|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
2-474 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 718.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 2 QPTDVLKQYFGYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPALLMPGLTLVISPLISLMKDQVDSLLNQQIA 81
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 82 ATFINSQCTFEESKERFSQICRSKFKLVYISPERLQNEFFTSLMKELPLAMVVIDEAHCVSQWGHDFRPSYGAISSWIEA 161
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 162 LPQRPVVsAFTATATEKVKGDMLALLGLQKPQLFIGGFDRPNLYFRVV--GNGDRMAFLEAYLREHRRDSGIIYGATRKD 239
Cdd:COG0514 164 LPNVPVL-ALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVpkPPDDKLAQLLDFLKEHPGGSGIVYCLSRKK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 240 VDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAG 319
Cdd:COG0514 243 VEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 320 RDGAPGECILLFSRQDIMIQNYLIERSVHDQQQQRHEKLLLRQMIDYCEQPGCLRRAILAYFGETPAwRDCGHCGNCDSP 399
Cdd:COG0514 323 RDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELA-EPCGNCDNCLGP 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553309361 400 KVEEKITPEVRLICLCVDELKGRFGMTMVCDILKGTANAKVRRYGFEGKASFGMLGDFSQEEIRSLIRTCLQLHF 474
Cdd:COG0514 402 PETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQLF 476
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
5-597 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273594 [Multi-domain] Cd Length: 591 Bit Score: 713.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 5 DVLKQYFGYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPALLMPGLTLVISPLISLMKDQVDSLLNQQIAATF 84
Cdd:TIGR01389 3 QVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 85 INSQCTFEESKERFSQICRSKFKLVYISPERLQNEFFTSLMKELPLAMVVIDEAHCVSQWGHDFRPSYGAISSWIEALPQ 164
Cdd:TIGR01389 83 LNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFPQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 165 RPVVsAFTATATEKVKGDMLALLGLQKPQLFIGGFDRPNLYFRVVGNGDRMAFLEAYLREHRRDSGIIYGATRKDVDRIY 244
Cdd:TIGR01389 163 VPRI-ALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEELA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 245 QRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAGRDGAP 324
Cdd:TIGR01389 242 ERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 325 GECILLFSRQDIMIQNYLIERSVHDQQQQRHEKLLLRQMIDYCEQPGCLRRAILAYFGETPAwRDCGHCGNCDSPKVEEK 404
Cdd:TIGR01389 322 AEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEV-EPCGNCDNCLDPPKSYD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 405 ITPEVRLICLCVDELKGRFGMTMVCDILKGTANAKVRRYGFEGKASFGMLGDFSQEEIRSLIRTCLQLHFLEQSDGQYPV 484
Cdd:TIGR01389 401 ATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIYIG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 485 LSLTAAGREQLQSGRTVV--RTKRIAAAPSAEKKKrFSADIDEValrpVFEILRSLRYRLAKEEQIPPFVIFSDATLWEI 562
Cdd:TIGR01389 481 LQLTEAARKVLKNEVEVLlrPFKVVAKEKTRVQKN-LSVGVDNA----LFEALRELRKEQADEQNVPPYVIFSDSTLREM 555
|
570 580 590
....*....|....*....|....*....|....*
gi 553309361 563 AGRRPQSLDELGEVKGVGSFKLHKYGHIFLEALRE 597
Cdd:TIGR01389 556 AEKRPATLNALLKIKGVGQNKLDRYGEAFLEVIRE 590
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
1-597 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 543.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 1 MQPTDVLKQYFGYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPALLMPGLTLVISPLISLMKDQVDSLLNQQI 80
Cdd:PRK11057 11 SLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 81 AATFINSQCTFEESKERFSQiCRS-KFKLVYISPERLQNEFFTSLMKELPLAMVVIDEAHCVSQWGHDFRPSYGAISSWI 159
Cdd:PRK11057 91 AAACLNSTQTREQQLEVMAG-CRTgQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 160 EALPQRPVVsAFTATATEKVKGDMLALLGLQKPQLFIGGFDRPNLYFRVVGNGDRMAFLEAYLREHRRDSGIIYGATRKD 239
Cdd:PRK11057 170 QRFPTLPFM-ALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 240 VDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAG 319
Cdd:PRK11057 249 VEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 320 RDGAPGECILLFSRQDIM-IQNYLIERSVHDQQQ-QRHEkllLRQMIDYCEQPGCLRRAILAYFGETPAwRDCGHCGNC- 396
Cdd:PRK11057 329 RDGLPAEAMLFYDPADMAwLRRCLEEKPAGQQQDiERHK---LNAMGAFAEAQTCRRLVLLNYFGEGRQ-EPCGNCDICl 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 397 DSPKVEEKITpEVRLICLCVDELKGRFGMTMVCDILKGTANAKVRRYGFEGKASFGMLGDFSQEEIRSLIRTCLQLHFLE 476
Cdd:PRK11057 405 DPPKQYDGLE-DAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVT 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 477 QSDGQYPVLSLTAAGREQLQSGRTV-VRTKRIAAAPSAEKKKRFSADIDevalRPVFEILRSLRYRLAKEEQIPPFVIFS 555
Cdd:PRK11057 484 QNIAQHSALQLTEAARPVLRGEVSLqLAVPRIVALKPRAMQKSFGGNYD----RKLFAKLRKLRKSIADEENIPPYVVFN 559
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 553309361 556 DATLWEIAGRRPQSLDELGEVKGVGSFKLHKYGHIFLEALRE 597
Cdd:PRK11057 560 DATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRA 601
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
5-453 |
3.31e-165 |
|
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: 479.27 E-value: 3.31e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 5 DVLKQYFGYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPALLMPGLTLVISPLISLMKDQVDSLLNQQIAATF 84
