|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
2-431 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 557.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 2 LINELKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLTDGMVLIVSPLLSLMEDQVTQLQKRGEkR 81
Cdd:COG0514 5 ALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGI-R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 82 VAAFNSLLSRAERGYVLRHLS--QYKFLFLSPEMLTNPSLLEQLKKQDIALYVVDEAHCVSQWGVDFRPEYQQLGKIREH 159
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRagELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 160 LGNPVTLALTATATDLVAKDIRQVLFDRQPKEVRQSVNRQNISLFVRKT--QQKEQELEQFMES-AHGAAIIYCATKKEV 236
Cdd:COG0514 164 LPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEhPGGSGIVYCLSRKKV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 237 ERLYHLFRER-FSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGR 315
Cdd:COG0514 244 EELAEWLREAgIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 316 DQEESAAILLYQSGDERIHYFFnqlsreqrqsfelyleyaaeqapfdelqkkwmelIQQSEKPenwvERLKRQEKEKefr 395
Cdd:COG0514 324 DGLPAEALLLYGPEDVAIQRFF----------------------------------IEQSPPD----EERKRVERAK--- 362
|
410 420 430
....*....|....*....|....*....|....*.
gi 488244010 396 LQQMLRYIHEEDCRRKFILAYFGEELSEkPQNCCDI 431
Cdd:COG0514 363 LDAMLAYAETTGCRRQFLLRYFGEELAE-PCGNCDN 397
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
6-428 |
3.81e-130 |
|
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: 389.05 E-value: 3.81e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 6 LKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLTDGMVLIVSPLLSLMEDQVTQLQKRGeKRVAAF 85
Cdd:TIGR01389 5 LKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAG-VAAAYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 86 NSLLSRAERGYVLRHLS--QYKFLFLSPEMLTNPSLLEQLKKQDIALYVVDEAHCVSQWGVDFRPEYQQLGKIREHLGNP 163
Cdd:TIGR01389 84 NSTLSAKEQQDIEKALVngELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFPQV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 164 VTLALTATATDLVAKDIRQVLFDRQPKEVRQSVNRQNISLFVRKTQQKEQELEQFMESAHG-AAIIYCATKKEVERLYHL 242
Cdd:TIGR01389 164 PRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGqSGIIYASSRKKVEELAER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 243 FRER-FSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESA 321
Cdd:TIGR01389 244 LESQgISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 322 AILLYQSGDERIHYFFnqlsreqrqsfelyleyaaeqapfdelqkkwmelIQQSEKPENwverLKRQEKEKefrLQQMLR 401
Cdd:TIGR01389 324 AILLYSPADIALLKRR----------------------------------IEQSEADDD----YKQIEREK---LRAMIA 362
|
410 420
....*....|....*....|....*..
gi 488244010 402 YIHEEDCRRKFILAYFGEELSEKPQNC 428
Cdd:TIGR01389 363 YCETQTCRRAYILRYFGENEVEPCGNC 389
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
6-447 |
1.96e-116 |
|
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: 349.84 E-value: 1.96e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 6 LKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLTDGMVLIVSPLLSLMEDQVTQLQKRGekrVAA- 84
Cdd:TIGR00614 3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALG---IPAt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 85 -FNSLLSRAERGYVLRHL--SQYKFLFLSPEML-TNPSLLEQLKKQ-DIALYVVDEAHCVSQWGVDFRPEYQQLGKIREH 159
Cdd:TIGR00614 80 fLNSAQTKEQQLNVLTDLkdGKIKLLYVTPEKIsASNRLLQTLEERkGITLIAVDEAHCISQWGHDFRPDYKALGSLKQK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 160 LGNPVTLALTATATDLVAKDIRQVLFDRQPKEVRQSVNRQNISLFV-RKTQQKEQELEQFMESAH--GAAIIYCATKKEV 236
Cdd:TIGR00614 160 FPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVrRKTPKILEDLLRFIRKEFegKSGIIYCPSRKKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 237 ERLY-HLFRERFSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGR 315
Cdd:TIGR00614 240 EQVAaELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 316 DQEESAAILLYQSGDerihyfFNQLSReqrqsfeLYLEyaaeqapfdelqkkwmeliqqsekpenwvERLKRQEKEKEFR 395
Cdd:TIGR00614 320 DGLPSECHLFYAPAD------MNRLRR-------LLME-----------------------------EPDGNFRTYKLKL 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488244010 396 LQQMLRYIHEEDCRRKFILAYFGEELSEK------PQNCCD-----IDGAKVELLPKKKDFSK 447
Cdd:TIGR00614 358 YEMMEYCLNSSTCRRLILLSYFGEKGFNKsfcimgTEKCCDncckrLDYKTKDVTDKVYDFGP 420
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
6-431 |
1.36e-103 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 321.28 E-value: 1.36e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 6 LKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLTDGMVLIVSPLLSLMEDQVTQLQKRGekrVAA- 84
Cdd:PRK11057 17 LQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANG---VAAa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 85 -FNSLLSRAERGYVLR--HLSQYKFLFLSPEMLTNPSLLEQLKKQDIALYVVDEAHCVSQWGVDFRPEYQQLGKIREHLG 161
Cdd:PRK11057 94 cLNSTQTREQQLEVMAgcRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRFP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 162 NPVTLALTATATDLVAKDIRQVLFDRQPKEVRQSVNRQNIS-LFVRKTQQKEQeLEQFMESAHG-AAIIYCATKKEVERL 239
Cdd:PRK11057 174 TLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRyTLVEKFKPLDQ-LMRYVQEQRGkSGIIYCNSRAKVEDT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 240 YHLFRER-FSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQE 318
Cdd:PRK11057 253 AARLQSRgISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 319 ESAAILLYQSGDerihyffnqlsreqrqsfELYLEYAAEQAPFDELQKkwmeliqqsekpenwVERLKrqekekefrLQQ 398
Cdd:PRK11057 333 PAEAMLFYDPAD------------------MAWLRRCLEEKPAGQQQD---------------IERHK---------LNA 370
|
410 420 430
....*....|....*....|....*....|...
