|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-474 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 740.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 1 MLQKAKEALSKYFGYDEFRGAQEKVIESILNKKDTVAIMPTGAGKSICYQIPALLTEGITIVISPLISLMKDQVDSLKAM 80
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 81 GIKATFINSSLNNLEIQERIFNANMGIYDLIYLAPERLESEGFCNSLNNLDISLIAVDEAHCVSQWGHDFRPSYTRISRF 160
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 161 IEGLEKRPIVtaftatatqtVKEDILKLLYLKEPEVFVTGVDRENLNFAVIRG--ENKDEFIYNYLNNNKGKIGIIYTST 238
Cdd:COG0514 161 RERLPNVPVLaltat-atprVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGGSGIVYCLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 239 RKDAESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAG 318
Cdd:COG0514 240 RKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 319 RAGRDGEKSECILLFSPRDIQIQKYFIDQGFLPPVRKNNEYNKLRAMVDYCYTSKCLRAYILEYFDEETnLENCGNCSTC 398
Cdd:COG0514 320 RAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEEL-AEPCGNCDNC 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499412780 399 NDDREEKDITIEAQKIFSCVYRMKESFGVNMIADTLKGSRNKKVLNAGLNRLSTYGIMSEFTQKQISSLINKLIAD 474
Cdd:COG0514 399 LGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
5-587 |
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: 728.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 5 AKEALSKYFGYDEFRGAQEKVIESILNKKDTVAIMPTGAGKSICYQIPALLTEGITIVISPLISLMKDQVDSLKAMGIKA 84
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 85 TFINSSLNNLEIQERIFNANMGIYDLIYLAPERLESEGFCNSLNNLDISLIAVDEAHCVSQWGHDFRPSYTRISRFIEGL 164
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 165 EKRPIVTAFTATATQtVKEDILKLLYLKEPEVFVTGVDRENLNFAVIRGENKDEFIYNYLNNNKGKIGIIYTSTRKDAES 244
Cdd:TIGR01389 161 PQVPRIALTATADAE-TRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 245 LYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDG 324
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 325 EKSECILLFSPRDIQIQKYFIDQGFLPPVRKNNEYNKLRAMVDYCYTSKCLRAYILEYFdEETNLENCGNCSTCNDDREE 404
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYF-GENEVEPCGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 405 KDITIEAQKIFSCVYRMKESFGVNMIADTLKGSRNKKVLNAGLNRLSTYGIMSEFTQKQISSLINKLIADGYLVTTDDKF 484
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 485 PVVKLQARANNVLKNKEPVY----------IKITKTKKISKPDNELLEILKDIRKEISQEAGIPPFMIFHDITLKELSEY 554
Cdd:TIGR01389 479 IGLQLTEAARKVLKNEVEVLlrpfkvvakeKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEK 558
|
570 580 590
....*....|....*....|....*....|...
gi 499412780 555 MPKDMENFLKIKGVGEKKAEVYGEKFISAICDY 587
Cdd:TIGR01389 559 RPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
5-587 |
7.50e-172 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 505.40 E-value: 7.50e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 5 AKEALSKYFGYDEFRGAQEKVIESILNKKDTVAIMPTGAGKSICYQIPALLTEGITIVISPLISLMKDQVDSLKAMGIKA 84
Cdd:PRK11057 13 AKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 85 TFINSSLNNLEIQERIFNANMGIYDLIYLAPERLESEGFCNSLNNLDISLIAVDEAHCVSQWGHDFRPSYTRISRFIEGL 164
Cdd:PRK11057 93 ACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 165 EKRPIVtAFTATATQTVKEDILKLLYLKEPEVFVTGVDRENLNFAVIRGENKDEFIYNYLNNNKGKIGIIYTSTRKDAES 244
Cdd:PRK11057 173 PTLPFM-ALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 245 LYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDG 324
Cdd:PRK11057 252 TAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 325 EKSECILLFSPRDIQIQKYFIDQGFLPPvRKNNEYNKLRAMVDYCYTSKCLRAYILEYFDeETNLENCGNCSTCNDDREE 404
Cdd:PRK11057 332 LPAEAMLFYDPADMAWLRRCLEEKPAGQ-QQDIERHKLNAMGAFAEAQTCRRLVLLNYFG-EGRQEPCGNCDICLDPPKQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 405 KDITIEAQKIFSCVYRMKESFGVNMIADTLKGSRNKKVLNAGLNRLSTYGIMSEFTQKQISSLINKLIADGYLVTTDDKF 484
Cdd:PRK11057 410 YDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 485 PVVKLQARANNVLKNKEP----------VYIKITKTKKISKPDNELLEILKDIRKEISQEAGIPPFMIFHDITLKELSEY 554
Cdd:PRK11057 490 SALQLTEAARPVLRGEVSlqlavprivaLKPRAMQKSFGGNYDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQ 569
|
570 580 590
....*....|....*....|....*....|...
