|
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: 868.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 2 MQETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQA 81
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 82 AYLNSSLTHKQQKEIEEQIKRGAIQFLYVAPERFENTFFLNLLRKIEIPLIAFDEAHCISKWGHDFRPSYQSVIQKVFTL 161
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 162 PQNFTIvALTATATAEVQQDIMSKLSIGQNDVVKTSTKRRNLIFKVNPTYQRQKFVVDYVANHEGQAGIIYCSTRKQVEE 241
Cdd:TIGR01389 161 PQVPRI-ALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 242 LHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDG 321
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 322 LKSECILLFSERDKGLHEYFITVSQADDDYKDKMGEKLTKMIQYTKTKKCLEATIVHYFEPNEnLEECNQCSNCIQENKT 401
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENE-VEPCGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 402 YDMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHGLMKNYTTSELSHLIDELRFKGYLNENDEI- 480
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIy 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 481 --LMCDTSVKQLLNNHTKVYTTPFKQKTKEK--VFINTVEGVDRALYRELVDVRKQLSDKLGIAPVSIFSDYTLEEFAKR 556
Cdd:TIGR01389 479 igLQLTEAARKVLKNEVEVLLRPFKVVAKEKtrVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEK 558
|
570 580 590
....*....|....*....|....*....|...
gi 1279652141 557 KPESKQEMIAIDGVGSYKLKHYCPKFIETIQSY 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: 678.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 2 MQETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQA 81
Cdd:COG0514 5 ALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 82 AYLNSSLTHKQQKEIEEQIKRGAIQFLYVAPERFENTFFLNLLRKIEIPLIAFDEAHCISKWGHDFRPSYQ---SVIQKv 158
Cdd:COG0514 85 AFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRrlgELRER- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 159 ftLPqNFTIVALTATATAEVQQDIMSKLSIGQNDVVKTSTKRRNLIFKVNPTYQRQK--FVVDYVANHEGQAGIIYCSTR 236
Cdd:COG0514 164 --LP-NVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKlaQLLDFLKEHPGGSGIVYCLSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 237 KQVEELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGR 316
Cdd:COG0514 241 KKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 317 AGRDGLKSECILLFSERDKGLHEYFITVSQADDDYKDKMGEKLTKMIQYTKTKKCLEATIVHYFepNENLEE-CNQCSNC 395
Cdd:COG0514 321 AGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYF--GEELAEpCGNCDNC 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279652141 396 IQENKTYDMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHGLMKNYTTSELSHLIDEL 468
Cdd:COG0514 399 LGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQL 471
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
3-587 |
1.79e-156 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 461.88 E-value: 1.79e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 3 QETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAA 82
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 83 YLNSSLTHKQQKEIEEQIKRGAIQFLYVAPERFENTFFLNLLRKIEIPLIAFDEAHCISKWGHDFRPSYQSVIQkvftLP 162
Cdd:PRK11057 94 CLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQ----LR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 163 QNFT---IVALTATATAEVQQDIMSKLSIGQNDVVKTSTKRRN----LIFKVNPTYQrqkfVVDYVANHEGQAGIIYCST 235
Cdd:PRK11057 170 QRFPtlpFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNirytLVEKFKPLDQ----LMRYVQEQRGKSGIIYCNS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 236 RKQVEELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAG 315
Cdd:PRK11057 246 RAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 316 RAGRDGLKSECILLFSERD-----KGLHEyfitvsQADDDYKDKMGEKLTKMIQYTKTKKCLEATIVHYFepNENLEE-C 389
Cdd:PRK11057 326 RAGRDGLPAEAMLFYDPADmawlrRCLEE------KPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYF--GEGRQEpC 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 390 NQCSNCIQENKTYDMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHGLMKNYTTSELSHLIDELR 469
Cdd:PRK11057 398 GNCDICLDPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 470 FKGYLNENdeILMcdTSVKQLLNNHTKVY------------TTPFKQKTKEKVFINTvegVDRALYRELVDVRKQLSDKL 537
Cdd:PRK11057 478 HLGLVTQN--IAQ--HSALQLTEAARPVLrgevslqlavprIVALKPRAMQKSFGGN---YDRKLFAKLRKLRKSIADEE 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1279652141 538 GIAPVSIFSDYTLEEFAKRKPESKQEMIAIDGVGSYKLKHYCPKFIETIQ 587
Cdd:PRK11057 551 NIPPYVVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIR 600
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
6-451 |
6.26e-139 |
|
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: 411.86 E-value: 6.26e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 6 LSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAAYLN 85
Cdd:TIGR00614 3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 86 SSLTHKQQKEIEEQIKRGAIQFLYVAPERF--ENTFFLNLLRKIEIPLIAFDEAHCISKWGHDFRPSYQSVIQKVFTLPq 163
