|
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 ... |
1-588 |
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: 872.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 1 MQETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQA 80
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 81 AYLNSSLTHKQQKKIEERIKRGAIQFLYVAPERFENTFFLNLLRKIKIPLIAFDEAHCISKWGHDFRPSYQSVIQKVFTL 160
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 161 PQNFTIvALTATATAEVQQDIMSKLSIGQNDVVKTSTKRRNLIFKVNPTYQRQKFVLDYVANHEGQAGIIYCSTRKQVEE 240
Cdd:TIGR01389 161 PQVPRI-ALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 241 LHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDG 320
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 321 LKSECILLFSERDKGLHEYFITVSQADDDYKDKMGEKLTKMIQYTKTKKCLEATIVHYFEPNEnLEECNQCSNCIQENKT 400
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENE-VEPCGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 401 YDMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHGLMKNYTTSELSHLIDELRFKGYLNENDEI- 479
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIy 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 480 --LMCDTSVKQLLNNHTKVYTTPFKQKTKEK--VFINTVEGVDRALYRELVDVRKQLSDTLGIAPVSIFSDYTLEEFAKR 555
Cdd:TIGR01389 479 igLQLTEAARKVLKNEVEVLLRPFKVVAKEKtrVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEK 558
|
570 580 590
....*....|....*....|....*....|...
gi 1545705904 556 KPESKQEMIAIDGVGSYKLKHYCPKFIETIQSY 588
Cdd:TIGR01389 559 RPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-467 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 679.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 1 MQETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQA 80
Cdd:COG0514 5 ALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 81 AYLNSSLTHKQQKKIEERIKRGAIQFLYVAPERFENTFFLNLLRKIKIPLIAFDEAHCISKWGHDFRPSYQ---SVIQKv 157
Cdd:COG0514 85 AFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRrlgELRER- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 158 ftLPqNFTIVALTATATAEVQQDIMSKLSIGQNDVVKTSTKRRNLIFKVNPTYQRQK--FVLDYVANHEGQAGIIYCSTR 235
Cdd:COG0514 164 --LP-NVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKlaQLLDFLKEHPGGSGIVYCLSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 236 KQVEELHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGR 315
Cdd:COG0514 241 KKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 316 AGRDGLKSECILLFSERDKGLHEYFITVSQADDDYKDKMGEKLTKMIQYTKTKKCLEATIVHYFepNENLEE-CNQCSNC 394
Cdd:COG0514 321 AGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYF--GEELAEpCGNCDNC 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1545705904 395 IQENKTYDMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHGLMKNYTTSELSHLIDEL 467
Cdd:COG0514 399 LGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQL 471
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
2-586 |
1.15e-156 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 462.26 E-value: 1.15e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 2 QETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAA 81
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 82 YLNSSLTHKQQKKIEERIKRGAIQFLYVAPERFENTFFLNLLRKIKIPLIAFDEAHCISKWGHDFRPSYQSVIQkvftLP 161
Cdd:PRK11057 94 CLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQ----LR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 162 QNFT---IVALTATATAEVQQDIMSKLSIGQNDVVKTSTKRRN----LIFKVNPTYQrqkfVLDYVANHEGQAGIIYCST 234
Cdd:PRK11057 170 QRFPtlpFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNirytLVEKFKPLDQ----LMRYVQEQRGKSGIIYCNS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 235 RKQVEELHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAG 314
Cdd:PRK11057 246 RAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 315 RAGRDGLKSECILLFSERD-----KGLHEyfitvsQADDDYKDKMGEKLTKMIQYTKTKKCLEATIVHYFepNENLEE-C 388
Cdd:PRK11057 326 RAGRDGLPAEAMLFYDPADmawlrRCLEE------KPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYF--GEGRQEpC 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 389 NQCSNCIQENKTYDMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHGLMKNYTTSELSHLIDELR 468
Cdd:PRK11057 398 GNCDICLDPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 469 FKGYLNENdeILMcdTSVKQLLNNHTKVY------------TTPFKQKTKEKVFINTvegVDRALYRELVDVRKQLSDTL 536
Cdd:PRK11057 478 HLGLVTQN--IAQ--HSALQLTEAARPVLrgevslqlavprIVALKPRAMQKSFGGN---YDRKLFAKLRKLRKSIADEE 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1545705904 537 GIAPVSIFSDYTLEEFAKRKPESKQEMIAIDGVGSYKLKHYCPKFIETIQ 586
