|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-474 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 720.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 1 MLEGAKNLLKKHFGYNEFRKAQEKVIESILKKEDTVAIMPTGAGKSICYQIPALIFGGVTVVISPLISLMKDQVDSLKEV 80
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 81 GIEATYINSSLNNLEIEERIFNAREGLYKLIYIAPERLESDSFVRSLNNLNIDLVAVDEAHCVSQWGHDFRPSYTKISSF 160
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 161 IRKLSKRPIV--------TaftatatetVRYDILNSLELQDPKVFVTGFDRENLSFSVIKG--EDKEKFIFDYLENNIGK 230
Cdd:COG0514 161 RERLPNVPVLaltatatpR---------VRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 231 VGIIYTSTRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHNIPKNM 310
Cdd:COG0514 232 SGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 311 EAYYQEAGRAGRDGEESECILLFSPNDIRLQKYFIDESFLSPERKNNEYNKLRAMVDYCYTSKCLRSYILEYFGeEPLEE 390
Cdd:COG0514 312 EAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFG-EELAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 391 KCNNCSTCNDNREEKDITLEAQKIFSCVYRMKERFGVNMVADVLRGSKNKKLLSLDLDGLSTYGIMEEFTQKDIVALMNK 470
Cdd:COG0514 391 PCGNCDNCLGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQ 470
|
....
gi 489584874 471 LIAD 474
Cdd:COG0514 471 LLAQ 474
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
5-587 |
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: 719.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 5 AKNLLKKHFGYNEFRKAQEKVIESILKKEDTVAIMPTGAGKSICYQIPALIFGGVTVVISPLISLMKDQVDSLKEVGIEA 84
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 85 TYINSSLNNLEIEERIFNAREGLYKLIYIAPERLESDSFVRSLNNLNIDLVAVDEAHCVSQWGHDFRPSYTKISSFIRKL 164
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 165 SKRPIVTAFTATATEtVRYDILNSLELQDPKVFVTGFDRENLSFSVIKGEDKEKFIFDYLENNIGKVGIIYTSTRKEAES 244
Cdd:TIGR01389 161 PQVPRIALTATADAE-TRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 245 LYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHNIPKNMEAYYQEAGRAGRDG 324
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 325 EESECILLFSPNDIRLQKYFIDESFLSPERKNNEYNKLRAMVDYCYTSKCLRSYILEYFGEEPLEEkCNNCSTCNDNREE 404
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEP-CGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 405 KDITLEAQKIFSCVYRMKERFGVNMVADVLRGSKNKKLLSLDLDGLSTYGIMEEFTQKDIVALMNKLIADDYMVTTDDKF 484
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 485 PVVRLRAKSYDVLKGKEAVAIKVSKIEKKVK----------ADNELLDRLKQLRKAISQEESVPPFMIFPDATLKELSEY 554
Cdd:TIGR01389 479 IGLQLTEAARKVLKNEVEVLLRPFKVVAKEKtrvqknlsvgVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEK 558
|
570 580 590
....*....|....*....|....*....|...
gi 489584874 555 MPTKEEDLLKIKGIGERKAEVYGERFIKSITEY 587
Cdd:TIGR01389 559 RPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
5-592 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 536.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 5 AKNLLKKHFGYNEFRKAQEKVIESILKKEDTVAIMPTGAGKSICYQIPALIFGGVTVVISPLISLMKDQVDSLKEVGIEA 84
Cdd:PRK11057 13 AKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 85 TYINSSLNNLEIEERIFNAREGLYKLIYIAPERLESDSFVRSLNNLNIDLVAVDEAHCVSQWGHDFRPSYTKISSFIRKL 164
Cdd:PRK11057 93 ACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 165 SKRPIVtAFTATATETVRYDILNSLELQDPKVFVTGFDRENLSFSVIkgedkEKF-----IFDYLENNIGKVGIIYTSTR 239
Cdd:PRK11057 173 PTLPFM-ALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLV-----EKFkpldqLMRYVQEQRGKSGIIYCNSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 240 KEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHNIPKNMEAYYQEAGR 319
Cdd:PRK11057 247 AKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 320 AGRDGEESECILLFSPNDIRLQKYFIDESFLSPErKNNEYNKLRAMVDYCYTSKCLRSYILEYFGEEPlEEKCNNCSTCN 399
Cdd:PRK11057 327 AGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQ-QDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGR-QEPCGNCDICL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 400 DNREEKDITLEAQKIFSCVYRMKERFGVNMVADVLRGSKNKKLLSLDLDGLSTYGIMEEFTQKDIVALMNKLIADDYMVT 479