Cdd:TIGR00614 83 SAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsaSNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFP- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 164 NFTIVALTATATAEVQQDIMSKLSIGQNDVVKTSTKRRNLIFKV-----NPTYQRQKFVVdyvANHEGQAGIIYCSTRKQ 238
Cdd:TIGR00614 162 NVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVrrktpKILEDLLRFIR---KEFEGKSGIIYCPSRKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 239 VEELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAG 318
Cdd:TIGR00614 239 VEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 319 RDGLKSECILLFSERDKGLHEYFItVSQADDDYKDKMGEKLTKMIQYTKTKKCLEATIVHYFE------------PNENL 386
Cdd:TIGR00614 319 RDGLPSECHLFYAPADMNRLRRLL-MEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGekgfnksfcimgTEKCC 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279652141 387 EECNQCSNCIQENKT---YDMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHG 451
Cdd:TIGR00614 398 DNCCKRLDYKTKDVTdkvYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYG 465
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
10-591 |
1.74e-96 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 319.53 E-value: 1.74e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 10 FGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAAYLNSSLT 89
Cdd:PLN03137 456 FGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGME 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 90 HKQQKEIEEQIKRGAIQF--LYVAPERFENTffLNLLRKIEI-------PLIAFDEAHCISKWGHDFRPSYQS--VIQKV 158
Cdd:PLN03137 536 WAEQLEILQELSSEYSKYklLYVTPEKVAKS--DSLLRHLENlnsrgllARFVIDEAHCVSQWGHDFRPDYQGlgILKQK 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 159 FtlpQNFTIVALTATATAEVQQDIMSKLSIGQNDVVKTSTKRRNLIFKVNPTYQR-----QKFVVDyvaNHEGQAGIIYC 233
Cdd:PLN03137 614 F---PNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKclediDKFIKE---NHFDECGIIYC 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 234 STRKQVEELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQE 313
Cdd:PLN03137 688 LSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQE 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 314 AGRAGRDGLKSECILLFSERDKGLHEYFITVSQAD--------------DDYKDKMGEKLTKMIQYTKT----KKCLEat 375
Cdd:PLN03137 768 CGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEqspmamgynrmassGRILETNTENLLRMVSYCENevdcRRFLQ-- 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 376 IVHYFEPNENLEECNQCSNCIQeNKTY---DMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHGL 452
Cdd:PLN03137 846 LVHFGEKFDSTNCKKTCDNCSS-SKSLidkDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGA 924
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 453 MKNYTTSELSHLIDELRFKGYLNENDEILMCDTSVKQLLN-NHTKVYT-------------TPFKQKTKEKVFINTVEG- 517
Cdd:PLN03137 925 GKHLSKGEASRILHYLVTEDILAEDVKKSDLYGSVSSLLKvNESKAYKlfsggqtiimrfpSSVKASKPSKFEATPAKGp 1004
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 518 ------------------VDRALYRELVDVRKQLSDKL------GIAPVSIFSDYTLEEFAKRKPESKQEMIAIDGVGSY 573
Cdd:PLN03137 1005 ltsgkqstlpmatpaqppVDLNLSAILYTALRKLRTALvkeagdGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKA 1084
|
650 660
....*....|....*....|...
gi 1279652141 574 KLKHYCPKFIETIQS-----YKT 591
Cdd:PLN03137 1085 KVSKYGDRLLETIEStineyYKT 1107
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
3-198 |
2.78e-96 |
|
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: 292.52 E-value: 2.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 3 QETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAA 82
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 83 YLNSSLTHKQQKEIEEQIKRGAIQFLYVAPERFENTFFLNLLRKI----EIPLIAFDEAHCISKWGHDFRPSYQSvIQKV 158
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLperkRLALIVVDEAHCVSQWGHDFRPDYLR-LGRL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1279652141 159 FTLPQNFTIVALTATATAEVQQDIMSKLSIGQNDVVKTST 198
Cdd:cd17920 160 RRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASF 199
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
4-198 |
1.11e-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: 247.17 E-value: 1.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 4 ETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLM----QGGTTIVISPLISLMKDQVDQLQAmGI 79
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPR-AI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 80 QAAYLNSSLTHKQQKEIEEQIKRGAIQFLYVAPERFENTFFLNLLR-KIEIPLIAFDEAHCISKWGHDFRPSYQSVIQKV 158
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRqTPPISLLVVDEAHCISEWSHNFRPDYLRLCRVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1279652141 159 FTLPQNFTIVALTATATAEVQQDIMSKLSIGQNDVVKTST 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 |
3.24e-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: 183.34 E-value: 3.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 3 QETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAA 82
Cdd:cd18015 7 KDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 83 YLNSSLTHKQQKEIEEQIKRGAIQF--LYVAPERF-ENTFFLNLLRKIE----IPLIAFDEAHCISKWGHDFRPSYQ--S 153
Cdd:cd18015 87 MLNASSSKEHVKWVHAALTDKNSELklLYVTPEKIaKSKRFMSKLEKAYnagrLARIAIDEVHCCSQWGHDFRPDYKklG 166
