|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
392-751 |
4.72e-117 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 371.78 E-value: 4.72e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 392 AEVFQALERL-GYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLyaqrSPCLTLVVSPLLSLMDDQVSDLP 470
Cdd:COG0514 3 DDALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALL----LPGLTLVVSPLIALMKDQVDALR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 471 SC-LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALvgcgaRGPGSLPQAAQLPPIAFAcIDEVHCLSQWSHNFRP 549
Cdd:COG0514 79 AAgIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERL-----LNPRFLELLRRLKISLFA-IDEAHCISQWGHDFRP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 550 CYLRVcKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAGEFELSGSANIPaNLHLSVS--MDRDSDQALVTLLQGdrf 627
Cdd:COG0514 153 DYRRL-GELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRP-NLRLEVVpkPPDDKLAQLLDFLKE--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 628 RTLDSVIIYCTRRKDTERVAALLRTclsmvgdsrpRGcgpeaI-AEAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGM 706
Cdd:COG0514 228 HPGGSGIVYCLSRKKVEELAEWLRE----------AG-----IrAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGM 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1039749727 707 GLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFMHPQ 751
Cdd:COG0514 293 GIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
395-597 |
6.55e-99 |
|
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: 312.27 E-value: 6.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 395 FQALERL-GYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLYAQRSPCLTLVVSPLLSLMDDQVSDLPSCL 473
Cdd:cd18018 1 LKLLRRVfGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMKDQVDALPRAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 474 KAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALvgcgaRGPGSLPQAAQLPPIAFACIDEVHCLSQWSHNFRPCYLR 553
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERL-----VNESFRELLRQTPPISLLVVDEAHCISEWSHNFRPDYLR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039749727 554 VCKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAGEFELSGS 597
Cdd:cd18018 156 LCRVLRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGP 199
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
402-750 |
7.19e-91 |
|
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: 300.53 E-value: 7.19e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 402 GYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLyaqrSPCLTLVVSPLLSLMDDQVSDLP-SCLKAACLHS 480
Cdd:TIGR00614 8 GLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALY----SDGITLVISPLISLMEDQVLQLQaLGIPATFLNS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 481 GMTKKQRESVLKKVRAAQVHVLIVSPEALvgCGARGPGSLPQAAQLppIAFACIDEVHCLSQWSHNFRPCYlRVCKVLRE 560
Cdd:TIGR00614 84 AQTKEQQLNVLTDLKDGKIKLLYVTPEKI--SASNRLLQTLEERKG--ITLIAVDEAHCISQWGHDFRPDY-KALGSLKQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 561 HMGVRCFLGLTATATRSTARDVAQHLGIAGEFELSGSANIPaNLHLSVsMDRDSD--QALVTLLQGdRFRTlDSVIIYCT 638
Cdd:TIGR00614 159 KFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRP-NLYYEV-RRKTPKilEDLLRFIRK-EFEG-KSGIIYCP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 639 RRKDTERVAALLRTclsmVGDSrprgcgpeaiAEAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVLH 718
Cdd:TIGR00614 235 SRKKVEQVAAELQK----LGLA----------AGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIH 300
|
330 340 350
....*....|....*....|....*....|..
gi 1039749727 719 LGLPPSFESYVQAIGRAGRDGKPAHCHLFMHP 750
Cdd:TIGR00614 301 YSLPKSMESYYQESGRAGRDGLPSECHLFYAP 332
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
395-751 |
6.17e-89 |
|
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: 299.30 E-value: 6.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 395 FQALER-LGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLYaqrsPCLTLVVSPLLSLMDDQVSDLPSC- 472
Cdd:TIGR01389 2 QQVLKRtFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLL----KGLTVVISPLISLMKDQVDQLRAAg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 473 LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgargPGSLPQAAQLPPIAFAcIDEVHCLSQWSHNFRPCYL 552
Cdd:TIGR01389 78 VAAAYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQ-----DYFLNMLQRIPIALVA-VDEAHCVSQWGHDFRPEYQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 553 RVCkVLREHMGVRCFLGLTATATRSTARDVAQHLGIAGEFELSGSANIPaNLHLSVSMDRDSDQALVTLLQGDRFRtldS 632
Cdd:TIGR01389 152 RLG-SLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRP-NLRFSVVKKNNKQKFLLDYLKKHRGQ---S 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 633 VIIYCTRRKDTERVAALLRTClsmvgdsrprgcGPEAIAeaYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPD 712
Cdd:TIGR01389 227 GIIYASSRKKVEELAERLESQ------------GISALA--YHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPN 292
|
330 340 350
....*....|....*....|....*....|....*....
gi 1039749727 713 VRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFMHPQ 751
Cdd:TIGR01389 293 VRFVIHYDMPGNLESYYQEAGRAGRDGLPAEAILLYSPA 331
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
386-750 |
2.39e-80 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 275.82 E-value: 2.39e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 386 QVAETPAEVFQAL-ERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLYaqrsPCLTLVVSPLLSLMDD 464
Cdd:PRK11057 5 EVLNLESLAKQVLqETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL----DGLTLVVSPLISLMKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 465 QVSDL-PSCLKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGcgargPGSLPQAAQLPPIAFAcIDEVHCLSQW 543
Cdd:PRK11057 81 QVDQLlANGVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMM-----DNFLEHLAHWNPALLA-VDEAHCISQW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 544 SHNFRPCYlRVCKVLREHMGVRCFLGLTATATRSTARDVAQHLGIAGEFELSGSANIPANLHLSVSMDRDSDQaLVTLLQ 623
Cdd:PRK11057 155 GHDFRPEY-AALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQ-LMRYVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 624 GDRFRtldSVIIYCTRRKDTERVAALLRTclsmvgdsrpRGCGpeaiAEAYHAGMSSQERRRVQQAFMRGHLRMVVATVA 703
Cdd:PRK11057 233 EQRGK---SGIIYCNSRAKVEDTAARLQS----------RGIS----AAAYHAGLDNDVRADVQEAFQRDDLQIVVATVA 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1039749727 704 FGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFMHP 750
Cdd:PRK11057 296 FGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDP 342
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
399-597 |
1.15e-65 |
|
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: 220.48 E-value: 1.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 399 ERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLyaqrSPCLTLVVSPLLSLMDDQVSDLPS-CLKAAC 477
Cdd:cd17920 6 EVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL----LDGVTLVVSPLISLMQDQVDRLQQlGIRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 478 LHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGCGARgpGSLPQAAQLPPIAFACIDEVHCLSQWSHNFRPCYLRVCKV 557
Cdd:cd17920 82 LNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFL--ELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039749727 558 LREHMGVrCFLGLTATATRSTARDVAQHLGIAGEFELSGS 597
Cdd:cd17920 160 RRALPGV-PILALTATATPEVREDILKRLGLRNPVIFRAS 198
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
603-747 |
2.25e-55 |
|
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: 188.19 E-value: 2.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 603 NLHLSVSMDRDSDQALVTLLQGDRFRTLDSVIIYCTRRKDTERVAALLRTClsmvGDSrprgcgpeaiAEAYHAGMSSQE 682
Cdd:cd18794 3 NLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSK----GIS----------AAAYHAGLEPSD 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039749727 683 RRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLF 747
Cdd:cd18794 69 RRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
402-747 |
3.18e-52 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 200.89 E-value: 3.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 402 GYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLyaqrSPCLTLVVSPLLSLMDDQVSDL-PSCLKAACLHS 480
Cdd:PLN03137 457 GNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALI----CPGITLVISPLVSLIQDQIMNLlQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 481 GMTKKQRESVLKKVRA--AQVHVLIVSPEALVGCGA--RGPGSLPQAAQLPPIAfacIDEVHCLSQWSHNFRPCYlRVCK 556
Cdd:PLN03137 533 GMEWAEQLEILQELSSeySKYKLLYVTPEKVAKSDSllRHLENLNSRGLLARFV---IDEAHCVSQWGHDFRPDY-QGLG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 557 VLREHMGVRCFLGLTATATRSTARDVAQHLGIAGEFELSGSANIPaNLHLSVSmdRDSDQALVTLLQGDRFRTLDSV-II 635
Cdd:PLN03137 609 ILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRP-NLWYSVV--PKTKKCLEDIDKFIKENHFDECgII 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 636 YCTRRKDTERVAALLRTClsmvGDSrprgcgpeaiAEAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRA 715
Cdd:PLN03137 686 YCLSRMDCEKVAERLQEF----GHK----------AAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRF 751
|
330 340 350
....*....|....*....|....*....|..
