|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
2-470 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 798.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 2 TPLQALHKYFGYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAVLLPGLTIVISPLIALMKDQVDSLNLNGIP 81
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 82 AAFLNSSQTPDEQRNITDRLKSNQIKLLYLAPERLFGTENklIDFLKSLPVSLFAIDEAHCISHWGHDFRPEYLMLAHLK 161
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRF--LELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 162 DHFKNIPVIALTATADKLTQKDILEKLNLRQPSVFISSFNRENITYRVTPK--NKSFNQLLNFLDGRRDDSGIIYCLSRK 239
Cdd:COG0514 162 ERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGGSGIVYCLSRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 240 STEALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGINKSNVRYVVHMDMPKNIEGYYQETGRA 319
Cdd:COG0514 242 KVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 320 GRDGLPSDAMLYYSPGDVIKLKNFVTL-DNNEEQSQILFDKLNDMAAYCELHTCRRKYLLNYFDEQATDNCGSCDICLSE 398
Cdd:COG0514 322 GRDGLPAEALLLYGPEDVAIQRFFIEQsPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLGP 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1928617818 399 FKKFDGTLIAQKALSAVARLNQRFGLGYVVDFLRGSKSEKIRDE-HKQLKTYGVGADISKAQWQRYLRELNAH 470
Cdd:COG0514 402 PETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFgHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
5-588 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273594 [Multi-domain] Cd Length: 591 Bit Score: 765.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 5 QALHKYFGYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAVLLPGLTIVISPLIALMKDQVDSLNLNGIPAAF 84
Cdd:TIGR01389 3 QVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 85 LNSSQTPDEQRNITDRLKSNQIKLLYLAPERLfgTENKLIDFLKSLPVSLFAIDEAHCISHWGHDFRPEYLMLAHLKDHF 164
Cdd:TIGR01389 83 LNSTLSAKEQQDIEKALVNGELKLLYVAPERL--EQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 165 KNIPVIALTATADKLTQKDILEKLNLRQPSVFISSFNRENITYRVTPKNKSFNQLLNFLDGRRDDSGIIYCLSRKSTEAL 244
Cdd:TIGR01389 161 PQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 245 AADLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGINKSNVRYVVHMDMPKNIEGYYQETGRAGRDGL 324
Cdd:TIGR01389 241 AERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 325 PSDAMLYYSPGDVIKLKNFVTLDN-NEEQSQILFDKLNDMAAYCELHTCRRKYLLNYFDEQATDNCGSCDICLSEFKKFD 403
Cdd:TIGR01389 321 PAEAILLYSPADIALLKRRIEQSEaDDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPKSYD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 404 GTLIAQKALSAVARLNQRFGLGYVVDFLRGSKSEKIRD-EHKQLKTYGVGADISKAQWQRYLRELNAHGYLQITDDAYPI 482
Cdd:TIGR01389 401 ATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQkGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIYIG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 483 VKLTDKSEAVLKGQQKVELTEAQII-EEKTEE----ALPFEASLFDQLKVVRLNFATMENLPAYVILSDATLLEMATYLP 557
Cdd:TIGR01389 481 LQLTEAARKVLKNEVEVLLRPFKVVaKEKTRVqknlSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKRP 560
|
570 580 590
....*....|....*....|....*....|.
gi 1928617818 558 QSMDELRHISGFGDVKLARYGREFLEVIKPY 588
Cdd:TIGR01389 561 ATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
1-586 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 700.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 1 MTPLQALHKYFGYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAVLLPGLTIVISPLIALMKDQVDSLNLNGI 80
Cdd:PRK11057 11 SLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 81 PAAFLNSSQTPDEQRNITDRLKSNQIKLLYLAPERLFgTENkLIDFLKSLPVSLFAIDEAHCISHWGHDFRPEYLMLAHL 160
Cdd:PRK11057 91 AAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLM-MDN-FLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 161 KDHFKNIPVIALTATADKLTQKDILEKLNLRQPSVFISSFNRENITYRVTPKNKSFNQLLNFLDGRRDDSGIIYCLSRKS 240
Cdd:PRK11057 169 RQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 241 TEALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGINKSNVRYVVHMDMPKNIEGYYQETGRAG 320
Cdd:PRK11057 249 VEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 321 RDGLPSDAMLYYSPGDVIKLKNFVTLDNNEEQSQILFDKLNDMAAYCELHTCRRKYLLNYFDEQATDNCGSCDICLSEFK 400
Cdd:PRK11057 329 RDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 401 KFDGTLIAQKALSAVARLNQRFGLGYVVDFLRGSKSEKIRDE-HKQLKTYGVGADISKAQWQRYLRELNAHGYLQITDDA 479
Cdd:PRK11057 409 QYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYgHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQ 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 480 YPIVKLTDKSEAVLKGQQKVELTEAQIIEEKTEEALP-----FEASLFDQLKVVRLNFATMENLPAYVILSDATLLEMAT 554
Cdd:PRK11057 489 HSALQLTEAARPVLRGEVSLQLAVPRIVALKPRAMQKsfggnYDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAE 568
|
570 580 590
....*....|....*....|....*....|..