|
170 180 190
....*....|....*....|....*....|....*
gi 1279652141 154 VIQKVFtlpQNFTIVALTATATAEVQQDIMSKLSI 188
Cdd:cd18015 167 ILKRQF---PNVPILGLTATATSKVLKDVQKILCI 198
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
6-197 |
5.09e-54 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 182.28 E-value: 5.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 6 LSHYFGYKSFRPGQEEIITKIL-NHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAAYL 84
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 85 NSSlthkQQKEIEEQIKRGAIQFLYVAPERFENTffLNLLRKIE--IPLIAFDEAHCISKWGHDFRPSYQ--SVIQKVft 160
Cdd:cd18017 84 GSA----QSQNVLDDIKMGKIRVIYVTPEFVSKG--LELLQQLRngITLIAIDEAHCVSQWGHDFRSSYRhlGSIRNR-- 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1279652141 161 LPqNFTIVALTATATAEVQQDIMSKLSIGQNDVVKTS 197
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 ... |
200-330 |
7.29e-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: 171.62 E-value: 7.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 200 RRNLIFKV---NPTYQRQKFVVDYVANHEGQAGIIYCSTRKQVEELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDR 276
Cdd:cd18794 1 RPNLFYSVrpkDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1279652141 277 VEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLF 330
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
2-188 |
1.31e-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: 168.08 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 2 MQETLSHYFGYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQA 81
Cdd:cd18016 5 MMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 82 AYLNSSLTHKQQKEIEEQIKRG--AIQFLYVAPE------RFENTFFlNLLRKIEIPLIAFDEAHCISKWGHDFRPSYQ- 152
Cdd:cd18016 85 TYLTGDKTDAEATKIYLQLSKKdpIIKLLYVTPEkisasnRLISTLE-NLYERKLLARFVIDEAHCVSQWGHDFRPDYKr 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1279652141 153 -SVIQKVFtlpQNFTIVALTATATAEVQQDIMSKLSI 188
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 ... |
3-191 |
2.36e-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: 161.87 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 3 QETLSHYFGYKSFR-PGQEEIITKILN-HQHTLGVLPTGGGKSICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQ 80
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKgNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 81 AAYLNSSLTHKQQKEIEEQIKRGA--IQFLYVAPERFENTFFL----NLLRKIEIPLIAFDEAHCISKWGHDFRPSYQSv 154
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEKpqTKFLYITPEMAATSSFQpllsSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLR- 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1279652141 155 IQKVFTLPQNFTIVALTATATAEVQQDIMSKLSIGQN 191
Cdd:cd18014 160 LGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| DpdF |
NF041063 |
protein DpdF; |
6-334 |
5.37e-39 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 153.14 E-value: 5.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 6 LSHYFGYKSFR-PGQEEII----------TKILNhqhtlgvLPTGGGKSICYQVPGLM---QGGTTIVISPLISLMKDQV 71
Cdd:NF041063 131 LAEALGFTHYRsPGQREAVraallappgsTLIVN-------LPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 72 DQLQAMGIQA--------AYlNSSLTHKQQKEIEEQIKRGAIQFLYVAPE------RFenTFF----LNLLRkieipLIA 133
Cdd:NF041063 204 RRARELLRRAgpdlggplAW-HGGLSAEERAAIRQRIRDGTQRILFTSPEsltgslRP--ALFdaaeAGLLR-----YLV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 134 FDEAHCISKWGHDFRPSYQSV---IQKVFTL---PQNFTIVALTATATAEvQQDIMSKL--SIGQNDVVKTSTKRRNLIF 205
Cdd:NF041063 276 VDEAHLVDQWGDGFRPEFQLLaglRRSLLRLapsGRPFRTLLLSATLTES-TLDTLETLfgPPGPFIVVSAVQLRPEPAY 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 206 KVNPT---YQRQKFVVDYVANhegqAG---IIYCSTRKQVEELHEALNNEKIKS-TIYHAGLTNKER---IEAQNDflyD 275
Cdd:NF041063 355 WVAKCdseEERRERVLEALRH----LPrplILYVTKVEDAEAWLQRLRAAGFRRvALFHGDTPDAERerlIEQWRE---N 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1279652141 276 RVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLFSERD 334
Cdd:NF041063 428 ELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDD 486
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
16-180 |
2.43e-27 |
|
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: 108.10 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 16 RPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGL------MQGGTTIVISPLISLMKDQVDQLQAMGIQAAY-LNSSL 88
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 89 THKQQKEIEEQIKRgaIQFLYVAPERFENTFFL-NLLRKIEipLIAFDEAHCISKWGhdFRPSYQSVIQKvftLPQNFTI 167
Cdd:pfam00270 81 GGDSRKEQLEKLKG--PDILVGTPGRLLDLLQErKLLKNLK--LLVLDEAHRLLDMG--FGPDLEEILRR---LPKKRQI 151
|
170
....*....|...
gi 1279652141 168 VALTATATAEVQQ 180
Cdd:pfam00270 152 LLLSATLPRNLED 164
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
215-321 |
3.67e-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: 3.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 215 KFVVDYVANHEGQAGIIYCSTRKQVEElHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSN 294
Cdd:pfam00271 4 EALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
|
90 100
....*....|....*....|....*..
