|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
6-502 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 755.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 6 NLIDNLKHYFGFDNFKGEQEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSLIMEGTAVVVSPLIALMKNQVDVI--NGIS 83
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALraAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 84 egdgvAHYLNSSLKKAEVDKVRTDIREGKTKLLYVAPESLNKEDNIEFLKTVKVSFYAIDEAHCISEWGHDFRPEYRKIR 163
Cdd:COG0514 84 -----AAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 164 NAIEVIGRAPIIALTATATAKVRTDIVRSLGIEGCAEFRSSFNRPNLYYEVRPKkSEDDTNKQIIRFIKQHAGKSGIIYC 243
Cdd:COG0514 159 ELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPK-PPDDKLAQLLDFLKEHPGGSGIVYC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 244 LSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQE 323
Cdd:COG0514 238 LSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 324 TGRAGRDGEEGICLVFYSRNDLKKLEKFMEGKPIAE--QDIGRQLLQETEAYAESSVCRRKLLLHYFGEEYPkENCGMCD 401
Cdd:COG0514 318 IGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEerKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELA-EPCGNCD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 402 NCRHPKTLIEAKEPLKIVLEAIKELKENFRQEYVIDFVKGRATDDLRDHKHDELAFFGAGEKVDVKMWNPVVRQALllgy 481
Cdd:COG0514 397 NCLGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLL---- 472
|
490 500
....*....|....*....|.
gi 738980454 482 ikksVENYGILKLTAKGERFI 502
Cdd:COG0514 473 ----AQLFGERKLERYGEAFL 489
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
11-603 |
0e+00 |
|
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: 640.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 11 LKHYFGFDNFKGEQEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSLIMEGTAVVVSPLIALMKNQVDVI--NGISegdgv 88
Cdd:TIGR01389 5 LKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLraAGVA----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 89 AHYLNSSLKKAEVDKVRTDIREGKTKLLYVAPESLNKEDNIEFLKTVKVSFYAIDEAHCISEWGHDFRPEYRKIRNAIEV 168
Cdd:TIGR01389 80 AAYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 169 IGRAPIIALTATATAKVRTDIVRSLGIEGCAEFRSSFNRPNLYYEVRPKKSEDDtnkQIIRFIKQHAGKSGIIYCLSRKK 248
Cdd:TIGR01389 160 FPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQK---FLLDYLKKHRGQSGIIYASSRKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 249 VEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAG 328
Cdd:TIGR01389 237 VEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 329 RDGEEGICLVFYSRNDLKKLEKFMEGK--PIAEQDIGRQLLQETEAYAESSVCRRKLLLHYFGEEYPkENCGMCDNCRHP 406
Cdd:TIGR01389 317 RDGLPAEAILLYSPADIALLKRRIEQSeaDDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEV-EPCGNCDNCLDP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 407 KTLIEAKEPLKIVLEAIKELKENFRQEYVIDFVKGRATDDLRDHKHDELAFFGAGEKVDVKMWNPVVRQALLLGYIKKSV 486
Cdd:TIGR01389 396 PKSYDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTEND 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 487 ENYGILKLTAKGERFIKSPESfmiVLDAEFKDEPNDAEAYGGGAVLDPE--LFSLLKALRKTVAHKHDVPPYVVFQDVSL 564
Cdd:TIGR01389 476 EIYIGLQLTEAARKVLKNEVE---VLLRPFKVVAKEKTRVQKNLSVGVDnaLFEALRELRKEQADEQNVPPYVIFSDSTL 552
|
570 580 590
....*....|....*....|....*....|....*....
gi 738980454 565 EQMAMMYPINEQELQNIQGVGAGKAKRYGKEFYTLISKY 603
Cdd:TIGR01389 553 REMAEKRPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
11-600 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 545.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 11 LKHYFGFDNFKGEQEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSLIMEGTAVVVSPLIALMKNQVDVI--NGISegdgv 88
Cdd:PRK11057 17 LQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLlaNGVA----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 89 AHYLNSSLKKAEVDKVRTDIREGKTKLLYVAPESLNKEDNIEFLKTVKVSFYAIDEAHCISEWGHDFRPEYRKIRNAIEV 168
Cdd:PRK11057 92 AACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 169 IGRAPIIALTATATAKVRTDIVRSLGIEGCAEFRSSFNRPNLYYEVRPKKSEDDtnkQIIRFIKQHAGKSGIIYCLSRKK 248
Cdd:PRK11057 172 FPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLD---QLMRYVQEQRGKSGIIYCNSRAK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 249 VEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAG 328
Cdd:PRK11057 249 VEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 329 RDGEEGICLVFYSRNDLKKLEKFMEGKPI-AEQDIGRQLLQETEAYAESSVCRRKLLLHYFGeEYPKENCGMCDNCRHPK 407
Cdd:PRK11057 329 RDGLPAEAMLFYDPADMAWLRRCLEEKPAgQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFG-EGRQEPCGNCDICLDPP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 408 TLIEAKEPLKIVLEAIKELKENFRQEYVIDFVKGRATDDLRDHKHDELAFFGAGEKVDVKMWNPVVRQALLLGYIKKSVE 487
Cdd:PRK11057 408 KQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIA 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 488 NYGILKLTAKGERFIKSPESFMIVLDAEFKDEPNDAE-AYGGGavLDPELFSLLKALRKTVAHKHDVPPYVVFQDVSLEQ 566
Cdd:PRK11057 488 QHSALQLTEAARPVLRGEVSLQLAVPRIVALKPRAMQkSFGGN--YDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIE 565
|
570 580 590
....*....|....*....|....*....|....
