|
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: 535.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 2 LINELKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLMEGLVIIVSPLLSLMEDQVTQLQKRGEkR 81
Cdd:COG0514 5 ALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGI-R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 82 VAAFNSLLSQSERRYVLRHLS--QYKFLFLSPEMLTNPSLLEHLKKQNIALYVVDEAHCVSQWGVDFRPEYQQLGKIRKL 159
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRagELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 160 LGNPVTLALTATATDLVARDIRHVLFDRPPKEIRQSVNRQNISLFVRKT--QQKEQELEHFM-ERAQGAAIIYCATKKEV 236
Cdd:COG0514 164 LPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLkEHPGGSGIVYCLSRKKV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 237 ERLYHLFRER-FTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGR 315
Cdd:COG0514 244 EELAEWLREAgIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 316 DQEESAAILFYQSGDERIHYFFnqlsreqrqsfelyleyateqapfdelqkkwmelIQQSEKPenwvERLKHQEKEKefr 395
Cdd:COG0514 324 DGLPAEALLLYGPEDVAIQRFF----------------------------------IEQSPPD----EERKRVERAK--- 362
|
410 420 430
....*....|....*....|....*....|....*.
gi 488252204 396 LQQMLRYINEENCRRKFILAYFGEKLSEkPQNCCDI 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 ... |
6-431 |
1.26e-132 |
|
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: 395.60 E-value: 1.26e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 6 LKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLMEGLVIIVSPLLSLMEDQVTQLQKRGeKRVAAF 85
Cdd:TIGR01389 5 LKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAG-VAAAYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 86 NSLLSQSERRYVLRHLS--QYKFLFLSPEMLTNPSLLEHLKKQNIALYVVDEAHCVSQWGVDFRPEYQQLGKIRKLLGNP 163
Cdd:TIGR01389 84 NSTLSAKEQQDIEKALVngELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFPQV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 164 VTLALTATATDLVARDIRHVLFDRPPKEIRQSVNRQNISLFVRKTQQKEQELEHFMERAQG-AAIIYCATKKEVERLYHL 242
Cdd:TIGR01389 164 PRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGqSGIIYASSRKKVEELAER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 243 FRER-FTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESA 321
Cdd:TIGR01389 244 LESQgISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 322 AILFYQSGDERIHYFFnqlsreqrqsfelyleyateqapfdelqkkwmelIQQSEKPENwverLKHQEKEKefrLQQMLR 401
Cdd:TIGR01389 324 AILLYSPADIALLKRR----------------------------------IEQSEADDD----YKQIEREK---LRAMIA 362
|
410 420 430
....*....|....*....|....*....|..
gi 488252204 402 YINEENCRRKFILAYFGEklsEKPQNC--CDI 431
Cdd:TIGR01389 363 YCETQTCRRAYILRYFGE---NEVEPCgnCDN 391
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
6-456 |
1.37e-110 |
|
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: 334.82 E-value: 1.37e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 6 LKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLMEGLVIIVSPLLSLMEDQVTQLQKRGekrVAA- 84
Cdd:TIGR00614 3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALG---IPAt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 85 -FNSLLSQSERRYVLRHL--SQYKFLFLSPEML-TNPSLLEHLKKQ-NIALYVVDEAHCVSQWGVDFRPEYQQLGKIRKL 159
Cdd:TIGR00614 80 fLNSAQTKEQQLNVLTDLkdGKIKLLYVTPEKIsASNRLLQTLEERkGITLIAVDEAHCISQWGHDFRPDYKALGSLKQK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 160 LGNPVTLALTATATDLVARDIRHVLFDRPPKEIRQSVNRQNISLFV-RKTQQKEQELEHFMERAQ--GAAIIYCATKKEV 236
Cdd:TIGR00614 160 FPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVrRKTPKILEDLLRFIRKEFegKSGIIYCPSRKKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 237 ERLY-HLFRERFTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGR 315
Cdd:TIGR00614 240 EQVAaELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 316 DQEESAAILFYQSGDerihyffnqlsreqrqsfelyleyateqapfdelqkkwmeliqqsekpENWVERLKHQEKEKEFR 395
Cdd:TIGR00614 320 DGLPSECHLFYAPAD------------------------------------------------MNRLRRLLMEEPDGNFR 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488252204 396 ------LQQMLRYINEENCRRKFILAYFGEKLSEK------PQNCCD-----IDGAKAELLPKRKLFSKTEQLHWETI 456
Cdd:TIGR00614 352 tyklklYEMMEYCLNSSTCRRLILLSYFGEKGFNKsfcimgTEKCCDncckrLDYKTKDVTDKVYDFGPQAQKALSAV 429
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
6-431 |
1.53e-98 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 308.18 E-value: 1.53e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 6 LKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLMEGLVIIVSPLLSLMEDQVTQLQKRGekrVAA- 84
Cdd:PRK11057 17 LQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANG---VAAa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 85 -FNSLLSQSERRYVLR--HLSQYKFLFLSPEMLTNPSLLEHLKKQNIALYVVDEAHCVSQWGVDFRPEYQQLGKIRKLLG 161
Cdd:PRK11057 94 cLNSTQTREQQLEVMAgcRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRFP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 162 NPVTLALTATATDLVARDIRHVLFDRPPKEIRQSVNRQNIS-LFVRKTQQKEQeLEHFMERAQG-AAIIYCATKKEVERL 239
Cdd:PRK11057 174 TLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRyTLVEKFKPLDQ-LMRYVQEQRGkSGIIYCNSRAKVEDT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 240 YHLFRER-FTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQE 318
Cdd:PRK11057 253 AARLQSRgISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 319 ESAAILFYQSGDerihyffnqlsreqrqsfELYLEYATEQAPFDELQKkwmeliqqsekpenwVERLKhqekekefrLQQ 398
Cdd:PRK11057 333 PAEAMLFYDPAD------------------MAWLRRCLEEKPAGQQQD---------------IERHK---------LNA 370
|
410 420 430
....*....|....*....|....*....|...
