|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
3-480 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 704.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 3 DPQQVLKKYFGYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALMIPGATVVISPLISLMKDQVDSMREYGIP 82
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 83 AAALNSSTAQEDVNPILRACYEGKIKLLYVTPERMEMDYFRYQLNFLEVNLVAIDEAHCISQWGHDFRPAYRKLKDGINA 162
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 163 LhTHPNVLALTATATKAVREDIGQQLDISEENFVITSFERKNLHFKLVN-APKNSRAYIVNYLKQHRGEAGIIYSNTRKK 241
Cdd:COG0514 164 L-PNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPkPPDDKLAQLLDFLKEHPGGSGIVYCLSRKK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 242 VEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQEAGRAG 321
Cdd:COG0514 243 VEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 322 RDGLESEAVMLFHPSDLRQFRWFIDNSEADESYRQVQYQKLQTISDYANTDECLQQFIVRYFGQDCP-PCGKCSNCLNSG 400
Cdd:COG0514 323 RDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAePCGNCDNCLGPP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 401 DFQDVTAEAQAIIGMVYDLDGRYGKRIVAQAVTGSKVKKISEIGGDECVHYGLLKGKKQADVSSLVDYLVSkgylQLVGD 480
Cdd:COG0514 403 ETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLA----QLFGE 478
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
5-588 |
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: 692.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 5 QQVLKKYFGYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALMIPGATVVISPLISLMKDQVDSMREYGIPAA 84
Cdd:TIGR01389 2 QQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 85 ALNSSTAQEDVNPILRACYEGKIKLLYVTPERMEMDYFRYQLNFLEVNLVAIDEAHCISQWGHDFRPAYRKLKDGINALH 164
Cdd:TIGR01389 82 YLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 165 THPnVLALTATATKAVREDIGQQLDISEENFVITSFERKNLHFKlVNAPKNSRAYIVNYLKQHRGEAGIIYSNTRKKVEG 244
Cdd:TIGR01389 162 QVP-RIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFS-VVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 245 LTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQEAGRAGRDG 324
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 325 LESEAVMLFHPSDLRQFRWFIDNSEADESYRQVQYQKLQTISDYANTDECLQQFIVRYFGQDCP-PCGKCSNCLNSGDFQ 403
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVePCGNCDNCLDPPKSY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 404 DVTAEAQAIIGMVYDLDGRYGKRIVAQAVTGSKVKKISEIGGDECVHYGLLKGKKQADVSSLVDYLVSKGYL-------Q 476
Cdd:TIGR01389 400 DATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLtendeiyI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 477 LVGDCYPLVHVTNRGWDVLDGKARVKRRQEVKSEQLAETGGDQVLFEELRKARRILAQKRGVPPFVIFSDLSLRDMAARK 556
Cdd:TIGR01389 480 GLQLTEAARKVLKNEVEVLLRPFKVVAKEKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKR 559
|
570 580 590
....*....|....*....|....*....|..
gi 499997441 557 PQTPEELLQCSGVGDAKLANYGKAMLAVIKKY 588
Cdd:TIGR01389 560 PATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
1-588 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 543.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 1 MLDPQQVLKKYFGYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALMIPGATVVISPLISLMKDQVDSMREYG 80
Cdd:PRK11057 10 ESLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 81 IPAAALNSSTAQEDVNPILRACYEGKIKLLYVTPERMEMDYFRYQLNFLEVNLVAIDEAHCISQWGHDFRPAYRKLKDgI 160
Cdd:PRK11057 90 VAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQ-L 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 161 NALHTHPNVLALTATATKAVREDIGQQLDISEENFVITSFERKNLHFKLVNAPKnSRAYIVNYLKQHRGEAGIIYSNTRK 240
Cdd:PRK11057 169 RQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFK-PLDQLMRYVQEQRGKSGIIYCNSRA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 241 KVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQEAGRA 320
Cdd:PRK11057 248 KVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 321 GRDGLESEAVMLFHPSDLRQFRWFIDNSEADESyRQVQYQKLQTISDYANTDECLQQFIVRYFGQDCP-PCGKCSNCLNS 399
Cdd:PRK11057 328 GRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQ-QDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQePCGNCDICLDP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 400 GDFQDVTAEAQAIIGMVYDLDGRYGKRIVAQAVTGSKVKKISEIGGDECVHYGLLKGKKQADVSSLVDYLVSKGYLQLVG 479
Cdd:PRK11057 407 PKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNI 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 480 DCYPLVHVTNRGWDVLDGKAR----VKRRQEVKSEQLAETGG---DQVLFEELRKARRILAQKRGVPPFVIFSDLSLRDM 552
Cdd:PRK11057 487 AQHSALQLTEAARPVLRGEVSlqlaVPRIVALKPRAMQKSFGgnyDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIEM 566
|
570 580 590
....*....|....*....|....*....|....*.
gi 499997441 553 AARKPQTPEELLQCSGVGDAKLANYGKAMLAVIKKY 588
Cdd:PRK11057 567 AEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAH 602
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
6-444 |
3.65e-152 |
|
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: 445.75 E-value: 3.65e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 6 QVLKKYFGYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALMIPGATVVISPLISLMKDQVDSMREYGIPAAA 85
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 86 LNSSTAQEDVNPILRACYEGKIKLLYVTPERM--EMDYFRYQLNFLEVNLVAIDEAHCISQWGHDFRPAYRKLkdgiNAL 163
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsaSNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKAL----GSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 164 HTH-PNV--LALTATATKAVREDIGQQLDISEENFVITSFERKNLHFKLVNAPKNSRAYIVNYL-KQHRGEAGIIYSNTR 239
Cdd:TIGR00614 157 KQKfPNVpvMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPKILEDLLRFIrKEFEGKSGIIYCPSR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 240 KKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQEAGR 319
Cdd:TIGR00614 237 KKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 320 AGRDGLESEAVMLFHPSDLRQFRWFIDnSEADESYRQVQYQKLQTISDYANTDECLQQFIVRYFGQDCP----------- 388
Cdd:TIGR00614 317 AGRDGLPSECHLFYAPADMNRLRRLLM-EEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFnksfcimgtek 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499997441 389 PCGKCSNCLNSG------DFQDVTAEAQAIIGMVYDLDGRYGKRIVAQAVTGSKVKKISEIG 444
Cdd:TIGR00614 396 CCDNCCKRLDYKtkdvtdKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGG 457
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
9-585 |
3.51e-102 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 334.94 E-value: 3.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 9 KKYFGYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALMIPGATVVISPLISLMKDQVDSMREYGIPAAALNS 88
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 89 STAQEDVNPILR--ACYEGKIKLLYVTPERM-EMDYFRYQLNFLEV-NLVA---IDEAHCISQWGHDFRPAYRKLkdGIn 161
Cdd:PLN03137 533 GMEWAEQLEILQelSSEYSKYKLLYVTPEKVaKSDSLLRHLENLNSrGLLArfvIDEAHCVSQWGHDFRPDYQGL--GI- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 162 ALHTHPN--VLALTATATKAVREDIGQQLDISeeNFVI--TSFERKNLHFKLVNAPKNSRAYIVNYLKQ-HRGEAGIIYS 236
Cdd:PLN03137 610 LKQKFPNipVLALTATATASVKEDVVQALGLV--NCVVfrQSFNRPNLWYSVVPKTKKCLEDIDKFIKEnHFDECGIIYC 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 237 NTRKKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQE 316
Cdd:PLN03137 688 LSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQE 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 317 AGRAGRDGLESEAVMLFHPSDLRQFRWFIDNSEADESYRQVQYQK---------------LQTISDYANTDECLQQFIVR 381
Cdd:PLN03137 768 CGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSPMAMGYNRmassgriletntenlLRMVSYCENEVDCRRFLQLV 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 382 YFGQ--DCPPCGK-CSNCLNSGDF--QDVTAEAQAIIGMVYDLDGRYGKRIVAQAVTGS---KVKKISEiggdECVH-YG 452
Cdd:PLN03137 848 HFGEkfDSTNCKKtCDNCSSSKSLidKDVTEIARQLVELVKLTGERFSSAHILEVYRGSlnqYVKKHRH----ETLSlHG 923
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 453 LLKGKKQADVSSLVDYLVSKGYLQ-------LVGDCYPLVHVTN-RGWDVLDGKARVKRR--QEVKSEQLAE-------- 514
Cdd:PLN03137 924 AGKHLSKGEASRILHYLVTEDILAedvkksdLYGSVSSLLKVNEsKAYKLFSGGQTIIMRfpSSVKASKPSKfeatpakg 1003
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 515 --TGGDQ-------------------VLFEELRKARRILAQK--RGVPPFVIFSDLSLRDMAARKPQTPEELLQCSGVGD 571
Cdd:PLN03137 1004 plTSGKQstlpmatpaqppvdlnlsaILYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGK 1083
|
650
....*....|....