gi 1928617818 555 YLPQSMDELRHISGFGDVKLARYGREFLEVIK 586
Cdd:PRK11057 569 QMPITASEMLSVNGVGQRKLERFGKPFMALIR 600
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
5-454 |
0e+00 |
|
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: 574.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 5 QALHKYFGYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAVLLPGLTIVISPLIALMKDQVDSLNLNGIPAAF 84
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 85 LNSSQTPDEQRNITDRLKSNQIKLLYLAPERLFGTENKLIDFLKSLPVSLFAIDEAHCISHWGHDFRPEYLMLAHLKDHF 164
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 165 KNIPVIALTATADKLTQKDILEKLNLRQPSVFISSFNRENITYRVTPK-NKSFNQLLNFLDGR-RDDSGIIYCLSRKSTE 242
Cdd:TIGR00614 161 PNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKtPKILEDLLRFIRKEfEGKSGIIYCPSRKKVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 243 ALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGINKSNVRYVVHMDMPKNIEGYYQETGRAGRD 322
Cdd:TIGR00614 241 QVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 323 GLPSDAMLYYSPGDVIKLKNFVTLDNNEEQSQILFDKLNDMAAYCELHTCRRKYLLNYFDEQATDN----------CGSC 392
Cdd:TIGR00614 321 GLPSECHLFYAPADMNRLRRLLMEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFNKsfcimgtekcCDNC 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928617818 393 DICL------SEFKKFDGTLIAQKALSAVARLNQRFGLGYVVDFLRGSKSEKIRD-EHKQLKTYGVGAD 454
Cdd:TIGR00614 401 CKRLdyktkdVTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDgGFRKHSLYGRGKD 469
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
9-585 |
2.40e-124 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 398.89 E-value: 2.40e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 9 KYFGYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAVLLPGLTIVISPLIALMKDQVDSLNLNGIPAAFLNSS 88
Cdd:PLN03137 454 KVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAG 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 89 QTPDEQRNITDRLKSN--QIKLLYLAPERLFGTENkLIDFLKSLP----VSLFAIDEAHCISHWGHDFRPEYLMLAHLKD 162
Cdd:PLN03137 534 MEWAEQLEILQELSSEysKYKLLYVTPEKVAKSDS-LLRHLENLNsrglLARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 163 HFKNIPVIALTATADKLTQKDILEKLNLRQPSVFISSFNRENITYRVTPK-NKSFNQLLNFL-DGRRDDSGIIYCLSRKS 240
Cdd:PLN03137 613 KFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKtKKCLEDIDKFIkENHFDECGIIYCLSRMD 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 241 TEALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGINKSNVRYVVHMDMPKNIEGYYQETGRAG 320
Cdd:PLN03137 693 CEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAG 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 321 RDGLPSDAMLYYSPGDVIKLKNFVTlDNNEEQSQ-------------IL---FDKLNDMAAYCELHT-CRRKYLLNYFDE 383
Cdd:PLN03137 773 RDGQRSSCVLYYSYSDYIRVKHMIS-QGGVEQSPmamgynrmassgrILetnTENLLRMVSYCENEVdCRRFLQLVHFGE 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 384 Q-ATDNCG-SCDICLS--EFKKFDGTLIAQKALSAVARLNQRFGLGYVVDFLRGSKSEKI-RDEHKQLKTYGVGADISKA 458
Cdd:PLN03137 852 KfDSTNCKkTCDNCSSskSLIDKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVkKHRHETLSLHGAGKHLSKG 931
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 459 QWQRYLRELNAHGYLQ---ITDDAY----PIVKLTD-KSEAVLKGQQKVEL---TEAQIIEEKTEEALP----------- 516
Cdd:PLN03137 932 EASRILHYLVTEDILAedvKKSDLYgsvsSLLKVNEsKAYKLFSGGQTIIMrfpSSVKASKPSKFEATPakgpltsgkqs 1011
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 517 ---------------FEASLFDQLKVVRLNFA--TMENLPAYVILSDATLLEMATYLPQSMDELRHISGFGDVKLARYGR 579
Cdd:PLN03137 1012 tlpmatpaqppvdlnLSAILYTALRKLRTALVkeAGDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKYGD 1091
|
....*.
gi 1928617818 580 EFLEVI 585
Cdd:PLN03137 1092 RLLETI 1097
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
4-201 |
2.26e-104 |
|
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: 316.78 E-value: 2.26e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 4 LQALHKYFGYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAVLLPGLTIVISPLIALMKDQVDSLNLNGIPAA 83
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 84 FLNSSQTPDEQRNITDRLKSNQIKLLYLAPERLfgTENKLIDFLKSLP----VSLFAIDEAHCISHWGHDFRPEYLMLAH 159
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERL--LSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1928617818 160 LKDHFKNIPVIALTATADKLTQKDILEKLNLRQPSVFISSFN 201
Cdd:cd17920 159 LRRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
4-196 |
1.24e-77 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 247.17 E-value: 1.24e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 4 LQALHKYFGYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAVLL----PGLTIVISPLIALMKDQVDSLNlNG 79
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLrrrgPGLTLVVSPLIALMKDQVDALP-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 80 IPAAFLNSSQTPDEQRNITDRLKSNQIKLLYLAPERLFGTENKLIdFLKSLPVSLFAIDEAHCISHWGHDFRPEYLMLAH 159
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFREL-LRQTPPISLLVVDEAHCISEWSHNFRPDYLRLCR 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1928617818 160 -LKDHFKNIPVIALTATADKLTQKDILEKLNLRQPSVF 196
Cdd:cd18018 159 vLRELLGAPPVLALTATATKRVVEDIASHLGIPESGVV 196
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
4-201 |
1.16e-67 |
|
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: 221.24 E-value: 1.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 4 LQALHKYFGYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAVLLPGLTIVISPLIALMKDQVDSLNLNGIPAA 83
Cdd:cd18016 6 MKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 84 FLNSSQTPDEQRNITDRLKSNQ--IKLLYLAPERLfGTENKLIDFLKSLP----VSLFAIDEAHCISHWGHDFRPEYLML 157