gi 488252204 399 MLRYINEENCRRKFILAYFGEKlSEKPQNCCDI 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 |
5.48e-93 |
|
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: 279.80 E-value: 5.48e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 5 ELKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLMEGLVIIVSPLLSLMEDQVTQLQKRGeKRVAA 84
Cdd:cd17920 3 ILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLG-IRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 85 FNSLLSQSERRYVLR--HLSQYKFLFLSPEMLTNPSLLEHLKKQN----IALYVVDEAHCVSQWGVDFRPEYQQLGKIRK 158
Cdd:cd17920 82 LNSTLSPEEKREVLLriKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLRR 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 488252204 159 LLGNPVTLALTATATDLVARDIRHVLFDRPPKEIRQSVN 197
Cdd:cd17920 162 ALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
7-430 |
9.83e-76 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 257.52 E-value: 9.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 7 KKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLMEGLVIIVSPLLSLMEDQVTQLQKrGEKRVAAFN 86
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQ-ANIPAASLS 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 87 SLLSQSERRYVLRHLS----QYKFLFLSPEMLT-NPSLLEHLKKQN----IALYVVDEAHCVSQWGVDFRPEYQQLGKIR 157
Cdd:PLN03137 532 AGMEWAEQLEILQELSseysKYKLLYVTPEKVAkSDSLLRHLENLNsrglLARFVIDEAHCVSQWGHDFRPDYQGLGILK 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 158 KLLGNPVTLALTATATDLVARDIRHVLFDRPPKEIRQSVNRQNISL-FVRKTQQKEQELEHFMERAQ--GAAIIYCATKK 234
Cdd:PLN03137 612 QKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYsVVPKTKKCLEDIDKFIKENHfdECGIIYCLSRM 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 235 EVERLYHLFRE-RFTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRA 313
Cdd:PLN03137 692 DCEKVAERLQEfGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRA 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 314 GRDQEESAAILFYQSGDE-RIHYFFNQLSREQRQSFELYLEYATEqapfdelqkkwmeliqqsekpenwvERLKHQEKEK 392
Cdd:PLN03137 772 GRDGQRSSCVLYYSYSDYiRVKHMISQGGVEQSPMAMGYNRMASS-------------------------GRILETNTEN 826
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 488252204 393 EFRlqqMLRYI-NEENCRRKFILAYFGEKL-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) ... |
6-188 |
1.44e-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: 219.82 E-value: 1.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 6 LKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLME----GLVIIVSPLLSLMEDQVTQLQKRgeKR 81
Cdd:cd18018 4 LRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPRA--IK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 82 VAAFNSLLSQSERRYVLRHL--SQYKFLFLSPEMLTNPSLLEHLK-KQNIALYVVDEAHCVSQWGVDFRPEYQQLGK-IR 157
Cdd:cd18018 82 AAALNSSLTREERRRILEKLraGEVKILYVSPERLVNESFRELLRqTPPISLLVVDEAHCISEWSHNFRPDYLRLCRvLR 161
|
170 180 190
....*....|....*....|....*....|.
gi 488252204 158 KLLGNPVTLALTATATDLVARDIRHVLFDRP 188
Cdd:cd18018 162 ELLGAPPVLALTATATKRVVEDIASHLGIPE 192
|
|
| DpdF |
NF041063 |
protein DpdF; |
6-353 |
7.39e-56 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 198.60 E-value: 7.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 6 LKKYFGFDSFR-PGQEEIIQALL---DGEDTLAILPTGTGKSLCYQ---LTGYLMEGLVIIVSPLLSLMEDQVTQLQKRG 78
Cdd:NF041063 131 LAEALGFTHYRsPGQREAVRAALlapPGSTLIVNLPTGSGKSLVAQapaLLASRQGGLTLVVVPTVALAIDQERRARELL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 79 EKRVA------AFNSLLSQSERRYVLRHL---SQyKFLFLSPEMLTNpSLLEHL----KKQNIALYVVDEAHCVSQWGVD 145
Cdd:NF041063 211 RRAGPdlggplAWHGGLSAEERAAIRQRIrdgTQ-RILFTSPESLTG-SLRPALfdaaEAGLLRYLVVDEAHLVDQWGDG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 146 FRPEYQQLGKIRKLL-------GNPVTLALTATATDLVARDIRHvLFDRPpkEIRQSVN----RQNISLFVRKTQQKEQE 214
Cdd:NF041063 289 FRPEFQLLAGLRRSLlrlapsgRPFRTLLLSATLTESTLDTLET-LFGPP--GPFIVVSavqlRPEPAYWVAKCDSEEER 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 215 LEHFME---RAQGAAIIYCATKKEVERLYHLFRE----RftVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGID 287
Cdd:NF041063 366 RERVLEalrHLPRPLILYVTKVEDAEAWLQRLRAagfrR--VALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMD 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488252204 288 KSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILFYQSGDERIHyffNQLSREQRQSFELYLE 353
Cdd:NF041063 444 KSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIA---KSLNRPKLISVEKGLE 506
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
3-180 |
1.94e-52 |
|
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: 175.35 E-value: 1.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 3 INELKKYFGFDSFRPGQEEIIQALL-DGEDTLAILPTGTGKSLCYQLTGYLMEGLVIIVSPLLSLMEDQVTQLQKRGekr 81
Cdd:cd18017 1 LNALNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 82 VAAfnSLLSQSERRYVLR--HLSQYKFLFLSPEM-LTNPSLLEHLKKQnIALYVVDEAHCVSQWGVDFRPEYQQLGKIRK 158
Cdd:cd18017 78 IPA--CFLGSAQSQNVLDdiKMGKIRVIYVTPEFvSKGLELLQQLRNG-ITLIAIDEAHCVSQWGHDFRSSYRHLGSIRN 154
|
170 180
....*....|....*....|..
