|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
2-473 |
7.04e-176 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 503.52 E-value: 7.04e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 2 KLEEYLYRWFGYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQEGTVLVVSPLLSLMEDQVTQLKyvvKN 81
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALR---AA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 82 --RVIAFNSFRTLHEKREAMKRLAS--YKFIFVSPEMLQSELLIRELKKVHISLFVVDEAHCISQWGYDFRPDYKKLNVV 157
Cdd:COG0514 81 giRAAFLNSSLSAEERREVLRALRAgeLKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 158 IENIGSPTVLALTATATKDVLRDIAESLNLENVTQHVYSIDRPNIAMEVQFVETiEEKKEALLEQV-MYLQGPGIVYCSS 236
Cdd:COG0514 161 RERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPP-DDKLAQLLDFLkEHPGGSGIVYCLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 237 RAWTERLTEYLRGKGVTgVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIHFHYPTNIASYLQEI 316
Cdd:COG0514 240 RKKVEELAEWLREAGIR-AAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 317 GRAGRDGEPSIAILLCSPldhdlpisiiEDelpsqsqiqflfsllqermfqtkelpieeveeicynaarfneqywrfiry 396
Cdd:COG0514 319 GRAGRDGLPAEALLLYGP----------ED-------------------------------------------------- 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446685642 397 hleqlgIIQQRKLMLESLSDeimtrliaevEIRLRNKYSELENMKSWIQVKGCRREYLLQQFGyrkEGELKNC--CDYC 473
Cdd:COG0514 339 ------VAIQRFFIEQSPPD----------EERKRVERAKLDAMLAYAETTGCRRQFLLRYFG---EELAEPCgnCDNC 398
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
3-355 |
4.82e-113 |
|
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: 346.67 E-value: 4.82e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 3 LEEYLYRWFGYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQEGTVLVVSPLLSLMEDQVTQLKyvvKNR 82
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLR---AAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 83 VIA--FNSFRTLHEKREAMKRLAS--YKFIFVSPEMLQSELLIRELKKVHISLFVVDEAHCISQWGYDFRPDYKKLNVVI 158
Cdd:TIGR01389 78 VAAayLNSTLSAKEQQDIEKALVNgeLKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 159 ENIGSPTVLALTATATKDVLRDIAESLNLENVTQHVYSIDRPNIAMEVqfVETIEEKKEALLEQVMYLQGPGIVYCSSRA 238
Cdd:TIGR01389 158 ERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSV--VKKNNKQKFLLDYLKKHRGQSGIIYASSRK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 239 WTERLTEYLRGKGVTGVAfYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIHFHYPTNIASYLQEIGR 318
Cdd:TIGR01389 236 KVEELAERLESQGISALA-YHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGR 314
|
330 340 350
....*....|....*....|....*....|....*..
gi 446685642 319 AGRDGEPSIAILLCSPLDHDLPISIIEDELPSQSQIQ 355
Cdd:TIGR01389 315 AGRDGLPAEAILLYSPADIALLKRRIEQSEADDDYKQ 351
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
7-347 |
4.42e-107 |
|
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: 327.50 E-value: 4.42e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 7 LYRWFGYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQEGTVLVVSPLLSLMEDQVTQLKyvvKNRVIA- 85
Cdd:TIGR00614 3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQ---ALGIPAt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 86 -FNSFRTLHEKREAMK--RLASYKFIFVSPE--MLQSELLIRELKKVHISLFVVDEAHCISQWGYDFRPDYKKLNVVIEN 160
Cdd:TIGR00614 80 fLNSAQTKEQQLNVLTdlKDGKIKLLYVTPEkiSASNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 161 IGSPTVLALTATATKDVLRDIAESLNLENVTQHVYSIDRPNIAMEVqfvetiEEKKEALLEQVM-YLQG-----PGIVYC 234
Cdd:TIGR00614 160 FPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEV------RRKTPKILEDLLrFIRKefegkSGIIYC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 235 SSRAWTERLTEYLRGKGVTGVAfYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIHFHYPTNIASYLQ 314
Cdd:TIGR00614 234 PSRKKVEQVAAELQKLGLAAGA-YHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQ 312
|
330 340 350
....*....|....*....|....*....|...
gi 446685642 315 EIGRAGRDGEPSIAILLCSPLDHDLPISIIEDE 347
Cdd:TIGR00614 313 ESGRAGRDGLPSECHLFYAPADMNRLRRLLMEE 345
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
4-336 |
3.56e-105 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 326.67 E-value: 3.56e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 4 EEYLYRWFGYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQEGTVLVVSPLLSLMEDQVTQLKyvvKNRV 83
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLL---ANGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 84 IA--FNSFRTLHEKREAMKRLAS--YKFIFVSPEMLQSELLIRELKKVHISLFVVDEAHCISQWGYDFRPDYKKLNVVIE 159
Cdd:PRK11057 91 AAacLNSTQTREQQLEVMAGCRTgqIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 160 NIGSPTVLALTATATKDVLRDIAESLNLENVTQHVYSIDRPNIAMevqfveTIEEKKEALLEQVMYLQGP----GIVYCS 235
Cdd:PRK11057 171 RFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRY------TLVEKFKPLDQLMRYVQEQrgksGIIYCN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 236 SRAWTERLTEYLRGKGVTgVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIHFHYPTNIASYLQE 315
Cdd:PRK11057 245 SRAKVEDTAARLQSRGIS-AAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQE 323
|
330 340
....*....|....*....|.
gi 446685642 316 IGRAGRDGEPSIAILLCSPLD 336
Cdd:PRK11057 324 TGRAGRDGLPAEAMLFYDPAD 344
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
4-198 |
2.43e-87 |
|
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: 266.71 E-value: 2.43e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 4 EEYLYRWFGYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQEGTVLVVSPLLSLMEDQVTQLKYVVKnRV 83
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGI-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 84 IAFNSFRTLHEKREAMKRLA--SYKFIFVSPEMLQSELLIRELKKVH----ISLFVVDEAHCISQWGYDFRPDYKKLNVV 157
Cdd:cd17920 80 AALNSTLSPEEKREVLLRIKngQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446685642 158 IENIGSPTVLALTATATKDVLRDIAESLNLENVTQHVYSID 198
Cdd:cd17920 160 RRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
2-337 |
9.05e-77 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 262.14 E-value: 9.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 2 KLEEYLYRWFGYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQEGTVLVVSPLLSLMEDQVTQLkyVVKN 81
Cdd:PLN03137 447 KLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNL--LQAN 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 82 RVIAFNSFRT-LHEKREAMKRLAS----YKFIFVSPEML-QSELLIRELKKVH----ISLFVVDEAHCISQWGYDFRPDY 151
Cdd:PLN03137 525 IPAASLSAGMeWAEQLEILQELSSeyskYKLLYVTPEKVaKSDSLLRHLENLNsrglLARFVIDEAHCVSQWGHDFRPDY 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 152 KKLNVVIENIGSPTVLALTATATKDVLRDIAESLNLENVTQHVYSIDRPNIAMEV-----QFVETIEE-KKEALLEQVmy 225
Cdd:PLN03137 605 QGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVvpktkKCLEDIDKfIKENHFDEC-- 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 226 lqgpGIVYCSSRAWTERLTEYLRGKGvTGVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIHFHY 305
Cdd:PLN03137 683 ----GIIYCLSRMDCEKVAERLQEFG-HKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSL 757
|
330 340 350
....*....|....*....|....*....|..