gi 499412780 555 MPKDMENFLKIKGVGEKKAEVYGEKFISAICDY 587
Cdd:PRK11057 570 MPITASEMLSVNGVGQRKLERFGKPFMALIRAH 602
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
9-455 |
5.73e-149 |
|
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: 441.52 E-value: 5.73e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 9 LSKYFGYDEFRGAQEKVIESILNKKDTVAIMPTGAGKSICYQIPALLTEGITIVISPLISLMKDQVDSLKAMGIKATFIN 88
Cdd:TIGR00614 3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 89 SSLNNLEIQERIFNANMGIYDLIYLAPERL-ESEGFCNSLNN-LDISLIAVDEAHCVSQWGHDFRPSYTRISRFIEGLEK 166
Cdd:TIGR00614 83 SAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsASNRLLQTLEErKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFPN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 167 RPIVTAFTATATQtVKEDILKLLYLKEPEVFVTGVDRENLNFAVIRGENKDEF-IYNYLNNN-KGKIGIIYTSTRKDAES 244
Cdd:TIGR00614 163 VPVMALTATASPS-VREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPKILEdLLRFIRKEfEGKSGIIYCPSRKKVEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 245 LYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDG 324
Cdd:TIGR00614 242 VAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRDG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 325 EKSECILLFSPRDIQIQKYFIDQgflPPVRKNNEY-NKLRAMVDYC-YTSKCLRAYILEYFDEETNLEN---------CG 393
Cdd:TIGR00614 322 LPSECHLFYAPADMNRLRRLLME---EPDGNFRTYkLKLYEMMEYClNSSTCRRLILLSYFGEKGFNKSfcimgtekcCD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499412780 394 NCSTCND----DREEK--DITIEAQKIFSCVYRMKESFGVNMIADTLKGSRNKKVLNAGLNRLSTYGI 455
Cdd:TIGR00614 399 NCCKRLDyktkDVTDKvyDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGR 466
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
11-652 |
4.92e-99 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 330.32 E-value: 4.92e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 11 KYFGYDEFRGAQEKVIESILNKKDTVAIMPTGAGKSICYQIPALLTEGITIVISPLISLMKDQVDSLKAMGIKATFINSS 90
Cdd:PLN03137 454 KVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAG 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 91 LNNLEIQE--RIFNANMGIYDLIYLAPERL-ESEGFCNSLNNLD----ISLIAVDEAHCVSQWGHDFRPSYTRISRFIEG 163
Cdd:PLN03137 534 MEWAEQLEilQELSSEYSKYKLLYVTPEKVaKSDSLLRHLENLNsrglLARFVIDEAHCVSQWGHDFRPDYQGLGILKQK 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 164 LEKRPiVTAFTATATQTVKEDILKLLYLKEPEVFVTGVDRENLNFAVIRGENK-----DEFIYNylnNNKGKIGIIYTST 238
Cdd:PLN03137 614 FPNIP-VLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKclediDKFIKE---NHFDECGIIYCLS 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 239 RKDAESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAG 318
Cdd:PLN03137 690 RMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECG 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 319 RAGRDGEKSECILLFSPRDIQIQKYFIDQGFLPP----------------VRKNNEyNKLRaMVDYCYTS-KCLRAYILE 381
Cdd:PLN03137 770 RAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQspmamgynrmassgriLETNTE-NLLR-MVSYCENEvDCRRFLQLV 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 382 YFDEETNLENCGN-CSTCNDDRE--EKDITIEAQKIFSCVYRMKESFGVNMIADTLKGSRNKKVLNAGLNRLSTYGIMSE 458
Cdd:PLN03137 848 HFGEKFDSTNCKKtCDNCSSSKSliDKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKH 927
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 459 FTQKQISSLINKLIADGYL---VTTDDKFPVVKLQARANN-------------VLK-----------------NKEPVYI 505
Cdd:PLN03137 928 LSKGEASRILHYLVTEDILaedVKKSDLYGSVSSLLKVNEskayklfsggqtiIMRfpssvkaskpskfeatpAKGPLTS 1007
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 506 KITKTKKISKPDN---------ELLEILKDIRKEISQEA--GIPPFMIFHDITLKELSEYMPKDMENFLKIKGVGEKKAE 574
Cdd:PLN03137 1008 GKQSTLPMATPAQppvdlnlsaILYTALRKLRTALVKEAgdGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVS 1087
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 575 VYGEKFI----SAICDYTKEKNITAKSNEEYDMNKKSKEKThvITYNLYKE-------GKNIKEISKERNLQT---STIE 640
Cdd:PLN03137 1088 KYGDRLLetieSTINEYYKTDKNSSSSNDSPDSGKRRRDEN--INPNVAEDddftkstSQSKKKTVKNKNKGVehgNSRE 1165
|
730
....*....|..
gi 499412780 641 EHLFKCLNEDMD 652
Cdd:PLN03137 1166 TDRRNQCDDDLD 1177
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
6-202 |
1.63e-91 |
|
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: 283.27 E-value: 1.63e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 6 KEALSKYFGYDEFRGAQEKVIESILNKKDTVAIMPTGAGKSICYQIPALLTEGITIVISPLISLMKDQVDSLKAMGIKAT 85
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 86 FINSSLNNLEIQERIFNANMGIYDLIYLAPERLESEGFCNSLNNLD----ISLIAVDEAHCVSQWGHDFRPSYTRISRFI 161
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499412780 162 EGLEKRPIVtaftatatQTVKEDILKLLYLKEPEVFVTGVD 202
Cdd:cd17920 161 RALPGVPILalta-tatPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
7-189 |
4.61e-66 |
|
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: 216.35 E-value: 4.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 7 EALSKYFGYDEFRGAQEKVIESILNKKDTVAIMPTGAGKSICYQIPALL----TEGITIVISPLISLMKDQVDSLKAmGI 82
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPR-AI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 83 KATFINSSLNNLEIQERIFNANMGIYDLIYLAPERLESEGFCNSLNNLD-ISLIAVDEAHCVSQWGHDFRPSYTRISRFI 161
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPpISLLVVDEAHCISEWSHNFRPDYLRLCRVL 160
|
170 180
....*....|....*....|....*...