gi 488252204 159 LLGNPVTLALTATATDLVARDI 180
Cdd:cd18017 155 RLPNVPIVALTATATPSVRDDI 176
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
4-204 |
2.44e-50 |
|
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: 169.96 E-value: 2.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 4 NELKKYFGFDSFR-PGQEEIIQALLDGE-DTLAILPTGTGKSLCYQLTGYLMEGLVIIVSPLLSLMEDQVTQLQKRgEKR 81
Cdd:cd18014 2 STLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTL-KIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 82 VAAFNSLLSQSERRYVL----RHLSQYKFLFLSPEMLTNPS---LLEHLKKQNIALY-VVDEAHCVSQWGVDFRPEYQQL 153
Cdd:cd18014 81 VDSLNSKLSAQERKRIIadleSEKPQTKFLYITPEMAATSSfqpLLSSLVSRNLLSYlVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488252204 154 GKIRKLLGNPVTLALTATATDLVARDIRHVLFdrppkeIRQSVNRQNISLF 204
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLR------LKKPVAIFKTPCF 205
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
6-197 |
2.47e-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: 170.24 E-value: 2.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 6 LKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLMEGLVIIVSPLLSLMEDQVTQLQKRGEKRVaAF 85
Cdd:cd18015 10 LKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISAT-ML 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 86 NSLLSQSERRYVLRHL----SQYKFLFLSPE-MLTNPSLLEHLKKQN----IALYVVDEAHCVSQWGVDFRPEYQQLGKI 156
Cdd:cd18015 89 NASSSKEHVKWVHAALtdknSELKLLYVTPEkIAKSKRFMSKLEKAYnagrLARIAIDEVHCCSQWGHDFRPDYKKLGIL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488252204 157 RKLLGNPVTLALTATATDLVARDIRHVLFDRPPKEIRQSVN 197
Cdd:cd18015 169 KRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
2-197 |
4.47e-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: 158.84 E-value: 4.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 2 LINELKKYFGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGYLMEGLVIIVSPLLSLMEDQVTQLQK----- 76
Cdd:cd18016 5 MMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSldipa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 77 ---RGEKRVAAFNSLLSQSERRYVLrhlsqYKFLFLSPEMLTNP----SLLEHLKKQN-IALYVVDEAHCVSQWGVDFRP 148
Cdd:cd18016 85 tylTGDKTDAEATKIYLQLSKKDPI-----IKLLYVTPEKISASnrliSTLENLYERKlLARFVIDEAHCVSQWGHDFRP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488252204 149 EYQQLGKIRKLLGNPVTLALTATATDLVARDIRHVLFDRPPKEIRQSVN 197
Cdd:cd18016 160 DYKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
198-326 |
1.04e-41 |
|
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: 144.66 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 198 RQNISLFVRK--------TQQKEQELEHFmeraQGAAIIYCATKKEVERLYHLFRER-FTVGYYHGGLDAAQRRQLQQQF 268
Cdd:cd18794 1 RPNLFYSVRPkdkkdeklDLLKRIKVEHL----GGSGIIYCLSRKECEQVAARLQSKgISAAAYHAGLEPSDRRDVQRKW 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488252204 269 VKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILFY 326
Cdd:cd18794 77 LRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
16-174 |
4.90e-30 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 114.65 E-value: 4.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 16 RPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLTGY------LMEGLVIIVSPLLSLMEDQVTQLQKRGEKRVAAFNSLL 89
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 90 SQSERRYVLRHLSQYKFLFLSPEMLTnpSLLEHLKK-QNIALYVVDEAHCVSQWGvdFRPEYQQLgkIRKLLGNPVTLAL 168
Cdd:pfam00270 81 GGDSRKEQLEKLKGPDILVGTPGRLL--DLLQERKLlKNLKLLVLDEAHRLLDMG--FGPDLEEI--LRRLPKKRQILLL 154
|
....*.
gi 488252204 169 TATATD 174
Cdd:pfam00270 155 SATLPR 160
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
8-186 |
1.03e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 98.33 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 8 KYFGFDSFRPGQEEIIQALLDGE-DTLAILPTGTGKSLCYQLT--GYLMEGL---VIIVSPLLSLMEDQVTQLQKRGEKR 81
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPalEALKRGKggrVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 82 VAAFNSLLSQSERRYVLRHL--SQYKFLFLSPEMLTNPSLLEHLKKQNIALYVVDEAHCVSQWGvdFRPEYQQLGKirKL 159
Cdd:smart00487 82 GLKVVGLYGGDSKREQLRKLesGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLK--LL 157
|
170 180
....*....|....*....|....*..
gi 488252204 160 LGNPVTLALTATATDLVARDIRHVLFD 186
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLND 184
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
210-315 |
1.15e-23 |
|
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: 95.36 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 210 QKEQELEHFMERAQGA-AIIYCATKKEVERLYHLFRERFTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDK 288
Cdd:pfam00271 1 EKLEALLELLKKERGGkVLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*..
gi 488252204 289 SDIRYVIHYDLPDSLENYVQEIGRAGR 315
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
11-349 |
9.93e-23 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 99.84 E-value: 9.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 11 GFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYqltgylmeGLviivsPLLSlmedqvtQLQKRGEKRVAAfnslL- 89
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAF--------LL-----PLLQ-------RLDPSRPRAPQA----Li 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 90 --------SQSERryVLRHLSQYKFLFLSP-----------EMLTNPS---------LLEHLKKQNIALY-----VVDEA 136
Cdd:COG0513 77 laptrelaLQVAE--ELRKLAKYLGLRVATvyggvsigrqiRALKRGVdivvatpgrLLDLIERGALDLSgvetlVLDEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 137 hcvsqwgvD------FRPEyqqlgkIRKLLGN-PV---TLALTATATDLVARDIRHVLFDrpPKEI---RQSVNRQNIS- 202
Cdd:COG0513 155 --------DrmldmgFIED------IERILKLlPKerqTLLFSATMPPEIRKLAKRYLKN--PVRIevaPENATAETIEq 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 203 --LFVRKtQQKEQELEHFMERAQ-GAAIIYCATKKEVERLYHLFRER-FTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIA 278
Cdd:COG0513 219 ryYLVDK-RDKLELLRRLLRDEDpERAIVFCNTKRGADRLAEKLQKRgISAAALHGDLSQGQRERALDAFRNGKIRVLVA 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488252204 279 TNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILFYqSGDERihYFFNQLSREQRQSFE 349
Cdd:COG0513 298 TDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLV-TPDER--RLLRAIEKLIGQKIE 365
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
192-326 |
2.20e-22 |
|
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: 92.19 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 192 IRQSVnrqnisLFVRKTQQKEQELEHFMERAQ-GAAIIYCATKKEVERLYHLFRER-FTVGYYHGGLDAAQRRQLQQQFV 269
Cdd:cd18787 1 IKQLY------VVVEEEEKKLLLLLLLLEKLKpGKAIIFVNTKKRVDRLAELLEELgIKVAALHGDLSQEERERALKKFR 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488252204 270 KNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILFY 326
Cdd:cd18787 75 SGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
19-324 |
2.64e-22 |
|
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: 100.30 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 19 QEEIIQALLDGEDTLAILPTGTGKSLCYQLtgYLMEGL-------VIIVSPLLSLMEDQVTQLQKRGEK-----RVAAFN 86
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLL--PVLEALledpgatALYLYPTKALARDQLRRLRELAEAlglgvRVATYD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 87 SLLSQSERRYVLRHlSQykFLFLSPEMLtNPSLLEHLKK-----QNIALYVVDEAHCVSqwGVdfrpeyqqLGK-----I 156
Cdd:COG1205 139 GDTPPEERRWIREH-PD--IVLTNPDML-HYGLLPHHTRwarffRNLRYVVIDEAHTYR--GV--------FGShvanvL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 157 RKL-------------------LGNPVTLA--LTATATDLVARD-----IRHVLFDRPP---KEIRQSVNRQNISLfvrk 207
Cdd:COG1205 205 RRLrricrhygsdpqfilasatIGNPAEHAerLTGRPVTVVDEDgsprgERTFVLWNPPlvdDGIRRSALAEAARL---- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 208 tqqkeqeLEHFMERaqGA-AIIYCATKKEVERLYHLFRERFTVGY-------YHGGLDAAQRRQLQQQFVKNQLQFLIAT 279
Cdd:COG1205 281 -------LADLVRE--GLrTLVFTRSRRGAELLARYARRALREPDladrvaaYRAGYLPEERREIERGLRSGELLGVVST 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 488252204 280 NAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAIL 324
Cdd:COG1205 352 NALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
237-316 |
1.08e-20 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 86.11 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 237 ERLYHLFRER-FTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGR 315
Cdd:smart00490 1 EELAELLKELgIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
.