gi 1039749727 716 VLHLGLPPSFESYVQAIGRAGRDGKPAHCHLF 747
Cdd:PLN03137 752 VIHHSLPKSIEGYHQECGRAGRDGQRSSCVLY 783
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
385-599 |
4.91e-40 |
|
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: 147.51 E-value: 4.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 385 GQVAETPAEVFQaLErlgyrAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLyaqrSPCLTLVVSPLLSLMDD 464
Cdd:cd18015 4 GKVKDTLKNVFK-LE-----KFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALC----SDGFTLVVSPLISLMED 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 465 QVSDLPSC-LKAACLHSGMTKKQRESVLKKVR--AAQVHVLIVSPEALVGcGARGPGSLPQAAQLPPIAFACIDEVHCLS 541
Cdd:cd18015 74 QLMALKKLgISATMLNASSSKEHVKWVHAALTdkNSELKLLYVTPEKIAK-SKRFMSKLEKAYNAGRLARIAIDEVHCCS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039749727 542 QWSHNFRPCYlrvckvlrEHMGV--RCF-----LGLTATATRSTARDVAQHLGIAGEFELSGSAN 599
Cdd:cd18015 153 QWGHDFRPDY--------KKLGIlkRQFpnvpiLGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DpdF |
NF041063 |
protein DpdF; |
383-751 |
6.90e-40 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 159.69 E-value: 6.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 383 PLGQVAETPAEVFQAlERLGYRAFR-PGQERAIMRILS---GiSTLLV-LPTGAGKSLCYQLPALLYAQRSPcLTLVVSP 457
Cdd:NF041063 118 LRRTLEPVPGDPFLA-EALGFTHYRsPGQREAVRAALLappG-STLIVnLPTGSGKSLVAQAPALLASRQGG-LTLVVVP 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 458 LLSLMDDQVSDLPSCLKAA--------CLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGCGARgpgSLPQAAQLPPI 529
Cdd:NF041063 195 TVALAIDQERRARELLRRAgpdlggplAWHGGLSAEERAAIRQRIRDGTQRILFTSPESLTGSLRP---ALFDAAEAGLL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 530 AFACIDEVHCLSQWSHNFRPCY----------LRVCKvlrEHMGVRCFLgLTATATRSTaRDVAQHL-GIAGEFEL-SGS 597
Cdd:NF041063 272 RYLVVDEAHLVDQWGDGFRPEFqllaglrrslLRLAP---SGRPFRTLL-LSATLTEST-LDTLETLfGPPGPFIVvSAV 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 598 anipanlHL----SVSMDRDSDQAlvtllqgDRFRT-LDSV-------IIYCTRRKDTERVAALLRTclsmVGDSRprgc 665
Cdd:NF041063 347 -------QLrpepAYWVAKCDSEE-------ERRERvLEALrhlprplILYVTKVEDAEAWLQRLRA----AGFRR---- 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 666 gpeaiAEAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCH 745
Cdd:NF041063 405 -----VALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSL 479
|
....*.
gi 1039749727 746 LFMHPQ 751
Cdd:NF041063 480 LIYTPD 485
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
402-588 |
1.15e-32 |
|
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: 125.66 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 402 GYRAFRPGQERAIMRIL-SGISTLLVLPTGAGKSLCYQLPALLYAQrspcLTLVVSPLLSLMDDQVSDLPSCLKAACLhs 480
Cdd:cd18017 9 GHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNS----LTLVISPLISLMEDQVLQLVMSNIPACF-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 481 gMTKKQRESVLKKVRAAQVHVLIVSPEAlvgcGARGPGSLPQ-AAQLPPIAfacIDEVHCLSQWSHNFRPCYlRVCKVLR 559
Cdd:cd18017 83 -LGSAQSQNVLDDIKMGKIRVIYVTPEF----VSKGLELLQQlRNGITLIA---IDEAHCVSQWGHDFRSSY-RHLGSIR 153
|
170 180
....*....|....*....|....*....