Cdd:PRK11057 551 NIPPYVVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIR 600
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
5-450 |
4.16e-138 |
|
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: 409.93 E-value: 4.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 5 LSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAAYLN 84
Cdd:TIGR00614 3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 85 SSLTHKQQKKIEERIKRGAIQFLYVAPERF--ENTFFLNLLRKIKIPLIAFDEAHCISKWGHDFRPSYQSVIQKVFTLPq 162
Cdd:TIGR00614 83 SAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsaSNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFP- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 163 NFTIVALTATATAEVQQDIMSKLSIGQNDVVKTSTKRRNLIFKV-----NPTYQRQKFVldyVANHEGQAGIIYCSTRKQ 237
Cdd:TIGR00614 162 NVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVrrktpKILEDLLRFI---RKEFEGKSGIIYCPSRKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 238 VEELHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAG 317
Cdd:TIGR00614 239 VEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 318 RDGLKSECILLFSERDKGLHEYFItVSQADDDYKDKMGEKLTKMIQYTKTKKCLEATIVHYFE------------PNENL 385
Cdd:TIGR00614 319 RDGLPSECHLFYAPADMNRLRRLL-MEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGekgfnksfcimgTEKCC 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1545705904 386 EECNQCSNCIQENKT---YDMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHG 450
Cdd:TIGR00614 398 DNCCKRLDYKTKDVTdkvYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYG 465
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
2-197 |
7.28e-97 |
|
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: 294.06 E-value: 7.28e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 2 QETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAA 81
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 82 YLNSSLTHKQQKKIEERIKRGAIQFLYVAPERFENTFFLNLLRKIK----IPLIAFDEAHCISKWGHDFRPSYQSvIQKV 157
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLR-LGRL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1545705904 158 FTLPQNFTIVALTATATAEVQQDIMSKLSIGQNDVVKTST 197
Cdd:cd17920 160 RRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASF 199
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
9-590 |
3.55e-95 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 316.07 E-value: 3.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 9 FGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAAYLNSSLT 88
Cdd:PLN03137 456 FGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGME 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 89 HKQQKKI--EERIKRGAIQFLYVAPER----------FENTFFLNLLRKIKIpliafDEAHCISKWGHDFRPSYQS--VI 154
Cdd:PLN03137 536 WAEQLEIlqELSSEYSKYKLLYVTPEKvaksdsllrhLENLNSRGLLARFVI-----DEAHCVSQWGHDFRPDYQGlgIL 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 155 QKVFtlpQNFTIVALTATATAEVQQDIMSKLSIGQNDVVKTSTKRRNLIFKVNPTYQR-----QKFVLDyvaNHEGQAGI 229
Cdd:PLN03137 611 KQKF---PNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKclediDKFIKE---NHFDECGI 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 230 IYCSTRKQVEELHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESY 309
Cdd:PLN03137 685 IYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGY 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 310 YQEAGRAGRDGLKSECILLFSERDKGLHEYFITVSQAD--------------DDYKDKMGEKLTKMIQYTKT----KKCL 371
Cdd:PLN03137 765 HQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEqspmamgynrmassGRILETNTENLLRMVSYCENevdcRRFL 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 372 EatIVHYFEPNENLEECNQCSNCIQeNKTY---DMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTT 448
Cdd:PLN03137 845 Q--LVHFGEKFDSTNCKKTCDNCSS-SKSLidkDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSL 921
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 449 HGLMKNYTTSELSHLIDELRFKGYLNENDEILMCDTSVKQLLN-NHTKVYT-------------TPFKQKTKEKVFINTV 514
Cdd:PLN03137 922 HGAGKHLSKGEASRILHYLVTEDILAEDVKKSDLYGSVSSLLKvNESKAYKlfsggqtiimrfpSSVKASKPSKFEATPA 1001
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 515 EG-------------------VDRALYRELVDVRKQLSDTL------GIAPVSIFSDYTLEEFAKRKPESKQEMIAIDGV 569
Cdd:PLN03137 1002 KGpltsgkqstlpmatpaqppVDLNLSAILYTALRKLRTALvkeagdGVMAYHIFGNATLQQISKRIPRTKEELLEINGL 1081
|
650 660
....*....|....*....|....*.