gi 488252204 316 D 316
Cdd:smart00490 81 A 81
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
10-362 |
7.88e-18 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 85.26 E-value: 7.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 10 FGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSL-----CYQLTGY-LMEGLVIIVSPLLSLMEdqvtQLQKRgekrVA 83
Cdd:PTZ00424 46 YGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTAtfviaALQLIDYdLNACQALILAPTRELAQ----QIQKV----VL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 84 AFNSLLS---------QSERRYVLRHLSQYKFLFLSPEMLTNPSLLEHLKKQNIALYVVDEAHCVSQWGvdFRpeyQQLG 154
Cdd:PTZ00424 118 ALGDYLKvrchacvggTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRG--FK---GQIY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 155 KIRKLLGNPVTLAL-TATATDlvarDIRHVL--FDRPPKEI---RQSVNRQNISLFVRKTQQKEQELEHFMERAQG---- 224
Cdd:PTZ00424 193 DVFKKLPPDVQVALfSATMPN----EILELTtkFMRDPKRIlvkKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETltit 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 225 AAIIYCATKKEVERLYHLFRER-FTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSL 303
Cdd:PTZ00424 269 QAIIYCNTRRKVDYLTKKMHERdFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488252204 304 ENYVQEIGRAGRDQEESAAILFYQSGDerihyffnqlsREQRQSFELYLEYATEQAPFD 362
Cdd:PTZ00424 349 ENYIHRIGRSGRFGRKGVAINFVTPDD-----------IEQLKEIERHYNTQIEEMPME 396
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
29-171 |
7.78e-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: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 29 GEDTLAILPTGTGKSLCYQLTGYLM----EGLVIIVSPLLSLMEDQVTQLQKRGEK--RVAAFNSlLSQSERRYVLRhLS 102
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRELFGPgiRVAVLVG-GSSAEEREKNK-LG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 103 QYKFLFLSPEMLTNPSL-LEHLKKQNIALYVVDEAHCVSQWGVDFRPEYQQLgkIRKLLGNPVTLALTAT 171
Cdd:cd00046 79 DADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALLIDSRGALILDLAV--RKAGLKNAQVILLSAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
16-404 |
2.15e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.53 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 16 RPGQEEIIQALL-----DGEDTLAILPTGTGKSL--CYQLTGYLMEGLVIIVSPLLSLMEdqvtQLQKRGEKRVAAFNSL 88
Cdd:COG1061 82 RPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlaLALAAELLRGKRVLVLVPRRELLE----QWAEELRRFLGDPLAG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 89 LSQSERryvlrhlsQYKFLFLSPEMLTNPSLLEHLKKqNIALYVVDEAHCVSqwgvdfRPEYQqlgKIRKLLGNPVTLAL 168
Cdd:COG1061 158 GGKKDS--------DAPITVATYQSLARRAHLDELGD-RFGLVIIDEAHHAG------APSYR---RILEAFPAAYRLGL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 169 TATATDLVARDIRHVLFDRPPKEIR-----------------------------QSVNRQNISLFVRKTQQKEQELEHFM 219
Cdd:COG1061 220 TATPFRSDGREILLFLFDGIVYEYSlkeaiedgylappeyygirvdltderaeyDALSERLREALAADAERKDKILRELL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 220 ER--AQGAAIIYCATKKEVERLYHLFRER-FTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIH 296
Cdd:COG1061 300 REhpDDRKTLVFCSSVDHAEALAELLNEAgIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 297 YDLPDSLENYVQEIGRAGRDQE--ESAAIL-FYQSGDERIHYFFNQLSREQRQSFELYLEYATEQAPFDELQKKWMELIQ 373
Cdd:COG1061 380 LRPTGSPREFIQRLGRGLRPAPgkEDALVYdFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKG 459
|
410 420 430
....*....|....*....|....*....|.
gi 488252204 374 QSEKPENWVERLKHQEKEKEFRLQQMLRYIN 404
Cdd:COG1061 460 ELEEELLEELELLEDALLLVLAELLLLELLA 490
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
11-333 |
9.40e-15 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 76.43 E-value: 9.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 11 GFDSFRPGQEEIIQALLDGEDTLAILPTGTGKS------LCYQLTGYLMEGLVIIVSPLLSLMEdQVTQLQKRGEKRVAA 84
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTaafslpLLHNLDPELKAPQILVLAPTRELAV-QVAEAMTDFSKHMRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 85 FNSLLSQSERRY--VLRHLSQykflflSPEML--TNPSLLEHLKK-----QNIALYVVDEAHCVSQWGvdFRPEYQQLgk 155
Cdd:PRK11634 104 VNVVALYGGQRYdvQLRALRQ------GPQIVvgTPGRLLDHLKRgtldlSKLSGLVLDEADEMLRMG--FIEDVETI-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 156 IRKLLGNPVTLALTATATDLVARDIRHvlFDRPPKEIR-QS--VNRQNIS--LFVRKTQQKEQELEHFMERAQ-GAAIIY 229
Cdd:PRK11634 174 MAQIPEGHQTALFSATMPEAIRRITRR--FMKEPQEVRiQSsvTTRPDISqsYWTVWGMRKNEALVRFLEAEDfDAAIIF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 230 CATKKE-VERLYHLFRERFTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQ 308
Cdd:PRK11634 252 VRTKNAtLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVH 331
|
330 340
....*....|....*....|....*
gi 488252204 309 EIGRAGRDQEESAAILFYQSGDERI 333
Cdd:PRK11634 332 RIGRTGRAGRAGRALLFVENRERRL 356
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
269-326 |
1.37e-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: 63.11 E-value: 1.37e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488252204 269 VKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRD-QEESAAILFY 326
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGgKDEGEVILFV 77
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
2-330 |
1.85e-12 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 69.17 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 2 LINELKKY---FGFDSFRPGQEEIIQALLDGEDTLAILPTGTGK------SLCYQLTG-------YLMEGLVIIVSPLLS 65
Cdd:PRK01297 94 LAPELMHAihdLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKtaafliSIINQLLQtpppkerYMGEPRALIIAPTRE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 66 L---MEDQVTQLQKRGEKRVAA------FNSLLSQSERRYVlrhlsqyKFLFLSPEMLTNPSLLEHLKKQNIALYVVDEA 136
Cdd:PRK01297 174 LvvqIAKDAAALTKYTGLNVMTfvggmdFDKQLKQLEARFC-------DILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 137 HCVSQWGvdFRPEYQQLGKIRKLLGNPVTLALTATATDLVARDIRHVLFDRPPKEIR-QSVNRQNIS--LFVRKTQQKEQ 213
Cdd:PRK01297 247 DRMLDMG--FIPQVRQIIRQTPRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEpENVASDTVEqhVYAVAGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 214 ELEHFM-ERAQGAAIIYCATKKEVERLY-HLFRERFTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDI 291
Cdd:PRK01297 325 LLYNLVtQNPWERVMVFANRKDEVRRIEeRLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350
....*....|....*....|....*....|....*....
