|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
2-428 |
3.00e-166 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 477.33 E-value: 3.00e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 2 LHDILRNKFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPTYLSGKPTLIISPLISLMDDQVMQLKINGEkR 81
Cdd:COG0514 5 ALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGI-R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 82 VTCIHSGMDEIEKKHNIKCLLHS--RFIFLSPEFLLQPSNFKLISMIDFGMIVLDEAHCLSEWGYDFRPHYALIGKVTKH 159
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRAGelKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 160 FKEAVVLALTATAPPHLQDDLTEMLAIQ-FNVIKTTMNRPNISFKHLNFHDDeDKIEWLLPFLQQ--SGPTIIYVSSKKM 236
Cdd:COG0514 164 LPNVPVLALTATATPRVRADIAEQLGLEdPRVFVGSFDRPNLRLEVVPKPPD-DKLAQLLDFLKEhpGGSGIVYCLSRKK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 237 CLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTIIHFHLSTSPSNYIQEIGRAG 316
Cdd:COG0514 243 VEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 317 RDGELSQAISLFQPDDKYILETLLFADMITEEdvqnfeigeflapdkqdvlttlhsfysigaLKQIfkqsfKRKQLGffR 396
Cdd:COG0514 323 RDGLPAEALLLYGPEDVAIQRFFIEQSPPDEE------------------------------RKRV-----ERAKLD--A 365
|
410 420 430
....*....|....*....|....*....|..
gi 581937761 397 MIGYCKLDQCRRKYLLEFFGEYPPAQDRCCDN 428
Cdd:COG0514 366 MLAYAETTGCRRQFLLRYFGEELAEPCGNCDN 397
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
4-428 |
1.68e-103 |
|
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: 316.33 E-value: 1.68e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 4 DILRNKFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPTYLSGKPTLIISPLISLMDDQVMQLKINGEKrVT 83
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIP-AT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 84 CIHSGMDEiEKKHNIKCLLHS---RFIFLSPEFLLQPSNF--KLISMIDFGMIVLDEAHCLSEWGYDFRPHYALIGKVTK 158
Cdd:TIGR00614 80 FLNSAQTK-EQQLNVLTDLKDgkiKLLYVTPEKISASNRLlqTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 159 HFKEAVVLALTATAPPHLQDDLTEMLAIQfNVIKTTM--NRPNISF----KHLNFHDDedkiewLLPFLQ--QSGPT-II 229
Cdd:TIGR00614 159 KFPNVPVMALTATASPSVREDILRQLNLL-NPQIFCTsfDRPNLYYevrrKTPKILED------LLRFIRkeFEGKSgII 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 230 YVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTIIHFHLSTSPSNYI 309
Cdd:TIGR00614 232 YCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 310 QEIGRAGRDGELSQAISLFQPDDKYILETllfadMITEEDVQNFeigeflapdkqdvlttlhsfysigalkqifkQSFKR 389
Cdd:TIGR00614 312 QESGRAGRDGLPSECHLFYAPADMNRLRR-----LLMEEPDGNF-------------------------------RTYKL 355
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 581937761 390 KQLgffRMIGYC-KLDQCRRKYLLEFFGE-------YPPAQDRCCDN 428
Cdd:TIGR00614 356 KLY---EMMEYClNSSTCRRLILLSYFGEkgfnksfCIMGTEKCCDN 399
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
4-428 |
2.80e-89 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 283.91 E-value: 2.80e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 4 DILRNKFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPTYLSGKPTLIISPLISLMDDQVMQLKINGEKrVT 83
Cdd:PRK11057 15 QVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVA-AA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 84 CIHSGMDEiEKKHNIKCLLHS---RFIFLSPEFLLQPSNFKLISMIDFGMIVLDEAHCLSEWGYDFRPHYALIGKVTKHF 160
Cdd:PRK11057 94 CLNSTQTR-EQQLEVMAGCRTgqiKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 161 KEAVVLALTATAPPHLQDDLTEMLAIQFNVIK-TTMNRPNISFKHLNFHDDEDKiewLLPFLQ----QSGptIIYVSSKK 235
Cdd:PRK11057 173 PTLPFMALTATADDTTRQDIVRLLGLNDPLIQiSSFDRPNIRYTLVEKFKPLDQ---LMRYVQeqrgKSG--IIYCNSRA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 236 MCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTIIHFHLSTSPSNYIQEIGRA 315
Cdd:PRK11057 248 KVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 316 GRDGELSQAISLFQPDDKYILETLLfadmitEEdvqnfeigeflapdKQDvlttlhsfysiGALKQIfkQSFKRKQLGFF 395
Cdd:PRK11057 328 GRDGLPAEAMLFYDPADMAWLRRCL------EE--------------KPA-----------GQQQDI--ERHKLNAMGAF 374
|
410 420 430
....*....|....*....|....*....|...
gi 581937761 396 rmigyCKLDQCRRKYLLEFFGEYppaQDRCCDN 428
Cdd:PRK11057 375 -----AEAQTCRRLVLLNYFGEG---RQEPCGN 399
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
3-187 |
4.14e-78 |
|
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: 241.67 E-value: 4.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 3 HDILRNKFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPTYLSGKPTLIISPLISLMDDQVMQLKINGeKRV 82
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLG-IRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 83 TCIHSGMDEIEKKHNIKCLLHS--RFIFLSPEFLLQPSNFKLI----SMIDFGMIVLDEAHCLSEWGYDFRPHYALIGKV 156
Cdd:cd17920 80 AALNSTLSPEEKREVLLRIKNGqyKLLYVTPERLLSPDFLELLqrlpERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRL 159
|
170 180 190
....*....|....*....|....*....|.