Cdd:cd18016 86 YLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKI-SASNRLISTLENLYerklLARFVIDEAHCVSQWGHDFRPDYKRL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1928617818 158 AHLKDHFKNIPVIALTATADKLTQKDILEKLNLRQPSVFISSFN 201
Cdd:cd18016 165 NMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
6-201 |
8.70e-65 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 213.77 E-value: 8.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 6 ALHKYFGYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAVLLPGLTIVISPLIALMKDQVDSLNLNGIPAAFL 85
Cdd:cd18015 9 TLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATML 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 86 NSSQTPDEQRNITDRL--KSNQIKLLYLAPERLFGTE---NKLIDFLKSLPVSLFAIDEAHCISHWGHDFRPEYLMLAHL 160
Cdd:cd18015 89 NASSSKEHVKWVHAALtdKNSELKLLYVTPEKIAKSKrfmSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRPDYKKLGIL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1928617818 161 KDHFKNIPVIALTATADKLTQKDILEKLNLRQPSVFISSFN 201
Cdd:cd18015 169 KRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
4-201 |
5.81e-63 |
|
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: 208.09 E-value: 5.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 4 LQALHKYFGYSEFRHEQETIIGRVL-NGHDVMALMPTGGGKSLCYQLPAVLLPGLTIVISPLIALMKDQVDSLNLNGIPA 82
Cdd:cd18017 1 LNALNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 83 AFLNSSQtpdeQRNITDRLKSNQIKLLYLAPErlFGTENK-LIDFLkSLPVSLFAIDEAHCISHWGHDFRPEYLMLAHLK 161
Cdd:cd18017 81 CFLGSAQ----SQNVLDDIKMGKIRVIYVTPE--FVSKGLeLLQQL-RNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1928617818 162 DHFKNIPVIALTATADKLTQKDILEKLNLRQPSVFISSFN 201
Cdd:cd18017 154 NRLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
202-332 |
7.85e-58 |
|
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: 192.04 E-value: 7.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 202 RENITYRVTPKNKSFNQLLNFLDGRR---DDSGIIYCLSRKSTEALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDE 278
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVehlGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1928617818 279 VKIMVATIAFGMGINKSNVRYVVHMDMPKNIEGYYQETGRAGRDGLPSDAMLYY 332
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
4-198 |
1.07e-57 |
|
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: 194.61 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 4 LQALHKYFGYSEFRHE-QETIIGRVLNGH-DVMALMPTGGGKSLCYQLPAVLLPGLTIVISPLIALMKDQVDSLNLNGIP 81
Cdd:cd18014 1 RSTLKKVFGHSDFKSPlQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 82 AAFLNSSQTPDEQRNITDRLKSN--QIKLLYLAPE--------RLFGTENKlidflKSLpVSLFAIDEAHCISHWGHDFR 151
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEkpQTKFLYITPEmaatssfqPLLSSLVS-----RNL-LSYLVVDEAHCVSQWGHDFR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1928617818 152 PEYLMLAHLKDHFKNIPVIALTATADKLTQKDILEKLNLRQPSVFIS 198
Cdd:cd18014 155 PDYLRLGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKPVAIFK 201
|
|
| DpdF |
NF041063 |
protein DpdF; |
38-337 |
4.77e-43 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 167.01 E-value: 4.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 38 PTGGGKSLCYQLPAVLLP---GLTIVISPLIALMKDQ----VDSLNLNGIPA----AFlnSSQTPDEQRN-ITDRLKSNQ 105
Cdd:NF041063 166 PTGSGKSLVAQAPALLASrqgGLTLVVVPTVALAIDQerraRELLRRAGPDLggplAW--HGGLSAEERAaIRQRIRDGT 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 106 IKLLYLAPE----RLFGT-----ENKLIdflkslpvSLFAIDEAHCISHWGHDFRPEYLMLAHL----------KDHFKn 166
Cdd:NF041063 244 QRILFTSPEsltgSLRPAlfdaaEAGLL--------RYLVVDEAHLVDQWGDGFRPEFQLLAGLrrsllrlapsGRPFR- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 167 ipVIALTATadkLTQKDI--LEKLnLRQPSVFI---SSFNRENITYRV----TPKNKsFNQLLN--------Fldgrrdd 229
Cdd:NF041063 315 --TLLLSAT---LTESTLdtLETL-FGPPGPFIvvsAVQLRPEPAYWVakcdSEEER-RERVLEalrhlprpL------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 230 sgIIYCLSRKSTEALAADLKDEGYSAeayhAGLDH-ATKARNQEAFLR----DEVKIMVATIAFGMGINKSNVRYVVHMD 304
Cdd:NF041063 381 --ILYVTKVEDAEAWLQRLRAAGFRR----VALFHgDTPDAERERLIEqwreNELDIVVATSAFGLGMDKSDVRTVIHAC 454
|
330 340 350
....*....|....*....|....*....|...
gi 1928617818 305 MPKNIEGYYQETGRAGRDGLPSDAMLYYSPGDV 337
Cdd:NF041063 455 VPETLDRFYQEVGRGGRDGKASLSLLIYTPDDL 487
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
398-503 |
6.35e-41 |
|
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: 144.99 E-value: 6.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 398 EFKKFDGTLIAQKALSAVARLNQRFGLGYVVDFLRGSKSEKIRD-EHKQLKTYGVGADISKAQWQRYLRELNAHGYLQIT 476
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQlGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*..
gi 1928617818 477 DDAYPIVKLTDKSEAVLKGQQKVELTE 503
Cdd:pfam09382 81 IEFYSVLKLTPKAREVLKGEEKVMLRV 107
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
403-493 |
8.61e-37 |
|
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: 132.60 E-value: 8.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 403 DGTLIAQKALSAVARLNQRFGLGYVVDFLRGSKSEKIRD-EHKQLKTYGVGADISKAQWQRYLRELNAHGYLQITDDAYP 481
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQkGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 1928617818 482 IVKLTDKSEAVL 493
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 ... |
618-705 |
5.26e-26 |
|
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: 102.20 E-value: 5.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 618 TQKESLNLFKAGKSIQQIAAERSLSPMTVEGHLTLFVQTGEL-EVTEFVDQGKIPAIQDAIESYGPERLAPLKEVLGDNY 696
Cdd:pfam14493 1 SAEITLELYKEGLSIEEIAEERGLKESTIEGHLAELIEAGEPvDIERLVSEEEQKEILDAIEKLGSESLKPIKEALPEEI 80
|
....*....