gi 488252204 292 RYVIHYDLPDSLENYVQEIGRAGRDQEESAAILFYQSGD 330
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
11-342 |
1.03e-11 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 66.74 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 11 GFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQL------TGYLMEG-------LVIIVSP---LLSLMEDQVTQL 74
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVpiisrcCTIRSGHpseqrnpLAMVLTPtreLCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 75 QKRgekrvAAFNSLL---SQSERRYVLRHLSQYKFLFLSPEMLTNpSLLEH-LKKQNIALYVVDEAHCVSQWGvdFRpey 150
Cdd:PLN00206 220 GKG-----LPFKTALvvgGDAMPQQLYRIQQGVELIVGTPGRLID-LLSKHdIELDNVSVLVLDEVDCMLERG--FR--- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 151 QQLGKIRKLLGNPVTLALTATATDLV-------ARDIRHVLF---DRPPKEIRQsvnrqnISLFVrKTQQKEQEL----- 215
Cdd:PLN00206 289 DQVMQIFQALSQPQVLLFSATVSPEVekfasslAKDIILISIgnpNRPNKAVKQ------LAIWV-ETKQKKQKLfdilk 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 216 --EHFMEraqgAAIIYCATKKEVErlyhLFRERFTVGY------YHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGID 287
Cdd:PLN00206 362 skQHFKP----PAVVFVSSRLGAD----LLANAITVVTglkalsIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVD 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 488252204 288 KSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILFYQSGDERIHYFFNQLSR 342
Cdd:PLN00206 434 LLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLK 488
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
198-325 |
1.62e-11 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 66.51 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 198 RQNIslFVRKTQQKEQELEHFMERAQGA-AIIYCATKKEVERLYH-LFRERFTVGYYHGGLDAAQRRQLQQQFVKNQLQF 275
Cdd:PRK04537 233 RQRI--YFPADEEKQTLLLGLLSRSEGArTMVFVNTKAFVERVARtLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEI 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488252204 276 LIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILF 325
Cdd:PRK04537 311 LVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
19-137 |
7.30e-11 |
|
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: 61.06 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 19 QEEIIQALLDGEDTLAILPTGTGKSLCYQLTgyLMEGL-------VIIVSPLLSLMEDQVTQLQKRGEK-----RVAAFN 86
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLP--ILEALlrdpgsrALYLYPTKALAQDQLRSLRELLEQlglgiRVATYD 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488252204 87 SLLSQSERRYVLRHLSQYkflflspeMLTNPSLLEH--LKK--------QNIALYVVDEAH 137
Cdd:cd17923 83 GDTPREERRAIIRNPPRI--------LLTNPDMLHYalLPHhdrwarflRNLRYVVLDEAH 135
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
227-324 |
1.35e-10 |
|
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: 59.19 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 227 IIYCATKKEVERLYHLFRERF--------TVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYD 298
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLveegplasKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*.
gi 488252204 299 LPDSLENYVQEIGRAGRDQEESAAIL 324
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
371-431 |
5.52e-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: 54.99 E-value: 5.52e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488252204 371 LIQQSEKPEnwverlkhQEKEKEF-RLQQMLRY-INEENCRRKFILAYFGEKLSEKPQNCCDI 431
Cdd:pfam16124 10 LIEQSEADE--------ERKEVELqKLQAMVAYcENTTDCRRKQLLRYFGEEFDSEPCGNCDN 64
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
27-368 |
1.02e-09 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 60.56 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 27 LDGEDTLAILPTGTGKSLCYQLTG--------YLMEG---LVIIVSPLLSLME---DQVTQLQKRGEKRVAAFNSLLSQS 92
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPTRELAEqirEQCNKFGASSKIRNTVAYGGVPKR 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 93 ERRYVLRHlsQYKFLFLSPEMLTNpsLLE----HLKKqnIALYVVDEAHCVSQWGvdFRPEyqqlgkIRKLLG----NPV 164
Cdd:PTZ00110 245 GQIYALRR--GVEILIACPGRLID--FLEsnvtNLRR--VTYLVLDEADRMLDMG--FEPQ------IRKIVSqirpDRQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 165 TLALTAT--------ATDLVARDIRHV----LFDRPPKEIRQSVnrqnislFVRKTQQKEQELEHFMER---AQGAAIIY 229
Cdd:PTZ00110 311 TLMWSATwpkevqslARDLCKEEPVHVnvgsLDLTACHNIKQEV-------FVVEEHEKRGKLKMLLQRimrDGDKILIF 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 230 CATKKEVERLYHLFR-ERFTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLENYVQ 308
Cdd:PTZ00110 384 VETKKGADFLTKELRlDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVH 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 309 EIGRAGRDQEESAAILFYQSGDERIHYFFNQLSREQRQSFELYLEYATEQAPFDELQKKW 368
Cdd:PTZ00110 464 RIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRW 523
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
2-315 |
1.05e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 60.68 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 2 LINELKKyFGFDSFRPGQEEIIQA-LLDGEDTLAILPTGTGKSLCYQL---TGYLMEGLVIIVSPLLSLMEdqvtqlQKR 77
Cdd:COG1204 11 VIEFLKE-RGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELailKALLNGGKALYIVPLRALAS------EKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 78 GEkrvaaFNSLLSQSERRYVL---------RHLSQYKFLFLSPEML-----TNPSLLEhlkkqNIALYVVDEAHCVsqwG 143
Cdd:COG1204 84 RE-----FKRDFEELGIKVGVstgdydsddEWLGRYDILVATPEKLdsllrNGPSWLR-----DVDLVVVDEAHLI---D 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 144 VDFR-PEYQQ-LGKIRKLLGNPVTLALTATA--TDLVAR--DIRHVLFDRPPKEIRQSVNRQNISLFVRKTQQKEQELEH 217
Cdd:COG1204 151 DESRgPTLEVlLARLRRLNPEAQIVALSATIgnAEEIAEwlDAELVKSDWRPVPLNEGVLYDGVLRFDDGSRRSKDPTLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 218 FMERA---QGAAIIYCATKKEVERL-------------------YHLFRERFT-------------------VGYYHGGL 256
Cdd:COG1204 231 LALDLleeGGQVLVFVSSRRDAESLakkladelkrrltpeereeLEELAEELLevseethtnekladclekgVAFHHAGL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488252204 257 DAAQRRQLQQQFVKNQLQFLIATNAFGMGIDK-------SDIRYVIHYDLPdSLEnYVQEIGRAGR 315
Cdd:COG1204 311 PSELRRLVEDAFREGLIKVLVATPTLAAGVNLparrviiRDTKRGGMVPIP-VLE-FKQMAGRAGR 374
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
226-325 |
2.36e-08 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 56.13 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 226 AIIYCATKKEVERLY-HLFRERFTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLE 304
Cdd:PRK04837 258 AIIFANTKHRCEEIWgHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCE 337
|
90 100
....*....|....*....|.