gi 1039749727 560 EHMGVRCFLGLTATATRSTARDVAQHLGI 588
Cdd:cd18017 154 NRLPNVPIVALTATATPSVRDDIIKNLNL 182
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
402-588 |
2.95e-32 |
|
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: 124.89 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 402 GYRAFR-PGQERAIMRILSGISTLLV-LPTGAGKSLCYQLPALLYAQrspcLTLVVSPLLSLMDDQVSDLPSC-LKAACL 478
Cdd:cd18014 9 GHSDFKsPLQEKATMAVVKGNKDVFVcMPTGAGKSLCYQLPALLAKG----ITIVISPLIALIQDQVDHLKTLkIRVDSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 479 HSGMTKKQRESVLKKVRAA--QVHVLIVSPEAlvgcgARGPGSLPQAAQLPP---IAFACIDEVHCLSQWSHNFRPCYLR 553
Cdd:cd18014 85 NSKLSAQERKRIIADLESEkpQTKFLYITPEM-----AATSSFQPLLSSLVSrnlLSYLVVDEAHCVSQWGHDFRPDYLR 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1039749727 554 VCKVLREHMGVRCfLGLTATATRSTARDVAQHLGI 588
Cdd:cd18014 160 LGALRSRYGHVPW-VALTATATPQVQEDIFAQLRL 193
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
400-588 |
1.53e-29 |
|
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: 117.24 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 400 RLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLyaqrSPCLTLVVSPLLSLMDDQVSDLPSC-LKAACL 478
Cdd:cd18016 12 KFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACV----SPGVTVVISPLRSLIVDQVQKLTSLdIPATYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 479 HSGMTKKQRESVLKKVRAAQ--VHVLIVSPEAlVGCGARGPGSLPQAAQLPPIAFACIDEVHCLSQWSHNFRPCYLRVcK 556
Cdd:cd18016 88 TGDKTDAEATKIYLQLSKKDpiIKLLYVTPEK-ISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPDYKRL-N 165
|
170 180 190
....*....|....*....|....*....|..
gi 1039749727 557 VLREHMGVRCFLGLTATATRSTARDVAQHLGI 588
Cdd:cd18016 166 MLRQKFPSVPMMALTATATPRVQKDILNQLKM 197
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
398-586 |
4.22e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 104.11 E-value: 4.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 398 LERLGYRAFRPGQERAIMRILSGI-STLLVLPTGAGKSLCYQLPALLYAQRSP-CLTLVVSPLLSLMDDQVSDL-----P 470
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKgGRVLVLVPTRELAEQWAEELkklgpS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 471 SCLKAACLHSGMTKKQResvLKKVRAAQVHVLIVSPEALVGCGARGPGSLPQaaqlppIAFACIDEVHCLSQWshNFRPC 550
Cdd:smart00487 81 LGLKVVGLYGGDSKREQ---LRKLESGKTDILVTTPGRLLDLLENDKLSLSN------VDLVILDEAHRLLDG--GFGDQ 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039749727 551 YLRVCKVLREHmgvRCFLGLTATATRSTARDVAQHL 586
Cdd:smart00487 150 LEKLLKLLPKN---VQLLLLSATPPEEIENLLELFL 182
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
407-580 |
1.60e-24 |
|
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: 101.17 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 407 RPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAQRSPCLTLVVSPLLSLMDDQVSDL-----PSCLKAACLH 479
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALeaLDKLDNGPQALVLAPTRELAEQIYEELkklgkGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 480 SGMTKKQRESVLKKvraaqVHVLIVSPEALVgcgargpGSLPQAAQLPPIAFACIDEVHCLSQWShnFRPCYLRVCKVLR 559
Cdd:pfam00270 81 GGDSRKEQLEKLKG-----PDILVGTPGRLL-------DLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEILRRLP 146
|
170 180
....*....|....*....|.
gi 1039749727 560 EHmgvRCFLGLTATATRSTAR 580
Cdd:pfam00270 147 KK---RQILLLSATLPRNLED 164
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
381-742 |
3.86e-23 |
|
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: 106.46 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 381 PGPLGQVAETPA----EVFQALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAQRSPClTLV 454
Cdd:COG1205 28 PAREARYAPWPDwlppELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLEDPGAT-ALY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 455 VSPLLSLMDDQVS-------DLPSCLKAACLHSGMTKKQRESVLKkvraaQVHVLIVSPEAL-VGCgargpgsLPQAAQL 526
Cdd:COG1205 107 LYPTKALARDQLRrlrelaeALGLGVRVATYDGDTPPEERRWIRE-----HPDIVLTNPDMLhYGL-------LPHHTRW 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 527 PPIaFAC-----IDEVHCL-----SQWSHNFRPcYLRVCkvlrEHMGVRC-FLGLTAT-------ATRSTARDVAQhlgI 588
Cdd:COG1205 175 ARF-FRNlryvvIDEAHTYrgvfgSHVANVLRR-LRRIC----RHYGSDPqFILASATignpaehAERLTGRPVTV---V 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 589 AGEFELSGSANI----PANLHLSVSMDRDSDQA-LVTLLQGDRFRTldsvIIYCTRRKDTERVAALLRtclsmvgDSRPR 663
Cdd:COG1205 246 DEDGSPRGERTFvlwnPPLVDDGIRRSALAEAArLLADLVREGLRT----LVFTRSRRGAELLARYAR-------RALRE 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039749727 664 GCGPEAIAeAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPA 742
Cdd:COG1205 315 PDLADRVA-AYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS 392
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
671-739 |
4.74e-21 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 88.42 E-value: 4.74e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039749727 671 AEAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDG 739
Cdd:smart00490 14 VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
634-742 |
1.38e-18 |
|
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: 83.46 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 634 IIYCTRRKDTERVAALLRTCLsmvgdsRPRGCGPEAIAeAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDV 713
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARL------VEEGPLASKVA-SYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGL 111
|
90 100
....*....|....*....|....*....