gi 1279652141 295 VRYVIHYNMPGDLESYYQEAGRAGRDG 321
Cdd:pfam00271 83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
8-203 |
3.83e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 100.26 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 8 HYFGYKSFRPGQEEIITKIL-NHQHTLGVLPTGGGKSICYQVPGLMQ-----GGTTIVISPLISLMKDQVDQLQAMGIQA 81
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLsGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 82 AYLNSSLTH-KQQKEIEEQIKRGAIQFLYVAPERFENTFFLNLLRKIEIPLIAFDEAHCISKWGHdfrpsYQSVIQKVFT 160
Cdd:smart00487 82 GLKVVGLYGgDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGF-----GDQLEKLLKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1279652141 161 LPQNFTIVALTATATAEVQQDimskLSIGQNDVVKTSTKRRNL 203
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENL----LELFLNDPVFIDVGFTPL 195
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
240-321 |
1.68e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 94.59 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 240 EELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGR 319
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1279652141 320 DG 321
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 ... |
403-491 |
2.31e-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: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 403 DMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHGLMKNYTTSELSHLIDELRFKGYLNENDE--- 479
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGryp 80
|
90
....*....|..
gi 1279652141 480 ILMCDTSVKQLL 491
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
201-330 |
6.89e-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: 88.72 E-value: 6.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 201 RNLIFKVNPTYQRQKFVVDYVANHEGQAGIIYCSTRKQVEELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVV 280
Cdd:cd18787 2 KQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1279652141 281 IATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLF 330
Cdd:cd18787 82 VATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
11-337 |
2.92e-18 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 87.51 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 11 GYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLMQ-----GGTT--IVISP---LIslmkDQV-DQLQAMGi 79
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRldpsrPRAPqaLILAPtreLA----LQVaEELRKLA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 80 qaAYLN-SSLT----HKQQKEIEeQIKRGAiQFLyVA-PERF-----ENTFFLNllrKIEIpLIaFDEAhciskwghD-- 146
Cdd:COG0513 96 --KYLGlRVATvyggVSIGRQIR-ALKRGV-DIV-VAtPGRLldlieRGALDLS---GVET-LV-LDEA--------Drm 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 147 ----FRPSyqsvIQKVFT-LPQNFTIVALTATATAEVQQdIMSKLsigQNDVVKTSTKRRNL--------IFKVNPtYQR 213
Cdd:COG0513 158 ldmgFIED----IERILKlLPKERQTLLFSATMPPEIRK-LAKRY---LKNPVRIEVAPENAtaetieqrYYLVDK-RDK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 214 QKFVVDYVANHEGQAGIIYCSTRKQVEELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKS 293
Cdd:COG0513 229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1279652141 294 NVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLFSERDKGL 337
Cdd:COG0513 309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRL 352
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
519-586 |
4.87e-18 |
|
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: 78.35 E-value: 4.87e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279652141 519 DRALYRELVDVRKQLSDKLGIAPVSIFSDYTLEEFAKRKPESKQEMIAIDGVGSYKLKHYCPKFIETI 586
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| 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 1279652141 16 RPGQEEIITKIL-----NHQHTLGVLPTGGGKSI----CYQvpGLMQGGTTIVISPLISLMKDQVDQLQamgiqaAYLNS 86
Cdd:COG1061 82 RPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELR------RFLGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 87 SLTHKQQKEIEEQIKRGAIQFLYVAP--ERFENTFflnllrkieiPLIAFDEAHciskwgHDFRPSYQSVIQKvftLPQN 164
Cdd:COG1061 154 PLAGGGKKDSDAPITVATYQSLARRAhlDELGDRF----------GLVIIDEAH------HAGAPSYRRILEA---FPAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 165 FtIVALTAT---------------------ATAEVQQD----------IMSKLSIGQNDVVKTSTKRRNLIFKVNPtyQR 213
Cdd:COG1061 215 Y-RLGLTATpfrsdgreillflfdgivyeySLKEAIEDgylappeyygIRVDLTDERAEYDALSERLREALAADAE--RK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 214 QKFVVDYVANH-EGQAGIIYCSTRKQVEELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDK 292
Cdd:COG1061 292 DKILRELLREHpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371
|
330 340
....*....|....*....|....*.
gi 1279652141 293 SNVRYVIhYNMP-GDLESYYQEAGRA 317
Cdd:COG1061 372 PRLDVAI-LLRPtGSPREFIQRLGRG 396
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
400-498 |
1.15e-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: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 400 KTYDMTREAKMIISCIARMKQQESYSVIIQVLRGEVTDYIKHHHYNELTTHGLMKNYTTSELSHLIDELRFKGYLNENDE 479
Cdd:pfam09382 3 ETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDIE 82
|
90 100
....*....|....*....|..
