|
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 ... |
2-589 |
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: 984.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 2 MQQTLSHYFGYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGLLLGGTTIVISPLISLMKDQVDQLKAMGIQA 81
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 82 AFLNSSLTQKEQQRIEKALSNGEIQFLYVAPERFENRYFLNLLQRIKIHLVAFDEAHCISKWGHDFRPSYQNVISKVFTL 161
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 162 PQDFtIIALTATATVEVQQDIREKLNIAQTDQIKTSTKRRNLIFKVNPTYQRQKFVLDYIKTHDEDAGIIYCSTRKQVEE 241
Cdd:TIGR01389 161 PQVP-RIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 242 LQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLESYYQEAGRAGRDG 321
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 322 LKSECILLFSERDINLHEYFITVSQADDDYKDKMGEKLTKMIQYTKTKKCLEATIVHYFEPNEkLEECEQCSNCVQQDKS 401
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENE-VEPCGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 402 YNMTQEAKMIISCIARMKQQESYSVIIQVLRGESTDYIKYKGYDQISTHGLMKGYTTSELSHLIDELRFKGFLNENDEI- 480
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIy 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 481 --LMCDTSIKKLLSNEVEVFTTPFKQKATEK--VFINTVEGVDRVLFSQLVEVRKKLSDKLTIAPVSIFSDYTLEEFAKR 556
Cdd:TIGR01389 479 igLQLTEAARKVLKNEVEVLLRPFKVVAKEKtrVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEK 558
|
570 580 590
....*....|....*....|....*....|...
gi 446906414 557 KPASKQDMINIDGVGSYKLKHYCPAFLETIQNY 589
Cdd:TIGR01389 559 RPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
2-468 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 686.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 2 MQQTLSHYFGYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGLLLGGTTIVISPLISLMKDQVDQLKAMGIQA 81
Cdd:COG0514 5 ALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 82 AFLNSSLTQKEQQRIEKALSNGEIQFLYVAPERFENRYFLNLLQRIKIHLVAFDEAHCISKWGHDFRPSYQNVISKVFTL 161
Cdd:COG0514 85 AFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRERL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 162 PqDFTIIALTATATVEVQQDIREKLNIAQTDQIKTSTKRRNLIFKVNPTYQRQK--FVLDYIKTHDEDAGIIYCSTRKQV 239
Cdd:COG0514 165 P-NVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKlaQLLDFLKEHPGGSGIVYCLSRKKV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 240 EELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLESYYQEAGRAGR 319
Cdd:COG0514 244 EELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 320 DGLKSECILLFSERDINLHEYFITVSQADDDYKDKMGEKLTKMIQYTKTKKCLEATIVHYF-EPNEklEECEQCSNCVQQ 398
Cdd:COG0514 324 DGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFgEELA--EPCGNCDNCLGP 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 399 DKSYNMTQEAKMIISCIARMKQQESYSVIIQVLRGESTDYIKYKGYDQISTHGLMKGYTTSELSHLIDEL 468
Cdd:COG0514 402 PETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQL 471
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
3-589 |
2.60e-161 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 474.20 E-value: 2.60e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 3 QQTLSHYFGYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGLLLGGTTIVISPLISLMKDQVDQLKAMGIQAA 82
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 83 FLNSSLTQKEQQRIEKALSNGEIQFLYVAPERFENRYFLNLLQRIKIHLVAFDEAHCISKWGHDFRPSYqnviSKVFTLP 162
Cdd:PRK11057 94 CLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEY----AALGQLR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 163 QDFT---IIALTATATVEVQQDIREKLNIAQTDQIKTSTKRRN----LIFKVNPTYQrqkfVLDYIKTHDEDAGIIYCST 235
Cdd:PRK11057 170 QRFPtlpFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNirytLVEKFKPLDQ----LMRYVQEQRGKSGIIYCNS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 236 RKQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLESYYQEAG 315
Cdd:PRK11057 246 RAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 316 RAGRDGLKSECILLFSERDIN-----LHEyfitvsQADDDYKDKMGEKLTKMIQYTKTKKCLEATIVHYFEPNEKlEECE 390
Cdd:PRK11057 326 RAGRDGLPAEAMLFYDPADMAwlrrcLEE------KPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQ-EPCG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 391 QCSNCVQQDKSYNMTQEAKMIISCIARMKQQESYSVIIQVLRGESTDYIKYKGYDQISTHGLMKGYTTSELSHLIDELRF 470
Cdd:PRK11057 399 NCDICLDPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 471 KGFLNENdeILMCDT-----SIKKLLSNEVEV-FTTP----FKQKATEKVFINTvegVDRVLFSQLVEVRKKLSDKLTIA 540
Cdd:PRK11057 479 LGLVTQN--IAQHSAlqlteAARPVLRGEVSLqLAVPrivaLKPRAMQKSFGGN---YDRKLFAKLRKLRKSIADEENIP 553
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 446906414 541 PVSIFSDYTLEEFAKRKPASKQDMINIDGVGSYKLKHYCPAFLETIQNY 589
Cdd:PRK11057 554 PYVVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAH 602
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
4-451 |
3.50e-143 |
|
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: 423.03 E-value: 3.50e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 4 QTLSHYFGYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGLLLGGTTIVISPLISLMKDQVDQLKAMGIQAAF 83
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 84 LNSSLTQKEQQRIEKALSNGEIQFLYVAPERF--ENRYFLNLLQRIKIHLVAFDEAHCISKWGHDFRPSYQNVISKVFTL 161
