|
Name |
Accession |
Description |
Interval |
E-value |
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
5-585 |
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: 784.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 5 ARAILQQNFGYQDFRNGQVDVISKLCAGEDTLAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAA 84
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 85 TFINSTLTNREIDIRLDAAFSGELKMLYIAPERIETPGFQRLIEQVPISLFAIDEAHCISQWGHDFRPSYLTLCDSLDKM 164
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 165 TRRPlVIALTATATQAVSDDICRLLKIRADSVVKTGFSRDNLAFQVVKGQDKDKYLIDYLTKNVTESGIIYASTRKEVER 244
Cdd:TIGR01389 161 PQVP-RIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 245 LHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDG 324
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 325 VPSDCILLFSPQDSRIQQFLIEQSEMDDERKQNEFAKLRQMTGYGYTEICLQKYIVQYFGDDEP-NCGKCSNCLDTREAT 403
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVePCGNCDNCLDPPKSY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 404 DITILAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKDASQKDVLQLIDYLTAEKYLQPTDSQFP 483
Cdd:TIGR01389 400 DATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIYI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 484 SLKLTDRAVSVLRGELKVERKQAKRAEKVK--------IDVNSDLFEKLREVRRELAAKHKVPPYIIFSDETLREMCAYM 555
Cdd:TIGR01389 480 GLQLTEAARKVLKNEVEVLLRPFKVVAKEKtrvqknlsVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKR 559
|
570 580 590
....*....|....*....|....*....|
gi 489828358 556 PQTEDALLEVKGIGAMKRDKYGAEFLAVLQ 585
Cdd:TIGR01389 560 PATLNALLKIKGVGQNKLDRYGEAFLEVIR 589
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-472 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 739.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 1 MIEQARAILQQNFGYQDFRNGQVDVISKLCAGEDTLAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSE 80
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 81 GIAATFINSTLTNREIDIRLDAAFSGELKMLYIAPERIETPGFQRLIEQVPISLFAIDEAHCISQWGHDFRPSYLTLCDS 160
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 161 LDKMTRRPlVIALTATATQAVSDDICRLLKIRADSVVKTGFSRDNLAFQVVKG--QDKDKYLIDYLTKNVTESGIIYAST 238
Cdd:COG0514 161 RERLPNVP-VLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGGSGIVYCLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 239 RKEVERLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAG 318
Cdd:COG0514 240 RKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 319 RAGRDGVPSDCILLFSPQDSRIQQFLIEQSEMDDERKQNEFAKLRQMTGYGYTEICLQKYIVQYFGDDEP-NCGKCSNCL 397
Cdd:COG0514 320 RAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAePCGNCDNCL 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489828358 398 DTREATDITILAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKDASQKDVLQLIDYLTAE 472
Cdd:COG0514 400 GPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
4-586 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 547.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 4 QARAILQQNFGYQDFRNGQVDVISKLCAGEDTLAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIA 83
Cdd:PRK11057 12 LAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 84 ATFINSTLTNREIDIRLDAAFSGELKMLYIAPERIETPGFQRLIEQVPISLFAIDEAHCISQWGHDFRPSYLTLCDSLDK 163
Cdd:PRK11057 92 AACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 164 MTRRPlVIALTATATQAVSDDICRLLKIRADSVVKTGFSRDNLAFQVVKGQDKDKYLIDYLTKNVTESGIIYASTRKEVE 243
Cdd:PRK11057 172 FPTLP-FMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 244 RLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRD 323
Cdd:PRK11057 251 DTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 324 GVPSDCILLFSPQDSRIQQFLIEQSEmDDERKQNEFAKLRQMTGYGYTEICLQKYIVQYFGD-DEPNCGKCSNCLDTREA 402
Cdd:PRK11057 331 GLPAEAMLFYDPADMAWLRRCLEEKP-AGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEgRQEPCGNCDICLDPPKQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 403 TDITILAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKDASQKDVLQLIDYLTAEKYLQPTDSQF 482
Cdd:PRK11057 410 YDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 483 PSLKLTDRAVSVLRGE----LKVERKQAKRAEKVKIDVNSD----LFEKLREVRRELAAKHKVPPYIIFSDETLREMCAY 554
Cdd:PRK11057 490 SALQLTEAARPVLRGEvslqLAVPRIVALKPRAMQKSFGGNydrkLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQ 569
|
570 580 590
....*....|....*....|....*....|..