gi 1279652141 480 ---ILMCDTSVKQLLNNHTKVY 498
Cdd:pfam09382 83 fysVLKLTPKAREVLKGEEKVM 104
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
11-347 |
7.37e-16 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 80.60 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 11 GYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGLM-------------QGGTTIVISPLISLMKdQVDQlqam 77
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctirsghpseqRNPLAMVLTPTRELCV-QVED---- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 78 giQAAYLNSSLTHK-----------QQKEieeQIKRGaIQFLYVAPERFentffLNLLRKIEIPL-----IAFDEAHCIS 141
Cdd:PLN00206 215 --QAKVLGKGLPFKtalvvggdampQQLY---RIQQG-VELIVGTPGRL-----IDLLSKHDIELdnvsvLVLDEVDCML 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 142 KWGhdFRpsyQSVIQKVFTLPQNfTIVALTATATAEVQ-------QDIMSkLSIGQNDVVKTSTKRrnLIFKVNPTYQRQ 214
Cdd:PLN00206 284 ERG--FR---DQVMQIFQALSQP-QVLLFSATVSPEVEkfasslaKDIIL-ISIGNPNRPNKAVKQ--LAIWVETKQKKQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 215 K-FVVDYVANHEGQAGIIYCSTRKQVEELHEALN-NEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDK 292
Cdd:PLN00206 355 KlFDILKSKQHFKPPAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1279652141 293 SNVRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLFSERDKGLHEYFITVSQA 347
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 ... |
230-329 |
8.56e-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: 71.90 E-value: 8.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 230 IIYCSTRKQVEEL---------HEALNNEKIKStiYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIH 300
Cdd:cd18797 39 IVFCRSRKLAELLlrylkarlvEEGPLASKVAS--YRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
|
90 100
....*....|....*....|....*....
gi 1279652141 301 YNMPGDLESYYQEAGRAGRDGLKSECILL 329
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
518-589 |
2.27e-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: 68.48 E-value: 2.27e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279652141 518 VDRALYRELVDVRKQLSDKLGIAPVSIFSDYTLEEFAKRKPESKQEMIAIDGVGSYKLKHYCPKFIETIQSY 589
Cdd:smart00341 3 RQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEA 74
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
19-321 |
4.57e-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: 75.26 E-value: 4.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 19 QEEIITKILNHQHTLGVLPTGGGKSICYQVP---GLMQ--GGTTIVISPLISLMKDQVDQLQAMgiqAAYLNSSL----- 88
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPvleALLEdpGATALYLYPTKALARDQLRRLREL---AEALGLGVrvaty 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 89 ---THKQQKEieeQIKRGAiQFLYVAP-----------ERFENtFFLNLlRkieipLIAFDEAHciskwghdfrpSYQSV 154
Cdd:COG1205 138 dgdTPPEERR---WIREHP-DIVLTNPdmlhygllphhTRWAR-FFRNL-R-----YVVIDEAH-----------TYRGV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 155 ---------------IQKVFTLPQnftIVALTAT-----ATAEvqqdimsKLsIGQN-DVVKTSTK---RRNLIFkVNP- 209
Cdd:COG1205 196 fgshvanvlrrlrriCRHYGSDPQ---FILASATignpaEHAE-------RL-TGRPvTVVDEDGSprgERTFVL-WNPp 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 210 ---TYQRQ-------KFVVDYVANheGQAGIIYCSTRKQVE----ELHEALNNEKIKSTI--YHAGLTNKERIEAQNDFL 273
Cdd:COG1205 264 lvdDGIRRsalaeaaRLLADLVRE--GLRTLVFTRSRRGAEllarYARRALREPDLADRVaaYRAGYLPEERREIERGLR 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1279652141 274 YDRVEVVIATNAFGMGIDKSNVRYVI--HYnmPGDLESYYQEAGRAGRDG 321
Cdd:COG1205 342 SGELLGVVSTNALELGIDIGGLDAVVlaGY--PGTRASFWQQAGRAGRRG 389
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
31-173 |
6.11e-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: 69.35 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 31 HTLGVLPTGGGKSICYQVP----GLMQGGTTIVISPLISLMKDQ---VDQLQAMGIQAAYLNSSLThkqqKEIEEQIKRG 103
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAalllLLKKGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSS----AEEREKNKLG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279652141 104 AIQFLYVAPERFENTF-FLNLLRKIEIPLIAFDEAHCISKWGHDFRPSYQSVIQKVFTLPQnftIVALTAT 173
Cdd:cd00046 79 DADIIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQ---VILLSAT 146
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
230-335 |
1.19e-10 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 63.69 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 230 IIYCSTRKQVEELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLES 309
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100
....*....|....*....|....*.
gi 1279652141 310 YYQEAGRAGRDGLKSECILLFSERDK 335
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDI 376
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
263-329 |
1.85e-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: 1.85e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279652141 263 KERIEAQNDfLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDG-LKSECILL 329
Cdd:cd18785 10 TNSIEHAEE-IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
333-395 |
4.78e-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: 4.78e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279652141 333 RDKGLHEYFITVSQADDDYKDKMGEKLTKMIQY-TKTKKCLEATIVHYFEPNENLEECNQCSNC 395
Cdd:pfam16124 2 QDVVRLRFLIEQSEADEERKEVELQKLQAMVAYcENTTDCRRKQLLRYFGEEFDSEPCGNCDNC 65
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
230-335 |
2.29e-09 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 60.17 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 230 IIYCSTRKQVEELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLES 309
Cdd:PTZ00110 381 LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIED 460
|
90 100
....*....|....*....|....*.