gi 1039749727 714 RAVLHLGLPPSFESYVQAIGRAGRDGKPA 742
Cdd:cd18797 112 DAVVLAGYPGSLASLWQQAGRAGRRGKDS 140
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
616-739 |
1.24e-17 |
|
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: 79.56 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 616 QALVTLLQGDRFrtlDSVIIYCTRRKDTErvAALLRTCLSMvgdsrprgcgpeaIAEAYHAGMSSQERRRVQQAFMRGHL 695
Cdd:pfam00271 4 EALLELLKKERG---GKVLIFSQTKKTLE--AELLLEKEGI-------------KVARLHGDLSQEEREEILEDFRKGKI 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1039749727 696 RMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDG 739
Cdd:pfam00271 66 DVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
612-747 |
2.44e-15 |
|
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: 73.70 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 612 RDSDQALVTLLQGDRFRTLDSVIIYCTRRKDTERVAALLRTClsmvgdsrprgcGPEAIAeaYHAGMSSQERRRVQQAFM 691
Cdd:cd18787 9 EEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEEL------------GIKVAA--LHGDLSQEERERALKKFR 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039749727 692 RGHLRMVVAT-VAfGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLF 747
Cdd:cd18787 75 SGKVRVLVATdVA-ARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITF 130
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
386-740 |
2.86e-15 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 80.32 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 386 QVAETP-AEVFQALERLGYRAFRPGQERAIMR-ILSGISTLLVLPTGAGKSLCYQLpALLYAQRSPCLTLVVSPLLSLMD 463
Cdd:COG1204 2 KVAELPlEKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAEL-AILKALLNGGKALYIVPLRALAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 464 DQVSDLPSCLKAACLHSGMTKKQRESVLKkvRAAQVHVLIVSPEALVgcgargpgSL--PQAAQLPPIAFACIDEVH--- 538
Cdd:COG1204 81 EKYREFKRDFEELGIKVGVSTGDYDSDDE--WLGRYDILVATPEKLD--------SLlrNGPSWLRDVDLVVVDEAHlid 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 539 ----------CLSqwshnfrpcylrvcKVLREHMGVRcFLGLTATA--------------TRSTARDVAQHLGIA--GEF 592
Cdd:COG1204 151 desrgptlevLLA--------------RLRRLNPEAQ-IVALSATIgnaeeiaewldaelVKSDWRPVPLNEGVLydGVL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 593 ELSGSANIPANLHLSVSMDrdsdqalvTLLQGDrfrtldSVIIYCTRRKDTERVAALLRTCLSMVGDSRPRGCGPEAIAE 672
Cdd:COG1204 216 RFDDGSRRSKDPTLALALD--------LLEEGG------QVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 673 ----------------------AYH-AGMSSQERRRVQQAFMRGHLRMVVAT--VAFGMGLdrPdVRAVL-----HLGLP 722
Cdd:COG1204 282 llevseethtnekladclekgvAFHhAGLPSELRRLVEDAFREGLIKVLVATptLAAGVNL--P-ARRVIirdtkRGGMV 358
|
410 420
....*....|....*....|
gi 1039749727 723 P--SFEsYVQAIGRAGRDGK 740
Cdd:COG1204 359 PipVLE-FKQMAGRAGRPGY 377
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
407-747 |
7.65e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.91 E-value: 7.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 407 RPGQERAIMRILSGIST-----LLVLPTGAGKSLcyqLPALLYAQ-RSPCLTLVVSPLLSLMDDQVSDLPSCLKAACLHS 480
Cdd:COG1061 82 RPYQQEALEALLAALERgggrgLVVAPTGTGKTV---LALALAAElLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 481 GmtKKQRESvlkkvraaqvHVLIVSPEALvgcgargpGSLPQAAQLPP-IAFACIDEVHclsqwsHNFRPCYLRVckvlR 559
Cdd:COG1061 159 G--KKDSDA----------PITVATYQSL--------ARRAHLDELGDrFGLVIIDEAH------HAGAPSYRRI----L 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 560 EHMGVRCFLGLTATATRSTARDVAQHL--GIAGEF---ELSgSANIPANLH-LSVSMDRDSDQALVTLLQGDRFRTLDS- 632
Cdd:COG1061 209 EAFPAAYRLGLTATPFRSDGREILLFLfdGIVYEYslkEAI-EDGYLAPPEyYGIRVDLTDERAEYDALSERLREALAAd 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 633 --------------------VIIYCTRRKDTERVAALLRTclsmvgdsrpRGCGPEAIaeayHAGMSSQERRRVQQAFMR 692
Cdd:COG1061 288 aerkdkilrellrehpddrkTLVFCSSVDHAEALAELLNE----------AGIRAAVV----TGDTPKKEREEILEAFRD 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 693 GHLRMVVATVAFGMGLDRPDVRAVLHLGlppSFES---YVQAIGRA--GRDGKPaHCHLF 747
Cdd:COG1061 354 GELRILVTVDVLNEGVDVPRLDVAILLR---PTGSpreFIQRLGRGlrPAPGKE-DALVY 409
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
423-573 |
1.54e-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: 72.05 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 423 TLLVLPTGAGKSLCYQLPALLYAQRSPCLTLVVSPLLSLMDDQVSDL----PSCLKAACLHSGMTKKQREsvlkKVRAAQ 498
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLrelfGPGIRVAVLVGGSSAEERE----KNKLGD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039749727 499 VHVLIVSPEALVGCGARGPGSLpqaaqLPPIAFACIDEVHCLSQWSHNFRPCYLRVCKVLREHMGVrcfLGLTAT 573
Cdd:cd00046 80 ADIIIATPDMLLNLLLREDRLF-----LKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV---ILLSAT 146
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
391-740 |
5.16e-14 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 75.57 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 391 PAEVFQALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPA---LLYAQRSPCLTLVVSPL--LSLmddQ 465
Cdd:COG0513 10 SPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLlqrLDPSRPRAPQALILAPTreLAL---Q 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 466 VSD--------LPscLKAACLHSGMT-KKQRESvLKKvraaQVHVLivspealVGCgargPGSLpqaaqlppiafacID- 535
Cdd:COG0513 87 VAEelrklakyLG--LRVATVYGGVSiGRQIRA-LKR----GVDIV-------VAT----PGRL-------------LDl 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 536 ---------EVHCLsqwshnfrpcylrvckVLRE-----HMG----VRCFLGLT----------ATATRSTARDVAQHLG 587
Cdd:COG0513 136 iergaldlsGVETL----------------VLDEadrmlDMGfiedIERILKLLpkerqtllfsATMPPEIRKLAKRYLK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 588 IAGEFELSGSANIPANLHLSVSM--DRDSDQALVTLLQGDRFrtlDSVIIYCTRRKDTERVAALLRTclsmvgdsrpRGc 665
Cdd:COG0513 200 NPVRIEVAPENATAETIEQRYYLvdKRDKLELLRRLLRDEDP---ERAIVFCNTKRGADRLAEKLQK----------RG- 265
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039749727 666 gpeAIAEAYHAGMSSQERRRVQQAFMRGHLRMVVAT-VAfGMGLDRPDVRAVLHLGLPPSFESYVQAIG---RAGRDGK 740
Cdd:COG0513 266 ---ISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARGIDIDDVSHVINYDLPEDPEDYVHRIGrtgRAGAEGT 340
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
632-748 |
3.36e-12 |
|
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: 65.36 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 632 SVIIYCTRRKDTERVAALLRtclsmvgdSRPRGCGPEAIAEAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRP 711
Cdd:cd18796 40 STLVFTNTRSQAERLAQRLR--------ELCPDRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIG 111
|
90 100 110
....*....|....*....|....*....|....*..