gi 489828358 555 MPQTEDALLEVKGIGAMKRDKYGAEFLAVLQQ 586
Cdd:PRK11057 570 MPITASEMLSVNGVGQRKLERFGKPFMALIRA 601
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
8-456 |
7.92e-155 |
|
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: 452.69 E-value: 7.92e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 8 ILQQNFGYQDFRNGQVDVISKLCAGEDTLAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAATFI 87
Cdd:TIGR00614 2 ILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 88 NSTLTNREIDIRLDAAFSGELKMLYIAPERIETPG--FQRLIEQVPISLFAIDEAHCISQWGHDFRPSYLTLcDSLDKMT 165
Cdd:TIGR00614 82 NSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNrlLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKAL-GSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 166 RRPLVIALTATATQAVSDDICRLLKIRADSVVKTGFSRDNLAFQVvkGQDKDKYLIDYLTKNVTE----SGIIYASTRKE 241
Cdd:TIGR00614 161 PNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEV--RRKTPKILEDLLRFIRKEfegkSGIIYCPSRKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 242 VERLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAG 321
Cdd:TIGR00614 239 VEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 322 RDGVPSDCILLFSPQD-SRIQQFLIEQSemdDERKQNEFAKLRQMTGYgYTEI--CLQKYIVQYFGDDEPN--------- 389
Cdd:TIGR00614 319 RDGLPSECHLFYAPADmNRLRRLLMEEP---DGNFRTYKLKLYEMMEY-CLNSstCRRLILLSYFGEKGFNksfcimgte 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489828358 390 --CGKCSNCLD------TREATDITILAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKD 456
Cdd:TIGR00614 395 kcCDNCCKRLDyktkdvTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKD 469
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
13-581 |
1.62e-105 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 344.19 E-value: 1.62e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 13 FGYQDFRNGQVDVISKLCAGEDTLAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAATFINSTLT 92
Cdd:PLN03137 456 FGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGME 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 93 ---NREIDIRLDAAFSgELKMLYIAPERI-ETPGFQRLIEQVP----ISLFAIDEAHCISQWGHDFRPSYLTLCDSLDKM 164
Cdd:PLN03137 536 waeQLEILQELSSEYS-KYKLLYVTPEKVaKSDSLLRHLENLNsrglLARFVIDEAHCVSQWGHDFRPDYQGLGILKQKF 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 165 TRRPlVIALTATATQAVSDDICRLLKIRADSVVKTGFSRDNLAFQVVKGQDKDKYLIDYLTK--NVTESGIIYASTRKEV 242
Cdd:PLN03137 615 PNIP-VLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKCLEDIDKFIKenHFDECGIIYCLSRMDC 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 243 ERLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGR 322
Cdd:PLN03137 694 EKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGR 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 323 DGVPSDCILLFSPQD-----SRIQQFLIEQSEM---------DDERKQNEFAKLRQMTGYGYTEI-CLQKYIVQYFGD-- 385
Cdd:PLN03137 774 DGQRSSCVLYYSYSDyirvkHMISQGGVEQSPMamgynrmasSGRILETNTENLLRMVSYCENEVdCRRFLQLVHFGEkf 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 386 DEPNCGK-CSNCLDTREAT--DITILAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKDASQKDV 462
Cdd:PLN03137 854 DSTNCKKtCDNCSSSKSLIdkDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLSKGEA 933
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 463 LQLIDYLTAEKYL-------------------------------QPTDSQFPS----LKLTDRAVSVLRGELKVERKQAK 507
Cdd:PLN03137 934 SRILHYLVTEDILaedvkksdlygsvssllkvneskayklfsggQTIIMRFPSsvkaSKPSKFEATPAKGPLTSGKQSTL 1013
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 508 RAEK-----VKIDVNSDLFEKLREVRRELA--AKHKVPPYIIFSDETLREMCAYMPQTEDALLEVKGIGAMKRDKYGAEF 580
Cdd:PLN03137 1014 PMATpaqppVDLNLSAILYTALRKLRTALVkeAGDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKYGDRL 1093
|
.