gi 488244010 399 MLRYIHEEDCRRKFILAYFGEElSEKPQNCCDI 431
Cdd:PRK11057 371 MGAFAEAQTCRRLVLLNYFGEG-RQEPCGNCDI 402
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
5-197 |
2.86e-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: 275.57 E-value: 2.86e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 5 ELKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLTDGMVLIVSPLLSLMEDQVTQLQKRGeKRVAA 84
Cdd:cd17920 3 ILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLG-IRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 85 FNSLLSRAERGYVLR--HLSQYKFLFLSPEMLTNPSLLEQLKKQD----IALYVVDEAHCVSQWGVDFRPEYQQLGKIRE 158
Cdd:cd17920 82 LNSTLSPEEKREVLLriKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLRR 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 488244010 159 HLGNPVTLALTATATDLVAKDIRQVLFDRQPKEVRQSVN 197
Cdd:cd17920 162 ALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
7-430 |
1.56e-80 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 271.00 E-value: 1.56e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 7 KKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLTDGMVLIVSPLLSLMEDQVTQLQKrGEKRVAAFN 86
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQ-ANIPAASLS 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 87 SLLSRAERGYVLRHLS----QYKFLFLSPEMLT-NPSLLEQLK----KQDIALYVVDEAHCVSQWGVDFRPEYQQLGKIR 157
Cdd:PLN03137 532 AGMEWAEQLEILQELSseysKYKLLYVTPEKVAkSDSLLRHLEnlnsRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILK 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 158 EHLGNPVTLALTATATDLVAKDIRQVLFDRQPKEVRQSVNRQNISL-FVRKTQQKEQELEQFMESAH--GAAIIYCATKK 234
Cdd:PLN03137 612 QKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYsVVPKTKKCLEDIDKFIKENHfdECGIIYCLSRM 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 235 EVERLYHLFRE-RFSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRA 313
Cdd:PLN03137 692 DCEKVAERLQEfGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRA 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 314 GRDQEESAAILLYQSGDE-RIHYFFNQLSREQRQSFELYLEYAAEqapfdelqkkwmeliqqsekpenwvERLKRQEKEK 392
Cdd:PLN03137 772 GRDGQRSSCVLYYSYSDYiRVKHMISQGGVEQSPMAMGYNRMASS-------------------------GRILETNTEN 826
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 488244010 393 EFRlqqMLRYIHEE-DCRRKFILAYFGEEL-SEKPQNCCD 430
Cdd:PLN03137 827 LLR---MVSYCENEvDCRRFLQLVHFGEKFdSTNCKKTCD 863
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
6-187 |
3.02e-69 |
|
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: 219.05 E-value: 3.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 6 LKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYL----TDGMVLIVSPLLSLMEDQVTQLQKRgeKR 81
Cdd:cd18018 4 LRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA--IK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 82 VAAFNSLLSRAERGYVLRHL--SQYKFLFLSPEMLTNPSLLEQLK-KQDIALYVVDEAHCVSQWGVDFRPEYQQLGK-IR 157
Cdd:cd18018 82 AAALNSSLTREERRRILEKLraGEVKILYVSPERLVNESFRELLRqTPPISLLVVDEAHCISEWSHNFRPDYLRLCRvLR 161
|
170 180 190
....*....|....*....|....*....|
gi 488244010 158 EHLGNPVTLALTATATDLVAKDIRQVLFDR 187
Cdd:cd18018 162 ELLGAPPVLALTATATKRVVEDIASHLGIP 191
|
|
| DpdF |
NF041063 |
protein DpdF; |
6-353 |
1.22e-64 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 222.86 E-value: 1.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 6 LKKYFGFDSFR-PGQEEIIQALL---DGEDTLAILPTGTGKSLCYQ---LTGYLTDGMVLIVSPLLSLMEDQVTQLQKRG 78
Cdd:NF041063 131 LAEALGFTHYRsPGQREAVRAALlapPGSTLIVNLPTGSGKSLVAQapaLLASRQGGLTLVVVPTVALAIDQERRARELL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 79 EKRVA------AFNSLLSRAERGYVLRHL---SQyKFLFLSPEMLT---NPSLLEQLKKQDIALYVVDEAHCVSQWGVDF 146
Cdd:NF041063 211 RRAGPdlggplAWHGGLSAEERAAIRQRIrdgTQ-RILFTSPESLTgslRPALFDAAEAGLLRYLVVDEAHLVDQWGDGF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 147 RPEYQQLGKIREHL-------GNPVTLALTATATDLVAKDIRqVLFDrQPKEVrQSVN----RQNISLFVRKTQQKEQEL 215
Cdd:NF041063 290 RPEFQLLAGLRRSLlrlapsgRPFRTLLLSATLTESTLDTLE-TLFG-PPGPF-IVVSavqlRPEPAYWVAKCDSEEERR 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 216 EQFMESAHGA---AIIYCATKKEVERLYHLFRER-FS-VGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSD 290
Cdd:NF041063 367 ERVLEALRHLprpLILYVTKVEDAEAWLQRLRAAgFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSD 446
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488244010 291 IRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILLYQSGDERIHyffNQLSREQRQSFELYLE 353
Cdd:NF041063 447 VRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIA---KSLNRPKLISVEKGLE 506
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
3-189 |
5.96e-55 |
|
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: 181.90 E-value: 5.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 3 INELKKYFGFDSFRPGQEEIIQALL-DGEDTLAILPTGTGKSLCYQLTGYLTDGMVLIVSPLLSLMEDQVTQLQKRGekr 81
Cdd:cd18017 1 LNALNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 82 VAAfnSLLSRAERGYVLR--HLSQYKFLFLSPEM-LTNPSLLEQLKKQdIALYVVDEAHCVSQWGVDFRPEYQQLGKIRE 158
Cdd:cd18017 78 IPA--CFLGSAQSQNVLDdiKMGKIRVIYVTPEFvSKGLELLQQLRNG-ITLIAIDEAHCVSQWGHDFRSSYRHLGSIRN 154
|
170 180 190
....*....|....*....|....*....|.