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 85 INSQCTFEESKERFSQICRSKFKLVYISPERL--QNEFFTSLMKELPLAMVVIDEAHCVSQWGHDFRPSYGAISSWIEAL 162
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsaSNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 163 PQRPVVsAFTATATEKVKGDMLALLGLQKPQLFIGGFDRPNLYFRVVGNGDRMAF--LEAYLREHRRDSGIIYGATRKDV 240
Cdd:TIGR00614 161 PNVPVM-ALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPKILEdlLRFIRKEFEGKSGIIYCPSRKKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 241 DRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAGR 320
Cdd:TIGR00614 240 EQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 321 DGAPGECILLFSRQDI-MIQNYLIErsVHDQQQQRHEKLLLRQMIDYCEQPGCLRRAILAYFGETPAWRDCGH------C 393
Cdd:TIGR00614 320 DGLPSECHLFYAPADMnRLRRLLME--EPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFNKSFCImgtekcC 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553309361 394 GNCDSPK------VEEK---ITPEVRLICLCVDELKGRFGMTMVCDILKGTANAKVRRYGFEGKASFGM 453
Cdd:TIGR00614 398 DNCCKRLdyktkdVTDKvydFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGR 466
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
8-595 |
1.58e-112 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 363.45 E-value: 1.58e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 8 KQYFGYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPALLMPGLTLVISPLISLMKDQVDSLLNQQIAATFINS 87
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 88 QCTFEESKERFSQIC--RSKFKLVYISPERLQNEffTSLMKELP-------LAMVVIDEAHCVSQWGHDFRPSYGAISSW 158
Cdd:PLN03137 533 GMEWAEQLEILQELSseYSKYKLLYVTPEKVAKS--DSLLRHLEnlnsrglLARFVIDEAHCVSQWGHDFRPDYQGLGIL 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 159 IEALPQRPVVsAFTATATEKVKGDMLALLGLQKPQLFIGGFDRPNLYFRVVGNGDR-MAFLEAYLRE-HRRDSGIIYGAT 236
Cdd:PLN03137 611 KQKFPNIPVL-ALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKcLEDIDKFIKEnHFDECGIIYCLS 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 237 RKDVDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAG 316
Cdd:PLN03137 690 RMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECG 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 317 RAGRDGAPGECILLFSRQDIMIQNYLIERSVHDQQQ---------------QRHEKLLLRqMIDYCEQP-GCLRRAILAY 380
Cdd:PLN03137 770 RAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSPmamgynrmassgrilETNTENLLR-MVSYCENEvDCRRFLQLVH 848
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 381 FGETPAWRDCGH-CGNCDSPK--VEEKITPEVRLICLCVDELKGRFGMTMVCDILKGTANAKVRRYGFEGKASFGMLGDF 457
Cdd:PLN03137 849 FGEKFDSTNCKKtCDNCSSSKslIDKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHL 928
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 458 SQEEIRSLIRTCLQLHFL----EQSDGQYPVLSLTAAGREQ----LQSGRTVVRtkRIAAAPSAEKKKRFSAD------- 522
Cdd:PLN03137 929 SKGEASRILHYLVTEDILaedvKKSDLYGSVSSLLKVNESKayklFSGGQTIIM--RFPSSVKASKPSKFEATpakgplt 1006
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 523 --------IDEVALRPV--------FEILRSLRYRLAKE--EQIPPFVIFSDATLWEIAGRRPQSLDELGEVKGVGSFKL 584
Cdd:PLN03137 1007 sgkqstlpMATPAQPPVdlnlsailYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKV 1086
|
650
....*....|.
gi 553309361 585 HKYGHIFLEAL 595
Cdd:PLN03137 1087 SKYGDRLLETI 1097
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
5-200 |
7.71e-96 |
|
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: 291.36 E-value: 7.71e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 5 DVLKQYFGYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPALLMPGLTLVISPLISLMKDQVDSLLNQQIAATF 84
Cdd:cd17920 2 QILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 85 INSQCTFEESKERFSQICRSKFKLVYISPERLQNEFFTSLMKELP----LAMVVIDEAHCVSQWGHDFRPSYGAISSWIE 160
Cdd:cd17920 82 LNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLRR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 553309361 161 ALPQRPVVsAFTATATEKVKGDMLALLGLQKPQLFIGGFD 200
Cdd:cd17920 162 ALPGVPIL-ALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
4-200 |
1.17e-68 |
|
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: 220.98 E-value: 1.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 4 TDVLKQYFGYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPALLM----PGLTLVISPLISLMKDQVDSLlNQQ 79
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLrrrgPGLTLVVSPLIALMKDQVDAL-PRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 80 IAATFINSQCTFEESKERFSQICRSKFKLVYISPERLQNEFFTSLMKEL-PLAMVVIDEAHCVSQWGHDFRPSYGAISSW 158
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTpPISLLVVDEAHCISEWSHNFRPDYLRLCRV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553309361 159 IEALPQRPVVSAFTATATEKVKGDMLALLGLQKPQLFIGGFD 200
Cdd:cd18018 160 LRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
4-200 |
5.19e-62 |
|
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: 204.14 E-value: 5.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 4 TDVLKQYFGYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPALLMPGLTLVISPLISLMKDQVDSLLNQQIAAT 83