gi 738980454 567 MAMMYPINEQELQNIQGVGAGKAKRYGKEFYTLI 600
Cdd:PRK11057 566 MAEQMPITASEMLSVNGVGQRKLERFGKPFMALI 599
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
11-461 |
2.61e-166 |
|
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: 486.97 E-value: 2.61e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 11 LKHYFGFDNFKGEQEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSLIMEGTAVVVSPLIALMKNQVDVI--NGISegdgv 88
Cdd:TIGR00614 3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLqaLGIP----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 89 AHYLNSSLKKAEVDKVRTDIREGKTKLLYVAPESLNKedNIEFLKTV----KVSFYAIDEAHCISEWGHDFRPEYRKIRN 164
Cdd:TIGR00614 78 ATFLNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISA--SNRLLQTLeerkGITLIAVDEAHCISQWGHDFRPDYKALGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 165 AIEVIGRAPIIALTATATAKVRTDIVRSLGIEGCAEFRSSFNRPNLYYEVRPKKSedDTNKQIIRFI-KQHAGKSGIIYC 243
Cdd:TIGR00614 156 LKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTP--KILEDLLRFIrKEFEGKSGIIYC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 244 LSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQE 323
Cdd:TIGR00614 234 PSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 324 TGRAGRDGEEGICLVFYSRNDLKKLEKFMEGKPIAE-QDIGRQLLQETEAYAESSVCRRKLLLHYFGEEYPKENCG---- 398
Cdd:TIGR00614 314 SGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGNfRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFNKSFCimgt 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738980454 399 --MCDNCR----HPKTLIEAKE-----PLKIVLEAIKELKENFRQEYVIDFVKGRATDDLRDHKHDELAFFGAG 461
Cdd:TIGR00614 394 ekCCDNCCkrldYKTKDVTDKVydfgpQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRG 467
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
6-593 |
1.13e-124 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 400.43 E-value: 1.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 6 NLIDNLKHYFGFDNFKGEQEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSLIMEGTAVVVSPLIALMKNQvdvINGISEG 85
Cdd:PLN03137 447 KLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQ---IMNLLQA 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 86 DGVAHYLNSSLKKAEVDKVRTDI--REGKTKLLYVAPESLNKED----NIEFLKTVKV-SFYAIDEAHCISEWGHDFRPE 158
Cdd:PLN03137 524 NIPAASLSAGMEWAEQLEILQELssEYSKYKLLYVTPEKVAKSDsllrHLENLNSRGLlARFVIDEAHCVSQWGHDFRPD 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 159 YRKIRNAIEVIGRAPIIALTATATAKVRTDIVRSLGIEGCAEFRSSFNRPNLYYEVRPK--KSEDDTNKqiirFIKQ-HA 235
Cdd:PLN03137 604 YQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKtkKCLEDIDK----FIKEnHF 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 236 GKSGIIYCLSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVIHYDIPK 315
Cdd:PLN03137 680 DECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPK 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 316 SLEGYYQETGRAGRDGEEGICLVFYSRNDLKKLeKFMEGKPIAEQ-----------DIGRQLLQETE------AYAESSV 378
Cdd:PLN03137 760 SIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRV-KHMISQGGVEQspmamgynrmaSSGRILETNTEnllrmvSYCENEV 838
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 379 -CRRKLLLHYFGEEYPKENCG-MCDNCRHPKTLIE--AKEPLKIVLEAIKELKENFRQEYVIDFVKGRATDDLRDHKHDE 454
Cdd:PLN03137 839 dCRRFLQLVHFGEKFDSTNCKkTCDNCSSSKSLIDkdVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHET 918
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 455 LAFFGAGE---KVDV-KMWNPVVRQALLLGYIKKSvENYG----ILK--------LTAKGERFI-KSPESFMIVLDAEFK 517
Cdd:PLN03137 919 LSLHGAGKhlsKGEAsRILHYLVTEDILAEDVKKS-DLYGsvssLLKvneskaykLFSGGQTIImRFPSSVKASKPSKFE 997
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 518 DEPNDAEAYGG-------GAVLDPE--------LFSLLKALRKTVAHK--HDVPPYVVFQDVSLEQMAMMYPINEQELQN 580
Cdd:PLN03137 998 ATPAKGPLTSGkqstlpmATPAQPPvdlnlsaiLYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLE 1077
|
650
....*....|...
