|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
38-203 |
5.59e-77 |
|
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: 246.34 E-value: 5.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 38 DKHVLLCASTASGKTEAAFFPILTLLSEEPPASVGALYIAPLKALINDQFERLTDLCAEG--GIPVWAWHGDVAQSRKRK 115
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEIdlEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 116 LIEHPSGILQITPESLEALLLRKHSviPRLFGDLRFIVIDEIHSLMRGDRGGQTMCLIERLARLSGSDPRRIGLSATIGD 195
Cdd:cd17922 81 QLKNPPGILITTPESLELLLVNKKL--RELFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKLTGRPLRRIGLSATLGN 158
|
....*...
gi 1821503202 196 PQKAADFL 203
Cdd:cd17922 159 LEEAAAFL 166
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1-614 |
1.19e-63 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 229.22 E-value: 1.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 1 MTVFERYAPF---VQDFiYAHRWEKLRSVQVAAGNAVFNtDKHVLLCASTASGKTEAAFFPILTLLSEEP-----PASVG 72
Cdd:COG1201 1 MSAEDVLSLLhpaVRAW-FAARFGAPTPPQREAWPAIAA-GESTLLIAPTGSGKTLAAFLPALDELARRPrpgelPDGLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 73 ALYIAPLKALINDqFER-----LTDLCAEGGIPVWAW-----HGDVAQSRKRKLIEHPSGILQITPESLEALLLRKHSvi 142
Cdd:COG1201 79 VLYISPLKALAND-IERnlrapLEEIGEAAGLPLPEIrvgvrTGDTPASERQRQRRRPPHILITTPESLALLLTSPDA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 143 PRLFGDLRFIVIDEIHSLMRGDRGGQTMCLIERLARLSGSDPRRIGLSATIGDPQKAADFLCGssrrgavvpQFEQPPVR 222
Cdd:COG1201 156 RELLRGVRTVIVDEIHALAGSKRGVHLALSLERLRALAPRPLQRIGLSATVGPLEEVARFLVG---------YEDPRPVT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 223 wrlamehffIAKTEEPHRTDyasVMVDAQVSDQRAadasdagkaagdalrqasqkPRPGAHSSkasaqlelesasdqAPA 302
Cdd:COG1201 227 ---------IVDAGAGKKPD---LEVLVPVEDLIE--------------------RFPWAGHL--------------WPH 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 303 SADPGLAYVFEHsagRKCLVFSNSREECEAVTSTLREycRRAGEPERFLIHHGNLSTPLRLDAEALMKeENALLTVCTTA 382
Cdd:COG1201 261 LYPRVLDLIEAH---RTTLVFTNTRSQAERLFQRLNE--LNPEDALPIAAHHGSLSREQRLEVEEALK-AGELRAVVATS 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 383 TLELGIDIGRLERAFQINAPFTVSAFLQRMGRTG-RRGSPPEMRFVmredeVDSREmlpaqlpwELIHGIGLVESWREdH 461
Cdd:COG1201 335 SLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEVSKGRLV-----PTHRD--------ELVECAAALEAARA-G 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 462 WVEPPRLERLPFSLLYHQTMAtLASEGELTPAELARRVLTLSPFRRISPQDYR-------TLLLHLLDTDQ---IQRTER 531
Cdd:COG1201 401 EIEARRPPRNPLDVLAQHIVA-MAAGGPFDVDELYAEVRRAYPYRDLTREDFDavldflaGGGPSLRAYERyarIVRDRV 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 532 GGLIVGLAGER---VTSGfkfyAVFQENEEYSVR--ADGQELGTL----VQPPPAGEKIAIAGRVWEVEEVDPKRhiVWC 602
Cdd:COG1201 480 DGRLGARRGAArlaRTNI----GTIPDRGMLKVRlvRGGRRLGELeeefVEELRPGDVFVLGGRSLRIERIRGMR--VYV 553
|
650
....*....|....*
gi 1821503202 603 RLTEG---RVPAFFG 614
Cdd:COG1201 554 RPAPGkppTVPSWFG 568
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
21-434 |
6.76e-52 |
|
