|
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: 791.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 5 AKVILQQNFGYQDFRDGQVDVISKLCAGEDALAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAA 84
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 85 TFINSTLTTHEINLRLDAAFSGEVKMLYIAPERIETPGFQRLIEQVPISLFAIDEAHCISQWGHDFRPSYLTLCDSLDRM 164
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 165 KKRPlVIALTATATQAVSDDICRLLKIGQNSVVKTGFSRDNLAFQVVKGQDKDKYLIDYLSKNKTESGIIYASTRKEVER 244
Cdd:TIGR01389 161 PQVP-RIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 245 LHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDG 324
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 325 VPSDCILLFSPQDSRIQQFLIEQSELDEERKQNEFAKLRQMTGYGYTEICLQKYIVQYFGDDE-ENCGKCSNCLDIREAT 403
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEvEPCGNCDNCLDPPKSY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 404 DVTIQAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKEDSQKDVLQLIDYLIAEKYLQPTDSQFP 483
Cdd:TIGR01389 400 DATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIYI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 484 SLKLTDRAVSVLRGELKVARKQAKRAEKVK--------LAVNSSLFEQLREVRRELASKHKVPPYIIFSDETLREMCAYL 555
Cdd:TIGR01389 480 GLQLTEAARKVLKNEVEVLLRPFKVVAKEKtrvqknlsVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKR 559
|
570 580 590
....*....|....*....|....*....|
gi 1893405659 556 PQDEEALLEVKGIGAMKRDKYGAAFLAVLQ 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: 741.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 1 MIEQAKVILQQNFGYQDFRDGQVDVISKLCAGEDALAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSE 80
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 81 GIAATFINSTLTTHEINLRLDAAFSGEVKMLYIAPERIETPGFQRLIEQVPISLFAIDEAHCISQWGHDFRPSYLTLCDS 160
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 161 LDRMKKRPlVIALTATATQAVSDDICRLLKIGQNSVVKTGFSRDNLAFQVVKG--QDKDKYLIDYLSKNKTESGIIYAST 238
Cdd:COG0514 161 RERLPNVP-VLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGGSGIVYCLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 239 RKEVERLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAG 318
Cdd:COG0514 240 RKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 319 RAGRDGVPSDCILLFSPQDSRIQQFLIEQSELDEERKQNEFAKLRQMTGYGYTEICLQKYIVQYFGDD-EENCGKCSNCL 397
Cdd:COG0514 320 RAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEElAEPCGNCDNCL 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1893405659 398 DIREATDVTIQAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKEDSQKDVLQLIDYLIAE 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: 551.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 4 QAKVILQQNFGYQDFRDGQVDVISKLCAGEDALAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIA 83
Cdd:PRK11057 12 LAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 84 ATFINSTLTTHEINLRLDAAFSGEVKMLYIAPERIETPGFQRLIEQVPISLFAIDEAHCISQWGHDFRPSYLTLCDSLDR 163
Cdd:PRK11057 92 AACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 164 MKKRPlVIALTATATQAVSDDICRLLKIGQNSVVKTGFSRDNLAFQVVKGQDKDKYLIDYLSKNKTESGIIYASTRKEVE 243
Cdd:PRK11057 172 FPTLP-FMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 244 RLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRD 323
Cdd:PRK11057 251 DTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 324 GVPSDCILLFSPQDSRIQQFLIEQSElDEERKQNEFAKLRQMTGYGYTEICLQKYIVQYFGD-DEENCGKCSNCLDIREA 402
Cdd:PRK11057 331 GLPAEAMLFYDPADMAWLRRCLEEKP-AGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEgRQEPCGNCDICLDPPKQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 403 TDVTIQAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKEDSQKDVLQLIDYLIAEKYLQPTDSQF 482
Cdd:PRK11057 410 YDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 483 PSLKLTDRAVSVLRGE----LKVARKQ-AKRAEKVKLA---VNSSLFEQLREVRRELASKHKVPPYIIFSDETLREMCAY 554
Cdd:PRK11057 490 SALQLTEAARPVLRGEvslqLAVPRIVaLKPRAMQKSFggnYDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQ 569
|
570 580 590
....*....|....*....|....*....|..
