZ00110 466 GRTGRAG 472
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
239-323 |
1.44e-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: 56.89 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 239 SRTTCEEVAYELK------IKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSME 312
Cdd:cd18796 47 TRSQAERLAQRLRelcpdrVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVA 126
|
90
....*....|.
gi 510821755 313 SYYQEIGRAGR 323
Cdd:cd18796 127 RLLQRLGRSGH 137
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
18-174 |
2.32e-09 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 56.16 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 18 FRPQQEEIINEVI--SGNDVLVL-MPTGGGKSVC-FQIPALLRDGVCIVISPLISLMKDQVDALKTngiaaaFLNSTQSF 93
Cdd:cd17926 1 LRPYQEEALEAWLahKNNRRGILvLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFED------FLGDSSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 94 EEQQKILEScykKEIALLYVS-PERLISDISSITSMTN-PSMFVIDEAHCISAwghdfrPEYRHIgllRQRFSHLPFIAL 171
Cdd:cd17926 75 LIGGGKKKD---FDDANVVVAtYQSLSNLAEEEKDLFDqFGLLIVDEAHHLPA------KTFSEI---LKELNAKYRLGL 142
|
...
gi 510821755 172 TAT 174
Cdd:cd17926 143 TAT 145
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
234-342 |
3.44e-09 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 59.07 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 234 IIYCLSRTTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMES 313
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100
....*....|....*....|....*....
gi 510821755 314 YYQEIGRAGRDGLPAATILYYNYSDLTML 342
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIEQL 379
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
21-174 |
5.25e-09 |
|
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: 56.05 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 21 QQEEIINEVISGNDVLVLMPTGGGKSVCFQIP---ALLRD-GVC-IVISPLISLMKDQVDALK------TNGIAAAFLNS 89
Cdd:cd17923 4 HQAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDpGSRaLYLYPTKALAQDQLRSLRelleqlGLGIRVATYDG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 90 TQSFEEQQKILEscykkeiallyvSPERLIsdissitsMTNPSM---------------------FVIDEAHCisawghd 148
Cdd:cd17923 84 DTPREERRAIIR------------NPPRIL--------LTNPDMlhyallphhdrwarflrnlryVVLDEAHT------- 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 510821755 149 frpeYR-----HIGLLRQRF--------SHLPFIALTAT 174
Cdd:cd17923 137 ----YRgvfgsHVALLLRRLrrlcrrygADPQFILTSAT 171
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
14-338 |
8.23e-09 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 58.00 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 14 GYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPA---LLRDGV----------CIVISP----LISLMKDQVDA 76
Cdd:PRK01297 106 GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIinqLLQTPPpkerymgeprALIIAPtrelVVQIAKDAAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 77 LKTNGIAAAFLNSTQSFEEQQKILEScykKEIALLYVSPERLIS-DISSITSMTNPSMFVIDEAHCISAWGhdFRPEYRH 155
Cdd:PRK01297 186 TKYTGLNVMTFVGGMDFDKQLKQLEA---RFCDILVATPGRLLDfNQRGEVHLDMVEVMVLDEADRMLDMG--FIPQVRQ 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 156 IglLRQ--RFSHLPFIALTAT-ADKVTrkDIIKQLhLKDPKIF-VSSFDRKNLSLDVRIGIKTKQ-KLEEITTFIKQNNS 230
Cdd:PRK01297 261 I--IRQtpRKEERQTLLFSATfTDDVM--NLAKQW-TTDPAIVeIEPENVASDTVEQHVYAVAGSdKYKLLYNLVTQNPW 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 231 LCGIIYCLSRTTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKS 310
Cdd:PRK01297 336 ERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPED 415
|
330 340
....*....|....*....|....*...