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsaSNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 162 PqDFTIIALTATATVEVQQDIREKLNIAQTDQIKTSTKRRNLIFKV-----NPTYQRQKFVldyIKTHDEDAGIIYCSTR 236
Cdd:TIGR00614 161 P-NVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVrrktpKILEDLLRFI---RKEFEGKSGIIYCPSR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 237 KQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLESYYQEAGR 316
Cdd:TIGR00614 237 KKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 317 AGRDGLKSECILLFSERDINLHEYFItVSQADDDYKDKMGEKLTKMIQYTKTKKCLEATIVHYFE------------PNE 384
Cdd:TIGR00614 317 AGRDGLPSECHLFYAPADMNRLRRLL-MEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGekgfnksfcimgTEK 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 385 KLEECEQCSNCVQQ---DKSYNMTQEAKMIISCIARMKQQESYSVIIQVLRGESTDYIKYKGYDQISTHG 451
Cdd:TIGR00614 396 CCDNCCKRLDYKTKdvtDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYG 465
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
3-198 |
1.05e-98 |
|
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: 298.68 E-value: 1.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 3 QQTLSHYFGYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGLLLGGTTIVISPLISLMKDQVDQLKAMGIQAA 82
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 83 FLNSSLTQKEQQRIEKALSNGEIQFLYVAPERFENRYFLNLLQRIK----IHLVAFDEAHCISKWGHDFRPSYQNvISKV 158
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLR-LGRL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446906414 159 FTLPQDFTIIALTATATVEVQQDIREKLNIAQTDQIKTST 198
Cdd:cd17920 160 RRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASF 199
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
10-587 |
4.77e-91 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 304.51 E-value: 4.77e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 10 FGYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGLLLGGTTIVISPLISLMKDQVDQLKAMGIQAAFLNSSLT 89
Cdd:PLN03137 456 FGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGME 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 90 QKEQQRIEKALS--NGEIQFLYVAPER----------FENRYFLNLLQRIKIhlvafDEAHCISKWGHDFRPSYQN--VI 155
Cdd:PLN03137 536 WAEQLEILQELSseYSKYKLLYVTPEKvaksdsllrhLENLNSRGLLARFVI-----DEAHCVSQWGHDFRPDYQGlgIL 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 156 SKVFtlpQDFTIIALTATATVEVQQDIREKLNIAQTDQIKTSTKRRNLIFKVNPTYQR-----QKFVLDyikTHDEDAGI 230
Cdd:PLN03137 611 KQKF---PNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKclediDKFIKE---NHFDECGI 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 231 IYCSTRKQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLESY 310
Cdd:PLN03137 685 IYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGY 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 311 YQEAGRAGRDGLKSECILLFSERDINLHEYFITVSQAD--------------DDYKDKMGEKLTKMIQYTKT----KKCL 372
Cdd:PLN03137 765 HQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEqspmamgynrmassGRILETNTENLLRMVSYCENevdcRRFL 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 373 EatIVHYFEPNEKLEECEQCSNCVQQ----DKsyNMTQEAKMIISCIARMKQQESYSVIIQVLRGESTDYIKYKGYDQIS 448
Cdd:PLN03137 845 Q--LVHFGEKFDSTNCKKTCDNCSSSksliDK--DVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLS 920
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 449 THGLMKGYTTSELSHLIDELRFKGFLNEN----------DEILMCDTS-IKKLLSNEVEV---FTTPFKQKATEKVFINT 514
Cdd:PLN03137 921 LHGAGKHLSKGEASRILHYLVTEDILAEDvkksdlygsvSSLLKVNESkAYKLFSGGQTIimrFPSSVKASKPSKFEATP 1000
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 515 VEG-------------------VDRVLFSQLVEVRKKLSDKLT------IAPVSIFSDYTLEEFAKRKPASKQDMINIDG 569
Cdd:PLN03137 1001 AKGpltsgkqstlpmatpaqppVDLNLSAILYTALRKLRTALVkeagdgVMAYHIFGNATLQQISKRIPRTKEELLEING 1080
|
650
....*....|....*...
gi 446906414 570 VGSYKLKHYCPAFLETIQ 587
Cdd:PLN03137 1081 LGKAKVSKYGDRLLETIE 1098
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
4-198 |
1.95e-79 |
|
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: 249.10 E-value: 1.95e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 4 QTLSHYFGYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGLLL----GGTTIVISPLISLMKDQVDQLKAmGI 79
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLrrrgPGLTLVVSPLIALMKDQVDALPR-AI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 80 QAAFLNSSLTQKEQQRIEKALSNGEIQFLYVAPERFENRYFLNLL-QRIKIHLVAFDEAHCISKWGHDFRPSYQNVISKV 158
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLrQTPPISLLVVDEAHCISEWSHNFRPDYLRLCRVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446906414 159 FTLPQDFTIIALTATATVEVQQDIREKLNIAQTDQIKTST 198
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPL 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
3-188 |
1.58e-58 |
|
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: 194.51 E-value: 1.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 3 QQTLSHYFGYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGLLLGGTTIVISPLISLMKDQVDQLKAMGIQAA 82
Cdd:cd18015 7 KDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 83 FLNSSLTQKEQQRIEKALSNGEIQF--LYVAPERF-ENRYFLNLLQRI----KIHLVAFDEAHCISKWGHDFRPSYQNV- 154
Cdd:cd18015 87 MLNASSSKEHVKWVHAALTDKNSELklLYVTPEKIaKSKRFMSKLEKAynagRLARIAIDEVHCCSQWGHDFRPDYKKLg 166
|
170 180 190
....*....|....*....|....*....|....