gi 1893405659 555 LPQDEEALLEVKGIGAMKRDKYGAAFLAVLQQ 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 |
2.08e-154 |
|
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: 451.53 E-value: 2.08e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 8 ILQQNFGYQDFRDGQVDVISKLCAGEDALAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAATFI 87
Cdd:TIGR00614 2 ILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 88 NSTLTTHEINLRLDAAFSGEVKMLYIAPERIETPG--FQRLIEQVPISLFAIDEAHCISQWGHDFRPSYLTLcDSLDRMK 165
Cdd:TIGR00614 82 NSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNrlLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKAL-GSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 166 KRPLVIALTATATQAVSDDICRLLKIGQNSVVKTGFSRDNLAFQVvkGQDKDKYLID---YLSKN-KTESGIIYASTRKE 241
Cdd:TIGR00614 161 PNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEV--RRKTPKILEDllrFIRKEfEGKSGIIYCPSRKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 242 VERLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAG 321
Cdd:TIGR00614 239 VEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 322 RDGVPSDCILLFSPQD-SRIQQFLIEqsELDEERKQNEFAKLRQMTGYGYTEICLQKYIVQYFGDD-----------EEN 389
Cdd:TIGR00614 319 RDGLPSECHLFYAPADmNRLRRLLME--EPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKgfnksfcimgtEKC 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1893405659 390 CGKCSNCLD--IREAT----DVTIQAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKE 456
Cdd:TIGR00614 397 CDNCCKRLDykTKDVTdkvyDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKD 469
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
13-581 |
1.59e-103 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 338.79 E-value: 1.59e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 13 FGYQDFRDGQVDVISKLCAGEDALAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAATFINSTLT 92
Cdd:PLN03137 456 FGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGME 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 93 ---THEINLRLDAAFSgEVKMLYIAPERI-ETPGFQRLIEQVP----ISLFAIDEAHCISQWGHDFRPSYLTLCDSLDRM 164
Cdd:PLN03137 536 waeQLEILQELSSEYS-KYKLLYVTPEKVaKSDSLLRHLENLNsrglLARFVIDEAHCVSQWGHDFRPDYQGLGILKQKF 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 165 KKRPlVIALTATATQAVSDDICRLLKIGQNSVVKTGFSRDNLAFQVVKGQDKDKYLID-YLSKNK-TESGIIYASTRKEV 242
Cdd:PLN03137 615 PNIP-VLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKCLEDIDkFIKENHfDECGIIYCLSRMDC 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 243 ERLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGR 322
Cdd:PLN03137 694 EKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGR 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 323 DGVPSDCILLFSPQD-----SRIQQFLIEQSELD-------------EERKQNefakLRQMTGYGYTEI-CLQKYIVQYF 383
Cdd:PLN03137 774 DGQRSSCVLYYSYSDyirvkHMISQGGVEQSPMAmgynrmassgrilETNTEN----LLRMVSYCENEVdCRRFLQLVHF 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 384 GD--DEENCGK-CSNCLDIREAT--DVTIQAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKEDS 458
Cdd:PLN03137 850 GEkfDSTNCKKtCDNCSSSKSLIdkDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLS 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 459 QKDVLQLIDYLIAEKYL-------------------------------QPTDSQFPS----LKLTDRAVSVLRGELKVAR 503
Cdd:PLN03137 930 KGEASRILHYLVTEDILaedvkksdlygsvssllkvneskayklfsggQTIIMRFPSsvkaSKPSKFEATPAKGPLTSGK 1009
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 504 KQAKRAEK-----VKLAVNSSLFEQLREVRRELA--SKHKVPPYIIFSDETLREMCAYLPQDEEALLEVKGIGAMKRDKY 576
Cdd:PLN03137 1010 QSTLPMATpaqppVDLNLSAILYTALRKLRTALVkeAGDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKY 1089
|
....*
gi 1893405659 577 GAAFL 581
Cdd:PLN03137 1090 GDRLL 1094
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
8-202 |
1.68e-94 |
|
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: 287.89 E-value: 1.68e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 8 ILQQNFGYQDFRDGQVDVISKLCAGEDALAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAATFI 87
Cdd:cd17920 3 ILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 88 NSTLTTHEINLRLDAAFSGEVKMLYIAPERIETPGFQRLIEQVP----ISLFAIDEAHCISQWGHDFRPSYLTLCDsLDR 163
Cdd:cd17920 83 NSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGR-LRR 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1893405659 164 MKKRPLVIALTATATQAVSDDICRLLKIGQNSVVKTGFS 202