gi 1279652141 310 YYQEAGRAGRDGLKSeCILLFSERDK 335
Cdd:PTZ00110 461 YVHRIGRTGRAGAKG-ASYTFLTPDK 485
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
215-329 |
2.84e-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: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 215 KFVVDYVANHEGQAgIIYCSTRKQVEELHEALNNekIKstIYHAGLTNKER--IEaqNDFLYDRVEVVIATNAFGMGID- 291
Cdd:cd18795 33 VLLKIETVSEGKPV-LVFCSSRKECEKTAKDLAG--IA--FHHAGLTREDRelVE--ELFREGLIKVLVATSTLAAGVNl 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1279652141 292 -------KSNVRYVIHYNMPGDLESYYQEAGRAGRDGL--KSECILL 329
Cdd:cd18795 106 partviiKGTQRYDGKGYRELSPLEYLQMIGRAGRPGFdtRGEAIIM 152
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
11-337 |
3.54e-08 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 56.40 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 11 GYKSFRPGQEEIITKILNHQHTLGVLPTGGGKSICYQVPGL------MQGGTTIVISPLISLmkdQVDQLQAMGIQAAYL 84
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTREL---AVQVAEAMTDFSKHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 85 NS----SLTHKQQKEIEEQIKRGAIQFLYVAPERFentffLNLLRKIEIPL-----IAFDEAHCISKWGhdFRPSYQSVI 155
Cdd:PRK11634 102 RGvnvvALYGGQRYDVQLRALRQGPQIVVGTPGRL-----LDHLKRGTLDLsklsgLVLDEADEMLRMG--FIEDVETIM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 156 QKVftlPQNFTIVALTATATAEVQQDIMSKLSIGQNDVVKTSTKRRNLIFKVNPT---YQRQKFVVDYVANHEGQAGIIY 232
Cdd:PRK11634 175 AQI---PEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTvwgMRKNEALVRFLEAEDFDAAIIF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 233 CSTRKQVEELHEALNNEKIKSTIYHaGLTNKERIEAQNDFLYD-RVEVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYY 311
Cdd:PRK11634 252 VRTKNATLEVAEALERNGYNSAALN-GDMNQALREQTLERLKDgRLDILIATDVAARGLDVERISLVVNYDIPMDSESYV 330
|
330 340
....*....|....*....|....*.
gi 1279652141 312 QEAGRAGRDGLKSECILLFSERDKGL 337
Cdd:PRK11634 331 HRIGRTGRAGRAGRALLFVENRERRL 356
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
14-174 |
1.62e-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: 51.49 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 14 SFRPGQEEIITKILNHQHTLGV-LPTGGGKSICYQ---VPGLMQGGTTIV-ISPLISL----MKDQVDQLQAMGIQAAYL 84
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVsAPTSSGKTLIAElaiLRALATSGGKAVyIAPTRALvnqkEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 85 NSSLTHKQQKEIEEQIkrgaiqflYVA-PERFENtfflnLLRKIEIP------LIAFDEAHCIskwGHDFR-PSYQSVIQ 156
Cdd:cd17921 81 TGDPSVNKLLLAEADI--------LVAtPEKLDL-----LLRNGGERliqdvrLVVVDEAHLI---GDGERgVVLELLLS 144
|
170
....*....|....*...
gi 1279652141 157 KVFTLPQNFTIVALTATA 174
Cdd:cd17921 145 RLLRINKNARFVGLSATL 162
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
215-334 |
1.78e-07 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 53.76 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 215 KFVVDYVANHEGQAGIIYCSTRKQVEELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSN 294
Cdd:PRK01297 324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1279652141 295 VRYVIHYNMPGDLESYYQEAGRAGRDGLKSECILLFSERD 334
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
13-173 |
3.41e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 50.36 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 13 KSFRPGQEEIITKILN-----HQHTLGVLPTGGGKS-----ICYQVPGLMQGGTTIVISPLISLMKDQVDQLQAMGIQAA 82
Cdd:pfam04851 2 LELRPYQIEAIENLLEsikngQKRGLIVMATGSGKTltaakLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 83 YLNSSLT--HKQQKEIEEQIKRGAIQFLYVAPERFENTFFLNllrkiEIPLIAFDEAHciskwgHDFRPSYQSVIQKVft 160
Cdd:pfam04851 82 EIGEIISgdKKDESVDDNKIVVTTIQSLYKALELASLELLPD-----FFDVIIIDEAH------RSGASSYRNILEYF-- 148
|
170
....*....|...
gi 1279652141 161 lpQNFTIVALTAT 173
Cdd:pfam04851 149 --KPAFLLGLTAT 159
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
227-329 |
5.76e-06 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 49.04 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 227 QAGIIYCSTRKQVEELHEALNNEKIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNMPGD 306
Cdd:PRK10590 246 QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNV 325
|
90 100
....*....|....*....|...