Cdd:PRK11057 405 DPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQ 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 480 TDDKFPVVRLRAKSYDVLKGKEAVAIKVSKIE--KKVKA--------DNELLDRLKQLRKAISQEESVPPFMIFPDATLK 549
Cdd:PRK11057 485 NIAQHSALQLTEAARPVLRGEVSLQLAVPRIValKPRAMqksfggnyDRKLFAKLRKLRKSIADEENIPPYVVFNDATLI 564
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 489584874 550 ELSEYMPTKEEDLLKIKGIGERKAEVYGERFIKSITEYMDEKG 592
Cdd:PRK11057 565 EMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAHVDGDD 607
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
7-455 |
2.07e-155 |
|
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: 458.47 E-value: 2.07e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 7 NLLKKHFGYNEFRKAQEKVIESILKKEDTVAIMPTGAGKSICYQIPALIFGGVTVVISPLISLMKDQVDSLKEVGIEATY 86
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 87 INSSLNNLEIEERIFNAREGLYKLIYIAPERL-ESDSFVRSLNN-LNIDLVAVDEAHCVSQWGHDFRPSYTKISSFIRKL 164
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsASNRLLQTLEErKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 165 SKRPIVTAFTATATEtVRYDILNSLELQDPKVFVTGFDRENLSFSVikGEDKEKFIFDYLENNI----GKVGIIYTSTRK 240
Cdd:TIGR00614 161 PNVPVMALTATASPS-VREDILRQLNLLNPQIFCTSFDRPNLYYEV--RRKTPKILEDLLRFIRkefeGKSGIIYCPSRK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 241 EAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHNIPKNMEAYYQEAGRA 320
Cdd:TIGR00614 238 KVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 321 GRDGEESECILLFSPNDI-RLQKYFIDEsflsPERKNNEY-NKLRAMVDYC-YTSKCLRSYILEYFGEEPL--------- 388
Cdd:TIGR00614 318 GRDGLPSECHLFYAPADMnRLRRLLMEE----PDGNFRTYkLKLYEMMEYClNSSTCRRLILLSYFGEKGFnksfcimgt 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489584874 389 EEKCNNCSTCND----NREEK--DITLEAQKIFSCVYRMKERFGVNMVADVLRGSKNKKLLSLDLDGLSTYGI 455
Cdd:TIGR00614 394 EKCCDNCCKRLDyktkDVTDKvyDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGR 466
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
10-608 |
1.73e-107 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 353.43 E-value: 1.73e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 10 KKHFGYNEFRKAQEKVIESILKKEDTVAIMPTGAGKSICYQIPALIFGGVTVVISPLISLMKDQVDSLKEVGIEATYINS 89
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 90 SLNNLEIEE--RIFNAREGLYKLIYIAPERL-ESDSFVRSLNNLN----IDLVAVDEAHCVSQWGHDFRPSYTKISSFIR 162
Cdd:PLN03137 533 GMEWAEQLEilQELSSEYSKYKLLYVTPEKVaKSDSLLRHLENLNsrglLARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 163 KLSKRPiVTAFTATATETVRYDILNSLELQDPKVFVTGFDRENLSFSVIKG-----EDKEKFIfdyLENNIGKVGIIYTS 237
Cdd:PLN03137 613 KFPNIP-VLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKtkkclEDIDKFI---KENHFDECGIIYCL 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 238 TRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHNIPKNMEAYYQEA 317
Cdd:PLN03137 689 SRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQEC 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 318 GRAGRDGEESECILLFSPND-IRLqKYFIDESFL-------------SPER---KNNEyNKLRaMVDYCYTS-KCLRSYI 379
Cdd:PLN03137 769 GRAGRDGQRSSCVLYYSYSDyIRV-KHMISQGGVeqspmamgynrmaSSGRileTNTE-NLLR-MVSYCENEvDCRRFLQ 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 380 LEYFGEEPLEEKC-NNCSTCNDNRE--EKDITLEAQKIFSCVYRMKERFGVNMVADVLRGSKNKKLLSLDLDGLSTYGIM 456
Cdd:PLN03137 846 LVHFGEKFDSTNCkKTCDNCSSSKSliDKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAG 925
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 457 EEFTQKDIVALMNKLIADDYM---VTTDDKFPVVRL-----RAKSYDVLKGKEAV------AIKVSKI------------ 510
Cdd:PLN03137 926 KHLSKGEASRILHYLVTEDILaedVKKSDLYGSVSSllkvnESKAYKLFSGGQTIimrfpsSVKASKPskfeatpakgpl 1005
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 511 ----------------EKKVKADNELLDRLKQLRKAISQE--ESVPPFMIFPDATLKELSEYMPTKEEDLLKIKGIGERK 572
Cdd:PLN03137 1006 tsgkqstlpmatpaqpPVDLNLSAILYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAK 1085
|
650 660 670
....*....|....*....|....*....|....*..