gi 489828358 581 L 581
Cdd:PLN03137 1094 L 1094
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
6-202 |
1.08e-95 |
|
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: 290.98 E-value: 1.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 6 RAILQQNFGYQDFRNGQVDVISKLCAGEDTLAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAAT 85
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 86 FINSTLTNREIDIRLDAAFSGELKMLYIAPERIETPGFQRLIEQVP----ISLFAIDEAHCISQWGHDFRPSYLTLCDsL 161
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGR-L 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489828358 162 DKMTRRPLVIALTATATQAVSDDICRLLKIRADSVVKTGFS 202
Cdd:cd17920 160 RRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
7-201 |
1.45e-80 |
|
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: 251.79 E-value: 1.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 7 AILQQNFGYQDFRNGQVDVISKLCAGEDTLAIMPTGGGKSLCYQIPALLFD----GLTIVVSPLISLMKDQVDALVSeGI 82
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPR-AI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 83 AATFINSTLTNREIDIRLDAAFSGELKMLYIAPERIETPGFQRLIEQV-PISLFAIDEAHCISQWGHDFRPSYLTLCDSL 161
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTpPISLLVVDEAHCISEWSHNFRPDYLRLCRVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489828358 162 DKMTRRPLVIALTATATQAVSDDICRLLKIRADSVVKTGF 201
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPL 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
3-193 |
1.91e-57 |
|
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: 191.81 E-value: 1.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 3 EQARAILQQNFGYQDFRNGQVDVISKLCAGEDTLAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGI 82
Cdd:cd18015 4 GKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 83 AATFINSTLTNREIDIRLDAAFSG--ELKMLYIAPERIETPgfQRLIEQVP-------ISLFAIDEAHCISQWGHDFRPS 153
Cdd:cd18015 84 SATMLNASSSKEHVKWVHAALTDKnsELKLLYVTPEKIAKS--KRFMSKLEkaynagrLARIAIDEVHCCSQWGHDFRPD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489828358 154 YLTLcDSLDKMTRRPLVIALTATATQAVSDDICRLLKIRA 193
Cdd:cd18015 162 YKKL-GILKRQFPNVPILGLTATATSKVLKDVQKILCIQK 200
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
203-333 |
2.65e-55 |
|
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: 183.18 E-value: 2.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 203 RDNLAFQVVKGQDKDKYLID---YLTKNVTESGIIYASTRKEVERLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDD 279
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLlkrIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489828358 280 IRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILLF 333
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
9-201 |
5.55e-54 |
|
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: 5.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 9 LQQNFGYQDFRNGQVDVI-SKLCAGEDTLAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAATFI 87
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIrSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 88 NSTLTNREidirLDAAFSGELKMLYIAPERIEtpGFQRLIEQVP--ISLFAIDEAHCISQWGHDFRPSYLTLcDSLDKMT 165
Cdd:cd18017 84 GSAQSQNV----LDDIKMGKIRVIYVTPEFVS--KGLELLQQLRngITLIAIDEAHCVSQWGHDFRSSYRHL-GSIRNRL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 489828358 166 RRPLVIALTATATQAVSDDICRLLKIRADSVVKTGF 201
Cdd:cd18017 157 PNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSF 192
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
6-192 |
4.17e-52 |
|
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: 177.28 E-value: 4.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 6 RAILQQNFGYQDFRNG-QVDVISKLCAGE-DTLAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIA 83
Cdd:cd18014 1 RSTLKKVFGHSDFKSPlQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 84 ATFINSTLTNREID-IRLD-AAFSGELKMLYIAPERIETPGFQRLIEQV----PISLFAIDEAHCISQWGHDFRPSYLTL 157
Cdd:cd18014 81 VDSLNSKLSAQERKrIIADlESEKPQTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 489828358 158 cDSLDKMTRRPLVIALTATATQAVSDDICRLLKIR 192
Cdd:cd18014 161 -GALRSRYGHVPWVALTATATPQVQEDIFAQLRLK 194
|
|
| DpdF |
NF041063 |
protein DpdF; |
8-340 |
1.39e-49 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 183.96 E-value: 1.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 8 ILQQNFGYQDFR-NGQVDVI-SKLCAGED-TLAI-MPTGGGKSLCYQIPALLF---DGLTIVVSPLISLMKDQVDALVsE 80
Cdd:NF041063 130 FLAEALGFTHYRsPGQREAVrAALLAPPGsTLIVnLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQERRAR-E 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 81 GIAATFI-----------NSTLTNREI--DIRldaafSGELKMLYIAPERIET---PGFQRLIEQVPISLFAIDEAHCIS 144
Cdd:NF041063 209 LLRRAGPdlggplawhggLSAEERAAIrqRIR-----DGTQRILFTSPESLTGslrPALFDAAEAGLLRYLVVDEAHLVD 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 145 QWGHDFRPSY----------LTLCDSldkmTRRPLVIALTATATQAVSDDICRLlkiradsvvktgFSRDNlAFQVVKGQ 214