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: 193.90 E-value: 6.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 21 EKLRSVQVAAGNAVFNtDKHVLLCASTASGKTEAAFFPILTLLSEEPPASvgALYIAPLKALINDQFERLTDLCAEGG-- 98
Cdd:COG1205 55 ERLYSHQAEAIEAARA-GKNVVIATPTASGKSLAYLLPVLEALLEDPGAT--ALYLYPTKALARDQLRRLRELAEALGlg 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 99 IPVWAWHGDVAQSRKRKLIEHPSgILQITPESLEALLLRKHSVIPRLFGDLRFIVIDEIHSLmRGDRGGQTMCLIERLAR 178
Cdd:COG1205 132 VRVATYDGDTPPEERRWIREHPD-IVLTNPDMLHYGLLPHHTRWARFFRNLRYVVIDEAHTY-RGVFGSHVANVLRRLRR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 179 LS---GSDPRRIGLSATIGDPQKAADFLCG---------SSRRGAVVPQFEQPPVRWRLamehffiakteephrtdyasv 246
Cdd:COG1205 210 ICrhyGSDPQFILASATIGNPAEHAERLTGrpvtvvdedGSPRGERTFVLWNPPLVDDG--------------------- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 247 mvdaqvsdQRAADASDAGKAAGDALRQasqkprpgahsskasaqlelesasdqapasadpglayvfehsaGRKCLVFSNS 326
Cdd:COG1205 269 --------IRRSALAEAARLLADLVRE-------------------------------------------GLRTLVFTRS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 327 REECEAVTSTLREYCRRAGEPERFLIHHGNLSTPLRLDAEALMKEENaLLTVCTTATLELGIDIGRLERAFQINAPFTVS 406
Cdd:COG1205 298 RRGAELLARYARRALREPDLADRVAAYRAGYLPEERREIERGLRSGE-LLGVVSTNALELGIDIGGLDAVVLAGYPGTRA 376
|
410 420
....*....|....*....|....*...
gi 1821503202 407 AFLQRMGRTGRRGSPPEMRFVMREDEVD 434
Cdd:COG1205 377 SFWQQAGRAGRRGQDSLVVLVAGDDPLD 404
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
9-513 |
4.08e-50 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 189.30 E-value: 4.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 9 PFVQDFIYAHRWEkLRSVQVAAGNAvFNTDKHVLLCASTASGKTEAAFFPILT-LLSEEPPASVG--ALYIAPLKALIND 85
Cdd:TIGR04121 1 SPFEAWFAARGWT-PRPFQLEMWAA-ALEGRSGLLIAPTGSGKTLAGFLPSLIdLAGPEAPKEKGlhTLYITPLRALAVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 86 QFERLTDLCAEGGIPvwaWH-----GDVAQSRKRKLIEHPSGILQITPESLEALLLRKHSviPRLFGDLRFIVIDEIHSL 160
Cdd:TIGR04121 79 IARNLQAPIEELGLP---IRvetrtGDTSSSERARQRKKPPDILLTTPESLALLLSYPDA--ARLFKDLRCVVVDEWHEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 161 MRGDRGGQTMCLIERLARLSgSDPRRIGLSATIGDPQKAADFLCGSSRRGAVVpqfeqppVRwrlamehffiakteephr 240
Cdd:TIGR04121 154 AGSKRGDQLELALARLRRLA-PGLRRWGLSATIGNLEEARRVLLGVGGAPAVL-------VR------------------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 241 tdyasvmvdaqvsdqraadASDAGKAAGDALRQASQKPRP-GAHSSKASAQlELESASDQApasadpglayvfehsagRK 319
Cdd:TIGR04121 208 -------------------GKLPKAIEVISLLPESEERFPwAGHLGLRALP-EVYAEIDQA-----------------RT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 320 CLVFSNSREECEAVTSTLREYCrragePERFL---IHHGNLSTPLRLDAEALMKEENALLTVCtTATLELGIDIGRLERA 396
Cdd:TIGR04121 251 TLVFTNTRSQAELWFQALWEAN-----PEFALpiaLHHGSLDREQRRWVEAAMAAGRLRAVVC-TSSLDLGVDFGPVDLV 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 397 FQINAPFTVSAFLQRMGRTGRR-GSPPEMRFVmredevdsremlPAQlPWELIHGIGLVESWREdHWVEPPRLERLPFSL 475
Cdd:TIGR04121 325 IQIGSPKGVARLLQRAGRSNHRpGEPSRALLV------------PTN-RLELLECAAAREAVAA-GAVEGRPPPPGPLDV 390
|
490 500 510
....*....|....*....|....*....|....*...