Cdd:cd17920 162 ALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
8-201 |
1.84e-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: 251.41 E-value: 1.84e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 8 ILQQNFGYQDFRDGQVDVISKLCAGEDALAIMPTGGGKSLCYQIPALLFD----GLTIVVSPLISLMKDQVDALVSeGIA 83
Cdd:cd18018 3 LLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPR-AIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 84 ATFINSTLTTHEINLRLDAAFSGEVKMLYIAPERIETPGFQRLIEQV-PISLFAIDEAHCISQWGHDFRPSYLTLCDSLD 162
Cdd:cd18018 82 AAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTpPISLLVVDEAHCISEWSHNFRPDYLRLCRVLR 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1893405659 163 RMKKRPLVIALTATATQAVSDDICRLLKIGQNSVVKTGF 201
Cdd:cd18018 162 ELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPL 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
3-191 |
3.85e-59 |
|
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: 196.05 E-value: 3.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 3 EQAKVILQQNFGYQDFRDGQVDVISKLCAGEDALAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGI 82
Cdd:cd18015 4 GKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 83 AATFINSTLTTHEINLRLDAAFSG--EVKMLYIAPERIETPgfQRLIEQVP-------ISLFAIDEAHCISQWGHDFRPS 153
Cdd:cd18015 84 SATMLNASSSKEHVKWVHAALTDKnsELKLLYVTPEKIAKS--KRFMSKLEkaynagrLARIAIDEVHCCSQWGHDFRPD 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1893405659 154 YLTLcDSLDRMKKRPLVIALTATATQAVSDDICRLLKI 191
Cdd:cd18015 162 YKKL-GILKRQFPNVPILGLTATATSKVLKDVQKILCI 198
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
203-333 |
2.75e-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: 2.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 203 RDNLAFQVVKGQDKDKYLID---YLSKNKTESGIIYASTRKEVERLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDD 279
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLlkrIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1893405659 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 |
2.99e-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: 179.97 E-value: 2.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 9 LQQNFGYQDFRDGQVDVI-SKLCAGEDALAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAATFI 87
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIrSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 88 NSTLTTHEinlrLDAAFSGEVKMLYIAPERIEtpGFQRLIEQVP--ISLFAIDEAHCISQWGHDFRPSYLTLcDSLDRMK 165
Cdd:cd18017 84 GSAQSQNV----LDDIKMGKIRVIYVTPEFVS--KGLELLQQLRngITLIAIDEAHCVSQWGHDFRSSYRHL-GSIRNRL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1893405659 166 KRPLVIALTATATQAVSDDICRLLKIGQNSVVKTGF 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 ... |
9-194 |
3.71e-53 |
|
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: 180.36 E-value: 3.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 9 LQQNFGYQDFR-DGQVDVISKLCAGE-DALAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAATF 86
Cdd:cd18014 4 LKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 87 INSTLTTHE---INLRLDAAfSGEVKMLYIAPERIETPGFQRLIEQV----PISLFAIDEAHCISQWGHDFRPSYLTLCD 159
Cdd:cd18014 84 LNSKLSAQErkrIIADLESE-KPQTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLRLGA 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1893405659 160 SLDRMKKRPLvIALTATATQAVSDDICRLLKIGQN 194
Cdd:cd18014 163 LRSRYGHVPW-VALTATATPQVQEDIFAQLRLKKP 196
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
8-201 |
2.09e-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: 170.39 E-value: 2.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 8 ILQQNFGYQDFRDGQVDVISKLCAGEDALAIMPTGGGKSLCYQIPALLFDGLTIVVSPLISLMKDQVDALVSEGIAATFI 87
Cdd:cd18016 8 IFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 88 NSTLTTHE---INLRLDAAfSGEVKMLYIAPERIETPG-----FQRLIEQVPISLFAIDEAHCISQWGHDFRPSYLTLCD 159
Cdd:cd18016 88 TGDKTDAEatkIYLQLSKK-DPIIKLLYVTPEKISASNrlistLENLYERKLLARFVIDEAHCVSQWGHDFRPDYKRLNM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1893405659 160 SLDRMKKRPlVIALTATATQAVSDDICRLLKIGQNSVVKTGF 201
Cdd:cd18016 167 LRQKFPSVP-MMALTATATPRVQKDILNQLKMLRPQVFTMSF 207
|
|
| DpdF |
NF041063 |
protein DpdF; |
8-340 |
4.31e-47 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 177.03 E-value: 4.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 8 ILQQNFGYQDFRD-GQVDVI-SKLCAGEDA--LAIMPTGGGKSLCYQIPALLF---DGLTIVVSPLISLMKDQVDAlvse 80