gi 446685642 306 PTNIASYLQEIGRAGRDGEPSIAILLCSPLDH 337
Cdd:PLN03137 758 PKSIEGYHQECGRAGRDGQRSSCVLYYSYSDY 789
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
4-190 |
2.18e-67 |
|
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: 215.58 E-value: 2.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 4 EEYLYRWFGYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQE----GTVLVVSPLLSLMEDQVTQLKYVV 79
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPRAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 80 KnrVIAFNSFRTLHEKREAMKRLAS--YKFIFVSPEMLQSELLIRELKKV-HISLFVVDEAHCISQWGYDFRPDYKKLNV 156
Cdd:cd18018 81 K--AAALNSSLTREERRRILEKLRAgeVKILYVSPERLVNESFRELLRQTpPISLLVVDEAHCISEWSHNFRPDYLRLCR 158
|
170 180 190
....*....|....*....|....*....|....*
gi 446685642 157 VI-ENIGSPTVLALTATATKDVLRDIAESLNLENV 190
Cdd:cd18018 159 VLrELLGAPPVLALTATATKRVVEDIASHLGIPES 193
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
2-188 |
4.48e-55 |
|
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: 183.72 E-value: 4.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 2 KLEEYLYRWFGYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQEGTVLVVSPLLSLMEDQVTQLKYvVKN 81
Cdd:cd18015 5 KVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKK-LGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 82 RVIAFNSFRTLHEKREAMKRL----ASYKFIFVSPE-MLQSELLIRELKKVH----ISLFVVDEAHCISQWGYDFRPDYK 152
Cdd:cd18015 84 SATMLNASSSKEHVKWVHAALtdknSELKLLYVTPEkIAKSKRFMSKLEKAYnagrLARIAIDEVHCCSQWGHDFRPDYK 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 446685642 153 KLNVVIENIGSPTVLALTATATKDVLRDIAESLNLE 188
Cdd:cd18015 164 KLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQ 199
|
|
| DpdF |
NF041063 |
protein DpdF; |
9-348 |
1.98e-53 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 193.20 E-value: 1.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 9 RWFGYSEFR-PGQKGVITDLL---EGKDVIAMLPTGRGKSMCYQLPGLM---QEGTVLVVSPLLSLMEDQVTQLKYVVKN 81
Cdd:NF041063 133 EALGFTHYRsPGQREAVRAALlapPGSTLIVNLPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQERRARELLRR 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 82 RVIAFNSFRTLH-----EKREAMK-RLAS--YKFIFVSPEMLQSEL---LIRELKKVHISLFVVDEAHCISQWGYDFRPD 150
Cdd:NF041063 213 AGPDLGGPLAWHgglsaEERAAIRqRIRDgtQRILFTSPESLTGSLrpaLFDAAEAGLLRYLVVDEAHLVDQWGDGFRPE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 151 YKKLNVVIENI-------GSPTVLALTATATKDVLRDIAESLNLENVTQHVYSID-RPNIAMEVQFVETIEEKKEALLEQ 222
Cdd:NF041063 293 FQLLAGLRRSLlrlapsgRPFRTLLLSATLTESTLDTLETLFGPPGPFIVVSAVQlRPEPAYWVAKCDSEEERRERVLEA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 223 VMYLQGPGIVYCSSRAWTERLTEYLRGKGVTGVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIH 302
Cdd:NF041063 373 LRHLPRPLILYVTKVEDAEAWLQRLRAAGFRRVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIH 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446685642 303 FHYPTNIASYLQEIGRAGRDGEPSIAILLCSPLDHDLP-----ISIIEDEL 348
Cdd:NF041063 453 ACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAkslnrPKLISVEK 503
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
2-189 |
6.27e-50 |
|
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: 169.57 E-value: 6.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 2 KLEEYlyrwFGYSEFRPGQKGVITDLLE-GKDVIAMLPTGRGKSMCYQLPGLMQEGTVLVVSPLLSLMEDQVTQLKyvVK 80
Cdd:cd18017 3 ALNEY----FGHSSFRPVQWKVIRSVLEeRRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLV--MS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 81 NRVIAFNSFRTLHEKREAMKrLASYKFIFVSPEMLQSEL-LIRELKKvHISLFVVDEAHCISQWGYDFRPDYKKLNVVIE 159
Cdd:cd18017 77 NIPACFLGSAQSQNVLDDIK-MGKIRVIYVTPEFVSKGLeLLQQLRN-GITLIAIDEAHCVSQWGHDFRSSYRHLGSIRN 154
|
170 180 190
....*....|....*....|....*....|
gi 446685642 160 NIGSPTVLALTATATKDVLRDIAESLNLEN 189
Cdd:cd18017 155 RLPNVPIVALTATATPSVRDDIIKNLNLRN 184
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
199-331 |
4.45e-49 |
|
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: 165.07 E-value: 4.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 199 RPNIAMEVQFVETIEEKKEALLEQVMY-LQGPGIVYCSSRAWTERLTEYLRGKGVTGVAfYHGGMEHEERMLIQQQFMND 277
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEhLGGSGIIYCLSRKECEQVAARLQSKGISAAA-YHAGLEPSDRRDVQRKWLRD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446685642 278 QLQLVICTSAFGMGVNKSNTRYIIHFHYPTNIASYLQEIGRAGRDGEPSIAILL 331
Cdd:cd18794 80 KIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
5-188 |
2.63e-46 |
|
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: 160.33 E-value: 2.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 5 EYLYRWFGYSEFR-PGQKGVITDLLEGK-DVIAMLPTGRGKSMCYQLPGLMQEGTVLVVSPLLSLMEDQVTQLKyVVKNR 82
Cdd:cd18014 2 STLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLK-TLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 83 VIAFNSFRTLHEKREAMKRLAS----YKFIFVSPEMLQS---ELLIRELKKVH-ISLFVVDEAHCISQWGYDFRPDYKKL 154
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESekpqTKFLYITPEMAATssfQPLLSSLVSRNlLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....