gi 499997441 572 AKLANYGKAMLAVI 585
Cdd:PLN03137 1084 AKVSKYGDRLLETI 1097
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
5-200 |
1.38e-99 |
|
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: 300.99 E-value: 1.38e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 5 QQVLKKYFGYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALMIPGATVVISPLISLMKDQVDSMREYGIPAA 84
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 85 ALNSSTAQEDVNPILRACYEGKIKLLYVTPERMEMDYF----RYQLNFLEVNLVAIDEAHCISQWGHDFRPAYRKLKDGI 160
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFlellQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499997441 161 NALHTHPnVLALTATATKAVREDIGQQLDISEENFVITSF 200
Cdd:cd17920 161 RALPGVP-ILALTATATPEVREDILKRLGLRNPVIFRASF 199
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
6-201 |
2.16e-77 |
|
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: 243.70 E-value: 2.16e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 6 QVLKKYFGYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALMI----PGATVVISPLISLMKDQVDSMREyGI 81
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLrrrgPGLTLVVSPLIALMKDQVDALPR-AI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 82 PAAALNSSTAQEDVNPILRACYEGKIKLLYVTPERMEMDYFRYQLNFLE-VNLVAIDEAHCISQWGHDFRPAYRKLKDGI 160
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPpISLLVVDEAHCISEWSHNFRPDYLRLCRVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499997441 161 NALHTHPNVLALTATATKAVREDIGQQLDISEENFVITSFE 201
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
5-200 |
8.70e-66 |
|
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: 213.77 E-value: 8.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 5 QQVLKKYFGYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALMIPGATVVISPLISLMKDQVDSMREYGIPAA 84
Cdd:cd18015 7 KDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 85 ALNSSTAQEDVNPILRACYEGK--IKLLYVTPERME-----MDYFR--YQLNFLEvnLVAIDEAHCISQWGHDFRPAYRK 155
Cdd:cd18015 87 MLNASSSKEHVKWVHAALTDKNseLKLLYVTPEKIAkskrfMSKLEkaYNAGRLA--RIAIDEVHCCSQWGHDFRPDYKK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499997441 156 LkdGInaLHTH-PNV--LALTATATKAVREDIGQQLDISEENFVITSF 200
Cdd:cd18015 165 L--GI--LKRQfPNVpiLGLTATATSKVLKDVQKILCIQKCLTFTASF 208
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
8-201 |
4.20e-59 |
|
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: 195.38 E-value: 4.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 8 LKKYFGYDSFRPGQREIIEKVFQ-GKNVLAVMPTGGGKSLCYQIPALMIPGATVVISPLISLMKDQVDSMREYGIPAAAL 86
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLEeRRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 87 NSSTAQEDVNpilrACYEGKIKLLYVTPERMEMDYFRYQLNFLEVNLVAIDEAHCISQWGHDFRPAYRKLKDGINALhth 166
Cdd:cd18017 84 GSAQSQNVLD----DIKMGKIRVIYVTPEFVSKGLELLQQLRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRL--- 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 499997441 167 PNV--LALTATATKAVREDIGQQLDISEENFVITSFE 201
Cdd:cd18017 157 PNVpiVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
6-200 |
1.24e-54 |
|
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: 184.26 E-value: 1.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 6 QVLKKYFGYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALMIPGATVVISPLISLMKDQVDSMREYGIPAAA 85
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 86 LNSSTAQEDVNPILRACYEGK--IKLLYVTPERMEMDYfRYQ---LNFLEVNLVA---IDEAHCISQWGHDFRPAYRKLK 157
Cdd:cd18016 87 LTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKISASN-RLIstlENLYERKLLArfvIDEAHCVSQWGHDFRPDYKRLN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499997441 158 DGINALHTHPnVLALTATATKAVREDIGQQLDISEENFVITSF 200
Cdd:cd18016 166 MLRQKFPSVP-MMALTATATPRVQKDILNQLKMLRPQVFTMSF 207
|
|
| DpdF |
NF041063 |
protein DpdF; |
3-340 |
1.95e-52 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 192.43 E-value: 1.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 3 DPqqVLKKYFGYDSFR-PGQREIIEKVF---QGKNVLAVMPTGGGKSLCYQIPALMIP---GATVVISPLISLMKDQVDS 75
Cdd:NF041063 128 DP--FLAEALGFTHYRsPGQREAVRAALlapPGSTLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALAIDQERR 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 76 MRE-------YGIPAAALNSSTAQEDVNPILRACYEGKIKLLYVTPERMeMDYFRYQL------NFLevNLVAIDEAHCI 142
Cdd:NF041063 206 AREllrragpDLGGPLAWHGGLSAEERAAIRQRIRDGTQRILFTSPESL-TGSLRPALfdaaeaGLL--RYLVVDEAHLV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 143 SQWGHDFRPAYRKLKDGINAL------HTHPNVLALTATATKAVREDI------GQQLDI-------SEENFVITSFERK 203
Cdd:NF041063 283 DQWGDGFRPEFQLLAGLRRSLlrlapsGRPFRTLLLSATLTESTLDTLetlfgpPGPFIVvsavqlrPEPAYWVAKCDSE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 204 NLHFKLV-----NAPKNSrayivnylkqhrgeagIIYSNTRKKVEGLTEFLRREGFN-VAAYHAGMSNEERAQVQDDFQY 277
Cdd:NF041063 363 EERRERVlealrHLPRPL----------------ILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRE 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499997441 278 DRIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQEAGRAGRDGLESEAVMLFHPSDLRQ 340
Cdd:NF041063 427 NELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDI 489
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
202-333 |
2.27e-52 |
|
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: 175.47 E-value: 2.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 202 RKNLHFKLVNAPKNSRAYI--VNYLKQHRGEAGIIYSNTRKKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDR 279
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDllKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 499997441 280 IPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQEAGRAGRDGLESEAVMLF 333
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
5-190 |
6.31e-51 |
|
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: 174.20 E-value: 6.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 5 QQVLKKYFGYDSFR-PGQREIIEKVFQGK-NVLAVMPTGGGKSLCYQIPALMIPGATVVISPLISLMKDQVDSMREYGIP 82
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 83 AAALNS-STAQEDVNPI--LRACYEgKIKLLYVTPERMEMDYFRYQLNFL----EVNLVAIDEAHCISQWGHDFRPAYRK 155