Cdd:cd18015 7 KDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 84 FINSQCTFEESKERFSQIC--RSKFKLVYISPERL--QNEFFTSLMKELP---LAMVVIDEAHCVSQWGHDFRPSYGAIS 156
Cdd:cd18015 87 MLNASSSKEHVKWVHAALTdkNSELKLLYVTPEKIakSKRFMSKLEKAYNagrLARIAIDEVHCCSQWGHDFRPDYKKLG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553309361 157 SWIEALPQRPVVsAFTATATEKVKGDMLALLGLQKPQLFIGGFD 200
Cdd:cd18015 167 ILKRQFPNVPIL-GLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
201-331 |
1.50e-60 |
|
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: 197.43 E-value: 1.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 201 RPNLYFRVV---GNGDRMAFLEAYLREHRRDSGIIYGATRKDVDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDR 277
Cdd:cd18794 1 RPNLFYSVRpkdKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 553309361 278 LAVIVATNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAGRDGAPGECILLF 331
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DpdF |
NF041063 |
protein DpdF; |
3-336 |
3.84e-60 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 214.39 E-value: 3.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 3 PTD-VLKQYFGYTAFR-PGQ-EAVVTALLQQRDS--LVIMPTGAGKSLCFQIPALLMP---GLTLVISPLISLMKDQ--- 71
Cdd:NF041063 126 PGDpFLAEALGFTHYRsPGQrEAVRAALLAPPGStlIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALAIDQerr 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 72 VDSLLNQQIAATFIN----SQCTFEESKERFSQICRSKFKLVYISPERLQneffTSLMKEL-------PLAMVVIDEAHC 140
Cdd:NF041063 206 ARELLRRAGPDLGGPlawhGGLSAEERAAIRQRIRDGTQRILFTSPESLT----GSLRPALfdaaeagLLRYLVVDEAHL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 141 VSQWGHDFRPSYGAISSWIEAL------PQRPVVSAFTATATEKVKgDMLALL--GLQKPQLFIGGFDR--PNLYF-RVV 209
Cdd:NF041063 282 VDQWGDGFRPEFQLLAGLRRSLlrlapsGRPFRTLLLSATLTESTL-DTLETLfgPPGPFIVVSAVQLRpePAYWVaKCD 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 210 GNGDRMAF-LEAyLREHRRDSgIIYGATRKDVDRIYQRLQRQGFS-VGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAF 287
Cdd:NF041063 361 SEEERRERvLEA-LRHLPRPL-ILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAF 438
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 553309361 288 GMGIDKSNVRFVIHYQMPKNMESYYQEAGRAGRDGAPGECILLFSRQDI 336
Cdd:NF041063 439 GLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDL 487
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
5-200 |
2.59e-58 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 193.45 E-value: 2.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 5 DVLKQYFGYTAFRPGQEAVVTALLQQR-DSLVIMPTGAGKSLCFQIPALLMPGLTLVISPLISLMKDQVDSLLNQQIAAT 83
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVIRSVLEERrDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 84 FINSqctfEESKERFSQICRSKFKLVYISPERLQN--EFFTSLMKELPLamVVIDEAHCVSQWGHDFRPSYGAISSWIEA 161
Cdd:cd18017 82 FLGS----AQSQNVLDDIKMGKIRVIYVTPEFVSKglELLQQLRNGITL--IAIDEAHCVSQWGHDFRSSYRHLGSIRNR 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 553309361 162 LPQRPVVsAFTATATEKVKGDMLALLGLQKPQLFIGGFD 200
Cdd:cd18017 156 LPNVPIV-ALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
5-200 |
5.40e-55 |
|
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: 185.42 E-value: 5.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 5 DVLKQYFGYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPALLMPGLTLVISPLISLMKDQVDSLLNQQIAATF 84
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 85 INSQCTFEESKERFSQICRSK--FKLVYISPE------RLQNEFFTSLMKELpLAMVVIDEAHCVSQWGHDFRPSYGAIS 156
Cdd:cd18016 87 LTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEkisasnRLISTLENLYERKL-LARFVIDEAHCVSQWGHDFRPDYKRLN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553309361 157 SWIEALPQRPVVsAFTATATEKVKGDMLALLGLQKPQLFIGGFD 200
Cdd:cd18016 166 MLRQKFPSVPMM-ALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
6-192 |
4.55e-52 |
|
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: 177.66 E-value: 4.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 6 VLKQYFGYTAFR-PGQEAVVTALLQQR-DSLVIMPTGAGKSLCFQIPALLMPGLTLVISPLISLMKDQVDSLLNQQIAAT 83
Cdd:cd18014 3 TLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 84 FINSQCTFEESKERFS--QICRSKFKLVYISPERLQNEFFTSLMKEL----PLAMVVIDEAHCVSQWGHDFRPSYGAISS 157
Cdd:cd18014 83 SLNSKLSAQERKRIIAdlESEKPQTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLRLGA 162
|
170 180 190
....*....|....*....|....*....|....*
gi 553309361 158 WIEALPQRPVVsAFTATATEKVKGDMLALLGLQKP 192
Cdd:cd18014 163 LRSRYGHVPWV-ALTATATPQVQEDIFAQLRLKKP 196
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
17-180 |
1.83e-27 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 108.48 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 17 RPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPAL------LMPGLTLVISPLISLMKDQVDSlLNQQIAATFINSQCT 90
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEE-LKKLGKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 91 F--EESKERFSQICRSkfKLVYISPERLQNEF-FTSLMKElpLAMVVIDEAHCVSQWGhdFRPSYGAIsswIEALPQRPV 167
Cdd:pfam00270 80 LggDSRKEQLEKLKGP--DILVGTPGRLLDLLqERKLLKN--LKLLVLDEAHRLLDMG--FGPDLEEI---LRRLPKKRQ 150
|
170
....*....|...