gi 581937761 157 TKHFKEAVVLALTATAPPHLQDDLTEMLAIQ 187
Cdd:cd17920 160 RRALPGVPILALTATATPEVREDILKRLGLR 190
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
8-436 |
4.48e-62 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 218.23 E-value: 4.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 8 NK--FGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPTYLSGKPTLIISPLISLMDDQVMQLkINGEKRVTCI 85
Cdd:PLN03137 452 NKkvFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNL-LQANIPAASL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 86 HSGMDEIEKKHNIK--CLLHSRF--IFLSPEFLLQPSNfkLISMID-------FGMIVLDEAHCLSEWGYDFRPHYALIG 154
Cdd:PLN03137 531 SAGMEWAEQLEILQelSSEYSKYklLYVTPEKVAKSDS--LLRHLEnlnsrglLARFVIDEAHCVSQWGHDFRPDYQGLG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 155 KVTKHFKEAVVLALTATAPPHLQDDLTEMLAIQFNVI-KTTMNRPNISF----KHLNFHDDEDKiewllpFLQQS----- 224
Cdd:PLN03137 609 ILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVfRQSFNRPNLWYsvvpKTKKCLEDIDK------FIKENhfdec 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 225 GptIIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTIIHFHLSTS 304
Cdd:PLN03137 683 G--IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKS 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 305 PSNYIQEIGRAGRDGELSQAISLFQPDDkYIletlLFADMITEEDVQnfeigeflapdkQDVLTTlhSFYSIGALKQIFK 384
Cdd:PLN03137 761 IEGYHQECGRAGRDGQRSSCVLYYSYSD-YI----RVKHMISQGGVE------------QSPMAM--GYNRMASSGRILE 821
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 581937761 385 QSFKrkqlGFFRMIGYCKLD-QCRRKYLLEFFGEYPPAQD--RCCDNDSNITDIV 436
Cdd:PLN03137 822 TNTE----NLLRMVSYCENEvDCRRFLQLVHFGEKFDSTNckKTCDNCSSSKSLI 872
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
3-187 |
7.19e-58 |
|
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: 189.39 E-value: 7.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 3 HDILRNKFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPTYL----SGKPTLIISPLISLMDDQVMQLK--I 76
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPraI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 77 ngekRVTCIHSGMDEIEKKHNIKcLLHSR---FIFLSPEFLLQPS---NFKLISMIdfGMIVLDEAHCLSEWGYDFRPHY 150
Cdd:cd18018 81 ----KAAALNSSLTREERRRILE-KLRAGevkILYVSPERLVNESfreLLRQTPPI--SLLVVDEAHCISEWSHNFRPDY 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 581937761 151 ALIGKVTKHFKEAV-VLALTATAPPHLQDDLTEMLAIQ 187
Cdd:cd18018 154 LRLCRVLRELLGAPpVLALTATATKRVVEDIASHLGIP 191
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
4-187 |
1.62e-50 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 170.62 E-value: 1.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 4 DILRNKFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPTYLSGKPTLIISPLISLMDDQVMQLKINGEKRVT 83
Cdd:cd18015 8 DTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 84 -CIHSGMDEIEKKH----NIKCLLhsRFIFLSPEFLLQPSNF-----KLISMIDFGMIVLDEAHCLSEWGYDFRPHYALI 153
Cdd:cd18015 88 lNASSSKEHVKWVHaaltDKNSEL--KLLYVTPEKIAKSKRFmskleKAYNAGRLARIAIDEVHCCSQWGHDFRPDYKKL 165
|
170 180 190
....*....|....*....|....*....|....
gi 581937761 154 GKVTKHFKEAVVLALTATAPPHLQDDLTEMLAIQ 187
Cdd:cd18015 166 GILKRQFPNVPILGLTATATSKVLKDVQKILCIQ 199
|
|
| DpdF |
NF041063 |
protein DpdF; |
5-332 |
3.57e-49 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 179.72 E-value: 3.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 5 ILRNKFGFENFK-PGQQEIIESIMS--QQHTLGI-LPTGSGKSLCYQIPTYLSGKP---TLIISPLISLMDDQ------V 71
Cdd:NF041063 130 FLAEALGFTHYRsPGQREAVRAALLapPGSTLIVnLPTGSGKSLVAQAPALLASRQgglTLVVVPTVALAIDQerrareL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 72 MQLKINGEKRVTCIHSGMDEIEKKhNIKCLLHS---RFIFLSPEFL---LQPSNFKLIS--MIdfGMIVLDEAHCLSEWG 143
Cdd:NF041063 210 LRRAGPDLGGPLAWHGGLSAEERA-AIRQRIRDgtqRILFTSPESLtgsLRPALFDAAEagLL--RYLVVDEAHLVDQWG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 144 YDFRPHYALIG-------KVTKHFKEAVVLALTATAPPHLQDDLTEMLAIQ--FNVIKTTMNRPNISFKHLNFHDDEDKI 214
Cdd:NF041063 287 DGFRPEFQLLAglrrsllRLAPSGRPFRTLLLSATLTESTLDTLETLFGPPgpFIVVSAVQLRPEPAYWVAKCDSEEERR 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 215 EWLL--------PFlqqsgptIIYVSSKKMCLNLAQLIYDSGFL-TGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFG 285
Cdd:NF041063 367 ERVLealrhlprPL-------ILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFG 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 581937761 286 MGINKKDIRTIIHfhlSTSPSN---YIQEIGRAGRDGELSQAISLFQPDD 332
Cdd:NF041063 440 LGMDKSDVRTVIH---ACVPETldrFYQEVGRGGRDGKASLSLLIYTPDD 486
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
4-194 |
8.41e-43 |
|
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: 149.54 E-value: 8.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 4 DILRNKFGFENFKPGQQEIIESIMSQQH-TLGILPTGSGKSLCYQIPTYLSGKPTLIISPLISLMDDQVMQLKINGEKRV 82
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVIRSVLEERRdNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 83 tCIHSGMDEIEKKhniKCLLHS-RFIFLSPEFLLqpSNFKLISMID--FGMIVLDEAHCLSEWGYDFRPHYALIGKVTKH 159
Cdd:cd18017 82 -FLGSAQSQNVLD---DIKMGKiRVIYVTPEFVS--KGLELLQQLRngITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNR 155
|
170 180 190
....*....|....*....|....*....|....*
gi 581937761 160 FKEAVVLALTATAPPHLQDDLTEMLAIQFNVIKTT 194
Cdd:cd18017 156 LPNVPIVALTATATPSVRDDIIKNLNLRNPQITCT 190
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
197-328 |
4.59e-40 |
|
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: 140.42 E-value: 4.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 197 RPNIsfkHLNFHDDEDKIEWLLPFLQQS-----GPTIIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFL 271
Cdd:cd18794 1 RPNL---FYSVRPKDKKDEKLDLLKRIKvehlgGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 581937761 272 NNDIPIIVATSAFGMGINKKDIRTIIHFHLSTSPSNYIQEIGRAGRDGELSQAISLF 328
Cdd:cd18794 78 RDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
3-190 |
1.99e-36 |
|
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: 132.98 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 3 HDILRNKFGFENFKPGQQE--IIESIMSQQHTLGILPTGSGKSLCYQIPTYLSGKPTLIISPLISLMDDQVMQLKiNGEK 80
Cdd:cd18014 1 RSTLKKVFGHSDFKSPLQEkaTMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLK-TLKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 81 RVTCIHSGMDEIEKKHNIKCL----LHSRFIFLSPEfLLQPSNFK-----LISMIDFGMIVLDEAHCLSEWGYDFRPHYA 151
Cdd:cd18014 80 RVDSLNSKLSAQERKRIIADLesekPQTKFLYITPE-MAATSSFQpllssLVSRNLLSYLVVDEAHCVSQWGHDFRPDYL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 581937761 152 LIGKVTKHFKEAVVLALTATAPPHLQDDLTEMLAIQFNV 190
Cdd:cd18014 159 RLGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKPV 197
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
2-187 |
8.72e-36 |
|
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: 131.49 E-value: 8.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 2 LHDILRNKFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPTYLSGKPTLIISPLISLMDDQVMQLK------ 75
Cdd:cd18016 5 MMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTsldipa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 76 --INGEKRVTCIHSGMDEIEKKHNIKCLLhsrfiFLSPEFLlqPSNFKLISMID-------FGMIVLDEAHCLSEWGYDF 146
Cdd:cd18016 85 tyLTGDKTDAEATKIYLQLSKKDPIIKLL-----YVTPEKI--SASNRLISTLEnlyerklLARFVIDEAHCVSQWGHDF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 581937761 147 RPHYALIGKVTKHFKEAVVLALTATAPPHLQDDLTEMLAIQ 187
Cdd:cd18016 158 RPDYKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKML 198
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
17-178 |
1.16e-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: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 17 PGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPTY------LSGKPTLIISPLISLMDDQVMQLK---INGEKRVTCIHS 87
Cdd:pfam00270 2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKklgKGLGLKVASLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 88 GMdeiEKKHNIKCLLHSRFIFLSPEFLLQPSNFKlISMIDFGMIVLDEAHCLSEWGydFRPHYALIGKVTKhfKEAVVLA 167
Cdd:pfam00270 82 GD---SRKEQLEKLKGPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMG--FGPDLEEILRRLP--KKRQILL 153
|
170
....*....|.