gi 489584874 573 AEVYGERFIKSITEYMDEK-GIDFNNMDNYEGTKSNK 608
Cdd:PLN03137 1086 VSKYGDRLLETIESTINEYyKTDKNSSSSNDSPDSGK 1122
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
6-202 |
2.94e-91 |
|
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: 282.50 E-value: 2.94e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 6 KNLLKKHFGYNEFRKAQEKVIESILKKEDTVAIMPTGAGKSICYQIPALIFGGVTVVISPLISLMKDQVDSLKEVGIEAT 85
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 86 YINSSLNNLEIEERIFNAREGLYKLIYIAPERLESDSFVRSLNNLN----IDLVAVDEAHCVSQWGHDFRPSYTKISSFI 161
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489584874 162 RKLSKRPIVtaftatatETVRYDILNSLELQDPKVFVTGFD 202
Cdd:cd17920 161 RALPGVPILalta-tatPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
7-202 |
7.98e-66 |
|
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: 215.97 E-value: 7.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 7 NLLKKHFGYNEFRKAQEKVIESILKKEDTVAIMPTGAGKSICYQIPALIF----GGVTVVISPLISLMKDQVDSLKEvGI 82
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLrrrgPGLTLVVSPLIALMKDQVDALPR-AI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 83 EATYINSSLNNLEIEERIFNAREGLYKLIYIAPERLESDSFVRSLNNL-NIDLVAVDEAHCVSQWGHDFRPSYTKISSFI 161
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTpPISLLVVDEAHCISEWSHNFRPDYLRLCRVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489584874 162 RKLSKRPIVTAFTATATETVRYDILNSLELQDPKVFVTGFD 202
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
203-333 |
3.71e-53 |
|
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: 179.33 E-value: 3.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 203 RENLSFSVIKGEDKEKFIFD---YLENNIGKVGIIYTSTRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDN 279
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLlkrIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489584874 280 IEIIVATNAFGMGIDKSNVRFVIHHNIPKNMEAYYQEAGRAGRDGEESECILLF 333
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
9-202 |
2.99e-52 |
|
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: 179.64 E-value: 2.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 9 LKKHFGYNEFRKAQEKVIESILKKEDTVAIMPTGAGKSICYQIPALIFGGVTVVISPLISLMKDQVDSLKEVGIEATYIN 88
Cdd:cd18016 9 FHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 89 SSLNNLEIEE--RIFNAREGLYKLIYIAPERL-ESDSFVRSLNNLN----IDLVAVDEAHCVSQWGHDFRPSYTKISSFI 161
Cdd:cd18016 89 GDKTDAEATKiyLQLSKKDPIIKLLYVTPEKIsASNRLISTLENLYerklLARFVIDEAHCVSQWGHDFRPDYKRLNMLR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489584874 162 RKLSKRPIVtAFTATATETVRYDILNSLELQDPKVFVTGFD 202
Cdd:cd18016 169 QKFPSVPMM-ALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
7-202 |
6.83e-52 |
|
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: 178.43 E-value: 6.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 7 NLLKKHFGYNEFRKAQEKVIESILK-KEDTVAIMPTGAGKSICYQIPALIFGGVTVVISPLISLMKDQVDSLKEVGIEAT 85
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVIRSVLEeRRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 86 YINSSlnnlEIEERIFNAREGLYKLIYIAPERLESD-SFVRSLNNlNIDLVAVDEAHCVSQWGHDFRPSYTKISSFIRKL 164
Cdd:cd18017 82 FLGSA----QSQNVLDDIKMGKIRVIYVTPEFVSKGlELLQQLRN-GITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 489584874 165 SKRPIVtAFTATATETVRYDILNSLELQDPKVFVTGFD 202
Cdd:cd18017 157 PNVPIV-ALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
5-202 |
1.18e-51 |
|
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: 178.33 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 5 AKNLLKKHFGYNEFRKAQEKVIESILKKEDTVAIMPTGAGKSICYQIPALIFGGVTVVISPLISLMKDQVDSLKEVGIEA 84
Cdd:cd18015 6 VKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 85 TYINSSLNNLE---IEERIFNAREGLyKLIYIAPERL-ESDSFVRSLNNLN----IDLVAVDEAHCVSQWGHDFRPSYTK 156
Cdd:cd18015 86 TMLNASSSKEHvkwVHAALTDKNSEL-KLLYVTPEKIaKSKRFMSKLEKAYnagrLARIAIDEVHCCSQWGHDFRPDYKK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489584874 157 ISSFIRKLSKRPIVTAFTATATETVRyDILNSLELQDPKVFVTGFD 202
Cdd:cd18015 165 LGILKRQFPNVPILGLTATATSKVLK-DVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
6-194 |
1.16e-49 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 172.66 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 6 KNLLKKHFGYNEFRKA-QEKVIESILKKE-DTVAIMPTGAGKSICYQIPALIFGGVTVVISPLISLMKDQVDSLKEVGIE 83
Cdd:cd18014 1 RSTLKKVFGHSDFKSPlQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 84 ATYINSSLNNLEIEERIFNAREGL--YKLIYIAPERLESDSFVRSLNNL----NIDLVAVDEAHCVSQWGHDFRPSYTKI 157
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEKpqTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 489584874 158 SSFIRKLSKRPIVtAFTATATETVRYDILNSLELQDP 194
Cdd:cd18014 161 GALRSRYGHVPWV-ALTATATPQVQEDIFAQLRLKKP 196
|
|
| DpdF |
NF041063 |
protein DpdF; |
35-354 |
3.72e-49 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 185.12 E-value: 3.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 35 TVAIMPTGAGKSICYQIPALIF---GGVTVVISPLISLMKDQVDSLKEVGIEAT--------YI--NSSLNNLEIEERIf 101
Cdd:NF041063 161 LIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQERRARELLRRAGpdlggplaWHggLSAEERAAIRQRI- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 102 naREGLYKLIYIAPErlesdSFVRSLNNLNIDL--------VAVDEAHCVSQWGHDFRPSYTKISSFIRKL-----SKRP 168
Cdd:NF041063 240 --RDGTQRILFTSPE-----SLTGSLRPALFDAaeagllryLVVDEAHLVDQWGDGFRPEFQLLAGLRRSLlrlapSGRP 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 169 IvtaftatatetvR------------YDILNSL--ELQDPKVFVTGFDRENLSFSVIKGEDKEkfifDYLENNIGKVG-- 232
Cdd:NF041063 313 F------------RtlllsatltestLDTLETLfgPPGPFIVVSAVQLRPEPAYWVAKCDSEE----ERRERVLEALRhl 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 233 ----IIYTSTRKEAESLYNKINKKGYK-VGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHNIP 307
Cdd:NF041063 377 prplILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVP 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 489584874 308 KNMEAYYQEAGRAGRDGEESECILLFSPNDIRLQKYFIDESFLSPER 354
Cdd:NF041063 457 ETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKSLNRPKLISVEK 503
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
402-507 |
5.06e-33 |
|
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: 122.65 E-value: 5.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 402 REEKDITLEAQKIFSCVYRMKERFGVNMVADVLRGSKNKKLLSLDLDGLSTYGIMEEFTQKDIVALMNKLIADDYMVTTD 481
Cdd:pfam09382 2 PETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDI 81
|
90 100
....*....|....*....|....*.