gi 1039749727 712 DVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFM 748
Cdd:cd18796 112 DVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLV 148
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
381-750 |
1.62e-10 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 65.18 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 381 PGPLGQVAET--PAEVFQALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLYAQRSPCL------- 451
Cdd:PTZ00110 126 PKPVVSFEYTsfPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLrygdgpi 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 452 TLVVSPLLSLMDdQVSD------LPSCLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALVGCGARGPGSLPQAAQ 525
Cdd:PTZ00110 206 VLVLAPTRELAE-QIREqcnkfgASSKIRNTVAYGGVPKRGQIYALRR----GVEILIACPGRLIDFLESNVTNLRRVTY 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 526 LppiafaCIDEVHclSQWSHNFRPCYLRVCKVLREHmgvRCFLGLTATATR---STARDVAQHLGI---AGEFELSGSAN 599
Cdd:PTZ00110 281 L------VLDEAD--RMLDMGFEPQIRKIVSQIRPD---RQTLMWSATWPKevqSLARDLCKEEPVhvnVGSLDLTACHN 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 600 IPANLHLsvsMDRDSDQALVTLLQGDRFRTLDSVIIYCTRRKDTERVAALLRTclsmvgDSRPRGCgpeaiaeaYHAGMS 679
Cdd:PTZ00110 350 IKQEVFV---VEEHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKELRL------DGWPALC--------IHGDKK 412
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039749727 680 SQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFMHP 750
Cdd:PTZ00110 413 QEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
403-736 |
2.48e-10 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 64.74 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 403 YRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALL-YAQRSP-------CLTLVVSPLLSL------------- 461
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDeLARRPRpgelpdgLRVLYISPLKALandiernlraple 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 462 -MDDQVSDLPSCLKAAcLHSGMTKkQREsvlkkvRAAQV----HVLIVSPEALvgcgargpgSL----PQAAQLppiaFA 532
Cdd:COG1201 102 eIGEAAGLPLPEIRVG-VRTGDTP-ASE------RQRQRrrppHILITTPESL---------ALlltsPDAREL----LR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 533 C-----IDEVHCL------SQWS------HNFRPCYLRVckvlrehmgvrcfLGLTATAtrstaRDVAQhlgiAGEFeLS 595
Cdd:COG1201 161 GvrtviVDEIHALagskrgVHLAlslerlRALAPRPLQR-------------IGLSATV-----GPLEE----VARF-LV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 596 GS----------ANIPANLHLSV-SMDRDSD--------------QALVTLLQGDRfrtldSVIIYC-TRRKdTERVAAL 649
Cdd:COG1201 218 GYedprpvtivdAGAGKKPDLEVlVPVEDLIerfpwaghlwphlyPRVLDLIEAHR-----TTLVFTnTRSQ-AERLFQR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 650 LRtclsmvgdsRPRGCGPEAIAeAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYV 729
Cdd:COG1201 292 LN---------ELNPEDALPIA-AHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLL 361
|
....*..
gi 1039749727 730 QAIGRAG 736
Cdd:COG1201 362 QRIGRAG 368
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
632-739 |
2.52e-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: 60.26 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 632 SVIIYCTRRKDTERVAALLRtclsmvgdsrprGCGpeaiaeAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRP 711
Cdd:cd18795 45 PVLVFCSSRKECEKTAKDLA------------GIA------FHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP 106
|
90 100 110
....*....|....*....|....*....|....*...
gi 1039749727 712 DVRAVLhLGLP----------PSFEsYVQAIGRAGRDG 739
Cdd:cd18795 107 ARTVII-KGTQrydgkgyrelSPLE-YLQMIGRAGRPG 142
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
698-748 |
5.48e-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: 56.56 E-value: 5.48e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1039749727 698 VVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGK-PAHCHLFM 748
Cdd:cd18785 26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKdEGEVILFV 77
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
635-736 |
5.97e-10 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 63.79 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 635 IYCTRRKDTERVAALLRTCLSMVGDSRPRGCG-PEAIAEAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDV 713
Cdd:PRK09751 267 LYAARLQRSPSIAVDAAHFESTSGATSNRVQSsDVFIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAV 346
|
90 100
....*....|....*....|...
gi 1039749727 714 RAVLHLGLPPSFESYVQAIGRAG 736
Cdd:PRK09751 347 DLVIQVATPLSVASGLQRIGRAG 369
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
380-772 |
1.91e-09 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 61.73 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 380 PPGPLGQVAET--PAEVFQALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPAL----------LYAQR 447
Cdd:PLN00206 116 VPPPILSFSSCglPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsrcctirsghPSEQR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 448 SPcLTLVVSPLLSLMDdQVSDlpsclKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEALVGCgargPGSL-----PQ 522
Cdd:PLN00206 196 NP-LAMVLTPTRELCV-QVED-----QAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGT----PGRLidllsKH 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 523 AAQLPPIAFACIDEVHCLSQwsHNFRPCYLRVCKVLREHMgvrcFLGLTATATRSTARdVAQHLGIAGEFELSGSANIP- 601
Cdd:PLN00206 265 DIELDNVSVLVLDEVDCMLE--RGFRDQVMQIFQALSQPQ----VLLFSATVSPEVEK-FASSLAKDIILISIGNPNRPn 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 602 -ANLHLSVSMD-RDSDQALVTLLQgDRFRTLDSVIIYCTRRKDtervAALLRTCLSMVGDSRprgcgpeaiAEAYHAGMS 679
Cdd:PLN00206 338 kAVKQLAIWVEtKQKKQKLFDILK-SKQHFKPPAVVFVSSRLG----ADLLANAITVVTGLK---------ALSIHGEKS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 680 SQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFMHPQvGSPISPD 759
Cdd:PLN00206 404 MKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE-DRNLFPE 482
|
410
....*....|....*.
gi 1039749727 760 ---QDRPRGSTIPRPL 772
Cdd:PLN00206 483 lvaLLKSSGAAIPREL 498
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
403-736 |
7.42e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 60.28 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 403 YRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPAL---------------LYAqrspcltLVVSPLLSLMDD--- 464
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIdelfrlgregeledkVYC-------LYVSPLRALNNDihr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 465 ----------QVS-----DLPScLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPE----ALVGcgargpgslPQAAQ 525
Cdd:PRK13767 103 nleeplteirEIAkergeELPE-IRVAIRTGDTSSYEKQKMLKK----PPHILITTPEslaiLLNS---------PKFRE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 526 -LPPIAFACIDEVHCLSQwshNFRPCYLRVC-KVLREHMG---VRcfLGLTATAtrSTARDVAQHLGIAGEFELSGSANI 600
Cdd:PRK13767 169 kLRTVKWVIVDEIHSLAE---NKRGVHLSLSlERLEELAGgefVR--IGLSATI--EPLEEVAKFLVGYEDDGEPRDCEI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 601 panlhLSVSMDRDSDQALVT----LLQGDR-------FRTLDSVI-------IYCTRRKDTERVAALLRTCLSMVGDSrp 662
Cdd:PRK13767 242 -----VDARFVKPFDIKVISpvddLIHTPAeeisealYETLHELIkehrttlIFTNTRSGAERVLYNLRKRFPEEYDE-- 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039749727 663 rgcgpEAIaEAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAG 736
Cdd:PRK13767 315 -----DNI-GAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
629-740 |
9.43e-08 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 55.99 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 629 TLDSVIIYCTRRKDTERVAALLR----TCLSMVGDsrprgcgpeaiaeayhagMSSQERRRVQQAFMRGHLRMVVATVAF 704
Cdd:PTZ00424 266 TITQAIIYCNTRRKVDYLTKKMHerdfTVSCMHGD------------------MDQKDRDLIMREFRSGSTRVLITTDLL 327
|
90 100 110
....*....|....*....|....*....|....*.
