|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
8-480 |
1.23e-169 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 486.57 E-value: 1.23e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 8 KTLFGISAFRGSQENIITRTMEGKHSLVIMPTGMGKSVCYQIPALLSEGLTIVISPLIALMQDQVDKLKRFGIDAEFVNS 87
Cdd:COG0514 10 KRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIRAAFLNS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 88 SLSAEERVLRYENLKQGKYKILYVSPERFRKSAFLEIFQNRKVSLLAVDEAHCVSQWGHDFRPDYSKISEFRKILKFPtt 167
Cdd:COG0514 90 SLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRERLPNVpv 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 168 maltatatKEIRSDILRQIGIseSETEIFDEGICRPNLYLEARSFPdPVSKRKEILSLLKgERKN--TIVYFNLIKNLES 245
Cdd:COG0514 170 laltatatPRVRADIAEQLGL--EDPRVFVGSFDRPNLRLEVVPKP-PDDKLAQLLDFLK-EHPGgsGIVYCLSRKKVEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 246 FGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPDIRRVIHAELPSSLESYYQEIGRAGRDG 325
Cdd:COG0514 246 LAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 326 EPSECLLFYNQDDLAVLMDFIEWQNPDsaffsrvyqtmkhtgealsslsyedlqarvvhknrgdhrlqtvlnlfdrhgvt 405
Cdd:COG0514 326 LPAEALLLYGPEDVAIQRFFIEQSPPD----------------------------------------------------- 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1614194638 406 sgetergnlrlrnilpetlsdpkllEDKKKAAQNRLYKMLMYLKSEVCRREFVYEYFDAKF-TRCDNCDICNGSPD 480
Cdd:COG0514 353 -------------------------EERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELaEPCGNCDNCLGPPE 403
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
11-479 |
5.72e-122 |
|
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: 368.63 E-value: 5.72e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 11 FGISAFRGSQENIITRTMEGKHSLVIMPTGMGKSVCYQIPALLSEGLTIVISPLIALMQDQVDKLKRFGIDAEFVNSSLS 90
Cdd:TIGR01389 9 FGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAAYLNSTLS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 91 AEERVLRYENLKQGKYKILYVSPERFRKSAFLEIFQNRKVSLLAVDEAHCVSQWGHDFRPDYSKISEFRKILKFPTTMAL 170
Cdd:TIGR01389 89 AKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFPQVPRIAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 171 TATATKEIRSDILRQIGIseSETEIFDEGICRPNLYLEA-RSFpdpvSKRKEILSLLKGER-KNTIVYFNLIKNLESFGE 248
Cdd:TIGR01389 169 TATADAETRQDIRELLRL--ADANEFITSFDRPNLRFSVvKKN----NKQKFLLDYLKKHRgQSGIIYASSRKKVEELAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 249 ALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPDIRRVIHAELPSSLESYYQEIGRAGRDGEPS 328
Cdd:TIGR01389 243 RLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 329 ECLLFYNQDDLAVLMDFIEWQNPDsaffsrvyqtmkhtgealsslsyedlqarvvhknrgdhrlqtvlnlfdrhgvtsge 408
Cdd:TIGR01389 323 EAILLYSPADIALLKRRIEQSEAD-------------------------------------------------------- 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1614194638 409 tergnlrlrnilpetlsdpkllEDKKKAAQNRLYKMLMYLKSEVCRREFVYEYF-DAKFTRCDNCDICNGSP 479
Cdd:TIGR01389 347 ----------------------DDYKQIEREKLRAMIAYCETQTCRRAYILRYFgENEVEPCGNCDNCLDPP 396
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
8-475 |
1.71e-113 |
|
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: 342.91 E-value: 1.71e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 8 KTLFGISAFRGSQENIITRTMEGKHSLVIMPTGMGKSVCYQIPALLSEGLTIVISPLIALMQDQVDKLKRFGIDAEFVNS 87
Cdd:TIGR00614 4 KKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFLNS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 88 SLSAEERVLRYENLKQGKYKILYVSPERFRKS-AFLEIFQNRK-VSLLAVDEAHCVSQWGHDFRPDYSKISEFRKilKFP 165
Cdd:TIGR00614 84 AQTKEQQLNVLTDLKDGKIKLLYVTPEKISASnRLLQTLEERKgITLIAVDEAHCISQWGHDFRPDYKALGSLKQ--KFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 166 TT--MALTATATKEIRSDILRQIGISESETEI--FDegicRPNLYLE-ARSFPDPVskrKEILSLLKGERK--NTIVYFN 238
Cdd:TIGR00614 162 NVpvMALTATASPSVREDILRQLNLLNPQIFCtsFD----RPNLYYEvRRKTPKIL---EDLLRFIRKEFEgkSGIIYCP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 239 LIKNLESFGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPDIRRVIHAELPSSLESYYQEI 318
Cdd:TIGR00614 235 SRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQES 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 319 GRAGRDGEPSECLLFYNQDDLAvlmdfiewqnpdsaffsrvyqtmkhtgealsslsyedlqarvvhknrgdhrlqtvlnl 398
Cdd:TIGR00614 315 GRAGRDGLPSECHLFYAPADMN---------------------------------------------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 399 fdrhgvtsgetergnlRLRNILPEtlsdpKLLEDKKKAAQNRLYKMLMYLKSEVCRREFVYEYFDAKFTR---------- 468
Cdd:TIGR00614 337 ----------------RLRRLLME-----EPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFNksfcimgtek 395
|
....*...