Cdd:cd18014 81 VDSLNSkLSAQERKRIIadLESEKP-QTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLR 159
|
170 180 190
....*....|....*....|....*....|....*
gi 499997441 156 LKDgINALHTHPNVLALTATATKAVREDIGQQLDI 190
Cdd:cd18014 160 LGA-LRSRYGHVPWVALTATATPQVQEDIFAQLRL 193
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
18-182 |
1.22e-33 |
|
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: 125.82 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 18 RPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPAL------MIPGATVVISPLISLMKDQVDSMREYGIP-----AAAL 86
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGlglkvASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 87 NSSTAQEDVNPIlracyeGKIKLLYVTPERMeMDYFRYQLNFLEVNLVAIDEAHCISQWGhdFRPAYRKLkdgINALHTH 166
Cdd:pfam00270 81 GGDSRKEQLEKL------KGPDILVGTPGRL-LDLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEI---LRRLPKK 148
|
170
....*....|....*.
gi 499997441 167 PNVLALTATATKAVRE 182
Cdd:pfam00270 149 RQILLLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
10-207 |
5.07e-29 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 114.13 E-value: 5.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 10 KYFGYDSFRPGQREIIEKVFQG-KNVLAVMPTGGGKSLCYQIPALM-----IPGATVVISPLISLMKDQVDSMREYGIPA 83
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 84 AALNSS-TAQEDVNPILRACYEGKIKLLYVTPERMEMDYFRYQLNFLEVNLVAIDEAHCISQWGhdFRPAYRKLkdgINA 162
Cdd:smart00487 82 GLKVVGlYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL---LKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499997441 163 LHTHPNVLALTATATKAVREDIGQQLDiseeNFVITSFERKNLHF 207
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLN----DPVFIDVGFTPLEP 197
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
403-506 |
4.42e-28 |
|
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: 108.39 E-value: 4.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 403 QDVTAEAQAIIGMVYDLDGRYGKRIVAQAVTGSKVKKISEIGGDECVHYGLLKGKKQADVSSLVDYLVSKGYLQLVGDCY 482
Cdd:pfam09382 5 VDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDIEFY 84
|
90 100
....*....|....*....|....
gi 499997441 483 PLVHVTNRGWDVLDGKARVKRRQE 506
Cdd:pfam09382 85 SVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
218-324 |
4.84e-26 |
|
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: 102.67 E-value: 4.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 218 AYIVNYLKQHRGEAGIIYSNTRKKVEgLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSN 297
Cdd:pfam00271 4 EALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
|
90 100
....*....|....*....|....*..
gi 499997441 298 VRFVLHANSAKNLEAYYQEAGRAGRDG 324
Cdd:pfam00271 83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
404-495 |
1.56e-23 |
|
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: 94.85 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 404 DVTAEAQAIIGMVYDLDGRYGKRIVAQAVTGSKVKKISEIGGDECVHYGLLKGKKQADVSSLVDYLVSKGYLQLVGDCYP 483
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 499997441 484 LVHVTNRGWDVL 495
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
21-350 |
7.43e-23 |
|
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: 103.38 E-value: 7.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 21 QREIIEKVFQGKNVLAVMPTGGGKSLCYQIPAL-MI---PGATVV-ISPLISLMKDQVDSMREY------GIPAAALNSS 89
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeALledPGATALyLYPTKALARDQLRRLRELaealglGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 90 TAQEDVNPILRACyegkiKLLYVTPErmeM---------DYFRyqlNFLEvNL--VAIDEAHcisqwghdfrpAY----- 153
Cdd:COG1205 141 TPPEERRWIREHP-----DIVLTNPD---MlhygllphhTRWA---RFFR-NLryVVIDEAH-----------TYrgvfg 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 154 -------RKLKDGINALHTHPNVLALTATatkavredIG------QQLdISEENFVIT-----SFERknlHFKLVNAP-- 213
Cdd:COG1205 198 shvanvlRRLRRICRHYGSDPQFILASAT--------IGnpaehaERL-TGRPVTVVDedgspRGER---TFVLWNPPlv 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 214 ----KNSRAYIVNYLKQHRGEAG---IIYSNTRKKVEGLTEFLRRE------GFNVAAYHAGMSNEERAQVQDDFQYDRI 280
Cdd:COG1205 266 ddgiRRSALAEAARLLADLVREGlrtLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGEL 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 281 PLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQEAGRAGRDGLESEAVMLFHPSDLRQFrwFIDNSEA 350
Cdd:COG1205 346 LGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVAGDDPLDQY--YVRHPEE 413
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
245-324 |
1.53e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 91.50 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 245 LTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQEAGRAGRDG 324
Cdd:smart00490 3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
518-585 |
1.05e-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: 88.75 E-value: 1.05e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499997441 518 DQVLFEELRKARRILAQKRGVPPFVIFSDLSLRDMAARKPQTPEELLQCSGVGDAKLANYGKAMLAVI 585
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
18-320 |
1.60e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 95.48 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 18 RPGQREIIEKVFQ-----GKNVLAVMPTGGGKSLCyqipALMI------PGATVVISPLISLMKDQVDSMREYgiPAAAL 86
Cdd:COG1061 82 RPYQQEALEALLAalergGGRGLVVAPTGTGKTVL----ALALaaellrGKRVLVLVPRRELLEQWAEELRRF--LGDPL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 87 NSSTAQEDVNPILRACYEGkiklLYVtpeRMEMDYFRYqlnflEVNLVAIDEAHcisqwgHDFRPAYRKLKDGINALHth 166
Cdd:COG1061 156 AGGGKKDSDAPITVATYQS----LAR---RAHLDELGD-----RFGLVIIDEAH------HAGAPSYRRILEAFPAAY-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 167 pnVLALTAT--------------ATKAVREDIGQQL---------------DISEENFVITSFErKNLHFKLVNAPKNSR 217
Cdd:COG1061 216 --RLGLTATpfrsdgreillflfDGIVYEYSLKEAIedgylappeyygirvDLTDERAEYDALS-ERLREALAADAERKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 218 AYIVNYLKQH-RGEAGIIYSNTRKKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKS 296
Cdd:COG1061 293 KILRELLREHpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVP 372
|
330 340
....*....|....*....|....