gi 510821755 311 MESYYQEIGRAGRDGLPAATILYYNYSD 338
Cdd:PRK01297 416 PDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
281-335 |
9.62e-08 |
|
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: 49.62 E-value: 9.62e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 510821755 281 LMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGRAGRDGLPAATILYYN 335
Cdd:cd18785 23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
14-323 |
4.06e-07 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 52.89 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 14 GYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALLRdgvcivisplisLMKDQVDALKTNGIAAAFLNSTQSF 93
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQH------------LITRQPHAKGRRPVRALILTPTREL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 94 EEQqkILESC--YKKEIAL------------------------LYVSPERLIS-DISSITSMTNPSMFVIDEAHCISAWG 146
Cdd:PRK10590 88 AAQ--IGENVrdYSKYLNIrslvvfggvsinpqmmklrggvdvLVATPGRLLDlEHQNAVKLDQVEILVLDEADRMLDMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 147 --HDFRpeyRHIGLLRQRFSHLPFIAltatadkvTRKDIIKQLH---LKDP-KIFVSsfdRKNLSLD-----VRIgIKTK 215
Cdd:PRK10590 166 fiHDIR---RVLAKLPAKRQNLLFSA--------TFSDDIKALAeklLHNPlEIEVA---RRNTASEqvtqhVHF-VDKK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 216 QKLEEITTFIKQNNSLCGIIYCLSRTTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGID 295
Cdd:PRK10590 231 RKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLD 310
|
330 340
....*....|....*....|....*...
gi 510821755 296 KSNVRWVIHYNLPKSMESYYQEIGRAGR 323
Cdd:PRK10590 311 IEELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
14-325 |
6.18e-07 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 52.25 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 14 GYDefRPQ--QEEIINEVISGNDVLVLMPTGGGKSVCFQIPAL--LRD--------GVCIVISP---LISLMKDQVDALK 78
Cdd:PRK11192 20 GYT--RPTaiQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALqhLLDfprrksgpPRILILTPtreLAMQVADQARELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 79 ----------TNGIAaaFLNSTQSFEEQQKILescykkeIA-----LLYVSPERLisDISSItsmtnpSMFVIDEAHCIS 143
Cdd:PRK11192 98 khthldiatiTGGVA--YMNHAEVFSENQDIV-------VAtpgrlLQYIKEENF--DCRAV------ETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 144 AWGhdFRPEYRHIGL-LRQRFSHLPFialTATADKVTRKDIIKQLhLKDP-KIFV--SSFDRKNLSLDVRIGIKTKQKLE 219
Cdd:PRK11192 161 DMG--FAQDIETIAAeTRWRKQTLLF---SATLEGDAVQDFAERL-LNDPvEVEAepSRRERKKIHQWYYRADDLEHKTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 220 EITTFIKQNNSLCGIIYCLSRTTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNV 299
Cdd:PRK11192 235 LLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
|
330 340
....*....|....*....|....*.
gi 510821755 300 RWVIHYNLPKSMESYYQEIGRAGRDG 325
Cdd:PRK11192 315 SHVINFDMPRSADTYLHRIGRTGRAG 340
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
17-174 |
2.80e-06 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 48.10 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 17 EFRPQQEEIINEVI-SGNDVLVLMPTGGGKSVCFQ---IPALLRDGVCIVISPLISLMKDQVDALKT-NGIAAAFLNSTQ 91
Cdd:cd18028 1 ELYPPQAEAVRAGLlKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRALASEKYEEFKKlEEIGLKVGISTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 92 SFEEQQKILESC------YKKEIALLYVSPErLISDIssitsmtnpSMFVIDEAHCISAWGHDFRPEYRhIGLLRQRFSH 165
Cdd:cd18028 81 DYDEDDEWLGDYdiivatYEKFDSLLRHSPS-WLRDV---------GVVVVDEIHLISDEERGPTLESI-VARLRRLNPN 149
|
....*....
gi 510821755 166 LPFIALTAT 174
Cdd:cd18028 150 TQIIGLSAT 158
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
32-174 |
4.84e-06 |
|
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: 47.19 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 32 GNDVLVLMPTGGGKSVCFQIPALLR------DGV-CIVISPLISLMKDQVDALKT--NGIAAAFL------NSTQSfeEQ 96
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSladepeKGVqVLYISPLKALINDQERRLEEplDEIDLEIPvavrhgDTSQS--EK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 97 QKIL-----------EScykkeIALLYVSP--ERLISDISSItsmtnpsmfVIDEahcisaWgHDFRPEYR--HIGLLRQ 161
Cdd:cd17922 79 AKQLknppgilittpES-----LELLLVNKklRELFAGLRYV---------VVDE------I-HALLGSKRgvQLELLLE 137
|
170
....*....|....*...