gi 446685642 155 NVVIENIGSPTVLALTATATKDVLRDIAESLNLE 188
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLK 194
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
7-189 |
1.69e-45 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 158.45 E-value: 1.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 7 LYRWFGYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQEGTVLVVSPLLSLMEDQVTQLKYVVknrvIAF 86
Cdd:cd18016 9 FHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLD----IPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 87 NSFRTLHEKREAMKRLA-------SYKFIFVSPEML-QSELLIRELKKVH----ISLFVVDEAHCISQWGYDFRPDYKKL 154
Cdd:cd18016 85 TYLTGDKTDAEATKIYLqlskkdpIIKLLYVTPEKIsASNRLISTLENLYerklLARFVIDEAHCVSQWGHDFRPDYKRL 164
|
170 180 190
....*....|....*....|....*....|....*
gi 446685642 155 NVVIENIGSPTVLALTATATKDVLRDIAESLNLEN 189
Cdd:cd18016 165 NMLRQKFPSVPMMALTATATPRVQKDILNQLKMLR 199
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
17-179 |
1.51e-31 |
|
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: 119.27 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 17 RPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGL------MQEGTVLVVSPLLSLMEDQVTQLKYVVKNRVIAFNSFR 90
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 91 TLHEKREAMKRLASYKFIFVSPEMLQSELLIRELKKvHISLFVVDEAHCISQWGydFRPDYKKlnvVIENI-GSPTVLAL 169
Cdd:pfam00270 81 GGDSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLK-NLKLLVLDEAHRLLDMG--FGPDLEE---ILRRLpKKRQILLL 154
|
170
....*....|
gi 446685642 170 TATATKDVLR 179
Cdd:pfam00270 155 SATLPRNLED 164
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
27-337 |
5.21e-26 |
|
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: 112.24 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 27 LLEGKDVIAMLPTGRGKSMCYQLP---GLMQE--GTVLVVSPLLSLMEDQVTQLKYVVKNRVIAFNSFR----TLHEKRE 97
Cdd:COG1205 68 ARAGKNVVIATPTASGKSLAYLLPvleALLEDpgATALYLYPTKALARDQLRRLRELAEALGLGVRVATydgdTPPEERR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 98 AMKRLASykFIFVSPEMLQSELL---------IRELKkvhisLFVVDEAHcisqwGYD----------FRpdykKLNVVI 158
Cdd:COG1205 148 WIREHPD--IVLTNPDMLHYGLLphhtrwarfFRNLR-----YVVIDEAH-----TYRgvfgshvanvLR----RLRRIC 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 159 ENIGS-PTVLALTATatkdvlrdIAESLNL-ENVT-QHVYSIDR---PNIAMEVQFVE---TIEEKKEALLEQVMYL--- 226
Cdd:COG1205 212 RHYGSdPQFILASAT--------IGNPAEHaERLTgRPVTVVDEdgsPRGERTFVLWNpplVDDGIRRSALAEAARLlad 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 227 ---QG-PGIVYCSSRAWTERLTEYLR-----GKGVTGVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSN- 296
Cdd:COG1205 284 lvrEGlRTLVFTRSRRGAELLARYARralrePDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGl 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446685642 297 --TryIIHfHYPTNIASYLQEIGRAGRDGEPSIAILLCS--PLDH 337
Cdd:COG1205 364 daV--VLA-GYPGTRASFWQQAGRAGRRGQDSLVVLVAGddPLDQ 405
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
11-191 |
1.49e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 103.73 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 11 FGYSEFRPGQKGVITDLLEG-KDVIAMLPTGRGKSMCYQLPGLMQ-----EGTVLVVSPLLSLMEDQVTQLKYVVKNRVI 84
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 85 AFNSFRTLHEKREAMKRLAS--YKFIFVSPEMLQSELLIRELKKVHISLFVVDEAHCISQWGydFRPDYKKLnvVIENIG 162
Cdd:smart00487 84 KVVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL--LKLLPK 159
|
170 180
....*....|....*....|....*....
gi 446685642 163 SPTVLALTATATKDVLRDIAESLNLENVT 191
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFI 188
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
241-323 |
4.66e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 92.66 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 241 ERLTEYLRGKGVtGVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIHFHYPTNIASYLQEIGRAG 320
Cdd:smart00490 1 EELAELLKELGI-KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79
|
...
gi 446685642 321 RDG 323
Cdd:smart00490 80 RAG 82
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
12-334 |
6.66e-21 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 94.83 E-value: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 12 GYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQ-----EGTV--LVVSPL--LSLmedQVTqlkyvvknr 82
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRldpsrPRAPqaLILAPTreLAL---QVA--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 83 viafnsfrtlhekrEAMKRLASYKFIFV---------SPEmlqsellIRELKK-VHI----------------------S 130
Cdd:COG0513 89 --------------EELRKLAKYLGLRVatvyggvsiGRQ-------IRALKRgVDIvvatpgrlldliergaldlsgvE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 131 LFVVDEAhcisqwgyD------FRPDykklnvvIENIgsptvLALT----------ATATKDVlRDIAESLnLENVTQHv 194
Cdd:COG0513 148 TLVLDEA--------DrmldmgFIED-------IERI-----LKLLpkerqtllfsATMPPEI-RKLAKRY-LKNPVRI- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 195 ySIDRPNIA---MEVQFVETIEEKKEALLEQVMYLQGPG--IVYCSSRAWTERLTEYLRGKGVTgVAFYHGGMEHEERML 269
Cdd:COG0513 205 -EVAPENATaetIEQRYYLVDKRDKLELLRRLLRDEDPEraIVFCNTKRGADRLAEKLQKRGIS-AAALHGDLSQGQRER 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446685642 270 IQQQFMNDQLQLVICT--SAFGMGVnkSNTRYIIHFHYPTNIASYLQEIGRAGRDGEPSIAILLCSP 334
Cdd:COG0513 283 ALDAFRNGKIRVLVATdvAARGIDI--DDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTP 347
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
7-336 |
1.47e-20 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 94.58 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 7 LYRWFGYSEFRPGQKGVITD-LLEGKDVIAMLPTGRGKSMCYQLP---GLMQEGTVLVVSPLLSLMEDQVTQLKYVVKNr 82
Cdd:COG1204 14 FLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAilkALLNGGKALYIVPLRALASEKYREFKRDFEE- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 83 vIAFNSFRTLHEKREAMKRLASYKFIFVSPEMLQSelLIRELKKV--HISLFVVDEAHCISqwgydfrpDYKK---LNVV 157