gi 499997441 297 NVRFVLHANSAKNLEAYYQEAGRA 320
Cdd:COG1061 373 RLDVAILLRPTGSPREFIQRLGRG 396
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
6-332 |
6.78e-20 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 93.04 E-value: 6.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 6 QVLKKyFGYDSFRPGQREIIEK-VFQGKNVLAVMPTGGGKSLCYQIPAL--MIPGATVV-ISPLISL----MKDQVDSMR 77
Cdd:COG1204 13 EFLKE-RGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLRALasekYREFKRDFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 78 EYGIPAAAlnSSTAQEDVNPILracyeGKIKLLYVTPERMEMdYFRYQLNFL-EVNLVAIDEAHCIsqwGHDFR-PAY-- 153
Cdd:COG1204 92 ELGIKVGV--STGDYDSDDEWL-----GRYDILVATPEKLDS-LLRNGPSWLrDVDLVVVDEAHLI---DDESRgPTLev 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 154 -----RKLKDGInalhthpNVLALTATATKAvrEDIGQQLDISeenfVITS-----------FERKNLHFKlvNAPKNSR 217
Cdd:COG1204 161 llarlRRLNPEA-------QIVALSATIGNA--EEIAEWLDAE----LVKSdwrpvplnegvLYDGVLRFD--DGSRRSK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 218 AYIVNYLKQHRGEAG--IIYSNTRKKVEG----------------------------------------LTEFLRREgfn 255
Cdd:COG1204 226 DPTLALALDLLEEGGqvLVFVSSRRDAESlakkladelkrrltpeereeleelaeellevseethtnekLADCLEKG--- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 256 VAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIdksN--VRFVLhANSAK--------NLEaYYQEAGRAGRDGL 325
Cdd:COG1204 303 VAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV---NlpARRVI-IRDTKrggmvpipVLE-FKQMAGRAGRPGY 377
|
....*....
gi 499997441 326 ES--EAVML 332
Cdd:COG1204 378 DPygEAILV 386
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
13-342 |
1.17e-19 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 91.75 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 13 GYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALM-----IPGAT--VVISP---LIslmkDQV-DSMREYGi 81
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQrldpsRPRAPqaLILAPtreLA----LQVaEELRKLA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 82 paAALNSSTA----QEDVNPILRACYEGkIKLLYVTPERMeMDYF-RYQLNFLEVNLVAIDEAhcisqwghD------FR 150
Cdd:COG0513 96 --KYLGLRVAtvygGVSIGRQIRALKRG-VDIVVATPGRL-LDLIeRGALDLSGVETLVLDEA--------DrmldmgFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 151 PAYRKLkdgINALHTHPNVLALTATATKAVREDIGQQL------DISEENFVITSFErknlHFKLVNAPKNSRAYIVNYL 224
Cdd:COG0513 164 EDIERI---LKLLPKERQTLLFSATMPPEIRKLAKRYLknpvriEVAPENATAETIE----QRYYLVDKRDKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 225 KQHRGEAGIIYSNTRKKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHA 304
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350
....*....|....*....|....*....|....*...
gi 499997441 305 NSAKNLEAYYQEAGRAGRDGLESEAVMLFHPSDLRQFR 342
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLR 354
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
335-397 |
9.45e-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: 80.41 E-value: 9.45e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499997441 335 PSDLRQFRWFIDNSEADESYRQVQYQKLQTISDYA-NTDECLQQFIVRYFGQ--DCPPCGKCSNCL 397
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCeNTTDCRRKQLLRYFGEefDSEPCGNCDNCL 66
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
518-588 |
4.02e-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: 79.26 E-value: 4.02e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499997441 518 DQVLFEELRKARRILAQKRGVPPFVIFSDLSLRDMAARKPQTPEELLQCSGVGDAKLANYGKAMLAVIKKY 588
Cdd:smart00341 4 QLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEA 74
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
31-175 |
1.04e-17 |
|
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: 80.14 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 31 GKNVLAVMPTGGGKSLCYQIPAL--MIPGA--TVVISPLISLMKDQVDSMREY---GIPAAALNSSTAQEDvnpiLRACY 103
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALllLLKKGkkVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEE----REKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499997441 104 EGKIKLLYVTPERMEMDYFRY-QLNFLEVNLVAIDEAHCISQWGHDFRPAYRklkDGINALHTHPNVLALTAT 175
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLREdRLFLKDLKLIIVDEAHALLIDSRGALILDL---AVRKAGLKNAQVILLSAT 146
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
206-333 |
8.22e-16 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 74.08 E-value: 8.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 206 HFKLVNAPKNSRAYIVNYLKQHRGEAGIIYSNTRKKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVA 285
Cdd:cd18787 4 LYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 499997441 286 TNAFGMGIDKSNVRFVLHANSAKNLEAYYQEAGRAGRDGLESEAVMLF 333
Cdd:cd18787 84 TDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
233-332 |
9.06e-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: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 233 IIYSNTRKKVEGLTEFLRRE-------GFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHAN 305
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARlveegplASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*..