gi 581937761 168 LTATAPPHLQD 178
Cdd:pfam00270 154 LSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
8-184 |
5.82e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 104.50 E-value: 5.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 8 NKFGFENFKPGQQEIIESIMS-QQHTLGILPTGSGKSLCYQIPTYLSGK-----PTLIISPLISLMDDQVMQLKINGEK- 80
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEALKrgkggRVLVLVPTRELAEQWAEELKKLGPSl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 81 --RVTCIHSGMDEIEKKHNIKcLLHSRFIFLSPEFLLQPSNFKLISMIDFGMIVLDEAHCLSEWGydFRPHYALIGKVTK 158
Cdd:smart00487 82 glKVVGLYGGDSKREQLRKLE-SGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLLP 158
|
170 180
....*....|....*....|....*.
gi 581937761 159 hfKEAVVLALTATAPPHLQDDLTEML 184
Cdd:smart00487 159 --KNVQLLLLSATPPEEIENLLELFL 182
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
212-319 |
1.08e-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: 98.05 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 212 DKIEWLLPFLQQS--GPTIIYVSSKKMcLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGIN 289
Cdd:pfam00271 1 EKLEALLELLKKErgGKVLIFSQTKKT-LEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 581937761 290 KKDIRTIIHFHLSTSPSNYIQEIGRAGRDG 319
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
240-319 |
7.65e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 89.19 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 240 LAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTIIHFHLSTSPSNYIQEIGRAGRDG 319
Cdd:smart00490 3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
19-459 |
3.51e-21 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 96.25 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 19 QQEIIESIMSQ-----QHTLGILPTGSGKSL----CYQipTYLSGKPTLIISPLISLMDdqvmQLKINGEKRVTCIHSGM 89
Cdd:COG1061 85 QQEALEALLAAlerggGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLE----QWAEELRRFLGDPLAGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 90 DEIEKKHNIkcllhsrfIFLSPEFLLQPSNFKLISMiDFGMIVLDEAHCLSEWGYDfrphyaligKVTKHFKEAVVLALT 169
Cdd:COG1061 159 GKKDSDAPI--------TVATYQSLARRAHLDELGD-RFGLVIIDEAHHAGAPSYR---------RILEAFPAAYRLGLT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 170 ATapPHLQDDLTEMLAIQFNV----------------------IKTTMNRPNISFKHLN-------FHDDEDKIEWLLPF 220
Cdd:COG1061 221 AT--PFRSDGREILLFLFDGIvyeyslkeaiedgylappeyygIRVDLTDERAEYDALSerlrealAADAERKDKILREL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 221 LQQSG---PTIIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTII 297
Cdd:COG1061 299 LREHPddrKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 298 HFHLSTSPSNYIQEIGRAgrdgelsqaisLFQPDDKyilETLLFADMITEEdvqnFEIGEFLAPDKQDvlttlHSFYSIG 377
Cdd:COG1061 379 LLRPTGSPREFIQRLGRG-----------LRPAPGK---EDALVYDFVGND----VPVLEELAKDLRD-----LAGYRVE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 378 ALKQIFKQSFKRKQLGFFRMIGYCKLDQCRRKYLLEFFGEYPPAQDRCCDNDSNITDIVILNKKKVIRSIGFDEKLQNLF 457
Cdd:COG1061 436 FLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELL 515
|
..