gi 1614194638 469 -CDNCDIC 475
Cdd:TIGR00614 396 cCDNCCKR 403
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
11-342 |
1.72e-101 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 316.27 E-value: 1.72e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 11 FGISAFRGSQENIITRTMEGKHSLVIMPTGMGKSVCYQIPALLSEGLTIVISPLIALMQDQVDKLKRFGIDAEFVNSSLS 90
Cdd:PRK11057 21 FGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAACLNSTQT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 91 AEERVLRYENLKQGKYKILYVSPERFRKSAFLEIFQNRKVSLLAVDEAHCVSQWGHDFRPDYSKISEFRKilKFPTTMAL 170
Cdd:PRK11057 101 REQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQ--RFPTLPFM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 171 TATATKE--IRSDILRQIGISESETEI--FDegicRPNL-YLEARSFpDPVSkrkEILSLLKGER-KNTIVYFNLIKNLE 244
Cdd:PRK11057 179 ALTATADdtTRQDIVRLLGLNDPLIQIssFD----RPNIrYTLVEKF-KPLD---QLMRYVQEQRgKSGIIYCNSRAKVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 245 SFGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPDIRRVIHAELPSSLESYYQEIGRAGRD 324
Cdd:PRK11057 251 DTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 330
|
330
....*....|....*...
gi 1614194638 325 GEPSECLLFYNQDDLAVL 342
Cdd:PRK11057 331 GLPAEAMLFYDPADMAWL 348
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
8-190 |
6.87e-83 |
|
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: 254.38 E-value: 6.87e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 8 KTLFGISAFRGSQENIITRTMEGKHSLVIMPTGMGKSVCYQIPALLSEGLTIVISPLIALMQDQVDKLKRFGIDAEFVNS 87
Cdd:cd17920 5 KEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAALNS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 88 SLSAEERVLRYENLKQGKYKILYVSPERFRKSAFLEIFQN----RKVSLLAVDEAHCVSQWGHDFRPDYSKISEFRKILK 163
Cdd:cd17920 85 TLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRlperKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLRRALP 164
|
170 180
....*....|....*....|....*..
gi 1614194638 164 FPTTMALTATATKEIRSDILRQIGISE 190
Cdd:cd17920 165 GVPILALTATATPEVREDILKRLGLRN 191
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
8-338 |
1.02e-70 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 244.03 E-value: 1.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 8 KTLFGISAFRGSQENIITRTMEGKHSLVIMPTGMGKSVCYQIPALLSEGLTIVISPLIALMQDQVDKLKRFGIDAEFVNS 87
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 88 SLSAEER--VLRYENLKQGKYKILYVSPERFRKSAFL----EIFQNRkvSLLA---VDEAHCVSQWGHDFRPDYSKISEF 158
Cdd:PLN03137 533 GMEWAEQleILQELSSEYSKYKLLYVTPEKVAKSDSLlrhlENLNSR--GLLArfvIDEAHCVSQWGHDFRPDYQGLGIL 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 159 RKilKFPTT--MALTATATKEIRSDILRQIGISEseTEIFDEGICRPNLYLEArsfpdpVSKRKEILSLL-KGERKNTIV 235
Cdd:PLN03137 611 KQ--KFPNIpvLALTATATASVKEDVVQALGLVN--CVVFRQSFNRPNLWYSV------VPKTKKCLEDIdKFIKENHFD 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 236 YFNLIKNLESfgeaLDLEKIPYRI---------YHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPDIRRVIHAE 306
Cdd:PLN03137 681 ECGIIYCLSR----MDCEKVAERLqefghkaafYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHS 756
|
330 340 350
....*....|....*....|....*....|..
gi 1614194638 307 LPSSLESYYQEIGRAGRDGEPSECLLFYNQDD 338
Cdd:PLN03137 757 LPKSIEGYHQECGRAGRDGQRSSCVLYYSYSD 788
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
10-191 |
5.18e-70 |
|
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: 221.36 E-value: 5.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 10 LFGISAFRGSQENIITRTMEGKHSLVIMPTGMGKSVCYQIPALL----SEGLTIVISPLIALMQDQVDKLKRFgIDAEFV 85
Cdd:cd18018 7 VFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA-IKAAAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 86 NSSLSAEERVLRYENLKQGKYKILYVSPERFRKSAFLEIFQNRK-VSLLAVDEAHCVSQWGHDFRPDYSKISEF-RKILK 163
Cdd:cd18018 86 NSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPpISLLVVDEAHCISEWSHNFRPDYLRLCRVlRELLG 165
|
170 180
....*....|....*....|....*...