gi 499997441 306 SAKNLEAYYQEAGRAGRDGLESEAVML 332
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
13-345 |
8.68e-13 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 70.97 E-value: 8.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 13 GYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALM-------------IPGATVVISP---LISLMKDQVdSM 76
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctirsghpseqRNPLAMVLTPtreLCVQVEDQA-KV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 77 REYGIP-AAALnssTAQEDVNPilRACY--EGKIKLLYVTPERMEMDYFRYQLNFLEVNLVAIDEAHCISQWGhdFRPAY 153
Cdd:PLN00206 219 LGKGLPfKTAL---VVGGDAMP--QQLYriQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG--FRDQV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 154 RKLkdgINALHThPNVLALTATATKAVrEDIGQQLdisEENFVITSFERKNLHFKLVNA------PKNSRAYIVNYL--K 225
Cdd:PLN00206 292 MQI---FQALSQ-PQVLLFSATVSPEV-EKFASSL---AKDIILISIGNPNRPNKAVKQlaiwveTKQKKQKLFDILksK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 226 QHRGEAGIIYSNTRKKVEGLTEFLRR-EGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHA 304
Cdd:PLN00206 364 QHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIF 443
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 499997441 305 NSAKNLEAYYQEAGRAGRDGLESEAVMLFHPSDLRQFRWFI 345
Cdd:PLN00206 444 DMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELV 484
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
21-324 |
6.17e-12 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 68.37 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 21 QREIIEKVFQGKNVLAVMPTGGGKSLC--YQIPALMIPG-ATVVISPLISLMKD---QVDSMREYGIpaaALNSSTAQED 94
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIaySAIYETFLAGlKSIYIVPLRSLAMEkyeELSRLRSLGM---RVKISIGDYD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 95 VNPILRACYEGKIkllyVTPERME--MDYFRYQLNflEVNLVAIDEAHCIsqwGHDFR-PAYRKLKDGINALHTHPNVLA 171
Cdd:PRK01172 104 DPPDFIKRYDVVI----LTSEKADslIHHDPYIIN--DVGLIVADEIHII---GDEDRgPTLETVLSSARYVNPDARILA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 172 LTATATKAvrEDIGQQLDIS--EENF---------------VITSFERKNLHFKL---------------VNAPKNSRAY 219
Cdd:PRK01172 175 LSATVSNA--NELAQWLNASliKSNFrpvplklgilyrkrlILDGYERSQVDINSliketvndggqvlvfVSSRKNAEDY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 220 IVNyLKQHRGEAG---IIYSNTRKKVEGLTEFLRRegfNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKS 296
Cdd:PRK01172 253 AEM-LIQHFPEFNdfkVSSENNNVYDDSLNEMLPH---GVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP 328
|
330 340 350
....*....|....*....|....*....|....*...
gi 499997441 297 nVRFV----------LHANSAKNLEAyYQEAGRAGRDG 324
Cdd:PRK01172 329 -ARLVivrditrygnGGIRYLSNMEI-KQMIGRAGRPG 364
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
233-342 |
3.07e-11 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 65.62 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 233 IIYSNTRKKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEA 312
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100 110
....*....|....*....|....*....|
gi 499997441 313 YYQEAGRAGRDGLESEAVMLFHPSDLRQFR 342
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIEQLK 380
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
201-322 |
5.54e-11 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 65.68 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 201 ERKNLHFKLVnapknSRAYIVNYLKQHRGEAgIIYSNTRKKVEGLTEFLrreGFNVAAYHAGMSNEERAQVQDDFQYDRI 280
Cdd:COG1202 405 EKIRIINKLV-----KREFDTKSSKGYRGQT-IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQEL 475
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 499997441 281 PLIVATNAFGMGID--KSNVRFVLHANSAK--NLEAYYQEAGRAGR 322
Cdd:COG1202 476 AAVVTTAALAAGVDfpASQVIFDSLAMGIEwlSVQEFHQMLGRAGR 521
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
207-332 |
7.31e-11 |
|
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: 60.64 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 207 FKLVNAPKNSRAYIVNYLK--QHRGEAG-IIYSNTRKKVEGLTEFLRregfNVAAYHAGMSNEERAQVQDDFQYDRIPLI 283
Cdd:cd18795 18 KLRVDVMNKFDSDIIVLLKieTVSEGKPvLVFCSSRKECEKTAKDLA----GIAFHHAGLTREDRELVEELFREGLIKVL 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499997441 284 VATNAFGMGID--------KSNVRFVlhANSAKNLEA--YYQEAGRAGRDGLES--EAVML 332
Cdd:cd18795 94 VATSTLAAGVNlpartviiKGTQRYD--GKGYRELSPleYLQMIGRAGRPGFDTrgEAIIM 152
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
465-587 |
9.51e-11 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 63.74 E-value: 9.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 465 LVDYLVSKGYLQLV-GDCYPLVHVTNRGWDVLDGKARVKRRQEVKSEQLAetggdqvLFEELRKARRILAQKRGVPPFVI 543
Cdd:COG0349 162 LLEELEREGRLEWAeEECARLLDPATYREDPEEAWLRLKGAWKLNPRQLA-------VLRELAAWREREARKRDVPRNRV 234
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 499997441 544 FSDLSLRDMAARKPQTPEELLQCSGVGDAKLANYGKAMLAVIKK 587
Cdd:COG0349 235 LKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAE 278
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
21-175 |
9.72e-11 |
|
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: 61.06 E-value: 9.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 21 QREIIEKVFQGKNVLAVMPTGGGKSLCYQIPAL----MIPGAT-VVISPLISLMKDQVDSMREY------GIPAAALNSS 89
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeallRDPGSRaLYLYPTKALAQDQLRSLRELleqlglGIRVATYDGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 90 TAQEDVnpilRACYEGKIKLLYVTPERMEMDYFRY---QLNFLEvNL--VAIDEAHC-ISQWGHDFRPAYRKLKDGINAL 163
Cdd:cd17923 85 TPREER----RAIIRNPPRILLTNPDMLHYALLPHhdrWARFLR-NLryVVLDEAHTyRGVFGSHVALLLRRLRRLCRRY 159
|
170
....*....|..
gi 499997441 164 HTHPNVLALTAT 175
Cdd:cd17923 160 GADPQFILTSAT 171
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
31-342 |
1.95e-10 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 63.64 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 31 GKNVLAVMPTGGGKSLCYQIPA--------LMIPG---ATVVISPLISLMKDQVDSMREYGIpAAALNSSTAQEDVnPIL 99
Cdd:PTZ00110 167 GRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPTRELAEQIREQCNKFGA-SSKIRNTVAYGGV-PKR 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 100 RACYEGK--IKLLYVTPERMeMDYFRYQL-NFLEVNLVAIDEAHCISQWGhdFRPAYRKLKDGInalhtHPN--VLALTA 174
Cdd:PTZ00110 245 GQIYALRrgVEILIACPGRL-IDFLESNVtNLRRVTYLVLDEADRMLDMG--FEPQIRKIVSQI-----RPDrqTLMWSA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 175 TATKAVRE------------------DIGQQLDISEENFVITSFERknlhfklvnapknsRAYIVNYLKQHRGEAG--II 234
Cdd:PTZ00110 317 TWPKEVQSlardlckeepvhvnvgslDLTACHNIKQEVFVVEEHEK--------------RGKLKMLLQRIMRDGDkiLI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 235 YSNTRKKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYY 314
Cdd:PTZ00110 383 FVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYV 462
|
330 340
....*....|....*....|....*...