Cdd:COG1204 93 -LGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDS--LLRNGPSWlrDVDLVVVDEAHLID--------DESRgptLEVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 158 IENI----GSPTVLALTATATKdvLRDIAESLNLENVT-------QHVYSIDRPNIAMEvQFVETIEEKKEALLEQVMYL 226
Cdd:COG1204 162 LARLrrlnPEAQIVALSATIGN--AEEIAEWLDAELVKsdwrpvpLNEGVLYDGVLRFD-DGSRRSKDPTLALALDLLEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 227 QGPGIVYCSSRAWTERLTEYLRG------------------------KGVT------------GVAFYHGGMEHEERMLI 270
Cdd:COG1204 239 GGQVLVFVSSRRDAESLAKKLADelkrrltpeereeleelaeellevSEEThtnekladclekGVAFHHAGLPSELRRLV 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446685642 271 QQQFMNDQLQLVICTSAFGMGVNKSNTRYIIH-----FHYPTNIASYLQEIGRAGRDG-EPS-IAILLCSPLD 336
Cdd:COG1204 319 EDAFREGLIKVLVATPTLAAGVNLPARRVIIRdtkrgGMVPIPVLEFKQMAGRAGRPGyDPYgEAILVAKSSD 391
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
191-332 |
2.38e-20 |
|
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: 87.61 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 191 TQHVYSIDRPNIAMEVQFVETIEEKKEALLEQVMYLQG-PGIVYCSSRAWTERLTEYLRGkgvtgVAFYHGGMEHEERML 269
Cdd:cd18795 6 EEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGkPVLVFCSSRKECEKTAKDLAG-----IAFHHAGLTREDREL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446685642 270 IQQQFMNDQLQLVICTSAFGMGVN--------KSNTRYIIHFHYPTNIASYLQEIGRAGR-----DGEpsiAILLC 332
Cdd:cd18795 81 VEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKGYRELSPLEYLQMIGRAGRpgfdtRGE---AIIMT 153
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
214-323 |
3.33e-20 |
|
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: 85.73 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 214 EKKEALLEQVMYLQGP-GIVYCSSRAWTErlTEYLRGKGVTGVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGV 292
Cdd:pfam00271 1 EKLEALLELLKKERGGkVLIFSQTKKTLE--AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 446685642 293 NKSNTRYIIHFHYPTNIASYLQEIGRAGRDG 323
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
12-330 |
6.14e-20 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 92.93 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 12 GYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQEGTV-------------LVVSP---LLSLMEDQVTQL 75
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIrsghpseqrnplaMVLTPtreLCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 76 --------KYVVKNRVIAfnsfRTLHEKREAMKrlasykFIFVSPEMLQSELLIRELKKVHISLFVVDEAHCISQWGydF 147
Cdd:PLN00206 220 gkglpfktALVVGGDAMP----QQLYRIQQGVE------LIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG--F 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 148 RPDYKKLnvvIENIGSPTVLALTATATKDVLRdIAESLNLENVTQHVYSIDRPNIAME--VQFVETiEEKKEALLEQVM- 224
Cdd:PLN00206 288 RDQVMQI---FQALSQPQVLLFSATVSPEVEK-FASSLAKDIILISIGNPNRPNKAVKqlAIWVET-KQKKQKLFDILKs 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 225 --YLQGPGIVYCSSRAWTERLTEYLRGkgVTGV--AFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYI 300
Cdd:PLN00206 363 kqHFKPPAVVFVSSRLGADLLANAITV--VTGLkaLSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQV 440
|
330 340 350
....*....|....*....|....*....|
gi 446685642 301 IHFHYPTNIASYLQEIGRAGRDGEPSIAIL 330
Cdd:PLN00206 441 IIFDMPNTIKEYIHQIGRASRMGEKGTAIV 470
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
231-331 |
1.04e-16 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 76.91 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 231 IVYCSSRAWTERLTEYLR------GKGVTGVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIHFH 304
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKarlveeGPLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*..
gi 446685642 305 YPTNIASYLQEIGRAGRDGEPSIAILL 331
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
207-332 |
1.20e-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: 76.39 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 207 QFVETI--EEKKEALLEQVMYLQGPG--IVYCSSRAWTERLTEYLRGKGVTgVAFYHGGMEHEERMLIQQQFMNDQLQLV 282
Cdd:cd18787 3 QLYVVVeeEEKKLLLLLLLLEKLKPGkaIIFVNTKKRVDRLAELLEELGIK-VAALHGDLSQEERERALKKFRSGKVRVL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446685642 283 ICTSAFGMGVNKSNTRYIIHFHYPTNIASYLQEIGRAGRDGEPSIAILLC 332
Cdd:cd18787 82 VATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
15-466 |
6.07e-16 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 80.45 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 15 EFRPGQKGVITDLL-----EGKDVIAMLPTGRGKS----MCYQlpGLMQEGTVLVVSPLLSLMEdqvtQLKyvvknrvIA 85
Cdd:COG1061 80 ELRPYQQEALEALLaalerGGGRGLVVAPTGTGKTvlalALAA--ELLRGKRVLVLVPRRELLE----QWA-------EE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 86 FNSFRTLHEKREAMKRLaSYKFIFVSPEMLQSELLIRELKKvHISLFVVDEAHCISqwgydfRPDYKKlnvVIENIGSPT 165
Cdd:COG1061 147 LRRFLGDPLAGGGKKDS-DAPITVATYQSLARRAHLDELGD-RFGLVIIDEAHHAG------APSYRR---ILEAFPAAY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 166 VLALTAT------ATKDVLR--------DIAESLNLENVTQHVYSIDRPNIAMEVQFVETIEEK-----------KEALL 220
Cdd:COG1061 216 RLGLTATpfrsdgREILLFLfdgivyeySLKEAIEDGYLAPPEYYGIRVDLTDERAEYDALSERlrealaadaerKDKIL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 221 EQVM---YLQGPGIVYCSSRAWTERLTEYLRGKGVTgVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNT 297
Cdd:COG1061 296 RELLrehPDDRKTLVFCSSVDHAEALAELLNEAGIR-AAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 298 RYIIhFHYPT-NIASYLQEIGRAGR---------------DGEPSIAILLCSPLDHDLPISIIEDELPSQSQIQFLFSLL 361
Cdd:COG1061 375 DVAI-LLRPTgSPREFIQRLGRGLRpapgkedalvydfvgNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKP 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 362 ------QERMFQTKELPIEEVEEICYNAARFNEQYWRFIRYHLEQLGIIQQRKLMLESLSDEIMTRLIAEVEIRLRNKYS 435
Cdd:COG1061 454 alevkgELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLL 533
|
490 500 510
....*....|....*....|....*....|.