gi 499412780 162 EGLEKRPIVTAFTATATQTVKEDILKLL 189
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVEDIASHL 188
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
203-333 |
2.47e-54 |
|
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: 182.41 E-value: 2.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 203 RENLNFAVIRGENKDEFI---YNYLNNNKGKIGIIYTSTRKDAESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDN 279
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLdllKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 499412780 280 INIIVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEKSECILLF 333
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
8-202 |
9.49e-53 |
|
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: 180.74 E-value: 9.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 8 ALSKYFGYDEFRGAQEKVIESIL-NKKDTVAIMPTGAGKSICYQIPALLTEGITIVISPLISLMKDQVDSLKAMGIKATF 86
Cdd:cd18017 3 ALNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 87 INSSLNNLEIQErifnANMGIYDLIYLAPERLESE-GFCNSLNNlDISLIAVDEAHCVSQWGHDFRPSYTRISRFIEGLE 165
Cdd:cd18017 83 LGSAQSQNVLDD----IKMGKIRVIYVTPEFVSKGlELLQQLRN-GITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLP 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 499412780 166 KRPIVtAFTATATQTVKEDILKLLYLKEPEVFVTGVD 202
Cdd:cd18017 158 NVPIV-ALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
3-202 |
5.23e-50 |
|
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: 173.71 E-value: 5.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 3 QKAKEALSKYFGYDEFRGAQEKVIESILNKKDTVAIMPTGAGKSICYQIPALLTEGITIVISPLISLMKDQVDSLKAMGI 82
Cdd:cd18015 4 GKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 83 KATFINSSlNNLEIQERIFNANMGIYD---LIYLAPERL-ESEGFCNSL---NNLD-ISLIAVDEAHCVSQWGHDFRPSY 154
Cdd:cd18015 84 SATMLNAS-SSKEHVKWVHAALTDKNSelkLLYVTPEKIaKSKRFMSKLekaYNAGrLARIAIDEVHCCSQWGHDFRPDY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499412780 155 TRISRFIEGLEKRPIVtAFTATATQTVKEDILKLLYLKEPEVFVTGVD 202
Cdd:cd18015 163 KKLGILKRQFPNVPIL-GLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
6-194 |
1.51e-47 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 166.88 E-value: 1.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 6 KEALSKYFGYDEFRGA-QEKVIESILNKK-DTVAIMPTGAGKSICYQIPALLTEGITIVISPLISLMKDQVDSLKAMGIK 83
Cdd:cd18014 1 RSTLKKVFGHSDFKSPlQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 84 ATFINSSLNNLEIQERI--FNANMGIYDLIYLAPERLESEGFCNSLNNL----DISLIAVDEAHCVSQWGHDFRPSYTRI 157
Cdd:cd18014 81 VDSLNSKLSAQERKRIIadLESEKPQTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 499412780 158 SRFIEGLEKRPIVtAFTATATQTVKEDILKLLYLKEP 194
Cdd:cd18014 161 GALRSRYGHVPWV-ALTATATPQVQEDIFAQLRLKKP 196
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
9-198 |
9.19e-45 |
|
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: 159.22 E-value: 9.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 9 LSKYFGYDEFRGAQEKVIESILNKKDTVAIMPTGAGKSICYQIPALLTEGITIVISPLISLMKDQVDSLKAMGIKATFIN 88
Cdd:cd18016 9 FHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 89 SSLNNLEiQERIFnANMG----IYDLIYLAPERLESEGFCNS-LNNL-DISLIA---VDEAHCVSQWGHDFRPSYTRISR 159
Cdd:cd18016 89 GDKTDAE-ATKIY-LQLSkkdpIIKLLYVTPEKISASNRLIStLENLyERKLLArfvIDEAHCVSQWGHDFRPDYKRLNM 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 499412780 160 FIEGLEKRPIVtAFTATATQTVKEDILKLLYLKEPEVFV 198
Cdd:cd18016 167 LRQKFPSVPMM-ALTATATPRVQKDILNQLKMLRPQVFT 204
|
|
| DpdF |
NF041063 |
protein DpdF; |
8-340 |
5.12e-44 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 169.71 E-value: 5.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 8 ALSKYFGYDEFRG-AQEKVIESIL--NKKDTVAI-MPTGAGKSICYQIPALL---TEGITIVISPLISLMKDQ----VDS 76
Cdd:NF041063 130 FLAEALGFTHYRSpGQREAVRAALlaPPGSTLIVnLPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQerraREL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 77 LKAMGIKATFI------NSSLNNLEIQERIFNANMGIydlIYLAPERLesegfCNSL---------NNLdISLIAVDEAH 141
Cdd:NF041063 210 LRRAGPDLGGPlawhggLSAEERAAIRQRIRDGTQRI---LFTSPESL-----TGSLrpalfdaaeAGL-LRYLVVDEAH 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 142 CVSQWGHDFRPSYTRISRFIEGL-----EKRPIVtaftatatqtvkedilKLL--------------------------- 189
Cdd:NF041063 281 LVDQWGDGFRPEFQLLAGLRRSLlrlapSGRPFR----------------TLLlsatltestldtletlfgppgpfivvs 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 190 --YLK-EPEVFVTGVDREnlnfavirgENKDEFIynylnnnkgkIG---------IIYTSTRKDAESLYSKLENKG-HKV 256
Cdd:NF041063 345 avQLRpEPAYWVAKCDSE---------EERRERV----------LEalrhlprplILYVTKVEDAEAWLQRLRAAGfRRV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 257 GVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEKSECILLFSPR 336
Cdd:NF041063 406 ALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPD 485
|
....