gi 488244010 159 HLGNPVTLALTATATDLVAKDIRQVLFDRQP 189
Cdd:cd18017 155 RLPNVPIVALTATATPSVRDDIIKNLNLRNP 185
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
6-197 |
8.42e-51 |
|
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: 171.39 E-value: 8.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 6 LKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLTDGMVLIVSPLLSLMEDQVTQLQKRGEKRVaAF 85
Cdd:cd18015 10 LKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISAT-ML 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 86 NSLLSRAERGYVLRHL----SQYKFLFLSPE-MLTNPSLLEQLKKQD----IALYVVDEAHCVSQWGVDFRPEYQQLGKI 156
Cdd:cd18015 89 NASSSKEHVKWVHAALtdknSELKLLYVTPEkIAKSKRFMSKLEKAYnagrLARIAIDEVHCCSQWGHDFRPDYKKLGIL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488244010 157 REHLGNPVTLALTATATDLVAKDIRQVLFDRQPKEVRQSVN 197
Cdd:cd18015 169 KRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
4-189 |
1.83e-48 |
|
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: 165.34 E-value: 1.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 4 NELKKYFGFDSFR-PGQEEIIQALLDGE-DTLAILPTGTGKSLCYQLTGYLTDGMVLIVSPLLSLMEDQVTQLQKRgEKR 81
Cdd:cd18014 2 STLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTL-KIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 82 VAAFNSLLSRAERGYVL----RHLSQYKFLFLSPEMLTNPS---LLEQLKKQDIALY-VVDEAHCVSQWGVDFRPEYQQL 153
Cdd:cd18014 81 VDSLNSKLSAQERKRIIadleSEKPQTKFLYITPEMAATSSfqpLLSSLVSRNLLSYlVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 488244010 154 GKIREHLGNPVTLALTATATDLVAKDIRQVLFDRQP 189
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
198-326 |
1.97e-48 |
|
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: 162.38 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 198 RQNISLFVRKTQQKEQELEQFMESA----HGAAIIYCATKKEVERLYHLFRER-FSVGYYHGGLDTAQRRQLQQQFVKNQ 272
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKvehlGGSGIIYCLSRKECEQVAARLQSKgISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 488244010 273 LQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILLY 326
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
2-197 |
1.25e-46 |
|
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: 160.38 E-value: 1.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 2 LINELKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLTDGMVLIVSPLLSLMEDQVtqlQKRGEKR 81
Cdd:cd18016 5 MMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQV---QKLTSLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 82 VAA--FNSLLSRAERGYVLRHLSQ----YKFLFLSPEMLTNP----SLLEQL-KKQDIALYVVDEAHCVSQWGVDFRPEY 150
Cdd:cd18016 82 IPAtyLTGDKTDAEATKIYLQLSKkdpiIKLLYVTPEKISASnrliSTLENLyERKLLARFVIDEAHCVSQWGHDFRPDY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488244010 151 QQLGKIREHLGNPVTLALTATATDLVAKDIRQVLFDRQPKEVRQSVN 197
Cdd:cd18016 162 KRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
16-174 |
4.53e-29 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 111.95 E-value: 4.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 16 RPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGY------LTDGMVLIVSPLLSLMEDQVTQLQKRGEKRVAAFNSLL 89
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 90 SRAERGYVLRHLSQYKFLFLSPEMLTnpSLLEQLKK-QDIALYVVDEAHCVSQWGvdFRPeyqQLGKIREHLGNPV-TLA 167
Cdd:pfam00270 81 GGDSRKEQLEKLKGPDILVGTPGRLL--DLLQERKLlKNLKLLVLDEAHRLLDMG--FGP---DLEEILRRLPKKRqILL 153
|
....*..
gi 488244010 168 LTATATD 174
Cdd:pfam00270 154 LSATLPR 160
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
210-315 |
2.42e-28 |
|
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: 108.07 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 210 QKEQELEQFMESAHGA-AIIYCATKKEVERLYHLFRERFSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDK 288
Cdd:pfam00271 1 EKLEALLELLKKERGGkVLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*..
gi 488244010 289 SDIRYVIHYDLPDSLENYVQEIGRAGR 315
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
237-316 |
4.01e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 98.44 E-value: 4.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 237 ERLYHLFRER-FSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGR 315
Cdd:smart00490 1 EELAELLKELgIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
.
gi 488244010 316 D 316
Cdd:smart00490 81 A 81
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
192-315 |
4.17e-25 |
|
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: 99.89 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 192 VRQSVnrqnisLFVRKTQQKEQELEQFMESAH-GAAIIYCATKKEVERLYHLFRER-FSVGYYHGGLDTAQRRQLQQQFV 269
Cdd:cd18787 1 IKQLY------VVVEEEEKKLLLLLLLLEKLKpGKAIIFVNTKKRVDRLAELLEELgIKVAALHGDLSQEERERALKKFR 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488244010 270 KNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGR 315
Cdd:cd18787 75 SGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
11-349 |
1.89e-24 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 104.84 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 11 GFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCY-----QLTGYLTDGMV--LIVSPL--LSLmedQVTQ-LQKRGEK 80
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFllpllQRLDPSRPRAPqaLILAPTreLAL---QVAEeLRKLAKY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 81 ---RVAA------FNSLLSRAERGY---------VLRHLSQYKFLFLSPEMLtnpslleqlkkqdialyVVDEAhcvsqw 142
Cdd:COG0513 98 lglRVATvyggvsIGRQIRALKRGVdivvatpgrLLDLIERGALDLSGVETL-----------------VLDEA------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 143 gvD------FRPEyqqLGKIREHLgnPV---TLALTATATDLVAKDIRQVLfdRQPKEV---RQSVNRQNIS---LFVRK 207
Cdd:COG0513 155 --DrmldmgFIED---IERILKLL--PKerqTLLFSATMPPEIRKLAKRYL--KNPVRIevaPENATAETIEqryYLVDK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 208 tQQKEQELEQFMESAH-GAAIIYCATKKEVERLYHLFRER-FSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMG 285
Cdd:COG0513 226 -RDKLELLRRLLRDEDpERAIVFCNTKRGADRLAEKLQKRgISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARG 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488244010 286 IDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILLYqSGDERihYFFNQLSREQRQSFE 349
Cdd:COG0513 305 IDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLV-TPDER--RLLRAIEKLIGQKIE 365
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
19-362 |
5.76e-24 |
|
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: 105.30 E-value: 5.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 19 QEEIIQALLDGEDTLAILPTGTGKSLCYQ---LTGYLTD--GMVLIVSPLLSLMEDQVTQLQKRGEK-----RVAAFNSL 88
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLlpvLEALLEDpgATALYLYPTKALARDQLRRLRELAEAlglgvRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 89 LSRAERGYVLRHlSQYkflflspeMLTNP---------------SLLEQLKkqdiaLYVVDEAHCVSqwGVdF------- 146
Cdd:COG1205 141 TPPEERRWIREH-PDI--------VLTNPdmlhygllphhtrwaRFFRNLR-----YVVIDEAHTYR--GV-Fgshvanv 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 147 --RpeyqqLGKIREHLG-NPVTLALTATATD--------------LVAKD-----IRQVLFDRQP---KEVRQSVNRQNI 201
Cdd:COG1205 204 lrR-----LRRICRHYGsDPQFILASATIGNpaehaerltgrpvtVVDEDgsprgERTFVLWNPPlvdDGIRRSALAEAA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 202 SLFVRKTQQKEQeleqfmesahgaAIIYCATKKEVERLYHLFRERF-------SVGYYHGGLDTAQRRQLQQQFVKNQLQ 274
Cdd:COG1205 279 RLLADLVREGLR------------TLVFTRSRRGAELLARYARRALrepdladRVAAYRAGYLPEERREIERGLRSGELL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 275 FLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILLyqSGDERI-HYFFNqlsreqrqSFELYLE 353
Cdd:COG1205 347 GVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLV--AGDDPLdQYYVR--------HPEELFE 416
|
....*....