gi 1545705904 570 GSYKLKHYCPKFIETIQS-----YKT 590
Cdd:PLN03137 1082 GKAKVSKYGDRLLETIEStineyYKT 1107
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
3-197 |
1.46e-78 |
|
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: 246.78 E-value: 1.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 3 ETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLM----QGGTTIVISPLISLMKDQVDQLQAmGI 78
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPR-AI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 79 QAAYLNSSLTHKQQKKIEERIKRGAIQFLYVAPERFENTFFLNLLR-KIKIPLIAFDEAHCISKWGHDFRPSYQSVIQKV 157
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRqTPPISLLVVDEAHCISEWSHNFRPDYLRLCRVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1545705904 158 FTLPQNFTIVALTATATAEVQQDIMSKLSIGQNDVVKTST 197
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 ... |
2-187 |
6.21e-54 |
|
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: 182.57 E-value: 6.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 2 QETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAA 81
Cdd:cd18015 7 KDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 82 YLNSSLTHKQQKKIEERIKRGAIQF--LYVAPERF-ENTFFLNLLRKI----KIPLIAFDEAHCISKWGHDFRPSYQ--S 152
Cdd:cd18015 87 MLNASSSKEHVKWVHAALTDKNSELklLYVTPEKIaKSKRFMSKLEKAynagRLARIAIDEVHCCSQWGHDFRPDYKklG 166
|
170 180 190
....*....|....*....|....*....|....*
gi 1545705904 153 VIQKVFtlpQNFTIVALTATATAEVQQDIMSKLSI 187
Cdd:cd18015 167 ILKRQF---PNVPILGLTATATSKVLKDVQKILCI 198
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
5-196 |
6.64e-53 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 179.20 E-value: 6.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 5 LSHYFGYKSFRPGQEEIITKIL-NHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAAYL 83
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 84 NSSlthkQQKKIEERIKRGAIQFLYVAPERFENTffLNLLRKIK--IPLIAFDEAHCISKWGHDFRPSYQ--SVIQKVft 159
Cdd:cd18017 84 GSA----QSQNVLDDIKMGKIRVIYVTPEFVSKG--LELLQQLRngITLIAIDEAHCVSQWGHDFRSSYRhlGSIRNR-- 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1545705904 160 LPqNFTIVALTATATAEVQQDIMSKLSIGQNDVVKTS 196
Cdd:cd18017 156 LP-NVPIVALTATATPSVRDDIIKNLNLRNPQITCTS 191
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
199-329 |
4.31e-51 |
|
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: 172.01 E-value: 4.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 199 RRNLIFKV---NPTYQRQKFVLDYVANHEGQAGIIYCSTRKQVEELHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDR 275
Cdd:cd18794 1 RPNLFYSVrpkDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1545705904 276 VEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLF 329
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
1-187 |
2.51e-48 |
|
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: 167.31 E-value: 2.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 1 MQETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQA 80
Cdd:cd18016 5 MMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 81 AYLNSSLTHKQQKKIEERIKRG--AIQFLYVAPE------RFENTFFlNLLRKIKIPLIAFDEAHCISKWGHDFRPSYQ- 151
Cdd:cd18016 85 TYLTGDKTDAEATKIYLQLSKKdpIIKLLYVTPEkisasnRLISTLE-NLYERKLLARFVIDEAHCVSQWGHDFRPDYKr 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1545705904 152 -SVIQKVFtlpQNFTIVALTATATAEVQQDIMSKLSI 187
Cdd:cd18016 164 lNMLRQKF---PSVPMMALTATATPRVQKDILNQLKM 197
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
2-190 |
1.18e-46 |
|
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: 163.03 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 2 QETLSHYFGYKSFR-PGQEEIITKILN-HQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQ 79
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKgNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 80 AAYLNSSLTHKQQKKIEERIKRGA--IQFLYVAPERFENTFFL----NLLRKIKIPLIAFDEAHCISKWGHDFRPSYQSv 153
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEKpqTKFLYITPEMAATSSFQpllsSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLR- 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1545705904 154 IQKVFTLPQNFTIVALTATATAEVQQDIMSKLSIGQN 190
Cdd:cd18014 160 LGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| DpdF |
NF041063 |
protein DpdF; |
5-333 |
4.23e-40 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 156.23 E-value: 4.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 5 LSHYFGYKSFR-PGQEEII----------TKILNhqhtlgvLPTGGGKSICYQVPGLM---QGGTTIVISPLISLMKDQV 70
Cdd:NF041063 131 LAEALGFTHYRsPGQREAVraallappgsTLIVN-------LPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 71 DQLQAMGIQA--------AYlNSSLTHKQQKKIEERIKRGAIQFLYVAPE------RFenTFF----LNLLRkikipLIA 132
Cdd:NF041063 204 RRARELLRRAgpdlggplAW-HGGLSAEERAAIRQRIRDGTQRILFTSPEsltgslRP--ALFdaaeAGLLR-----YLV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 133 FDEAHCISKWGHDFRPSYQSV---IQKVFTL---PQNFTIVALTATATAEvQQDIMSKL--SIGQNDVVKTSTKRRNLIF 204
Cdd:NF041063 276 VDEAHLVDQWGDGFRPEFQLLaglRRSLLRLapsGRPFRTLLLSATLTES-TLDTLETLfgPPGPFIVVSAVQLRPEPAY 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 205 KVNPT---YQRQKFVLDYVANhegqAG---IIYCSTRKQVEELHEALNSEKIKS-TIYHAGLTNKER---IEAQNDflyD 274
Cdd:NF041063 355 WVAKCdseEERRERVLEALRH----LPrplILYVTKVEDAEAWLQRLRAAGFRRvALFHGDTPDAERerlIEQWRE---N 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1545705904 275 RVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLFSERD 333
Cdd:NF041063 428 ELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDD 486
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
15-179 |
7.77e-28 |
|
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: 109.64 E-value: 7.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 15 RPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGL------MQGGTTIVISPLISLMKDQVDQLQAMGIQAAY-LNSSL 87
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 88 THKQQKKIEERIKRgaIQFLYVAPERFENTFFL-NLLRKIKipLIAFDEAHCISKWGhdFRPSYQSVIQKvftLPQNFTI 166
Cdd:pfam00270 81 GGDSRKEQLEKLKG--PDILVGTPGRLLDLLQErKLLKNLK--LLVLDEAHRLLDMG--FGPDLEEILRR---LPKKRQI 151
|
170
....*....|...