Cdd:NF041063 130 FLAEALGFTHYRSpGQREAVrAALLAPPGStlIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQERR---- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 81 giAATFINSTLTTHEINLrldaAFSGEV-----KMLYiapERIETpGFQRLI----EQVPISL---------------FA 136
Cdd:NF041063 206 --ARELLRRAGPDLGGPL----AWHGGLsaeerAAIR---QRIRD-GTQRILftspESLTGSLrpalfdaaeagllryLV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 137 IDEAHCISQWGHDFRPSY----------LTLCDSLDRMKkrplVIALTATATQAVSDDICRLlkigqnsvvktgFSRDNl 206
Cdd:NF041063 276 VDEAHLVDQWGDGFRPEFqllaglrrslLRLAPSGRPFR----TLLLSATLTESTLDTLETL------------FGPPG- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 207 AFQVVKGQdkdkYL---IDY-LSKNKTESG----------------IIYASTRKEVERLHAFLLKKGVES-GMYHGGMTD 265
Cdd:NF041063 339 PFIVVSAV----QLrpePAYwVAKCDSEEErrervlealrhlprplILYVTKVEDAEAWLQRLRAAGFRRvALFHGDTPD 414
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1893405659 266 LARQE----WQEkflyDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILLFSPQDSRI 340
Cdd:NF041063 415 AERERlieqWRE----NELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDI 489
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
400-505 |
3.45e-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: 130.74 E-value: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 400 REATDVTIQAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKEDSQKDVLQLIDYLIAEKYLQPTD 479
Cdd:pfam09382 2 PETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDI 81
|
90 100
....*....|....*....|....*.
gi 1893405659 480 SQFPSLKLTDRAVSVLRGELKVARKQ 505
Cdd:pfam09382 82 EFYSVLKLTPKAREVLKGEEKVMLRV 107
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
404-495 |
1.16e-33 |
|
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: 123.35 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 404 DVTIQAQQVFSCIKRMGERFGKVLIAKVLTGSADQKVKDWRFDELSTYGLMKEDSQKDVLQLIDYLIAEKYLQPTDSQFP 483
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 1893405659 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 |
4.64e-25 |
|
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: 99.59 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 215 DKDKYLIDYLSKNKTESGIIYASTRKEVErLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFGMGIN 294
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 1893405659 295 KSNVRFVIHYNIPRNIEAYYQEAGRAGRDG 324
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
19-183 |
1.81e-23 |
|
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: 97.31 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 19 RDGQVDVISKLCAGEDALAIMPTGGGKSLCYQIPAL-----LFDGL-TIVVSPLISLMKDQVDALVSEGI-AATFINSTL 91
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdkLDNGPqALVLAPTRELAEQIYEELKKLGKgLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 92 TTHEINLRLDAAfsGEVKMLYIAPERIETP-GFQRLIEQVpiSLFAIDEAHCISQWGhdFRPSYLTLcdsLDRMKKRPLV 170
Cdd:pfam00270 81 GGDSRKEQLEKL--KGPDILVGTPGRLLDLlQERKLLKNL--KLLVLDEAHRLLDMG--FGPDLEEI---LRRLPKKRQI 151
|
170
....*....|...
gi 1893405659 171 IALTATATQAVSD 183
Cdd:pfam00270 152 LLLSATLPRNLED 164
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
243-324 |
6.25e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 92.66 E-value: 6.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 243 ERLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGR 322
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1893405659 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 ... |
520-584 |
1.67e-21 |
|
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: 88.36 E-value: 1.67e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1893405659 520 LFEQLREVRRELASKHKVPPYIIFSDETLREMCAYLPQDEEALLEVKGIGAMKRDKYGAAFLAVL 584
Cdd:pfam00570 4 LLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
13-192 |
5.71e-21 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 91.01 E-value: 5.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 13 FGYQDFRDGQVDVISKLCAGE-DALAIMPTGGGKSLCYQIPALLF-----DGLTIVVSPLISLMKDQVDALVSEGIAATF 86
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 87 INSTLTT-HEINLRLDAAFSGEVKMLYIAPERIETPGFQRLIEQVPISLFAIDEAHCISQWGhdFRPSYLTLcdsLDRMK 165
Cdd:smart00487 84 KVVGLYGgDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL---LKLLP 158
|
170 180
....*....|....*....|....*..