gi 510821755 162 RFSH-----LPFIALTAT 174
Cdd:cd17922 138 RLRKltgrpLRRIGLSAT 155
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
1-139 |
1.24e-05 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members 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: 350697 [Multi-domain] Cd Length: 199 Bit Score: 46.55 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 1 MSLSaQEILQKYFGYDEFRP---QQEEIInEVISGNDVLVLMPTGGGKSVCFQIPALLR----DGVC--IVISPLISLMK 71
Cdd:cd17939 2 MGLS-EDLLRGIYAYGFEKPsaiQQRAIV-PIIKGRDVIAQAQSGTGKTATFSIGALQRidttVRETqaLVLAPTRELAQ 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510821755 72 DQVDALKTNG----IAAAFLNSTQSFEEQQKILEscYKKEIALlyVSPERLISDISSIT-SMTNPSMFVIDEA 139
Cdd:cd17939 80 QIQKVVKALGdymgVKVHACIGGTSVREDRRKLQ--YGPHIVV--GTPGRVFDMLQRRSlRTDKIKMFVLDEA 148
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
216-325 |
7.04e-05 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 42.96 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 216 QKLEEI-TTFIKQNNSLCGIIYCLSRTTCEEVA-----YELKIKGINAGY----------YHAGMNARERERVQENFIND 279
Cdd:cd18802 10 QKLIEIlREYFPKTPDFRGIIFVERRATAVVLSrllkeHPSTLAFIRCGFligrgnssqrKRSLMTQRKQKETLDKFRDG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 510821755 280 DLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGRAGRDG 325
Cdd:cd18802 90 ELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
11-197 |
8.73e-05 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 43.89 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 11 KYFGYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPA--LL-------RDGV-CIVISPLISLmkdqvdALKTN 80
Cdd:cd17942 6 EEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAieLLyklkfkpRNGTgVIIISPTREL------ALQIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 81 GIAAAFL-NSTQSF----------EEQQKIlescyKKEIALLYVSPERLISDISSITSMT--NPSMFVIDEAHCISAWGh 147
Cdd:cd17942 80 GVAKELLkYHSQTFgivigganrkAEAEKL-----GKGVNILVATPGRLLDHLQNTKGFLykNLQCLIIDEADRILEIG- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510821755 148 dFRPEYRHI-GLLRQRFSHLPFialtaTADKVTRKDIIKQLHLKDPKIFVS 197
Cdd:cd17942 154 -FEEEMRQIiKLLPKRRQTMLF-----SATQTRKVEDLARISLKKKPLYVG 198
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
194-342 |
2.31e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 44.18 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 194 IFVSSfdRKN-LSLDVRIGIKTKQKLEEittfiKQNNSLCGI---IYCLSRT-TCEEVAYELKiKGinAGYYHAGMNARE 268
Cdd:PRK02362 248 VFVSS--RRNaEGFAKRAASALKKTLTA-----AERAELAELaeeIREVSDTeTSKDLADCVA-KG--AAFHHAGLSREH 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 269 RERVQENFINDDLMVVCATIAFGMGIDKSNVRWVI----HYN-----LPKSMESYYQEIGRAGRDGL-P--AATILYYNY 336
Cdd:PRK02362 318 RELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIrdyrRYDggagmQPIPVLEYHQMAGRAGRPGLdPygEAVLLAKSY 397
|
....*.