gi 1821503202 476 LYhQTMATLASEGELTPAELARRVLTLSPFRRISPQDY 513
Cdd:TIGR04121 391 LA-QHLLTLACGGGFDPDELFAEVRSTAPYADLTREEF 427
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
39-418 |
5.19e-42 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 165.44 E-value: 5.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 39 KHVLLCASTASGKTEAAFFPI---LTLLSEEP--PASVGALYIAPLKALINDQ----FERLTDLCAE--------GGIPV 101
Cdd:PRK13767 48 KNVLISSPTGSGKTLAAFLAIideLFRLGREGelEDKVYCLYVSPLRALNNDIhrnlEEPLTEIREIakergeelPEIRV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 102 WAWHGDVAQSRKRKLIEHPSGILQITPESLeALLLrkhsVIPRL---FGDLRFIVIDEIHSLMRGDRGGQTMCLIERLAR 178
Cdd:PRK13767 128 AIRTGDTSSYEKQKMLKKPPHILITTPESL-AILL----NSPKFrekLRTVKWVIVDEIHSLAENKRGVHLSLSLERLEE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 179 LSGSDPRRIGLSATIGDPQKAADFLCGSSRRGA-----VVpqfeqpPVRWRLAMEhffiakteephrtdyasVMVDAQVS 253
Cdd:PRK13767 203 LAGGEFVRIGLSATIEPLEEVAKFLVGYEDDGEprdceIV------DARFVKPFD-----------------IKVISPVD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 254 DQRAADASDAGKAAGDALrqasqkprpgahsskasaqLELesasdqapasadpglayVFEHsagRKCLVFSNSREECEAV 333
Cdd:PRK13767 260 DLIHTPAEEISEALYETL-------------------HEL-----------------IKEH---RTTLIFTNTRSGAERV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 334 TSTLREYCrragePERFLI-----HHGNLSTPLRLDAEALMKeeNALLTVCTTAT-LELGIDIGRLERAFQINAPFTVSA 407
Cdd:PRK13767 301 LYNLRKRF-----PEEYDEdnigaHHSSLSREVRLEVEEKLK--RGELKVVVSSTsLELGIDIGYIDLVVLLGSPKSVSR 373
|
410
....*....|.
gi 1821503202 408 FLQRMGRTGRR 418
Cdd:PRK13767 374 LLQRIGRAGHR 384
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
294-430 |
7.10e-42 |
|
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: 149.72 E-value: 7.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 294 ESASDQAPASADPGLAYVFEHSAGRKCLVFSNSREECEAVTSTLREYCRRAGEPERFLIHHGNLSTPLRLDAEALMKEEN 373
Cdd:cd18796 15 EIFPWAGESGADAYAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRVPPDFIALHHGSLSRELREEVEAALKRGD 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821503202 374 aLLTVCTTATLELGIDIGRLERAFQINAPFTVSAFLQRMGRTGRRGSPPEMRFVMRE 430
Cdd:cd18796 95 -LKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLVPT 150
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
23-200 |
3.71e-39 |
|
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: 143.11 E-value: 3.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 23 LRSVQVAAGNAVFNtDKHVLLCASTASGKTEAAFFPILTLLSEEPpaSVGALYIAPLKALINDQFERLTDLCA--EGGIP 100
Cdd:cd17923 1 LYSHQAEAIEAARA-GRSVVVTTGTASGKSLCYQLPILEALLRDP--GSRALYLYPTKALAQDQLRSLRELLEqlGLGIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 101 VWAWHGDVAQSRKRKLIEHPSGILQITPESLEALLLRKHSVIPRLFGDLRFIVIDEIHSLmRGDRGGQTMCLIERLARLS 180
Cdd:cd17923 78 VATYDGDTPREERRAIIRNPPRILLTNPDMLHYALLPHHDRWARFLRNLRYVVLDEAHTY-RGVFGSHVALLLRRLRRLC 156
|
170 180
....*....|....*....|...
gi 1821503202 181 ---GSDPRRIGLSATIGDPQKAA 200
Cdd:cd17923 157 rryGADPQFILTSATIGNPAEHA 179
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
24-202 |
1.30e-30 |
|
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: 118.11 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 24 RSVQVAAGNAVFNtDKHVLLCASTASGKTEAAFFPILTLLSEEPPASVgALYIAPLKALINDQFERLTDLCAEGGIPVWA 103
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQ-ALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 104 WHGDVAQSRKRKLIEHPSgILQITPESLEALLLRKhsvipRLFGDLRFIVIDEIHSLMRGDRGGQtmclIERLARLSGSD 183
Cdd:pfam00270 79 LLGGDSRKEQLEKLKGPD-ILVGTPGRLLDLLQER-----KLLKNLKLLVLDEAHRLLDMGFGPD----LEEILRRLPKK 148
|
170
....*....|....*....