gi 553309361 168 VSAFTATATEKVK 180
Cdd:pfam00270 151 ILLLSATLPRNLE 163
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
12-345 |
1.50e-26 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 112.55 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 12 GYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPAL--LMPGL-----TLVISP---LIslmkdqvdsllnQQIA 81
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPtreLA------------LQVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 82 ATFinsqctfeeskERFSQICRSKFKLVY----ISPE----------------RL-----QNEFFTSLMKelplaMVVID 136
Cdd:COG0513 89 EEL-----------RKLAKYLGLRVATVYggvsIGRQiralkrgvdivvatpgRLldlieRGALDLSGVE-----TLVLD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 137 EAhcvsqwghD------FRPsygAISSWIEALPQRPVVSAFTATATEKVKGdmLALLGLQKPQlFIGgFDRPNL------ 204
Cdd:COG0513 153 EA--------DrmldmgFIE---DIERILKLLPKERQTLLFSATMPPEIRK--LAKRYLKNPV-RIE-VAPENAtaetie 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 205 -YFRVVGNGDRMAFLEAYLREHRRDSGIIYGATRKDVDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVA 283
Cdd:COG0513 218 qRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVA 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553309361 284 TNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAGRDGAPGECILLFSRQDI-MIQNylIER 345
Cdd:COG0513 298 TDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERrLLRA--IEK 358
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
241-322 |
6.46e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 98.44 E-value: 6.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 241 DRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAGR 320
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 553309361 321 DG 322
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
213-322 |
1.39e-24 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 98.44 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 213 DRMAFLEAYLREHRRDSGIIYGATRKDVDRIYqRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGID 292
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 553309361 293 KSNVRFVIHYQMPKNMESYYQEAGRAGRDG 322
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
10-205 |
2.34e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.95 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 10 YFGYTAFRPGQEAVVTALLQ-QRDSLVIMPTGAGKSLCFQIPALL-----MPGLTLVISPLISLMKDQVDSLlnQQIAAT 83
Cdd:smart00487 3 KFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEEL--KKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 84 FINSQCTF---EESKERFSQICRSKFKLVYISPERLQNEFFTSLMKELPLAMVVIDEAHCVSQWGhdFRPSYGAIsswIE 160
Cdd:smart00487 81 LGLKVVGLyggDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL---LK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553309361 161 ALPQRPVVSAFTATATEKVkgDMLALLGLQKPQLFIGGFDRPNLY 205
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEI--ENLLELFLNDPVFIDVGFTPLEPI 198
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
205-331 |
3.97e-23 |
|
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: 95.27 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 205 YFRVVGNGDR-MAFLEAYLREHRRDSGIIYGATRKDVDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVA 283
Cdd:cd18787 4 LYVVVEEEEKkLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 553309361 284 TNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAGRDGAPGECILLF 331
Cdd:cd18787 84 TDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
399-506 |
4.94e-22 |
|
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: 91.06 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 399 PKVEEKITPEVRLICLCVDELKGRFGMTMVCDILKGTANAKVRRYGFEGKASFGMLGDFSQEEIRSLIRTCLQLHFLEQS 478
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*...
gi 553309361 479 DGQYPVLSLTAAGREQLQSGRTVVRTKR 506
Cdd:pfam09382 81 IEFYSVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
405-493 |
1.33e-21 |
|
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: 89.46 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 405 ITPEVRLICLCVDELKGRFGMTMVCDILKGTANAKVRRYGFEGKASFGMLGDFSQEEIRSLIRTCLQLHFLEQSDGQYPV 484
Cdd:smart00956 2 VTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYPY 81
|
....*....
gi 553309361 485 LSLTAAGRE 493
Cdd:smart00956 82 LKLTEKARP 90
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
333-396 |
9.38e-20 |
|
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
Pssm-ID: 465031 [Multi-domain] Cd Length: 66 Bit Score: 83.11 E-value: 9.38e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553309361 333 RQDIMIQNYLIERSVHDQQQQRHEKLLLRQMIDYCE-QPGCLRRAILAYFGETPAWRDCGHCGNC 396
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCEnTTDCRRKQLLRYFGEEFDSEPCGNCDNC 65
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
17-331 |
4.93e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 90.85 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 17 RPGQEAVVTALLQQRDS-----LVIMPTGAGKSLCFQ--IPALLMPGLTLVISPLISLMKdqvdsllnqQIAATFINSQC 89
Cdd:COG1061 82 RPYQQEALEALLAALERgggrgLVVAPTGTGKTVLALalAAELLRGKRVLVLVPRRELLE---------QWAEELRRFLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 90 TFEESKERFSqicrSKFKLVYISPERLQNEFFTSLMKELPlAMVVIDEAHcvsqwgHDFRPSYGAIsswIEALPQRPVVs 169
Cdd:COG1061 153 DPLAGGGKKD----SDAPITVATYQSLARRAHLDELGDRF-GLVIIDEAH------HAGAPSYRRI---LEAFPAAYRL- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 170 AFTATATEKVKGDMLALL----------------GLQKPQLFIGGFDR------------PNLYFRVVGNGDRM-AFLEA 220
Cdd:COG1061 218 GLTATPFRSDGREILLFLfdgivyeyslkeaiedGYLAPPEYYGIRVDltderaeydalsERLREALAADAERKdKILRE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 221 YLREHRRDS-GIIYGATRKDVDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFV 299
Cdd:COG1061 298 LLREHPDDRkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVA 377
|
330 340 350
....*....|....*....|....*....|..