gi 510821755 337 SDLTML 342
Cdd:PRK02362 398 DELDEL 403
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
6-194 |
3.12e-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: 42.04 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 6 QEILQKYfGYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPAL---------LRDGV-CIVISP---LISLMKD 72
Cdd:cd00268 2 LKALKKL-GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekllpepkkKGRGPqALVLAPtreLAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 73 QVDAL-KTNGIAAAFLNSTQSFEEQQKILescyKKEIALLYVSPERLISDISS-ITSMTNPSMFVIDEAhcisawghD-- 148
Cdd:cd00268 81 VARKLgKGTGLKVAAIYGGAPIKKQIEAL----KKGPDIVVGTPGRLLDLIERgKLDLSNVKYLVLDEA--------Drm 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 510821755 149 ----FRPEYRHIgllrqrFSHLPF----IALTATADKVTRKdIIKQLhLKDPKI 194
Cdd:cd00268 149 ldmgFEEDVEKI------LSALPKdrqtLLFSATLPEEVKE-LAKKF-LKNPVR 194
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
14-197 |
3.48e-04 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 41.89 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 14 GYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPALLR---------DGV-CIVISPLISLMKDQVDALKTNG-- 81
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKlyrerwtpeDGLgALIISPTRELAMQIFEVLRKVGky 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 82 --IAAAFLNSTQSFEEQQKILEScykkeIALLYVSPERLIS--DISSITSMTNPSMFVIDEAHCISAWGhdFRPEYRHIg 157
Cdd:cd17941 89 hsFSAGLIIGGKDVKEEKERINR-----MNILVCTPGRLLQhmDETPGFDTSNLQMLVLDEADRILDMG--FKETLDAI- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 510821755 158 llrqrFSHLP----FIALTATADKvTRKDIIKqLHLKDPkIFVS 197
Cdd:cd17941 161 -----VENLPksrqTLLFSATQTK-SVKDLAR-LSLKNP-EYIS 196
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
17-174 |
5.77e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 40.73 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 17 EFRPQQEEIINEVISG-----NDVLVLMPTGGGKSVC-FQIPALLRDGV----CIVISPLISLMKDQVDALKTNGIAAAF 86
Cdd:pfam04851 3 ELRPYQIEAIENLLESikngqKRGLIVMATGSGKTLTaAKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 87 LN---STQSFEEQQ---KILESCYKKEIALLYVSPERLISDissitsmtNPSMFVIDEAHcisawgHDFRPEYRHIgllR 160
Cdd:pfam04851 83 IGeiiSGDKKDESVddnKIVVTTIQSLYKALELASLELLPD--------FFDVIIIDEAH------RSGASSYRNI---L 145
|
170
....*....|....
gi 510821755 161 QRFSHLPFIALTAT 174
Cdd:pfam04851 146 EYFKPAFLLGLTAT 159
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
234-323 |
9.59e-04 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 42.13 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 234 IIYCLSRTTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDD--LMVVCATIAFGMGIDKSNVRWVIHYNLPKSM 311
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLWWNP 632
|
90
....*....|..
gi 510821755 312 ESYYQEIGRAGR 323
Cdd:COG0553 633 AVEEQAIDRAHR 644
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
22-139 |
1.13e-03 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 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: 350696 [Multi-domain] Cd Length: 204 Bit Score: 40.77 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 22 QEEIINEVISGNDVLVLMPTGGGKSVCFQIPaLLRDGVCIVISP---LISLMKDQVDALKTN----GIAAAFLNSTQSFE 94
Cdd:cd17938 26 QAEAIPLILGGGDVLMAAETGSGKTGAFCLP-VLQIVVALILEPsreLAEQTYNCIENFKKYldnpKLRVALLIGGVKAR 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 510821755 95 EQQKILEScykkEIALLYVSPERLISDISS-ITSMTNPSMFVIDEA 139
Cdd:cd17938 105 EQLKRLES----GVDIVVGTPGRLEDLIKTgKLDLSSVRFFVLDEA 146
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
13-139 |
1.71e-03 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 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: 350722 [Multi-domain] Cd Length: 211 Bit Score: 40.26 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 13 FGYDEFRPQQEEIINEVIS-GNDVLVLMPTGGGKSVCFQIPALLRdgvciVISPLISLMKDQVDAL---KTNGIAaafln 88