gi 1614194638 164 FPTTMALTATATKEIRSDILRQIGISES 191
Cdd:cd18018 166 APPVLALTATATKRVVEDIASHLGIPES 193
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
8-165 |
1.94e-56 |
|
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: 186.42 E-value: 1.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 8 KTLFGISAFRGSQENIITRTMEGKHSLVIMPTGMGKSVCYQIPALLSEGLTIVISPLIALMQDQVDKLKRFGIDAEFVNS 87
Cdd:cd18015 11 KNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATMLNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 88 SLSAEE--RVLRYENLKQGKYKILYVSPERFRKSAFL-----EIFQNRKVSLLAVDEAHCVSQWGHDFRPDYSKISefrk 160
Cdd:cd18015 91 SSSKEHvkWVHAALTDKNSELKLLYVTPEKIAKSKRFmskleKAYNAGRLARIAIDEVHCCSQWGHDFRPDYKKLG---- 166
|
....*..
gi 1614194638 161 ILK--FP 165
Cdd:cd18015 167 ILKrqFP 173
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
8-188 |
1.03e-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: 171.50 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 8 KTLFGISAFRGS-QENIITRTMEGKHSL-VIMPTGMGKSVCYQIPALLSEGLTIVISPLIALMQDQVDKLKRFGIDAEFV 85
Cdd:cd18014 5 KKVFGHSDFKSPlQEKATMAVVKGNKDVfVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRVDSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 86 NSSLSAEERVLRYENLKQG--KYKILYVSPERFRKSAFLEIFQN----RKVSLLAVDEAHCVSQWGHDFRPDYSKISEFR 159
Cdd:cd18014 85 NSKLSAQERKRIIADLESEkpQTKFLYITPEMAATSSFQPLLSSlvsrNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALR 164
|
170 180
....*....|....*....|....*....
gi 1614194638 160 KILKFPTTMALTATATKEIRSDILRQIGI 188
Cdd:cd18014 165 SRYGHVPWVALTATATPQVQEDIFAQLRL 193
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
4-188 |
2.99e-48 |
|
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: 164.56 E-value: 2.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 4 LAECKTLFGISAFRGSQENIITRTME-GKHSLVIMPTGMGKSVCYQIPALLSEGLTIVISPLIALMQDQVDKLKRFGIDA 82
Cdd:cd18017 1 LNALNEYFGHSSFRPVQWKVIRSVLEeRRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 83 EFVNSSLSAEERvlryENLKQGKYKILYVSPERFRKSAFLEIFQNRKVSLLAVDEAHCVSQWGHDFRPDYSKISEFRKIL 162
Cdd:cd18017 81 CFLGSAQSQNVL----DDIKMGKIRVIYVTPEFVSKGLELLQQLRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRL 156
|
170 180
....*....|....*....|....*.
gi 1614194638 163 KFPTTMALTATATKEIRSDILRQIGI 188
Cdd:cd18017 157 PNVPIVALTATATPSVRDDIIKNLNL 182
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
11-192 |
2.10e-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: 159.99 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 11 FGISAFRGSQENIITRTMEGKHSLVIMPTGMGKSVCYQIPALLSEGLTIVISPLIALMQDQVDKLKRFGIDAEFVNSSLS 90
Cdd:cd18016 13 FGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLTGDKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 91 AEERVLRYENLKQGK--YKILYVSPERFRKS-----AFLEIFQNRKVSLLAVDEAHCVSQWGHDFRPDYSKISEFRKilK 163
Cdd:cd18016 93 DAEATKIYLQLSKKDpiIKLLYVTPEKISASnrlisTLENLYERKLLARFVIDEAHCVSQWGHDFRPDYKRLNMLRQ--K 170
|
170 180 190
....*....|....*....|....*....|.
gi 1614194638 164 FPT--TMALTATATKEIRSDILRQIGISESE 192
Cdd:cd18016 171 FPSvpMMALTATATPRVQKDILNQLKMLRPQ 201
|
|
| DpdF |
NF041063 |
protein DpdF; |
34-341 |
8.23e-43 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 162.00 E-value: 8.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 34 LVIMPTGMGKSVCYQIPALLS---EGLTIVISPLIALMQDQVDKLKRF--GIDAEFVN-----SSLSAEERVLRYENLKQ 103
Cdd:NF041063 162 IVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQERRARELlrRAGPDLGGplawhGGLSAEERAAIRQRIRD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 104 GKYKILYVSPERFRKS---AFLEIFQNRKVSLLAVDEAHCVSQWGHDFRPDYSKISEFRKILkfpttmALTATATKEIRS 180
Cdd:NF041063 242 GTQRILFTSPESLTGSlrpALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSL------LRLAPSGRPFRT 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 181 dILRQIGISES--ET--EIFDEG-----IC----RPNLYLEARSFPDPVSKRKEILSLLKG----------ERKNTIVYF 237
Cdd:NF041063 316 -LLLSATLTEStlDTleTLFGPPgpfivVSavqlRPEPAYWVAKCDSEEERRERVLEALRHlprplilyvtKVEDAEAWL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 238 NLIKNlESFGEaldlekipYRIYHGQLPPEKRKRIQESFlkSKDQL--LLATNAFGMGVDKPDIRRVIHAELPSSLESYY 315
Cdd:NF041063 395 QRLRA-AGFRR--------VALFHGDTPDAERERLIEQW--RENELdiVVATSAFGLGMDKSDVRTVIHACVPETLDRFY 463
|
330 340
....*....|....*....|....*.