gi 499997441 315 QEAGRAGRDGLESEAVMLFHPSDLRQFR 342
Cdd:PTZ00110 463 HRIGRTGRAGAKGASYTFLTPDKYRLAR 490
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
13-342 |
4.22e-10 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 62.56 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 13 GYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALMIPGATV------VISPLISLMKDQVDSMREY-----GI 81
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELkapqilVLAPTRELAVQVAEAMTDFskhmrGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 82 PAAALNSSTaQEDVNpiLRACYEGKiKLLYVTPERMeMDYF-RYQLNFLEVNLVAIDEAHCISQWG--HDFRPAYRKLKD 158
Cdd:PRK11634 105 NVVALYGGQ-RYDVQ--LRALRQGP-QIVVGTPGRL-LDHLkRGTLDLSKLSGLVLDEADEMLRMGfiEDVETIMAQIPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 159 GinalhtHPNVLaLTATATKAVREDIGQQLDISEENFVITSferknlhfkLVNAPKNSRAY-----------IVNYLKQH 227
Cdd:PRK11634 180 G------HQTAL-FSATMPEAIRRITRRFMKEPQEVRIQSS---------VTTRPDISQSYwtvwgmrkneaLVRFLEAE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 228 RGEAGIIYSNTRKKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHANSA 307
Cdd:PRK11634 244 DFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIP 323
|
330 340 350
....*....|....*....|....*....|....*
gi 499997441 308 KNLEAYYQEAGRAGRDGLESEAVMLFHPSDLRQFR 342
Cdd:PRK11634 324 MDSESYVHRIGRTGRAGRAGRALLFVENRERRLLR 358
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
225-322 |
3.88e-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: 55.73 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 225 KQHRGEAGIIYSNTRKKVEGLTEFLRR------EGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNV 298
Cdd:cd18796 34 LLERHKSTLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDV 113
|
90 100
....*....|....*....|....
gi 499997441 299 RFVLHANSAKNLEAYYQEAGRAGR 322
Cdd:cd18796 114 DLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
5-322 |
1.29e-08 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 57.90 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 5 QQVLKKYfGYDSFRPGQREIIEK-VFQGKNVLAVMPTGGGKSLCYQIPA----LMIPGATVVISPLISLMKDQVDSMREY 79
Cdd:PRK00254 13 KRVLKER-GIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMvnklLREGGKAVYLVPLKALAEEKYREFKDW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 80 ---GIPAAALNSSTAQEDVnpilracYEGKIKLLYVTPERMEmDYFRYQLNFL-EVNLVAIDEAHCIsqwGHDFRPAyrK 155
Cdd:PRK00254 92 eklGLRVAMTTGDYDSTDE-------WLGKYDIIIATAEKFD-SLLRHGSSWIkDVKLVVADEIHLI---GSYDRGA--T 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 156 LKDGINALHTHPNVLALTATATKAvrEDIGQQLDISeenFVITSFE----RKNLHF---------KLVNAPKNSRAYIVN 222
Cdd:PRK00254 159 LEMILTHMLGRAQILGLSATVGNA--EELAEWLNAE---LVVSDWRpvklRKGVFYqgflfwedgKIERFPNSWESLVYD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 223 YLKqhRGEAGIIYSNTRKKVE-----------------------GLTEFLRREGFN----------VAAYHAGMSNEERA 269
Cdd:PRK00254 234 AVK--KGKGALVFVNTRRSAEkealelakkikrfltkpelralkELADSLEENPTNeklkkalrggVAFHHAGLGRTERV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499997441 270 QVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLhansaKNLEAY-------------YQEAGRAGR 322
Cdd:PRK00254 312 LIEDAFREGLIKVITATPTLSAGINLPAFRVII-----RDTKRYsnfgwedipvleiQQMMGRAGR 372
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
16-192 |
2.21e-08 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 54.19 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 16 SFRPGQREIIEKVFQ-GKNVLAVMPTGGGKSLCYQ---IPALMIPGATVV-ISPLISLMKDQVDSMREYGIPaaaLNSST 90
Cdd:cd17921 1 LLNPIQREALRALYLsGDSVLVSAPTSSGKTLIAElaiLRALATSGGKAVyIAPTRALVNQKEADLRERFGP---LGKNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 91 AQEDVNPILRACYEGKIKLLYVTPERME-MDYFRYQLNFLEVNLVAIDEAHCISQwGHdfR-PAYRKLKDGINALHTHPN 168
Cdd:cd17921 78 GLLTGDPSVNKLLLAEADILVATPEKLDlLLRNGGERLIQDVRLVVVDEAHLIGD-GE--RgVVLELLLSRLLRINKNAR 154
|
170 180
....*....|....*....|....
gi 499997441 169 VLALTATATKAvrEDIGQQLDISE 192
Cdd:cd17921 155 FVGLSATLPNA--EDLAEWLGVED 176
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
16-175 |
3.36e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 53.06 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 16 SFRPGQREIIEKV-----FQGKNVLAVMPTGGGKSLCY-QIPALMIPGA----TVVISPLISLMKDQVDSMREYGIPAAA 85
Cdd:pfam04851 3 ELRPYQIEAIENLlesikNGQKRGLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 86 LNSSTAQE------DVNPILRACYEGKIKLLYVTPERMEMDYFryqlnflevNLVAIDEAHcisqwgHDFRPAYRKLKDG 159
Cdd:pfam04851 83 IGEIISGDkkdesvDDNKIVVTTIQSLYKALELASLELLPDFF---------DVIIIDEAH------RSGASSYRNILEY 147
|
170
....*....|....*.
gi 499997441 160 INALHthpnVLALTAT 175
Cdd:pfam04851 148 FKPAF----LLGLTAT 159
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
16-191 |
2.94e-07 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 50.78 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 16 SFRPGQREIIEKVFQgKNVLAVMPTGGGKSLcyqIPA-LMI------PGATVV-ISPLISLMKDQVDSMREY-GIPaaal 86
Cdd:cd18033 2 PLRDYQFTIVQKALF-QNTLVALPTGLGKTF---IAAvVMLnyyrwfPKGKIVfMAPTKPLVSQQIEACYKItGIP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 87 NSSTAQ--EDVNPILRACYEGKIKLLYVTPERMEMDYFRYQLNFLEVNLVAIDEAHcisqwghdfRP----AYRKLKDGI 160
Cdd:cd18033 74 SSQTAEltGSVPPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAH---------RAtgnyAYCQVVREL 144
|
170 180 190
....*....|....*....|....*....|....
gi 499997441 161 NALHTHPNVLALTAT---ATKAVREDIgQQLDIS 191
Cdd:cd18033 145 MRYNSHFRILALTATpgsKLEAVQQVI-DNLLIS 177
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
16-143 |
3.94e-07 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 50.41 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 16 SFRPGQREIIEK-VFQGKNVLAVMPTGGGKSLCYQ---IPALMIPGATVVISPLISLMKDQVDSMREY-------GIPAA 84
Cdd:cd18028 1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRALASEKYEEFKKLeeiglkvGISTG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 499997441 85 ALNSSTAQEDVNPILRACYEGKIKLLYVTPERMEmdyfryqlnflEVNLVAIDEAHCIS 143
Cdd:cd18028 81 DYDEDDEWLGDYDIIVATYEKFDSLLRHSPSWLR-----------DVGVVVVDEIHLIS 128
|
|
| RQC_minor_1 |
NF041107 |
RQC-minor-1 family DNA-binding protein; The DNA-binding RQC domain (PF09382) appears primarily ... |
418-544 |
6.76e-07 |
|
RQC-minor-1 family DNA-binding protein; The DNA-binding RQC domain (PF09382) appears primarily in RecQ, a DNA helicase involved in recombination, replication, and repair. However, it appears also in this uncharacterized protein family, to which we give the name "RQC-minor-1 family DNA-binding protein." A majority of members contain an additional C-terminal predicted zinc-ribbon domain. Members appear not to show any conserved gene neighborhood.