gi 581937761 458 LR 459
Cdd:COG1061 516 LL 517
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
209-328 |
2.61e-20 |
|
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: 86.41 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 209 DDEDKIEWLLPFLQQS---GPTIIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFG 285
Cdd:cd18787 9 EEEEKKLLLLLLLLEKlkpGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 581937761 286 MGINKKDIRTIIHFHLSTSPSNYIQEIGRAGRDGELSQAISLF 328
Cdd:cd18787 89 RGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
11-354 |
4.34e-19 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 89.05 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 11 GFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIP------TYLSGKP-TLIISP---LISLMDDQVMQLKINGEK 80
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPllqrldPSRPRAPqALILAPtreLALQVAEELRKLAKYLGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 81 RVTCIHSGMD---EIEK-KHN----------IKCLLHSRFIFLSpefllqpsnfklismiDFGMIVLDEA-HCLSEwGyd 145
Cdd:COG0513 101 RVATVYGGVSigrQIRAlKRGvdivvatpgrLLDLIERGALDLS----------------GVETLVLDEAdRMLDM-G-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 146 FRPHyalIGKVTKHF-KEAVVLALTATAPPHLQDDLTEML--AIQFNVIKTTMNRPNIsfKHLNFH-DDEDKIEWLLPFL 221
Cdd:COG0513 162 FIED---IERILKLLpKERQTLLFSATMPPEIRKLAKRYLknPVRIEVAPENATAETI--EQRYYLvDKRDKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 222 QQSGP--TIIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVAT--SAFGMGInkKDIRTII 297
Cdd:COG0513 237 RDEDPerAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdvAARGIDI--DDVSHVI 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581937761 298 HFHLSTSPSNYIQEIG---RAGRDGElsqAISLFQPDDKYILETLL-FADM-ITEEDVQNFE 354
Cdd:COG0513 315 NYDLPEDPEDYVHRIGrtgRAGAEGT---AISLVTPDERRLLRAIEkLIGQkIEEEELPGFE 373
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
225-319 |
7.18e-17 |
|
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: 77.59 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 225 GPTIIYVSSKKMCLNLAQLIydSGFltGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGIN--------------- 289
Cdd:cd18795 44 KPVLVFCSSRKECEKTAKDL--AGI--AFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviikgtqryd 119
|
90 100 110
....*....|....*....|....*....|
gi 581937761 290 KKDIRTIihfhlstSPSNYIQEIGRAGRDG 319
Cdd:cd18795 120 GKGYREL-------SPLEYLQMIGRAGRPG 142
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
2-317 |
4.46e-16 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 80.32 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 2 LHDILRnKFGFENFKPGQQEIIES-IMSQQHTLGILPTGSGKSLCYQIP---TYLSGKPTLIISPLISLMDDQVMQLKIN 77
Cdd:COG1204 11 VIEFLK-ERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAilkALLNGGKALYIVPLRALASEKYREFKRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 78 GEK---RVTcIHSGMDEIEKKhnikcLLHSRFIF-LSPEfllqpsnfKLISMI--------DFGMIVLDEAHCLS----- 140
Cdd:COG1204 90 FEElgiKVG-VSTGDYDSDDE-----WLGRYDILvATPE--------KLDSLLrngpswlrDVDLVVVDEAHLIDdesrg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 141 ---EWgydfrphyaLIGKVTKHFKEAVVLALTATAP-PhlqDDLTEMLAIqfNVIKTT----------MNRPNISFKHLN 206
Cdd:COG1204 156 ptlEV---------LLARLRRLNPEAQIVALSATIGnA---EEIAEWLDA--ELVKSDwrpvplnegvLYDGVLRFDDGS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 207 FHDDEDKIEWLLPFLQQSGPTIIYVSSKKMCLNLAQLIYD--SGFLT--------------------------------- 251
Cdd:COG1204 222 RRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADelKRRLTpeereeleelaeellevseethtnekladclek 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581937761 252 --GIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGIN-----------KKDIRTIIhfhlstSPSNYIQEIGRAGR 317
Cdd:COG1204 302 gvAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNlparrviirdtKRGGMVPI------PVLEFKQMAGRAGR 374
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
11-339 |
1.51e-15 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 78.68 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 11 GFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIP------TYLSGKPT-------LIISP---LISLMDDQVMQL 74
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrccTIRSGHPSeqrnplaMVLTPtreLCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 75 KiNGEKRVTCIHSGMDEIEKK-HNIKCLLHsrFIFLSPEFLLQPSNFKLISMIDFGMIVLDEAHCLSEWGydFRPHyalI 153
Cdd:PLN00206 220 G-KGLPFKTALVVGGDAMPQQlYRIQQGVE--LIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG--FRDQ---V 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 154 GKVTKHFKEAVVLALTATAPPHLQDDLTEMLAIQFNVIKTTMNRPNISFKHLN-FHDDEDKIEWLLPFLQQSG----PTI 228
Cdd:PLN00206 292 MQIFQALSQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAiWVETKQKKQKLFDILKSKQhfkpPAV 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 229 IYVSSKKMCLNLAQLIydsGFLTGI----YHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTIIHFHLSTS 304
Cdd:PLN00206 372 VFVSSRLGADLLANAI---TVVTGLkalsIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNT 448
|
330 340 350
....*....|....*....|....*....|....*
gi 581937761 305 PSNYIQEIGRAGRDGELSQAISLFQPDDKYILETL 339
Cdd:PLN00206 449 IKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPEL 483
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
31-171 |
5.82e-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: 71.67 E-value: 5.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 31 HTLGILPTGSGKSLCYQIPTYLS----GKPTLIISPLISLMDDQVMQLK--INGEKRVTCIHSGMDEIEKKHNIkcLLHS 104
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRelFGPGIRVAVLVGGSSAEEREKNK--LGDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581937761 105 RFIFLSPEFLLQPSNFKLISMI-DFGMIVLDEAHCLSEWGYDFRPHYALIGKvtKHFKEAVVLALTAT 171
Cdd:cd00046 81 DIIIATPDMLLNLLLREDRLFLkDLKLIIVDEAHALLIDSRGALILDLAVRK--AGLKNAQVILLSAT 146
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
27-334 |
7.62e-15 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 76.74 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 27 MSQQHTLGILPTGSGKSLCYQIPT-----------YLSGKPTLIISP---LISLMDDQVMQLKINGEKRVTCIHSGMDE- 91
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAivhinaqpllrYGDGPIVLVLAPtreLAEQIREQCNKFGASSKIRNTVAYGGVPKr 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 92 ---IEKKHNIKCLLH--SRFIflspEFLlqPSNFKLISMIDFgmIVLDEAHCLSEWGydFRPHyalIGKVTKHFK-EAVV 165
Cdd:PTZ00110 245 gqiYALRRGVEILIAcpGRLI----DFL--ESNVTNLRRVTY--LVLDEADRMLDMG--FEPQ---IRKIVSQIRpDRQT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 166 LALTATAPPHLQD---DLTEMLAIQFNVIKTTMNR-PNISfKHLNFHDDEDKIEWLLPFLQQ----SGPTIIYVSSKKMC 237
Cdd:PTZ00110 312 LMWSATWPKEVQSlarDLCKEEPVHVNVGSLDLTAcHNIK-QEVFVVEEHEKRGKLKMLLQRimrdGDKILIFVETKKGA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 238 LNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTIIHFHLSTSPSNYIQEIGRAGR 317
Cdd:PTZ00110 391 DFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGR 470
|
330
....*....|....*..