gi 1928617818 697 SYTEIKAVV 705
Cdd:pfam14493 81 SYFEIRLVL 89
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
20-178 |
9.30e-26 |
|
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: 104.25 E-value: 9.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 20 QETIIGRVLNGHDVMALMPTGGGKSLCYQLPAV------LLPGLTIVISPLIALMKDQVDSL-NLNGIPAAFLNSSQTPD 92
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELkKLGKGLGLKVASLLGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 93 EQRNITDRLKSNQIklLYLAPERLFgtenKLIDFLKSLP-VSLFAIDEAHCISHWGhdFRPEY-LMLAHLKdhfKNIPVI 170
Cdd:pfam00270 84 SRKEQLEKLKGPDI--LVGTPGRLL----DLLQERKLLKnLKLLVLDEAHRLLDMG--FGPDLeEILRRLP---KKRQIL 152
|
....*...
gi 1928617818 171 ALTATADK 178
Cdd:pfam00270 153 LLSATLPR 160
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
242-323 |
1.41e-21 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 89.19 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 242 EALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGINKSNVRYVVHMDMPKNIEGYYQETGRAGR 321
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1928617818 322 DG 323
Cdd:smart00490 81 AG 82
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
9-208 |
1.95e-21 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 92.94 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 9 KYFGYSEFRHEQETIIGRVLNG-HDVMALMPTGGGKSLCYQLPAVLL-----PGLTIVISPLIALMKDQVDSL-----NL 77
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELkklgpSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 78 NGIPAAFLNSSQTPDEQRnitdRLKSNQIKLLYLAPERLFgtENKLIDFLKSLPVSLFAIDEAHCISHWGhdFRPEYLML 157
Cdd:smart00487 82 GLKVVGLYGGDSKREQLR----KLESGKTDILVTTPGRLL--DLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1928617818 158 ahLKDHFKNIPVIALTATADKLTQKDIleKLNLRQPSVFISSFNR-ENITYR 208
Cdd:smart00487 154 --LKLLPKNVQLLLLSATPPEEIENLL--ELFLNDPVFIDVGFTPlEPIEQF 201
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
4-341 |
5.75e-20 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 92.90 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 4 LQALHKyFGYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAV--LLPGL-----TIVISP---LIALMKDQVD 73
Cdd:COG0513 14 LKALAE-LGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPtreLALQVAEELR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 74 SLnlngipAAFLN---------SSQTPdeqrnitdrlksnQIKLLYLAPERLFGTENKLIDFLKSLPVSLFAI-----DE 139
Cdd:COG0513 93 KL------AKYLGlrvatvyggVSIGR-------------QIRALKRGVDIVVATPGRLLDLIERGALDLSGVetlvlDE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 140 AhcishwghD------FRPEylmlahLKDHFKNIPVIALT----ATADKlTQKDILEKLnLRQPsVFISsFNRENIT--- 206
Cdd:COG0513 154 A--------DrmldmgFIED------IERILKLLPKERQTllfsATMPP-EIRKLAKRY-LKNP-VRIE-VAPENATaet 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 207 -----YRVTPKNKsFNQLLNFLDGRRDDSGIIYCLSRKSTEALAADLKDEGYSAEAYHAGLDHatKARNQ--EAFLRDEV 279
Cdd:COG0513 216 ieqryYLVDKRDK-LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQ--GQRERalDAFRNGKI 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1928617818 280 KIMVAT-IAfGMGINKSNVRYVVHMDMPKNIEgYYQ----ETGRAGRDGLpsdAMLYYSPGDVIKLK 341
Cdd:COG0513 293 RVLVATdVA-ARGIDIDDVSHVINYDLPEDPE-DYVhrigRTGRAGAEGT---AISLVTPDERRLLR 354
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
334-396 |
3.28e-19 |
|
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
Pssm-ID: 465031 [Multi-domain] Cd Length: 66 Bit Score: 81.95 E-value: 3.28e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1928617818 334 PGDVIKLKNFVTLDN-NEEQSQILFDKLNDMAAYCE-LHTCRRKYLLNYFDEQA-TDNCGSCDICL 396
Cdd:pfam16124 1 YQDVVRLRFLIEQSEaDEERKEVELQKLQAMVAYCEnTTDCRRKQLLRYFGEEFdSEPCGNCDNCL 66
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
216-323 |
4.37e-19 |
|
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: 83.03 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 216 FNQLLNFLDGRRDDSGIIYCLSRKSTEA--LaadLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGIN 293
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLEAelL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 1928617818 294 KSNVRYVVHMDMPKNIEGYYQETGRAGRDG 323
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
518-585 |
5.26e-19 |
|
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: 81.43 E-value: 5.26e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1928617818 518 EASLFDQLKVVRLNFATMENLPAYVILSDATLLEMATYLPQSMDELRHISGFGDVKLARYGREFLEVI 585
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
207-324 |
7.99e-19 |
|
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: 82.94 E-value: 7.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 207 YRVTPKNKSFNQLLNFLDGRRDDSGIIYCLSRKSTEALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATI 286
Cdd:cd18787 6 VVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1928617818 287 AFGMGINKSNVRYVVHMDMPKNIEGYYQ---ETGRAGRDGL 324
Cdd:cd18787 86 VAARGLDIPGVDHVINYDLPRDAEDYVHrigRTGRAGRKGT 126
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
521-589 |
5.07e-15 |
|
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: 70.40 E-value: 5.07e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1928617818 521 LFDQLKVVRLNFATMENLPAYVILSDATLLEMATYLPQSMDELRHISGFGDVKLARYGREFLEVIKPYC 589
Cdd:smart00341 7 LLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEAS 75
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
30-175 |