Pssm-ID: 469031 [Multi-domain] Cd Length: 173 Bit Score: 49.49 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 418 DLDGRYGKRIVAQAVTGSKVKKISEIGGDECVHYGLLKGKKQADVSSLVDYLVSKGYLQL--VGDcYPLVHVTNRGWdvl 495
Cdd:NF041107 16 EIIATGGRTMLAKILKGSKDKKVLELGLDQCPAYGYYKSLTLEEITAKIDWMIKHDYLEIeyDGR-LPLLVFTERGW--- 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 499997441 496 dgkarvkrrqEVKSEQLAETggdqvLFEELRKArrilAQKRGVPPFVIF 544
Cdd:NF041107 92 ----------EIEREQYADE-----LLQEWEEW----LEQGKQPPDMIY 121
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
277-333 |
6.76e-07 |
|
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: 46.93 E-value: 6.76e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 499997441 277 YDRIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQEAGRAGRDGLESEAVMLF 333
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILF 76
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
201-332 |
2.07e-06 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 50.33 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 201 ERKNLH--FKLVNAPKNSRAYIVNYLKQHRGEAGIIYSNTRKKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYD 278
Cdd:PRK11192 215 ERKKIHqwYYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDG 294
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 499997441 279 RIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQEAGRAGRDGLESEAVML 332
Cdd:PRK11192 295 RVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
12-342 |
2.18e-06 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 50.71 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 12 FGYDSFrpgQREIIEKVFQGKNVLAVMPTGGGKSL--CYQIpALMIPGATVVI--SPLISL----MKDQVdsmREYGipA 83
Cdd:COG4581 24 FELDPF---QEEAILALEAGRSVLVAAPTGSGKTLvaEFAI-FLALARGRRSFytAPIKALsnqkFFDLV---ERFG--A 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 84 AALNSSTAQEDVNP----------ILRacyegkiKLLYVTPERMEmdyfryqlnflEVNLVAIDEAHCISqwghD-FRpa 152
Cdd:COG4581 95 ENVGLLTGDASVNPdapivvmtteILR-------NMLYREGADLE-----------DVGVVVMDEFHYLA----DpDR-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 153 yrklkdG------INALHTHPNVLALTATATKAvrEDIGQQLD-ISEENFVITSFERK-NLHFKLVNAPK---------- 214
Cdd:COG4581 151 ------GwvweepIIHLPARVQLVLLSATVGNA--EEFAEWLTrVRGETAVVVSEERPvPLEFHYLVTPRlfplfrvnpe 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 215 ----NSRAYIVNYLkQHRGEAGIIYSN-TRKKVEG-------------------------------------LTEFLRRe 252
Cdd:COG4581 223 llrpPSRHEVIEEL-DRGGLLPAIVFIfSRRGCDEaaqqllsarlttkeeraeireaidefaedfsvlfgktLSRLLRR- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 253 GfnVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIdksNV--RFVLHANSAK-------NLEA--YYQEAGRAG 321
Cdd:COG4581 301 G--IAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGI---NMpaRTVVFTKLSKfdgerhrPLTAreFHQIAGRAG 375
|
410 420
....*....|....*....|....
gi 499997441 322 RDGLESE--AVMLFHP-SDLRQFR 342
Cdd:COG4581 376 RRGIDTEghVVVLAPEhDDPKKFA 399
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
16-175 |
2.68e-06 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 48.20 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 16 SFRPGQREIIEKVFQGKNVLAVMPTGGGKS-----LC----YQIPALMiPGATVVISPLISLMKDQVDSMREY-GIPAAA 85
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPAGR-KGKVVFLANKVPLVEQQKEVFRKHfERPGYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 86 LNSSTAQEDVNPILRACYEGKiKLLYVTPERMEMDYFRYQLNFLE-VNLVAIDEAHCISQwGHDFRP-AYRKLKDGINAL 163
Cdd:cd17927 81 VTGLSGDTSENVSVEQIVESS-DVIIVTPQILVNDLKSGTIVSLSdFSLLVFDECHNTTK-NHPYNEiMFRYLDQKLGSS 158
|
170
....*....|..
gi 499997441 164 HTHPNVLALTAT 175
Cdd:cd17927 159 GPLPQILGLTAS 170
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
222-324 |
3.38e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 49.91 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 222 NYLKQHRGEAGIIYSNTRKKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFV 301
Cdd:PRK01297 328 NLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHV 407
|
90 100
....*....|....*....|...
gi 499997441 302 LHANSAKNLEAYYQEAGRAGRDG 324
Cdd:PRK01297 408 INFTLPEDPDDYVHRIGRTGRAG 430
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
13-332 |
4.59e-06 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 49.42 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 13 GYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALMI------------PGATVVISPLISLMKDQVDSMREYg 80
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHlitrqphakgrrPVRALILTPTRELAAQIGENVRDY- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 81 ipAAALNSST----AQEDVNPILRAcYEGKIKLLYVTPERMEMDYFRYQLNFLEVNLVAIDEAHCISQWG--HDFR---- 150
Cdd:PRK10590 99 --SKYLNIRSlvvfGGVSINPQMMK-LRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGfiHDIRrvla 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 151 --PAYRKlkdgiNALHTHPNVLALTATATKAVREDIgqQLDISEENfviTSFERKNLHFKLVNApKNSRAYIVNYLKQHR 228
Cdd:PRK10590 176 klPAKRQ-----NLLFSATFSDDIKALAEKLLHNPL--EIEVARRN---TASEQVTQHVHFVDK-KRKRELLSQMIGKGN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 229 GEAGIIYSNTRKKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHANSAK 308
Cdd:PRK10590 245 WQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPN 324
|
330 340
....*....|....*....|....