gi 1545705904 167 VALTATATAEVQQ 179
Cdd:pfam00270 152 LLLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
7-202 |
3.54e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 100.26 E-value: 3.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 7 HYFGYKSFRPGQEEIITKIL-NHQHTLGVLPTGGGKSICYQVPGLMQ-----GGTTIVISPLISLMKDQVDQLQAMGIQA 80
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLsGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 81 AYLNSSLTH-KQQKKIEERIKRGAIQFLYVAPERFENTFFLNLLRKIKIPLIAFDEAHCISKWGHdfrpsYQSVIQKVFT 159
Cdd:smart00487 82 GLKVVGLYGgDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGF-----GDQLEKLLKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1545705904 160 LPQNFTIVALTATATAEVQQDimskLSIGQNDVVKTSTKRRNL 202
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENL----LELFLNDPVFIDVGFTPL 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
214-320 |
4.11e-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: 97.28 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 214 KFVLDYVANHEGQAGIIYCSTRKQVEElHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSN 293
Cdd:pfam00271 4 EALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
|
90 100
....*....|....*....|....*..
gi 1545705904 294 VRYVIHYNMPGDLESYYQEAGRAGRDG 320
Cdd:pfam00271 83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
239-320 |
1.83e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 94.20 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 239 EELHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGR 318
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1545705904 319 DG 320
Cdd:smart00490 81 AG 82
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
402-490 |
2.44e-21 |
|
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: 88.69 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 402 DMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHGLMKNYTTSELSHLIDELRFKGYLNENDE--- 478
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGryp 80
|
90
....*....|..
gi 1545705904 479 ILMCDTSVKQLL 490
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
200-329 |
8.18e-21 |
|
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: 88.33 E-value: 8.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 200 RNLIFKVNPTYQRQKFVLDYVANHEGQAGIIYCSTRKQVEELHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVV 279
Cdd:cd18787 2 KQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1545705904 280 IATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLF 329
Cdd:cd18787 82 VATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
203-336 |
8.54e-18 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 85.97 E-value: 8.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 203 IFKVNPtYQRQKFVLDYVANHEGQAGIIYCSTRKQVEELHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIAT 282
Cdd:COG0513 220 YYLVDK-RDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVAT 298
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1545705904 283 NAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLFSERDKGL 336
Cdd:COG0513 299 DVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRL 352
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
399-497 |
1.25e-17 |
|
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: 78.73 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 399 KTYDMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHGLMKNYTTSELSHLIDELRFKGYLNENDE 478
Cdd:pfam09382 3 ETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDIE 82
|
90 100
....*....|....*....|..
gi 1545705904 479 ---ILMCDTSVKQLLNNHTKVY 497
Cdd:pfam09382 83 fysVLKLTPKAREVLKGEEKVM 104
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
15-316 |
1.56e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 85.85 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 15 RPGQEEIITKIL-----NHQHTLGVLPTGGGKSI----CYQvpGLMQGGTTIVISPLISLMKDQVDQLQAmgiqaaYLNS 85
Cdd:COG1061 82 RPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRR------FLGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 86 SLTHKQQKKIEERIKRGAIQFLYVAP--ERFENTFflnllrkikiPLIAFDEAHciskwgHDFRPSYQSVIQKvftLPQN 163
Cdd:COG1061 154 PLAGGGKKDSDAPITVATYQSLARRAhlDELGDRF----------GLVIIDEAH------HAGAPSYRRILEA---FPAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 164 FtIVALTAT---------------------ATAEVQQD----------IMSKLSIGQNDVVKTSTKRRNLIFKVNPtyqR 212
Cdd:COG1061 215 Y-RLGLTATpfrsdgreillflfdgivyeySLKEAIEDgylappeyygIRVDLTDERAEYDALSERLREALAADAE---R 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 213 QKFVLDYVANHEGQ--AGIIYCSTRKQVEELHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGID 290
Cdd:COG1061 291 KDKILRELLREHPDdrKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVD 370
|
330 340
....*....|....*....|....*..