gi 446906414 155 ISKvfTLPQDFTIIALTATATVEVQQDIREKLNI 188
Cdd:cd18015 167 ILK--RQFPNVPILGLTATATSKVLKDVQKILCI 198
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
6-197 |
4.52e-55 |
|
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: 184.98 E-value: 4.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 6 LSHYFGYETFRPGQEEIISKVL-DHRNVLGVLPTGGGKSICYQVPGLLLGGTTIVISPLISLMKDQVDQLKAMGIQAAFL 84
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 85 NSSLTQKEQQRIEkalsNGEIQFLYVAPERFENRyfLNLLQRIKIH--LVAFDEAHCISKWGHDFRPSYQNVISKVFTLP 162
Cdd:cd18017 84 GSAQSQNVLDDIK----MGKIRVIYVTPEFVSKG--LELLQQLRNGitLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 446906414 163 qDFTIIALTATATVEVQQDIREKLNIAQTDQIKTS 197
Cdd:cd18017 158 -NVPIVALTATATPSVRDDIIKNLNLRNPQITCTS 191
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
200-330 |
3.18e-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: 175.09 E-value: 3.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 200 RRNLIFKVNPT------YQRQKFVLDYiktHDEDAGIIYCSTRKQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFL 273
Cdd:cd18794 1 RPNLFYSVRPKdkkdekLDLLKRIKVE---HLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446906414 274 FDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLESYYQEAGRAGRDGLKSECILLF 330
Cdd:cd18794 78 RDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
2-188 |
4.65e-50 |
|
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: 171.93 E-value: 4.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 2 MQQTLSHYFGYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGLLLGGTTIVISPLISLMKDQVDQLKAMGIQA 81
Cdd:cd18016 5 MMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 82 AFLNSSLTQKEQQRIEKALSNGE--IQFLYVAPER----------FENRYFLNLLQRIKIhlvafDEAHCISKWGHDFRP 149
Cdd:cd18016 85 TYLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKisasnrlistLENLYERKLLARFVI-----DEAHCVSQWGHDFRP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446906414 150 SYQ--NVISKVFtlpQDFTIIALTATATVEVQQDIREKLNI 188
Cdd:cd18016 160 DYKrlNMLRQKF---PSVPMMALTATATPRVQKDILNQLKM 197
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
3-198 |
9.49e-49 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 168.42 E-value: 9.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 3 QQTLSHYFGYETFR-PGQEEIISKVLDHR-NVLGVLPTGGGKSICYQVPGLLLGGTTIVISPLISLMKDQVDQLKAMGIQ 80
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 81 AAFLNSSLTQKEQQRIEKALSNG--EIQFLYVAPER----FENRYFLNLLQRIKIHLVAFDEAHCISKWGHDFRPSYQ-- 152
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEkpQTKFLYITPEMaatsSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLrl 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446906414 153 -NVISKVFTLPqdftIIALTATATVEVQQDIREKLNIAQT-DQIKTST 198
Cdd:cd18014 161 gALRSRYGHVP----WVALTATATPQVQEDIFAQLRLKKPvAIFKTPC 204
|
|
| DpdF |
NF041063 |
protein DpdF; |
6-337 |
2.89e-39 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 153.91 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 6 LSHYFGYETFR-PGQEEIIskvldhRNVL----G-----VLPTGGGKSICYQVPGLLL---GGTTIVISPLISLMKDQVD 72
Cdd:NF041063 131 LAEALGFTHYRsPGQREAV------RAALlappGstlivNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQER 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 73 QLKAMGIQAAFLN-------SSLTQKEQQRIEKALSNGEIQFLYVAPE------RFenryflnLLQRI----KIHLVAFD 135
Cdd:NF041063 205 RARELLRRAGPDLggplawhGGLSAEERAAIRQRIRDGTQRILFTSPEsltgslRP-------ALFDAaeagLLRYLVVD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 136 EAHCISKWGHDFRPSYQNVISKVFTL------PQDFTIIALTATATVEVQQDIREKLNIAQTDQIKTSTKRRNlifkvNP 209
Cdd:NF041063 278 EAHLVDQWGDGFRPEFQLLAGLRRSLlrlapsGRPFRTLLLSATLTESTLDTLETLFGPPGPFIVVSAVQLRP-----EP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 210 TY---------QRQKFVLDYIKThdedAG---IIYCSTRKQVEELQEALES---QKIDSViyHAGLSNKEREEAQNDFLF 274
Cdd:NF041063 353 AYwvakcdseeERRERVLEALRH----LPrplILYVTKVEDAEAWLQRLRAagfRRVALF--HGDTPDAERERLIEQWRE 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446906414 275 DRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLESYYQEAGRAGRDGLKSECILLFSERDINL 337
Cdd:NF041063 427 NELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDI 489
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
16-180 |
9.53e-29 |
|
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: 112.34 E-value: 9.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 16 RPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGL------LLGGTTIVISPLISLMKDQVDQLKAMGIQAAF-LNSSL 88
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 89 TQKEQQRIEKALSNGEIqfLYVAPERFENRYFL-NLLQRIKihLVAFDEAHCISKWGhdFRPSYQNVISKvftLPQDFTI 167
Cdd:pfam00270 81 GGDSRKEQLEKLKGPDI--LVGTPGRLLDLLQErKLLKNLK--LLVLDEAHRLLDMG--FGPDLEEILRR---LPKKRQI 151
|
170
....*....|...
gi 446906414 168 IALTATATVEVQQ 180
Cdd:pfam00270 152 LLLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
8-187 |
2.47e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 103.73 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 8 HYFGYETFRPGQEEIISKVLDH-RNVLGVLPTGGGKSICYQVPGLLL-----GGTTIVISPLISLMKDQVDQLKAMGIQA 81
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 82 AFLNSSL-TQKEQQRIEKALSNGEIQFLYVAPERFENRYFLNLLQRIKIHLVAFDEAHCISKWGhdFRPSYQNVISKvft 160
Cdd:smart00487 82 GLKVVGLyGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKL--- 156
|
170 180
....*....|....*....|....*..
gi 446906414 161 LPQDFTIIALTATATVEVQQDIREKLN 187
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLN 183
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
11-337 |
9.25e-25 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 107.16 E-value: 9.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 11 GYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGL--LLGGT-----TIVISP---LIslmkDQV-DQLKAMGi 79
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPtreLA----LQVaEELRKLA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 80 qaAFLN-SSLT------QKEQQRiekALSNGeIQFLyVA-PERFenryfLNLLQR--IKIHLVAF---DEAhciskwghD 146
Cdd:COG0513 96 --KYLGlRVATvyggvsIGRQIR---ALKRG-VDIV-VAtPGRL-----LDLIERgaLDLSGVETlvlDEA--------D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 147 ------FRPSYQNVISKvftLPQDFTIIALTATATVEVQQDIREKLN----IAQTDQIKTSTKRRNLIFKVNPtYQRQKF 216
Cdd:COG0513 156 rmldmgFIEDIERILKL---LPKERQTLLFSATMPPEIRKLAKRYLKnpvrIEVAPENATAETIEQRYYLVDK-RDKLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 217 VLDYIKTHDEDAGIIYCSTRKQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVR 296
Cdd:COG0513 232 LRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVS 311
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446906414 297 FVIHYNMPGDLESYYQEAGRAGRDGLKSECILLFSERDINL 337
Cdd:COG0513 312 HVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRL 352
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
215-321 |
1.57e-24 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 98.44 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 215 KFVLDYIKTHDEDAGIIYCSTRKQVEElQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSN 294
Cdd:pfam00271 4 EALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
|
90 100
....*....|....*....|....*..