gi 1039749727 705 GMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGK 740
Cdd:PTZ00424 328 ARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGR 363
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
671-737 |
1.53e-07 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 55.67 E-value: 1.53e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039749727 671 AEAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVlhlglppsFES------------YVQAIGRAGR 737
Cdd:COG1202 451 AAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVI--------FDSlamgiewlsvqeFHQMLGRAGR 521
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
410-469 |
2.14e-07 |
|
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: 52.20 E-value: 2.14e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039749727 410 QERAIMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAQRSPClTLVVSPLLSLMDDQVSDL 469
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLRDPGSR-ALYLYPTKALAQDQLRSL 65
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
406-573 |
3.67e-07 |
|
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: 50.77 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 406 FRPGQERAIMRILSGIST---LLVLPTGAGKSLC-YQLPALLYAQRspclTLVVSPLLSLMDDQVSDLpsclkAACLHSG 481
Cdd:cd17926 1 LRPYQEEALEAWLAHKNNrrgILVLPTGSGKTLTaLALIAYLKELR----TLIVVPTDALLDQWKERF-----EDFLGDS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 482 MTKKQRESVLKKVRAAQvhVLIVSPEALVGCGARGPGSLPQAAQLppIAfaciDEVHCLS--QWSHnfrpcylrvckvLR 559
Cdd:cd17926 72 SIGLIGGGKKKDFDDAN--VVVATYQSLSNLAEEEKDLFDQFGLL--IV----DEAHHLPakTFSE------------IL 131
|
170
....*....|....
gi 1039749727 560 EHMGVRCFLGLTAT 573
Cdd:cd17926 132 KELNAKYRLGLTAT 145
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
396-510 |
2.42e-06 |
|
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: 49.36 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 396 QALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPAL------LYAQRSPCLTLVVSPL--LSLmddQVS 467
Cdd:cd00268 3 KALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekllpePKKKGRGPQALVLAPTreLAM---QIA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1039749727 468 DL------PSCLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALV 510
Cdd:cd00268 80 EVarklgkGTGLKVAAIYGGAPIKKQIEALKK----GPDIVVGTPGRLL 124
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
634-739 |
3.20e-06 |
|
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: 47.97 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 634 IIYCTRR----------KDTERVAALLRtCLSMVGDSRprgcgpeaIAEAYHAGMSSQERRRVQQAFMRGHLRMVVATVA 703
Cdd:cd18802 29 IIFVERRatavvlsrllKEHPSTLAFIR-CGFLIGRGN--------SSQRKRSLMTQRKQKETLDKFRDGELNLLIATSV 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 1039749727 704 FGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDG 739
Cdd:cd18802 100 LEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
414-505 |
7.82e-06 |
|
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: 47.71 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 414 IMRILSGISTLLVLPTGAGKS---LCYQLPALLYAQRSpcltLVVSPLLSLMDdQVSD--------LPSCLKAACLHSGM 482
Cdd:cd17924 26 AKRLLRGKSFAIIAPTGVGKTtfgLATSLYLASKGKRS----YLIFPTKSLVK-QAYErlskyaekAGVEVKILVYHSRL 100
|
90 100
....*....|....*....|...
gi 1039749727 483 TKKQRESVLKKVRAAQVHVLIVS 505
Cdd:cd17924 101 KKKEKEELLEKIEKGDFDILVTT 123
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
387-739 |
8.33e-06 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 49.94 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 387 VAETPAEVFQALERL-GYRAFR--PGQERAIMRILSGISTLLVLPTGAGKSL-----CYQlpALLYAQRSPCLTlvvsPL 458
Cdd:COG4581 4 SPARADARLEALADFaEERGFEldPFQEEAILALEAGRSVLVAAPTGSGKTLvaefaIFL--ALARGRRSFYTA----PI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 459 --LSLmddqvsdlpsclkaaclhsgmtKKQRESVlKKVRAAQVHVL----IVSPEALVGCG----------ARGPGslpq 522
Cdd:COG4581 78 kaLSN----------------------QKFFDLV-ERFGAENVGLLtgdaSVNPDAPIVVMtteilrnmlyREGAD---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 523 aaqLPPIAFACIDEVHCLSQwshNFR-----------PCYLRvckvlrehmgvrcFLGLTATAtrSTARDVAQHL-GIAG 590
Cdd:COG4581 131 ---LEDVGVVVMDEFHYLAD---PDRgwvweepiihlPARVQ-------------LVLLSATV--GNAEEFAEWLtRVRG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 591 EFELSGSANIPANLHLSVSM-DRDSDQALVT---LLQGDRFRTLDS--------VIIYC-TRRKDTERVAALLRTCLS-- 655
Cdd:COG4581 190 ETAVVVSEERPVPLEFHYLVtPRLFPLFRVNpelLRPPSRHEVIEEldrggllpAIVFIfSRRGCDEAAQQLLSARLTtk 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 656 --------MVGD-------------SRPRGCGpeaIAeAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPdVR 714
Cdd:COG4581 270 eeraeireAIDEfaedfsvlfgktlSRLLRRG---IA-VHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMP-AR 344
|
410 420 430
....*....|....*....|....*....|....*.
gi 1039749727 715 AVL-----------HLGLPPSfeSYVQAIGRAGRDG 739
Cdd:COG4581 345 TVVftklskfdgerHRPLTAR--EFHQIAGRAGRRG 378
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
406-593 |
1.49e-05 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 46.87 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 406 FRPGQERAIMRI-LSGISTLLVLPTGAGKSLCYQLPALLYAQRSPCLTLVVSPLLSLMDDQVSDLPSCLKAACLHSGMtk 484
Cdd:cd17921 2 LNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 485 KQRESVLKKVRAAQVHVLIVSPEALVGCGARGPGSLPQAAQLppiafACIDEVHCLSQWShnfRPCYLRVC--KVLREHM 562
Cdd:cd17921 80 LTGDPSVNKLLLAEADILVATPEKLDLLLRNGGERLIQDVRL-----VVVDEAHLIGDGE---RGVVLELLlsRLLRINK 151
|
170 180 190
....*....|....*....|....*....|.