Cdd:NF041063 284 QWGDGFRPEFqllaglrrslLRLAPS----GRPFRTLLLSATLTESTLDTLETL------------FGPPG-PFIVVSAV 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 215 dkdkYL---IDY-LTKNVTESG----------------IIYASTRKEVERLHSFLQKKGVES-GMYHGGMTDLARK---- 269
Cdd:NF041063 347 ----QLrpePAYwVAKCDSEEErrervlealrhlprplILYVTKVEDAEAWLQRLRAAGFRRvALFHGDTPDAERErlie 422
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489828358 270 DWQEkflyDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILLFSPQDSRI 340
Cdd:NF041063 423 QWRE----NELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDI 489
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
8-201 |
2.58e-49 |
|
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: 170.01 E-value: 2.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 8 ILQQNFGYQDFRNGQVDVISKLCAGEDTLAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAATFI 87
Cdd:cd18016 8 IFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 88 NSTLTNREIDiRLDAAFSGE---LKMLYIAPERIETPG-----FQRLIEQVPISLFAIDEAHCISQWGHDFRPSYLTLCD 159
Cdd:cd18016 88 TGDKTDAEAT-KIYLQLSKKdpiIKLLYVTPEKISASNrlistLENLYERKLLARFVIDEAHCVSQWGHDFRPDYKRLNM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489828358 160 SLDKMTRRPlVIALTATATQAVSDDICRLLKIRADSVVKTGF 201
Cdd:cd18016 167 LRQKFPSVP-MMALTATATPRVQKDILNQLKMLRPQVFTMSF 207
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
399-505 |
1.31e-36 |
|
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: 131.89 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 399 TREATDITILAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKDASQKDVLQLIDYLTAEKYLQPT 478
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*..
gi 489828358 479 DSQFPSLKLTDRAVSVLRGELKVERKQ 505
Cdd:pfam09382 81 IEFYSVLKLTPKAREVLKGEEKVMLRV 107
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
404-495 |
2.63e-32 |
|
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: 119.50 E-value: 2.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 404 DITILAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKDASQKDVLQLIDYLTAEKYLQPTDSQFP 483
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 489828358 484 SLKLTDRAVSVL 495
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
215-324 |
7.35e-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: 96.51 E-value: 7.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 215 DKDKYLIDYLTKNVTESGIIYASTRKEVErLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAFGMGIN 294
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 489828358 295 KSNVRFVIHYNIPRNIEAYYQEAGRAGRDG 324
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
243-324 |
3.12e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 93.82 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 243 ERLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGR 322
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 489828358 323 DG 324
Cdd:smart00490 81 AG 82
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
519-584 |
9.09e-23 |
|
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: 91.83 E-value: 9.09e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489828358 519 DLFEKLREVRRELAAKHKVPPYIIFSDETLREMCAYMPQTEDALLEVKGIGAMKRDKYGAEFLAVL 584
Cdd:pfam00570 3 ALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
22-183 |
4.66e-22 |
|
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: 93.08 E-value: 4.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 22 QVDVISKLCAGEDTLAIMPTGGGKSLCYQIPAL-----LFDGL-TIVVSPLISLMKDQVDALVSEGI-AATFINSTLTNR 94
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdkLDNGPqALVLAPTRELAEQIYEELKKLGKgLGLKVASLLGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 95 EIDIRLDAAfsGELKMLYIAPERIETP-GFQRLIEQVpiSLFAIDEAHCISQWGhdFRPSYLTLCDSLDKMTRrplVIAL 173
Cdd:pfam00270 84 SRKEQLEKL--KGPDILVGTPGRLLDLlQERKLLKNL--KLLVLDEAHRLLDMG--FGPDLEEILRRLPKKRQ---ILLL 154
|
170
....*....|
gi 489828358 174 TATATQAVSD 183
Cdd:pfam00270 155 SATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
13-189 |
1.06e-20 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 90.24 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 13 FGYQDFRNGQVDVISKLCAGE-DTLAIMPTGGGKSLCYQIPALLF-----DGLTIVVSPLISLMKDQVDALVSEGIAATF 86
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 87 INSTLTNRE-IDIRLDAAFSGELKMLYIAPERIETPGFQRLIEQVPISLFAIDEAHCISQWGhdFRPSYLTLCDSLDKMT 165
Cdd:smart00487 84 KVVGLYGGDsKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLLPKNV 161
|
170 180
....*....|....*....|....
gi 489828358 166 RRplvIALTATATQAVsDDICRLL 189
Cdd:smart00487 162 QL---LLLSATPPEEI-ENLLELF 181
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
208-322 |
3.57e-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: 86.79 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 208 FQVVKGQDKDKYLIDYL-TKNVTESGIIYASTRKEVERLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVAT 286
Cdd:cd18787 5 YVVVEEEEKKLLLLLLLlEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVAT 84
|
90 100 110
....*....|....*....|....*....|....*.