gi 446906414 295 VRFVIHYNMPGDLESYYQEAGRAGRDG 321
Cdd:pfam00271 83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
240-321 |
1.84e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 97.28 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 240 EELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLESYYQEAGRAGR 319
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 446906414 320 DG 321
Cdd:smart00490 81 AG 82
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
201-330 |
6.56e-22 |
|
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: 91.41 E-value: 6.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 201 RNLIFKVNPTYQRQKFVLDYIKTHDEDAGIIYCSTRKQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVV 280
Cdd:cd18787 2 KQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446906414 281 VATNAFGMGIDKSNVRFVIHYNMPGDLESYYQEAGRAGRDGLKSECILLF 330
Cdd:cd18787 82 VATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
403-491 |
7.75e-22 |
|
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: 89.84 E-value: 7.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 403 NMTQEAKMIISCIARMKQQESYSVIIQVLRGESTDYIKYKGYDQISTHGLMKGYTTSELSHLIDELRFKGFLNENDE--- 479
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGryp 80
|
90
....*....|..
gi 446906414 480 ILMCDTSIKKLL 491
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
400-497 |
2.65e-18 |
|
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: 80.66 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 400 KSYNMTQEAKMIISCIARMKQQESYSVIIQVLRGESTDYIKYKGYDQISTHGLMKGYTTSELSHLIDELRFKGFLNENDE 479
Cdd:pfam09382 3 ETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDIE 82
|
90 100
....*....|....*....|.
gi 446906414 480 ---ILMCDTSIKKLLSNEVEV 497
Cdd:pfam09382 83 fysVLKLTPKAREVLKGEEKV 103
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
16-317 |
1.05e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 86.62 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 16 RPGQEEIISKVL-----DHRNVLGVLPTGGGKSI----CYQvpGLLLGGTTIVISPLISLmkdqVDQLKAMgIQAAFLNS 86
Cdd:COG1061 82 RPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRREL----LEQWAEE-LRRFLGDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 87 SLTQKEQQRiekalsNGEIQFlyVAPERFENRYFLNLLQRiKIHLVAFDEAHciskwgHDFRPSYQNVISKvftLPQDFt 166
Cdd:COG1061 155 LAGGGKKDS------DAPITV--ATYQSLARRAHLDELGD-RFGLVIIDEAH------HAGAPSYRRILEA---FPAAY- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 167 IIALTAT--------------------------------ATVEVQQdIREKLNIAQTDQIKTSTKRRNLIFKVNPtyQRQ 214
Cdd:COG1061 216 RLGLTATpfrsdgreillflfdgivyeyslkeaiedgylAPPEYYG-IRVDLTDERAEYDALSERLREALAADAE--RKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 215 KFVLDYIKTH-DEDAGIIYCSTRKQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKS 293
Cdd:COG1061 293 KILRELLREHpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVP 372
|
330 340
....*....|....*....|....*
gi 446906414 294 NVRFVIhYNMP-GDLESYYQEAGRA 317
Cdd:COG1061 373 RLDVAI-LLRPtGSPREFIQRLGRG 396
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
519-586 |
1.01e-16 |
|
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: 74.49 E-value: 1.01e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446906414 519 DRVLFSQLVEVRKKLSDKLTIAPVSIFSDYTLEEFAKRKPASKQDMINIDGVGSYKLKHYCPAFLETI 586
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
230-329 |
3.02e-16 |
|
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: 75.76 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 230 IIYCSTRKQVE----ELQEALE-----SQKIDSviYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIH 300
Cdd:cd18797 39 IVFCRSRKLAElllrYLKARLVeegplASKVAS--YRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
|
90 100
....*....|....*....|....*....
gi 446906414 301 YNMPGDLESYYQEAGRAGRDGLKSECILL 329
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
11-347 |
5.71e-16 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 80.99 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 11 GYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVP------GLLLGGTT-------IVISPLISLMKDQVDQLKAM 77
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrccTIRSGHPSeqrnplaMVLTPTRELCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 78 GIQAAFLNSSLTQKE---QQ--RIEKAlsngeIQFLYVAPERFenryfLNLLQRIKIHL-----VAFDEAHCISKWGhdF 147
Cdd:PLN00206 220 GKGLPFKTALVVGGDampQQlyRIQQG-----VELIVGTPGRL-----IDLLSKHDIELdnvsvLVLDEVDCMLERG--F 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 148 RpsyQNVISKVFTLPQDfTIIALTATATVEVQQ---DIREKLNIAQTDQIKTSTKR-RNLIFKVNPTYQRQK-FVLDYIK 222
Cdd:PLN00206 288 R---DQVMQIFQALSQP-QVLLFSATVSPEVEKfasSLAKDIILISIGNPNRPNKAvKQLAIWVETKQKKQKlFDILKSK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 223 THDEDAGIIYCSTRKQVEELQEALE-SQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHY 301
Cdd:PLN00206 364 QHFKPPAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIF 443
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446906414 302 NMPGDLESYYQEAGRAGRDGLKSECILLFSERDINLHEYFITVSQA 347
Cdd:PLN00206 444 DMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKS 489
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
11-337 |
6.80e-16 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 81.05 E-value: 6.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 11 GYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGL------LLGGTTIVISPLISL-------MKDQVDQLKAM 77
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTRELavqvaeaMTDFSKHMRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 78 GIQAAFlnssltqkEQQRIE---KALSNGEiQFLYVAPERFenryfLNLLQRIKIHL-----VAFDEAHCISKWGhdFRP 149
Cdd:PRK11634 105 NVVALY--------GGQRYDvqlRALRQGP-QIVVGTPGRL-----LDHLKRGTLDLsklsgLVLDEADEMLRMG--FIE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 150 SYQNVISKVftlPQDFTIIALTATATVEVQQDIREKLNIAQTDQIKTSTKRRNLIFKVNPT---YQRQKFVLDYIKTHDE 226
Cdd:PRK11634 169 DVETIMAQI---PEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTvwgMRKNEALVRFLEAEDF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 227 DAGIIYCSTRKQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGD 306
Cdd:PRK11634 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
|
330 340 350
....*....|....*....|....*....|.