gi 488244010 354 YAAEQAPFD 362
Cdd:COG1205 417 RPPEAAVID 425
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
8-186 |
8.36e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 98.72 E-value: 8.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 8 KYFGFDSFRPGQEEIIQALLDGE-DTLAILPTGTGKSLCYQLT-----GYLTDGMVLIVSPLLSLMEDQVTQLQKRGEKR 81
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPalealKRGKGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 82 VAAFNSLLSRAERGYVLRHL--SQYKFLFLSPEMLTNPSLLEQLKKQDIALYVVDEAHCVSQWGvdFRPEYQQLGKIREH 159
Cdd:smart00487 82 GLKVVGLYGGDSKREQLRKLesGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLLPK 159
|
170 180
....*....|....*....|....*..
gi 488244010 160 lgNPVTLALTATATDLVAKDIRQVLFD 186
Cdd:smart00487 160 --NVQLLLLSATPPEEIENLLELFLND 184
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
16-467 |
1.07e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 94.71 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 16 RPGQEEIIQALL-----DGEDTLAILPTGTGKSL--CYQLTGYLTDGMVLIVSPLLSLMEdqvtQLQKRgekrvaaFNSL 88
Cdd:COG1061 82 RPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlaLALAAELLRGKRVLVLVPRRELLE----QWAEE-------LRRF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 89 LSRAERGyVLRHLSQYKFLFLSPEMLTNPSLLEQLKKqDIALYVVDEAHCVSqwgvdfRPEYQqlgKIREHLGNPVTLAL 168
Cdd:COG1061 151 LGDPLAG-GGKKDSDAPITVATYQSLARRAHLDELGD-RFGLVIIDEAHHAG------APSYR---RILEAFPAAYRLGL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 169 TAT----------------------ATDLVAK------DIRQVLFDRQPKEVRQSVNRQNIS-LFVRKTQQKEQELEQFM 219
Cdd:COG1061 220 TATpfrsdgreillflfdgivyeysLKEAIEDgylappEYYGIRVDLTDERAEYDALSERLReALAADAERKDKILRELL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 220 ESAHG--AAIIYCATKKEVERLYHLFRER-FSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIH 296
Cdd:COG1061 300 REHPDdrKTLVFCSSVDHAEALAELLNEAgIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 297 YDLPDSLENYVQEIGRAGRDQEESAAILLYQSGDERIHYFFNQLSREQRQsfelyleyAAEQAPFDELQKKWMELIQQSE 376
Cdd:COG1061 380 LRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVGNDVPVLEELAKDLRDL--------AGYRVEFLDEEESEELALLIAV 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 377 KPENWVERLKRQEKEKEFRLQQMLRYIHEEDCRRKFILAYFGEELSEKPQNCCDIDGAKVELLPKKKDFSKTEPLHWESI 456
Cdd:COG1061 452 KPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLL 531
|
490
....*....|.
gi 488244010 457 LLNLFKKNMEH 467
Cdd:COG1061 532 LLLLLELLELL 542
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
10-323 |
2.22e-16 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 80.64 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 10 FGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSL-----CYQLTGY-LTDGMVLIVSPLLSLMEdqvtQLQKRGeKRVA 83
Cdd:PTZ00424 46 YGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTAtfviaALQLIDYdLNACQALILAPTRELAQ----QIQKVV-LALG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 84 AFNSLLSRAERG--YVLRHLSQYK----FLFLSPEMLTNPSLLEQLKKQDIALYVVDEAHCVSQWGvdFRpeyQQLGKIR 157
Cdd:PTZ00424 121 DYLKVRCHACVGgtVVRDDINKLKagvhMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRG--FK---GQIYDVF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 158 EHLGNPVTLAL-TATATDlvakDIRQVL--FDRQPKEV---RQSVNRQNISLF---VRKTQQKEQELEQFMESAH-GAAI 227
Cdd:PTZ00424 196 KKLPPDVQVALfSATMPN----EILELTtkFMRDPKRIlvkKDELTLEGIRQFyvaVEKEEWKFDTLCDLYETLTiTQAI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 228 IYCATKKEVERLYHLFRER-FSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENY 306
Cdd:PTZ00424 272 IYCNTRRKVDYLTKKMHERdFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENY 351
|
330
....*....|....*..
gi 488244010 307 VQEIGRAGRDQEESAAI 323
Cdd:PTZ00424 352 IHRIGRSGRFGRKGVAI 368
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
29-171 |
8.74e-16 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 74.36 E-value: 8.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 29 GEDTLAILPTGTGKSLCYQLTGYL----TDGMVLIVSPLLSLMEDQVTQLQKRGEK--RVAAFNSLLSRAERGYvlRHLS 102
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLlllkKGKKVLVLVPTKALALQTAERLRELFGPgiRVAVLVGGSSAEEREK--NKLG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 103 QYKFLFLSPEMLTNPSL-LEQLKKQDIALYVVDEAHCVSQWGVDFRPEYQQLgkIREHLGNPVTLALTAT 171
Cdd:cd00046 79 DADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALLIDSRGALILDLAV--RKAGLKNAQVILLSAT 146
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
11-333 |
1.93e-15 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 78.74 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 11 GFDSFRPGQEEIIQALLDGEDTLAILPTGTGKS------LCYQLTGYLTDGMVLIVSPLLSLMEdQVTQLQKRGEKRVAA 84
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTaafslpLLHNLDPELKAPQILVLAPTRELAV-QVAEAMTDFSKHMRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 85 FNSL-LSRAERGYV-LRHLSQykflflSPEML--TNPSLLEQLKKQDIAL-----YVVDEAHCVSQWGvdFRPEYQQ-LG 154
Cdd:PRK11634 104 VNVVaLYGGQRYDVqLRALRQ------GPQIVvgTPGRLLDHLKRGTLDLsklsgLVLDEADEMLRMG--FIEDVETiMA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 155 KI-REHLgnpvTLALTATATDLVAKDIRQvlFDRQPKEVR-QS--VNRQNISLFVRKTQ--QKEQELEQFMESAH-GAAI 227
Cdd:PRK11634 176 QIpEGHQ----TALFSATMPEAIRRITRR--FMKEPQEVRiQSsvTTRPDISQSYWTVWgmRKNEALVRFLEAEDfDAAI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 228 IYCATKKE-VERLYHLFRERFSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENY 306
Cdd:PRK11634 250 IFVRTKNAtLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESY 329
|
330 340
....*....|....*....|....*..
gi 488244010 307 VQEIGRAGRDQEESAAILLYQSGDERI 333
Cdd:PRK11634 330 VHRIGRTGRAGRAGRALLFVENRERRL 356
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
227-325 |
2.95e-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: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 227 IIYCATKKEVERLYHLFRERF--------SVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYD 298
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLveegplasKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*..