gi 738980454 581 IQGVGAGKAKRYG 593
Cdd:PLN03137 1078 INGLGKAKVSKYG 1090
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
9-206 |
4.75e-91 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 282.50 E-value: 4.75e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 9 DNLKHYFGFDNFKGEQEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSLIMEGTAVVVSPLIALMKNQVDVI--NGISegd 86
Cdd:cd17920 2 QILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLqqLGIR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 87 gvAHYLNSSLKKAEVDKVRTDIREGKTKLLYVAPESLNKEDNIEFLKTVK----VSFYAIDEAHCISEWGHDFRPEYRKI 162
Cdd:cd17920 79 --AAALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 738980454 163 RNAIEVIGRAPIIALTATATAKVRTDIVRSLGIEGCAEFRSSFN 206
Cdd:cd17920 157 GRLRRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
207-340 |
2.18e-64 |
|
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: 209.76 E-value: 2.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 207 RPNLYYEVRPKKSEDDTNKQIIRFIKQHAGKSGIIYCLSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMED 286
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 738980454 287 IDVIVATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAGRDGEEGICLVFY 340
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
9-206 |
2.43e-62 |
|
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: 207.22 E-value: 2.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 9 DNLKHYFGFDNFKGEQEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSLIMEGTAVVVSPLIALMKNQVDVIN--GISegd 86
Cdd:cd18015 8 DTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKklGIS--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 87 gvAHYLNSSLKKAEVDKVRTDIREGKT--KLLYVAPESLNKEDniEFLKTV-------KVSFYAIDEAHCISEWGHDFRP 157
Cdd:cd18015 85 --ATMLNASSSKEHVKWVHAALTDKNSelKLLYVTPEKIAKSK--RFMSKLekaynagRLARIAIDEVHCCSQWGHDFRP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 738980454 158 EYRKIRNAIEVIGRAPIIALTATATAKVRTDIVRSLGIEGCAEFRSSFN 206
Cdd:cd18015 161 DYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
10-206 |
1.14e-61 |
|
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: 205.18 E-value: 1.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 10 NLKHYFGFDNFKGEQEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSLIME----GTAVVVSPLIALMKNQVD-VINGISe 84
Cdd:cd18018 3 LLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDaLPRAIK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 85 gdgvAHYLNSSLKKAEVDKVRTDIREGKTKLLYVAPESLNKEDNIEFLKTVK-VSFYAIDEAHCISEWGHDFRPEYRKIR 163
Cdd:cd18018 82 ----AAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPpISLLVVDEAHCISEWSHNFRPDYLRLC 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 738980454 164 NAI-EVIGRAPIIALTATATAKVRTDIVRSLGIEGCAEFRSSFN 206
Cdd:cd18018 158 RVLrELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
8-195 |
3.49e-53 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 181.90 E-value: 3.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 8 IDNLKHYFGFDNFKGEQEAIIRHLL-AGYDAFVLMPTGGGKSLCYQLPSLIMEGTAVVVSPLIALMKNQVD--VINGISe 84
Cdd:cd18017 1 LNALNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLqlVMSNIP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 85 gdgvahylNSSLKKAEVDKVRTDIREGKTKLLYVAPESLNKedNIEFLKTVK--VSFYAIDEAHCISEWGHDFRPEYRKI 162
Cdd:cd18017 80 --------ACFLGSAQSQNVLDDIKMGKIRVIYVTPEFVSK--GLELLQQLRngITLIAIDEAHCVSQWGHDFRSSYRHL 149
|
170 180 190
....*....|....*....|....*....|...
gi 738980454 163 RNAIEVIGRAPIIALTATATAKVRTDIVRSLGI 195
Cdd:cd18017 150 GSIRNRLPNVPIVALTATATPSVRDDIIKNLNL 182
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
1-206 |
5.12e-53 |
|
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: 181.95 E-value: 5.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 1 MTKEvnLIDNLKHYFGFDNFKGEQEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSLIMEGTAVVVSPLIALMknqVDVIN 80
Cdd:cd18016 1 HSKE--MMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLI---VDQVQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 81 GISEGDGVAHYLNSSLKKAEVDKVRTDIREGK--TKLLYVAPESLNKE----DNIEFLKTVK-VSFYAIDEAHCISEWGH 153
Cdd:cd18016 76 KLTSLDIPATYLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKISASnrliSTLENLYERKlLARFVIDEAHCVSQWGH 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 738980454 154 DFRPEYRKIRNAIEVIGRAPIIALTATATAKVRTDIVRSLGIEGCAEFRSSFN 206
Cdd:cd18016 156 DFRPDYKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
11-204 |
6.54e-48 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 168.03 E-value: 6.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 11 LKHYFGFDNFKGE-QEAIIRHLLAG-YDAFVLMPTGGGKSLCYQLPSLIMEGTAVVVSPLIALMKNQVDVINGIsegdGV 88
Cdd:cd18014 4 LKKVFGHSDFKSPlQEKATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTL----KI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 89 -AHYLNSSLKKAEVDKVRTDIREG--KTKLLYVAPE---SLNKEDNIEFL-KTVKVSFYAIDEAHCISEWGHDFRPEYRK 161
Cdd:cd18014 80 rVDSLNSKLSAQERKRIIADLESEkpQTKFLYITPEmaaTSSFQPLLSSLvSRNLLSYLVVDEAHCVSQWGHDFRPDYLR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 738980454 162 IRNAIEVIGRAPIIALTATATAKVRTDIVRSLGIEG-CAEFRSS 204
Cdd:cd18014 160 LGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKpVAIFKTP 203
|
|
| DpdF |
NF041063 |
protein DpdF; |
11-346 |
2.21e-47 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 180.11 E-value: 2.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 11 LKHYFGFDNFK--GEQEAIIRHLLAGYDAFVL--MPTGGGKSLCYQLPSLI---MEGTAVVVSPLIALMKNQ----VDVI 79
Cdd:NF041063 131 LAEALGFTHYRspGQREAVRAALLAPPGSTLIvnLPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQerraRELL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 80 N--GISEGDGVAHYlnSSLKKAEVDKVRTDIREGKTKLLYVAPESLNK----------EDNieFLKTVkvsfyAIDEAHC 147