gi 446685642 436 ELENMKSWIQVKGCRREYLLQQFGYRKEGEL 466
Cdd:COG1061 534 LLLELLELLAALLRLEELAALLLKELLRAAL 564
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
30-174 |
4.37e-15 |
|
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: 72.44 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 30 GKDVIAMLPTGRGKSMCYQLP----GLMQEGTVLVVSPLLSLMEDQVTQLK--YVVKNRVIAFNSFRTLHEKREamKRLA 103
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAalllLLKKGKKVLVLVPTKALALQTAERLRelFGPGIRVAVLVGGSSAEEREK--NKLG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446685642 104 SYKFIFVSPEMLQSELLIRELKKVH-ISLFVVDEAHCISQWGYDFRPDYkklnVVIENIGSPTVLALTATAT 174
Cdd:cd00046 79 DADIIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALILD----LAVRKAGLKNAQVILLSAT 146
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
1-336 |
3.40e-14 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 74.48 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 1 MKLEEYLYRW-FGYSEFRPG--QKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGL------MQEGTVLVVSPLLSLMEdq 71
Cdd:PTZ00424 33 LKLNEDLLRGiYSYGFEKPSaiQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALqlidydLNACQALILAPTRELAQ-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 72 vtQLKYVVKnrviAFNSFRTLH--------EKREAMKRLASYKFIFV-SPEMLQSELLIRELKKVHISLFVVDEAHCISQ 142
Cdd:PTZ00424 111 --QIQKVVL----ALGDYLKVRchacvggtVVRDDINKLKAGVHMVVgTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 143 WGYD------FRPDYKKLNVVIENIGSPT-VLALTATATKDVLRDIA--ESLNLENVTQHVYSIDRPNIAMEvqfveTIE 213
Cdd:PTZ00424 185 RGFKgqiydvFKKLPPDVQVALFSATMPNeILELTTKFMRDPKRILVkkDELTLEGIRQFYVAVEKEEWKFD-----TLC 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 214 EkkeaLLEQVMYLQGpgIVYCSSRAWTERLTEYLRGKGVTgVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVN 293
Cdd:PTZ00424 260 D----LYETLTITQA--IIYCNTRRKVDYLTKKMHERDFT-VSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGID 332
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446685642 294 KSNTRYIIHFHYPTNIASYLQEIGRAGRDGEPSIAILLCSPLD 336
Cdd:PTZ00424 333 VQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDD 375
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
28-323 |
2.20e-13 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 72.50 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 28 LEGKDVIAMLPTGRGKSMCYQLPG--------LMQEG---TVLVVSPLLSLMEDqvtqlkyvVKNRVIAFNSFRTLHE-- 94
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPTRELAEQ--------IREQCNKFGASSKIRNtv 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 95 ------KREAMKRLASYKFIFVS-P----EMLQSEllIRELKKVhiSLFVVDEAHCISQWGydFRPDYKKLnvvIENIgS 163
Cdd:PTZ00110 237 ayggvpKRGQIYALRRGVEILIAcPgrliDFLESN--VTNLRRV--TYLVLDEADRMLDMG--FEPQIRKI---VSQI-R 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 164 P--TVLALTATATKDVlRDIAESLNLENVTQ-HVYSIDRP---NIAMEVQFVETIEEKKE--ALLEQVMYLQGPGIVYCS 235
Cdd:PTZ00110 307 PdrQTLMWSATWPKEV-QSLARDLCKEEPVHvNVGSLDLTachNIKQEVFVVEEHEKRGKlkMLLQRIMRDGDKILIFVE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 236 SRAWTERLTEYLRGKGVTGVAFyHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIHFHYPTNIASYLQE 315
Cdd:PTZ00110 386 TKKGADFLTKELRLDGWPALCI-HGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHR 464
|
....*...
gi 446685642 316 IGRAGRDG 323
Cdd:PTZ00110 465 IGRTGRAG 472
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
12-329 |
1.55e-09 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 59.93 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 12 GYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCY---------QLP----GLMQEGTVLVVSP----LLSLMEDQVTQ 74
Cdd:PRK01297 106 GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFlisiinqllQTPppkeRYMGEPRALIIAPtrelVVQIAKDAAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 75 LKYVVKNrVIAFNSFRTLHEKREAMKrlASYKFIFV-SPEMLqseLLIRELKKVH---ISLFVVDEAHCISQWGydFRPD 150
Cdd:PRK01297 186 TKYTGLN-VMTFVGGMDFDKQLKQLE--ARFCDILVaTPGRL---LDFNQRGEVHldmVEVMVLDEADRMLDMG--FIPQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 151 YKKLNVVIENIGSPTVLALTATATKDVLrDIA------------ESLNL--ENVTQHVYSIDRPNIAMEVQFVETIEEkk 216
Cdd:PRK01297 258 VRQIIRQTPRKEERQTLLFSATFTDDVM-NLAkqwttdpaiveiEPENVasDTVEQHVYAVAGSDKYKLLYNLVTQNP-- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 217 ealLEQVMylqgpgiVYCSSRAWTERLTEYLRGKGVTgVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSN 296
Cdd:PRK01297 335 ---WERVM-------VFANRKDEVRRIEERLVKDGIN-AAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
|
330 340 350
....*....|....*....|....*....|...
gi 446685642 297 TRYIIHFHYPTNIASYLQEIGRAGRDGEPSIAI 329
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSI 436
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
215-321 |
4.30e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 59.08 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 215 KKEALLEQVMYLQGPG---IVYCSSRAWTERLTEYLRGKGVtGVAFYHGGMEHEERMLIQQQFMNDQ--LQLVICTSAFG 289
Cdd:COG0553 534 KLEALLELLEELLAEGekvLVFSQFTDTLDLLEERLEERGI-EYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGG 612
|
90 100 110
....*....|....*....|....*....|..