gi 1893405659 166 KRPLVIALTATATQAVsDDICRLLKIG 192
Cdd:smart00487 159 KNVQLLLLSATPPEEI-ENLLELFLND 184
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
208-322 |
1.17e-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: 87.95 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 208 FQVVKGQDKDKYLIDYL-SKNKTESGIIYASTRKEVERLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVAT 286
Cdd:cd18787 5 YVVVEEEEKKLLLLLLLlEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVAT 84
|
90 100 110
....*....|....*....|....*....|....*.
gi 1893405659 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 |
6.31e-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: 83.88 E-value: 6.31e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1893405659 335 PQDSRIQQFLIEQSELDEERKQNEFAKLRQMTGYG-YTEICLQKYIVQYFGD--DEENCGKCSNCL 397
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCeNTTDCRRKQLLRYFGEefDSEPCGNCDNCL 66
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
210-363 |
3.77e-18 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 87.12 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 210 VVKGQDKDKYLIDYLSKNKTESGIIYASTRKEVERLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAF 289
Cdd:COG0513 222 LVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 290 GMGINKSNVRFVIHYNIPRNIEAYYQEAG---RAGRDGVpsdCILLFSPQDSR----IQQFL---IEQSELD--EERKQN 357
Cdd:COG0513 302 ARGIDIDDVSHVINYDLPEDPEDYVHRIGrtgRAGAEGT---AISLVTPDERRllraIEKLIgqkIEEEELPgfEPVEEK 378
|
....*.
gi 1893405659 358 EFAKLR 363
Cdd:COG0513 379 RLERLK 384
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
520-586 |
3.47e-17 |
|
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: 76.57 E-value: 3.47e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1893405659 520 LFEQLREVRRELASKHKVPPYIIFSDETLREMCAYLPQDEEALLEVKGIGAMKRDKYGAAFLAVLQQ 586
Cdd:smart00341 7 LLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQE 73
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
210-338 |
1.79e-14 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 76.10 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 210 VVKGQDKDKYLIDYLSKNKTESGIIYASTRKEVERLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAF 289
Cdd:PRK01297 316 AVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVA 395
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1893405659 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 ... |
218-332 |
1.40e-13 |
|
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: 68.44 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 218 KYLIDYLSKNKTESgIIYASTRKEVERLHAFLLKKGVESGM-------YHGGMTDLARQEWQEKFLYDDIRVIVATNAFG 290
Cdd:cd18797 25 ARLFADLVRAGVKT-IVFCRSRKLAELLLRYLKARLVEEGPlaskvasYRAGYLAEDRREIEAELFNGELLGVVATNALE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1893405659 291 MGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILL 332
Cdd:cd18797 104 LGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
118-346 |
1.66e-12 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 69.82 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 118 IETPGfqRLI--------EQVPISLFAIDEAHCISQWGhdFRPSYLTLCDSLdrmkKRPLVIALTATATQAVSDDICRLL 189
Cdd:PLN00206 251 VGTPG--RLIdllskhdiELDNVSVLVLDEVDCMLERG--FRDQVMQIFQAL----SQPQVLLFSATVSPEVEKFASSLA 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 190 K------IGQ----NSVVKtgfsrdNLAFQVVKGQDKDKyLIDYL-SKNK-TESGIIYASTRKEVERL-HAFLLKKGVES 256
Cdd:PLN00206 323 KdiilisIGNpnrpNKAVK------QLAIWVETKQKKQK-LFDILkSKQHfKPPAVVFVSSRLGADLLaNAITVVTGLKA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 257 GMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILLFSPQ 336
Cdd:PLN00206 396 LSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE 475
|
250
....*....|
gi 1893405659 337 DSRIQQFLIE 346
Cdd:PLN00206 476 DRNLFPELVA 485
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
12-322 |
1.62e-11 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 66.84 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 12 NFGYQDFRDGQVDVISK-LCAGEDALAIMPTGGGKSLCYQIPAL--LFDGLTIV-VSPLIslmkdqvdALVSEgIAATF- 86