gi 1279652141 307 LESYYQEAGRAGRDGLKSECILL 329
Cdd:PRK10590 326 PEDYVHRIGRTGRAAATGEALSL 348
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
224-319 |
1.26e-05 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 48.35 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 224 HEGQAgIIYCSTRKQVEELHEALNnekIKSTIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFG---------------- 287
Cdd:COG1202 426 YRGQT-IIFTNSRRRCHEIARALG---YKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAagvdfpasqvifdsla 501
|
90 100 110
....*....|....*....|....*....|..
gi 1279652141 288 MGIDKSNVRyvihynmpgdleSYYQEAGRAGR 319
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 ... |
19-74 |
2.27e-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: 2.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279652141 19 QEEIITKILNHQHTLGVLPTGGGKSICYQVP---GLMQ--GGTTIVISPLISLMKDQVDQL 74
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRdpGSRALYLYPTKALAQDQLRSL 65
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
230-388 |
4.20e-05 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 46.65 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 230 IIYCSTRKQVEELHEALNNEKIKSTIY--------HAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHY 301
Cdd:COG1111 357 IVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskegDKGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 302 -NMPGDLESyYQEAGRAGRDGLKSECILLFSE-RDkglhEYFITVSQADDDYKDKMGEKLTKMIQY---TKTKKCLEATI 376
Cdd:COG1111 437 ePVPSEIRS-IQRKGRTGRKREGRVVVLIAKGtRD----EAYYWSSRRKEKKMKSILKKLKKLLDKqekEKLKESAQATL 511
|
170
....*....|..
gi 1279652141 377 VHYFEPNENLEE 388
Cdd:COG1111 512 DEFESIKELAED 523
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
14-193 |
4.98e-05 |
|
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: 44.24 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 14 SFRPGQEEIITKILnHQHTLGVLPTGGGKSICYQVpgLMQG-------GTTIVISPLISLMKDQVDQ-LQAMGI---QAA 82
Cdd:cd18033 2 PLRDYQFTIVQKAL-FQNTLVALPTGLGKTFIAAV--VMLNyyrwfpkGKIVFMAPTKPLVSQQIEAcYKITGIpssQTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 83 YLNSSLTHKQQKEIEEQiKRgaiqFLYVAPERFENtfflNLLRKI----EIPLIAFDEAHCISKwghdfRPSYQSVIQKV 158
Cdd:cd18033 79 ELTGSVPPTKRAELWAS-KR----VFFLTPQTLEN----DLKEGDcdpkSIVCLVIDEAHRATG-----NYAYCQVVREL 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 1279652141 159 FTLPQNFTIVALTAT---ATAEVQQdIMSKLSIGQNDV 193
Cdd:cd18033 145 MRYNSHFRILALTATpgsKLEAVQQ-VIDNLLISHIEI 181
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
13-173 |
1.46e-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: 43.19 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 13 KSFRPGQEEIITKILNHQHTLGVLPTGGGKS-----IC----YQVPGlMQGGTTIVISPLISLMKDQVDQLQAMGIQAAY 83
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPA-GRKGKVVFLANKVPLVEQQKEVFRKHFERPGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 84 LNSSLT-HKQQKEIEEQIKRGAiQFLYVAPERFENTFF-LNLLRKIEIPLIAFDEAHCISKwGHDFRP---SYQSviQKV 158
Cdd:cd17927 80 KVTGLSgDTSENVSVEQIVESS-DVIIVTPQILVNDLKsGTIVSLSDFSLLVFDECHNTTK-NHPYNEimfRYLD--QKL 155
|
170
....*....|....*
gi 1279652141 159 FTLPQNFTIVALTAT 173
Cdd:cd17927 156 GSSGPLPQILGLTAS 170
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
230-319 |
1.71e-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: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 230 IIYCSTRKQVEELHEALNN----EKIKSTIY-HAGLTNKE-RIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHYNM 303
Cdd:cd18796 42 LVFTNTRSQAERLAQRLRElcpdRVPPDFIAlHHGSLSRElREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90
....*....|....*.
gi 1279652141 304 PGDLESYYQEAGRAGR 319
Cdd:cd18796 122 PKSVARLLQRLGRSGH 137
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
19-321 |
1.88e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 44.49 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 19 QEEIITKILNHQHTLGVLPTGGGKS-ICYQV--PGLMQGGTTIVISPLISLMKDQVDQLqaMGIQAAYLNSSLTHKQQKE 95
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTlIAYSAiyETFLAGLKSIYIVPLRSLAMEKYEEL--SRLRSLGMRVKISIGDYDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 96 IEEQIKRGAIqfLYVAPERFENTFFLNLLRKIEIPLIAFDEAHCIskwGHDFR-PSYQSVIQKVFTLPQNFTIVALTATA 174
Cdd:PRK01172 105 PPDFIKRYDV--VILTSEKADSLIHHDPYIINDVGLIVADEIHII---GDEDRgPTLETVLSSARYVNPDARILALSATV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 175 TaevqqDIMSKLSIGQNDVVKTSTkrRNLIFKVNPTYQRQKF-------------VVDYVANHEGQAgIIYCSTRKQVEE 241
Cdd:PRK01172 180 S-----NANELAQWLNASLIKSNF--RPVPLKLGILYRKRLIldgyersqvdinsLIKETVNDGGQV-LVFVSSRKNAED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 242 LHEAL-------NNEKIKS------------------TIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSnVR 296
Cdd:PRK01172 252 YAEMLiqhfpefNDFKVSSennnvyddslnemlphgvAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP-AR 330
|
330 340 350
....*....|....*....|....*....|....