gi 489828358 287 NAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGR 322
Cdd:cd18787 85 DVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
335-397 |
2.61e-19 |
|
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: 81.95 E-value: 2.61e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489828358 335 PQDSRIQQFLIEQSEMDDERKQNEFAKLRQMTGYG-YTEICLQKYIVQYFGD--DEPNCGKCSNCL 397
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCeNTTDCRRKQLLRYFGEefDSEPCGNCDNCL 66
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
514-586 |
5.13e-18 |
|
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: 78.88 E-value: 5.13e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489828358 514 IDVNSDLFEKLREVRRELAAKHKVPPYIIFSDETLREMCAYMPQTEDALLEVKGIGAMKRDKYGAEFLAVLQQ 586
Cdd:smart00341 1 RERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQE 73
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
210-353 |
3.23e-17 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 84.04 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 210 VVKGQDKDKYLIDYLTKNVTESGIIYASTRKEVERLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAF 289
Cdd:COG0513 222 LVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVA 301
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489828358 290 GMGINKSNVRFVIHYNIPRNIEAYYQEAG---RAGRDGVpsdCILLFSPQDSR----IQQFL---IEQSEMDDE 353
Cdd:COG0513 302 ARGIDIDDVSHVINYDLPEDPEDYVHRIGrtgRAGAEGT---AISLVTPDERRllraIEKLIgqkIEEEELPGF 372
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
210-338 |
3.37e-14 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 75.33 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 210 VVKGQDKDKYLIDYLTKNVTESGIIYASTRKEVERLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAF 289
Cdd:PRK01297 316 AVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVA 395
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489828358 290 GMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILLFSPQDS 338
Cdd:PRK01297 396 GRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDA 444
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
223-332 |
8.32e-14 |
|
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: 68.82 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 223 YLTKNVTESG---IIYASTRKEVERLHSFLQKKGVESGM-------YHGGMTDLARKDWQEKFLYDDIRVIVATNAFGMG 292
Cdd:cd18797 26 RLFADLVRAGvktIVFCRSRKLAELLLRYLKARLVEEGPlaskvasYRAGYLAEDRREIEAELFNGELLGVVATNALELG 105
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489828358 293 INKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILL 332
Cdd:cd18797 106 IDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
22-346 |
9.61e-14 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 74.49 E-value: 9.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 22 QVDVISKLCAGEDTLAIMPTGGGKSLCYQIPALlfDGL-------TIVVSPLISLMKDQVDALVS------EGI-AATFI 87
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVL--EALledpgatALYLYPTKALARDQLRRLRElaealgLGVrVATYD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 88 NSTLTN--REI----DIRL---DaafsgelkMLY--IAPERietPGFQRLIEQVpiSLFAIDEAHcisqwghdfrpSY-- 154
Cdd:COG1205 139 GDTPPEerRWIrehpDIVLtnpD--------MLHygLLPHH---TRWARFFRNL--RYVVIDEAH-----------TYrg 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 155 -------------LTLCDSLDkmtRRPLVIALTAT---ATQAVSddicRLLKIRADSVVKTG--FSRDNLAF----QVVK 212
Cdd:COG1205 195 vfgshvanvlrrlRRICRHYG---SDPQFILASATignPAEHAE----RLTGRPVTVVDEDGspRGERTFVLwnppLVDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 213 GQDKDKYLI-DYLTKNVTESG---IIYASTRKEVERLHSFLQKKGVESGM------YHGGMTDLARKDWQEKFLYDDIRV 282
Cdd:COG1205 268 GIRRSALAEaARLLADLVREGlrtLVFTRSRRGAELLARYARRALREPDLadrvaaYRAGYLPEERREIERGLRSGELLG 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489828358 283 IVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILLfsPQDSRIQQFLIE 346
Cdd:COG1205 348 VVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLV--AGDDPLDQYYVR 409
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
118-346 |
1.31e-11 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 67.12 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 118 IETPGfqRLI--------EQVPISLFAIDEAHCISQWGhdFRPSYLTLCDSLDKmtrrPLVIALTATATQAVSDDICRLL 189
Cdd:PLN00206 251 VGTPG--RLIdllskhdiELDNVSVLVLDEVDCMLERG--FRDQVMQIFQALSQ----PQVLLFSATVSPEVEKFASSLA 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 190 KIRAdsVVKTGFS-RDNLAFQV----VKGQDKDKYLIDYLTKNV--TESGIIYASTRKEVERLHSFLQK-KGVESGMYHG 261
Cdd:PLN00206 323 KDII--LISIGNPnRPNKAVKQlaiwVETKQKKQKLFDILKSKQhfKPPAVVFVSSRLGADLLANAITVvTGLKALSIHG 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 262 GMTDLARKDWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILLFSPQDSRIQ 341
Cdd:PLN00206 401 EKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLF 480
|
....*
gi 489828358 342 QFLIE 346
Cdd:PLN00206 481 PELVA 485
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
32-176 |
5.80e-11 |
|