gi 489584874 482 DKFPVVRLRAKSYDVLKGKEAVAIKV 507
Cdd:pfam09382 82 EFYSVLKLTPKAREVLKGEEKVMLRV 107
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
406-497 |
1.34e-28 |
|
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: 109.49 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 406 DITLEAQKIFSCVYRMKERFGVNMVADVLRGSKNKKLLSLDLDGLSTYGIMEEFTQKDIVALMNKLIADDYMVTTDDKFP 485
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 489584874 486 VVRLRAKSYDVL 497
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| HTH_40 |
pfam14493 |
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of ... |
614-702 |
6.80e-28 |
|
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of helicase proteins.
Pssm-ID: 464189 Cd Length: 89 Bit Score: 107.59 E-value: 6.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 614 THVLSYNLYKEGKSIKEIADERNLKAITIQEHLFKCLSEGMEVDLDNFIKKDYERLILDTIKKVGGTKLKPVKDELPPEV 693
Cdd:pfam14493 1 SAEITLELYKEGLSIEEIAEERGLKESTIEGHLAELIEAGEPVDIERLVSEEEQKEILDAIEKLGSESLKPIKEALPEEI 80
|
....*....
gi 489584874 694 DYMCIKSVW 702
Cdd:pfam14493 81 SYFEIRLVL 89
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
19-170 |
4.09e-25 |
|
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: 102.32 E-value: 4.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 19 RKAQEKVIESILKKEDTVAIMPTGAGKSICYQIPALIF------GGVTVVISPLISLMKDQVDSLKEVGIEATY-INSSL 91
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAldkldnGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 92 NNLEIEERIFNAREglYKLIYIAPERLesDSFVRSLNNL-NIDLVAVDEAHCVSQWGhdFRPSYTKISSFIRKlsKRPIV 170
Cdd:pfam00270 81 GGDSRKEQLEKLKG--PDILVGTPGRL--LDLLQERKLLkNLKLLVLDEAHRLLDMG--FGPDLEEILRRLPK--KRQIL 152
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
243-324 |
4.20e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 96.51 E-value: 4.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 243 ESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHNIPKNMEAYYQEAGRAGR 322
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 489584874 323 DG 324
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
215-324 |
1.12e-22 |
|
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: 93.43 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 215 DKEKFIFDYLENNIGKVGIIYTSTRKEAESLYnKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGID 294
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 489584874 295 KSNVRFVIHHNIPKNMEAYYQEAGRAGRDG 324
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
335-398 |
3.43e-22 |
|
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: 90.43 E-value: 3.43e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489584874 335 PNDIRLQKYFIDESFLSPERKNNEYNKLRAMVDYC-YTSKCLRSYILEYFGEEPLEEKCNNCSTC 398
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCeNTTDCRRKQLLRYFGEEFDSEPCGNCDNC 65
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
517-584 |
1.25e-21 |
|
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.
Pssm-ID: 425755 [Multi-domain] Cd Length: 68 Bit Score: 88.75 E-value: 1.25e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489584874 517 DNELLDRLKQLRKAISQEESVPPFMIFPDATLKELSEYMPTKEEDLLKIKGIGERKAEVYGERFIKSI 584
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
11-163 |
6.48e-21 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 91.40 E-value: 6.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 11 KHFGYNEFRKAQEKVIESILKKE-DTVAIMPTGAGKSICYQIPALIF-----GGVTVVISPLISLMKDQVDSLKEVGIEA 84
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 85 TYINSSL-NNLEIEERIFNAREGLYKLIYIAPERLESDSFVRSLNNLNIDLVAVDEAHCVSQWGhdFRPSYTKISSFIRK 163
Cdd:smart00487 82 GLKVVGLyGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLLPK 159
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
210-333 |
9.82e-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: 9.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 210 VIKGEDKEKFIFDYL--ENNIGKVgIIYTSTRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATN 287
Cdd:cd18787 7 VVEEEEKKLLLLLLLleKLKPGKA-IIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489584874 288 AFGMGIDKSNVRFVIHHNIPKNMEAYYQEAGRAGRDGEESECILLF 333
Cdd:cd18787 86 VAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
233-332 |
5.23e-20 |
|
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: 86.93 E-value: 5.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 233 IIYTSTRKEAESL-------YNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHN 305
Cdd:cd18797 39 IVFCRSRKLAELLlrylkarLVEEGPLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*..