Cdd:NF041063 211 RraGPDLGGPLAWH--GGLSAEERAAIRQRIRDGTQRILFTSPESLTGslrpalfdaaEAG--LLRYL-----VVDEAHL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 148 ISEWGHDFRPEYRKI----RNAIEV--IGRAP-IIALTATATAKVRTDIvRSL--GIEGCAEFRSSFNRPNLYYEVRPKK 218
Cdd:NF041063 282 VDQWGDGFRPEFQLLaglrRSLLRLapSGRPFrTLLLSATLTESTLDTL-ETLfgPPGPFIVVSAVQLRPEPAYWVAKCD 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 219 SEDDTNKQIIRFIKqHAGKSGIIYCLSRKKVEELAAVLLANDIK-AAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFG 297
Cdd:NF041063 361 SEEERRERVLEALR-HLPRPLILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFG 439
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 738980454 298 MGIDKPDVRFVIHYDIPKSLEGYYQETGRAGRDGEEGICLVFYSRNDLK 346
Cdd:NF041063 440 LGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLD 488
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
24-186 |
4.74e-26 |
|
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: 105.02 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 24 QEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSLIM------EGTAVVVSPLIALMKNQVDVINGISEGDGVAhyLNSSLK 97
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAldkldnGPQALVLAPTRELAEQIYEELKKLGKGLGLK--VASLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 98 KAEVDKVRTDIRegKTKLLYVAPESLnkEDNIEFLKTVK-VSFYAIDEAHCISEWGhdFRPEYRKIRNAIEVIGRapIIA 176
Cdd:pfam00270 82 GDSRKEQLEKLK--GPDILVGTPGRL--LDLLQERKLLKnLKLLVLDEAHRLLDMG--FGPDLEEILRRLPKKRQ--ILL 153
|
170
....*....|
gi 738980454 177 LTATATAKVR 186
Cdd:pfam00270 154 LSATLPRNLE 163
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
250-331 |
4.20e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 93.43 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 250 EELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAGR 329
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 738980454 330 DG 331
Cdd:smart00490 81 AG 82
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
210-340 |
5.48e-23 |
|
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: 94.88 E-value: 5.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 210 LYYEVrpkKSEDDTNKQIIRFIKQHAGKSGIIYCLSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDV 289
Cdd:cd18787 4 LYVVV---EEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 738980454 290 IVATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAGRDGEEGICLVFY 340
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
227-331 |
3.17e-22 |
|
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: 91.89 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 227 IIRFIKQHAGKSGIIYCLSRKKVEElAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVR 306
Cdd:pfam00271 6 LLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVD 84
|
90 100
....*....|....*....|....*
gi 738980454 307 FVIHYDIPKSLEGYYQETGRAGRDG 331
Cdd:pfam00271 85 LVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
211-362 |
9.34e-22 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 98.68 E-value: 9.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 211 YYEVrpkkSEDDTNKQIIRFIKQHAGKSGIIYCLSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVI 290
Cdd:COG0513 220 YYLV----DKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVL 295
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738980454 291 VAT-IAfGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAGRDGEEGICLVFYSRND---LKKLEKFMeGKPIAEQDI 362
Cdd:COG0513 296 VATdVA-ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDErrlLRAIEKLI-GQKIEEEEL 369
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
406-513 |
4.97e-21 |
|
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure. The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 462780 [Multi-domain] Cd Length: 108 Bit Score: 88.75 E-value: 4.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 406 PKTLIEAKEPLKIVLEAIKELKENFRQEYVIDFVKGRATDDLRDHKHDELAFFGAGEKVDVKMWNPVVRQALLLGYIKKS 485
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*...
gi 738980454 486 VENYGILKLTAKGERFIKSPESFMIVLD 513
Cdd:pfam09382 81 IEFYSVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
342-404 |
2.66e-20 |
|
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: 85.03 E-value: 2.66e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738980454 342 RNDLKKLEKFMEGKPIAE--QDIGRQLLQETEAYAESSV-CRRKLLLHYFGEEYPKENCGMCDNCR 404
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEerKEVELQKLQAMVAYCENTTdCRRKQLLRYFGEEFDSEPCGNCDNCL 66
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
13-215 |
5.73e-20 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 88.70 E-value: 5.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 13 HYFGFDNFKGEQEAIIRHLLAGY-DAFVLMPTGGGKSLCYQLPSLI-----MEGTAVVVSPLIALMKNQVDVINGISEG- 85
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGPSl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 86 DGVAHYLNSSLKKAEVdkvRTDIREGKTKLLYVAPESLNKEDNIEFLKTVKVSFYAIDEAHCISEWGhdFRPEYRKIRNa 165
Cdd:smart00487 82 GLKVVGLYGGDSKREQ---LRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLK- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 738980454 166 iEVIGRAPIIALTATATAKVRTDIvrSLGIEGCAEFRSSFnRPNLYYEVR 215
Cdd:smart00487 156 -LLPKNVQLLLLSATPPEEIENLL--ELFLNDPVFIDVGF-TPLEPIEQF 201
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
412-502 |
5.24e-18 |
|
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure; The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 214936 [Multi-domain] Cd Length: 92 Bit Score: 79.44 E-value: 5.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 412 AKEPLKIVLEAIKELKENFRQEYVIDFVKGRATDDLRDHKHDELAFFGAGEKVDVKMWNPVVRQALLLGYIKKSVENYGI 491
Cdd:smart00956 2 VTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYPY 81
|
90
....*....|.