1.20e-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: 71.67 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 30 GHDVMALMPTGGGKSLCYQLPAVLL----PGLTIVISPLIALMKDQ---VDSLNLNGIPAAFLNSSQTPDEQRNITDRLK 102
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEEREKNKLGDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1928617818 103 snqiKLLYLAPERLFgteNKL--IDFLKSLPVSLFAIDEAHCISHWGHDFRPEYlmLAHLKDHFKNIPVIALTAT 175
Cdd:cd00046 81 ----DIIIATPDMLL---NLLlrEDRLFLKDLKLIIVDEAHALLIDSRGALILD--LAVRKAGLKNAQVILLSAT 146
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
16-323 |
1.59e-12 |
|
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: 71.02 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 16 FRHeQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAV--LL--PGLT-IVISPLIALMKDQVDSLN------LNGIPAAF 84
Cdd:COG1205 58 YSH-QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLedPGATaLYLYPTKALARDQLRRLRelaealGLGVRVAT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 85 LNSSQTPDEQRNITDR---LKSN--QIKLLYLAPERLFgtenklIDFLKSLpvSLFAIDEAHCI-----SHWGHDFRpey 154
Cdd:COG1205 137 YDGDTPPEERRWIREHpdiVLTNpdMLHYGLLPHHTRW------ARFFRNL--RYVVIDEAHTYrgvfgSHVANVLR--- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 155 lMLAHLKDHFKNIPV-IALTAT-------ADKLTQKD---ILEKLNLRQPSVFISSFNRENITYRVTPKNKSFNQLLNFL 223
Cdd:COG1205 206 -RLRRICRHYGSDPQfILASATignpaehAERLTGRPvtvVDEDGSPRGERTFVLWNPPLVDDGIRRSALAEAARLLADL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 224 --DGRRddsGIIYCLSRKSTEALAADLKDE------GYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGINKS 295
Cdd:COG1205 285 vrEGLR---TLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIG 361
|
330 340
....*....|....*....|....*...
gi 1928617818 296 NVRYVVHMDMPKNIEGYYQETGRAGRDG 323
Cdd:COG1205 362 GLDAVVLAGYPGTRASFWQQAGRAGRRG 389
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
4-331 |
2.13e-11 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 67.18 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 4 LQALHKyFGYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAV--LLPGL----TIVISPLIALMKDQVDSLN- 76
Cdd:PRK11634 18 LEALND-LGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnLDPELkapqILVLAPTRELAVQVAEAMTd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 77 ----LNGIPAAFLNSSQTPDEQrnitdrlksnqIKLLYLAPERLFGTENKLIDFLKSLPVSL-----FAIDEAHCISHWG 147
Cdd:PRK11634 97 fskhMRGVNVVALYGGQRYDVQ-----------LRALRQGPQIVVGTPGRLLDHLKRGTLDLsklsgLVLDEADEMLRMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 148 HDFRPEYLMLAHLKDHFKNIPVIALTATADKLTQKDILEKLNLR-QPSVFissfNRENI--TYRVTPKNKSFNQLLNFLD 224
Cdd:PRK11634 166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRiQSSVT----TRPDIsqSYWTVWGMRKNEALVRFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 225 GRRDDSGIIYCLSRKSTEALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGINKSNVRYVVHMD 304
Cdd:PRK11634 242 AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYD 321
|
330 340
....*....|....*....|....*..
gi 1928617818 305 MPKNIEGYYQETGRAGRDGLPSDAMLY 331
Cdd:PRK11634 322 IPMDSESYVHRIGRTGRAGRAGRALLF 348
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
11-324 |
1.58e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 64.15 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 11 FGYSEFRHEQETIIGR-VLNGHDVMALMPTGGGKSLCYQLPAV--LLPGLTIV-ISPLIALMKDQVDSLNlngipAAF-- 84
Cdd:COG1204 18 RGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLRALASEKYREFK-----RDFee 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 85 --LNSSQTPDEQRNITDRLKSNQIklLYLAPER---LFGTENKLIDflkslPVSLFAIDEAHCIshwGHDFR-PEY-LML 157
Cdd:COG1204 93 lgIKVGVSTGDYDSDDEWLGRYDI--LVATPEKldsLLRNGPSWLR-----DVDLVVVDEAHLI---DDESRgPTLeVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 158 AHLKDHFKNIPVIALTATADKLtqKDILEKLNlrqpSVFISSfnreniTYRVTPKNKSF--NQLLNFLDGRR-------- 227
Cdd:COG1204 163 ARLRRLNPEAQIVALSATIGNA--EEIAEWLD----AELVKS------DWRPVPLNEGVlyDGVLRFDDGSRrskdptla 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 228 ------DDSG--IIYCLSRKSTEALAADLKDE------------------------GYSAEAY-------------HAGL 262
Cdd:COG1204 231 laldllEEGGqvLVFVSSRRDAESLAKKLADElkrrltpeereeleelaeellevsEETHTNEkladclekgvafhHAGL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 263 DHATKARNQEAFLRDEVKIMVAT--IAfgMGINKSnVRYVV----HMDMPKNIEG--YYQETGRAGRDGL 324
Cdd:COG1204 311 PSELRRLVEDAFREGLIKVLVATptLA--AGVNLP-ARRVIirdtKRGGMVPIPVleFKQMAGRAGRPGY 377
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
15-303 |
1.75e-10 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 64.28 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 15 EFRHEQETIIGRVL-----NGHDVMALMPTGGGKSL----CYQlpAVLLPGLTIVISPLIALMKDQVDSLnlngipAAFL 85
Cdd:COG1061 80 ELRPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEEL------RRFL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 86 NSSQTPDEQRNITDRLksnqikllylaperLFGTENKLI--DFLKSLP--VSLFAIDEAHcishwgHDFRPEYLMLAhlk 161
Cdd:COG1061 152 GDPLAGGGKKDSDAPI--------------TVATYQSLArrAHLDELGdrFGLVIIDEAH------HAGAPSYRRIL--- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 162 DHFKNIPVIALTATADKLTQKDILEKL-----------------NLRQPSVFI--SSFNRENITYRVtpKNKSFNQLLNF 222
Cdd:COG1061 209 EAFPAAYRLGLTATPFRSDGREILLFLfdgivyeyslkeaiedgYLAPPEYYGirVDLTDERAEYDA--LSERLREALAA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 223 LDGR-------------RDDSGIIYCLSRKSTEALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFG 289
Cdd:COG1061 287 DAERkdkilrellrehpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLN 366
|
330
....*....|....