gi 489584874 306 IPKNMEAYYQEAGRAGRDGEESECILL 332
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
210-340 |
6.06e-18 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 86.74 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 210 VIKGEDKEKFIFDYLENNIGKVGIIYTSTRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAF 289
Cdd:COG0513 222 LVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVA 301
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489584874 290 GMGIDKSNVRFVIHHNIPKNMEAYYQEAGRAGRDGEESECILLFSPNDIRL 340
Cdd:COG0513 302 ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRL 352
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
22-336 |
4.94e-17 |
|
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: 85.27 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 22 QEKVIESILKKEDTVAIMPTGAGKSICYQIPAL--IF---GGVTVVISPLISLMKDQVDSLKEvgieatYINSSLNNLEI 96
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLedpGATALYLYPTKALARDQLRRLRE------LAEALGLGVRV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 97 EerIF------NAREGLYK---LIYIAPERLES---------DSFVRSLnnlniDLVAVDEAHcvsqwghdfrpSYTKI- 157
Cdd:COG1205 135 A--TYdgdtppEERRWIREhpdIVLTNPDMLHYgllphhtrwARFFRNL-----RYVVIDEAH-----------TYRGVf 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 158 ----SSFIRKLsKRpIVTaftatatetvRYD-----ILNSLELQDPKVF---VTGfdrenLSFSVIkGED-----KEKFI 220
Cdd:COG1205 197 gshvANVLRRL-RR-ICR----------HYGsdpqfILASATIGNPAEHaerLTG-----RPVTVV-DEDgsprgERTFV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 221 F-----------------------DYLENNIgKVgIIYTSTRKEAESLYNKINKK------GYKVGVYHAGLNDEERKRT 271
Cdd:COG1205 259 LwnpplvddgirrsalaeaarllaDLVREGL-RT-LVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREI 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489584874 272 QEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHNIPKNMEAYYQEAGRAGRDGEESECILLFSPN 336
Cdd:COG1205 337 ERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVAGDD 401
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
517-591 |
7.92e-17 |
|
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.
Pssm-ID: 128635 [Multi-domain] Cd Length: 81 Bit Score: 75.80 E-value: 7.92e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489584874 517 DNELLDRLKQLRKAISQEESVPPFMIFPDATLKELSEYMPTKEEDLLKIKGIGERKAEVYGERFIKSITEYMDEK 591
Cdd:smart00341 4 QLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDSP 78
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
17-347 |
2.45e-16 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 82.77 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 17 EFRKAQEKVIESIL-----KKEDTVAIMPTGAGKSI----CYQipALIFGGVTVVISPLISLMKDQVDSLKEVgieatyi 87
Cdd:COG1061 80 ELRPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRF------- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 88 nsslnnLEIEERIFNAREGLYKLIYIAPERLESDSFVRSLNNlNIDLVAVDEAHcvsqwgHDFRPSYTKIssfIRKLSKR 167
Cdd:COG1061 151 ------LGDPLAGGGKKDSDAPITVATYQSLARRAHLDELGD-RFGLVIIDEAH------HAGAPSYRRI---LEAFPAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 168 PIV-----------TAFTATATETVRYDI-LNSLE----LQDPKVFV--TGFDRENLSFSVIK----------GEDKEKF 219
Cdd:COG1061 215 YRLgltatpfrsdgREILLFLFDGIVYEYsLKEAIedgyLAPPEYYGirVDLTDERAEYDALSerlrealaadAERKDKI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 220 IFDYLENNIGKV-GIIYTSTRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNV 298
Cdd:COG1061 295 LRELLREHPDDRkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRL 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489584874 299 RFVIHHNIPKNMEAYYQEAGRA--GRDGEESECILLFSPNDIRLQKYFIDE 347
Cdd:COG1061 375 DVAILLRPTGSPREFIQRLGRGlrPAPGKEDALVYDFVGNDVPVLEELAKD 425
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
33-167 |
2.60e-15 |
|
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: 73.59 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 33 EDTVAIMPTGAGKSICYQIPAL----IFGGVTVVISPLISLMKDQVDSLKEV---GIEATYINSSLNnleIEERiFNARE 105
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALllllKKGKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSS---AEER-EKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489584874 106 GLYKLIYIAPERLESDS-FVRSLNNLNIDLVAVDEAHCVSQWGHDFRPSYTKISSFIRKLSKR 167
Cdd:cd00046 78 GDADIIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV 140
|
|
| YpbB |
COG4955 |
Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown]; |
618-699 |
1.15e-13 |
|
Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown];
Pssm-ID: 443982 [Multi-domain] Cd Length: 346 Bit Score: 72.74 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 618 SYNLYKEGKSIKEIADERNLKAITIQEHLFKCLSEGMEVDLDNFIKKDYERLILDTIKKVGGTKLKPVKDELpPEVDYMC 697
Cdd:COG4955 255 TYQLLQQGLSLEEIAQIRRLKLSTIEDHLVEIAIKDPDFPIEPFVNKEDQQEIIQAIEKLGTWKLKEIKEQL-PDLSYFQ 333
|
..
gi 489584874 698 IK 699
Cdd:COG4955 334 IR 335
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
210-337 |
1.95e-11 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 66.86 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 210 VIKGEDKEKFIFDYL-ENNIGKVgIIYTSTRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNA 288
Cdd:PRK01297 316 AVAGSDKYKLLYNLVtQNPWERV-MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDV 394
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489584874 289 FGMGIDKSNVRFVIHHNIPKNMEAYYQEAGRAGRDGEESECILLFSPND 337
Cdd:PRK01297 395 AGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
233-332 |
2.87e-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: 56.94 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 233 IIYTSTRKEAESLYNKInkkgykvgvyhaglndeerkrtqedfsfdniEIIVATNAFGMGIDKSNVRFVIHHNIPKNMEA 312
Cdd:cd18785 7 IVFTNSIEHAEEIASSL-------------------------------EILVATNVLGEGIDVPSLDTVIFFDPPSSAAS 55
|
90 100
....*....|....*....|.