gi 738980454 492 LKLTAKGERFI 502
Cdd:smart00956 82 LKLTEKARPVL 92
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
24-340 |
1.56e-15 |
|
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: 80.65 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 24 QEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSL--IMEG---TAVVVSPLIALMKNQVDVINGISEGDGVahylnsSLKK 98
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLEDpgaTALYLYPTKALARDQLRRLRELAEALGL------GVRV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 99 AEVD-----KVRTDIREgKTKLLYVAPESLN------KEDNIEFLKTVKvsFYAIDEAHcisewghdfrpEY-------- 159
Cdd:COG1205 135 ATYDgdtppEERRWIRE-HPDIVLTNPDMLHygllphHTRWARFFRNLR--YVVIDEAH-----------TYrgvfgshv 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 160 ----RKIRNAIEVIGRAP-IIALTAT-----ATAKvrtdivRSLG-----IEGCAEFRSS----FNRPNLYYEVRPKKSE 220
Cdd:COG1205 201 anvlRRLRRICRHYGSDPqFILASATignpaEHAE------RLTGrpvtvVDEDGSPRGErtfvLWNPPLVDDGIRRSAL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 221 DDTNKQIIRFIKQhaGKSGIIYCLSRKKVEELAAVL--------LANDIkaAPYHAGLDSEVRSKTQDQFLMEDIDVIVA 292
Cdd:COG1205 275 AEAARLLADLVRE--GLRTLVFTRSRRGAELLARYArralrepdLADRV--AAYRAGYLPEERREIERGLRSGELLGVVS 350
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 738980454 293 TIAFGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAGRDGEEGicLVFY 340
Cdd:COG1205 351 TNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS--LVVL 396
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
240-333 |
9.37e-15 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 71.90 E-value: 9.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 240 IIYCLSRKKVEELAAVLLANDIKAAP-------YHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVIHYD 312
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEGPlaskvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|.
gi 738980454 313 IPKSLEGYYQETGRAGRDGEE 333
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKD 139
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
136-348 |
1.12e-14 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 77.52 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 136 KVSFYAIDEAHCISEWGhdFRPEYRKIRNAIEvigRAPIIALTATATA---KVRTDIVRSLGIEGCAEFrssfNRPN--- 209
Cdd:PLN00206 270 NVSVLVLDEVDCMLERG--FRDQVMQIFQALS---QPQVLLFSATVSPeveKFASSLAKDIILISIGNP----NRPNkav 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 210 ----LYYEVRPKKseddtnKQI--IRFIKQHAGKSGIIYCLSRKKVEELA-AVLLANDIKAAPYHAGLDSEVRSKTQDQF 282
Cdd:PLN00206 341 kqlaIWVETKQKK------QKLfdILKSKQHFKPPAVVFVSSRLGADLLAnAITVVTGLKALSIHGEKSMKERREVMKSF 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738980454 283 LMEDIDVIVATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAGRDGEEGICLVFY---SRNDLKKL 348
Cdd:PLN00206 415 LVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVneeDRNLFPEL 483
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
25-455 |
2.22e-14 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 76.60 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 25 EAIIRHLLAGYDAFVL-MPTGGGKSLcyqLPSLIME-----GTAVVVSPLIALMKNQVDvingisegdgvahylnsSLKK 98
Cdd:COG1061 90 EALLAALERGGGRGLVvAPTGTGKTV---LALALAAellrgKRVLVLVPRRELLEQWAE-----------------ELRR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 99 AEVDKVRTDIREGKTKLLYVA-PESLNKEDNIEFLKTvKVSFYAIDEAHcisewgHDFRPEYRKIRNAIEvigRAPIIAL 177
Cdd:COG1061 150 FLGDPLAGGGKKDSDAPITVAtYQSLARRAHLDELGD-RFGLVIIDEAH------HAGAPSYRRILEAFP---AAYRLGL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 178 TATAtakVRTD-----IVRSLGI-----------EG-CAEFR-----SSFNRPNLYYEVRPKK------SEDDTNKQIIR 229
Cdd:COG1061 220 TATP---FRSDgreilLFLFDGIvyeyslkeaieDGyLAPPEyygirVDLTDERAEYDALSERlrealaADAERKDKILR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 230 -FIKQHAG-KSGIIYCLSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRF 307
Cdd:COG1061 297 eLLREHPDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 308 VIHYDIPKSLEGYYQETGRAGRDGEEGICLVFY-----SRNDLKKL---EKFMEGKPIAEQDIGRQLLQETEAYAESSVC 379
Cdd:COG1061 377 AILLRPTGSPREFIQRLGRGLRPAPGKEDALVYdfvgnDVPVLEELakdLRDLAGYRVEFLDEEESEELALLIAVKPALE 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738980454 380 RRKLLLHYFGEEYPKENcgMCDNCRHPKTLIEAKEPLKIVLEAIKELKENFRQEYVIDFVKGRATDDLRDHKHDEL 455
Cdd:COG1061 457 VKGELEEELLEELELLE--DALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLL 530
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
533-600 |
4.50e-14 |
|
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.