gi 446906414 307 LESYYQEAGRAGRDGLKSECILLFSERDINL 337
Cdd:PRK11634 326 SESYVHRIGRTGRAGRAGRALLFVENRERRL 356
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
19-321 |
1.95e-15 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 79.88 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 19 QEEIISKVLDHRNVLGVLPTGGGKSICYQVPGL--LL---GGTTIVISPLISLMKDQVDQLKAM------GIQAAFLNSS 87
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLedpGATALYLYPTKALARDQLRRLRELaealglGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 88 LTQKEQQRIekaLSNGEIqflyvapeRFENRYFLN------------LLQRIKihLVAFDEAHciskwghdfrpSYQNV- 154
Cdd:COG1205 141 TPPEERRWI---REHPDI--------VLTNPDMLHygllphhtrwarFFRNLR--YVVIDEAH-----------TYRGVf 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 155 ---ISKVF--------TLPQDFTIIAltATATVEVQQDIREKLniaqTDQ----IKTSTK---RRNLIFkVNP----TYQ 212
Cdd:COG1205 197 gshVANVLrrlrricrHYGSDPQFIL--ASATIGNPAEHAERL----TGRpvtvVDEDGSprgERTFVL-WNPplvdDGI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 213 RQ-----------KFVLDYIKThdedagIIYCSTRKQVE----ELQEALESQKIDSVI--YHAGLSNKEREEAQNDFLFD 275
Cdd:COG1205 270 RRsalaeaarllaDLVREGLRT------LVFTRSRRGAEllarYARRALREPDLADRVaaYRAGYLPEERREIERGLRSG 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446906414 276 RVKVVVATNAFGMGIDKSNVRFVI--HYnmPGDLESYYQEAGRAGRDG 321
Cdd:COG1205 344 ELLGVVSTNALELGIDIGGLDAVVlaGY--PGTRASFWQQAGRAGRRG 389
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
31-173 |
2.26e-14 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 70.51 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 31 NVLGVLPTGGGKSICYQVPGLLL----GGTTIVISPLISLMKDQVDQLKA---MGIQAAFLNSSLTQKEQqrieKALSNG 103
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRElfgPGIRVAVLVGGSSAEER----EKNKLG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446906414 104 EIQFLYVAPERFENRYFLNLLQRIK-IHLVAFDEAHCISKWGHDFRPSYQNVISKVFTLPQdftIIALTAT 173
Cdd:cd00046 79 DADIIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQ---VILLSAT 146
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
518-589 |
1.74e-12 |
|
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: 63.09 E-value: 1.74e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446906414 518 VDRVLFSQLVEVRKKLSDKLTIAPVSIFSDYTLEEFAKRKPASKQDMINIDGVGSYKLKHYCPAFLETIQNY 589
Cdd:smart00341 3 RQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEA 74
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
230-335 |
2.15e-11 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 66.00 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 230 IIYCSTRKQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLES 309
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100
....*....|....*....|....*.
gi 446906414 310 YYQEAGRAGRDGLKSECILLFSERDI 335
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDI 376
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
10-325 |
4.14e-11 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 65.69 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 10 FGYETFRPGQEEIISK-VLDHRNVLGVLPTGGGKS------ICYQvpgLLLGGTTIVISPLISL----MKDQVDQLKAMG 78
Cdd:COG1204 18 RGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTliaelaILKA---LLNGGKALYIVPLRALasekYREFKRDFEELG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 79 IQAAFLNSSLtqkeqQRIEKALSNGEIqflYVA-PERFE----NRYflNLLQRIKihLVAFDEAHCIskwGHDFR-PSYQ 152
Cdd:COG1204 95 IKVGVSTGDY-----DSDDEWLGRYDI---LVAtPEKLDsllrNGP--SWLRDVD--LVVVDEAHLI---DDESRgPTLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 153 NVISKVFTLPQDFTIIALtaTATVEVQQDIREKLNIAQ-------TDQIKTSTKRRNLIFKvnPTYQRQKFV-LDYIKTH 224
Cdd:COG1204 160 VLLARLRRLNPEAQIVAL--SATIGNAEEIAEWLDAELvksdwrpVPLNEGVLYDGVLRFD--DGSRRSKDPtLALALDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 225 DEDAG--IIYCSTRKQVEELQEALeSQKIDSVIY--------------------------------------HAGLSNKE 264
Cdd:COG1204 236 LEEGGqvLVFVSSRRDAESLAKKL-ADELKRRLTpeereeleelaeellevseethtnekladclekgvafhHAGLPSEL 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446906414 265 R---EEAqndFLFDRVKVVVATNAFGMGIdksN--VRFVI------HYNMPGDLESYYQEAGRAGRDGLKSE 325
Cdd:COG1204 315 RrlvEDA---FREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAGRPGYDPY 380
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
11-337 |
2.51e-10 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 62.65 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 11 GYEtfRPG--QEEIISKVLDHRNVLGVLPTGGGKSICYQVPGL--LL-------GGTTIVI-SP---LISLMKDQVDQLk 75
Cdd:PRK11192 20 GYT--RPTaiQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALqhLLdfprrksGPPRILIlTPtreLAMQVADQAREL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 76 amgiqAAFLNSSL----------TQKEqqriekALSngEIQFLYVA-PERfenryflnLLQRIK--------IHLVAFDE 136
Cdd:PRK11192 97 -----AKHTHLDIatitggvaymNHAE------VFS--ENQDIVVAtPGR--------LLQYIKeenfdcraVETLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 137 A---------HCISKWGHDFRPSYQNVIskvF--TLP----QDFTIIALTATATVEVQQDIREKLNIAQ----TDQIKts 197
Cdd:PRK11192 156 AdrmldmgfaQDIETIAAETRWRKQTLL---FsaTLEgdavQDFAERLLNDPVEVEAEPSRRERKKIHQwyyrADDLE-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 198 tkrrnlifkvnptyqrQKFVL--DYIKTHDEDAGIIYCSTRKQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFD 275
Cdd:PRK11192 231 ----------------HKTALlcHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDG 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446906414 276 RVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLESYYQEAGRAGRDGLKSECILLFSERDINL 337
Cdd:PRK11192 295 RVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLL 356
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
27-323 |
3.29e-10 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 62.87 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 27 LDHRNVLGVLPTGGGKSICYQVPGL-------LL----GGTTIVISPLISLmkdqVDQLKAMGIQaaFLNSSLTQ----- 90
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAIvhinaqpLLrygdGPIVLVLAPTREL----AEQIREQCNK--FGASSKIRntvay 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 91 ----KEQQRIekALSNGeIQFLYVAPERFENRYFLNLLQRIKIHLVAFDEAHCISKWGhdFRPSYQNVISKVftLPQDFT 166
Cdd:PTZ00110 239 ggvpKRGQIY--ALRRG-VEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMG--FEPQIRKIVSQI--RPDRQT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 167 IIaLTATATVEVQQDIRE-------KLNIAQTDqIKTSTKRRNLIFKVNPTYQRQKF--VLDYIkTHDEDAGIIYCSTRK 237
Cdd:PTZ00110 312 LM-WSATWPKEVQSLARDlckeepvHVNVGSLD-LTACHNIKQEVFVVEEHEKRGKLkmLLQRI-MRDGDKILIFVETKK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 238 QVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLESYYQEAGRA 317
Cdd:PTZ00110 389 GADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRT 468
|
....*.