gi 1545705904 291 KSNVRYVIhYNMP-GDLESYYQEAGRA 316
Cdd:COG1061 371 VPRLDVAI-LLRPtGSPREFIQRLGRG 396
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
518-585 |
2.24e-17 |
|
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: 76.42 E-value: 2.24e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1545705904 518 DRALYRELVDVRKQLSDTLGIAPVSIFSDYTLEEFAKRKPESKQEMIAIDGVGSYKLKHYCPKFIETI 585
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
10-346 |
2.25e-16 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 82.14 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 10 GYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLM-------------QGGTTIVISPLISLMKdQVDQlqam 76
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctirsghpseqRNPLAMVLTPTRELCV-QVED---- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 77 giQAAYLNSSLTHK-----------QQKkieERIKRGaIQFLYVAPERFentffLNLLRKIKIPL-----IAFDEAHCIS 140
Cdd:PLN00206 215 --QAKVLGKGLPFKtalvvggdampQQL---YRIQQG-VELIVGTPGRL-----IDLLSKHDIELdnvsvLVLDEVDCML 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 141 KWGhdFRpsyQSVIQKVFTLPQNfTIVALTATATAEVQ-------QDIMSkLSIGQNDVVKTSTKRrnLIFKVNPTYQRQ 213
Cdd:PLN00206 284 ERG--FR---DQVMQIFQALSQP-QVLLFSATVSPEVEkfasslaKDIIL-ISIGNPNRPNKAVKQ--LAIWVETKQKKQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 214 K-FVLDYVANHEGQAGIIYCSTRKQVEELHEALN-SEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDK 291
Cdd:PLN00206 355 KlFDILKSKQHFKPPAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1545705904 292 SNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLFSERDKGLHEYFITVSQA 346
Cdd:PLN00206 435 LRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKS 489
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
229-328 |
2.36e-15 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 73.45 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 229 IIYCSTRKQVEEL---------HEALNSEKIKStiYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIH 299
Cdd:cd18797 39 IVFCRSRKLAELLlrylkarlvEEGPLASKVAS--YRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
|
90 100
....*....|....*....|....*....
gi 1545705904 300 YNMPGDLESYYQEAGRAGRDGLKSECILL 328
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
18-320 |
1.81e-14 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 76.80 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 18 QEEIITKILNHQHTLGVLPTGGGKSICYQVP---GLMQ--GGTTIVISPLISLMKDQVDQLQAMgiqAAYLNSSL----- 87
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPvleALLEdpGATALYLYPTKALARDQLRRLREL---AEALGLGVrvaty 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 88 ---THKQQKKieeRIKRGA-----------IQFLYVaperfeNTFFLNLLRKIKipLIAFDEAHciskwghdfrpSYQSV 153
Cdd:COG1205 138 dgdTPPEERR---WIREHPdivltnpdmlhYGLLPH------HTRWARFFRNLR--YVVIDEAH-----------TYRGV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 154 ---------------IQKVFTLPQnftIVALTAT-----ATAEvqqdimsKLsIGQN-DVVKTSTK---RRNLIFkVNP- 208
Cdd:COG1205 196 fgshvanvlrrlrriCRHYGSDPQ---FILASATignpaEHAE-------RL-TGRPvTVVDEDGSprgERTFVL-WNPp 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 209 ---TYQRQ-------KFVLDYVANheGQAGIIYCSTRKQVE----ELHEALNSEKIKSTI--YHAGLTNKERIEAQNDFL 272
Cdd:COG1205 264 lvdDGIRRsalaeaaRLLADLVRE--GLRTLVFTRSRRGAEllarYARRALREPDLADRVaaYRAGYLPEERREIERGLR 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1545705904 273 YDRVEVVIATNAFGMGIDKSNVRYVI--HYnmPGDLESYYQEAGRAGRDG 320
Cdd:COG1205 342 SGELLGVVSTNALELGIDIGGLDAVVlaGY--PGTRASFWQQAGRAGRRG 389
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
517-592 |
2.55e-14 |
|
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: 68.09 E-value: 2.55e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1545705904 517 VDRALYRELVDVRKQLSDTLGIAPVSIFSDYTLEEFAKRKPESKQEMIAIDGVGSYKLKHYCPKFIETIQSYKTSI 592
Cdd:smart00341 3 RQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDSP 78
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
30-172 |
3.29e-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: 70.12 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 30 HTLGVLPTGGGKSICYQVP----GLMQGGTTIVISPLISLMKDQ---VDQLQAMGIQAAYLNSSLThkqqKKIEERIKRG 102
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAalllLLKKGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSS----AEEREKNKLG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1545705904 103 AIQFLYVAPERFENTFFLNLLRKIK-IPLIAFDEAHCISKWGHDFRPSYQSVIQKVFTLPQnftIVALTAT 172
Cdd:cd00046 79 DADIIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQ---VILLSAT 146
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
262-328 |
1.79e-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: 57.33 E-value: 1.79e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1545705904 262 KERIEAQNDfLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDG-LKSECILL 328
Cdd:cd18785 10 TNSIEHAEE-IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
229-334 |
2.42e-10 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 62.54 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 229 IIYCSTRKQVEELHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLES 308
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100
....*....|....*....|....*.