gi 499997441 309 NLEAYYQEAGRAGRDGLESEAVML 332
Cdd:PRK10590 325 VPEDYVHRIGRTGRAAATGEALSL 348
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
31-140 |
1.06e-05 |
|
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: 46.04 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 31 GKNVLAVMPTGGGKSLCYQIPAL---MIPGATVV----ISPLISLMKDQVDSMREY------GIPAAALNSSTAQEDVNP 97
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALsslADEPEKGVqvlyISPLKALINDQERRLEEPldeidlEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 499997441 98 ILRACYEgkikLLYVTPERME--MDYFRYQLNFLEVNLVAIDEAH 140
Cdd:cd17922 81 QLKNPPG----ILITTPESLEllLVNKKLRELFAGLRYVVVDEIH 121
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
3-63 |
2.82e-05 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 47.23 E-value: 2.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499997441 3 DPQQVLKKYFGYDSFRPGQREIIEKVFQ----GKNVLAVMPTGGGKSLCYQIPALMI---PGATVVIS 63
Cdd:COG1199 1 ADDGLLALAFPGFEPRPGQREMAEAVARalaeGRHLLIEAGTGTGKTLAYLVPALLAareTGKKVVIS 68
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
243-335 |
3.67e-05 |
|
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: 44.26 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 243 EGLTEFLRREgFNVAAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGID--KSNVRFVLHANSAkNLEAYYQEAGRA 320
Cdd:cd18811 52 EYLKERFRPE-LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDvpNATVMVIEDAERF-GLSQLHQLRGRV 129
|
90
....*....|....*
gi 499997441 321 GRDGLESEAVMLFHP 335
Cdd:cd18811 130 GRGDHQSYCLLVYKD 144
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
220-294 |
5.39e-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: 43.23 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 220 IVNYLKQHR--GEAGIIYSNTRKKVEGLTEFLRREGFNVAAYHAGMSNEERAQVQDDFQ---YDRIpLIVATNAFGMGID 294
Cdd:cd18793 16 LLELLEELRepGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedpDIRV-FLLSTKAGGVGLN 94
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1-46 |
2.12e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 44.49 E-value: 2.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 499997441 1 MLDPqqVLKKYF--GYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSL 46
Cdd:PRK13767 17 LLRP--YVREWFkeKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTL 62
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
5-54 |
3.68e-04 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 42.04 E-value: 3.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 499997441 5 QQVLKKYfGYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALM 54
Cdd:cd00268 2 LKALKKL-GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILE 50
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
21-140 |
4.43e-04 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 41.35 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 21 QREIIEKVFQGKNVLAVMPTGGGKSlcyqIPALMIP--------GATVVISPLISLMKDQVDSMREY---GIPAAALNSS 89
Cdd:cd18035 6 YQVLIAAVALNGNTLIVLPTGLGKT----IIAILVAadrltkkgGKVLILAPSRPLVEQHAENLKRVlniPDKITSLTGE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499997441 90 TAQEDVNPILRACyegkiKLLYVTPERMEMDYFRYQLNFLEVNLVAIDEAH 140
Cdd:cd18035 82 VKPEERAERWDAS-----KIIVATPQVIENDLLAGRITLDDVSLLIFDEAH 127
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
17-144 |
5.60e-04 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350780 [Multi-domain] Cd Length: 189 Bit Score: 41.21 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 17 FRPGQREIIEKVFQ-GKNVLAVMPTGGGKSLCYQIPALMI----PGATVV-ISPLISLMKDQVDSMREYGIPAAALNSST 90
Cdd:cd18022 2 FNPIQTQVFHTLYHtDNNVLLGAPTGSGKTIAAELAMFRAfnkyPGSKVVyIAPLKALVRERVDDWKKRFEEKLGKKVVE 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499997441 91 AQEDVNPILRACYEGKIklLYVTPERME--------MDYFRyqlnflEVNLVAIDEAHCISQ 144
Cdd:cd18022 82 LTGDVTPDMKALADADI--IITTPEKWDgisrswqtREYVQ------QVSLIIIDEIHLLGS 135
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
17-175 |
7.94e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 39.98 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 17 FRPGQREIIEKVFQGKN----VLaVMPTGGGKSLC-YQIPALMIPGATVVISPLISLMKDQVDSMREYGIPAA-ALNSST 90
Cdd:cd17926 1 LRPYQEEALEAWLAHKNnrrgIL-VLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSiGLIGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 91 AQEDVNpilracyegKIKLLYVTPERMEMDYFRYQLNFLEVNLVAIDEAHCISQwghdfrPAYRKLKDGINAlhthPNVL 170
Cdd:cd17926 80 KKKDFD---------DANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPA------KTFSEILKELNA----KYRL 140
|
....*
gi 499997441 171 ALTAT 175
Cdd:cd17926 141 GLTAT 145
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
206-322 |
7.97e-04 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 40.03 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 206 HFKLVNAPKNSRAyivnylkqhrgeagIIYSNTRKKVEGLTEFLRREGFNVAA----------YHAGMSNEERAQVQDDF 275
Cdd:cd18801 21 HFKKKQEGSDTRV--------------IIFSEFRDSAEEIVNFLSKIRPGIRAtrfigqasgkSSKGMSQKEQKEVIEQF 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499997441 276 QYDRIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQEAGRAGR 322
Cdd:cd18801 87 RKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
238-321 |
9.70e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 42.22 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 238 TRKKVEGLTEFLRRegfnvaAYHAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGIDKSNVRFVLHANSAKNLEAYYQEA 317
Cdd:PRK09751 292 TSNRVQSSDVFIAR------SHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRI 365
|
....
gi 499997441 318 GRAG 321
Cdd:PRK09751 366 GRAG 369
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
10-184 |
4.76e-03 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 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: 350700 [Multi-domain] Cd Length: 198 Bit Score: 38.50 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 10 KYFGYDSFRPGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALMI----------PGATVVISP-----------LISL 68
Cdd:cd17942 6 EEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELlyklkfkprnGTGVIIISPtrelalqiygvAKEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 69 MKDQVDSmreYGIPAAALNSSTAQEDVnpilracyeGK-IKLLYVTPERMeMDYFRYQLNFLEVNL--VAIDEAHCISQW 145
Cdd:cd17942 86 LKYHSQT---FGIVIGGANRKAEAEKL---------GKgVNILVATPGRL-LDHLQNTKGFLYKNLqcLIIDEADRILEI 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 499997441 146 GhdFRPAYRKLkdgINALHTHPNVLALTATATKAVrEDI 184
Cdd:cd17942 153 G--FEEEMRQI---IKLLPKRRQTMLFSATQTRKV-EDL 185
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
222-324 |
5.27e-03 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 39.71 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997441 222 NYLKQHRGEAGIIYSNTRKKVEGLTEFLRREGFNVAAY--------HAGMSNEERAQVQDDFQYDRIPLIVATNAFGMGI 293
Cdd:COG1111 346 EQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskegDKGLTQKEQIEILERFRAGEFNVLVATSVAEEGL 425
|
90 100 110
....*....|....*....|....*....|....*..
gi 499997441 294 DKSNVRFVLhansakNLEA------YYQEAGRAGRDG 324
Cdd:COG1111 426 DIPEVDLVI------FYEPvpseirSIQRKGRTGRKR 456
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
19-54 |
8.87e-03 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 37.95 E-value: 8.87e-03
10 20 30
....*....|....*....|....*....|....*.
gi 499997441 19 PGQREIIEKVFQGKNVLAVMPTGGGKSLCYQIPALM 54
Cdd:cd17957 15 PIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQ 50
|
|
| |