gi 581937761 318 DGELSQAISLFQPdDKY 334
Cdd:PTZ00110 471 AGAKGASYTFLTP-DKY 486
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
209-340 |
4.57e-13 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 70.99 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 209 DDEDKIEWLLPFLQQSGP--TIIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGM 286
Cdd:PRK11776 225 SPDERLPALQRLLLHHQPesCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAAR 304
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 581937761 287 GINKKDIRTIIHFHLSTSPSNYIQEIGRAGRDGELSQAISLFQPDDKY---ILETLL 340
Cdd:PRK11776 305 GLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQranAIEDYL 361
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
1-336 |
6.07e-13 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 70.33 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 1 MLHDIlrNKFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPT-------------YLSGKPTLIISP----L 63
Cdd:PRK01297 98 LMHAI--HDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIinqllqtpppkerYMGEPRALIIAPtrelV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 64 ISLMDDQVMQLKINGEKRVTCIhSGMD-EIEKKHnikclLHSRF---IFLSPEFLL---QPSNFKLiSMIDFgmIVLDEA 136
Cdd:PRK01297 176 VQIAKDAAALTKYTGLNVMTFV-GGMDfDKQLKQ-----LEARFcdiLVATPGRLLdfnQRGEVHL-DMVEV--MVLDEA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 137 HCLSEWGydFRPHYALIGKVTKHFKEAVVLALTATapphLQDDLTEmLAIQFNV------IKTTMNRPNISFKHLNFHDD 210
Cdd:PRK01297 247 DRMLDMG--FIPQVRQIIRQTPRKEERQTLLFSAT----FTDDVMN-LAKQWTTdpaiveIEPENVASDTVEQHVYAVAG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 211 EDKIEWLLPFLQQSG--PTIIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGI 288
Cdd:PRK01297 320 SDKYKLLYNLVTQNPweRVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGI 399
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 581937761 289 NKKDIRTIIHFHLSTSPSNYIQEIGRAGRDGELSQAISLFQPDDKYIL 336
Cdd:PRK01297 400 HIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQL 447
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
4-333 |
2.58e-12 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 68.31 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 4 DILRN--KFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSL-----CYQIPTY-LSGKPTLIISPLISLMDD-QVMQL 74
Cdd:PTZ00424 38 DLLRGiySYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTAtfviaALQLIDYdLNACQALILAPTRELAQQiQKVVL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 75 KINGEKRVTCiHS---GMDEIEKKHNIKCLLHsrFIFLSPEFLLQPSNFKLISMIDFGMIVLDEAHCLSEWGYDFRPHya 151
Cdd:PTZ00424 118 ALGDYLKVRC-HAcvgGTVVRDDINKLKAGVH--MVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIY-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 152 ligKVTKHFKEAVVLAL-TATAPphlqDDLTEmLAIQFN-------VIKTTMNRPNISFKHLNFHDDEDKIEWLLPFLQQ 223
Cdd:PTZ00424 193 ---DVFKKLPPDVQVALfSATMP----NEILE-LTTKFMrdpkrilVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYET 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 224 SGPT--IIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTIIHFHL 301
Cdd:PTZ00424 265 LTITqaIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDL 344
|
330 340 350
....*....|....*....|....*....|..
gi 581937761 302 STSPSNYIQEIGRAGRDGELSQAISLFQPDDK 333
Cdd:PTZ00424 345 PASPENYIHRIGRSGRFGRKGVAINFVTPDDI 376
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
182-327 |
7.27e-11 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 64.20 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 182 EMLAIQFNVIKTTMNRPNISFKhlnfhDDEDKIEWLLPFLQQS--GPTIIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMN 259
Cdd:PRK04537 218 EKLVVETETITAARVRQRIYFP-----ADEEKQTLLLGLLSRSegARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVP 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581937761 260 YQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTIIHFHLSTSPSNYIQEIGRAGRDGELSQAISL 327
Cdd:PRK04537 293 QKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
15-171 |
3.54e-09 |
|
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: 55.39 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 15 FKPGQQEIIESI---MSQQHTLGILPTGSGKSLC-YQIPTYLSGKPTLIISPLISLMDdqvmQLKINGEKRVTCIHSGMD 90
Cdd:cd17926 1 LRPYQEEALEAWlahKNNRRGILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLD----QWKERFEDFLGDSSIGLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 91 EIEKKHNIKCLLH------SRFIFLSPEFLLQPsnfklismiDFGMIVLDEAHclsewgydfrpHYA--LIGKVTKHFKE 162
Cdd:cd17926 77 GGGKKKDFDDANVvvatyqSLSNLAEEEKDLFD---------QFGLLIVDEAH-----------HLPakTFSEILKELNA 136
|
....*....
gi 581937761 163 AVVLALTAT 171
Cdd:cd17926 137 KYRLGLTAT 145
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
8-328 |
3.73e-09 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 58.71 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 8 NKFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPTYLSGKPTLIiSPlislmddQVMQLKINGEKRVTCIHS 87
Cdd:PRK11634 22 NDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELK-AP-------QILVLAPTRELAVQVAEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 88 GMDEIEKKHNIKCL-LHS---------------RFIFLSPEFLLQPSNFKLISMIDFGMIVLDEAHCLSEWGY--DFRph 149
Cdd:PRK11634 94 MTDFSKHMRGVNVVaLYGgqrydvqlralrqgpQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFieDVE-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 150 yALIGKVTKHFKEAVvlaLTATAPPHLQ-------DDLTEmLAIQFNVikTTmnRPNISFKHLNFHDDEdKIEWLLPFLQ 222
Cdd:PRK11634 172 -TIMAQIPEGHQTAL---FSATMPEAIRritrrfmKEPQE-VRIQSSV--TT--RPDISQSYWTVWGMR-KNEALVRFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 223 QSG--PTIIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTIIHFH 300
Cdd:PRK11634 242 AEDfdAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYD 321
|
330 340
....*....|....*....|....*...
gi 581937761 301 LSTSPSNYIQEIGRAGRDGELSQAIsLF 328
Cdd:PRK11634 322 IPMDSESYVHRIGRTGRAGRAGRAL-LF 348
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
17-171 |
6.18e-09 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 54.99 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 17 PGQQEIIESI---MSQQHTLGIL--PTGSGKSLCY-QIPTYLSGK----PTLIISPLISLMDdqvmQLKINGEKRVTCIH 86
Cdd:pfam04851 6 PYQIEAIENLlesIKNGQKRGLIvmATGSGKTLTAaKLIARLFKKgpikKVLFLVPRKDLLE----QALEEFKKFLPNYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 87 SGMDEIEKKHNIKCLLHSRFIFLSPEFLLQPSNFKLISMID--FGMIVLDEAHclsewgydfRPHYALIGKVTKHFKEAV 164
Cdd:pfam04851 82 EIGEIISGDKKDESVDDNKIVVTTIQSLYKALELASLELLPdfFDVIIIDEAH---------RSGASSYRNILEYFKPAF 152
|
....*..