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: 60.88 E-value: 5.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 32 GEDTLAIMPTGGGKSLCYQIPALL----FDGLTIVVSPLISLMKDQ---VDALVSEGIAATFINSTLTNREidirLDAAF 104
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLlllkKGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEE----REKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489828358 105 SGELKMLYIAPERIETPG-FQRLIEQVPISLFAIDEAHCISQWGHDFRPSYLTLCDSLDKmtrRPLVIALTAT 176
Cdd:cd00046 77 LGDADIIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLK---NAQVILLSAT 146
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
215-337 |
1.36e-10 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 63.31 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 215 DKDKYLID-----YLTKNVTESgIIYASTRKEVERLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAF 289
Cdd:PTZ00424 249 EKEEWKFDtlcdlYETLTITQA-IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLL 327
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489828358 290 GMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILLFSPQD 337
Cdd:PTZ00424 328 ARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDD 375
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
276-332 |
5.24e-09 |
|
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: 53.09 E-value: 5.24e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489828358 276 LYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDG-VPSDCILL 332
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
31-320 |
7.32e-09 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 58.50 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 31 AGEDTLAIMPTGGGKSL----CYQipALLFDGLTIVVSPLISLMKDQVDALvsegiAATFINSTLTNREIDIRLDAAFSG 106
Cdd:COG1061 99 GGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEEL-----RRFLGDPLAGGGKKDSDAPITVAT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 107 eLKMLYIAPERIETPGFQRLIeqvpislfAIDEAHcisqwgHDFRPSYLTLCDSLDKmtrrPLVIALTAT---------- 176
Cdd:COG1061 172 -YQSLARRAHLDELGDRFGLV--------IIDEAH------HAGAPSYRRILEAFPA----AYRLGLTATpfrsdgreil 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 177 ------------ATQAVSDDICRLLKIRAdsvVKTGFSRDNLAFQVVKGQDKDKY----------LIDYLTKNV-TESGI 233
Cdd:COG1061 233 lflfdgivyeysLKEAIEDGYLAPPEYYG---IRVDLTDERAEYDALSERLREALaadaerkdkiLRELLREHPdDRKTL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 234 IYASTRKEVERLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYnipRNIEA- 312
Cdd:COG1061 310 VFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILL---RPTGSp 386
|
330
....*....|
gi 489828358 313 --YYQEAGRA 320
Cdd:COG1061 387 reFIQRLGRG 396
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
233-324 |
1.85e-08 |
|
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: 53.71 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 233 IIYASTRKEVERLHSFLqkKGVesGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAFGMGIN--------KSNVRFVIHY 304
Cdd:cd18795 47 LVFCSSRKECEKTAKDL--AGI--AFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKG 122
|
90 100
....*....|....*....|
gi 489828358 305 NIPRNIEAYYQEAGRAGRDG 324
Cdd:cd18795 123 YRELSPLEYLQMIGRAGRPG 142
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
12-322 |
4.97e-08 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 55.67 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 12 NFGYQDFRNGQVDVISK-LCAGEDTLAIMPTGGGKSLCYQIPAL--LFDGLTIV-VSPLIslmkdqvdALVSEgIAATFi 87
Cdd:COG1204 17 ERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLR--------ALASE-KYREF- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 88 NSTLTNREI-------DIRLDAAFSGELKMLYIAPERietpgFQRLIEQVP-----ISLFAIDEAHCIsqwGHDFR-PSY 154
Cdd:COG1204 87 KRDFEELGIkvgvstgDYDSDDEWLGRYDILVATPEK-----LDSLLRNGPswlrdVDLVVVDEAHLI---DDESRgPTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 155 LTLCDSLDKMTRRPLVIALTATATQAvsDDICRLLKirADSVV--------KTG-FSRDNLAFQvvkgqDK----DKYLI 221
Cdd:COG1204 159 EVLLARLRRLNPEAQIVALSATIGNA--EEIAEWLD--AELVKsdwrpvplNEGvLYDGVLRFD-----DGsrrsKDPTL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 222 DYLTKNVTESG--IIYASTRKEVE----RLHSFLQ-----------------------------------KKGVesGMYH 260
Cdd:COG1204 230 ALALDLLEEGGqvLVFVSSRRDAEslakKLADELKrrltpeereeleelaeellevseethtnekladclEKGV--AFHH 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489828358 261 GGMTDLARKDWQEKFLYDDIRVIVATNAFGMGIN--KSNVrfVIH-----YNIPRNIEAYYQEAGRAGR 322
Cdd:COG1204 308 AGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNlpARRV--IIRdtkrgGMVPIPVLEFKQMAGRAGR 374
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
230-322 |
5.62e-08 |
|
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: 52.27 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 230 ESGIIYASTRKEVERLHSFLQKKGVESG-----MYHGGMTDLARKDWQEKFLYD-DIRVIVATNAFGMGINKSNVRFVIH 303
Cdd:cd18796 39 KSTLVFTNTRSQAERLAQRLRELCPDRVppdfiALHHGSLSRELREEVEAALKRgDLKVVVATSSLELGIDIGDVDLVIQ 118
|
90
....*....|....*....