gi 1545705904 309 YYQEAGRAGRDGLKSECILLFSERDK 334
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDI 376
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
332-394 |
4.17e-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: 55.76 E-value: 4.17e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1545705904 332 RDKGLHEYFITVSQADDDYKDKMGEKLTKMIQY-TKTKKCLEATIVHYFEPNENLEECNQCSNC 394
Cdd:pfam16124 2 QDVVRLRFLIEQSEADEERKEVELQKLQAMVAYcENTTDCRRKQLLRYFGEEFDSEPCGNCDNC 65
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
161-334 |
5.98e-10 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 62.10 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 161 PQNFTIVALTATATAEVQQDIMsklsigqndVVKTSTKRRNLifkvnptyqrqKFVLDYVANHEGQAgIIYCSTRKQVEE 240
Cdd:PTZ00110 334 PVHVNVGSLDLTACHNIKQEVF---------VVEEHEKRGKL-----------KMLLQRIMRDGDKI-LIFVETKKGADF 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 241 LHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDG 320
Cdd:PTZ00110 393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
|
170
....*....|....
gi 1545705904 321 LKSeCILLFSERDK 334
Cdd:PTZ00110 473 AKG-ASYTFLTPDK 485
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
229-328 |
2.89e-08 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 53.33 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 229 IIYCSTRKQVEELheALNSEKIKstIYHAGLTNKER--IEaqNDFLYDRVEVVIATNAFGMGID--------KSNVRYVI 298
Cdd:cd18795 47 LVFCSSRKECEKT--AKDLAGIA--FHHAGLTREDRelVE--ELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDG 120
|
90 100 110
....*....|....*....|....*....|..
gi 1545705904 299 HYNMPGDLESYYQEAGRAGRDGL--KSECILL 328
Cdd:cd18795 121 KGYRELSPLEYLQMIGRAGRPGFdtRGEAIIM 152
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
10-336 |
2.90e-08 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 56.78 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 10 GYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGL------MQGGTTIVISPLISLmkdQVDQLQAMGIQAAYL 83
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTREL---AVQVAEAMTDFSKHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 84 NS----SLTHKQQKKIEERIKRGAIQFLYVAPERFENTFFLNLLRKIKIPLIAFDEAHCISKWGhdFRPSYQSVIQKVft 159
Cdd:PRK11634 102 RGvnvvALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG--FIEDVETIMAQI-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 160 lPQNFTIVALTATATAEVQQDIMSKLSIGQNDVVKTSTKRRNLIFKVNPT---YQRQKFVLDYVANHEGQAGIIYCSTRK 236
Cdd:PRK11634 178 -PEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTvwgMRKNEALVRFLEAEDFDAAIIFVRTKN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 237 QVEELHEALNSEKIKSTIYHaGLTNKERIEAQNDFLYD-RVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGR 315
Cdd:PRK11634 257 ATLEVAEALERNGYNSAALN-GDMNQALREQTLERLKDgRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGR 335
|
330 340
....*....|....*....|.
gi 1545705904 316 AGRDGLKSECILLFSERDKGL 336
Cdd:PRK11634 336 TGRAGRAGRALLFVENRERRL 356
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
12-172 |
1.09e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 51.52 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 12 KSFRPGQEEIITKILN-----HQHTLGVLPTGGGKS-----ICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAA 81
Cdd:pfam04851 2 LELRPYQIEAIENLLEsikngQKRGLIVMATGSGKTltaakLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 82 YLNSSLT--HKQQKKIEERIKRGAIQFLYVAPERFENTFFLNllrkiKIPLIAFDEAHciskwgHDFRPSYQSVIQKVft 159
Cdd:pfam04851 82 EIGEIISgdKKDESVDDNKIVVTTIQSLYKALELASLELLPD-----FFDVIIIDEAH------RSGASSYRNILEYF-- 148
|
170
....*....|...
gi 1545705904 160 lpQNFTIVALTAT 172
Cdd:pfam04851 149 --KPAFLLGLTAT 159
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
214-333 |
1.76e-07 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 53.76 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 214 KFVLDYVANHEGQAGIIYCSTRKQVEELHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSN 293
Cdd:PRK01297 324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1545705904 294 VRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLFSERD 333
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
13-173 |
6.73e-07 |
|
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: 49.95 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 13 SFRPGQEEIITKILNHQHTLGV-LPTGGGKSICYQ---VPGLMQGGTTIV-ISPLISL----MKDQVDQLQAMGIQAAYL 83
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVsAPTSSGKTLIAElaiLRALATSGGKAVyIAPTRALvnqkEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 84 NSSLTHKQQKKIEERIkrgaiqflYVA-PERFENtfflnLLRK------IKIPLIAFDEAHCIskwGHDFR-PSYQSVIQ 155
Cdd:cd17921 81 TGDPSVNKLLLAEADI--------LVAtPEKLDL-----LLRNggerliQDVRLVVVDEAHLI---GDGERgVVLELLLS 144
|
170
....*....|....*...
gi 1545705904 156 KVFTLPQNFTIVALTATA 173
Cdd:cd17921 145 RLLRINKNARFVGLSATL 162
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
226-328 |
5.80e-06 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 49.04 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 226 QAGIIYCSTRKQVEELHEALNSEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGD 305
Cdd:PRK10590 246 QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNV 325
|
90 100
....*....|....*....|...