gi 581937761 165 VLALTAT 171
Cdd:pfam04851 153 LLGLTAT 159
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
277-320 |
2.71e-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: 50.78 E-value: 2.71e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 581937761 277 IIVATSAFGMGINKKDIRTIIHFHLSTSPSNYIQEIGRAGRDGE 320
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
209-337 |
5.63e-08 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 54.95 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 209 DDEDKIEWLLPFLQQSGPT--IIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGM 286
Cdd:PRK11192 228 DLEHKTALLCHLLKQPEVTrsIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAAR 307
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 581937761 287 GINKKDIRTIIHFHLSTSPSNYIQEIGRAGRDGELSQAISLFQPDDKYILE 337
Cdd:PRK11192 308 GIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLG 358
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
19-337 |
2.78e-07 |
|
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: 52.92 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 19 QQEIIESIMSQQHTLGILPTGSGKSLCYQIP---TYLSGKPT--LIISPLISLMDDQV---MQLKINGEKRVTC--IHSG 88
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPvleALLEDPGAtaLYLYPTKALARDQLrrlRELAEALGLGVRVatYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 89 MDEIEKKhniKCLLHSRFIFLSPEFL---LQPSNFK---LISMIDFgmIVLDEAHclsewGYD--FRPHYALIGK----V 156
Cdd:COG1205 141 TPPEERR---WIREHPDIVLTNPDMLhygLLPHHTRwarFFRNLRY--VVIDEAH-----TYRgvFGSHVANVLRrlrrI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 157 TKHF-KEAVVLALTATA--PPHLQDDLTEMlaiQFNVIKTTMN-RPNISFKHLNFHDDEDKIEW--------LLPFLQQS 224
Cdd:COG1205 211 CRHYgSDPQFILASATIgnPAEHAERLTGR---PVTVVDEDGSpRGERTFVLWNPPLVDDGIRRsalaeaarLLADLVRE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 225 G-PTIIYVSSKKMclnlAQLIY-------DSGFLTG---IYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGInkkDI 293
Cdd:COG1205 288 GlRTLVFTRSRRG----AELLAryarralREPDLADrvaAYRAGYLPEERREIERGLRSGELLGVVSTNALELGI---DI 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 581937761 294 ----RTIIHfHLSTSPSNYIQEIGRAGRDGELSQAISLFQPD--DKYILE 337
Cdd:COG1205 361 ggldAVVLA-GYPGTRASFWQQAGRAGRRGQDSLVVLVAGDDplDQYYVR 409
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
396-428 |
5.19e-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: 46.90 E-value: 5.19e-07
10 20 30
....*....|....*....|....*....|....*.
gi 581937761 396 RMIGYCK-LDQCRRKYLLEFFGEYPPAQDrC--CDN 428
Cdd:pfam16124 30 AMVAYCEnTTDCRRKQLLRYFGEEFDSEP-CgnCDN 64
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
227-325 |
5.69e-07 |
|
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: 48.79 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 227 TIIYVSSKKMC----LNLAQLIYDSGFLTG---IYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTIIHF 299
Cdd:cd18797 38 TIVFCRSRKLAelllRYLKARLVEEGPLASkvaSYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117
|
90 100
....*....|....*....|....*.
gi 581937761 300 HLSTSPSNYIQEIGRAGRDGELSQAI 325
Cdd:cd18797 118 GYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
210-327 |
2.10e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 49.97 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 210 DEDKIEWLLPFLQQSGP--TIIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIVATSAFGMG 287
Cdd:PRK04837 239 NEEKMRLLQTLIEEEWPdrAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARG 318
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 581937761 288 INKKDIRTIIHFHLSTSPSNYIQEIGRAGRDGELSQAISL 327
Cdd:PRK04837 319 LHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
19-137 |
6.37e-06 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 46.42 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 19 QQEIIESIMSQQHTLGILPTGSGKSLCYQIPT-----YLSGKPTLIISPLISLMDDQVMQL-----KINGEKRVTCIHSG 88
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPIleallRDPGSRALYLYPTKALAQDQLRSLrelleQLGLGIRVATYDGD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 581937761 89 MDEIEKKHNIKclLHSRFIFLSPEFL----LQPSNF--KLISMIDFgmIVLDEAH 137
Cdd:cd17923 85 TPREERRAIIR--NPPRILLTNPDMLhyalLPHHDRwaRFLRNLRY--VVLDEAH 135
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
19-282 |
6.71e-06 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 48.54 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 19 QQEIIE---SIMSQQHTLGIL--PTGSGKslcyqipTYLS-----------GKPTLIIS-PLISLMDDQVMQLKINGEKR 81
Cdd:COG1203 132 QNEALElalEAAEEEPGLFILtaPTGGGK-------TEAAllfalrlaakhGGRRIIYAlPFTSIINQTYDRLRDLFGED 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 82 VTCIHSG-------MDEIEKKHNIKCLLHSRFiFLSP----------EFLLQPSNFKLISMidFGM----IVLDEAHcls 140
Cdd:COG1203 205 VLLHHSLadldlleEEEEYESEARWLKLLKEL-WDAPvvvttidqlfESLFSNRKGQERRL--HNLansvIILDEVQ--- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 141 ewgyDFRPHY-ALIGKVTKHFKEA---VVLaLTATAPPHLQDDLTEMlaiqFNVIKTTMNRPNISFKHLNFH-------- 208
Cdd:COG1203 279 ----AYPPYMlALLLRLLEWLKNLggsVIL-MTATLPPLLREELLEA----YELIPDEPEELPEYFRAFVRKrvelkegp 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 209 -DDEDKIEWLLPFLQQSGPTIIYVSSKKMCLNLAQLIYDSGFLTGIY--HGDMNYQERHTVQQQ---FLNNDIP-IIVAT 281
Cdd:COG1203 350 lSDEELAELILEALHKGKSVLVIVNTVKDAQELYEALKEKLPDEEVYllHSRFCPADRSEIEKEikeRLERGKPcILVST 429
|
.