gi 1614194638 316 QEIGRAGRDGEPSECLLFYNQDDLAV 341
Cdd:NF041063 464 QEVGRGGRDGKASLSLLIYTPDDLDI 489
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
202-334 |
2.79e-38 |
|
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: 135.80 E-value: 2.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 202 RPNLYLEARsfpdPVSKRKEILSLLKGERKN-----TIVYFNLIKNLESFGEALDLEKIPYRIYHGQLPPEKRKRIQESF 276
Cdd:cd18794 1 RPNLFYSVR----PKDKKDEKLDLLKRIKVEhlggsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKW 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1614194638 277 LKSKDQLLLATNAFGMGVDKPDIRRVIHAELPSSLESYYQEIGRAGRDGEPSECLLFY 334
Cdd:cd18794 77 LRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
20-164 |
1.40e-27 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 108.10 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 20 QENIITRTMEGKHSLVIMPTGMGKSVCYQIPAL------LSEGLTIVISPLIALMQDQVDKLKRFGIDAEF-VNSSLSAE 92
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLLGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 93 ERVLRYENLKqgKYKILYVSPERfrksaFLEIFQNRK----VSLLAVDEAHCVSQWGhdFRPDYSKI----SEFRKILKF 164
Cdd:pfam00270 84 SRKEQLEKLK--GPDILVGTPGR-----LLDLLQERKllknLKLLVLDEAHRLLDMG--FGPDLEEIlrrlPKKRQILLL 154
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
217-325 |
7.77e-24 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 95.74 E-value: 7.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 217 SKRKEILSLLKGERKN-TIVYFNLIKNLEsFGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVD 295
Cdd:pfam00271 1 EKLEALLELLKKERGGkVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 1614194638 296 KPDIRRVIHAELPSSLESYYQEIGRAGRDG 325
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
244-325 |
4.95e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 92.66 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 244 ESFGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPDIRRVIHAELPSSLESYYQEIGRAGR 323
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1614194638 324 DG 325
Cdd:smart00490 81 AG 82
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
11-155 |
4.30e-22 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 93.71 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 11 FGISAFRGSQENIITRTMEGKHSLVI-MPTGMGKSVCYQIPALL-----SEGLTIVISPLIALMQDQVDKLKRFGIDAEF 84
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILaAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1614194638 85 VNSSL-SAEERVLRYENLKQGKYKILYVSPERFRKSAFLEIFQNRKVSLLAVDEAHCVSQWGhdFRPDYSKI 155
Cdd:smart00487 84 KVVGLyGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL 153
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
30-163 |
3.52e-17 |
|
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: 78.21 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 30 GKHSLVIMPTGMGKSVCYQIPALLS----EGLTIVISPLIALMQDQVDKLKRF---GIDAEFVNSSLSAEERvlryENLK 102
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEER----EKNK 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1614194638 103 QGKYKILYVSPERFRKS-AFLEIFQNRKVSLLAVDEAHCVSQWGHDFRPDYskISEFRKILK 163
Cdd:cd00046 77 LGDADIIIATPDMLLNLlLREDRLFLKDLKLIIVDEAHALLIDSRGALILD--LAVRKAGLK 136
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
21-335 |
1.77e-16 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 81.99 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 21 ENIITRTMEGKHS-LVIMPTGMGKSV----CYQipALLSEGLTIVISPLIALMQDQVDKLKRFGIDAEFVNSSlsaeerv 95
Cdd:COG1061 90 EALLAALERGGGRgLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAGGGK------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 96 lryenlKQGKYKILYVSPERFRKSAFLEIFQNRkVSLLAVDEAHcvsqwgHDFRPDYSKISE---FRKILKF---Pttma 169
Cdd:COG1061 161 ------KDSDAPITVATYQSLARRAHLDELGDR-FGLVIIDEAH------HAGAPSYRRILEafpAAYRLGLtatP---- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 170 ltatatkeIRSD-----ILRQIGI--SESETEIFDEGICRP--------------NLYLEARSF------PDPVSKRKEI 222
Cdd:COG1061 224 --------FRSDgreilLFLFDGIvyEYSLKEAIEDGYLAPpeyygirvdltderAEYDALSERlrealaADAERKDKIL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 223 LSLLK--GERKNTIVYFNLIKNLESFGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPDIR 300
Cdd:COG1061 296 RELLRehPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLD 375
|
330 340 350
....*....|....*....|....*....|....*
gi 1614194638 301 RVIHAELPSSLESYYQEIGRAGRDGEPSECLLFYN 335
Cdd:COG1061 376 VAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYD 410
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
225-334 |
2.91e-16 |
|
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: 75.24 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 225 LLKGERKNTIVYFNLIKNLESFGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPDIRRVIH 304
Cdd:cd18787 22 LEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVDHVIN 101
|
90 100 110
....*....|....*....|....*....|
gi 1614194638 305 AELPSSLESYYQEIGRAGRDGEPSECLLFY 334
Cdd:cd18787 102 YDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
20-358 |
3.81e-14 |
|
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: 74.87 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 20 QENIITRTMEGKHSLVIMPTGMGKSVCYQIPALlsEGL-------TIVISPLIALMQDQVDKLKRF------GIDAEFVN 86
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVL--EALledpgatALYLYPTKALARDQLRRLRELaealglGVRVATYD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 87 SSLSAEER--VLRYENlkqgkykILYVSP-----------ERFRKsaFLeifqnRKVSLLAVDEAHC---V--SQWGHDF 148
Cdd:COG1205 139 GDTPPEERrwIREHPD-------IVLTNPdmlhygllphhTRWAR--FF-----RNLRYVVIDEAHTyrgVfgSHVANVL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 149 RpdyskisEFRKILKFpttmaltatatkeIRSD---IL-------------RQIG-----ISES------------ETEI 195
Cdd:COG1205 205 R-------RLRRICRH-------------YGSDpqfILasatignpaehaeRLTGrpvtvVDEDgsprgertfvlwNPPL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 196 FDEGIcRPNLYLEARsfpdpvskrkEILSLLKGERKNTIVYFNLIKNLE----SFGEALDLEKIPYRI--YHGQLPPEKR 269
Cdd:COG1205 265 VDDGI-RRSALAEAA----------RLLADLVREGLRTLVFTRSRRGAEllarYARRALREPDLADRVaaYRAGYLPEER 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 270 KRIQESfLKSKDQL-LLATNAFGMGVDKPDIRRVIHAELPSSLESYYQEIGRAGRDGEPSecllfynqddLAVL------ 342
Cdd:COG1205 334 REIERG-LRSGELLgVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS----------LVVLvagddp 402
|
410
....*....|....*...