gi 1928617818 290 MGINKSNVRYVVHM 303
Cdd:COG1061 367 EGVDVPRLDVAILL 380
|
|
| YpbB |
COG4955 |
Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown]; |
610-711 |
3.20e-10 |
|
Uncharacterized conserved protein YpbB, contains C-terminal HTH domain [Function unknown];
Pssm-ID: 443982 [Multi-domain] Cd Length: 346 Bit Score: 62.34 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 610 PRSEKVSNTQKESLNLFKAGKSIQQIAAERSLSPMTVEGHL---TLFVQtgELEVTEFVDQGKIPAIQDAIESYGPERLA 686
Cdd:COG4955 243 LKESLLTQSAQKTYQLLQQGLSLEEIAQIRRLKLSTIEDHLveiAIKDP--DFPIEPFVNKEDQQEIIQAIEKLGTWKLK 320
|
90 100
....*....|....*....|....*
gi 1928617818 687 PLKEVLGDnYSYTEIKAVVSWLKRE 711
Cdd:COG4955 321 EIKEQLPD-LSYFQIRLVLAKRERE 344
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
20-331 |
4.43e-09 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 59.42 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 20 QETIIGRVLNGHDVMALMPTGGGKSLCYQLPAVLL-------------PGLTIVISP---LIALMKDQVDSLNlNGIP-- 81
Cdd:PLN00206 148 QMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcctirsghpseqrNPLAMVLTPtreLCVQVEDQAKVLG-KGLPfk 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 82 -AAFLNSSQTPdeqrnitdrlksNQIKLLYLAPERLFGTENKLIDFLKSLPVSL-----FAIDEAHCISHWGhdFRPEYL 155
Cdd:PLN00206 227 tALVVGGDAMP------------QQLYRIQQGVELIVGTPGRLIDLLSKHDIELdnvsvLVLDEVDCMLERG--FRDQVM 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 156 MLahlkdhFKNIP---VIALTATadkLTQKdiLEKL--NLRQPSVFIS--SFNRENITYR-----VTPKNKSfNQLLNFL 223
Cdd:PLN00206 293 QI------FQALSqpqVLLFSAT---VSPE--VEKFasSLAKDIILISigNPNRPNKAVKqlaiwVETKQKK-QKLFDIL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 224 DGRRD--DSGIIYCLSRKSTEALA-ADLKDEGYSAEAYHAglDHATKAR--NQEAFLRDEVKIMVATIAFGMGINKSNVR 298
Cdd:PLN00206 361 KSKQHfkPPAVVFVSSRLGADLLAnAITVVTGLKALSIHG--EKSMKERreVMKSFLVGEVPVIVATGVLGRGVDLLRVR 438
|
330 340 350
....*....|....*....|....*....|...
gi 1928617818 299 YVVHMDMPKNIEGYYQETGRAGRDGLPSDAMLY 331
Cdd:PLN00206 439 QVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVF 471
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
28-334 |
4.74e-09 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 59.40 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 28 LNGHDVMALMPTGGGKSLCYQLPAV--------LLPG---LTIVISPLIALMKDQVDSLNLNGIPAAFLNSSQ---TPde 93
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAIvhinaqplLRYGdgpIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAyggVP-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 94 qrnitdrlKSNQIKLLYLAPERLFGTENKLIDFLKS-----LPVSLFAIDEAHCISHWGHD---------FRP--EYLM- 156
Cdd:PTZ00110 243 --------KRGQIYALRRGVEILIACPGRLIDFLESnvtnlRRVTYLVLDEADRMLDMGFEpqirkivsqIRPdrQTLMw 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 157 ----------LAHlkDHFKNIPVIALTATADKLTQKDILEKLNLRQpsvfissfNRENITyrvtpKNKSFNQLLnFLDGr 226
Cdd:PTZ00110 315 satwpkevqsLAR--DLCKEEPVHVNVGSLDLTACHNIKQEVFVVE--------EHEKRG-----KLKMLLQRI-MRDG- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 227 rdDSGIIYCLSRKSTEALAADLKDEGYSAEAYHAgldhaTKARNQEAFLRDEVK-----IMVATIAFGMGINKSNVRYVV 301
Cdd:PTZ00110 378 --DKILIFVETKKGADFLTKELRLDGWPALCIHG-----DKKQEERTWVLNEFKtgkspIMIATDVASRGLDVKDVKYVI 450
|
330 340 350
....*....|....*....|....*....|...