gi 1545705904 306 LESYYQEAGRAGRDGLKSECILL 328
Cdd:PRK10590 326 PEDYVHRIGRTGRAAATGEALSL 348
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
223-318 |
1.20e-05 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 48.35 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 223 HEGQAgIIYCSTRKQVEELHEALNsekIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFG---------------- 286
Cdd:COG1202 426 YRGQT-IIFTNSRRRCHEIARALG---YKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAagvdfpasqvifdsla 501
|
90 100 110
....*....|....*....|....*....|..
gi 1545705904 287 MGIDKSNVRyvihynmpgdleSYYQEAGRAGR 318
Cdd:COG1202 502 MGIEWLSVQ------------EFHQMLGRAGR 521
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
18-73 |
2.26e-05 |
|
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: 45.27 E-value: 2.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1545705904 18 QEEIITKILNHQHTLGVLPTGGGKSICYQVP---GLMQ--GGTTIVISPLISLMKDQVDQL 73
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRdpGSRALYLYPTKALAQDQLRSL 65
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
229-387 |
4.65e-05 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 46.26 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 229 IIYCSTRKQVEELHEALNSEKIKSTIY--------HAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHY 300
Cdd:COG1111 357 IVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskegDKGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 301 -NMPGDLESyYQEAGRAGRDGLKSECILLFSE-RDkglhEYFITVSQADDDYKDKMGEKLTKMIQY---TKTKKCLEATI 375
Cdd:COG1111 437 ePVPSEIRS-IQRKGRTGRKREGRVVVLIAKGtRD----EAYYWSSRRKEKKMKSILKKLKKLLDKqekEKLKESAQATL 511
|
170
....*....|..
gi 1545705904 376 VHYFEPNENLEE 387
Cdd:COG1111 512 DEFESIKELAED 523
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
229-318 |
1.77e-04 |
|
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: 42.25 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 229 IIYCSTRKQVEELHEALNS----EKIKSTIY-HAGLTNKE-RIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNM 302
Cdd:cd18796 42 LVFTNTRSQAERLAQRLRElcpdRVPPDFIAlHHGSLSRElREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90
....*....|....*.
gi 1545705904 303 PGDLESYYQEAGRAGR 318
Cdd:cd18796 122 PKSVARLLQRLGRSGH 137
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
13-192 |
2.10e-04 |
|
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: 42.31 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 13 SFRPGQEEIITKILnHQHTLGVLPTGGGKSICYQVpgLMQG-------GTTIVISPLISLMKDQVDQ-LQAMGI---QAA 81
Cdd:cd18033 2 PLRDYQFTIVQKAL-FQNTLVALPTGLGKTFIAAV--VMLNyyrwfpkGKIVFMAPTKPLVSQQIEAcYKITGIpssQTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 82 YLNSSlTHKQQKKIEERIKRgaiqFLYVAPERFENtfflNLLRKIK----IPLIAFDEAHCISKwghdfRPSYQSVIQKV 157
Cdd:cd18033 79 ELTGS-VPPTKRAELWASKR----VFFLTPQTLEN----DLKEGDCdpksIVCLVIDEAHRATG-----NYAYCQVVREL 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 1545705904 158 FTLPQNFTIVALTAT---ATAEVQQdIMSKLSIGQNDV 192
Cdd:cd18033 145 MRYNSHFRILALTATpgsKLEAVQQ-VIDNLLISHIEI 181
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
229-438 |
2.61e-04 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 44.09 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 229 IIYCSTRKQVEELHEALNSEKIK--------STIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHY 300
Cdd:PRK13766 369 IVFTQYRDTAEKIVDLLEKEGIKavrfvgqaSKDGDKGMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFY 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 301 N-MPGDLESyYQEAGRAGRDGlKSECILLFSE--RDKGlheYFItVSQADD--------DYKDKMGEKLTKMIQYTKTK- 368
Cdd:PRK13766 449 EpVPSEIRS-IQRKGRTGRQE-EGRVVVLIAKgtRDEA---YYW-SSRRKEkkmkeelkNLKGILNKKLQELDEEQKGEe 522
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1545705904 369 --KCLEATIVHYFEPNENLEECNQCSNCIQENKTYDMTREAKMII------SCIARMKQQESYSVIIQVLrgEVTDYI 438
Cdd:PRK13766 523 eeKDEQLSLDDFVKSKGKEEEEEEEKEEKDKETEEDEPEGPKIIVdsrelrSNVARHLKRLGAEVELKTL--EVGDYV 598
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
12-172 |
5.63e-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: 41.65 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 12 KSFRPGQEEIITKILNHQHTLGVLPTGGGKS-----IC----YQVPGlMQGGTTIVISPLISLMKDQVDQLQAMGIQAAY 82
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPA-GRKGKVVFLANKVPLVEQQKEVFRKHFERPGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 83 LNSSLTHKQQKKI--EERIKRGAIqfLYVAPERFENTFF-LNLLRKIKIPLIAFDEAHCISKwGHDFRP---SYQSviQK 156
Cdd:cd17927 80 KVTGLSGDTSENVsvEQIVESSDV--IIVTPQILVNDLKsGTIVSLSDFSLLVFDECHNTTK-NHPYNEimfRYLD--QK 154
|
170
....*....|....*.