Cdd:cd17964 12 MGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQS-----LLNTKPAGRRSGVSALiisPTRELA----- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510821755 89 sTQSFEEQQKILEscYKKEIALLYV-----------------------SPERL---ISDISSITSMTNPSMFVIDEA 139
Cdd:cd17964 82 -LQIAAEAKKLLQ--GLRKLRVQSAvggtsrraelnrlrrgrpdilvaTPGRLidhLENPGVAKAFTDLDYLVLDEA 155
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
13-326 |
1.78e-03 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 41.46 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 13 FGYDEFrpqQEEIINEVISGNDVLVLMPTGGGKSV-----CFQipALLRDGVCIVISPLISLmkdqvdalktngiaaafl 87
Cdd:COG4581 24 FELDPF---QEEAILALEAGRSVLVAAPTGSGKTLvaefaIFL--ALARGRRSFYTAPIKAL------------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 88 nSTQSFEEQQKIL-----------ES--------CYKKEIA--LLYVSPERLiSDISSItsmtnpsmfVIDEAHCIS--- 143
Cdd:COG4581 81 -SNQKFFDLVERFgaenvglltgdASvnpdapivVMTTEILrnMLYREGADL-EDVGVV---------VMDEFHYLAdpd 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 144 ---AWghdfrpeyrHIGLLrqrfsHLP----FIALTAT-------ADKVTRK----DIIKQLHLKDP-KIFVSSFDRKNL 204
Cdd:COG4581 150 rgwVW---------EEPII-----HLParvqLVLLSATvgnaeefAEWLTRVrgetAVVVSEERPVPlEFHYLVTPRLFP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 205 SLDVRIGIKTKQKLEEITTFIKQNNSLCGIIYCLSRTTCEEVAYEL------------KIKGI--------NAGYY---- 260
Cdd:COG4581 216 LFRVNPELLRPPSRHEVIEELDRGGLLPAIVFIFSRRGCDEAAQQLlsarlttkeeraEIREAidefaedfSVLFGktls 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 261 ----------HAGMNARERERVQENFINDDLMVVCATIAFGMGIdksNV--RWVIHYNLPK----SMES-----YYQEIG 319
Cdd:COG4581 296 rllrrgiavhHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGI---NMpaRTVVFTKLSKfdgeRHRPltareFHQIAG 372
|
....*..
gi 510821755 320 RAGRDGL 326
Cdd:COG4581 373 RAGRRGI 379
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
6-65 |
1.95e-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: 39.87 E-value: 1.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510821755 6 QEILQKyFGYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPAL----------LRDGV-CIVISP 65
Cdd:cd17960 2 LDVVAE-LGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeillkrkanlKKGQVgALIISP 71
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
6-54 |
2.28e-03 |
|
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: 39.59 E-value: 2.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 510821755 6 QEILQKYF--GYDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPAL 54
Cdd:cd17940 8 RELLMGIFekGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPIL 58
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
6-139 |
2.68e-03 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It 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: 350714 [Multi-domain] Cd Length: 231 Bit Score: 39.92 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 6 QEILQKyFGYDEFRPQQEEIINEVISGN---------DVLVLMPTGGGKSVCFQIPAL--LRDGV-----CIVISP---L 66
Cdd:cd17956 2 LKNLQN-NGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPIVqaLSKRVvprlrALIVVPtkeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 67 ISLMKDQVDALKTN-GIAAAFLNSTQSFEEQQKILESC----YKKEIALLYVSPERLISDISSITSMT--NPSMFVIDEA 139
Cdd:cd17956 81 VQQVYKVFESLCKGtGLKVVSLSGQKSFKKEQKLLLVDtsgrYLSRVDILVATPGRLVDHLNSTPGFTlkHLRFLVIDEA 160
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
234-325 |
2.99e-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: 38.23 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 234 IIYCLSRTTCEEVAYELKIKGINAGYYHAGMNARERERVQENFINDD--LMVVCATIAFGMGID--KSNVrwVIHYNLP- 308
Cdd:cd18793 31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNltAANR--VILYDPWw 108
|
90
....*....|....*...