gi 488252204 305 NYVQEIGRAGRDQEESAAILF 325
Cdd:PRK04837 338 DYVHRIGRTGRAGASGHSISL 358
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
11-315 |
3.20e-08 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 55.58 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 11 GFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCYQLtgylmeglviivsPLLSLMEDQvtQLQKRGEKRVAAF----- 85
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTL-------------PLLQHLITR--QPHAKGRRPVRALiltpt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 86 NSLLSQ------SERRYV-LRHLSQYKFLFLSPEML----------TNPSLLEHLKKQN------IALYVVDEAHCVSQW 142
Cdd:PRK10590 85 RELAAQigenvrDYSKYLnIRSLVVFGGVSINPQMMklrggvdvlvATPGRLLDLEHQNavkldqVEILVLDEADRMLDM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 143 GV--DFR-------PEYQQL-----------GKIRKLLGNPVTLAltatatdlVARDirhvlfDRPPKEIRQSVNrqnis 202
Cdd:PRK10590 165 GFihDIRrvlaklpAKRQNLlfsatfsddikALAEKLLHNPLEIE--------VARR------NTASEQVTQHVH----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 203 lFVRKtqQKEQELEHFM--ERAQGAAIIYCATKKEVERLY-HLFRERFTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIAT 279
Cdd:PRK10590 226 -FVDK--KRKRELLSQMigKGNWQQVLVFTRTKHGANHLAeQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVAT 302
|
330 340 350
....*....|....*....|....*....|....*.
gi 488252204 280 NAFGMGIDKSDIRYVIHYDLPDSLENYVQEIGRAGR 315
Cdd:PRK10590 303 DIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
29-175 |
7.36e-08 |
|
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: 51.82 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 29 GEDTLAILPTGTGKSL------CYQLTGYLMEGL-VIIVSPLLSLMEDQVTQLQKRGEK-----RVAAFNSLLSQSERRY 96
Cdd:cd17922 1 GRNVLIAAPTGSGKTEaaflpaLSSLADEPEKGVqVLYISPLKALINDQERRLEEPLDEidleiPVAVRHGDTSQSEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 97 VLRHLSQykFLFLSPE----MLTNPSLLEHLKkqNIALYVVDEAHCV--SQWGVDFRpeyQQLGKIRKLLG-NPVTLALT 169
Cdd:cd17922 81 QLKNPPG--ILITTPEslelLLVNKKLRELFA--GLRYVVVDEIHALlgSKRGVQLE---LLLERLRKLTGrPLRRIGLS 153
|
....*.
gi 488252204 170 ATATDL 175
Cdd:cd17922 154 ATLGNL 159
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
19-333 |
3.14e-07 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 52.64 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 19 QEEIIQALLDGEDTLAILPTGTGKSLCYQLtgylmeglviivsPLLSLMEDqvTQLQKRGEKRV---AAFNSLLSQSERR 95
Cdd:PRK11192 28 QAEAIPPALDGRDVLGSAPTGTGKTAAFLL-------------PALQHLLD--FPRRKSGPPRIlilTPTRELAMQVADQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 96 yvLRHLSQYKFLFLS-----------PEML---------TNPSLLEHLKKQN-----IALYVVDEAHCVSQWGvdFRPEY 150
Cdd:PRK11192 93 --ARELAKHTHLDIAtitggvaymnhAEVFsenqdivvaTPGRLLQYIKEENfdcraVETLILDEADRMLDMG--FAQDI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 151 QQLG---KIRKLlgnpvTLALTAT-ATDLVARDIRHVLFD----------RPPKEIRQSVNRQN-----ISLFVRKTQQK 211
Cdd:PRK11192 169 ETIAaetRWRKQ-----TLLFSATlEGDAVQDFAERLLNDpveveaepsrRERKKIHQWYYRADdlehkTALLCHLLKQP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 212 EqelehfMERAqgaaIIYCATKKEVERLYHLFRER-FTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSD 290
Cdd:PRK11192 244 E------VTRS----IVFVRTRERVHELAGWLRKAgINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDD 313
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 488252204 291 IRYVIHYDLPDSLENYVQEIGRAGRDQEESAAILFYQSGDERI 333
Cdd:PRK11192 314 VSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLL 356
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
14-171 |
9.02e-07 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 48.87 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 14 SFRPGQEEIIQA-LLDGEDTLAILPTGTGKSLCYQLTG--YLMEG-LVIIVSPLLSLMEDQVTQLQKRGEK--RVAafns 87
Cdd:cd18028 1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMvnTLLEGgKALYLVPLRALASEKYEEFKKLEEIglKVG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 88 lLSQSERRYVLRHLSQYKFLFLSPEMLTnpSLLEHLKK--QNIALYVVDEAHCVSQWGVDFRPEYqQLGKIRKLLGNPVT 165
Cdd:cd18028 77 -ISTGDYDEDDEWLGDYDIIVATYEKFD--SLLRHSPSwlRDVGVVVVDEIHLISDEERGPTLES-IVARLRRLNPNTQI 152
|
....*.