gi 489584874 313 YYQEAGRAGRDG-EESECILL 332
Cdd:cd18785 56 YIQRVGRAGRGGkDEGEVILF 76
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
233-332 |
5.47e-10 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 58.33 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 233 IIYTSTRKEAESLYNKInkKGykVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGID--------KSNVRFVIHH 304
Cdd:cd18795 47 LVFCSSRKECEKTAKDL--AG--IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKG 122
|
90 100 110
....*....|....*....|....*....|
gi 489584874 305 NIPKNMEAYYQEAGRAGRDG--EESECILL 332
Cdd:cd18795 123 YRELSPLEYLQMIGRAGRPGfdTRGEAIIM 152
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
215-338 |
6.92e-10 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 61.77 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 215 DKEKFIFDYL----ENNIGKVGIIYTSTRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFG 290
Cdd:PTZ00424 249 EKEEWKFDTLcdlyETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLA 328
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489584874 291 MGIDKSNVRFVIHHNIPKNMEAYYQEAGRAGRDGEESECILLFSPNDI 338
Cdd:PTZ00424 329 RGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDI 376
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
233-334 |
3.21e-09 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 56.12 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 233 IIYTSTRKEAESLYNKINKKGYK------VGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHNI 306
Cdd:cd18796 42 LVFTNTRSQAERLAQRLRELCPDrvppdfIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90 100
....*....|....*....|....*...
gi 489584874 307 PKNMEAYYQEAGRAGRDGEESECILLFS 334
Cdd:cd18796 122 PKSVARLLQRLGRSGHRPGAASKGRLVP 149
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
216-345 |
9.99e-09 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 58.26 E-value: 9.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 216 KEKFIFDYL--ENNIGKVGIIYTSTRKEAESLYNKINK-KGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMG 292
Cdd:PLN00206 352 KKQKLFDILksKQHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRG 431
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489584874 293 IDKSNVRFVIHHNIPKNMEAYYQEAGRAGRDGEESECILLFSPNDIRLQKYFI 345
Cdd:PLN00206 432 VDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELV 484
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
2-322 |
1.57e-08 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 57.60 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 2 LEGAKNLLKKhFGYNEFRKAQEKVIESILKKEDTVAI-MPTGAGKSICYQIPAL--IFGGVTVV-ISPLISL----MKDQ 73
Cdd:COG1204 8 LEKVIEFLKE-RGIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTLIAELAILkaLLNGGKALyIVPLRALasekYREF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 74 VDSLKEVGIEaTYInSSLNNLEIEERIFNAReglyklIYIA-PERLesDSFVRSLNNL--NIDLVAVDEAHCVsqwGHDF 150
Cdd:COG1204 87 KRDFEELGIK-VGV-STGDYDSDDEWLGRYD------ILVAtPEKL--DSLLRNGPSWlrDVDLVVVDEAHLI---DDES 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 151 R-PSYTKISSFIRKLSKRPIVtaftatatetvrydILNS---------LELQDPKVFVTG----------FDRENLSF-- 208
Cdd:COG1204 154 RgPTLEVLLARLRRLNPEAQI--------------VALSatignaeeiAEWLDAELVKSDwrpvplnegvLYDGVLRFdd 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 209 -SVIKGEDKEKFIFDYLENNiGKVgIIYTSTRKEAESLYNKINKK-----------------------------GYK--- 255
Cdd:COG1204 220 gSRRSKDPTLALALDLLEEG-GQV-LVFVSSRRDAESLAKKLADElkrrltpeereeleelaeellevseethtNEKlad 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 256 -----VGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIdksN--VRFVIHHNI-------PKNMEaYYQEAGRAG 321
Cdd:COG1204 298 clekgVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV---NlpARRVIIRDTkrggmvpIPVLE-FKQMAGRAG 373
|
.
gi 489584874 322 R 322
Cdd:COG1204 374 R 374
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
214-330 |
1.68e-08 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 57.65 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 214 EDKEKFIFDYLENNIGKVGIIYTSTRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGI 293
Cdd:PRK04537 242 EEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGL 321
|
90 100 110
....*....|....*....|....*....|....*..
gi 489584874 294 DKSNVRFVIHHNIPKNMEAYYQEAGRAGRDGEESECI 330
Cdd:PRK04537 322 HIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAI 358
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
233-342 |
2.93e-08 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 57.09 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 233 IIYTSTRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHNIPKNMEA 312
Cdd:PTZ00110 381 LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIED 460
|
90 100 110
....*....|....*....|....*....|
gi 489584874 313 YYQEAGRAGRDGEESECILLFSPNDIRLQK 342
Cdd:PTZ00110 461 YVHRIGRTGRAGAKGASYTFLTPDKYRLAR 490
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
22-141 |
3.05e-08 |
|
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: 54.13 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 22 QEKVIESILKKEDTVAIMPTGAGKSICYQIPAL-----IFGGVTVVISPLISLMKDQVDSLKEVGIE-------ATYINS 89