gi 446685642 290 MGVNKSNTRYIIHFHYPTNIASYLQEIGRAGR 321
Cdd:COG0553 613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHR 644
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
277-332 |
1.18e-08 |
|
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: 51.94 E-value: 1.18e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446685642 277 DQLQLVICTSAFGMGVNKSNTRYIIHFHYPTNIASYLQEIGRAGRDG-EPSIAILLC 332
Cdd:cd18785 21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
209-323 |
2.49e-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: 52.48 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 209 VETIEEKKEALLEQVMYLQGPG---IVYCSSRAWTERLTEYLRGKGVTgVAFYHGGMEHEERMLIQQQFMNDQ--LQLVI 283
Cdd:cd18793 6 EEVVSGKLEALLELLEELREPGekvLIFSQFTDTLDILEEALRERGIK-YLRLDGSTSSKERQKLVDRFNEDPdiRVFLL 84
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446685642 284 CTSAFGMGVNKSNTRYIIHFHYPTNIASYLQEIGRAGRDG 323
Cdd:cd18793 85 STKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIG 124
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
24-138 |
3.59e-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: 53.36 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 24 ITDLLEGKDVIAMLPTGRGKSMCYQLP---GLMQE--GTVLVVSPLLSLMEDQVTQLKYVVKN--RVIAFNSF--RTLHE 94
Cdd:cd17923 9 IEAARAGRSVVVTTGTASGKSLCYQLPileALLRDpgSRALYLYPTKALAQDQLRSLRELLEQlgLGIRVATYdgDTPRE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446685642 95 KREAMKRlASYKFIFVSPEMLQSELLIRELKKVHIS----LFVVDEAH 138
Cdd:cd17923 89 ERRAIIR-NPPRILLTNPDMLHYALLPHHDRWARFLrnlrYVVLDEAH 135
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1-321 |
4.45e-08 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 55.98 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 1 MKLEEY--------LYRWFGYSEFRPGQ-KGVITDLLEGKDVIAMLPTGRGKSMCYQLP---GLMQEG--TVLVVsPLLS 66
Cdd:PRK00254 1 MKVDELrvderikrVLKERGIEELYPPQaEALKSGVLEGKNLVLAIPTASGKTLVAEIVmvnKLLREGgkAVYLV-PLKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 67 LMEDQVTQLKYVVKnrvIAFNSFRTLHEKREAMKRLASYKFIFVSPEMLQSEL-----LIRELKkvhisLFVVDEAHCIS 141
Cdd:PRK00254 80 LAEEKYREFKDWEK---LGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLrhgssWIKDVK-----LVVADEIHLIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 142 QwgydfRPDYKKLNVVIENI-GSPTVLALTATATKDvlRDIAESLNLENVTQH---------VY----------SIDRPN 201
Cdd:PRK00254 152 S-----YDRGATLEMILTHMlGRAQILGLSATVGNA--EELAEWLNAELVVSDwrpvklrkgVFyqgflfwedgKIERFP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 202 IAMEVQFVETIEEKKEALL--------EQVM---------YLQGPGIVYCSSRA-------WTERLTEYLRGkgvtGVAF 257
Cdd:PRK00254 225 NSWESLVYDAVKKGKGALVfvntrrsaEKEAlelakkikrFLTKPELRALKELAdsleenpTNEKLKKALRG----GVAF 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446685642 258 YHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIH--FHYPT------NIASYLQEIGRAGR 321
Cdd:PRK00254 301 HHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRdtKRYSNfgwediPVLEIQQMMGRAGR 372
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
12-350 |
2.22e-07 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 53.31 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 12 GYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGL------MQEGTVLVVSPLLSLMEdQVTQL-----KYVVK 80
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTRELAV-QVAEAmtdfsKHMRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 81 NRVIAFNSFRTLHEKREAMKRLAsyKFIFVSPEMLQSELLIRELKKVHISLFVVDEAHCISQWGydFRPDykklnvvIEN 160
Cdd:PRK11634 104 VNVVALYGGQRYDVQLRALRQGP--QIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG--FIED-------VET 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 161 I------GSPTVLaLTATA-------TKDVLRDIAESLNLENVTQhvysidRPNIAMEVQFVETIeEKKEALleqVMYLQ 227
Cdd:PRK11634 173 ImaqipeGHQTAL-FSATMpeairriTRRFMKEPQEVRIQSSVTT------RPDISQSYWTVWGM-RKNEAL---VRFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 228 G----PGIVYCSSRAWTERLTEYLRGKGVTGVAFyHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIHF 303
Cdd:PRK11634 242 AedfdAAIIFVRTKNATLEVAEALERNGYNSAAL-NGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446685642 304 HYPTNIASYLQEIGRAGRDGEPSIAIL--------LCSPLDHDLPISIIEDELPS 350
Cdd:PRK11634 321 DIPMDSESYVHRIGRTGRAGRAGRALLfvenrerrLLRNIERTMKLTIPEVELPN 375
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
27-190 |
1.11e-06 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 48.87 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 27 LLEGKDVIAMLPTGRGKSMCYQL---PGLMQEGTVLVVSPLLSLMEDqvtqlKYvvknrviafNSFRTLHEK-------- 95
Cdd:cd18028 14 LLKGENLLISIPTASGKTLIAEMamvNTLLEGGKALYLVPLRALASE-----KY---------EEFKKLEEIglkvgist 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 96 ---REAMKRLASYKFIFVSPEMLQSEL-----LIRElkkvhISLFVVDEAHCISqwgydfrpDYKK---LNVVIENI--- 161
Cdd:cd18028 80 gdyDEDDEWLGDYDIIVATYEKFDSLLrhspsWLRD-----VGVVVVDEIHLIS--------DEERgptLESIVARLrrl 146
|
170 180 190
....*....|....*....|....*....|
gi 446685642 162 -GSPTVLALTATATKdvLRDIAESLNLENV 190
Cdd:cd18028 147 nPNTQIIGLSATIGN--PDELAEWLNAELV 174
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
231-320 |
4.79e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 49.54 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 231 IVYCSSRAWTERLTEYL--------------------------------RGKGVTGVAFYHGGMEHEERMLIQQQFMNDQ 278
Cdd:PRK09751 248 IVFTNSRGLAEKLTARLnelyaarlqrspsiavdaahfestsgatsnrvQSSDVFIARSHHGSVSKEQRAITEQALKSGE 327
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446685642 279 LQLVICTSAFGMGVNKSNTRYIIHFHYPTNIASYLQEIGRAG 320
Cdd:PRK09751 328 LRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
15-172 |
6.50e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.13 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 15 EFRPGQKGVITDLLEG-----KDVIAMLPTGRGKSMC-----YQLPGLMQEGTVLVVSPLLSLMEdqvtQLKYVVKNRVI 84
Cdd:pfam04851 3 ELRPYQIEAIENLLESikngqKRGLIVMATGSGKTLTaakliARLFKKGPIKKVLFLVPRKDLLE----QALEEFKKFLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 85 AFNSFRTLHEKREAMKRLASYKFIFVSPEMLQSELLIRELKKV--HISLFVVDEAHCISqwgydfRPDYKKlnvVIENIG 162
Cdd:pfam04851 79 NYVEIGEIISGDKKDESVDDNKIVVTTIQSLYKALELASLELLpdFFDVIIIDEAHRSG------ASSYRN---ILEYFK 149
|
170
....*....|
gi 446685642 163 SPTVLALTAT 172
Cdd:pfam04851 150 PAFLLGLTAT 159
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
241-323 |
1.00e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 48.34 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 241 ERLTEYLRgkgvTGVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVN--------KSNTRY-IIHFHYPTNIaS 311
Cdd:PRK01172 278 DSLNEMLP----HGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNlparlvivRDITRYgNGGIRYLSNM-E 352
|
90
....*....|..