Cdd:COG1204 17 ERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLR--------ALASE-KYREFk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 87 -------INSTLTTHEInlRLDAAFSGEVKMLYIAPERietpgFQRLIEQVP-----ISLFAIDEAHCIsqwGHDFR-PS 153
Cdd:COG1204 88 rdfeelgIKVGVSTGDY--DSDDEWLGRYDILVATPEK-----LDSLLRNGPswlrdVDLVVVDEAHLI---DDESRgPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 154 YLTLCDSLDRMKKRPLVIALTATATQAvsDDICRLLKigqNSVVKTGFSRDNLAFQVVKGQD---KDKY------LIDYL 224
Cdd:COG1204 158 LEVLLARLRRLNPEAQIVALSATIGNA--EEIAEWLD---AELVKSDWRPVPLNEGVLYDGVlrfDDGSrrskdpTLALA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 225 SKNKTESG--IIYASTRKEVE---------------------------RLHAF------------LLKKGVesGMYHGGM 263
Cdd:COG1204 233 LDLLEEGGqvLVFVSSRRDAEslakkladelkrrltpeereeleelaeELLEVseethtnekladCLEKGV--AFHHAGL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1893405659 264 TDLARQEWQEKFLYDDIRVIVATNAFGMGIN--KSNVrfVIH-----YNIPRNIEAYYQEAGRAGR 322
Cdd:COG1204 311 PSELRRLVEDAFREGLIKVLVATPTLAAGVNlpARRV--IIRdtkrgGMVPIPVLEFKQMAGRAGR 374
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
22-346 |
2.19e-11 |
|
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: 66.78 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 22 QVDVISKLCAGEDALAIMPTGGGKSLCYQIPALlfDGL-------TIVVSPLISLMKDQVDALvsegiaATFINSTLtth 94
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVL--EALledpgatALYLYPTKALARDQLRRL------RELAEALG--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 95 einLRLDAA-FSGEVKmlyiAPER----------IETP------------GFQRLIEQVpiSLFAIDEAHcisqwghdfr 151
Cdd:COG1205 130 ---LGVRVAtYDGDTP----PEERrwirehpdivLTNPdmlhygllphhtRWARFFRNL--RYVVIDEAH---------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 152 pSY---------------LTLCDsldRMKKRPLVIALTAT-------ATQ-------AVSDDicrllkiG---------- 192
Cdd:COG1205 191 -TYrgvfgshvanvlrrlRRICR---HYGSDPQFILASATignpaehAERltgrpvtVVDED-------Gsprgertfvl 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 193 -QNSVVKTGFSRDNLAFQVvkgqdkdkYLIDYLSKN--KTesgIIYASTRKEVERLHAFLLKKGVESGM------YHGGM 263
Cdd:COG1205 260 wNPPLVDDGIRRSALAEAA--------RLLADLVREglRT---LVFTRSRRGAELLARYARRALREPDLadrvaaYRAGY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 264 TDLARQEWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILLfsPQDSRIQQF 343
Cdd:COG1205 329 LPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLV--AGDDPLDQY 406
|
...
gi 1893405659 344 LIE 346
Cdd:COG1205 407 YVR 409
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
32-176 |
1.48e-10 |
|
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: 59.72 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 32 GEDALAIMPTGGGKSLCYQIPALL----FDGLTIVVSPLISLMKDQ---VDALVSEGIAATFINSTLTTHEinlrLDAAF 104
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLlllkKGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEE----REKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1893405659 105 SGEVKMLYIAPERIETPG-FQRLIEQVPISLFAIDEAHCISQWGHDFRPSYLTLCdslDRMKKRPLVIALTAT 176
Cdd:cd00046 77 LGDADIIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVR---KAGLKNAQVILLSAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
19-320 |
4.55e-09 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 59.27 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 19 RDGQVDVISKLCA-----GEDALAIMPTGGGKSL----CYQipALLFDGLTIVVSPLISLMKDQVDALvsegiAATFINS 89
Cdd:COG1061 82 RPYQQEALEALLAalergGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEEL-----RRFLGDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 90 TLTTHEINLRLDAAFSGeVKMLYIAPERIETPGFQRLIeqvpislfAIDEAHcisqwgHDFRPSYLTLcdsLDRMKKRPl 169
Cdd:COG1061 155 LAGGGKKDSDAPITVAT-YQSLARRAHLDELGDRFGLV--------IIDEAH------HAGAPSYRRI---LEAFPAAY- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 170 VIALTAT----------------------ATQAVSDDICRLLKIgqnSVVKTGFSRDNLAFQVVKGQDKDKY-------- 219
Cdd:COG1061 216 RLGLTATpfrsdgreillflfdgivyeysLKEAIEDGYLAPPEY---YGIRVDLTDERAEYDALSERLREALaadaerkd 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 220 --LIDYLSKN-KTESGIIYASTRKEVERLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFGMGINKS 296
Cdd:COG1061 293 kiLRELLREHpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVP 372
|
330 340
....*....|....*....|....*..