gi 1279652141 297 YVIHYNMP--GDLESYY-------QEAGRAGRDG 321
Cdd:PRK01172 331 LVIVRDITryGNGGIRYlsnmeikQMIGRAGRPG 364
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
230-439 |
9.38e-04 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 42.17 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 230 IIYCSTRKQVEELHEALNNEKIK--------STIYHAGLTNKERIEAQNDFLYDRVEVVIATNAFGMGIDKSNVRYVIHY 301
Cdd:PRK13766 369 IVFTQYRDTAEKIVDLLEKEGIKavrfvgqaSKDGDKGMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFY 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 302 N-MPGDLESyYQEAGRAGRDGlKSECILLFSE--RDKGlheYFItVSQADD--------DYKDKMGEKLTKMIQYTKTK- 369
Cdd:PRK13766 449 EpVPSEIRS-IQRKGRTGRQE-EGRVVVLIAKgtRDEA---YYW-SSRRKEkkmkeelkNLKGILNKKLQELDEEQKGEe 522
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1279652141 370 --KCLEATIVHYFEPNENLEECNQCSNCIQENKTYDMTREAKMII------SCIARMKQQESYSVIIQVLrgEVTDYI 439
Cdd:PRK13766 523 eeKDEQLSLDDFVKSKGKEEEEEEEKEEKDKETEEDEPEGPKIIVdsrelrSNVARHLKRLGAEVELKTL--EVGDYV 598
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
15-138 |
1.35e-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: 39.60 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 15 FRPGQEEIITKILNHQHTLG---VLPTGGGKS------ICYqvpgLMQgGTTIVISPLISLMKDQVDQLQAMGIQAA-YL 84
Cdd:cd17926 1 LRPYQEEALEAWLAHKNNRRgilVLPTGSGKTltalalIAY----LKE-LRTLIVVPTDALLDQWKERFEDFLGDSSiGL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1279652141 85 NSSLTHKQQKEIEEQIKRGAIQFLYVAPERFENTFFLnllrkieipLIAFDEAH 138
Cdd:cd17926 76 IGGGKKKDFDDANVVVATYQSLSNLAEEEKDLFDQFG---------LLIVDEAH 120
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
230-327 |
2.54e-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: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 230 IIYCSTRKQVEELHEALNNEKIKSTIYHAGLTNKERIEAQNDF---LYDRVeVVIATNAFGMGIDKSNVRYVIHY----N 302
Cdd:cd18793 31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnedPDIRV-FLLSTKAGGVGLNLTAANRVILYdpwwN 109
|
90 100
....*....|....*....|....*
gi 1279652141 303 mPGDLEsyyQEAGRAGRDGLKSECI 327
Cdd:cd18793 110 -PAVEE---QAIDRAHRIGQKKPVV 130
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
215-329 |
3.23e-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: 38.34 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 215 KFVVDYVANHEGQAGIIYCSTRKQV-------EELHEALNNEKIKSTI--------YHAGLTNKERIEAQNDFLYDRVEV 279
Cdd:cd18802 14 EILREYFPKTPDFRGIIFVERRATAvvlsrllKEHPSTLAFIRCGFLIgrgnssqrKRSLMTQRKQKETLDKFRDGELNL 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1279652141 280 VIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGlkSECILL 329
Cdd:cd18802 94 LIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYILM 141
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
19-106 |
5.44e-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: 38.34 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279652141 19 QEEIITKILN-----HQHTL-GVlpTGGGKSICY-----QVpgLMQGGTTIVISPLISLMKDQVDQLQA-MGIQAAYLNS 86
Cdd:cd17929 1 QRKAYEAIVSslggfKTFLLhGV--TGSGKTEVYielieKV--LAKGKQVLVLVPEISLTPQLIKRFKKrFGDKVAVLHS 76
|
90 100
....*....|....*....|
gi 1279652141 87 SLTHKQQKEIEEQIKRGAIQ 106
Cdd:cd17929 77 KLSDKERADEWRKIKRGEAK 96
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
6-61 |
5.95e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 39.52 E-value: 5.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1279652141 6 LSHYFGYKSFRPGQEEIITKI---LNHQHTLgVL--PTGGGKSICYQVPGL---MQGGTTIVIS 61
Cdd:COG1199 6 LALAFPGFEPRPGQREMAEAVaraLAEGRHL-LIeaGTGTGKTLAYLVPALlaaRETGKKVVIS 68
|
|
| |