gi 1614194638 343 MD--FIewQNPDsAFFSR 358
Cdd:COG1205 403 LDqyYV--RHPE-ELFER 417
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
267-334 |
2.47e-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: 2.47e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1614194638 267 EKRKRIQESFlkskdQLLLATNAFGMGVDKPDIRRVIHAELPSSLESYYQEIGRAGRDG-EPSECLLFY 334
Cdd:cd18785 14 EHAEEIASSL-----EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
230-328 |
3.31e-12 |
|
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: 63.82 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 230 RKNTIVYFNLIKN-LEsfGEALDLEKIpyRIYHGQLPPEKRKRIqESFLKSKDQL-LLATNAFGMGVDKPDIRRVIHAEL 307
Cdd:cd18797 45 RKLAELLLRYLKArLV--EEGPLASKV--ASYRAGYLAEDRREI-EAELFNGELLgVVATNALELGIDIGGLDAVVLAGY 119
|
90 100
....*....|....*....|.
gi 1614194638 308 PSSLESYYQEIGRAGRDGEPS 328
Cdd:cd18797 120 PGSLASLWQQAGRAGRRGKDS 140
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
214-347 |
1.42e-11 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 66.35 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 214 DPVSKRKEILSLLKGE---RKNTIVYFNLIKNLESFGEALDL-EKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNA 289
Cdd:PLN00206 348 ETKQKKQKLFDILKSKqhfKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGV 427
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1614194638 290 FGMGVDKPDIRRVIHAELPSSLESYYQEIGRAGRDGEPSECLLFYNQDDLAVLMDFIE 347
Cdd:PLN00206 428 LGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
20-139 |
1.65e-08 |
|
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: 54.13 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 20 QENIITRTMEGKHSLVIMPTGMGKSVCYQIP---ALLSEGLT--IVISPLIALMQDQVDKLKRF------GIDAEFVNSS 88
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDPGSraLYLYPTKALAQDQLRSLRELleqlglGIRVATYDGD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1614194638 89 LSAEERvlryENLKQGKYKILYVSPER-----FRKSAFLEIFQnRKVSLLAVDEAH 139
Cdd:cd17923 85 TPREER----RAIIRNPPRILLTNPDMlhyalLPHHDRWARFL-RNLRYVVLDEAH 135
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
28-337 |
4.91e-08 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 55.16 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 28 MEGKHSLVIMPTGMGKSVCYQIPA--------LLSEG---LTIVISPLIALMQDQVDKLKRFGIDAEFVNSSL--SAEER 94
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAygGVPKR 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 95 VLRYEnLKQGkYKILYVSPERFRKsaFLEifQN----RKVSLLAVDEAHCVSQWGhdFRPDYSKISEF----RKILKFpt 166
Cdd:PTZ00110 245 GQIYA-LRRG-VEILIACPGRLID--FLE--SNvtnlRRVTYLVLDEADRMLDMG--FEPQIRKIVSQirpdRQTLMW-- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 167 tmalTATATKEIRS---DILRQIGISESETEIfDEGICR---PNLY-LEARsfpDPVSKRKEILSLLKGERKNTIVYFNL 239
Cdd:PTZ00110 315 ----SATWPKEVQSlarDLCKEEPVHVNVGSL-DLTACHnikQEVFvVEEH---EKRGKLKMLLQRIMRDGDKILIFVET 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 240 IKNLESFGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPDIRRVIHAELPSSLESYYQEIG 319
Cdd:PTZ00110 387 KKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIG 466
|
330
....*....|....*...