gi 1545705904 157 VFTLPQNFTIVALTAT 172
Cdd:cd17927 155 LGSSGPLPQILGLTAS 170
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
14-137 |
9.84e-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: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 14 FRPGQEEIITKILNHQHTLG---VLPTGGGKS------ICYqvpgLMQgGTTIVISPLISLMKDQVDQLQAMGIQAA-YL 83
Cdd:cd17926 1 LRPYQEEALEAWLAHKNNRRgilVLPTGSGKTltalalIAY----LKE-LRTLIVVPTDALLDQWKERFEDFLGDSSiGL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1545705904 84 NSSLTHKQQKKIEERIKRGAIQFLYVAPERFENTFFLnllrkikipLIAFDEAH 137
Cdd:cd17926 76 IGGGKKKDFDDANVVVATYQSLSNLAEEEKDLFDQFG---------LLIVDEAH 120
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
229-326 |
2.66e-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: 38.23 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 229 IIYCSTRKQVEELHEALNSEKIKSTIYHAGLTNKERIEAQNDF---LYDRVeVVIATNAFGMGIDKSNVRYVIHY----N 301
Cdd:cd18793 31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnedPDIRV-FLLSTKAGGVGLNLTAANRVILYdpwwN 109
|
90 100
....*....|....*....|....*
gi 1545705904 302 mPGDLEsyyQEAGRAGRDGLKSECI 326
Cdd:cd18793 110 -PAVEE---QAIDRAHRIGQKKPVV 130
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
18-320 |
3.72e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 40.25 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 18 QEEIITKILNHQHTLGVLPTGGGKS-ICYQV--PGLMQGGTTIVISPLISLMKDQVDQLqaMGIQAAYLNSSLTHKQQKK 94
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTlIAYSAiyETFLAGLKSIYIVPLRSLAMEKYEEL--SRLRSLGMRVKISIGDYDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 95 IEERIKRGAIqfLYVAPERFENTFFLNLLRKIKIPLIAFDEAHCIskwGHDFR-PSYQSVIQKVFTLPQNFTIVALTATA 173
Cdd:PRK01172 105 PPDFIKRYDV--VILTSEKADSLIHHDPYIINDVGLIVADEIHII---GDEDRgPTLETVLSSARYVNPDARILALSATV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 174 TaevqqDIMSKLSIGQNDVVKTSTkrRNLIFKVNPTYQRQKFVLDY-------------VANHEGQAgIIYCSTRKQVEE 240
Cdd:PRK01172 180 S-----NANELAQWLNASLIKSNF--RPVPLKLGILYRKRLILDGYersqvdinslikeTVNDGGQV-LVFVSSRKNAED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 241 LHEAL-------NSEKIKS------------------TIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSnVR 295
Cdd:PRK01172 252 YAEMLiqhfpefNDFKVSSennnvyddslnemlphgvAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP-AR 330
|
330 340 350
....*....|....*....|....*....|....
gi 1545705904 296 YVIHYNMP--GDLESYY-------QEAGRAGRDG 320
Cdd:PRK01172 331 LVIVRDITryGNGGIRYlsnmeikQMIGRAGRPG 364
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
257-328 |
4.29e-03 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 37.96 E-value: 4.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1545705904 257 AGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGlkSECILL 328
Cdd:cd18802 72 SLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYILM 141
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
5-60 |
5.94e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 39.52 E-value: 5.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1545705904 5 LSHYFGYKSFRPGQEEIITKI---LNHQHTLgVL--PTGGGKSICYQVPGL---MQGGTTIVIS 60
Cdd:COG1199 6 LALAFPGFEPRPGQREMAEAVaraLAEGRHL-LIeaGTGTGKTLAYLVPALlaaRETGKKVVIS 68
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
18-105 |
6.25e-03 |
|
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: 37.96 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545705904 18 QEEIITKILN-----HQHTL-GVlpTGGGKSICY-----QVpgLMQGGTTIVISPLISLMKDQVDQLQA-MGIQAAYLNS 85
Cdd:cd17929 1 QRKAYEAIVSslggfKTFLLhGV--TGSGKTEVYielieKV--LAKGKQVLVLVPEISLTPQLIKRFKKrFGDKVAVLHS 76
|
90 100
....*....|....*....|
gi 1545705904 86 SLTHKQQKKIEERIKRGAIQ 105
Cdd:cd17929 77 KLSDKERADEWRKIKRGEAK 96
|
|
| |