Pssm-ID: 425755 [Multi-domain] Cd Length: 68 Bit Score: 67.56 E-value: 4.50e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738980454 533 DPELFSLLKALRKTVAHKHDVPPYVVFQDVSLEQMAMMYPINEQELQNIQGVGAGKAKRYGKEFYTLI 600
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
34-180 |
9.65e-14 |
|
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: 68.97 E-value: 9.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 34 GYDAFVLMPTGGGKSLCYQLP----SLIMEGTAVVVSPLIALMKNQVDVINGISEGDGVAHYLNSSLKKAEvdkvRTDIR 109
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAalllLLKKGKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVGGSSAEE----REKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738980454 110 EGKTKLLYVAPESLNK---EDNIEFLKTVKVsfYAIDEAHCISEWGHDFRPEYRKIRNAIEviGRAPIIALTAT 180
Cdd:cd00046 77 LGDADIIIATPDMLLNlllREDRLFLKDLKL--IIVDEAHALLIDSRGALILDLAVRKAGL--KNAQVILLSAT 146
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
535-604 |
2.55e-13 |
|
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.
Pssm-ID: 128635 [Multi-domain] Cd Length: 81 Bit Score: 65.78 E-value: 2.55e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 535 ELFSLLKALRKTVAHKHDVPPYVVFQDVSLEQMAMMYPINEQELQNIQGVGAGKAKRYGKEFYTLISKYC 604
Cdd:smart00341 6 RLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEAS 75
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
240-350 |
8.70e-13 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 70.63 E-value: 8.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 240 IIYCLSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVIHYDIPKSLEG 319
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100 110
....*....|....*....|....*....|.
gi 738980454 320 YYQETGRAGRDGEEGICLVFYSRNDLKKLEK 350
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIEQLKE 381
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
219-329 |
5.48e-10 |
|
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: 58.43 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 219 SEDDTNKQIIRFIKQ-HAGKSGIIYCLSRKKVEELAAVL------LANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIV 291
Cdd:cd18796 20 AGESGADAYAEVIFLlERHKSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVV 99
|
90 100 110
....*....|....*....|....*....|....*...
gi 738980454 292 ATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAGR 329
Cdd:cd18796 100 ATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
283-340 |
6.56e-10 |
|
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: 55.79 E-value: 6.56e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 738980454 283 LMEDIDVIVATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAGRDG-EEGICLVFY 340
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
240-303 |
1.38e-09 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 61.45 E-value: 1.38e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738980454 240 IIYCLSRKKVEELAAVLlanDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKP 303
Cdd:COG1202 431 IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFP 491
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
217-339 |
4.40e-09 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 55.64 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 217 KKSEDDTNKQIIRFIKQHAGKSG-IIYCLSRKKVEELAAVLlandIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIA 295
Cdd:cd18795 23 VMNKFDSDIIVLLKIETVSEGKPvLVFCSSRKECEKTAKDL----AGIAFHHAGLTREDRELVEELFREGLIKVLVATST 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 738980454 296 FGMGIDKPDVRFVI----HYD------IPkSLEgYYQETGRAGRDG--EEGICLVF 339
Cdd:cd18795 99 LAAGVNLPARTVIIkgtqRYDgkgyreLS-PLE-YLQMIGRAGRPGfdTRGEAIIM 152
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
224-353 |
5.05e-09 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 59.48 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 224 NKQIIRFIKQHAGKSGIIYCLSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKP 303
Cdd:PRK11634 233 NEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVE 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 738980454 304 DVRFVIHYDIPKSLEGYYQETGRAGRDGEEGICLVFY---SRNDLKKLEKFME 353
Cdd:PRK11634 313 RISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVenrERRLLRNIERTMK 365
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
229-331 |
1.08e-08 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 58.03 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 229 RFIKQHAGKSGIIYCLSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFV 308
Cdd:PRK11192 238 HLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHV 317
|
90 100
....*....|....*....|....*.