gi 1614194638 320 RAGRDGEPSECLLFYNQD 337
Cdd:PTZ00110 467 RTGRAGAKGASYTFLTPD 484
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
217-335 |
6.28e-08 |
|
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: 51.32 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 217 SKRKEILSLLKGERKNT---IVYFNLIKNLESFGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKD--QLLLATNAFG 291
Cdd:cd18793 11 GKLEALLELLEELREPGekvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGG 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1614194638 292 MGVDKPDIRRVIHAEL---PSSLEsyyQEIGRAGRDGEPSECLLFYN 335
Cdd:cd18793 91 VGLNLTAANRVILYDPwwnPAVEE---QAIDRAHRIGQKKPVVVYRL 134
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
11-323 |
1.23e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 54.13 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 11 FGISAFRGSQENIITRT-MEGKHSLVIMPTGMGKSVCYQIPAL--LSEGLTIV-ISPLIALMQDQVDKLKR----FGIDA 82
Cdd:COG1204 18 RGIEELYPPQAEALEAGlLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLRALASEKYREFKRdfeeLGIKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 83 EfvnssLSAEERVLRYENLkqGKYKILYVSPERF-----RKSAFLeifqnRKVSLLAVDEAHCVsqwGHDFR-PDY-SKI 155
Cdd:COG1204 98 G-----VSTGDYDSDDEWL--GRYDILVATPEKLdsllrNGPSWL-----RDVDLVVVDEAHLI---DDESRgPTLeVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 156 SEFRKIlkfpttmaltataTKEIR-----------SDILRQIGISESETEIfdegicRPN------LYLEARSFPDPVSK 218
Cdd:COG1204 163 ARLRRL-------------NPEAQivalsatignaEEIAEWLDAELVKSDW------RPVplnegvLYDGVLRFDDGSRR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 219 RKE-ILSL---LKGERKNTIVYFNLIKNLESFGEAL--------------DLEKIPYRI--------------------- 259
Cdd:COG1204 224 SKDpTLALaldLLEEGGQVLVFVSSRRDAESLAKKLadelkrrltpeereELEELAEELlevseethtnekladclekgv 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1614194638 260 --YHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPdIRRVIHAEL-------PSSLEsYYQEIGRAGR 323
Cdd:COG1204 304 afHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIIRDTkrggmvpIPVLE-FKQMAGRAGR 374
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
214-347 |
1.32e-07 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 53.61 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 214 DPVSKRKEILSLLKGER-KNTIVYFNLIKNLESFGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGM 292
Cdd:COG0513 224 DKRDKLELLRRLLRDEDpERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1614194638 293 GVDKPDIRRVIHAELPSSLESYYQEIGRAGRDGEPSECLLFYNQDDLAVLMDfIE 347
Cdd:COG0513 304 GIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRA-IE 357
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
262-338 |
2.05e-07 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 53.38 E-value: 2.05e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1614194638 262 GQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPDIRRVIHAELPSSLESYYQEIGRAGRDGEPSECLLFYNQDD 338
Cdd:PRK01297 367 GDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
231-333 |
2.22e-07 |
|
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: 50.34 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 231 KNTIVYFNLIKNLESFGEAL------DLEKIPYRIYHGQLPPEKRKRIqESFLKSKD-QLLLATNAFGMGVDKPDIRRVI 303
Cdd:cd18796 39 KSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEV-EAALKRGDlKVVVATSSLELGIDIGDVDLVI 117
|
90 100 110
....*....|....*....|....*....|.
gi 1614194638 304 HAELPSSLESYYQEIGRAG-RDGEPSECLLF 333
Cdd:cd18796 118 QIGSPKSVARLLQRLGRSGhRPGAASKGRLV 148
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
431-475 |
2.99e-07 |
|
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: 47.28 E-value: 2.99e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1614194638 431 EDKKKAAQNRLYKMLMYLKSEV-CRREFVYEYFDAKFTR--CDNCDIC 475
Cdd:pfam16124 18 EERKEVELQKLQAMVAYCENTTdCRRKQLLRYFGEEFDSepCGNCDNC 65
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
20-139 |
5.66e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 49.21 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 20 QENIITRTMEG-----KHSLVIMPTGMGKSVCY-QIPALLSEGL----TIVISPLIALMQDQVDKLKRFGIDAEFVNSSL 89
Cdd:pfam04851 8 QIEAIENLLESikngqKRGLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVEIGEII 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1614194638 90 SAEERVLRYENLK------QGKYKILYVSPERFRKSAFLEIFqnrkvsllaVDEAH 139
Cdd:pfam04851 88 SGDKKDESVDDNKivvttiQSLYKALELASLELLPDFFDVII---------IDEAH 134
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
218-325 |
3.42e-06 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 49.17 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 218 KRKEILSLLKGER-KNTIVYFNLIKNLESFGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDK 296
Cdd:PRK11192 232 KTALLCHLLKQPEvTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDI 311
|
90 100
....*....|....*....|....*....
gi 1614194638 297 PDIRRVIHAELPSSLESYYQEIGRAGRDG 325
Cdd:PRK11192 312 DDVSHVINFDMPRSADTYLHRIGRTGRAG 340
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
261-344 |
5.68e-06 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 48.67 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 261 HGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPDIRRVIHAELPSSLESYYQEIGRAGRDGEPSECLLFYNQDDLA 340
Cdd:PTZ00424 298 HGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIE 377
|
....
gi 1614194638 341 VLMD 344
Cdd:PTZ00424 378 QLKE 381
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
24-139 |
8.42e-06 |
|
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: 45.37 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 24 ITRTMEGKHSLVIMPTGMGKSVC-YQIPALLSEGLTIVISPLIALMQDQVDKLKRFGIDAEFvnsslsaeeRVLRYENLK 102
Cdd:cd17926 12 WLAHKNNRRGILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSI---------GLIGGGKKK 82
|
90 100 110
....*....|....*....|....*....|....*...