gi 510821755 309 -KSMESyyQEIGRAGRDG 325
Cdd:cd18793 109 nPAVEE--QAIDRAHRIG 124
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
17-140 |
3.00e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 39.34 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 17 EFRPQQEEIINEVISGNDVLVLMPTGGGKS-----VC----FQIPAlLRDGVCIVISPLISLMKDQVDA---------LK 78
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPA-GRKGKVVFLANKVPLVEQQKEVfrkhferpgYK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510821755 79 TNGIAAAflNSTQSFEEQqkILESCykkeiALLYVSPERLISDISS--ITSMTNPSMFVIDEAH 140
Cdd:cd17927 81 VTGLSGD--TSENVSVEQ--IVESS-----DVIIVTPQILVNDLKSgtIVSLSDFSLLVFDECH 135
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
260-334 |
3.09e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 40.68 E-value: 3.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510821755 260 YHAGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGRAGRDGLPAATILYY 334
Cdd:PRK09751 307 HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVGGVSKGLFF 381
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
233-323 |
5.71e-03 |
|
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: 37.15 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 233 GIIYCLSRTTCEEVAYELKIKGINAGYYHAG--MNARERERVQENFINDDLMVVCATIA-FGMGIDKSNVRWVIHYNLPK 309
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFFGELKPPILVTVDlLTTGVDIPEVDNVVFLRPTE 88
|
90
....*....|....
gi 510821755 310 SMESYYQEIGRAGR 323
Cdd:cd18799 89 SRTLFLQMLGRGLR 102
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
15-322 |
5.87e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 39.87 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 15 YDEFRPQQEEIINEVISGNDVLVLMPTGGGKSVCFQIPAL-----------LRDGV-CIVISPLISLMKD---------- 72
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIdelfrlgregeLEDKVyCLYVSPLRALNNDihrnleeplt 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 73 ------QVDALKTNGIAAAFLNSTQSFEEQQKIL-----------EScykkeIALLYVSP---ERLiSDISSItsmtnps 132
Cdd:PRK13767 110 eireiaKERGEELPEIRVAIRTGDTSSYEKQKMLkkpphilittpES-----LAILLNSPkfrEKL-RTVKWV------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 133 mfVIDEAHCISAwghdfrpEYR--HIGLLRQRFSHL---PF--IALTATA---DKVTR-----KDIIKQlhlKDPKI--- 194
Cdd:PRK13767 177 --IVDEIHSLAE-------NKRgvHLSLSLERLEELaggEFvrIGLSATIeplEEVAKflvgyEDDGEP---RDCEIvda 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510821755 195 -FVSSFDRKNLSLDVRIGIKTKQKL-----EEITTFIKQN-NSLcgiIYCLSRTTCEEVAYELK------IKGINAGYYH 261
Cdd:PRK13767 245 rFVKPFDIKVISPVDDLIHTPAEEIsealyETLHELIKEHrTTL---IFTNTRSGAERVLYNLRkrfpeeYDEDNIGAHH 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510821755 262 AGMNARERERVQENFINDDLMVVCATIAFGMGIDKSNVRWVIHYNLPKSMESYYQEIGRAG 322
Cdd:PRK13767 322 SSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
129-192 |
7.50e-03 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA 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: 350769 [Multi-domain] Cd Length: 207 Bit Score: 38.04 E-value: 7.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510821755 129 TNPSMFVIDEAHCISAWGhdFRPE---YRHIGLLRQRFSHLpfIALTATADKVTRKDIIKQLHLKDP 192
Cdd:cd18011 119 EEWDLVVVDEAHKLRNSG--GGKEtkrYKLGRLLAKRARHV--LLLTATPHNGKEEDFRALLSLLDP 181
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
545-592 |
8.85e-03 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 38.70 E-value: 8.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 510821755 545 VPAYIIFSDATLHEMADKKPLTTSEMLSITGVGEYKFDRYGEEFLDLI 592
Cdd:COG0349 229 VPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAV 276
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
18-66 |
9.97e-03 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 37.62 E-value: 9.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 510821755 18 FRPQQEEIINEVISGND-VLVLMPTGGGKSVCFQIpALLR------DGVCIVISPL 66
Cdd:cd18021 4 FNPIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAEL-ALLRhwrqnpKGRAVYIAPM 58
|
|
| |