gi 488244010 299 LPDSLENYVQEIGRAGRDQEESAAILL 325
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
2-315 |
9.36e-15 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 76.10 E-value: 9.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 2 LINELKKY---FGFDSFRPGQEEIIQALLDGEDTLAILPTGTGK------SLCYQLTG-------YLTDGMVLIVSPL-- 63
Cdd:PRK01297 94 LAPELMHAihdLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKtaafliSIINQLLQtpppkerYMGEPRALIIAPTre 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 64 -----------------LSLM--------EDQVTQLQKRG-EKRVAAFNSLLSRAERGYVlrHLSQYKFLflspemltnp 117
Cdd:PRK01297 174 lvvqiakdaaaltkytgLNVMtfvggmdfDKQLKQLEARFcDILVATPGRLLDFNQRGEV--HLDMVEVM---------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 118 slleqlkkqdialyVVDEAHCVSQWGvdFRPEYQQLGKIREHLGNPVTLALTATATDLVAKDIRQVLFDR-----QPKEV 192
Cdd:PRK01297 242 --------------VLDEADRMLDMG--FIPQVRQIIRQTPRKEERQTLLFSATFTDDVMNLAKQWTTDPaiveiEPENV 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 193 RQSVNRQNIslFVRKTQQKEQELEQFM-ESAHGAAIIYCATKKEVERLY-HLFRERFSVGYYHGGLDTAQRRQLQQQFVK 270
Cdd:PRK01297 306 ASDTVEQHV--YAVAGSDKYKLLYNLVtQNPWERVMVFANRKDEVRRIEeRLVKDGINAAQLSGDVPQHKRIKTLEGFRE 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 488244010 271 NQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGR 315
Cdd:PRK01297 384 GKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGR 428
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
11-342 |
1.48e-14 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 75.59 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 11 GFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQL----------TGYLTD-----GMVLIVSPLLSL-MEDQVTQL 74
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVpiisrcctirSGHPSEqrnplAMVLTPTRELCVqVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 75 QKRGEKRVA------AFNSLLSRAERGYVLrhlsqykflflspeMLTNPS-LLEQLKKQDIAL-----YVVDEAHCVSQW 142
Cdd:PLN00206 220 GKGLPFKTAlvvggdAMPQQLYRIQQGVEL--------------IVGTPGrLIDLLSKHDIELdnvsvLVLDEVDCMLER 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 143 GvdFRpeyQQLGKIREHLGNPVTLALTATATDLV-------AKDIRQVLFDrQPKEVRQSVNRqnISLFVRKTQQKEQEL 215
Cdd:PLN00206 286 G--FR---DQVMQIFQALSQPQVLLFSATVSPEVekfasslAKDIILISIG-NPNRPNKAVKQ--LAIWVETKQKKQKLF 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 216 EQFMESAH--GAAIIYCATKKEVERLYHLFR-----ERFSVgyyHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDK 288
Cdd:PLN00206 358 DILKSKQHfkPPAVVFVSSRLGADLLANAITvvtglKALSI---HGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 488244010 289 SDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILLYQSGDERIHYFFNQLSR 342
Cdd:PLN00206 435 LRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLK 488
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
269-326 |
2.24e-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: 62.34 E-value: 2.24e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488244010 269 VKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILLY 326
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILF 76
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
2-315 |
4.04e-12 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 68.00 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 2 LINELKKyFGFDSFRPGQEEIIQA-LLDGEDTLAILPTGTGKSLCYQL---TGYLTDGMVLIVSPLLSL----MEDQVTQ 73
Cdd:COG1204 11 VIEFLKE-RGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELailKALLNGGKALYIVPLRALasekYREFKRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 74 LQKRGEKRVAAFNSLLSRAERgyvlrhLSQYKFLFLSPEML-----TNPSLLEqlkkqDIALYVVDEAHCVsqwGVDFR- 147
Cdd:COG1204 90 FEELGIKVGVSTGDYDSDDEW------LGRYDILVATPEKLdsllrNGPSWLR-----DVDLVVVDEAHLI---DDESRg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 148 PEYQQ-LGKIREHLGNPVTLALTATA--TDLVAK--DIRQVLFDRQPKEVRQSVNRQNISLFVRKTQQKEQELEQFMESA 222
Cdd:COG1204 156 PTLEVlLARLRRLNPEAQIVALSATIgnAEEIAEwlDAELVKSDWRPVPLNEGVLYDGVLRFDDGSRRSKDPTLALALDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 223 ---HGAAIIYCATKKEVERL-------------------YHLFRERFS-------------------VGYYHGGLDTAQR 261
Cdd:COG1204 236 leeGGQVLVFVSSRRDAESLakkladelkrrltpeereeLEELAEELLevseethtnekladclekgVAFHHAGLPSELR 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488244010 262 RQLQQQFVKNQLQFLIATNAFGMGIDK-------SDIRYVIHYDLPdSLEnYVQEIGRAGR 315
Cdd:COG1204 316 RLVEDAFREGLIKVLVATPTLAAGVNLparrviiRDTKRGGMVPIP-VLE-FKQMAGRAGR 374
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
198-323 |
6.50e-12 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 67.67 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 198 RQNIslFVRKTQQKEQELEQFMESAHGA-AIIYCATKKEVERLYH-LFRERFSVGYYHGGLDTAQRRQLQQQFVKNQLQF 275
Cdd:PRK04537 233 RQRI--YFPADEEKQTLLLGLLSRSEGArTMVFVNTKAFVERVARtLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEI 310
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488244010 276 LIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAI 323
Cdd:PRK04537 311 LVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAI 358
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
27-368 |
1.23e-11 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 66.72 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 27 LDGEDTLAILPTGTGKSLCYQLTGYL----------TDG-MVLIVSPLLSLMEdqvtqlQKRGEKRV-AAFNSLLSRAER 94
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAIVhinaqpllryGDGpIVLVLAPTRELAE------QIREQCNKfGASSKIRNTVAY 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 95 GYVLRHLSQY------KFLFLSPEMLTNpsLLEQ----LKKqdIALYVVDEAHCVSQWGvdFRPEYQQL-GKIREhlgNP 163
Cdd:PTZ00110 239 GGVPKRGQIYalrrgvEILIACPGRLID--FLESnvtnLRR--VTYLVLDEADRMLDMG--FEPQIRKIvSQIRP---DR 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 164 VTLALTATATDLVAKDIRQvLFDRQPKEVR-QSVNR---QNISLFVRKTQQKEQE------LEQFMESAhGAAIIYCATK 233
Cdd:PTZ00110 310 QTLMWSATWPKEVQSLARD-LCKEEPVHVNvGSLDLtacHNIKQEVFVVEEHEKRgklkmlLQRIMRDG-DKILIFVETK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 234 KEVERLYHLFR-ERFSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGR 312
Cdd:PTZ00110 388 KGADFLTKELRlDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGR 467
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 488244010 313 AGRDQEESAAILLYQSGDERIHYFFNQLSREQRQSFELYLEYAAEQAPFDELQKKW 368
Cdd:PTZ00110 468 TGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRW 523
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
226-323 |
2.84e-11 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 64.99 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 226 AIIYCATKKEVERLY-HLFRERFSVGYYHGglDTAQRRQLQ--QQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDS 302
Cdd:PRK04837 258 AIIFANTKHRCEEIWgHLAADGHRVGLLTG--DVAQKKRLRilEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDD 335
|
90 100
....*....|....*....|.