gi 499412780 337 DIQI 340
Cdd:NF041063 486 DLDI 489
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
402-504 |
6.57e-38 |
|
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: 136.51 E-value: 6.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 402 REEKDITIEAQKIFSCVYRMKESFGVNMIADTLKGSRNKKVLNAGLNRLSTYGIMSEFTQKQISSLINKLIADGYLVTTD 481
Cdd:pfam09382 2 PETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDI 81
|
90 100
....*....|....*....|...
gi 499412780 482 DKFPVVKLQARANNVLKNKEPVY 504
Cdd:pfam09382 82 EFYSVLKLTPKAREVLKGEEKVM 104
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
406-497 |
1.19e-35 |
|
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: 129.52 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 406 DITIEAQKIFSCVYRMKESFGVNMIADTLKGSRNKKVLNAGLNRLSTYGIMSEFTQKQISSLINKLIADGYLVTTDDKFP 485
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 499412780 486 VVKLQARANNVL 497
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| HTH_40 |
pfam14493 |
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of ... |
611-699 |
1.52e-30 |
|
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of helicase proteins.
Pssm-ID: 464189 Cd Length: 89 Bit Score: 114.91 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 611 THVITYNLYKEGKNIKEISKERNLQTSTIEEHLFKCLNEDMDINIDDLIKKDYEKIILDAIKKIGGSKLKPIKDALPEEV 690
Cdd:pfam14493 1 SAEITLELYKEGLSIEEIAEERGLKESTIEGHLAELIEAGEPVDIERLVSEEEQKEILDAIEKLGSESLKPIKEALPEEI 80
|
....*....
gi 499412780 691 DYMSIKSVW 699
Cdd:pfam14493 81 SYFEIRLVL 89
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
243-324 |
3.52e-26 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 102.29 E-value: 3.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 243 ESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGR 322
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 499412780 323 DG 324
Cdd:smart00490 81 AG 82
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
22-170 |
7.33e-25 |
|
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: 101.55 E-value: 7.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 22 QEKVIESILNKKDTVAIMPTGAGKSICYQIPAL------LTEGITIVISPLISLMKDQVDSLKAM----GIKATFINSSL 91
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLgkglGLKVASLLGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 92 NNLEIQERIFNAnmgiyDLIYLAPERLESegFCNSLNNL-DISLIAVDEAHCVSQWGhdFRPSYTRISRFIEglEKRPIV 170
Cdd:pfam00270 84 SRKEQLEKLKGP-----DILVGTPGRLLD--LLQERKLLkNLKLLVLDEAHRLLDMG--FGPDLEEILRRLP--KKRQIL 152
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
215-324 |
9.96e-25 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 99.21 E-value: 9.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 215 NKDEFIYNYLNNNKGKIGIIYTSTRKDAESLYSkLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGID 294
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 499412780 295 KSNVRYVIHYNMPKNMEAYYQEAGRAGRDG 324
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
208-333 |
8.24e-24 |
|
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: 97.19 E-value: 8.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 208 FAVIRGENKDEFIYNYL--NNNKGKIgIIYTSTRKDAESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVA 285
Cdd:cd18787 5 YVVVEEEEKKLLLLLLLleKLKPGKA-IIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 499412780 286 TNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEKSECILLF 333
Cdd:cd18787 84 TDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
335-398 |
1.17e-22 |
|
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: 91.58 E-value: 1.17e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499412780 335 PRDIQIQKYFIDQGFLPPVRKNNEYNKLRAMVDYC-YTSKCLRAYILEYFDEETNLENCGNCSTC 398
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCeNTTDCRRKQLLRYFGEEFDSEPCGNCDNC 65
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
183-343 |
2.78e-22 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 99.84 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 183 EDILKLL--YLKEPeVFVTgVDRENLN-------FAVIRGENKDEFIYNYLNNNKGKIGIIYTSTRKDAESLYSKLENKG 253
Cdd:COG0513 188 PEIRKLAkrYLKNP-VRIE-VAPENATaetieqrYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRG 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 254 HKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEKSECILLF 333
Cdd:COG0513 266 ISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLV 345
|
170
....*....|....
gi 499412780 334 SPRDI----QIQKY 343
Cdd:COG0513 346 TPDERrllrAIEKL 359
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
11-162 |
3.08e-21 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 92.17 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 11 KYFGYDEFRGAQEKVIESIL-NKKDTVAIMPTGAGKSICYQIPALLT-----EGITIVISPLISLMKDQVDSLKAMGIKA 84
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLsGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499412780 85 TFINSSL-NNLEIQERIFNANMGIYDLIYLAPERLESEGFCNSLNNLDISLIAVDEAHCVSQWGhdFRPSYTRISRFIE 162
Cdd:smart00487 82 GLKVVGLyGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLLP 158
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
517-584 |
6.01e-21 |
|
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: 86.82 E-value: 6.01e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499412780 517 DNELLEILKDIRKEISQEAGIPPFMIFHDITLKELSEYMPKDMENFLKIKGVGEKKAEVYGEKFISAI 584
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
17-332 |
1.63e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 86.62 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 17 EFRGAQEKVIESIL-----NKKDTVAIMPTGAGKSI----CYQipALLTEGITIVISPLISLMKDQVDSLKAmgiKATFI 87
Cdd:COG1061 80 ELRPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRR---FLGDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 88 NSSLNNLEIQERIFNANmgiYDLIYLAPERlesegfcNSLNNlDISLIAVDEAHcvsqwgHDFRPSYTRI-----SRFIE 162
Cdd:COG1061 155 LAGGGKKDSDAPITVAT---YQSLARRAHL-------DELGD-RFGLVIIDEAH------HAGAPSYRRIleafpAAYRL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 163 GL-------EKRPIVTAFTATATQTVK-EDILKLLYLKEPEVFVTGVD-----------RENLNFAVIRG-ENKDEFIYN 222
Cdd:COG1061 218 GLtatpfrsDGREILLFLFDGIVYEYSlKEAIEDGYLAPPEYYGIRVDltderaeydalSERLREALAADaERKDKILRE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 223 YLNNN-KGKIGIIYTSTRKDAESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYV 301
Cdd:COG1061 298 LLREHpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVA 377
|
330 340 350
....*....|....*....|....*....|...