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeallrDPGSRALYLYPTKALAQDQLRSLRELLEQlglgirvATYDGD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489584874 90 SlnnlEIEERIFNAREGlYKLIYIAPERLE------SDSFVRSLNNLniDLVAVDEAH 141
Cdd:cd17923 85 T----PREERRAIIRNP-PRILLTNPDMLHyallphHDRWARFLRNL--RYVVLDEAH 135
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
207-340 |
3.82e-07 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 53.31 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 207 SFSVIKGEDKEKFIFDYLENNIGKVGIIYTSTRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVAT 286
Cdd:PRK11634 223 SYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIAT 302
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489584874 287 NAFGMGIDKSNVRFVIHHNIPKNMEAYYQEAGRAGRDGEESECILLFSPNDIRL 340
Cdd:PRK11634 303 DVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRL 356
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
17-157 |
6.03e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 49.98 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 17 EFRKAQEKVIESIL-----KKEDTVAIMPTGAGKSICY-QIPALIF--GGV--TVVISPLISLMKDQVDSLKEVGIEATY 86
Cdd:pfam04851 3 ELRPYQIEAIENLLesiknGQKRGLIVMATGSGKTLTAaKLIARLFkkGPIkkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489584874 87 INSSLNNLEIEER------IFNAREGLYKLIYIAPERLESDSFvrslnnlniDLVAVDEAHcvsqwgHDFRPSYTKI 157
Cdd:pfam04851 83 IGEIISGDKKDESvddnkiVVTTIQSLYKALELASLELLPDFF---------DVIIIDEAH------RSGASSYRNI 144
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
17-145 |
2.54e-06 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 48.41 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 17 EFRKAQEKVIESILKKEDTVAI-MPTGAGKSIC--YQIPALI--FGGVTVVISPLISLMKDQVDSLKEVGIEAtYINSSL 91
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVsAPTSSGKTLIaeLAILRALatSGGKAVYIAPTRALVNQKEADLRERFGPL-GKNVGL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489584874 92 NNLEIEERIFNAREglyKLIYIA-PERLesDSFVRSLNNL---NIDLVAVDEAHCVSQ 145
Cdd:cd17921 80 LTGDPSVNKLLLAE---ADILVAtPEKL--DLLLRNGGERliqDVRLVVVDEAHLIGD 132
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
520-586 |
5.56e-06 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 49.10 E-value: 5.56e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489584874 520 LLDRLKQLRKAISQEESVPPFMIFPDATLKELSEYMPTKEEDLLKIKGIGERKAEVYGERFIKSITE 586
Cdd:COG0349 212 VLRELAAWREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAE 278
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
233-322 |
5.85e-06 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 49.89 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 233 IIYTSTRKEAESLYNKInkkGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGID--KSNVRF---------V 301
Cdd:COG1202 431 IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDfpASQVIFdslamgiewL 507
|
90 100
....*....|....*....|.
gi 489584874 302 ihhnipkNMEAYYQEAGRAGR 322
Cdd:COG1202 508 -------SVQEFHQMLGRAGR 521
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
209-335 |
7.34e-06 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 46.57 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 209 SVIKGEDKEKfIFDYLENNI---GKVGIIYTSTR-------KEAESLYNKINKK---GYKVGVYHAGLNDEERKRTQEDF 275
Cdd:cd18811 5 YLIFHTRLDK-VYEFVREEIakgRQAYVIYPLIEesekldlKAAVAMYEYLKERfrpELNVGLLHGRLKSDEKDAVMAEF 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489584874 276 SFDNIEIIVATNAFGMGIDKSNVR-FVIHHNIPKNMEAYYQEAGRAGRDGEESECILLFSP 335
Cdd:cd18811 84 REGEVDILVSTTVIEVGVDVPNATvMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYKD 144
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
225-332 |
1.52e-05 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 47.88 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 225 ENNIGKVgIIYTSTRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHH 304
Cdd:PRK10590 242 KGNWQQV-LVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
90 100
....*....|....*....|....*...
gi 489584874 305 NIPKNMEAYYQEAGRAGRDGEESECILL 332
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSL 348
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
233-325 |
1.88e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 47.66 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 233 IIYTSTRKEAESLYNKINKKGYKVGVYHAGLNDEERKRTQEDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHNIPKNMEA 312
Cdd:PRK04837 259 IIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCED 338
|
90
....*....|...
gi 489584874 313 YYQEAGRAGRDGE 325
Cdd:PRK04837 339 YVHRIGRTGRAGA 351
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
210-335 |
6.99e-05 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain] Cd Length: 160 Bit Score: 43.79 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 210 VIKGEDKEKfIFDYLENNI---GKVGIIYT-------STRKEAESLYNKINKK--GYKVGVYHAGLNDEERKRTQEDFSF 277
Cdd:cd18792 6 VIPHDDLDL-VYEAIERELargGQVYYVYPrieesekLDLKSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFRE 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489584874 278 DNIEIIVATNAFGMGIDKSNVRFVIHHNIPK-NMEAYYQEAGRAGRDGEESECILLFSP 335
Cdd:cd18792 85 GEYDILVSTTVIEVGIDVPNANTMIIEDADRfGLSQLHQLRGRVGRGKHQSYCYLLYPD 143