gi 488244010 303 LENYVQEIGRAGRDQEESAAI 323
Cdd:PRK04837 336 CEDYVHRIGRTGRAGASGHSI 356
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
371-431 |
2.04e-10 |
|
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: 56.53 E-value: 2.04e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488244010 371 LIQQSEKPEnwverlKRQEKEKEfRLQQMLRY-IHEEDCRRKFILAYFGEELSEKPQNCCDI 431
Cdd:pfam16124 10 LIEQSEADE------ERKEVELQ-KLQAMVAYcENTTDCRRKQLLRYFGEEFDSEPCGNCDN 64
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
19-333 |
9.95e-10 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 60.34 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 19 QEEIIQALLDGEDTLAILPTGTGKSLCYQLTG--YLTD--------GMVLIVSP---LLSLMEDQVTQLQKRGEKRVAAF 85
Cdd:PRK11192 28 QAEAIPPALDGRDVLGSAPTGTGKTAAFLLPAlqHLLDfprrksgpPRILILTPtreLAMQVADQARELAKHTHLDIATI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 86 NSLLSRAERGYVLRhlSQYKFLFLSPEmltnpSLLEQLKK-----QDIALYVVDEAHCVSQWGvdFRPEYQQLGKirEHL 160
Cdd:PRK11192 108 TGGVAYMNHAEVFS--ENQDIVVATPG-----RLLQYIKEenfdcRAVETLILDEADRMLDMG--FAQDIETIAA--ETR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 161 GNPVTLALTAT-ATDLVAKDIRQVLFD----------RQPKEVRQSVNRQN-----ISLFVRKTQQKEQEleqfmesahg 224
Cdd:PRK11192 177 WRKQTLLFSATlEGDAVQDFAERLLNDpveveaepsrRERKKIHQWYYRADdlehkTALLCHLLKQPEVT---------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 225 AAIIYCATKKEVERLYHLFRER-FSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSL 303
Cdd:PRK11192 247 RSIVFVRTRERVHELAGWLRKAgINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSA 326
|
330 340 350
....*....|....*....|....*....|
gi 488244010 304 ENYVQEIGRAGRDQEESAAILLYQSGDERI 333
Cdd:PRK11192 327 DTYLHRIGRTGRAGRKGTAISLVEAHDHLL 356
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
208-315 |
2.05e-09 |
|
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: 56.02 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 208 TQQKEQELEQFMESAHGAAIIYCATKKEVERLYhlfRERFSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGID 287
Cdd:cd18795 28 DSDIIVLLKIETVSEGKPVLVFCSSRKECEKTA---KDLAGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVN 104
|
90 100 110
....*....|....*....|....*....|....*..
gi 488244010 288 --------KSDIRY-VIHYDLPDSLEnYVQEIGRAGR 315
Cdd:cd18795 105 lpartviiKGTQRYdGKGYRELSPLE-YLQMIGRAGR 140
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
19-137 |
3.52e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 56.05 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 19 QEEIIQALLDGEDTLAILPTGTGKSLCYQL-----TGYLTDGMVLIVSPLLSLMEDQVTQLQKRGEK-----RVAAFNSL 88
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLpileaLLRDPGSRALYLYPTKALAQDQLRSLRELLEQlglgiRVATYDGD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488244010 89 LSRAERGYVLRHLSQYkflflspeMLTNPSLLEQL----KKQDIALY------VVDEAH 137
Cdd:cd17923 85 TPREERRAIIRNPPRI--------LLTNPDMLHYAllphHDRWARFLrnlryvVLDEAH 135
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
221-315 |
3.60e-09 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 55.35 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 221 SAHGAAIIYCATKKEVERLYHLFRERFS-------VGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRY 293
Cdd:cd18796 36 ERHKSTLVFTNTRSQAERLAQRLRELCPdrvppdfIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDL 115
|
90 100
....*....|....*....|..
gi 488244010 294 VIHYDLPDSLENYVQEIGRAGR 315
Cdd:cd18796 116 VIQIGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
16-183 |
2.34e-08 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members 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: 350790 [Multi-domain] Cd Length: 163 Bit Score: 53.33 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 16 RPGQEEIIQALLD----GED-TLAILPTGTGK-----SLCYQLTGYLTDGMVLIVSPllslMEDQVTQLQKrgekrvaAF 85
Cdd:cd18032 2 RYYQQEAIEALEEarekGQRrALLVMATGTGKtytaaFLIKRLLEANRKKRILFLAH----REELLEQAER-------SF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 86 NSLLSRAERGYVL---RHLSQYKFLFLSPEMLTNPSLLEQLKKQDIALYVVDEAHcvsqwgvdfRPEYQQLGKIREHLGN 162
Cdd:cd18032 71 KEVLPDGSFGNLKggkKKPDDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAH---------HAIASSYRKILEYFEP 141
|
170 180
....*....|....*....|.
gi 488244010 163 PVTLALTATATDLVAKDIRQV 183
Cdd:cd18032 142 AFLLGLTATPERTDGLDTYEL 162
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
11-325 |
6.29e-08 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 54.81 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 11 GFDSFRPGQEEIIQALLDGEDTLAILPTGTGKslcyqltgylTDGMVLivsPLLSLMEDQvtQLQKRGEKRVAAFNSLLS 90
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGK----------TAGFTL---PLLQHLITR--QPHAKGRRPVRALILTPT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 91 R---AERGYVLRHLSQYKFL---------FLSPEML----------TNPSLLEQLKKQD------IALYVVDEAHCVSQW 142
Cdd:PRK10590 85 RelaAQIGENVRDYSKYLNIrslvvfggvSINPQMMklrggvdvlvATPGRLLDLEHQNavkldqVEILVLDEADRMLDM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 143 GV--DFRPEYQQLGKIREHLgnpvtlALTATATDLVAKDIRQVLfdRQPKEVrqSVNRQN-----ISLFVRKTQQK-EQE 214
Cdd:PRK10590 165 GFihDIRRVLAKLPAKRQNL------LFSATFSDDIKALAEKLL--HNPLEI--EVARRNtaseqVTQHVHFVDKKrKRE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 215 LEQFM--ESAHGAAIIYCATKKEVERLY-HLFRERFSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDI 291
Cdd:PRK10590 235 LLSQMigKGNWQQVLVFTRTKHGANHLAeQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEEL 314
|
330 340 350
....*....|....*....|....*....|....