gi 499412780 302 IhYNMP-KNMEAYYQEAGRAGRDGE-KSECILL 332
Cdd:COG1061 378 I-LLRPtGSPREFIQRLGRGLRPAPgKEDALVY 409
|
|
| YpbB |
COG4955 |
Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown]; |
614-696 |
2.54e-17 |
|
Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown];
Pssm-ID: 443982 [Multi-domain] Cd Length: 346 Bit Score: 83.91 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 614 ITYNLYKEGKNIKEISKERNLQTSTIEEHLFKCLNEDMDINIDDLIKKDYEKIILDAIKKIGGSKLKPIKDALPeEVDYM 693
Cdd:COG4955 254 KTYQLLQQGLSLEEIAQIRRLKLSTIEDHLVEIAIKDPDFPIEPFVNKEDQQEIIQAIEKLGTWKLKEIKEQLP-DLSYF 332
|
...
gi 499412780 694 SIK 696
Cdd:COG4955 333 QIR 335
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
233-332 |
7.56e-16 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 74.99 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 233 IIYTSTRKDAESLYS-------KLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYN 305
Cdd:cd18797 39 IVFCRSRKLAELLLRylkarlvEEGPLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*..
gi 499412780 306 MPKNMEAYYQEAGRAGRDGEKSECILL 332
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
22-332 |
1.34e-15 |
|
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: 80.65 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 22 QEKVIESILNKKDTVAIMPTGAGKSICYQIPALltEGI-------TIVISPLISLMKDQVDSLKAMgikatfinsslnnl 94
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVL--EALledpgatALYLYPTKALARDQLRRLREL-------------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 95 eIQERIFNANMGIYD-----------------LI---------YLAPERLESEGFCNslnnldISLIAVDEAHcvsqwgh 148
Cdd:COG1205 125 -AEALGLGVRVATYDgdtppeerrwirehpdiVLtnpdmlhygLLPHHTRWARFFRN------LRYVVIDEAH------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 149 dfrpSYT------------RISRFIEGLEKRPIVtaftatatqtvkedILKLLYLKEPEVF---VTGVDrenlnFAVI-- 211
Cdd:COG1205 191 ----TYRgvfgshvanvlrRLRRICRHYGSDPQF--------------ILASATIGNPAEHaerLTGRP-----VTVVde 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 212 ----RGEnKDEFIYNYLNNNKGKI--------------------GIIYTSTRKDAESLYSKLENK------GHKVGVYHA 261
Cdd:COG1205 248 dgspRGE-RTFVLWNPPLVDDGIRrsalaeaarlladlvreglrTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRA 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499412780 262 GLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVI--HYnmPKNMEAYYQEAGRAGRDGEKSECILL 332
Cdd:COG1205 327 GYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVlaGY--PGTRASFWQQAGRAGRRGQDSLVVLV 397
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
517-594 |
3.80e-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: 68.09 E-value: 3.80e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499412780 517 DNELLEILKDIRKEISQEAGIPPFMIFHDITLKELSEYMPKDMENFLKIKGVGEKKAEVYGEKFISAICDYTKEKNIT 594
Cdd:smart00341 4 QLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDSPSEA 81
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
33-167 |
2.95e-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: 67.43 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 33 KDTVAIMPTGAGKSICYQIPALL----TEGITIVISPLISLMKDQVDSLKA---MGIKATFINSSlNNLEIQERIFNANm 105
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLlllkKGKKVLVLVPTKALALQTAERLRElfgPGIRVAVLVGG-SSAEEREKNKLGD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499412780 106 giYDLIYLAPERLEsegfcNSLNNL------DISLIAVDEAHCVSQWGHDFRPSYTRISRFIEGLEKR 167
Cdd:cd00046 80 --ADIIIATPDMLL-----NLLLREdrlflkDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV 140
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
181-347 |
1.81e-12 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 69.86 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 181 VKEDILKLLYLKEpevFVTGVDRENLNFAVIrgenKDefIYNYLNNNKGkigIIYTSTRKDAESLYSKLENKGHKVGVYH 260
Cdd:PTZ00424 231 VKKDELTLEGIRQ---FYVAVEKEEWKFDTL----CD--LYETLTITQA---IIYCNTRRKVDYLTKKMHERDFTVSCMH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 261 AGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEKSECILLFSPRDIQ- 339
Cdd:PTZ00424 299 GDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEq 378
|
170
....*....|.