gi 488252204 166 LALTAT 171
Cdd:cd18028 153 IGLSAT 158
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
208-315 |
1.13e-06 |
|
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: 48.32 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 208 TQQKEQELEHFMERAQGAAIIYCATKKEVERLYhlfRERFTVGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGID 287
Cdd:cd18795 28 DSDIIVLLKIETVSEGKPVLVFCSSRKECEKTA---KDLAGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVN 104
|
90 100 110
....*....|....*....|....*....|....*..
gi 488252204 288 --------KSDIRY-VIHYDLPDSLEnYVQEIGRAGR 315
Cdd:cd18795 105 lpartviiKGTQRYdGKGYRELSPLE-YLQMIGRAGR 140
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
14-180 |
2.20e-06 |
|
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: 48.03 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 14 SFRPGQEEII-QALLDGEDTLAILPTGTGKSLCYQLTGYL----MEGLVIIVSPLLSLMEDQVTQLQKR---GEKRVAAF 85
Cdd:cd17921 1 LLNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRalatSGGKAVYIAPTRALVNQKEADLRERfgpLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 86 NSllsqsERRYVLRHLSQYKFLFLSPEMLTNPSL-LEHLKKQNIALYVVDEAHCVSQwgvdfrPEY-----QQLGKIRKL 159
Cdd:cd17921 81 TG-----DPSVNKLLLAEADILVATPEKLDLLLRnGGERLIQDVRLVVVDEAHLIGD------GERgvvleLLLSRLLRI 149
|
170 180
....*....|....*....|.
gi 488252204 160 LGNPVTLALTATATDlvARDI 180
Cdd:cd17921 150 NKNARFVGLSATLPN--AEDL 168
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
14-181 |
4.66e-06 |
|
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: 47.43 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 14 SFRPGQEEIIQALLDGEDTLAILPTGTGKSLcyqLTGYLME-----------GLVIIVSPLLSLMEDQVTQLQKRGEK-- 80
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTF---VAVLICEhhlkkfpagrkGKVVFLANKVPLVEQQKEVFRKHFERpg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 81 -RVAAFNSLLSQSERRYVLrhLSQYKFLFLSPEMLTNpSLL--EHLKKQNIALYVVDEAHCVSQWGV----DFRPEYQQL 153
Cdd:cd17927 79 yKVTGLSGDTSENVSVEQI--VESSDVIIVTPQILVN-DLKsgTIVSLSDFSLLVFDECHNTTKNHPyneiMFRYLDQKL 155
|
170 180
....*....|....*....|....*...
gi 488252204 154 GKIRKllgNPVTLALTATATDLVARDIR 181
Cdd:cd17927 156 GSSGP---LPQILGLTASPGVGGAKNTE 180
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
2-46 |
4.32e-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: 4.32e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 488252204 2 LINELKKYfGFDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCY 46
Cdd:cd00268 1 LLKALKKL-GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAF 44
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
232-315 |
2.37e-04 |
|
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: 41.48 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 232 TKKEVERLYHLFRERFT-------VGYYHGGLDAAQRRQLQQQFVKNQLQFLIATNAFGMGIDKSDIRYVIHYDLPDSLE 304
Cdd:cd18796 47 TRSQAERLAQRLRELCPdrvppdfIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVA 126
|
90
....*....|.
gi 488252204 305 NYVQEIGRAGR 315
Cdd:cd18796 127 RLLQRLGRSGH 137
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
14-171 |
4.28e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 40.73 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 14 SFRPGQEEIIQALLDGEDT-----LAILPTGTGKSLCY-QLTGYLMEGL----VIIVSPLLSLMEDQVTQLQKRGEKrvA 83
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKNgqkrgLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPN--Y 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 84 AFNSLLSQSERRyvLRHLSQYKFLFLSPEMLTNPSLL--EHLKKQNIALYVVDEAHCVSqwgvdfRPEYQQlgkIRKLLG 161
Cdd:pfam04851 81 VEIGEIISGDKK--DESVDDNKIVVTTIQSLYKALELasLELLPDFFDVIIIDEAHRSG------ASSYRN---ILEYFK 149
|
170
....*....|
gi 488252204 162 NPVTLALTAT 171
Cdd:pfam04851 150 PAFLLGLTAT 159
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
15-171 |
1.03e-03 |
|
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: 39.60 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 15 FRPGQEEIIQALLDGE-DTLAI--LPTGTGKSLC-YQLTGYLMEGLVIIVSPLLSLMED---------QVTQLQKRGEKR 81
Cdd:cd17926 1 LRPYQEEALEAWLAHKnNRRGIlvLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQwkerfedflGDSSIGLIGGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 82 VAAFNSL-----LSQSerryVLRHLSQYKFLFLSPEMLtnpsllehlkkqnialyVVDEAH--CVSQWgvdfrpeyqqlG 154
Cdd:cd17926 81 KKDFDDAnvvvaTYQS----LSNLAEEEKDLFDQFGLL-----------------IVDEAHhlPAKTF-----------S 128
|
170
....*....|....*..
gi 488252204 155 KIRKLLGNPVTLALTAT 171
Cdd:cd17926 129 EILKELNAKYRLGLTAT 145
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
7-185 |
1.61e-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: 39.62 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 7 KKYFGFDSFRPgQEEIIQALLDGEDTLAILPTGTGKS---LCYQLTGYLMEGLVIIVSPLLSLMEDQVTQLQKRGEK--- 80
Cdd:cd17924 11 KKKTGFPPWGA-QRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSLYLASKGKRSYLIFPTKSLVKQAYERLSKYAEKagv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 81 --RVAAFNSLLSQSERRYVLRHLS--QYKFL-----FLSPEMltnpsllEHLKKQNIALYVVDEAHCV--SQWGVDfrpe 149
Cdd:cd17924 90 evKILVYHSRLKKKEKEELLEKIEkgDFDILvttnqFLSKNF-------DLLSNKKFDFVFVDDVDAVlkSSKNID---- 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 488252204 150 yqqlgKIRKLLGNPVTLALTATATdlvARDIRHVLF 185
Cdd:cd17924 159 -----RLLKLLGFGQLVVSSATGR---PRGIRPLLF 186
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
12-167 |
2.33e-03 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 39.16 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 12 FDSFRPGQEEIIQALLDGEDTLAI-LPTGTGKSLCYQLTgyLM-------EGLVIIVSPLLSL----MEDQVTQLQKRGE 79
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVgAPTGSGKTVCAELA--LLrhwrqnpKGRAVYIAPMQELvdarYKDWRAKFGPLLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 80 KRVAAFNSLLSQSerryvLRHLSQYKFLFLSPEMLTNPSLLEHLKK--QNIALYVVDEAHCVsqwGVDFRPEYQ------ 151
Cdd:cd18021 79 KKVVKLTGETSTD-----LKLLAKSDVILATPEQWDVLSRRWKQRKnvQSVELFIADELHLI---GGENGPVYEvvvsrm 150
|
170 180
....*....|....*....|...