gi 553309361 300 IHYQMPKNMESYYQEAGRAGRDGAPGECILLF 331
Cdd:COG1061 378 ILLRPTGSPREFIQRLGRGLRPAPGKEDALVY 409
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
531-595 |
6.75e-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: 81.04 E-value: 6.75e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553309361 531 VFEILRSLRYRLAKEEQIPPFVIFSDATLWEIAGRRPQSLDELGEVKGVGSFKLHKYGHIFLEAL 595
Cdd:pfam00570 4 LLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
20-349 |
5.48e-18 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 87.97 E-value: 5.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 20 QEAVVTALLQQRDSLVIMPTGAGKSLCFQIPALLM----PGLT-LVISPLISLMKDQVDSL--LNQQI-----AATFINS 87
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAlledPGATaLYLYPTKALARDQLRRLreLAEALglgvrVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 88 QctfeESKERfSQIcRSKFKLVYISPERL------QNEFFTSLMKELplAMVVIDEAHcvsqwghdfrpSY----GAISS 157
Cdd:COG1205 141 T----PPEER-RWI-REHPDIVLTNPDMLhygllpHHTRWARFFRNL--RYVVIDEAH-----------TYrgvfGSHVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 158 WI--------EALPQRPVV---SAFTATATEkvkgdmLA--LLGL-----------QKPQLFIggFDRPNLYFRVVgngD 213
Cdd:COG1205 202 NVlrrlrricRHYGSDPQFilaSATIGNPAE------HAerLTGRpvtvvdedgspRGERTFV--LWNPPLVDDGI---R 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 214 RMAFLEA------YLREHRRdsGIIYGATRKDVDRIYQRLQRQ------GFSVGRYHAGLSDEERRRVQEAFSYDRLAVI 281
Cdd:COG1205 271 RSALAEAarlladLVREGLR--TLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGELLGV 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553309361 282 VATNAFGMGIDKSNVRFVI--HYqmPKNMESYYQEAGRAGRDGAPGECILLfSRQDIM----IQN--YLIERSVHD 349
Cdd:COG1205 349 VSTNALELGIDIGGLDAVVlaGY--PGTRASFWQQAGRAGRRGQDSLVVLV-AGDDPLdqyyVRHpeELFERPPEA 421
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
28-325 |
4.18e-16 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 81.36 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 28 LQQRDSLVIMPTGAGKSLCFQIPA--------LLMPG---LTLVISPLISLMkDQVDSLLNQQIAATFINSQCTFEESKE 96
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPTRELA-EQIREQCNKFGASSKIRNTVAYGGVPK 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 97 RFSQIC-RSKFKLVYISPERLQN---EFFTSLMKelpLAMVVIDEAHCVSQWGhdFRPSYGAISSWIEalPQRPVVsAFT 172
Cdd:PTZ00110 244 RGQIYAlRRGVEILIACPGRLIDfleSNVTNLRR---VTYLVLDEADRMLDMG--FEPQIRKIVSQIR--PDRQTL-MWS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 173 ATATEKVKGDMLALLGLQKPQLFIGGFD-----RPNLYFRVVGNGDRMAFLEAYLREHRRDSG--IIYGATRKDVDRIYQ 245
Cdd:PTZ00110 316 ATWPKEVQSLARDLCKEEPVHVNVGSLDltachNIKQEVFVVEEHEKRGKLKMLLQRIMRDGDkiLIFVETKKGADFLTK 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 246 RLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAGRDGAPG 325
Cdd:PTZ00110 396 ELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKG 475
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
524-598 |
1.01e-15 |
|
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: 72.33 E-value: 1.01e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553309361 524 DEVALRpVFEILRSLRYRLAKEEQIPPFVIFSDATLWEIAGRRPQSLDELGEVKGVGSFKLHKYGHIFLEALREF 598
Cdd:smart00341 1 RERQLR-LLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEA 74
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
231-322 |
4.09e-15 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 72.67 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 231 IIYGATRKDVDRIY----QRLQRQGFSVGR---YHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQ 303
Cdd:cd18797 39 IVFCRSRKLAELLLrylkARLVEEGPLASKvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90
....*....|....*....
gi 553309361 304 MPKNMESYYQEAGRAGRDG 322
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRG 137
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
208-335 |
1.90e-13 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 73.02 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 208 VVGNGDRMAFLEAYLREHRRDSGIIYgATRKD-VDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNA 286
Cdd:PRK01297 316 AVAGSDKYKLLYNLVTQNPWERVMVF-ANRKDeVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDV 394
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 553309361 287 FGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAGRDGAPGECILLFSRQD 335
Cdd:PRK01297 395 AGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
231-336 |
2.06e-12 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 69.08 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 231 IIYGATRKDVDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPKNMES 310
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100
....*....|....*....|....*.
gi 553309361 311 YYQEAGRAGRDGAPGECILLFSRQDI 336
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDI 376
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
275-330 |
7.45e-12 |
|
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: 61.18 E-value: 7.45e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 553309361 275 YDRLAVIVATNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAGRDGA-PGECILL 330
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKdEGEVILF 76
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
216-320 |
3.92e-11 |
|
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: 61.51 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 216 AFLEAYLREHRRDSG-IIYGATRKDVDRIYQRL------QRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFG 288
Cdd:cd18796 26 DAYAEVIFLLERHKStLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLE 105
|
90 100 110
....*....|....*....|....*....|..
gi 553309361 289 MGIDKSNVRFVIHYQMPKNMESYYQEAGRAGR 320
Cdd:cd18796 106 LGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
12-335 |
6.39e-11 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 64.81 E-value: 6.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 12 GYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIP-----ALLMPG--------LTLVISP---LISLMKDQVdSL 75
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrcCTIRSGhpseqrnpLAMVLTPtreLCVQVEDQA-KV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 76 LNQQIAatFINSQCTFEESKERfsQICRSK--FKLVYISPERLqnefFTSLMK-ELPLA---MVVIDEAHCVSQWGhdFR 149
Cdd:PLN00206 219 LGKGLP--FKTALVVGGDAMPQ--QLYRIQqgVELIVGTPGRL----IDLLSKhDIELDnvsVLVLDEVDCMLERG--FR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 150 PSYGAIsswIEALPQrPVVSAFTAT---ATEKVKGDMLALLGLqkpqLFIGGFDRPNLYFRVVG------NGDRMAFLEA 220
Cdd:PLN00206 289 DQVMQI---FQALSQ-PQVLLFSATvspEVEKFASSLAKDIIL----ISIGNPNRPNKAVKQLAiwvetkQKKQKLFDIL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 221 YLREHRRDSGIIYGATRKDVDRIYQRLQR-QGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFV 299
Cdd:PLN00206 361 KSKQHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQV 440
|
330 340 350
....*....|....*....|....*....|....*.