gi 499412780 340 ---IQKYFIDQ 347
Cdd:PTZ00424 379 lkeIERHYNTQ 389
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
195-332 |
1.28e-11 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 62.96 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 195 EVFVTGVDRENLNFAVIRGENKDEFIY-NYLNNNKGKIGIIYTSTRKDAESLYSKLenKGhkVGVYHAGLGDEQRKKIQE 273
Cdd:cd18795 8 YVLGFNGLGIKLRVDVMNKFDSDIIVLlKIETVSEGKPVLVFCSSRKECEKTAKDL--AG--IAFHHAGLTREDRELVEE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499412780 274 DFSFDNINIIVATNAFGMGID--------KSNVRYVIHYNMPKNMEAYYQEAGRAGRDG--EKSECILL 332
Cdd:cd18795 84 LFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKGYRELSPLEYLQMIGRAGRPGfdTRGEAIIM 152
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
22-355 |
1.41e-11 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 67.24 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 22 QEKVIESILNKKDTVAIMPTGAGKSICYQIPAL-------------LTEGITIVISP----LISLMKDQVDSLKAMGIKA 84
Cdd:PRK01297 114 QAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIInqllqtpppkeryMGEPRALIIAPtrelVVQIAKDAAALTKYTGLNV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 85 -TFINSSlnNLEIQERIFNANMgiYDLIYLAPERL---ESEGFCNslnnLD-ISLIAVDEAHCVSQWGhdFRPSYTRISR 159
Cdd:PRK01297 194 mTFVGGM--DFDKQLKQLEARF--CDILVATPGRLldfNQRGEVH----LDmVEVMVLDEADRMLDMG--FIPQVRQIIR 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 160 FIEGLEKRPIVTAFTAtatqtVKEDILKLL--YLKEPEVF------VTGVDRENLNFAVIrGENKDEFIYNYLNNNKGKI 231
Cdd:PRK01297 264 QTPRKEERQTLLFSAT-----FTDDVMNLAkqWTTDPAIVeiepenVASDTVEQHVYAVA-GSDKYKLLYNLVTQNPWER 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 232 GIIYTSTRKDAESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNME 311
Cdd:PRK01297 338 VMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPD 417
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 499412780 312 AYYQEAGRAGRDGEKSECIlLFSPRDiqiqkyfiDQGFLPPVRK 355
Cdd:PRK01297 418 DYVHRIGRTGRAGASGVSI-SFAGED--------DAFQLPEIEE 452
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
233-332 |
3.67e-11 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 59.25 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 233 IIYTSTRKDAESLYSKLEnkghkvgvyhaglgdeqrkkiqedfsfdninIIVATNAFGMGIDKSNVRYVIHYNMPKNMEA 312
Cdd:cd18785 7 IVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSAAS 55
|
90 100
....*....|....*....|.
gi 499412780 313 YYQEAGRAGRDG-EKSECILL 332
Cdd:cd18785 56 YIQRVGRAGRGGkDEGEVILF 76
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
233-330 |
1.05e-10 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 64.22 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 233 IIYTSTRKDAESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEA 312
Cdd:PRK04837 259 IIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCED 338
|
90
....*....|....*...
gi 499412780 313 YYQEAGRAGRDGEKSECI 330
Cdd:PRK04837 339 YVHRIGRTGRAGASGHSI 356
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
185-330 |
1.33e-10 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 64.59 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 185 ILKLLY--LKEPEVFVtgVDRENLNFAVIR-------GENKDEFIYNYLNNNKGKIGIIYTSTRKDAESLYSKLENKGHK 255
Cdd:PRK04537 206 VLELAYehMNEPEKLV--VETETITAARVRqriyfpaDEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYR 283
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499412780 256 VGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEKSECI 330
Cdd:PRK04537 284 VGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAI 358
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
233-327 |
1.49e-10 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 59.97 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 233 IIYTSTRKDAESLYSKLENK------GHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNM 306
Cdd:cd18796 42 LVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90 100
....*....|....*....|..
gi 499412780 307 PKNMEAYYQEAGRAG-RDGEKS 327
Cdd:cd18796 122 PKSVARLLQRLGRSGhRPGAAS 143
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
2-322 |
8.56e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 61.83 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 2 LQKAKEALSKyFGYDEFRGAQEKVIES-ILNKKDTVAIMPTGAGKSICYQIPAL--LTEGITIV-ISPLISLMKDQVDSL 77
Cdd:COG1204 8 LEKVIEFLKE-RGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLRALASEKYREF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 78 KA----MGIKATfINSSlnNLEIQERIFnanmGIYDLIYLAPERLES-----EGFCNslnnlDISLIAVDEAH------- 141
Cdd:COG1204 87 KRdfeeLGIKVG-VSTG--DYDSDDEWL----GRYDILVATPEKLDSllrngPSWLR-----DVDLVVVDEAHliddesr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 142 --------------C-----------------VSQW------GHDFRPS-------YTRISRFIEGLEKRpivtaftata 177
Cdd:COG1204 155 gptlevllarlrrlNpeaqivalsatignaeeIAEWldaelvKSDWRPVplnegvlYDGVLRFDDGSRRS---------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 178 tqtvKEDILKLLY--LKEPE---VFVTGVDR-ENL--NFAVIRGENKDEFIYNYLNNNKGKIgiIYTSTRKDAESLYSKL 249
Cdd:COG1204 225 ----KDPTLALALdlLEEGGqvlVFVSSRRDaESLakKLADELKRRLTPEEREELEELAEEL--LEVSEETHTNEKLADC 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 250 ENKGhkVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIdksN--VRYVI----HYNMPKNMEA--YYQEAGRAG 321
Cdd:COG1204 299 LEKG--VAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV---NlpARRVIirdtKRGGMVPIPVleFKQMAGRAG 373
|
.