gi 446906414 318 GRDGLK 323
Cdd:PTZ00110 469 GRAGAK 474
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
230-329 |
3.40e-10 |
|
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: 58.72 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 230 IIYCSTRKQVEELqealeSQKIDSV-IYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGID--------KSNVRFVIH 300
Cdd:cd18795 47 LVFCSSRKECEKT-----AKDLAGIaFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGK 121
|
90 100 110
....*....|....*....|....*....|.
gi 446906414 301 YNMPGDLESYYQEAGRAGRDGL--KSECILL 329
Cdd:cd18795 122 GYRELSPLEYLQMIGRAGRPGFdtRGEAIIM 152
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
333-395 |
3.75e-10 |
|
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: 56.14 E-value: 3.75e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446906414 333 RDINLHEYFITVSQADDDYKDKMGEKLTKMIQY-TKTKKCLEATIVHYFEPNEKLEECEQCSNC 395
Cdd:pfam16124 2 QDVVRLRFLIEQSEADEERKEVELQKLQAMVAYcENTTDCRRKQLLRYFGEEFDSEPCGNCDNC 65
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
273-329 |
5.96e-10 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 55.79 E-value: 5.96e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446906414 273 LFDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLESYYQEAGRAGRDG-LKSECILL 329
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
230-319 |
2.38e-08 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 53.42 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 230 IIYCSTRKQVE----ELQEALESQKIDSVIY--HAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHYNM 303
Cdd:cd18796 42 LVFTNTRSQAErlaqRLRELCPDRVPPDFIAlhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90
....*....|....*.
gi 446906414 304 PGDLESYYQEAGRAGR 319
Cdd:cd18796 122 PKSVARLLQRLGRSGH 137
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
19-321 |
5.19e-08 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 56.04 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 19 QEEIISKVLDHRNVLGVLPTGGGKS-ICYQV--PGLLLGGTTIVISPLISLMKDQVDQLkamgiqaaflnsSLTQKEQQR 95
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTlIAYSAiyETFLAGLKSIYIVPLRSLAMEKYEEL------------SRLRSLGMR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 96 IEKALSNgeiqflYVAPERFENRYFLNLLQRIK----IH----------LVAFDEAHCIskwGHDFR-PSYQNVISKVFT 160
Cdd:PRK01172 95 VKISIGD------YDDPPDFIKRYDVVILTSEKadslIHhdpyiindvgLIVADEIHII---GDEDRgPTLETVLSSARY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 161 LPQDFTIIALTATatVEVQQDIREKLNIAQtdqIKTSTkrRNLIFKVNPTYQRQKF----------VLDYIKTHDEDAG- 229
Cdd:PRK01172 166 VNPDARILALSAT--VSNANELAQWLNASL---IKSNF--RPVPLKLGILYRKRLIldgyersqvdINSLIKETVNDGGq 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 230 -IIYCSTRKQVEELQEALeSQKIDSV--------------------------IYHAGLSNKEREEAQNDFLFDRVKVVVA 282
Cdd:PRK01172 239 vLVFVSSRKNAEDYAEML-IQHFPEFndfkvssennnvyddslnemlphgvaFHHAGLSNEQRRFIEEMFRNRYIKVIVA 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446906414 283 TNAFGMGIDKSnVRFVIHYNMP--GDLESYY-------QEAGRAGRDG 321
Cdd:PRK01172 318 TPTLAAGVNLP-ARLVIVRDITryGNGGIRYlsnmeikQMIGRAGRPG 364
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
230-319 |
5.03e-07 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 52.97 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 230 IIYCSTRKQVEELQEALEsqkIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGID--KSNVRFvihynmpgdl 307
Cdd:COG1202 431 IIFTNSRRRCHEIARALG---YKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDfpASQVIF---------- 497
|
90 100
....*....|....*....|....