gi 1893405659 297 NVRFVIHYnipRNIEA---YYQEAGRA 320
Cdd:COG1061 373 RLDVAILL---RPTGSpreFIQRLGRG 396
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
276-332 |
4.81e-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: 4.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1893405659 276 LYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDG-VPSDCILL 332
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
215-337 |
6.28e-09 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 58.30 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 215 DKDKY----LIDYLSKNKTESGIIYASTRKEVERLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFG 290
Cdd:PTZ00424 249 EKEEWkfdtLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLA 328
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1893405659 291 MGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILLFSPQD 337
Cdd:PTZ00424 329 RGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDD 375
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
218-322 |
9.35e-09 |
|
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: 54.58 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 218 KYLIDYLSKNKteSGIIYASTRKEVERLHAFLLKKGVESG-----MYHGGMTDLARQEWQEKFLYD-DIRVIVATNAFGM 291
Cdd:cd18796 29 AEVIFLLERHK--STLVFTNTRSQAERLAQRLRELCPDRVppdfiALHHGSLSRELREEVEAALKRgDLKVVVATSSLEL 106
|
90 100 110
....*....|....*....|....*....|.
gi 1893405659 292 GINKSNVRFVIHYNIPRNIEAYYQEAGRAGR 322
Cdd:cd18796 107 GIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
233-324 |
1.80e-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: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 233 IIYASTRKEVERLHAFLlkKGVesGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFGMGIN--------KSNVRFVIHY 304
Cdd:cd18795 47 LVFCSSRKECEKTAKDL--AGI--AFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKG 122
|
90 100
....*....|....*....|
gi 1893405659 305 NIPRNIEAYYQEAGRAGRDG 324
Cdd:cd18795 123 YRELSPLEYLQMIGRAGRPG 142
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
464-586 |
2.43e-07 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 52.95 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 464 QLIDYLIAEKYLQPTDSQFpsLKLTDRAVSVLRGELKVAR-KQAKRAEKVKLAVnsslfeqLREV---RRELASKHKVPP 539
Cdd:COG0349 161 KLLEELEREGRLEWAEEEC--ARLLDPATYREDPEEAWLRlKGAWKLNPRQLAV-------LRELaawREREARKRDVPR 231
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1893405659 540 YIIFSDETLREMCAYLPQDEEALLEVKGIGAMKRDKYGAAFLAVLQQ 586
Cdd:COG0349 232 NRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAE 278
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
207-364 |
2.61e-07 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 53.70 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 207 AFQVVKGQDKDKYLIDYLSKNKTESGIIYASTRKEVERLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVAT 286
Cdd:PRK11634 223 SYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIAT 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 287 NAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGVPSDCILLFSPQDSR------------IQQFLIEQSELDEER 354
Cdd:PRK11634 303 DVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRllrniertmkltIPEVELPNAELLGKR 382
|
170
....*....|.
gi 1893405659 355 KQNEFA-KLRQ 364
Cdd:PRK11634 383 RLEKFAaKVQQ 393
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
31-369 |
3.11e-06 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 50.16 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 31 AGEDALAIMPTGGGKSLCYQIPALLF----------DG-LTIVVSP---LISLMKDQvdalvsegiAATFINSTltthei 96
Cdd:PTZ00110 166 SGRDMIGIAETGSGKTLAFLLPAIVHinaqpllrygDGpIVLVLAPtreLAEQIREQ---------CNKFGASS------ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 97 NLRLDAAFSGevkmlyiAPERIETPGFQRLIE---QVPISLFAIDEAHCISQwghdFRPSYLTLcDSLDRM--------- 164
Cdd:PTZ00110 231 KIRNTVAYGG-------VPKRGQIYALRRGVEiliACPGRLIDFLESNVTNL----RRVTYLVL-DEADRMldmgfepqi 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 165 KK-----RPLVIALTATAT-----QAVSDDICRLLKIGQN--SVVKTGFSRDNLAFQVVKGQDKDKYLIDYLSK--NKTE 230
Cdd:PTZ00110 299 RKivsqiRPDRQTLMWSATwpkevQSLARDLCKEEPVHVNvgSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRimRDGD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 231 SGIIYASTRKEVERLHAFLLKKGVESGMYHGGmtdlARQEwQEKFLYDDIR-----VIVATNAFGMGINKSNVRFVIHYN 305
Cdd:PTZ00110 379 KILIFVETKKGADFLTKELRLDGWPALCIHGD----KKQE-ERTWVLNEFKtgkspIMIATDVASRGLDVKDVKYVINFD 453