gi 499412780 322 R 322
Cdd:COG1204 374 R 374
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
226-335 |
4.47e-09 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 59.40 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 226 NNKGKIgIIYTSTRKDAESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYN 305
Cdd:PTZ00110 375 RDGDKI-LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFD 453
|
90 100 110
....*....|....*....|....*....|
gi 499412780 306 MPKNMEAYYQEAGRAGRDGEKSECILLFSP 335
Cdd:PTZ00110 454 FPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
214-340 |
5.26e-07 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 52.64 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 214 ENKDEFIYNYLNNNKGKIGIIYTSTRKDAESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGI 293
Cdd:PRK11192 230 EHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGI 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499412780 294 DKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEKSECILLFSPRDIQI 340
Cdd:PRK11192 310 DIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLL 356
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
218-332 |
1.23e-06 |
|
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: 48.36 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 218 EFIYNYLNNNKGKIGIIYTSTRKDAESLYSKLENK-------------GHKVGVYHAGLGDEQRKKIQ--EDFSFDNINI 282
Cdd:cd18802 14 EILREYFPKTPDFRGIIFVERRATAVVLSRLLKEHpstlafircgfliGRGNSSQRKRSLMTQRKQKEtlDKFRDGELNL 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 499412780 283 IVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGekSECILL 332
Cdd:cd18802 94 LIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYILM 141
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
232-331 |
1.54e-06 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 51.33 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 232 GIIYTSTRKDAESLYSKLE-NKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNM 310
Cdd:PLN00206 370 AVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTI 449
|
90 100
....*....|....*....|.
gi 499412780 311 EAYYQEAGRAGRDGEKSECIL 331
Cdd:PLN00206 450 KEYIHQIGRASRMGEKGTAIV 470
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
22-141 |
7.77e-06 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 46.81 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 22 QEKVIESILNKKDTVAIMPTGAGKSICYQIP---ALLTE-GIT-IVISPLISLMKDQVDSLKA----MGIKATF------ 86
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDpGSRaLYLYPTKALAQDQLRSLRElleqLGLGIRVatydgd 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 499412780 87 --INSSLNNLEIQERIFNANmgiYDLIYLA--PERLESEGFCNSLNnldisLIAVDEAH 141
Cdd:cd17923 85 tpREERRAIIRNPPRILLTN---PDMLHYAllPHHDRWARFLRNLR-----YVVLDEAH 135
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
22-145 |
1.07e-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: 46.49 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 22 QEKVIESILNKKDTVAI-MPTGAGKSICYQ---IPALLTEGITIV-ISPLISLMKDQVDSLKAMgikatFINSSLNNLEI 96
Cdd:cd17921 6 QREALRALYLSGDSVLVsAPTSSGKTLIAElaiLRALATSGGKAVyIAPTRALVNQKEADLRER-----FGPLGKNVGLL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 499412780 97 --QERIFNANMGIYDLIYLAPERLEsegfcNSLNNL------DISLIAVDEAHCVSQ 145
Cdd:cd17921 81 tgDPSVNKLLLAEADILVATPEKLD-----LLLRNGgerliqDVRLVVVDEAHLIGD 132
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
211-337 |
2.88e-05 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 47.54 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 211 IRGENKDEFIYNYLNNNKGKIGIIYTSTRKDAESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFG 290
Cdd:PRK11634 227 VWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAA 306
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499412780 291 MGIDKSNVRYVIHYNMPKNMEAYYQEAGRAGRDGEKSECILLFSPRD 337
Cdd:PRK11634 307 RGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRE 353
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
233-322 |
3.82e-05 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 47.19 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 233 IIYTSTRKDAESLYSKLenkGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFG----------------MGIDKS 296
Cdd:COG1202 431 IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAagvdfpasqvifdslaMGIEWL 507
|
90 100
....*....|....*....|....*.
gi 499412780 297 NVRyvihynmpknmeAYYQEAGRAGR 322
Cdd:COG1202 508 SVQ------------EFHQMLGRAGR 521
|
|
| RQC_minor_1 |
NF041107 |
RQC-minor-1 family DNA-binding protein; The DNA-binding RQC domain (PF09382) appears primarily ... |
426-477 |
5.52e-05 |
|
RQC-minor-1 family DNA-binding protein; The DNA-binding RQC domain (PF09382) appears primarily in RecQ, a DNA helicase involved in recombination, replication, and repair. However, it appears also in this uncharacterized protein family, to which we give the name "RQC-minor-1 family DNA-binding protein." A majority of members contain an additional C-terminal predicted zinc-ribbon domain. Members appear not to show any conserved gene neighborhood.
Pssm-ID: 469031 [Multi-domain] Cd Length: 173 Bit Score: 44.10 E-value: 5.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 499412780 426 GVNMIADTLKGSRNKKVLNAGLNRLSTYGIMSEFTQKQISSLINKLIADGYL 477
Cdd:NF041107 22 GRTMLAKILKGSKDKKVLELGLDQCPAYGYYKSLTLEEITAKIDWMIKHDYL 73
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
17-157 |
6.03e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 43.81 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 17 EFRGAQEKVIESILN-----KKDTVAIMPTGAGKSICY-QIPALLTE----GITIVISPLISLMKDQVDSLKAMGIKATF 86
Cdd:pfam04851 3 ELRPYQIEAIENLLEsikngQKRGLIVMATGSGKTLTAaKLIARLFKkgpiKKVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499412780 87 INSSLNNLEIQERIFNANM------GIYDLIYLAPERLESEGFcnslnnldiSLIAVDEAHcvsqwgHDFRPSYTRI 157
Cdd:pfam04851 83 IGEIISGDKKDESVDDNKIvvttiqSLYKALELASLELLPDFF---------DVIIIDEAH------RSGASSYRNI 144
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
521-586 |
7.65e-05 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 45.63 E-value: 7.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499412780 521 LEILKDI---RKEISQEAGIPPFMIFHDITLKELSEYMPKDMENFLKIKGVGEKKAEVYGEKFISAICD 586
Cdd:COG0349 210 LAVLRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAE 278
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
238-324 |
8.09e-05 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350192 [Multi-domain] Cd Length: 135 Bit Score: 42.93 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 238 TRKDAESLYSKLE-NKGHKVGVYHAGLGDEQRKKIQEDFSFDNI--NIIVATNAFGMGIDkSNVRYVIHYNMPK---NME 311
Cdd:cd18805 26 SRKDIFSLKREIEkRTGLKCAVIYGALPPETRRQQARLFNDPESgyDVLVASDAIGMGLN-LNIRRVIFSSLSKfdgNEM 104
|
90
....*....|....*....