gi 581937761 282 S 282
Cdd:COG1203 430 Q 430
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
46-186 |
7.09e-06 |
|
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: 46.41 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 46 YQIPTYLSGKPTLIISPLISLMDDQVMQLKINGEKRVTCIHsGMDEIEKKHNIKCLLHSRFIFL-SPEFLLQPSNFklIS 124
Cdd:cd17919 42 YLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVVYH-GSQRERAQIRAKEKLDKFDVVLtTYETLRRDKAS--LR 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581937761 125 MIDFGMIVLDEAHCLSEWGydfrphyALIGKVTKHFKEAVVLALTATaPphLQDDLTEMLAI 186
Cdd:cd17919 119 KFRWDLVVVDEAHRLKNPK-------SQLSKALKALRAKRRLLLTGT-P--LQNNLEELWAL 170
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
203-340 |
1.17e-05 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 47.50 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 203 KHLNFHDDEDKIEwLLPFLQQSG---PTIIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIPIIV 279
Cdd:PRK10590 222 QHVHFVDKKRKRE-LLSQMIGKGnwqQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLV 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581937761 280 ATSAFGMGINKKDIRTIIHFHLSTSPSNYIQEIGRAGRDGELSQAISLFQPDDKYIL---ETLL 340
Cdd:PRK10590 301 ATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLrdiEKLL 364
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
7-136 |
1.28e-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: 45.78 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 7 RNKFGFENFKPgQQEIIESIMSQQHTLGILPTGSGKS---LCYQIPTYLSGKPTLIISPLISLMDdQV------MQLKIN 77
Cdd:cd17924 11 KKKTGFPPWGA-QRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSLYLASKGKRSYLIFPTKSLVK-QAyerlskYAEKAG 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581937761 78 GEKRVTCIHSGMDEIEKKHNIKCLLHSRF-IFL-SPEFLlqPSNFKLISMIDFGMIVLDEA 136
Cdd:cd17924 89 VEVKILVYHSRLKKKEKEELLEKIEKGDFdILVtTNQFL--SKNFDLLSNKKFDFVFVDDV 147
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
54-183 |
1.10e-04 |
|
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 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: 350763 [Multi-domain] Cd Length: 245 Bit Score: 43.52 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 54 GKPTLIISPLiSLMDDQVMQLKINGEKRVTCIHSGMDEIEKKHNIKCLLHSrfIFLSPEFLLQPSNFKLiSMIDFGMIVL 133
Cdd:cd18005 70 KKPVLIVAPL-SVLYNWKDELDTWGHFEVGVYHGSRKDDELEGRLKAGRLE--VVVTTYDTLRRCIDSL-NSINWSAVIA 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 581937761 134 DEAHCLsewgydfRPHYALIGKVTKHFKEAVVLALTATApphLQDDLTEM 183
Cdd:cd18005 146 DEAHRI-------KNPKSKLTQAMKELKCKVRIGLTGTL---LQNNMKEL 185
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
15-188 |
1.26e-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: 42.63 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 15 FKPGQQEIIESIMSQQHTLGI-LPTGSGKSLCYQIPTYL----SGKPTLIISPLISLMDDQVMQLK---INGEKRVTcIH 86
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVsAPTSSGKTLIAELAILRalatSGGKAVYIAPTRALVNQKEADLRerfGPLGKNVG-LL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 87 SGmdeiEKKHNIKCLLHSRFIFLSPE-FLLQPSNFKLISMIDFGMIVLDEAHCL--SEWGYDFRphyALIGKVTKHFKEA 163
Cdd:cd17921 81 TG----DPSVNKLLLAEADILVATPEkLDLLLRNGGERLIQDVRLVVVDEAHLIgdGERGVVLE---LLLSRLLRINKNA 153
|
170 180
....*....|....*....|....*..
gi 581937761 164 VVLALTATA--PPHLQDDLTEMLAIQF 188
Cdd:cd17921 154 RFVGLSATLpnAEDLAEWLGVEDLIRF 180
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
213-319 |
1.38e-04 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 41.69 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 213 KIEWLLPFLQQSGPT----IIYVSSKKMcLN-LAQLIYDSGFLTGIYHGDMNYQERHTVQQQFlNNDIPIIV---ATSAF 284
Cdd:cd18793 12 KLEALLELLEELREPgekvLIFSQFTDT-LDiLEEALRERGIKYLRLDGSTSSKERQKLVDRF-NEDPDIRVfllSTKAG 89
|
90 100 110
....*....|....*....|....*....|....*
gi 581937761 285 GMGINKKDIRTIIHFHLSTSPSNYIQEIGRAGRDG 319
Cdd:cd18793 90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIG 124
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
2-49 |
3.37e-04 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It 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: 350714 [Multi-domain] Cd Length: 231 Bit Score: 41.85 E-value: 3.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 581937761 2 LHDILRNkFGFENFKPGQQEIIESIMSQQHTLGIL---------PTGSGKSLCYQIP 49
Cdd:cd17956 1 LLKNLQN-NGITSAFPVQAAVIPWLLPSSKSTPPYrpgdlcvsaPTGSGKTLAYVLP 56
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
9-177 |
3.51e-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: 41.68 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 9 KFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPTYL------------SGKPTLIISP---LISLMDDQVMQ 73
Cdd:cd17958 7 KQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIhldlqpipreqrNGPGVLVLTPtreLALQIEAECSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 74 LKINGEKRVtCIHSG------MDEIEKKHNIkcllhsrfIFLSPEFL--LQPSNFKLISMIDFgmIVLDEAHCLSEWGyd 145
Cdd:cd17958 87 YSYKGLKSV-CVYGGgnrneqIEDLSKGVDI--------IIATPGRLndLQMNNVINLKSITY--LVLDEADRMLDMG-- 153
|
170 180 190
....*....|....*....|....*....|...
gi 581937761 146 FRPHyalIGKVTKHFKEAVVLALT-ATAPPHLQ 177
Cdd:cd17958 154 FEPQ---IRKILLDIRPDRQTIMTsATWPDGVR 183
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
52-182 |
5.42e-04 |
|
SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.