gi 1039749727 563 GVRcFLGLTATAtrSTARDVAQHLGIAGEFE 593
Cdd:cd17921 152 NAR-FVGLSATL--PNAEDLAEWLGVEDLIR 179
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
327-739 |
1.65e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 48.76 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 327 EGDRDDKQPISTLEEVAQRTGTASCHHSAGEETQPAAPELQVPHCPTPMSPLYPPGP-------LGQVAETPAE------ 393
Cdd:PRK01297 11 KGEAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKPkpaslwkLEDFVVEPQEgktrfh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 394 -------VFQALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLYAQRSPC---------LTLVVSP 457
Cdd:PRK01297 91 dfnlapeLMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPpkerymgepRALIIAP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 458 LLSLMDDQVSDLPSCLKAACLH-----SGMT-KKQresvLKKVRAAQVHVLIVSPEALVGCGARGPGSLPQaaqlppIAF 531
Cdd:PRK01297 171 TRELVVQIAKDAAALTKYTGLNvmtfvGGMDfDKQ----LKQLEARFCDILVATPGRLLDFNQRGEVHLDM------VEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 532 ACIDEVHCLsqWSHNFRPcylRVCKVLRE--HMGVRCFLGLTATATRSTARDVAQHL--GIAGEFELSGSANIPANLHLS 607
Cdd:PRK01297 241 MVLDEADRM--LDMGFIP---QVRQIIRQtpRKEERQTLLFSATFTDDVMNLAKQWTtdPAIVEIEPENVASDTVEQHVY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 608 VSMDRDSDQALVTLLQGDRFrtlDSVIIYCTRRKDTERVAALLRTclsmvgdsrprgcgpEAIAEAYHAGMSSQERR-RV 686
Cdd:PRK01297 316 AVAGSDKYKLLYNLVTQNPW---ERVMVFANRKDEVRRIEERLVK---------------DGINAAQLSGDVPQHKRiKT 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1039749727 687 QQAFMRGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDG 739
Cdd:PRK01297 378 LEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAG 430
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
392-510 |
2.26e-05 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 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: 350712 [Multi-domain] Cd Length: 203 Bit Score: 46.54 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 392 AEVFQALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAQRSPCLTLVVSPLLSL---MDDQV 466
Cdd:cd17954 9 EELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILqaLLENPQRFFALVLAPTRELaqqISEQF 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1039749727 467 SDLPSC--LKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALV 510
Cdd:cd17954 89 EALGSSigLKSAVLVGGMDMMAQAIALAK----KPHVIVATPGRLV 130
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
406-573 |
4.23e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.97 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 406 FRPGQERAIMRILSGIST-----LLVLPTGAGKSLCY-QLPALLYAQRSPCLTLVVSPLLSLMDDQVSDLPSCLKAACLH 479
Cdd:pfam04851 4 LRPYQIEAIENLLESIKNgqkrgLIVMATGSGKTLTAaKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 480 SGMTKKQResvlKKVRAAQVHVLIVSPEALVGCgargpgSLPQAAQLPPIAFACI--DEVHCL--SQWSH---NFRPCYL 552
Cdd:pfam04851 84 GEIISGDK----KDESVDDNKIVVTTIQSLYKA------LELASLELLPDFFDVIiiDEAHRSgaSSYRNileYFKPAFL 153
|
170 180
....*....|....*....|.
gi 1039749727 553 rvckvlrehmgvrcfLGLTAT 573
Cdd:pfam04851 154 ---------------LGLTAT 159
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
420-540 |
5.08e-05 |
|
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: 44.88 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 420 GISTLLVLPTGAGKSLCYQLPAL--LYAQRSPCL-TLVVSPLLSLMDDQVSDLPSCLKAACL-------HSGMTKKQRES 489
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALssLADEPEKGVqVLYISPLKALINDQERRLEEPLDEIDLeipvavrHGDTSQSEKAK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1039749727 490 VLKKVRaaqvHVLIVSPEAL----VGCGARGpgslpqaaQLPPIAFACIDEVHCL 540
Cdd:cd17922 81 QLKNPP----GILITTPESLelllVNKKLRE--------LFAGLRYVVVDEIHAL 123
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
683-743 |
7.36e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 46.50 E-value: 7.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039749727 683 RRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAH 743
Cdd:PRK04837 294 RLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGH 354
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
394-506 |
1.01e-04 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members 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: 350716 [Multi-domain] Cd Length: 197 Bit Score: 44.76 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 394 VFQALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALL--------YAQRSPCLTLVVSPLLSL---M 462
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIhldlqpipREQRNGPGVLVLTPTRELalqI 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1039749727 463 DDQVSD-LPSCLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSP 506
Cdd:cd17958 81 EAECSKySYKGLKSVCVYGGGNRNEQIEDLSK----GVDIIIATP 121
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
394-509 |
1.18e-04 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 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: 350706 [Multi-domain] Cd Length: 231 Bit Score: 45.05 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 394 VFQALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLYAQRSPCLT---------LVVSPLLSLMdD 464
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAegpfnaprgLVITPSRELA-E 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1039749727 465 QVS--------DLPscLKAACLHSGMTKKQresvLKKVRAAQVHVLIVSPEAL 509
Cdd:cd17948 80 QIGsvaqslteGLG--LKVKVITGGRTKRQ----IRNPHFEEVDILVATPGAL 126
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
633-772 |
1.38e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 46.03 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 633 VIIYCTRRKDTERVAALLRTCLSMVGD----SRPRGCGPEAIAEA-------YHAGMSSQERRRVQQAFMRGHLRMVVAT 701
Cdd:PRK01172 239 VLVFVSSRKNAEDYAEMLIQHFPEFNDfkvsSENNNVYDDSLNEMlphgvafHHAGLSNEQRRFIEEMFRNRYIKVIVAT 318
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039749727 702 VAFGMGLDRP-------DVRAVLHLGLPP-SFESYVQAIGRAGRDGKPAHCHLFMHpqVGSPISPDQDRPRGSTIPRPL 772
Cdd:PRK01172 319 PTLAAGVNLParlvivrDITRYGNGGIRYlSNMEIKQMIGRAGRPGYDQYGIGYIY--AASPASYDAAKKYLSGEPEPV 395
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
371-510 |
2.66e-04 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 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: 350807 [Multi-domain] Cd Length: 234 Bit Score: 43.84 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 371 CPTPMSPLYPpgplgqvAETPAEVFQALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLYAQRSPC 450
Cdd:cd18049 19 CPKPVLNFYE-------ANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPF 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039749727 451 LT-------LVVSPLLSLMdDQVSDLP-----SC-LKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALV 510
Cdd:cd18049 92 LErgdgpicLVLAPTRELA-QQVQQVAaeygrACrLKSTCIYGGAPKGPQIRDLER----GVEICIATPGRLI 159
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
674-748 |
3.50e-04 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 41.69 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 674 YHAGMSSQERRRVQQAFMR--GHLRMVVATVAFGMGL-----DRpdvraVLHLGLP--PSFESyvQAIGRAGRDG--KPA 742
Cdd:cd18793 57 LDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGVGLnltaaNR-----VILYDPWwnPAVEE--QAIDRAHRIGqkKPV 129
|
....*.