gi 489828358 304 YNIPRNIEAYYQEAGRAGR 322
Cdd:cd18796 119 IGSPKSVARLLQRLGRSGH 137
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
524-586 |
5.88e-08 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 54.88 E-value: 5.88e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489828358 524 LREV---RRELAAKHKVPPYIIFSDETLREMCAYMPQTEDALLEVKGIGAMKRDKYGAEFLAVLQQ 586
Cdd:COG0349 213 LRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAE 278
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
174-364 |
8.35e-07 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 52.16 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 174 TATATQAVSDDICRLLK----IRADSVVKTgfsRDNLA--FQVVKGQDKDKYLIDYLTKNVTESGIIYASTRKEVERLHS 247
Cdd:PRK11634 187 SATMPEAIRRITRRFMKepqeVRIQSSVTT---RPDISqsYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 248 FLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPS 327
Cdd:PRK11634 264 ALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAG 343
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489828358 328 DCILLFSPQDSR------------IQQFLIEQSEMDDERKQNEFA-KLRQ 364
Cdd:PRK11634 344 RALLFVENRERRllrniertmkltIPEVELPNAELLGKRRLEKFAaKVQQ 393
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
31-369 |
2.89e-06 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 50.16 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 31 AGEDTLAIMPTGGGKSLCYQIPALLF----------DG-LTIVVSP---LISLMKDQvdalvsegiAATFinstltNREI 96
Cdd:PTZ00110 166 SGRDMIGIAETGSGKTLAFLLPAIVHinaqpllrygDGpIVLVLAPtreLAEQIREQ---------CNKF------GASS 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 97 DIRLDAAFSGELKMLYIAPER------IETPGfqRLIEQVP--------ISLFAIDEAHCISQWGhdFRPSYLTLCDSLd 162
Cdd:PTZ00110 231 KIRNTVAYGGVPKRGQIYALRrgveilIACPG--RLIDFLEsnvtnlrrVTYLVLDEADRMLDMG--FEPQIRKIVSQI- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 163 kmtrRPLVIALTATAT-----QAVSDDICR--LLKIRADSVVKTGFSRDNLAFQVVKGQDKDKYLIDYLTKNVTESG--I 233
Cdd:PTZ00110 306 ----RPDRQTLMWSATwpkevQSLARDLCKeePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGDkiL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 234 IYASTRKEVERLHSFLQKKGVESGMYHGGmtdlaRKDWQEKFLYDDIR-----VIVATNAFGMGINKSNVRFVIHYNIPR 308
Cdd:PTZ00110 382 IFVETKKGADFLTKELRLDGWPALCIHGD-----KKQEERTWVLNEFKtgkspIMIATDVASRGLDVKDVKYVINFDFPN 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489828358 309 NIEAYYQEAGRAGRDGVPSDCILLFSPQDSRIQQFLI------------EQSEMDDERKQNEfaKLRQMTGYG 369
Cdd:PTZ00110 457 QIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVkvlreakqpvppELEKLSNERSNGT--ERRRWGGYG 527
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
22-77 |
5.05e-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: 47.19 E-value: 5.05e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489828358 22 QVDVISKLCAGEDTLAIMPTGGGKSLCYQIPAllFDGL-------TIVVSPLISLMKDQVDAL 77
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPI--LEALlrdpgsrALYLYPTKALAQDQLRSL 65
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
6-322 |
1.40e-05 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 47.88 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 6 RAILQQnfGYQDFRNGQVDVISKLCAGEDTLAIMPTGGGKSLCYQIPALLFdgltIVVSPLISLMKDQVDALV----SEG 81
Cdd:PRK10590 14 RAVAEQ--GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQH----LITRQPHAKGRRPVRALIltptREL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 82 IAATFINSTLTNREIDIRLDAAFSGelkmLYIAPER----------IETPG------FQRLIEQVPISLFAIDEAHCISQ 145
Cdd:PRK10590 88 AAQIGENVRDYSKYLNIRSLVVFGG----VSINPQMmklrggvdvlVATPGrlldleHQNAVKLDQVEILVLDEADRMLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 146 WG--HDFRpsyltlcDSLDKMTRRPLVIALTATatqaVSDDICRLLKIRADSVVKTGFSRDNLA-------FQVVKGQDK 216
Cdd:PRK10590 164 MGfiHDIR-------RVLAKLPAKRQNLLFSAT----FSDDIKALAEKLLHNPLEIEVARRNTAseqvtqhVHFVDKKRK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 217 DKYLIDYLTKNVTESGIIYASTRKEVERLHSFLQKKGVESGMYHGGMTDLARKDWQEKFLYDDIRVIVATNAFGMGINKS 296
Cdd:PRK10590 233 RELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIE 312
|
330 340
....*....|....*....|....*.