gi 1614194638 103 QGKYKILYVS-PERFRKSAFLEIFQNRKVSLLAVDEAH 139
Cdd:cd17926 83 DFDDANVVVAtYQSLSNLAEEEKDLFDQFGLLIVDEAH 120
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
249-325 |
1.28e-05 |
|
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: 45.24 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 249 ALDLEKIPYriYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPdIRRVI----------HAELPSSLEsYYQEI 318
Cdd:cd18795 60 AKDLAGIAF--HHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP-ARTVIikgtqrydgkGYRELSPLE-YLQMI 135
|
....*..
gi 1614194638 319 GRAGRDG 325
Cdd:cd18795 136 GRAGRPG 142
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
20-143 |
1.76e-05 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 45.33 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 20 QENIITRTMEGKHSLVI-MPTGMGKSVC--YQIPALL--SEGLTIVISPLIALMQDQVDKLKRFGIDAEFVNSSLSAEER 94
Cdd:cd17921 6 QREALRALYLSGDSVLVsAPTSSGKTLIaeLAILRALatSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPS 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1614194638 95 VLryeNLKQGKYKILYVSPERFR-KSAFLEIFQNRKVSLLAVDEAHCVSQ 143
Cdd:cd17921 86 VN---KLLLAEADILVATPEKLDlLLRNGGERLIQDVRLVVVDEAHLIGD 132
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
261-335 |
1.89e-05 |
|
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: 44.64 E-value: 1.89e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1614194638 261 HGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPD--IRRVIHAElPSSLESYYQEIGRAGRDGEPSECLLFYN 335
Cdd:cd18811 68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatVMVIEDAE-RFGLSQLHQLRGRVGRGDHQSYCLLVYK 143
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
215-335 |
2.52e-05 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 44.57 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 215 PVSKRKEILSLLKGE-RKNTIVYF--NLI--------KNLESFGEALDlEKIPYR---IYHGQLPPEKRKRIQESFLKSK 280
Cdd:cd18792 8 PHDDLDLVYEAIERElARGGQVYYvyPRIeesekldlKSIEALAEELK-ELVPEArvaLLHGKMTEDEKEAVMLEFREGE 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1614194638 281 DQLLLATNAFGMGVDKPDIRRVI--HAELpSSLESYYQEIGRAGRDGEPSECLLFYN 335
Cdd:cd18792 87 YDILVSTTVIEVGIDVPNANTMIieDADR-FGLSQLHQLRGRVGRGKHQSYCYLLYP 142
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
218-347 |
4.62e-05 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 45.57 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 218 KRK-EILSLLKGERK-NTIVYFNLIKN-LESFGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGV 294
Cdd:PRK10590 230 KRKrELLSQMIGKGNwQQVLVFTRTKHgANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGL 309
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1614194638 295 DKPDIRRVIHAELPSSLESYYQEIGRAGRDGEPSECLLFYNQDDLAVLMDfIE 347
Cdd:PRK10590 310 DIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRD-IE 361
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
18-138 |
7.86e-05 |
|
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: 43.47 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 18 GSQENIITRTMEGKHSLVIMPTGMGKSVCYQIPAL---LSEGLTIVISPLIALMQDQVDKLKRFGIDAE------FVNSS 88
Cdd:cd17924 20 GAQRTWAKRLLRGKSFAIIAPTGVGKTTFGLATSLylaSKGKRSYLIFPTKSLVKQAYERLSKYAEKAGvevkilVYHSR 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1614194638 89 LSAEERVLRYENLKQGKYKILYVSPERFRKSAflEIFQNRKVSLLAVDEA 138
Cdd:cd17924 100 LKKKEKEELLEKIEKGDFDILVTTNQFLSKNF--DLLSNKKFDFVFVDDV 147
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
235-334 |
8.82e-05 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350197 [Multi-domain] Cd Length: 151 Bit Score: 42.72 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 235 VYF--NLIKNLESFGEALDlEKIP---YRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPDIRR-VIHAELP 308
Cdd:cd18810 28 VFYvhNRIESIEKLATQLR-QLVPearIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTiIIERADK 106
|
90 100
....*....|....*....|....*.
gi 1614194638 309 SSLESYYQEIGRAGRDGEPSECLLFY 334
Cdd:cd18810 107 FGLAQLYQLRGRVGRSKERAYAYFLY 132
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
227-323 |
1.44e-04 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 44.50 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 227 KGERKNTIVYFNLIKNLESFGEALDlekIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMGVDKPdIRRVIHAE 306
Cdd:COG1202 424 KGYRGQTIIFTNSRRRCHEIARALG---YKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFP-ASQVIFDS 499
|
90 100
....*....|....*....|..