gi 446685642 312 YLQEIGRAGRDG 323
Cdd:PRK01172 353 IKQMIGRAGRPG 364
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
56-172 |
1.32e-05 |
|
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: 45.63 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 56 GTVLVVSPLlSLMEDQVTQLKYVVKN-RVIAFNSFRTLHEKREAMKRLASYKFIFVSPEMLQSEllIRELKKVHISLFVV 134
Cdd:cd17919 51 GPVLVVCPL-SVLENWEREFEKWTPDlRVVVYHGSQRERAQIRAKEKLDKFDVVLTTYETLRRD--KASLRKFRWDLVVV 127
|
90 100 110
....*....|....*....|....*....|....*...
gi 446685642 135 DEAHCISQWGydfrpdyKKLNVVIENIGSPTVLALTAT 172
Cdd:cd17919 128 DEAHRLKNPK-------SQLSKALKALRAKRRLLLTGT 158
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
27-191 |
1.49e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 45.58 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 27 LLEGKDVIAMlPTGRGKS------MCYQLPglMQEGTVLVVSPLLSLMEDQVTQLKYV--VKNRVIAFNSfRTLHEKREa 98
Cdd:cd18035 14 ALNGNTLIVL-PTGLGKTiiailvAADRLT--KKGGKVLILAPSRPLVEQHAENLKRVlnIPDKITSLTG-EVKPEERA- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 99 mKRLASYKFIFVSPEMLQSELLIRELKKVHISLFVVDEAH-CISQWGYDF-RPDYKKlnvvieNIGSPTVLALTAT--AT 174
Cdd:cd18035 89 -ERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHhAVGNYAYVYiAHRYKR------EANNPLILGLTASpgSD 161
|
170
....*....|....*..
gi 446685642 175 KDVLRDIAESLNLENVT 191
Cdd:cd18035 162 KEKIMEICENLGIEHIE 178
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
27-323 |
3.15e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 46.49 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 27 LLEGKDVIAMLPTGRGKSMCYQLPGLMQ---EGTVLVVSPLLSLMEDQVTQLK----YVVknRV-IAFNSFrtlhEKREA 98
Cdd:PRK02362 36 LLDGKNLLAAIPTASGKTLIAELAMLKAiarGGKALYIVPLRALASEKFEEFErfeeLGV--RVgISTGDY----DSRDE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 99 mkRLASYKFIFVSPEMLQSelLIRE----LKKvhISLFVVDEAHCIsqwgyDFRPDYKKLNVVIE-----NIGSpTVLAL 169
Cdd:PRK02362 110 --WLGDNDIIVATSEKVDS--LLRNgapwLDD--ITCVVVDEVHLI-----DSANRGPTLEVTLAklrrlNPDL-QVVAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 170 TATATKDvlRDIAESLNLENVT---------QHVYSIDRPNIAMEVQFVETiEEKKEAL------LEQvmylQGPGIVYC 234
Cdd:PRK02362 178 SATIGNA--DELADWLDAELVDsewrpidlrEGVFYGGAIHFDDSQREVEV-PSKDDTLnlvldtLEE----GGQCLVFV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 235 SSR------------AWTERLT-----------EYLRGKGVT------------GVAFYHGGMEHEERMLIQQQFMNDQL 279
Cdd:PRK02362 251 SSRrnaegfakraasALKKTLTaaeraelaelaEEIREVSDTetskdladcvakGAAFHHAGLSREHRELVEDAFRDRLI 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446685642 280 QLVICTSAFGMGVNKSNTRYIIHfHY----------PTNIASYLQEIGRAGRDG 323
Cdd:PRK02362 331 KVISSTPTLAAGLNLPARRVIIR-DYrrydggagmqPIPVLEYHQMAGRAGRPG 383
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-137 |
4.98e-05 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 44.12 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 12 GYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLM------QEGTV--LVVSPLLSLMEDQVTQLKYVVKNRV 83
Cdd:cd17957 9 GYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQklgkprKKKGLraLILAPTRELASQIYRELLKLSKGTG 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 84 IAFNSFRTLHEKREAMKRLASYKF-IFVSPEMlqseLLIRELKKVHISL-----FVVDEA 137
Cdd:cd17957 89 LRIVLLSKSLEAKAKDGPKSITKYdILVSTPL----RLVFLLKQGPIDLssveyLVLDEA 144
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
231-331 |
6.72e-05 |
|
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: 43.02 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 231 IVYCSSRAWTERLTEYLR---GKGVTGVAFY--HGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIHFHY 305
Cdd:cd18796 42 LVFTNTRSQAERLAQRLRelcPDRVPPDFIAlhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90 100
....*....|....*....|....*..
gi 446685642 306 PTNIASYLQEIGRAG-RDGEPSIAILL 331
Cdd:cd18796 122 PKSVARLLQRLGRSGhRPGAASKGRLV 148
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
14-172 |
1.00e-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: 43.58 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 14 SEFRPGQKGVITDLLEGKDVIAMLPTGRGKS-----MC----YQLPGlMQEGTVLVVSPLLSLMEDQVTQLKYVV---KN 81
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPA-GRKGKVVFLANKVPLVEQQKEVFRKHFerpGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 82 RVIAFnSFRTLHEKReAMKRLASYKFIFVSPEMLQSELL-IRELKKVHISLFVVDEAH-CISQWGYD---FRPDYKKLNV 156
Cdd:cd17927 80 KVTGL-SGDTSENVS-VEQIVESSDVIIVTPQILVNDLKsGTIVSLSDFSLLVFDECHnTTKNHPYNeimFRYLDQKLGS 157
|
170
....*....|....*.