gi 1039749727 743 HCHLFM 748
Cdd:cd18793 130 VVYRLI 135
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
611-740 |
3.54e-04 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 44.41 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 611 DRDSDQALVTLLQgdRFRTlDSVIIYCTRRKDTERVAALLRtclsMVGDSrprgcgpeaiAEAYHAGMSSQERRRVQQAF 690
Cdd:PRK11776 226 PDERLPALQRLLL--HHQP-ESCVVFCNTKKECQEVADALN----AQGFS----------ALALHGDLEQRDRDQVLVRF 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1039749727 691 MRGHLRMVVAT-VAfGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGK 740
Cdd:PRK11776 289 ANRSCSVLVATdVA-ARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGS 338
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
473-516 |
3.92e-04 |
|
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: 41.72 E-value: 3.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1039749727 473 LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVSPEAlvgcgARG 516
Cdd:cd18787 52 IKVAALHGDLSQEERERALKKFRSGKVRVLVATDVA-----ARG 90
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
615-748 |
6.02e-04 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 44.07 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 615 DQALVTLLQGDRFrtlDSVIIYCTRRKDTERVA-ALLRTCLSmvgdsrprgcgpeaiAEAYHAGMSSQERRRVQQAFMRG 693
Cdd:PRK11634 233 NEALVRFLEAEDF---DAAIIFVRTKNATLEVAeALERNGYN---------------SAALNGDMNQALREQTLERLKDG 294
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1039749727 694 HLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGRDGKPAHCHLFM 748
Cdd:PRK11634 295 RLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFV 349
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
439-505 |
1.00e-03 |
|
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: 39.89 E-value: 1.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039749727 439 LPALLYAQRSPClTLVVSPLLSLMDDQVSDLPSCLKAACLHSGMTKKQRESVLKKVRAAQVHVLIVS 505
Cdd:pfam00271 6 LLELLKKERGGK-VLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVAT 71
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
371-510 |
1.64e-03 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 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: 350808 [Multi-domain] Cd Length: 271 Bit Score: 41.92 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 371 CPTPMSPLYPpgplgqvAETPAEVFQALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPALLYAQRSP- 449
Cdd:cd18050 57 CPKPVFAFHQ-------ANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPy 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039749727 450 --------CLTLVVSPLLSLMDDQVSD---LPSCLKAACLHSGMTKKQRESVLKKvraaQVHVLIVSPEALV 510
Cdd:cd18050 130 lergdgpiCLVLAPTRELAQQVQQVADdygKSSRLKSTCIYGGAPKGPQIRDLER----GVEICIATPGRLI 197
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
634-748 |
2.13e-03 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 41.85 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 634 IIYCTRRKDTERVAALLRTclsmvgdsrprgcgpEAIAEAYHAGMSSQERRrvQQA---FMRGHLRMVVAT-VAfGMGLD 709
Cdd:PRK11192 249 IVFVRTRERVHELAGWLRK---------------AGINCCYLEGEMVQAKR--NEAikrLTDGRVNVLVATdVA-ARGID 310
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1039749727 710 RPDVRAVLHLGLPPSFESYVQAIGRAGRDGKP--------AHCHLFM 748
Cdd:PRK11192 311 IDDVSHVINFDMPRSADTYLHRIGRTGRAGRKgtaislveAHDHLLL 357
|
|
| ZnF_C2HC |
smart00343 |
zinc finger; |
301-315 |
2.43e-03 |
|
zinc finger;
Pssm-ID: 197667 [Multi-domain] Cd Length: 17 Bit Score: 36.27 E-value: 2.43e-03
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
675-755 |
3.03e-03 |
|
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: 39.63 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 675 HAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPD--VRAVLH---LGLppsfESYVQAIGRAGRDGKPAHCHLFMH 749
Cdd:cd18811 68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatVMVIEDaerFGL----SQLHQLRGRVGRGDHQSYCLLVYK 143
|
....*.
gi 1039749727 750 PQVGSP 755
Cdd:cd18811 144 DPLTET 149
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
430-573 |
4.82e-03 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350677 [Multi-domain] Cd Length: 182 Bit Score: 39.47 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 430 GAGK-----SLCYQLpalLYAQRSPCLTLVVSPlLSLMDDQVSDL----PScLKAACLHSgmTKKQRESVLKKVRAAQVH 500
Cdd:cd17919 29 GLGKtlqaiAFLAYL---LKEGKERGPVLVVCP-LSVLENWEREFekwtPD-LRVVVYHG--SQRERAQIRAKEKLDKFD 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039749727 501 VLIVSPEALVGCgargpgslpqAAQLPPIAFACI--DEVHCL----SQWShnfrpcylRVCKVLREHMgvRcfLGLTAT 573
Cdd:cd17919 102 VVLTTYETLRRD----------KASLRKFRWDLVvvDEAHRLknpkSQLS--------KALKALRAKR--R--LLLTGT 158
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
674-739 |
5.20e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 41.10 E-value: 5.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039749727 674 YHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVLH--------LGLPP-SFESYVQAIGRAGRDG 739
Cdd:PRK02362 309 HHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRdyrrydggAGMQPiPVLEYHQMAGRAGRPG 383
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
674-737 |
5.58e-03 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 40.96 E-value: 5.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039749727 674 YHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVL-------HLGLP--PSFESYvQAIGRAGR 737
Cdd:PRK00254 301 HHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIrdtkrysNFGWEdiPVLEIQ-QMMGRAGR 372
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
671-737 |
5.59e-03 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 40.56 E-value: 5.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039749727 671 AEAYHAGMSSQERRRVQQAFMRGHLRMVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAIGRAGR 737
Cdd:PRK10590 272 SAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
371-449 |
6.52e-03 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 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: 350711 [Multi-domain] Cd Length: 222 Bit Score: 39.67 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039749727 371 CPTPMSPLYPPGplgqvaeTPAEVFQALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLPAL--LYAQRS 448
Cdd:cd17953 7 CPKPIQKWSQCG-------LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhIKDQRP 79
|
.
gi 1039749727 449 P 449
Cdd:cd17953 80 V 80
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
473-505 |
6.85e-03 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 36.81 E-value: 6.85e-03
10 20 30
....*....|....*....|....*....|...
gi 1039749727 473 LKAACLHSGMTKKQRESVLKKVRAAQVHVLIVS 505
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVAT 44
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
393-440 |
7.32e-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: 7.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1039749727 393 EVFQALERLGYRAFRPGQERAIMRILSGISTLLVLPTGAGKSLCYQLP 440
Cdd:cd17959 11 PLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIP 58
|
|
| |