gi 488252204 152 -----QLGK-IRKL-LGNPVTLA 167
Cdd:cd18021 151 ryissQLEKpIRIVgLSSSLANA 173
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
19-171 |
2.69e-03 |
|
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: 38.65 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 19 QEEIIQALLDGEDTLAILPTGTGKSLC------YQLTGYlmEGLVIIVSPLLSLMEDQVTQLQK--RGEKRVAAFNSLLS 90
Cdd:cd18035 6 YQVLIAAVALNGNTLIVLPTGLGKTIIailvaaDRLTKK--GGKVLILAPSRPLVEQHAENLKRvlNIPDKITSLTGEVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 91 QSERRYVLRhlsQYKFLFLSPEMLTNPSLLEHLKKQNIALYVVDEAH-CVSQWGVDFRPEyqqlgKIRKLLGNPVTLALT 169
Cdd:cd18035 84 PEERAERWD---ASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHhAVGNYAYVYIAH-----RYKREANNPLILGLT 155
|
..
gi 488252204 170 AT 171
Cdd:cd18035 156 AS 157
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
16-179 |
2.88e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) 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: 350794 [Multi-domain] Cd Length: 204 Bit Score: 39.00 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 16 RPGQEEIIQALLDGEDTLAILPTGTGKSLC--YQLTGYLME-------GLVIIVSPLLSLMEDQVTQLQK--RGEKRVAA 84
Cdd:cd18036 4 RNYQLELVLPALRGKNTIICAPTGSGKTRVavYICRHHLEKrrsagekGRVVVLVNKVPLVEQQLEKFFKyfRKGYKVTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 85 FNSllSQSERRYVLRHLSQYKFLFLSPEMLTNpSLL-----EHLKKQNIALYVVDEAHCVSQWGV----DFRPEYQQLGK 155
Cdd:cd18036 84 LSG--DSSHKVSFGQIVKASDVIICTPQILIN-NLLsgreeERVYLSDFSLLIFDECHHTQKEHPynkiMRMYLDKKLSS 160
|
170 180
....*....|....*....|....
gi 488252204 156 IRKLlgnPVTLALTATATDLVARD 179
Cdd:cd18036 161 QGPL---PQILGLTASPGVGGARS 181
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
6-46 |
3.14e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 39.91 E-value: 3.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 488252204 6 LKKYFGFDSFRPGQ----EEIIQALLDGEDTLAILPTGTGKSLCY 46
Cdd:COG1199 6 LALAFPGFEPRPGQremaEAVARALAEGRHLLIEAGTGTGKTLAY 50
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
12-137 |
5.14e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 39.48 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 12 FDSFRPGQEEIIQALLDGEDTLAILPTGTGKSLCY------QLTGYLMEG------LVIIVSPLLSLMED---------- 69
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAflaiidELFRLGREGeledkvYCLYVSPLRALNNDihrnleeplt 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 70 QVTQL-QKRGEK----RVAAFNSLLSQSERRYVLR---HLsqykfLFLSPE----MLTNPSLLEHLKkqNIALYVVDEAH 137
Cdd:PRK13767 110 EIREIaKERGEElpeiRVAIRTGDTSSYEKQKMLKkppHI-----LITTPEslaiLLNSPKFREKLR--TVKWVIVDEIH 182
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
3-344 |
7.43e-03 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 39.03 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 3 INELKKYFGFDSFRPGQEEIIQA-LLDGEDTLAILPTGTGKSLCYQLT---GYLMEG--LVIIVsPLLSLMEDQVTQLQ- 75
Cdd:PRK00254 12 IKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVmvnKLLREGgkAVYLV-PLKALAEEKYREFKd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 76 --KRGEKRVAAFNSLLSQSErryvlrHLSQYKFLFLSPEMLTnpSLLEHLKK--QNIALYVVDEAHCVSQWGVDFRPEY- 150
Cdd:PRK00254 91 weKLGLRVAMTTGDYDSTDE------WLGKYDIIIATAEKFD--SLLRHGSSwiKDVKLVVADEIHLIGSYDRGATLEMi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 151 --QQLGKIRKL-----LGNPVTLALTATAtDLVARDIRHV-----------LF------DRPPKE----IRQSVNRQNIS 202
Cdd:PRK00254 163 ltHMLGRAQILglsatVGNAEELAEWLNA-ELVVSDWRPVklrkgvfyqgfLFwedgkiERFPNSweslVYDAVKKGKGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 203 L-FV---RKTQQKEQELEHFMERAqgaaiiycATKKEVERLYHLFRE--------------RFTVGYYHGGLDAAQRRQL 264
Cdd:PRK00254 242 LvFVntrRSAEKEALELAKKIKRF--------LTKPELRALKELADSleenptneklkkalRGGVAFHHAGLGRTERVLI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 265 QQQFVKNQLQFLIATNAFGMGIDKSDIRYVIH----------YDLPdSLEnYVQEIGRAGRDQ--EESAAILFYQSGDER 332
Cdd:PRK00254 314 EDAFREGLIKVITATPTLSAGINLPAFRVIIRdtkrysnfgwEDIP-VLE-IQQMMGRAGRPKydEVGEAIIVATTEEPS 391
|
410 420
....*....|....*....|..
gi 488252204 333 I---HY-------FFNQLSREQ 344
Cdd:PRK00254 392 KlmeRYifgkpekLFSMLSNES 413
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
16-183 |
9.98e-03 |
|
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: 36.77 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 16 RPGQEEIIQALLD----GED-TLAILPTGTGK-----SLCYQLTGYLMEGLVIIVSPllslMEDQVTQLQKrgekrvaAF 85
Cdd:cd18032 2 RYYQQEAIEALEEarekGQRrALLVMATGTGKtytaaFLIKRLLEANRKKRILFLAH----REELLEQAER-------SF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488252204 86 NSLLSQSERRYVL---RHLSQYKFLFLSPEMLTNPSLLEHLKKQNIALYVVDEAHcvsqwgvdfRPEYQQLGKIRKLLGN 162
Cdd:cd18032 71 KEVLPDGSFGNLKggkKKPDDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAH---------HAIASSYRKILEYFEP 141
|
170 180
....*....|....*....|.
gi 488252204 163 PVTLALTATATDLVARDIRHV 183
Cdd:cd18032 142 AFLLGLTATPERTDGLDTYEL 162
|
|
| |