gi 446685642 157 VIENigsPTVLALTAT 172
Cdd:cd17927 158 SGPL---PQILGLTAS 170
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
15-142 |
1.29e-04 |
|
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: 43.02 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 15 EFRPGQKGVITDL-LEGKDVIAMLPTGRGKSMCYQLPGLM----QEGTVLVVSPLLSLMeDQVTQ-----LKYVVKNrVI 84
Cdd:cd17921 1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRalatSGGKAVYIAPTRALV-NQKEAdlrerFGPLGKN-VG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446685642 85 AFNSFRTlhekrEAMKRLASYKFIFVSPEMLQSELL-IRELKKVHISLFVVDEAHCISQ 142
Cdd:cd17921 79 LLTGDPS-----VNKLLLAEADILVATPEKLDLLLRnGGERLIQDVRLVVVDEAHLIGD 132
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
3-137 |
2.74e-04 |
|
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: 41.93 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 3 LEEYLYRWFGYSEFRPgQKGVITDLLEGKDVIAMLPTGRGKS---MCYQLPGLMQEGTVLVVSPLLSLMEDQVTQL---- 75
Cdd:cd17924 6 FEEFFKKKTGFPPWGA-QRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSLYLASKGKRSYLIFPTKSLVKQAYERLskya 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446685642 76 -KYVVKNRVIAFNSFRTLHEKREAMKRLASYKF-IFVSPEMLQSElLIRELKKVHISLFVVDEA 137
Cdd:cd17924 85 eKAGVEVKILVYHSRLKKKEKEELLEKIEKGDFdILVTTNQFLSK-NFDLLSNKKFDFVFVDDV 147
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
16-172 |
3.50e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 40.75 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 16 FRPGQKGVITDLLEGKD----VIAMlPTGRGKSMC-YQLPGLMQEGTVLVVSPLLSLMEDqvtqlkyvVKNRVIAFNSFR 90
Cdd:cd17926 1 LRPYQEEALEAWLAHKNnrrgILVL-PTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQ--------WKERFEDFLGDS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 91 TLHE-KREAMKRLASYKFIFVSPEMLQSELLIRELKKVHISLFVVDEAHCISQwgydfrpdyKKLNVVIENIGSPTVLAL 169
Cdd:cd17926 72 SIGLiGGGKKKDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPA---------KTFSEILKELNAKYRLGL 142
|
...
gi 446685642 170 TAT 172
Cdd:cd17926 143 TAT 145
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
11-50 |
4.10e-04 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 41.79 E-value: 4.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446685642 11 FGYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLP 50
Cdd:cd17960 8 LGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIP 47
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
12-50 |
5.14e-04 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 5.14e-04
10 20 30
....*....|....*....|....*....|....*....
gi 446685642 12 GYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLP 50
Cdd:cd17955 18 GIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP 56
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
27-176 |
5.85e-04 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 41.30 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 27 LLEGKDVIAMLPTGRGKSMCYQLPGLM-------QEGT-----VLVVSPLLSL---MEDQVTqlKYVVKN-RVIAFNSFR 90
Cdd:cd17958 24 ILQGIDLIGVAQTGTGKTLAYLLPGFIhldlqpiPREQrngpgVLVLTPTRELalqIEAECS--KYSYKGlKSVCVYGGG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 91 TLHEKREAMKRLAsyKFIFVSPEMLQSELLIRELKKVHISLFVVDEAHCISQWGY---------DFRPDykKLNVVIENI 161
Cdd:cd17958 102 NRNEQIEDLSKGV--DIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFepqirkillDIRPD--RQTIMTSAT 177
|
170
....*....|....*
gi 446685642 162 GSPTVLALTATATKD 176
Cdd:cd17958 178 WPDGVRRLAQSYLKD 192
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
1-50 |
5.90e-04 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 41.14 E-value: 5.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446685642 1 MKLEEYLYRWF---GYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLP 50
Cdd:cd17959 6 MGLSPPLLRAIkkkGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIP 58
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
241-331 |
7.17e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 40.41 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 241 ERLTEYLRGKGVtgVAFYHGGMEHEERMLIQQQFMNDQLQLVICTSAFGMGVNKSNTRYIIHFHYPTNIASYLQEI-GRA 319
Cdd:cd18811 52 EYLKERFRPELN--VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRV 129
|
90
....*....|..
gi 446685642 320 GRDGEPSIAILL 331
Cdd:cd18811 130 GRGDHQSYCLLV 141
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
14-203 |
1.75e-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: 39.77 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 14 SEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQL---------PGLMQEGTVLVVSPLLSLMEDQVTQ-LKYVvkNRV 83
Cdd:cd18036 1 LELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYicrhhlekrRSAGEKGRVVVLVNKVPLVEQQLEKfFKYF--RKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 84 IAFNSFRTLHEKREAMKRLA-SYKFIFVSPEMLQSELL-IRELKKVHISLF---VVDEAH-CISQWGYD---FRPDYKKL 154
Cdd:cd18036 79 YKVTGLSGDSSHKVSFGQIVkASDVIICTPQILINNLLsGREEERVYLSDFsllIFDECHhTQKEHPYNkimRMYLDKKL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446685642 155 NvviENIGSPTVLALTATATKDVLRDIAESLNlenvtqHVY----SIDRPNIA 203
Cdd:cd18036 159 S---SQGPLPQILGLTASPGVGGARSFEEALE------HILklcaNLDASVIA 202
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
1-137 |
2.72e-03 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 39.23 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 1 MKLEEYLYRW-FGYSEFRPG--QKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQ------EGTVLVVSPLLSL---M 68
Cdd:cd17939 2 MGLSEDLLRGiYAYGFEKPSaiQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRidttvrETQALVLAPTRELaqqI 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446685642 69 EDQVTQLKYVVKNRVIAFNSFRTLHEKREAMKrlASYKFIFVSPEMLQSELLIRELKKVHISLFVVDEA 137
Cdd:cd17939 82 QKVVKALGDYMGVKVHACIGGTSVREDRRKLQ--YGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEA 148
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
1-178 |
3.99e-03 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 38.58 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 1 MKLEEYLYRW-FGYSEFRPG--QKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQ------EGTVLVVSPLLSLmedq 71
Cdd:cd18046 4 MNLKESLLRGiYAYGFEKPSaiQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQidtslkATQALVLAPTREL---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685642 72 VTQLKYVvknrVIAFNSFRTLH--------EKREAMKRLASYKFIFV-SP----EMLQSelliRELKKVHISLFVVDEAH 138
Cdd:cd18046 80 AQQIQKV----VMALGDYMGIKchaciggtSVRDDAQKLQAGPHIVVgTPgrvfDMINR----RYLRTDYIKMFVLDEAD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446685642 139 CISQWG-----YDFrpdYKKLNVVIEnigsptVLALTATATKDVL 178
Cdd:cd18046 152 EMLSRGfkdqiYDI---FQKLPPDTQ------VVLLSATMPNDVL 187
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-54 |
7.31e-03 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 37.81 E-value: 7.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446685642 12 GYSEFRPGQKGVITDLLEGKDVIAMLPTGRGKSMCYQLPGLMQ 54
Cdd:cd00268 9 GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEK 51
|
|
| |