gi 1928617818 302 HMDMPKNIEGYYQETGRAGRDGLPSDAMLYYSP 334
Cdd:PTZ00110 451 NFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
275-332 |
2.03e-08 |
|
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: 51.55 E-value: 2.03e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1928617818 275 LRDEVKIMVATIAFGMGINKSNVRYVVHMDMPKNIEGYYQETGRAGRDG-LPSDAMLYY 332
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
16-141 |
5.91e-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: 53.36 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 16 FRHEQETIiGRVLNGHDVMALMPTGGGKSLCYQLPAV--LL--PGLT-IVISPLIALMKDQVDSLN--LNGIPAAFLNSS 88
Cdd:cd17923 2 YSHQAEAI-EAARAGRSVVVTTGTASGKSLCYQLPILeaLLrdPGSRaLYLYPTKALAQDQLRSLRelLEQLGLGIRVAT 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1928617818 89 QTPDEQRNITDRLKSNQIKLLYLAPERLFGT----ENKLIDFLKSLpvSLFAIDEAH 141
Cdd:cd17923 81 YDGDTPREERRAIIRNPPRILLTNPDMLHYAllphHDRWARFLRNL--RYVVLDEAH 135
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
232-342 |
6.19e-08 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 55.60 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 232 IIYCLSRKSTEALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGINKSNVRYVVHMDMPKNIEG 311
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100 110
....*....|....*....|....*....|.
gi 1928617818 312 YYQETGRAGRDGLPSDAMLYYSPGDVIKLKN 342
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIEQLKE 381
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
529-643 |
6.87e-08 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 55.26 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 529 RLNFATMENLPAYVILSDATLLEMATYLPQSMDELRHISGFGDVKLARYGREFLEVIKpycAANGLTSKVKPKAAKQRQS 608
Cdd:COG0349 220 REREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVA---EALALPEEELPEPPRRLPL 296
|
90 100 110
....*....|....*....|....*....|....*
gi 1928617818 609 KPRSEKVsntqkesLNLFKAgkSIQQIAAERSLSP 643
Cdd:COG0349 297 SPGYKAL-------LKLLKA--LLKEVAEELGVAP 322
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
232-324 |
9.08e-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: 52.17 E-value: 9.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 232 IIYCLSRKSTEALAADLKDEGYsaeaYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGIN--------KSNVRYVVHM 303
Cdd:cd18795 47 LVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKG 122
|
90 100
....*....|....*....|.
gi 1928617818 304 DMPKNIEGYYQETGRAGRDGL 324
Cdd:cd18795 123 YRELSPLEYLQMIGRAGRPGF 143
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
232-330 |
1.01e-07 |
|
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: 51.49 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 232 IIYCLSRKSTEALAADLKDEGYSAE-------AYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGINKSNVRYVVHMD 304
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEGplaskvaSYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*.
gi 1928617818 305 MPKNIEGYYQETGRAGRDGLPSDAML 330
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
12-321 |
4.28e-06 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 49.81 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 12 GYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAVLL------------PGLTIVISP---LIALMKDQVDS-- 74
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHlitrqphakgrrPVRALILTPtreLAAQIGENVRDys 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 75 --LNLNGIpAAFLNSSQTPDEQRnitdrLKSNqIKLLYLAPERLFGTENKliDFLKSLPVSLFAIDEAHCISHWG--HDF 150
Cdd:PRK10590 100 kyLNIRSL-VVFGGVSINPQMMK-----LRGG-VDVLVATPGRLLDLEHQ--NAVKLDQVEILVLDEADRMLDMGfiHDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 151 RPeylMLAHLKDHFKNIpviALTAT-ADKLtqKDILEKLnLRQP-SVFISSFN--RENIT---YRVTPKNKsfNQLLNFL 223
Cdd:PRK10590 171 RR---VLAKLPAKRQNL---LFSATfSDDI--KALAEKL-LHNPlEIEVARRNtaSEQVTqhvHFVDKKRK--RELLSQM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 224 DGRRD-DSGIIYCLSRKSTEALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGINKSNVRYVVH 302
Cdd:PRK10590 240 IGKGNwQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
|
330
....*....|....*....
gi 1928617818 303 MDMPKNIEGYYQETGRAGR 321
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGR 338
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
20-177 |
6.76e-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: 47.26 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 20 QETIIGRVLNGHD-VMALMPTGGGKSLCYQLPAVLL----PGLTIVISPLIALMKDQVDSLNLNGIPAAFLNSSQTPDEQ 94
Cdd:cd17921 6 QREALRALYLSGDsVLVSAPTSSGKTLIAELAILRAlatsGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 95 RNITDRLKSNqikLLYLAPERLFGTENKLIDFLKSlPVSLFAIDEAHCISH------WghdfrpEYLmLAHLKDHFKNIP 168
Cdd:cd17921 86 VNKLLLAEAD---ILVATPEKLDLLLRNGGERLIQ-DVRLVVVDEAHLIGDgergvvL------ELL-LSRLLRINKNAR 154
|
....*....