gi 553309361 300 IHYQMPKNMESYYQEAGRAGRDGAPGECILLFSRQD 335
Cdd:PLN00206 441 IIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEED 476
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
5-384 |
2.41e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 62.99 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 5 DVLKQyFGYTAFRPGQEAVVTALLQQRDSLVI-MPTGAGKSLCFQIP---ALLMPGLTLVISPLISLmkdqvdsllnqqi 80
Cdd:COG1204 13 EFLKE-RGIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTLIAELAilkALLNGGKALYIVPLRAL------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 81 aatfINsqctfeESKERFSQICRSKFKLVYIS-------PERLQN--------EFFTSLMKELP-----LAMVVIDEAHC 140
Cdd:COG1204 79 ----AS------EKYREFKRDFEELGIKVGVStgdydsdDEWLGRydilvatpEKLDSLLRNGPswlrdVDLVVVDEAHL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 141 VsqwGHDFR---------------------------PSYGAISSWIEAlpqRPVVSAFTATAtekvkgdmlallglqkpq 193
Cdd:COG1204 149 I---DDESRgptlevllarlrrlnpeaqivalsatiGNAEEIAEWLDA---ELVKSDWRPVP------------------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 194 LFIGGFDRPNLYF--RVVGNGDRMAFLeayLREHRRDSG--IIYGATRKDV----DRIYQRLQRQGFS------------ 253
Cdd:COG1204 205 LNEGVLYDGVLRFddGSRRSKDPTLAL---ALDLLEEGGqvLVFVSSRRDAeslaKKLADELKRRLTPeereeleelaee 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 254 ---------------------VGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIdksN--VRFVI----HYQMPK 306
Cdd:COG1204 282 llevseethtnekladclekgVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV---NlpARRVIirdtKRGGMV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 307 NMES--YYQEAGRAGRdgaP-----GECILLFSRQDIMiqNYLIERSVHDQQ-----QQRHEKLLLRQMIDYCEQPGCLR 374
Cdd:COG1204 359 PIPVleFKQMAGRAGR---PgydpyGEAILVAKSSDEA--DELFERYILGEPepirsKLANESALRTHLLALIASGFANS 433
|
490
....*....|.
gi 553309361 375 RA-ILAYFGET 384
Cdd:COG1204 434 REeLLDFLENT 444
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
34-174 |
3.76e-10 |
|
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: 58.57 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 34 LVIMPTGAGKSLCFQIPA---LLMPGL-TLVISPLISLMKDQ---VDSLLNQQIAATFINSqctFEESKERFSQIcRSKF 106
Cdd:cd00046 5 LITAPTGSGKTLAALLAAlllLLKKGKkVLVLVPTKALALQTaerLRELFGPGIRVAVLVG---GSSAEEREKNK-LGDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553309361 107 KLVYISPERLqnefFTSLMKEL-----PLAMVVIDEAHCVSQWGHDFRPSYGAIssWIEALPQRPVVSaFTAT 174
Cdd:cd00046 81 DIIIATPDML----LNLLLREDrlflkDLKLIIVDEAHALLIDSRGALILDLAV--RKAGLKNAQVIL-LSAT 146
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
16-174 |
7.25e-10 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 58.07 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 16 FRPGQEAVVTALL-----QQRDSLVIMPTGAGKSLC-FQIPALLMPGL----TLVISPLISLMKDQVDSLLNQQIAATFI 85
Cdd:pfam04851 4 LRPYQIEAIENLLesiknGQKRGLIVMATGSGKTLTaAKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 86 NsqctfEESKERFSQICRSKFKLVYISPERLQNEFFTSLMKELPLA--MVVIDEAHcvsqwgHDFRPSYGAIsswIEALp 163
Cdd:pfam04851 84 G-----EIISGDKKDESVDDNKIVVTTIQSLYKALELASLELLPDFfdVIIIDEAH------RSGASSYRNI---LEYF- 148
|
170
....*....|.
gi 553309361 164 QRPVVSAFTAT 174
Cdd:pfam04851 149 KPAFLLGLTAT 159
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
12-347 |
1.28e-09 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 61.02 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 12 GYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPAL--LMPGL----TLVISPLISL-------MKDQVDSLLNQ 78
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnLDPELkapqILVLAPTRELavqvaeaMTDFSKHMRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 79 QIAATFinsqctfeeSKERFS---QICRSKFKLVYISPERLQNEFFTSLMKELPLAMVVIDEAHCVSQWGhdFRPSYGAI 155
Cdd:PRK11634 105 NVVALY---------GGQRYDvqlRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG--FIEDVETI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 156 SSWIEALPQrpvVSAFTATATEKVKgdMLALLGLQKPQ---LFIGGFDRPNL---YFRVVG---NGDRMAFLEAylreHR 226
Cdd:PRK11634 174 MAQIPEGHQ---TALFSATMPEAIR--RITRRFMKEPQevrIQSSVTTRPDIsqsYWTVWGmrkNEALVRFLEA----ED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 227 RDSGIIYGATRKDVDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPK 306
Cdd:PRK11634 245 FDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM 324
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 553309361 307 NMESYYQEAGRAGRDGAPGECILLF-SRQDIMIQNylIERSV 347
Cdd:PRK11634 325 DSESYVHRIGRTGRAGRAGRALLFVeNRERRLLRN--IERTM 364
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
534-597 |
5.35e-09 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 58.34 E-value: 5.35e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553309361 534 ILRSL---RYRLAKEEQIPPFVIFSDATLWEIAGRRPQSLDELGEVKGVGSFKLHKYGHIFLEALRE 597
Cdd:COG0349 212 VLRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAE 278
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
189-330 |
1.90e-08 |
|
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: 53.71 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 189 LQKPQLFIGG-FDRPNLYFRVVGNGDRMAFLEayLREHRRDSG-IIYGATRKDVDRIYQRLqrqgFSVGRYHAGLSDEER 266
Cdd:cd18795 5 LEEYVLGFNGlGIKLRVDVMNKFDSDIIVLLK--IETVSEGKPvLVFCSSRKECEKTAKDL----AGIAFHHAGLTREDR 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553309361 267 RRVQEAFSYDRLAVIVATNAFGMGID--------KSNVRFVIHYQMPKNMESYYQEAGRAGRdgaP-----GECILL 330
Cdd:cd18795 79 ELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKGYRELSPLEYLQMIGRAGR---PgfdtrGEAIIM 152
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
16-174 |
2.75e-08 |
|
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: 53.08 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 16 FRPGQEAVVTALLQ---QRDSLVIMPTGAGKSLC-FQIPALLMPGLTLVISPLISLMKDQVDsllnqQIAATFINSQCTF 91
Cdd:cd17926 1 LRPYQEEALEAWLAhknNRRGILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKE-----RFEDFLGDSSIGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 92 EESKERFSQICRSkfklVYIS-PERLQNEFFT-SLMKELPLAMVViDEAHcvsqwgHdfrpsYGAiSSWIEALPQ--RPV 167
Cdd:cd17926 76 IGGGKKKDFDDAN----VVVAtYQSLSNLAEEeKDLFDQFGLLIV-DEAH------H-----LPA-KTFSEILKElnAKY 138
|
....*..