Pssm-ID: 425504 [Multi-domain] Cd Length: 289 Bit Score: 41.90 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 52 LSGKPTLIISPLiSLMDDQVMQLK---INGEKRVTCIHSGMDEIEKKHNIKCLLHSRFIFL-SPEFLLQPSNfkLISMID 127
Cdd:pfam00176 47 NWGGPTLIVVPL-SLLHNWMNEFErwvSPPALRVVVLHGNKRPQERWKNDPNFLADFDVVItTYETLRKHKE--LLKKVH 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 581937761 128 FGMIVLDEAHCLsewgydfRPHYALIGKVTKHFKEAVVLALTATaPphLQDDLTE 182
Cdd:pfam00176 124 WHRIVLDEGHRL-------KNSKSKLSKALKSLKTRNRWILTGT-P--LQNNLEE 168
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
8-136 |
6.51e-04 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 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: 350711 [Multi-domain] Cd Length: 222 Bit Score: 41.21 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 8 NKFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPTYL-----------SGKPTLIISPLISLmddqVMQLKI 76
Cdd:cd17953 28 KKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRhikdqrpvkpgEGPIGLIMAPTREL----ALQIYV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581937761 77 NGEK-------RVTCIHSG------MDEIEKKHNIKCLLHSRFIflspeFLLQPSNFKLISMIDFGMIVLDEA 136
Cdd:cd17953 104 ECKKfskalglRVVCVYGGsgiseqIAELKRGAEIVVCTPGRMI-----DILTANNGRVTNLRRVTYVVLDEA 171
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
19-137 |
9.08e-04 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain] Cd Length: 200 Bit Score: 40.33 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 19 QQEIIESIMsQQHTLGILPTGSGKSLC----------YQIPTYLSGKPTLIISPLISLMDDQVMQLKIN---------GE 79
Cdd:cd18034 7 QLELFEAAL-KRNTIVVLPTGSGKTLIavmlikemgeLNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHtdlkvgeysGE 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581937761 80 KRVTCIHSGM--DEIEKKHNIKC-------LLHSRFIFLSpefllqpsnfklismiDFGMIVLDEAH 137
Cdd:cd18034 86 MGVDKWTKERwkEELEKYDVLVMtaqilldALRHGFLSLS----------------DINLLIFDECH 136
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
227-317 |
1.16e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 38.69 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 227 TIIYVSSKKMCLNLAQLIYDSGFLTGIYHGD--MNYQERHTVQQQFLNND-IPIIVATSAFGMGINKKDIRTIIHFHLST 303
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFFGELkPPILVTVDLLTTGVDIPEVDNVVFLRPTE 88
|
90
....*....|....
gi 581937761 304 SPSNYIQEIGRAGR 317
Cdd:cd18799 89 SRTLFLQMLGRGLR 102
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
15-173 |
1.21e-03 |
|
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: 39.62 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 15 FKPGQQEIIES-IMSQQHTLGILPTGSGKSLCYQ---IPTYLSGKPTLIISPLISLMDDQVMQLKINGEKRVTC-IHSGM 89
Cdd:cd18028 2 LYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRALASEKYEEFKKLEEIGLKVgISTGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 90 DEIEKKHnikcLLHSRFIFLSPE---FLLQPSnfklISMI-DFGMIVLDEAHCLSEwgYDFRPHY-ALIGKVTKHFKEAV 164
Cdd:cd18028 82 YDEDDEW----LGDYDIIVATYEkfdSLLRHS----PSWLrDVGVVVVDEIHLISD--EERGPTLeSIVARLRRLNPNTQ 151
|
....*....
gi 581937761 165 VLALTATAP 173
Cdd:cd18028 152 IIGLSATIG 160
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
8-136 |
2.16e-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: 39.35 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 8 NKFGFENFKPGQQEIIESIMSQQHTLGILPTGSGKSLCYQIPT---------YLSGKP-TLIISP---L---ISlmdDQV 71
Cdd:cd00268 6 KKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPIlekllpepkKKGRGPqALVLAPtreLamqIA---EVA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581937761 72 MQLKINGEKRVTCIHSGMD----EIEKKHNI-------KCLLHsrfiflspefLLQPSNFKLiSMIDFgmIVLDEA 136
Cdd:cd00268 83 RKLGKGTGLKVAAIYGGAPikkqIEALKKGPdivvgtpGRLLD----------LIERGKLDL-SNVKY--LVLDEA 145
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
208-317 |
2.84e-03 |
|
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: 38.01 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 208 HDDEDKIEWLLPFLQQSGPTIIYVSSKK----MCLNLAQLIYDSGF--LTGIYHGDMNYQERHTVQQQFLNNDIPIIVAT 281
Cdd:cd18796 22 ESGADAYAEVIFLLERHKSTLVFTNTRSqaerLAQRLRELCPDRVPpdFIALHHGSLSRELREEVEAALKRGDLKVVVAT 101
|
90 100 110
....*....|....*....|....*....|....*.
gi 581937761 282 SAFGMGINKKDIRTIIHFHLSTSPSNYIQEIGRAGR 317
Cdd:cd18796 102 SSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
213-317 |
3.10e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 40.21 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 213 KIEWLLPFLQQ----SGPTIIYVSSKKMCLNLAQLIYDSGFLTGIYHGDMNYQERHTVQQQFLNNDIP--IIVATSAFGM 286
Cdd:COG0553 534 KLEALLELLEEllaeGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGE 613
|
90 100 110
....*....|....*....|....*....|.
gi 581937761 287 GINKKDIRTIIHFHLSTSPSNYIQEIGRAGR 317
Cdd:COG0553 614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHR 644
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
214-319 |
4.09e-03 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 37.57 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 214 IEWLLPFLQQSGP--TIIYVSSKKMCLNLAQLI---------YDSGFLTGIYHGDMNYQERHTVQQQ------FLNNDIP 276
Cdd:cd18802 13 IEILREYFPKTPDfrGIIFVERRATAVVLSRLLkehpstlafIRCGFLIGRGNSSQRKRSLMTQRKQketldkFRDGELN 92
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90 100 110 120
....*....|....*....|....*....|....*....|...
gi 581937761 277 IIVATSAFGMGINKKDIRTIIHFHLSTSPSNYIQEIGRAGRDG 319
Cdd:cd18802 93 LLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
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| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
19-137 |
4.18e-03 |
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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: 37.96 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 19 QQEIIESIMS-----QQHTL-GIlpTGSGKSLCY--QIPTYL-SGKPTLIISPLISLmddqVMQLKINGEKR----VTCI 85
Cdd:cd17929 1 QRKAYEAIVSslggfKTFLLhGV--TGSGKTEVYieLIEKVLaKGKQVLVLVPEISL----TPQLIKRFKKRfgdkVAVL 74
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581937761 86 HSGMDEIEKKHN--------IKCLLHSRF-IFLSpefllqpsnFKlismiDFGMIVLDEAH 137
Cdd:cd17929 75 HSKLSDKERADEwrkikrgeAKVVIGARSaLFAP---------FK-----NLGLIIVDEEH 121
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| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
126-186 |
4.82e-03 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA 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: 350769 [Multi-domain] Cd Length: 207 Bit Score: 38.42 E-value: 4.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 126 IDFGMIVLDEAHCLSEWG-------YDFrphYALIGKVTKHfkeavVLALTATapPHL--QDDLTEMLAI 186
Cdd:cd18011 119 EEWDLVVVDEAHKLRNSGggketkrYKL---GRLLAKRARH-----VLLLTAT--PHNgkEEDFRALLSL 178
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| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
258-317 |
8.24e-03 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is 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. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain] Cd Length: 143 Bit Score: 36.56 E-value: 8.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581937761 258 MNYQERHTVQQQFLNNDIPIIVATSAFGMGINKKDIRTIIHFHLSTSPSNYIQEIGRAGR 317
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
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