gi 1614194638 307 LPS-----SLESYYQEIGRAGR 323
Cdd:COG1202 500 LAMgiewlSVQEFHQMLGRAGR 521
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
21-139 |
2.26e-04 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350687 [Multi-domain] Cd Length: 178 Bit Score: 41.81 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 21 ENIITRTMEGKHSLVIMPTGMGKSVCY--QIPALLSEGLT-IVISPLIALMQDQVDKLK-RFGIDAEFVNSSLSAEERVL 96
Cdd:cd17929 6 EAIVSSLGGFKTFLLHGVTGSGKTEVYieLIEKVLAKGKQvLVLVPEISLTPQLIKRFKkRFGDKVAVLHSKLSDKERAD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1614194638 97 RYENLKQGKYKILyVSPerfRKSAFLEiFQNrkVSLLAVDEAH 139
Cdd:cd17929 86 EWRKIKRGEAKVV-IGA---RSALFAP-FKN--LGLIIVDEEH 121
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
258-333 |
2.72e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 43.76 E-value: 2.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1614194638 258 RIYHGQLPPEKRkRIQESFLKSKD-QLLLATNAFGMGVDKPDIRRVIHAELPSSLESYYQEIGRAGRD-GEPSECLLF 333
Cdd:PRK09751 305 RSHHGSVSKEQR-AITEQALKSGElRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQvGGVSKGLFF 381
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
16-139 |
4.17e-04 |
|
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: 41.65 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 16 FRGSQENIITRTMEGKHSLVIMPTGMGKS-----VC----YQIPAlLSEGLTIVISPLIALMQDQVDKLKR-FGIDAEFV 85
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPA-GRKGKVVFLANKVPLVEQQKEVFRKhFERPGYKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1614194638 86 nSSLSAEERV-LRYENLKQGkYKILYVSPERFRKSAF-LEIFQNRKVSLLAVDEAH 139
Cdd:cd17927 82 -TGLSGDTSEnVSVEQIVES-SDVIIVTPQILVNDLKsGTIVSLSDFSLLVFDECH 135
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
40-152 |
5.82e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350677 [Multi-domain] Cd Length: 182 Bit Score: 40.63 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 40 GMGK-----SVC-YQIPALLSEGLTIVISPLIALMQdQVDKLKRFGIDAEFVNSSLSAEERVLRYENLKQGKYKILYVSP 113
Cdd:cd17919 29 GLGKtlqaiAFLaYLLKEGKERGPVLVVCPLSVLEN-WEREFEKWTPDLRVVVYHGSQRERAQIRAKEKLDKFDVVLTTY 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1614194638 114 ERFRKsaFLEIFQNRKVSLLAVDEAHCV-------SQWGHDFRPDY 152
Cdd:cd17919 108 ETLRR--DKASLRKFRWDLVVVDEAHRLknpksqlSKALKALRAKR 151
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
216-333 |
1.06e-03 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 41.76 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 216 VSKRKEILSLLKGERKNTIVYFNLIKN--LEsFGEALDLEKIPYRIYHGQLPPEKRKRIQESFLKSKDQLLLATNAFGMG 293
Cdd:PRK11634 230 MRKNEALVRFLEAEDFDAAIIFVRTKNatLE-VAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARG 308
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1614194638 294 VDKPDIRRVIHAELPSSLESYYQEIGRAGRDGEPSECLLF 333
Cdd:PRK11634 309 LDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
24-148 |
2.00e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 40.68 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 24 ITRTMEGKHSLVI-MPTGMGKSVCYQIPALLS---EGLTIVIS-PLIALmQDQVdklkrFGIDAEFVNSSLSAEervLRY 98
Cdd:COG1199 26 VARALAEGRHLLIeAGTGTGKTLAYLVPALLAareTGKKVVIStATKAL-QEQL-----VEKDLPLLRKALGLP---LRV 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1614194638 99 ENLKqGKYKilYVSPERFRKSAFLEIFQNRKVSLLAVDEAHCVSQWGHDF 148
Cdd:COG1199 97 ALLK-GRSN--YLCLRRLEQALQEGDDLDDEELLLARILAWASETWTGDR 143
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
30-139 |
2.78e-03 |
|
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: 38.72 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 30 GKHSLVIMPTGMGKSVCYQIPALLS------EGLTIV-ISPLIALMQDQVDKLKR------FGIDAEFVNSSLSAEERVL 96
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSladepeKGVQVLyISPLKALINDQERRLEEpldeidLEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1614194638 97 RYENLKQgkykILYVSPERF-----RKsAFLEIFQNrkVSLLAVDEAH 139
Cdd:cd17922 81 QLKNPPG----ILITTPESLelllvNK-KLRELFAG--LRYVVVDEIH 121
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
215-335 |
3.57e-03 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 39.75 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614194638 215 PVSKRKEILSLLKGE----RKNTIVYfNLIKnlESfgEALDL-------EKI-----PYRIY--HGQLPPEKRKRIQESF 276
Cdd:PRK10917 453 PDSRRDEVYERIREEiakgRQAYVVC-PLIE--ES--EKLDLqsaeetyEELqeafpELRVGllHGRMKPAEKDAVMAAF 527
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1614194638 277 LKSKDQLLLATNAFGMGVDKPD---IrrVI-HAE---LpSSLesyYQEIGRAGRDGEPSECLLFYN 335
Cdd:PRK10917 528 KAGEIDILVATTVIEVGVDVPNatvM--VIeNAErfgL-AQL---HQLRGRVGRGAAQSYCVLLYK 587
|
|
| |