gi 553309361 168 VSAFTAT 174
Cdd:cd17926 139 RLGLTAT 145
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
12-192 |
3.75e-07 |
|
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: 50.75 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 12 GYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPAL---------LMPGL-TLVISPLISLMKDQVDSLlnQQI- 80
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLeklyrerwtPEDGLgALIISPTRELAMQIFEVL--RKVg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 81 ------AATFINSQcTFEESKERFSQIcrskfKLVYISPER-LQNefftslMKELP------LAMVVIDEAHCVSQWGhd 147
Cdd:cd17941 87 kyhsfsAGLIIGGK-DVKEEKERINRM-----NILVCTPGRlLQH------MDETPgfdtsnLQMLVLDEADRILDMG-- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553309361 148 FRPSYGAIsswIEALPQRPVVSAFTATATEKVKgdMLALLGLQKP 192
Cdd:cd17941 153 FKETLDAI---VENLPKSRQTLLFSATQTKSVK--DLARLSLKNP 192
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
9-139 |
4.52e-07 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 50.28 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 9 QYFGYTAFRPGQEAVVTAllqqrdslvimPTGAGKSLCFQIPAL--LM--PGLT-LVISPLISLMKDQVDSL--LNQQIA 81
Cdd:cd17923 5 QAEAIEAARAGRSVVVTT-----------GTASGKSLCYQLPILeaLLrdPGSRaLYLYPTKALAQDQLRSLreLLEQLG 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553309361 82 ATFINSQCTFEESKERFSQICRSKFKLVYISPERL------QNEFFTSLMKELPLamVVIDEAH 139
Cdd:cd17923 74 LGIRVATYDGDTPREERRAIIRNPPRILLTNPDMLhyallpHHDRWARFLRNLRY--VVLDEAH 135
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
5-192 |
1.78e-06 |
|
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: 49.11 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 5 DVLKQyFGYTAFRPGQEAVVTALLQQRDSLVIMPTGAGKSLCFQIPALLM----------PGLT-LVISPLISLmKDQVD 73
Cdd:cd17960 3 DVVAE-LGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEIllkrkanlkkGQVGaLIISPTREL-ATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 74 SLLNQQIAATFINSQCTF----EESKERFSQICRSKFKLVYISPERLqNEFFTSLMKELP---LAMVVIDEAHCVSQWGh 146
Cdd:cd17960 81 EVLQSFLEHHLPKLKCQLliggTNVEEDVKKFKRNGPNILVGTPGRL-EELLSRKADKVKvksLEVLVLDEADRLLDLG- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553309361 147 dFRPSYGAIsswIEALPQRPVVSAFTATATEKVkgDMLALLGLQKP 192
Cdd:cd17960 159 -FEADLNRI---LSKLPKQRRTGLFSATQTDAV--EELIKAGLRNP 198
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
231-320 |
4.81e-06 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 49.50 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 231 IIYGATRKDVDRIYQRLqrqGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGID--KSNVRFvihyqmpknm 308
Cdd:COG1202 431 IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDfpASQVIF---------- 497
|
90 100
....*....|....*....|....
gi 553309361 309 ES------------YYQEAGRAGR 320
Cdd:COG1202 498 DSlamgiewlsvqeFHQMLGRAGR 521
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
20-322 |
5.97e-06 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 49.11 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 20 QEAVVTALLQQRDSLVIMPTGAGKSLC--FQIPALLMPGL-TLVISPLISLMKDQVDSLLNQQIAATFINSQCTFEESKE 96
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIaySAIYETFLAGLkSIYIVPLRSLAMEKYEELSRLRSLGMRVKISIGDYDDPP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 97 RFSQicrsKFKLVYISPERLQnefftSLMKELP-----LAMVVIDEAHCVsqwGHDFR-PSYGAISSWIEALPQRPVVSA 170
Cdd:PRK01172 107 DFIK----RYDVVILTSEKAD-----SLIHHDPyiindVGLIVADEIHII---GDEDRgPTLETVLSSARYVNPDARILA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 171 FTATATEK-----------VKGDMLAL---LG-LQKPQLFIGGFDRP----NLYFR--VVGNGDRMAFLEAYLREHR--- 226
Cdd:PRK01172 175 LSATVSNAnelaqwlnaslIKSNFRPVplkLGiLYRKRLILDGYERSqvdiNSLIKetVNDGGQVLVFVSSRKNAEDyae 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 227 -------RDSGIIYGATRKDV-DRIYQRLQRQGfsVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSnVRF 298
Cdd:PRK01172 255 mliqhfpEFNDFKVSSENNNVyDDSLNEMLPHG--VAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP-ARL 331
|
330 340 350
....*....|....*....|....*....|....