gi 738980454 309 IHYDIPKSLEGYYQE---TGRAGRDG 331
Cdd:PRK11192 318 INFDMPRSADTYLHRigrTGRAGRKG 343
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
24-146 |
3.11e-08 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 54.13 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 24 QEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSL--IME---GTAVVVSPLIALMKNQVDVINGIsegdgvAHYLNSSLKK 98
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLRdpgSRALYLYPTKALAQDQLRSLREL------LEQLGLGIRV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 738980454 99 AEVD-----KVRTDIREGKTKLLYVAPESL------NKEDNIEFLKTVKvsFYAIDEAH 146
Cdd:cd17923 79 ATYDgdtprEERRAIIRNPPRILLTNPDMLhyallpHHDRWARFLRNLR--YVVLDEAH 135
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
222-370 |
9.60e-08 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 55.30 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 222 DTNKQIIRFIKQHAGKSGIIYCLSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGID 301
Cdd:PRK01297 321 DKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIH 400
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738980454 302 KPDVRFVIHYDIPKSLEGYYQETGRAGRDGEEGICLVFYSRNDLKKLekfmegkPIAEQDIGRQLLQET 370
Cdd:PRK01297 401 IDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQL-------PEIEELLGRKISCEM 462
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
225-368 |
2.00e-07 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 54.39 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 225 KQIIRFIKQHAGKSgIIYCLSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPD 304
Cdd:PTZ00110 367 KMLLQRIMRDGDKI-LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKD 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738980454 305 VRFVIHYDIPKSLEGYYQETGRAGRDGEEGICLVFYSRNDLK---KLEKFMEGkpiAEQDIGRQLLQ 368
Cdd:PTZ00110 446 VKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRlarDLVKVLRE---AKQPVPPELEK 509
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
24-369 |
1.07e-06 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 51.82 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 24 QEAIIRHLLAGyDAFVL-MPTGGGKSLCYQLP---SLIMEGTAVVVSPLIALmknqvdvingISEgdgVAHYLNSSLKKA 99
Cdd:COG1204 28 AEALEAGLLEG-KNLVVsAPTASGKTLIAELAilkALLNGGKALYIVPLRAL----------ASE---KYREFKRDFEEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 100 EVD-KVRTDIREGKTKLL-----YVA-PESL-----NKEDNIEflktvKVSFYAIDEAHCISEwghdfrpEYRKIRnaIE 167
Cdd:COG1204 94 GIKvGVSTGDYDSDDEWLgrydiLVAtPEKLdsllrNGPSWLR-----DVDLVVVDEAHLIDD-------ESRGPT--LE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 168 VI--------GRAPIIALTATAT-AKvrtDIVRSLGiegCAEFRSSFnRP---NLYYEVRPKKSEDDTN----KQIIRFI 231
Cdd:COG1204 160 VLlarlrrlnPEAQIVALSATIGnAE---EIAEWLD---AELVKSDW-RPvplNEGVLYDGVLRFDDGSrrskDPTLALA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 232 KQHAGKSG--IIYCLSRKKVEELAAVL------------------LANDIKAAP-------------------YHAGLDS 272
Cdd:COG1204 233 LDLLEEGGqvLVFVSSRRDAESLAKKLadelkrrltpeereeleeLAEELLEVSeethtnekladclekgvafHHAGLPS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 273 EVRSKTQDQFLMEDIDVIVAT--IAfgMGIDKP-------DVRFVIHYDIPkSLEgYYQETGRAGRDGE----EGICLVF 339
Cdd:COG1204 313 ELRRLVEDAFREGLIKVLVATptLA--AGVNLParrviirDTKRGGMVPIP-VLE-FKQMAGRAGRPGYdpygEAILVAK 388
|
410 420 430
....*....|....*....|....*....|
gi 738980454 340 YSRNDLKKLEKFMEGKPiaeQDIGRQLLQE 369
Cdd:COG1204 389 SSDEADELFERYILGEP---EPIRSKLANE 415
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
275-339 |
5.84e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 49.20 E-value: 5.84e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738980454 275 RSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAGRDGEEGICLVF 339
Cdd:PRK04837 294 RLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
217-356 |
3.78e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 47.19 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 217 KKSEDDTNkQIIRFIKQHAGKSgIIYCLSRKKVEELAAVLLA-----NDIKA--------------------APYHAGLD 271
Cdd:PRK01172 219 ERSQVDIN-SLIKETVNDGGQV-LVFVSSRKNAEDYAEMLIQhfpefNDFKVssennnvyddslnemlphgvAFHHAGLS 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 272 SEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPdVRFVIHYDIPKSLEGYY---------QETGRAGRDG--EEGICLVFY 340
Cdd:PRK01172 297 NEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP-ARLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPGydQYGIGYIYA 375
|
170
....*....|....*..
gi 738980454 341 -SRNDLKKLEKFMEGKP 356
Cdd:PRK01172 376 aSPASYDAAKKYLSGEP 392
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
219-367 |
4.22e-04 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 43.79 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 219 SEDDTNKQIIRFIKQHAGKSGIIYCLSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVAT--IAF 296
Cdd:PRK04537 240 ADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATdvAAR 319
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738980454 297 GMGIDkpDVRFVIHYDIPKSLEGYYQETGRAGRDGEEGICLVF----YSRNdLKKLEKFMEGKpIAEQDIGRQLL 367
Cdd:PRK04537 320 GLHID--GVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFacerYAMS-LPDIEAYIEQK-IPVEPVTAELL 390
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
267-356 |
9.17e-04 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 42.62 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 267 HAGLDSEVRsKTQDQfLMED--IDVIVATIAFGMGIDKPdVRFVI-----------HYDIpKSLEgYYQETGRAGRDG-- 331
Cdd:COG4581 306 HAGMLPKYR-RLVEE-LFQAglLKVVFATDTLAVGINMP-ARTVVftklskfdgerHRPL-TARE-FHQIAGRAGRRGid 380
|
90 100
....*....|....*....|....*.