gi 446906414 308 ES------------YYQEAGRAGR 319
Cdd:COG1202 498 DSlamgiewlsvqeFHQMLGRAGR 521
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
8-334 |
5.86e-07 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 52.22 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 8 HYFGYETFRPGQEEIISKVLDHRNVLGVLPTGGGK------SICYQ-----VPGLLLGGT--TIVISP----LISLMKDQ 70
Cdd:PRK01297 103 HDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKtaafliSIINQllqtpPPKERYMGEprALIIAPtrelVVQIAKDA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 71 VDQLKAMGIQAAFLNSSLTQKEQQrieKALSNGEIQFLYVAPERFenryfLNLLQRIKIHL-----VAFDEAHCISKWGh 145
Cdd:PRK01297 183 AALTKYTGLNVMTFVGGMDFDKQL---KQLEARFCDILVATPGRL-----LDFNQRGEVHLdmvevMVLDEADRMLDMG- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 146 dFRPSYQNVISKVFTLPQDFTIIaLTATATVEVQQDIREKLNIAQTDQI----KTSTKRRNLIFKVNPTyQRQKFVLDYI 221
Cdd:PRK01297 254 -FIPQVRQIIRQTPRKEERQTLL-FSATFTDDVMNLAKQWTTDPAIVEIepenVASDTVEQHVYAVAGS-DKYKLLYNLV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 222 KTHDEDAGIIYCSTRKQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHY 301
Cdd:PRK01297 331 TQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINF 410
|
330 340 350
....*....|....*....|....*....|...
gi 446906414 302 NMPGDLESYYQEAGRAGRDGLKSECILLFSERD 334
Cdd:PRK01297 411 TLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
14-173 |
7.10e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.51 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 14 TFRPGQEEIISKVL-----DHRNVLGVLPTGGGKS-----ICYQVPGLLLGGTTIVISPLISLMKDQVDQLKAMGIQAAF 83
Cdd:pfam04851 3 ELRPYQIEAIENLLesiknGQKRGLIVMATGSGKTltaakLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 84 LNSSLTQKEQQRIEKA----LSNgeIQFLYVAPERFENRYFLNllqriKIHLVAFDEAHciskwgHDFRPSYQNVISKVf 159
Cdd:pfam04851 83 IGEIISGDKKDESVDDnkivVTT--IQSLYKALELASLELLPD-----FFDVIIIDEAH------RSGASSYRNILEYF- 148
|
170
....*....|....
gi 446906414 160 tlpQDFTIIALTAT 173
Cdd:pfam04851 149 ---KPAFLLGLTAT 159
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
19-138 |
8.06e-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: 46.81 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 19 QEEIISKVLDHRNVLGVLPTGGGKSICYQVPGL--LL---GGTTIVISPLISLMKDQVDQLKAM------GIQAAFLN-- 85
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLrdpGSRALYLYPTKALAQDQLRSLRELleqlglGIRVATYDgd 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446906414 86 SSLTQKEQQRIEKA---LSNGEIQFLYVAPERFENRYFLNLLQrikihLVAFDEAH 138
Cdd:cd17923 85 TPREERRAIIRNPPrilLTNPDMLHYALLPHHDRWARFLRNLR-----YVVLDEAH 135
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
14-174 |
9.10e-06 |
|
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: 46.49 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 14 TFRPGQEEIISKVLDH-RNVLGVLPTGGGKSICYQ---VPGLLLGGTTIV-ISPLISLMKDQVDQLKAMGIQAAFLNSSL 88
Cdd:cd17921 1 LLNPIQREALRALYLSgDSVLVSAPTSSGKTLIAElaiLRALATSGGKAVyIAPTRALVNQKEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 89 TQKEQQRIEKAlsnGEIQFLYVAPERFENR-YFLNLLQRIKIHLVAFDEAHCIskwGHDFR-PSYQNVISKVFTLPQDFT 166
Cdd:cd17921 81 TGDPSVNKLLL---AEADILVATPEKLDLLlRNGGERLIQDVRLVVVDEAHLI---GDGERgVVLELLLSRLLRINKNAR 154
|
....*...
gi 446906414 167 IIALTATA 174
Cdd:cd17921 155 FVGLSATL 162
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
230-329 |
2.27e-05 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 47.11 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 230 IIYCSTRKQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLES 309
Cdd:PRK10590 249 LVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPED 328
|
90 100
....*....|....*....|
gi 446906414 310 YYQEAGRAGRDGLKSECILL 329
Cdd:PRK10590 329 YVHRIGRTGRAAATGEALSL 348
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
132-322 |
2.83e-05 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 47.24 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 132 VAFDEAHCISkwghD-FR-PSYQNVIskvFTLPQDFTIIALTATA--TVEVQQDIREKLNiaQTDQIKT----------- 196
Cdd:COG4581 137 VVMDEFHYLA----DpDRgWVWEEPI---IHLPARVQLVLLSATVgnAEEFAEWLTRVRG--ETAVVVSeerpvplefhy 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 197 -STKRRNLIFKVNPTYQRQKFVLDYIKTHDEDAG---IIYCSTRKQVEELQEAL---------ESQKIDSVI-------- 255
Cdd:COG4581 208 lVTPRLFPLFRVNPELLRPPSRHEVIEELDRGGLlpaIVFIFSRRGCDEAAQQLlsarlttkeERAEIREAIdefaedfs 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 256 -----------------YHAGLSN--KEREEAqndfLFDR--VKVVVATNAFGMGIdksnvrfvihyNMP---------- 304
Cdd:COG4581 288 vlfgktlsrllrrgiavHHAGMLPkyRRLVEE----LFQAglLKVVFATDTLAVGI-----------NMPartvvftkls 352
|
250 260
....*....|....*....|....*..
gi 446906414 305 ---G----DLES--YYQEAGRAGRDGL 322
Cdd:COG4581 353 kfdGerhrPLTAreFHQIAGRAGRRGI 379
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
20-106 |
3.07e-04 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350687 [Multi-domain] Cd Length: 178 Bit Score: 41.81 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 20 EEIISKVLDHRNVL--GVlpTGGGKSICY-----QVpgLLLGGTTIVISPLISLMKDQVDQLKA-MGIQAAFLNSSLTQK 91
Cdd:cd17929 6 EAIVSSLGGFKTFLlhGV--TGSGKTEVYielieKV--LAKGKQVLVLVPEISLTPQLIKRFKKrFGDKVAVLHSKLSDK 81
|
90
....*....|....*
gi 446906414 92 EQQRIEKALSNGEIQ 106
Cdd:cd17929 82 ERADEWRKIKRGEAK 96
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
234-322 |
5.01e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 43.02 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 234 STRKQVEELQEALESqkiDSVIYHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMG--------IDKSNVRFVIHYNM-P 304
Cdd:PRK02362 290 SDTETSKDLADCVAK---GAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGlnlparrvIIRDYRRYDGGAGMqP 366
|
90
....*....|....*...