gi 488244010 292 RYVIHYDLPDSLENYVQEIGRAGRDQEESAAILL 325
Cdd:PRK10590 315 PHVVNYELPNVPEDYVHRIGRTGRAAATGEALSL 348
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
14-171 |
2.65e-06 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 47.71 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 14 SFRPGQEEIIQA-LLDGEDTLAILPTGTGKSLCYQLTG---YLTDGMVLIVSPLLSLMEDQVTQLQKRGEK--RVAAfnS 87
Cdd:cd18028 1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMvntLLEGGKALYLVPLRALASEKYEEFKKLEEIglKVGI--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 88 LLSRAERGYvlrHLSQYKFLFLSPEMLTnpSLLEQLKK--QDIALYVVDEAHCVSQWGVDFRPEYqQLGKIREHLGNPVT 165
Cdd:cd18028 79 TGDYDEDDE---WLGDYDIIVATYEKFD--SLLRHSPSwlRDVGVVVVDEIHLISDEERGPTLES-IVARLRRLNPNTQI 152
|
....*.
gi 488244010 166 LALTAT 171
Cdd:cd18028 153 IGLSAT 158
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
14-184 |
1.43e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 45.89 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 14 SFRPGQEEIIQALLDGEDTLAILPTGTGKS-----LC-YQLTGYLTD--GMVLIVSPLLSLMEDQVTQLQKRGEK---RV 82
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICeHHLKKFPAGrkGKVVFLANKVPLVEQQKEVFRKHFERpgyKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 83 AAFNSLLSRAERGYVLrhLSQYKFLFLSPEMLTNpSLL--EQLKKQDIALYVVDEAHCVSQWGV----DFRPEYQQLGKI 156
Cdd:cd17927 82 TGLSGDTSENVSVEQI--VESSDVIIVTPQILVN-DLKsgTIVSLSDFSLLVFDECHNTTKNHPyneiMFRYLDQKLGSS 158
|
170 180
....*....|....*....|....*...
gi 488244010 157 REhlgNPVTLALTATATDLVAKDIRQVL 184
Cdd:cd17927 159 GP---LPQILGLTASPGVGGAKNTEEAL 183
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
252-314 |
2.30e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 47.23 E-value: 2.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488244010 252 YHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAG 314
Cdd:PRK09751 307 HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
14-141 |
2.85e-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: 44.56 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 14 SFRPGQEEII-QALLDGEDTLAILPTGTGKSLCYQLTGYLT----DGMVLIVSPLLSLMEDQVTQLQKR---GEKRVAAF 85
Cdd:cd17921 1 LLNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRAlatsGGKAVYIAPTRALVNQKEADLRERfgpLGKNVGLL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488244010 86 NSLLSRAergyvLRHLSQYKFLFLSPEMLTNPSL-LEQLKKQDIALYVVDEAHCVSQ 141
Cdd:cd17921 81 TGDPSVN-----KLLLAEADILVATPEKLDLLLRnGGERLIQDVRLVVVDEAHLIGD 132
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
215-315 |
2.89e-05 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 46.76 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 215 LEQFMESAHgAAIIYCATKKEVERLYHLFRER-FSVGYYHGGLDTAQRRQLQQQFVKNQ--LQFLIATNAFGMGIDKSDI 291
Cdd:COG0553 542 LEELLAEGE-KVLVFSQFTDTLDLLEERLEERgIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAA 620
|
90 100
....*....|....*....|....*.
gi 488244010 292 RYVIHYDLPDS--LENyvQEIGRAGR 315
Cdd:COG0553 621 DHVIHYDLWWNpaVEE--QAIDRAHR 644
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
2-46 |
4.70e-05 |
|
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: 44.35 E-value: 4.70e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 488244010 2 LINELKKYfGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCY 46
Cdd:cd00268 1 LLKALKKL-GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAF 44
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
19-171 |
4.80e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 44.04 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 19 QEEIIQALLDGEDTLAILPTGTGKSL------CYQLTGYltDGMVLIVSPLLSLMEDQVTQLQK--RGEKRVAAFNSLLS 90
Cdd:cd18035 6 YQVLIAAVALNGNTLIVLPTGLGKTIiailvaADRLTKK--GGKVLILAPSRPLVEQHAENLKRvlNIPDKITSLTGEVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 91 RAERGYVLRhlsQYKFLFLSPEMLTNPSLLEQLKKQDIALYVVDEAH-CVSQWGVDFRPEyqqlgKIREHLGNPVTLALT 169
Cdd:cd18035 84 PEERAERWD---ASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHhAVGNYAYVYIAH-----RYKREANNPLILGLT 155
|
..
gi 488244010 170 AT 171
Cdd:cd18035 156 AS 157
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
29-175 |
5.42e-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: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 29 GEDTLAILPTGTGKSL------CYQLTGYLTDGM-VLIVSPLLSLMEDQVTQLQKRGEK-----RVAAFNSLLSRAERGY 96
Cdd:cd17922 1 GRNVLIAAPTGSGKTEaaflpaLSSLADEPEKGVqVLYISPLKALINDQERRLEEPLDEidleiPVAVRHGDTSQSEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 97 VLRHLSQykFLFLSPE----MLTNPSLLEQLKkqDIALYVVDEAHCV--SQWGVDFRPEYQQLGKIREhlGNPVTLALTA 170
Cdd:cd17922 81 QLKNPPG--ILITTPEslelLLVNKKLRELFA--GLRYVVVDEIHALlgSKRGVQLELLLERLRKLTG--RPLRRIGLSA 154
|
....*
gi 488244010 171 TATDL 175
Cdd:cd17922 155 TLGNL 159
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
14-171 |
7.30e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 43.04 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 14 SFRPGQEEIIQALLDGEDT-----LAILPTGTGKS-----LCYQLTGYLTDGMVLIVSPLLSLMEDQVTQLQKRGEKRVA 83
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKNgqkrgLIVMATGSGKTltaakLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 84 AFNSLLSRAERgyvlRHLSQYKFLFLSPEMLTNPSLL--EQLKKQDIALYVVDEAHCVSqwgvdfRPEYQQlgkIREHLG 161
Cdd:pfam04851 83 IGEIISGDKKD----ESVDDNKIVVTTIQSLYKALELasLELLPDFFDVIIIDEAHRSG------ASSYRN---ILEYFK 149
|
170
....*....|
gi 488244010 162 NPVTLALTAT 171
Cdd:pfam04851 150 PAFLLGLTAT 159
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
205-317 |
1.01e-04 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 42.19 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 205 VRKTQQKEQEL-EQFMESAHGAAIIYCATKKEVERLYHLFRE------RFSVGYYHGG--------LDTAQRRQLQ--QQ 267
Cdd:cd18802 6 IPKLQKLIEILrEYFPKTPDFRGIIFVERRATAVVLSRLLKEhpstlaFIRCGFLIGRgnssqrkrSLMTQRKQKEtlDK 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488244010 268 FVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQ 317
Cdd:cd18802 86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
226-316 |
1.54e-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: 41.69 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 226 AIIYCATKKEVERLYHLFRER-FSVGYYHGGLDTAQRRQLQQQFVKNQ--LQFLIATNAFGMGIDKSDIRYVIHYDLP-- 300
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERgIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPWwn 109
|
90
....*....|....*.