gi 738980454 332 EEGICLVFYSR-NDLKKLEKFMEGKP 356
Cdd:COG4581 381 TEGHVVVLAPEhDDPKKFARLASARP 406
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
7-54 |
9.68e-04 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 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: 350707 [Multi-domain] Cd Length: 214 Bit Score: 41.03 E-value: 9.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 738980454 7 LIDNLKHYFGFDNFKGEQEAIIRHLLAGYDAFVLMPTGGGKSLCYQLP 54
Cdd:cd17949 1 LVSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLP 48
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
257-331 |
1.01e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 42.64 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 257 LANDIK--AAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVIH----YD-------IPkSLEgYYQE 323
Cdd:PRK02362 298 LADCVAkgAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRdyrrYDggagmqpIP-VLE-YHQM 375
|
....*...
gi 738980454 324 TGRAGRDG 331
Cdd:PRK02362 376 AGRAGRPG 383
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
280-331 |
1.04e-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: 39.88 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 738980454 280 DQFLMEDIDVIVATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAGRDG 331
Cdd:cd18802 84 DKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
250-356 |
1.10e-03 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 42.50 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 250 EELAAVLLANdikAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVIH----------YDIPkSLEg 319
Cdd:PRK00254 288 EKLKKALRGG---VAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRdtkrysnfgwEDIP-VLE- 362
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 738980454 320 YYQETGRAGRD--GEEGICLVFYSRNDLKKL-EKFMEGKP 356
Cdd:PRK00254 363 IQQMMGRAGRPkyDEVGEAIIVATTEEPSKLmERYIFGKP 402
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
511-602 |
2.17e-03 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 41.01 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 511 VLDAEFKDEPNDAEAY---GGGAVLDPELFSLLKAL---RKTVAHKHDVPPYVVFQDVSLEQMAMMYPINEQELQNIQGV 584
Cdd:COG0349 181 RLLDPATYREDPEEAWlrlKGAWKLNPRQLAVLRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGL 260
|
90
....*....|....*...
gi 738980454 585 GAGKAKRYGKEFYTLISK 602
Cdd:COG0349 261 SPGEIRRHGEELLAAVAE 278
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
252-329 |
4.58e-03 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 40.18 E-value: 4.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738980454 252 LAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVIHYDIPKSLEGYYQETGRAGR 329
Cdd:PRK10590 261 LAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
240-329 |
4.68e-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: 38.11 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 240 IIYCLSRKKVEELAAVLLAND--IKA--------APYHAGLDSEVRSKTQDQFLMEDIDVIVATIAFGMGIDKPDVRFVI 309
Cdd:cd18801 34 IIFSEFRDSAEEIVNFLSKIRpgIRAtrfigqasGKSSKGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLII 113
|
90 100
....*....|....*....|
gi 738980454 310 HYDIPKSLEGYYQETGRAGR 329
Cdd:cd18801 114 CYDASPSPIRMIQRMGRTGR 133
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
34-180 |
4.74e-03 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 38.33 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 34 GYDAFVLMPTGGGKSLCYQLPSL--IME----GTAVV-VSPLIALMKNQVDVINGISEGDGVAhylnsslkkaevdkVRT 106
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALssLADepekGVQVLyISPLKALINDQERRLEEPLDEIDLE--------------IPV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 107 DIREGKTK-------------LLYVAPESL----NKEDNIEFLKTVKvsFYAIDEAHCI--SEWGHDFRPEYRKIRNAIe 167
Cdd:cd17922 67 AVRHGDTSqsekakqlknppgILITTPESLelllVNKKLRELFAGLR--YVVVDEIHALlgSKRGVQLELLLERLRKLT- 143
|
170
....*....|...
gi 738980454 168 vIGRAPIIALTAT 180
Cdd:cd17922 144 -GRPLRRIGLSAT 155
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
24-166 |
6.10e-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: 38.58 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 24 QEAIIRHLLAGYDAFVLMPTGGGKSLCYQLPSL--IMEGTAVVVSPLIALM-------KNQV-DVINGISEGDGVAHYL- 92
Cdd:cd00268 17 QAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekLLPEPKKKGRGPQALVlaptrelAMQIaEVARKLGKGTGLKVAAi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 93 ---NSSLKKAEVDKVRTDIregktkllYVA-PESLNkeDNIE--FLKTVKVSFYAIDEAhcisewghD------FRPEYR 160
Cdd:cd00268 97 yggAPIKKQIEALKKGPDI--------VVGtPGRLL--DLIErgKLDLSNVKYLVLDEA--------DrmldmgFEEDVE 158
|
....*.
gi 738980454 161 KIRNAI 166
Cdd:cd00268 159 KILSAL 164
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
213-329 |
9.64e-03 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB 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: 350177 [Multi-domain] Cd Length: 171 Bit Score: 37.61 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738980454 213 EVRPKKSE-DDTNKQIIRFIKQhaGKSGIIYCLSRKKVEELAAVLLANDIKAAPYHAGLDSEVRSKTQDQFLMEDIDVIV 291
Cdd:cd18790 5 EVRPTEGQvDDLLGEIRKRVAR--GERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLV 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 738980454 292 ATIAFGMGIDKPDVRFVIHYDIPKslEGYY-------QETGRAGR 329
Cdd:cd18790 83 GINLLREGLDLPEVSLVAILDADK--EGFLrsetsliQTIGRAAR 125
|
|
| |