gi 489828358 297 NVRFVIHYNIPRNIEAYYQEAGRAGR 322
Cdd:PRK10590 313 ELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
224-324 |
4.63e-05 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 46.26 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 224 LTKNVTESGIIYASTRKEVERLHSFLQKKGVESGMYHG--------GMTDLARKDWQEKFLYDDIRVIVATNAFGMGINK 295
Cdd:COG1111 348 LGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDI 427
|
90 100 110
....*....|....*....|....*....|
gi 489828358 296 SNVRFVIHY-NIPRNIEaYYQEAGRAGRDG 324
Cdd:COG1111 428 PEVDLVIFYePVPSEIR-SIQRKGRTGRKR 456
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
218-324 |
4.63e-05 |
|
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: 43.62 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 218 KYLIDYLTKNVTESG--IIYASTRKEVERLHSFLQKKGVESGMYHGGMTDLARKDWQEKF--LYDDIRVIVATNAFGMGI 293
Cdd:cd18793 14 EALLELLEELREPGEkvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFneDPDIRVFLLSTKAGGVGL 93
|
90 100 110
....*....|....*....|....*....|...
gi 489828358 294 NKSNVRFVIHYNIPRN--IEAyyQEAGRAGRDG 324
Cdd:cd18793 94 NLTAANRVILYDPWWNpaVEE--QAIDRAHRIG 124
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
32-176 |
5.63e-04 |
|
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: 41.03 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 32 GEDTLAIMPTGGGKSLCYQIPAL--LFD-----GLTIVVSPLISLMKDQVDALvsegiaatfiNSTLTNREIDIRL---- 100
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALssLADepekgVQVLYISPLKALINDQERRL----------EEPLDEIDLEIPVavrh 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 101 -DAAFSGELKM-------LYIAPERIE----TPGFQRLIEQVpiSLFAIDEAHCISQwghDFRPSYL-TLCDSLDKMTRR 167
Cdd:cd17922 71 gDTSQSEKAKQlknppgiLITTPESLElllvNKKLRELFAGL--RYVVVDEIHALLG---SKRGVQLeLLLERLRKLTGR 145
|
170
....*....|
gi 489828358 168 PLV-IALTAT 176
Cdd:cd17922 146 PLRrIGLSAT 155
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
227-324 |
3.39e-03 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 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: 350192 [Multi-domain] Cd Length: 135 Bit Score: 37.92 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 227 NVTESGIIYASTRKEVERLHSFLQKK-GVESGMYHGGMTDLARKDWQEKF-----LYDdirVIVATNAFGMGINkSNVRF 300
Cdd:cd18805 15 NLRPGDCVVAFSRKDIFSLKREIEKRtGLKCAVIYGALPPETRRQQARLFndpesGYD---VLVASDAIGMGLN-LNIRR 90
|
90 100 110
....*....|....*....|....*....|...
gi 489828358 301 VIHYNIP-------RNIEAYY--QEAGRAGRDG 324
Cdd:cd18805 91 VIFSSLSkfdgnemRPLSPSEvkQIAGRAGRFG 123
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
273-332 |
7.01e-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: 37.19 E-value: 7.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828358 273 EKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGvpSDCILL 332
Cdd:cd18802 84 DKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYILM 141
|
|
| |