gi 553309361 299 VIHYQMPK----------NMEsYYQEAGRAGRDG 322
Cdd:PRK01172 332 VIVRDITRygnggirylsNME-IKQMIGRAGRPG 364
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
214-338 |
1.49e-05 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 47.63 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 214 RMAFLEAYLREHRRDSGIIYGATRKDVDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDK 293
Cdd:PRK11192 232 KTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDI 311
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 553309361 294 SNVRFVIHYQMPKNMESYYQEAGRAGRDGAPGECILLFSRQDIMI 338
Cdd:PRK11192 312 DDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLL 356
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
257-344 |
1.58e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 48.38 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 257 YHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAGRD--GAPGECILLFSRQ 334
Cdd:PRK09751 307 HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQvgGVSKGLFFPRTRR 386
|
90
....*....|
gi 553309361 335 DIMIQNYLIE 344
Cdd:PRK09751 387 DLVDSAVIVE 396
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
16-143 |
1.75e-05 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 45.72 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 16 FRPGQEAVVTALLQQRDSLVI-MPTGAGKSLCFQIPALL----MPGLTLVISPLISLMkDQVDSLLNQQIAATFIN-SQC 89
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVsAPTSSGKTLIAELAILRalatSGGKAVYIAPTRALV-NQKEADLRERFGPLGKNvGLL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 90 TFEESKERFSQicrSKFKLVYISPERLQN------EFFTSlmkelPLAMVVIDEAHCVSQ 143
Cdd:cd17921 81 TGDPSVNKLLL---AEADILVATPEKLDLllrnggERLIQ-----DVRLVVVDEAHLIGD 132
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
214-322 |
2.17e-05 |
|
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: 44.39 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 214 RMAFLEAYLREHRRDSG--IIYGATRKDVDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFS--YDRLAVIVATNAFGM 289
Cdd:cd18793 12 KLEALLELLEELREPGEkvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|....*
gi 553309361 290 GIDKSNVRFVIHYQMPKN--MESyyQEAGRAGRDG 322
Cdd:cd18793 92 GLNLTAANRVILYDPWWNpaVEE--QAIDRAHRIG 124
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
231-330 |
2.25e-05 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 47.11 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 231 IIYGATRKDVDRIYQRLQRQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPKNMES 310
Cdd:PRK10590 249 LVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPED 328
|
90 100
....*....|....*....|
gi 553309361 311 YYQEAGRAGRDGAPGECILL 330
Cdd:PRK10590 329 YVHRIGRTGRAAATGEALSL 348
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
31-139 |
6.43e-05 |
|
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: 43.73 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 31 RDSLVIMPTGAGKSLCFQIPAL-------LMPGLTLVISPLISLMKDQVDSLlnqQIAATFINSQCTFE------ESKER 97
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALssladepEKGVQVLYISPLKALINDQERRL---EEPLDEIDLEIPVAvrhgdtSQSEK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 553309361 98 FSQICRSKFKLVyISPERLQ----NEFFTSLMKElpLAMVVIDEAH 139
Cdd:cd17922 79 AKQLKNPPGILI-TTPESLElllvNKKLRELFAG--LRYVVVDEIH 121
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
257-330 |
7.32e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 45.72 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 257 YHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIH-YQ--------MPKNMESYYQEAGRAGRDGA-P-G 325
Cdd:PRK02362 309 HHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRdYRrydggagmQPIPVLEYHQMAGRAGRPGLdPyG 388
|
....*
gi 553309361 326 ECILL 330
Cdd:PRK02362 389 EAVLL 393
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
218-322 |
7.59e-05 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 45.70 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 218 LEAYLREHRRDSGIIYGatrkdvdRIYQRLQRQGFSVgrYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIdksNV- 296
Cdd:COG4581 275 IREAIDEFAEDFSVLFG-------KTLSRLLRRGIAV--HHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGI---NMp 342
|
90 100 110
....*....|....*....|....*....|....*.
gi 553309361 297 -RFVIHYQMPK-NMES--------YYQEAGRAGRDG 322
Cdd:COG4581 343 aRTVVFTKLSKfDGERhrpltareFHQIAGRAGRRG 378
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
251-330 |
1.14e-03 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 39.50 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 251 GFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPKNMESYYQEAGRAGRDGApgECILL 330
Cdd:cd18802 64 GNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNS--KYILM 141
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
239-331 |
1.96e-03 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members 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: 350178 [Multi-domain] Cd Length: 171 Bit Score: 39.44 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 239 DVDRIYQRLQRQ--GFSVGRY-----HAGLSDEERRRVQEAFSYDRLAVIVATN-A-FGMGIDksNVRFVI--------H 301
Cdd:cd18791 55 EIERLCELLREEllSPDLGKLlvlplHSSLPPEEQQRVFEPPPPGVRKVVLATNiAeTSITIP--GVVYVIdsglvkekV 132
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 553309361 302 YQMPKNMESYY----------QEAGRAGRDGaPGECILLF 331
Cdd:cd18791 133 YDPRTGLSSLVtvwiskasaeQRAGRAGRTR-PGKCYRLY 171
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
11-196 |
2.65e-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: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 11 FGYTAFRPGQEAVVTALLQQ---------RDSLVIMPTGAGKSLCFQIP---ALL---MPGL-TLVISPlislMKDqvds 74
Cdd:cd17956 8 NGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPivqALSkrvVPRLrALIVVP----TKE---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 75 lLNQQIAATF-------------INSQCTFEESKERFSQICR----SKFKLVYISPERL-----QNEFFTslMKELPLam 132
Cdd:cd17956 80 -LVQQVYKVFeslckgtglkvvsLSGQKSFKKEQKLLLVDTSgrylSRVDILVATPGRLvdhlnSTPGFT--LKHLRF-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 133 VVIDEA----------------HCVSQWGHDFRPSYGAiSSWIEALPQRPVVSAFTATAT---EKvkgdmLALLGLQKPQ 193
Cdd:cd17956 155 LVIDEAdrllnqsfqdwletvmKALGRPTAPDLGSFGD-ANLLERSVRPLQKLLFSATLTrdpEK-----LSSLKLHRPR 228
|
...
gi 553309361 194 LFI 196
Cdd:cd17956 229 LFT 231
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
238-330 |
5.22e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 38.09 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553309361 238 KDVDRIYQRLQ---RQGFSVGRYHAGLSDEERRRVQEAFSYDRLAVIVATNAFGMGIDKSNVRFVIHYQMPK-NMESYYQ 313
Cdd:cd18811 45 KAAVAMYEYLKerfRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERfGLSQLHQ 124
|
90
....*....|....*..
gi 553309361 314 EAGRAGRDGAPGECILL 330
Cdd:cd18811 125 LRGRVGRGDHQSYCLLV 141
|
|
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