gi 1928617818 169 VIALTATAD 177
Cdd:cd17921 155 FVGLSATLP 163
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
207-323 |
4.85e-05 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 46.47 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 207 YRVTPKNKSFNQLLNFLDGRRDDSGIIYCLSRKSTEALAADLKDEGYSAeAYHAGlDHATKARNQ--EAFLRDEVKIMVA 284
Cdd:PRK11192 224 YRADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINC-CYLEG-EMVQAKRNEaiKRLTDGRVNVLVA 301
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1928617818 285 TIAFGMGINKSNVRYVVHMDMPKNIEGYYQE---TGRAGRDG 323
Cdd:PRK11192 302 TDVAARGIDIDDVSHVINFDMPRSADTYLHRigrTGRAGRKG 343
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
4-323 |
6.87e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 46.06 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 4 LQALHKyFGYSEFRHEQETIIGRVLNGHDVMALMPTGGGK------SLCYQLPAVLLPG-------LTIVISP----LIA 66
Cdd:PRK01297 99 MHAIHD-LGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKtaafliSIINQLLQTPPPKerymgepRALIIAPtrelVVQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 67 LMKDQVDSLNLNGIPAAFLNSSQTPDEQRNitdRLKSNQIKLLYLAPERLfgtenklIDFLKSLPVSL-----FAIDEAH 141
Cdd:PRK01297 178 IAKDAAALTKYTGLNVMTFVGGMDFDKQLK---QLEARFCDILVATPGRL-------LDFNQRGEVHLdmvevMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 142 CISHWGhdFRPEYLMLAHLKDHFKNIPVIALTATadklTQKDI--LEKLNLRQPSVF------ISSFNRENITYRVTPKN 213
Cdd:PRK01297 248 RMLDMG--FIPQVRQIIRQTPRKEERQTLLFSAT----FTDDVmnLAKQWTTDPAIVeiepenVASDTVEQHVYAVAGSD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 214 KsFNQLLNFLDGRRDDSGIIYCLSRKSTEALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGIN 293
Cdd:PRK01297 322 K-YKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIH 400
|
330 340 350
....*....|....*....|....*....|
gi 1928617818 294 KSNVRYVVHMDMPKNIEGYYQETGRAGRDG 323
Cdd:PRK01297 401 IDGISHVINFTLPEDPDDYVHRIGRTGRAG 430
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
226-321 |
1.10e-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: 43.02 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 226 RRDDSGIIYCLSRKSTEALAADLKDEGYS------AEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFGMGINKSNVRY 299
Cdd:cd18796 36 ERHKSTLVFTNTRSQAERLAQRLRELCPDrvppdfIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDL 115
|
90 100
....*....|....*....|..
gi 1928617818 300 VVHMDMPKNIEGYYQETGRAGR 321
Cdd:cd18796 116 VIQIGSPKSVARLLQRLGRSGH 137
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
232-321 |
1.29e-04 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 45.27 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 232 IIYCLSRKSTEALAADLkdeGYSAEAYHAGLDHATKARNQEAFLRDEVKIMVATIAFG----------------MGINKS 295
Cdd:COG1202 431 IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAagvdfpasqvifdslaMGIEWL 507
|
90 100
....*....|....*....|....*.
gi 1928617818 296 NVRyvvhmdmpkniEgYYQETGRAGR 321
Cdd:COG1202 508 SVQ-----------E-FHQMLGRAGR 521
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
15-323 |
3.76e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 43.72 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 15 EFRHEQETIIGRVLNGHDVMALMPTGGGKSLC--YQLPAVLLPGL-TIVISPLIALMKDQVD------SLNLNgIPAAFL 85
Cdd:PRK01172 22 ELYDHQRMAIEQLRKGENVIVSVPTAAGKTLIaySAIYETFLAGLkSIYIVPLRSLAMEKYEelsrlrSLGMR-VKISIG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 86 NSSQTPDeqrnitdRLKSNQIKLLylaperlfgTENKLIDFLKSLP-----VSLFAIDEAHCIshwGHDFRPEYL--MLA 158
Cdd:PRK01172 101 DYDDPPD-------FIKRYDVVIL---------TSEKADSLIHHDPyiindVGLIVADEIHII---GDEDRGPTLetVLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 159 HLKDHFKNIPVIALTATADKLTQkdILEKLNlrqPSVFISSFN----RENITYRvtpknksfNQLlnFLDGRR------- 227
Cdd:PRK01172 162 SARYVNPDARILALSATVSNANE--LAQWLN---ASLIKSNFRpvplKLGILYR--------KRL--ILDGYErsqvdin 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 228 -------DDSG--IIYCLSRKSTEALA----------ADLKDEGYSAEAY---------------HAGLDHATKARNQEA 273
Cdd:PRK01172 227 sliketvNDGGqvLVFVSSRKNAEDYAemliqhfpefNDFKVSSENNNVYddslnemlphgvafhHAGLSNEQRRFIEEM 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1928617818 274 FLRDEVKIMVATIAFGMGINKSnVRYVVHMDMPKNIEGYY---------QETGRAGRDG 323
Cdd:PRK01172 307 FRNRYIKVIVATPTLAAGVNLP-ARLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPG 364
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
30-175 |
2.93e-03 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 39.10 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 30 GHDVMALMPTGGGKSLcyqlpAVLLPGLT------------IVISPLIALMKDQVDSLN--LNGIPAAFLNSSQTPDEQR 95
Cdd:cd17922 1 GRNVLIAAPTGSGKTE-----AAFLPALSsladepekgvqvLYISPLKALINDQERRLEepLDEIDLEIPVAVRHGDTSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 96 NITDRLKSNQIKLLYLAPERLFG--TENKLIDFLKSLpvSLFAIDEAHCI--SHWGHDFRpeyLMLAHLKD-HFKNIPVI 170
Cdd:cd17922 76 SEKAKQLKNPPGILITTPESLELllVNKKLRELFAGL--RYVVVDEIHALlgSKRGVQLE---LLLERLRKlTGRPLRRI 150
|
....*
gi 1928617818 171 ALTAT 175
Cdd:cd17922 151 GLSAT 155
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
4-67 |
5.98e-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: 5.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1928617818 4 LQALHKYfGYSEFRHEQETIIGRVLNGHDVMALMPTGGGKSLCYQLPAV--LLPGLTIVISPLIAL 67
Cdd:cd00268 2 LKALKKL-GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekLLPEPKKKGRGPQAL 66
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
232-332 |
9.07e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 39.44 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928617818 232 IIYCLSRKSTEALAADLKDEGYSAEAYHAGLDHATKARNQEAFLRDE--VKIMVATIAFGMGINKSNVRYVVHMDMPKNI 309
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLWWNP 632
|
90 100
....*....|....*....|...
gi 1928617818 310 EGYYQETGRAGRDGLPSDAMLYY 332
Cdd:COG0553 633 AVEEQAIDRAHRIGQTRDVQVYK 655
|
|
| |