gi 488244010 301 DSLENyvQEIGRAGRD 316
Cdd:cd18793 110 PAVEE--QAIDRAHRI 123
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
15-171 |
2.52e-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: 41.14 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 15 FRPGQEEIIQALLDGE-DTLAI--LPTGTGKSLC-YQLTGYLTDGMVLIVSPLLSLMEdqvtqlqkrgeKRVAAFNSLLS 90
Cdd:cd17926 1 LRPYQEEALEAWLAHKnNRRGIlvLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLD-----------QWKERFEDFLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 91 RAERGYV----LRHLSQYKFLFLSPEMLTNPSLLEQLKKQDIALYVVDEAH--CVSQWgvdfrpeyqqlGKIREHLGNPV 164
Cdd:cd17926 70 DSSIGLIgggkKKDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHhlPAKTF-----------SEILKELNAKY 138
|
....*..
gi 488244010 165 TLALTAT 171
Cdd:cd17926 139 RLGLTAT 145
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
12-314 |
1.00e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 41.80 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 12 FDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLC---------YQL--TGYLTDGM-VLIVSPLLSLMED---------- 69
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAaflaiidelFRLgrEGELEDKVyCLYVSPLRALNNDihrnleeplt 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 70 QVTQL-QKRGEK----RVAAFNSLLSRAERGYVLR---HLsqykfLFLSPE----MLTNPSLLEQLKkqDIALYVVDEAH 137
Cdd:PRK13767 110 EIREIaKERGEElpeiRVAIRTGDTSSYEKQKMLKkppHI-----LITTPEslaiLLNSPKFREKLR--TVKWVIVDEIH 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 138 CV--SQWGVDFRPEYQQLGKIREhlGNPVTLALTATATDL--VAKDIRQVLFDRQPKEVR----QSVNRQNISL------ 203
Cdd:PRK13767 183 SLaeNKRGVHLSLSLERLEELAG--GEFVRIGLSATIEPLeeVAKFLVGYEDDGEPRDCEivdaRFVKPFDIKVispvdd 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 204 FVRKTQQKEQE-----LEQFMESaHGAAIIYCATKKEVER-LYHLfRERFS-------VGYYHGGLDTAQRRQLQQQFVK 270
Cdd:PRK13767 261 LIHTPAEEISEalyetLHELIKE-HRTTLIFTNTRSGAERvLYNL-RKRFPeeydednIGAHHSSLSREVRLEVEEKLKR 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 488244010 271 NQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAG 314
Cdd:PRK13767 339 GELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
237-326 |
1.07e-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: 39.63 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 237 ERLYHLFRERFSVGYYHGGLDTAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDlPD--SLENYVQEIGRAG 314
Cdd:cd18811 52 EYLKERFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED-AErfGLSQLHQLRGRVG 130
|
90
....*....|..
gi 488244010 315 RDQEESAAILLY 326
Cdd:cd18811 131 RGDHQSYCLLVY 142
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
8-140 |
1.19e-03 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 40.28 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 8 KYFGFDSFRPGQEEIIQA--LLDGEDTLAILPTGTGKSLCYQL----TGYLTDGMVLIVSPLLSLMEDQVTQLQKRGEK- 80
Cdd:cd18026 10 AKKGIKKLYDWQKECLSLpgLLEGRNLVYSLPTSGGKTLVAEIlmlkRLLERRKKALFVLPYVSIVQEKVDALSPLFEEl 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488244010 81 --RVAAFNSLLSRAERgyvlRHLSQYKFLFLSPE---MLTNpSLLEQLKKQDIALYVVDEAHCVS 140
Cdd:cd18026 90 gfRVEGYAGNKGRSPP----KRRKSLSVAVCTIEkanSLVN-SLIEEGRLDELGLVVVDELHMLG 149
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
7-136 |
2.29e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain] Cd Length: 189 Bit Score: 39.23 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 7 KKYFGFDSFRPgQEEIIQALLDGEDTLAILPTGTGKS---LCYQLTGYLTDGMVLIVSPLLSLMEDQVTQLQKRGEK--- 80
Cdd:cd17924 11 KKKTGFPPWGA-QRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSLYLASKGKRSYLIFPTKSLVKQAYERLSKYAEKagv 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488244010 81 --RVAAFNSLLSRAERGYVLRHLS--QYKFL-----FLSPEMltnpsllEQLKKQDIALYVVDEA 136
Cdd:cd17924 90 evKILVYHSRLKKKEKEELLEKIEkgDFDILvttnqFLSKNF-------DLLSNKKFDFVFVDDV 147
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
6-46 |
3.57e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 39.91 E-value: 3.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 488244010 6 LKKYFGFDSFRPGQ----EEIIQALLDGEDTLAILPTGTGKSLCY 46
Cdd:COG1199 6 LALAFPGFEPRPGQremaEAVARALAEGRHLLIEAGTGTGKTLAY 50
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
233-315 |
7.86e-03 |
|
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: 36.77 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 233 KKEVERLYHLfreRFSVGYyhGGLDTAQRRQLQQQFV--KNQLQFLIATNAFGMGIDKSdIRYVIHYDL--PDSLEN--- 305
Cdd:cd18805 34 KREIEKRTGL---KCAVIY--GALPPETRRQQARLFNdpESGYDVLVASDAIGMGLNLN-IRRVIFSSLskFDGNEMrpl 107
|
90
....*....|....
gi 488244010 306 YVQEI----GRAGR 315
Cdd:cd18805 108 SPSEVkqiaGRAGR 121
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
2-82 |
8.90e-03 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 37.44 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488244010 2 LINELKKYfGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYL-----------TDG-MVLIVSPLLSL--- 66
Cdd:cd17958 1 IMKEIKKQ-GFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIhldlqpipreqRNGpGVLVLTPTRELalq 79
|
90
....*....|....*.
gi 488244010 67 MEDQVTQLQKRGEKRV 82
Cdd:cd17958 80 IEAECSKYSYKGLKSV 95
|
|
| |