gi 446906414 305 GDLESYYQEAGRAGRDGL 322
Cdd:PRK02362 367 IPVLEYHQMAGRAGRPGL 384
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
14-186 |
5.96e-04 |
|
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: 41.26 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 14 TFRPGQEEIISKVLDHRNVLGVLPTGGGKS-----IC----YQVPGlLLGGTTIVISPLISLMKDQVDQLKAMGIQAAFL 84
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPA-GRKGKVVFLANKVPLVEQQKEVFRKHFERPGYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 85 NSSLT--QKEQQRIEKALSNGEIqfLYVAPERFENRYF-LNLLQRIKIHLVAFDEAHCISKWGhdfrpSYQNVI-----S 156
Cdd:cd17927 81 VTGLSgdTSENVSVEQIVESSDV--IIVTPQILVNDLKsGTIVSLSDFSLLVFDECHNTTKNH-----PYNEIMfryldQ 153
|
170 180 190
....*....|....*....|....*....|
gi 446906414 157 KVFTLPQDFTIIALTATATVEVQQDIREKL 186
Cdd:cd17927 154 KLGSSGPLPQILGLTASPGVGGAKNTEEAL 183
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
14-173 |
6.64e-04 |
|
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: 40.78 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 14 TFRPGQEEIISK-VLDHRNVLGVLPTGGGKSICYQ---VPGLLLGGTTIVISPLISLMKDQVDQLK---AMGIQAAflns 86
Cdd:cd18028 1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRALASEKYEEFKkleEIGLKVG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 87 sLTQKEQQRIEKALSNGEIqfLYVAPERFEN--RYFLNLLQRIKihLVAFDEAHCISKWGHDfrPSYQNVISKVFTLPQD 164
Cdd:cd18028 77 -ISTGDYDEDDEWLGDYDI--IVATYEKFDSllRHSPSWLRDVG--VVVVDEIHLISDEERG--PTLESIVARLRRLNPN 149
|
....*....
gi 446906414 165 FTIIALTAT 173
Cdd:cd18028 150 TQIIGLSAT 158
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
256-335 |
1.05e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 42.22 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 256 YHAGLSNKEREEAQNDFLFDRVKVVVATNAFGMGIDKSNVRFVIHYNMPGDLESYYQEAGRAGRD--GLKSECILLFSER 333
Cdd:PRK09751 307 HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQvgGVSKGLFFPRTRR 386
|
..
gi 446906414 334 DI 335
Cdd:PRK09751 387 DL 388
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
215-327 |
1.18e-03 |
|
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: 39.38 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 215 KFVLDYIKTHDEDAG--IIYCSTRKQVEELQEALESQKIDSVIYHAGLSNKEREEAQNDFLFD-RVKVV-VATNAFGMGI 290
Cdd:cd18793 14 EALLELLEELREPGEkvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVFlLSTKAGGVGL 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446906414 291 DKSNVRFVIHY----NmPGDLEsyyQEAGRAGRDGLKSECI 327
Cdd:cd18793 94 NLTAANRVILYdpwwN-PAVEE---QAIDRAHRIGQKKPVV 130
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
30-138 |
1.21e-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: 39.87 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 30 RNVLGVLPTGGGK------SICYQVPGLLLGGTTIV-ISPLISLMKDQVDQLKAM------GIQAAFLNSSLTQKEQQRI 96
Cdd:cd17922 2 RNVLIAAPTGSGKteaaflPALSSLADEPEKGVQVLyISPLKALINDQERRLEEPldeidlEIPVAVRHGDTSQSEKAKQ 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446906414 97 EKALSNgeiqFLYVAPERFE----NRYFLNLLQRIKihLVAFDEAH 138
Cdd:cd17922 82 LKNPPG----ILITTPESLElllvNKKLRELFAGLR--YVVVDEIH 121
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
11-187 |
4.46e-03 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 38.58 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 11 GYETFRPGQEEIISKVLDHRNVLGVLPTGGGKSICYQVPGL--LLGGTTIVISPLISLM-----------KDQVDQL-KA 76
Cdd:cd00268 9 GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekLLPEPKKKGRGPQALVlaptrelamqiAEVARKLgKG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 77 MGIQAAFLNSSLTQKEQqriEKALSNGeIQFLyVA-PERfenryFLNLLQRIKIHL-----VAFDEAhciskwghD---- 146
Cdd:cd00268 89 TGLKVAAIYGGAPIKKQ---IEALKKG-PDIV-VGtPGR-----LLDLIERGKLDLsnvkyLVLDEA--------Drmld 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446906414 147 --FRPSYQNVISKvftLPQDFTIIALTATATVEVQQDIREKLN 187
Cdd:cd00268 151 mgFEEDVEKILSA---LPKDRQTLLFSATLPEEVKELAKKFLK 190
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
15-138 |
5.61e-03 |
|
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: 37.67 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446906414 15 FRPGQEEIISKVLDHRN----VLgVLPTGGGKSIC-YQVPGLLLGGTTIVISPLISLMKDQVDQLKAMGIQAA-FLNSSL 88
Cdd:cd17926 1 LRPYQEEALEAWLAHKNnrrgIL-VLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSiGLIGGG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446906414 89 TQKEQQRIEKALSNGEIQFLYVAPERFENRYFLNLLqrikihlvaFDEAH 138
Cdd:cd17926 80 KKKDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLI---------VDEAH 120
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
6-61 |
9.80e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 38.75 E-value: 9.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446906414 6 LSHYF-GYEtFRPGQEEI---ISKVLDHRNVLgVL--PTGGGKSICYQVPGLLL---GGTTIVIS 61
Cdd:COG1199 6 LALAFpGFE-PRPGQREMaeaVARALAEGRHL-LIeaGTGTGKTLAYLVPALLAareTGKKVVIS 68
|
|
| |