gi 499412780 312 ------AYYQEAGRAGRDG 324
Cdd:cd18805 105 rplspsEVKQIAGRAGRFG 123
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
233-332 |
1.12e-04 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 45.18 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 233 IIYTSTRKDAESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEA 312
Cdd:PRK10590 249 LVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPED 328
|
90 100
....*....|....*....|
gi 499412780 313 YYQEAGRAGRDGEKSECILL 332
Cdd:PRK10590 329 YVHRIGRTGRAAATGEALSL 348
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
22-324 |
1.35e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 45.26 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 22 QEKVIESILNKKDTVAIMPTGAGKSIC--YQIPALLTEGI-TIVISPLISLMKD---QVDSLKAMGIKATFinsSLNNLE 95
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIaySAIYETFLAGLkSIYIVPLRSLAMEkyeELSRLRSLGMRVKI---SIGDYD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 96 IQERIFNAnmgiYDLIYLAPERLESEGFCNSLNNLDISLIAVDEAHCVsqwGHDFR----PSYTRISRFIEGlEKRPIVT 171
Cdd:PRK01172 104 DPPDFIKR----YDVVILTSEKADSLIHHDPYIINDVGLIVADEIHII---GDEDRgptlETVLSSARYVNP-DARILAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 172 AFTATATQTVKEDI-------------LKLLYLKEPEVFVTGVDRENLNFAVIRGENKDEfiynylnnnkGKIGIIYTST 238
Cdd:PRK01172 176 SATVSNANELAQWLnasliksnfrpvpLKLGILYRKRLILDGYERSQVDINSLIKETVND----------GGQVLVFVSS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 239 RKDAESL---------------YSKLENKG----------HKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGI 293
Cdd:PRK01172 246 RKNAEDYaemliqhfpefndfkVSSENNNVyddslnemlpHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGV 325
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 499412780 294 D--------KSNVRYVIHYNMP-KNMEAyYQEAGRAGRDG 324
Cdd:PRK01172 326 NlparlvivRDITRYGNGGIRYlSNMEI-KQMIGRAGRPG 364
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
22-141 |
2.38e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 41.91 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 22 QEKVIESILNKKDT---VAIMPTGAGKSIC-YQIPALLTEGITIVISPLISLMKDQVDslkamGIKATFINSSLNNLEIQ 97
Cdd:cd17926 5 QEEALEAWLAHKNNrrgILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKE-----RFEDFLGDSSIGLIGGG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 499412780 98 ERIFNANMGI----YDLIYLAPERLEsegfcnSLNNLDiSLIAVDEAH 141
Cdd:cd17926 80 KKKDFDDANVvvatYQSLSNLAEEEK------DLFDQF-GLLIVDEAH 120
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
240-335 |
3.01e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 41.95 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 240 KDAESLYSKLENK---GHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPK-NMEAYYQ 315
Cdd:cd18811 45 KAAVAMYEYLKERfrpELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERfGLSQLHQ 124
|
90 100
....*....|....*....|
gi 499412780 316 EAGRAGRDGEKSECILLFSP 335
Cdd:cd18811 125 LRGRVGRGDHQSYCLLVYKD 144
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
240-336 |
6.43e-04 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 41.10 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 240 KDAESLYSKLENK--GHKVGVYHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPK-NMEAYYQE 316
Cdd:cd18792 45 KSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRfGLSQLHQL 124
|
90 100
....*....|....*....|
gi 499412780 317 AGRAGRDGEKSECILLFSPR 336
Cdd:cd18792 125 RGRVGRGKHQSYCYLLYPDP 144
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
233-330 |
8.48e-04 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 40.15 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499412780 233 IIYTSTRKDAESLYSKLENKGHKVGVYHAGLGDEQRKKIQEDFSFD-NINI-IVATNAFGMGIDKSNVRYVIHYNMPKN- 309
Cdd:cd18793 31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKAGGVGLNLTAANRVILYDPWWNp 110
|
90 100
....*....|....*....|..
gi 499412780 310 -MEAyyQEAGRAGRDGEKSECI 330
Cdd:cd18793 111 aVEE--QAIDRAHRIGQKKPVV 130
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
22-54 |
1.72e-03 |
|
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: 40.12 E-value: 1.72e-03
10 20 30
....*....|....*....|....*....|...
gi 499412780 22 QEKVIESILNKKDTVAIMPTGAGKSICYQIPAL 54
Cdd:cd00268 17 QAQAIPLILSGRDVIGQAQTGSGKTLAFLLPIL 49
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
259-321 |
2.35e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 41.45 E-value: 2.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499412780 259 YHAGLGDEQRKKIQEDFSFDNINIIVATNAFGMGIDKSNVRYVIHYNMPKNMEAYYQEAGRAG 321
Cdd:PRK09751 307 HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
5-64 |
9.31e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 39.14 E-value: 9.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499412780 5 AKEALSKYFGYDEFRGAQ----EKVIESILNKKDTVAIMPTGAGKSICYQIPALL---TEGITIVIS 64
Cdd:COG1199 2 DDGLLALAFPGFEPRPGQremaEAVARALAEGRHLLIEAGTGTGKTLAYLVPALLaarETGKKVVIS 68
|
|
| |