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
18-141 |
3.40e-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: 41.52 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 18 FRKAQEKVIESILKKEDT---VAIMPTGAGKSIC-YQIPALIFGGVTVVISPLISLMKDQVDslkevGIEATYINSSLNN 93
Cdd:cd17926 1 LRPYQEEALEAWLAHKNNrrgILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKE-----RFEDFLGDSSIGL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489584874 94 LEIEERIFNAReglyKLIYIA-PERLESDSFVRSLNNLNIDLVAVDEAH 141
Cdd:cd17926 76 IGGGKKKDFDD----ANVVVAtYQSLSNLAEEEKDLFDQFGLLIVDEAH 120
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
208-332 |
3.58e-04 |
|
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: 41.42 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 208 FSVIKGEDKEKFIFDYLENNIGKVGIIYTSTRKEAESLY-----NKINKKGYKVGV----------YHAGLNDEERKRTQ 272
Cdd:cd18802 4 VVIPKLQKLIEILREYFPKTPDFRGIIFVERRATAVVLSrllkeHPSTLAFIRCGFligrgnssqrKRSLMTQRKQKETL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 273 EDFSFDNIEIIVATNAFGMGIDKSNVRFVIHHNIPKNMEAYYQEAGRAGRdgEESECILL 332
Cdd:cd18802 84 DKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARA--PNSKYILM 141
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
7-140 |
4.05e-04 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain] Cd Length: 189 Bit Score: 41.93 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 7 NLLKKHFGYNEFrKAQEKVIESILKKEDTVAIMPTGAGKSICYQIPALIF---GGVTVVISPLISLMKDQVDSLKEVG-- 81
Cdd:cd17924 8 EFFKKKTGFPPW-GAQRTWAKRLLRGKSFAIIAPTGVGKTTFGLATSLYLaskGKRSYLIFPTKSLVKQAYERLSKYAek 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489584874 82 ----IEATYINSSLNNLEIEERIFNAREGLYKlIYIAPERLESDSFvRSLNNLNIDLVAVDEA 140
Cdd:cd17924 87 agveVKILVYHSRLKKKEKEELLEKIEKGDFD-ILVTTNQFLSKNF-DLLSNKKFDFVFVDDV 147
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
4-64 |
4.99e-04 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 43.37 E-value: 4.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489584874 4 GAKNLLKKHFGYNEFRKAQEKVIESILK--KEDTVAIM--PTGAGKSICYQIPALIF---GGVTVVIS 64
Cdd:COG1199 1 ADDGLLALAFPGFEPRPGQREMAEAVARalAEGRHLLIeaGTGTGKTLAYLVPALLAareTGKKVVIS 68
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
17-324 |
2.93e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 41.02 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 17 EFRKAQEKVIESILKKEDTVAIMPTGAGKS-ICYQ--IPALIFGGVTVVISPLISLMKDQVDSLKEVGIEATYINSSLNN 93
Cdd:PRK01172 22 ELYDHQRMAIEQLRKGENVIVSVPTAAGKTlIAYSaiYETFLAGLKSIYIVPLRSLAMEKYEELSRLRSLGMRVKISIGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 94 LEiEERIFNAReglYKLIYIAPERLES----DSFVrsLNnlNIDLVAVDEAHCVsqwGHDFR-PSYTKISSFIRKLSKRP 168
Cdd:PRK01172 102 YD-DPPDFIKR---YDVVILTSEKADSlihhDPYI--IN--DVGLIVADEIHII---GDEDRgPTLETVLSSARYVNPDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 169 IVTAFTATatetvrydILNSLELQ---DPKVFVTGFDRENLSFSVI------------KGEDKEKFIFDYLENNiGKVgI 233
Cdd:PRK01172 171 RILALSAT--------VSNANELAqwlNASLIKSNFRPVPLKLGILyrkrlildgyerSQVDINSLIKETVNDG-GQV-L 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 234 IYTSTRKEAE---------------------------SLYNKINKKGykVGVYHAGLNDEERKRTQEDFSFDNIEIIVAT 286
Cdd:PRK01172 241 VFVSSRKNAEdyaemliqhfpefndfkvssennnvydDSLNEMLPHG--VAFHHAGLSNEQRRFIEEMFRNRYIKVIVAT 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 489584874 287 NAFGMGIDKSnVRFVIHHNIPK----------NMEAyYQEAGRAGRDG 324
Cdd:PRK01172 319 PTLAAGVNLP-ARLVIVRDITRygnggirylsNMEI-KQMIGRAGRPG 364
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
6-65 |
4.10e-03 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 39.21 E-value: 4.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489584874 6 KNLLKKhfGYNEFRKAQEKVIESILKKEDTVAIMPTGAGKSICYQIPAL--------IFGGVTVVISP 65
Cdd:cd17959 14 RAIKKK--GYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIeklkahspTVGARALILSP 79
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
22-54 |
6.04e-03 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 38.58 E-value: 6.04e-03
10 20 30
....*....|....*....|....*....|...
gi 489584874 22 QEKVIESILKKEDTVAIMPTGAGKSICYQIPAL 54
Cdd:cd00268 17 QAQAIPLILSGRDVIGQAQTGSGKTLAFLLPIL 49
|
|
| Glyco_hydro_57 |
pfam03065 |
Glycosyl hydrolase family 57; This family includes alpha-amylase (EC:3.2.1.1), ... |
63-247 |
6.07e-03 |
|
Glycosyl hydrolase family 57; This family includes alpha-amylase (EC:3.2.1.1), 4--glucanotransferase (EC:2.4.1.-) and amylopullulanase enzymes.
Pssm-ID: 397267 [Multi-domain] Cd Length: 293 Bit Score: 39.27 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 63 ISPLISLMKDQVDSLK-EVGIEATY--INSSLNNLE-IEERIFNAREGLYKLI------YIAPERLESDSFVRSLNNLNI 132
Cdd:pfam03065 87 NPEVLELFRELAESGQvELLTSPYYhpLLPLLPDSEdFIAQVKMARELYREYFgveprgFWLPELAYSPDILKILAELGF 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489584874 133 DLVAVDEAHCVSQWGHDFRPSYTK---ISSFIR--KLSK----RPIVTAFTATATETVRYdiLNSLELQDPKVFVTGFDR 203
Cdd:pfam03065 167 EYVFTDGYAFILAGLSPYRPYYIEnggLAVFFRnyELSDdigfRFSAKSWEQAADKFANW--LKGIEGEQSDVVLIFLDG 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489584874 204 ENLsfsvikGEDKEKFIFDYLEN---NIGKVGIIYTSTRKEAESLYN 247
Cdd:pfam03065 245 ETF------GHWPETGILDFLRWlpeELEKHGIIELVTPSEAIKRFK 285
|
|
| |