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1893405659 306 IPRNIEAYYQEAGRAGRDGVPSDCILLFSPQDSRIQQFLI------------EQSELDEERKQNEfaKLRQMTGYG 369
Cdd:PTZ00110 454 FPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVkvlreakqpvppELEKLSNERSNGT--ERRRWGGYG 527
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
22-77 |
8.90e-06 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 46.42 E-value: 8.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1893405659 22 QVDVISKLCAGEDALAIMPTGGGKSLCYQIPAllFDGL-------TIVVSPLISLMKDQVDAL 77
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPI--LEALlrdpgsrALYLYPTKALAQDQLRSL 65
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
224-324 |
2.94e-05 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 47.03 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 224 LSKNKTESGIIYASTRKEVERLHAFLLKKGVESGMYHG--------GMTDLARQEWQEKFLYDDIRVIVATNAFGMGINK 295
Cdd:COG1111 348 LGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDI 427
|
90 100 110
....*....|....*....|....*....|
gi 1893405659 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 |
3.41e-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: 44.00 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 218 KYLIDYLSKNKTESG--IIYASTRKEVERLHAFLLKKGVESGMYHGGMTDLARQEWQEKF--LYDDIRVIVATNAFGMGI 293
Cdd:cd18793 14 EALLELLEELREPGEkvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFneDPDIRVFLLSTKAGGVGL 93
|
90 100 110
....*....|....*....|....*....|...
gi 1893405659 294 NKSNVRFVIHYNIPRN--IEAyyQEAGRAGRDG 324
Cdd:cd18793 94 NLTAANRVILYDPWWNpaVEE--QAIDRAHRIG 124
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
233-322 |
1.24e-04 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 44.80 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 233 IIYASTRKEVERLHAFLLKKGVESGMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPRNIEA 312
Cdd:PRK10590 249 LVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPED 328
|
90
....*....|
gi 1893405659 313 YYQEAGRAGR 322
Cdd:PRK10590 329 YVHRIGRTGR 338
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
224-324 |
2.87e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 40.63 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 224 LSKNKTESGIIYASTRKEVERLHAFLLKKGVESGMYHG--------GMTDLARQEWQEKFLYDDIRVIVATNAFGMGINK 295
Cdd:PRK13766 360 LGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaskdgdkGMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDI 439
|
90 100 110
....*....|....*....|....*....|...
gi 1893405659 296 SNVRFVIHYN-IP---RNIeayyQEAGRAGRDG 324
Cdd:PRK13766 440 PSVDLVIFYEpVPseiRSI----QRKGRTGRQE 468
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
11-78 |
3.61e-03 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 39.10 E-value: 3.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1893405659 11 QNFGYQDFRDGQVDVISKLCAGEDALAIMPTGGGKSLCYQIPAllfdgLTIVVSPLISLMKDQVDALV 78
Cdd:cd17960 6 AELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPV-----LEILLKRKANLKKGQVGALI 68
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
218-332 |
3.90e-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: 37.96 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 218 KYLIDYLSKNKTESGIIYASTRKEVERLHAFL---------LKKGVESGMYHG------GMTDLARQEWQEKFLYDDIRV 282
Cdd:cd18802 14 EILREYFPKTPDFRGIIFVERRATAVVLSRLLkehpstlafIRCGFLIGRGNSsqrkrsLMTQRKQKETLDKFRDGELNL 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1893405659 283 IVATNAFGMGINKSNVRFVIHYNIPRNIEAYYQEAGRAGRDGvpSDCILL 332
Cdd:cd18802 94 LIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYILM 141
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
257-338 |
4.76e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 38.09 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893405659 257 GMYHGGMTDLARQEWQEKFLYDDIRVIVATNAFGMGINKSNVRFVIHYNIPR-NIEAYYQEAGRAGRDGVPSDCILLFSP 335
Cdd:cd18811 65 GLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERfGLSQLHQLRGRVGRGDHQSYCLLVYKD 144
|
...
gi 1893405659 336 QDS 338
Cdd:cd18811 145 PLT 147
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
32-77 |
6.37e-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: 37.95 E-value: 6.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1893405659 32 GEDALAIMPTGGGKSLCYQIPAL--LFD-----GLTIVVSPLISLMKDQVDAL 77
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALssLADepekgVQVLYISPLKALINDQERRL 53
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