gi 1821503202 184 PRRIGLSATIgdPQKAADF 202
Cdd:pfam00270 149 RQILLLSATL--PRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
15-196 |
3.60e-30 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 118.36 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 15 IYAHRWEKLRSVQVAAGNAVFNTDKHVLLCASTASGKTEAAFFPILTLLSEEPPASVgaLYIAPLKALINDQFERLTDLC 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV--LVLVPTRELAEQWAEELKKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 95 AE-GGIPVWAWHGDVAQSRKRKLIEHPSGILQITPESLEALLLRKhsviPRLFGDLRFIVIDEIHSLMRGDRGGQTMCLI 173
Cdd:smart00487 79 PSlGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLEND----KLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180
....*....|....*....|...
gi 1821503202 174 ERLARlsgsDPRRIGLSATIGDP 196
Cdd:smart00487 155 KLLPK----NVQLLLLSATPPEE 173
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-419 |
5.38e-30 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 125.39 E-value: 5.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 1 MTVFERYAPFVQDFIYAHRWEKLRSVQVAAGNAVFNTDKHVLLCASTASGKTEAAFFPILTLLSEEPPAsvgaLYIAPLK 80
Cdd:COG1204 1 MKVAELPLEKVIEFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGKA----LYIVPLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 81 ALINDQFERLTDLCAEGGIPVWAWHGDVaQSRKRKLIEhpSGILQITPESLEALLLRKHSVIPrlfgDLRFIVIDEIHSL 160
Cdd:COG1204 77 ALASEKYREFKRDFEELGIKVGVSTGDY-DSDDEWLGR--YDILVATPEKLDSLLRNGPSWLR----DVDLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 161 MRGDRGGQTMCLIERLARLsGSDPRRIGLSATIGDPQKAADFLcgssrrGAVVPQFEQPPVRWRLA-MEHFFIAKTEEPH 239
Cdd:COG1204 150 DDESRGPTLEVLLARLRRL-NPEAQIVALSATIGNAEEIAEWL------DAELVKSDWRPVPLNEGvLYDGVLRFDDGSR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 240 RTDYASVmvdaqvsdqraadasdagKAAGDALRQASQkprpgA---HSSKASAQLELESASDQAPASADPGLAYVFEHSA 316
Cdd:COG1204 223 RSKDPTL------------------ALALDLLEEGGQ-----VlvfVSSRRDAESLAKKLADELKRRLTPEEREELEELA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 317 gRKCLVFSNSREECEAVTSTLReycRRAGeperflIHHGNLSTPLRLDAEALMKEENALLTVCTTaTLELGID------- 389
Cdd:COG1204 280 -EELLEVSEETHTNEKLADCLE---KGVA------FHHAGLPSELRRLVEDAFREGLIKVLVATP-TLAAGVNlparrvi 348
|
410 420 430
....*....|....*....|....*....|
gi 1821503202 390 IGRLERAFqiNAPFTVSAFLQRMGRTGRRG 419
Cdd:COG1204 349 IRDTKRGG--MVPIPVLEFKQMAGRAGRPG 376
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
27-203 |
5.50e-27 |
|
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: 108.50 E-value: 5.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 27 QVAAGNAVFNTDKHVLLCASTASGKTEAAFFPILTLLSEEPPAsvgALYIAPLKALINDQFERLTDLCAEGGIPVWAWHG 106
Cdd:cd17921 6 QREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK---AVYIAPTRALVNQKEADLRERFGPLGKNVGLLTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 107 DVaQSRKRKLIEhpSGILQITPESLEALLLRKHSvipRLFGDLRFIVIDEIHSLMRGDRGGQTMCLIERLARLSGSdPRR 186
Cdd:cd17921 83 DP-SVNKLLLAE--ADILVATPEKLDLLLRNGGE---RLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRINKN-ARF 155
|
170
....*....|....*..
gi 1821503202 187 IGLSATIGDPQKAADFL 203
Cdd:cd17921 156 VGLSATLPNAEDLAEWL 172
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
45-506 |
2.39e-25 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 113.10 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 45 ASTASGKTEAAFFPILTLLSEE---------PPASVGALYIAPLKAL--------------INDQFERLTDLCAEggIPV 101
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFREggedtreahKRKTSRILYISPIKALgtdvqrnlqiplkgIADERRRRGETEVN--LRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 102 WAWHGDVAQSRKRKLIEHPSGILQITPESLEALLLRKHSVIPRlfgDLRFIVIDEIHSLMRGDRGGQTMCLIERLARLSG 181
Cdd:PRK09751 81 GIRTGDTPAQERSKLTRNPPDILITTPESLYLMLTSRARETLR---GVETVIIDEVHAVAGSKRGAHLALSLERLDALLH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 182 SDPRRIGLSATIGDPQKAADFLcGSSRRGAVVpqfeQPPvrwrlAMEHFFIakteephrtdyaSVMVDAQVSDQRAADAS 261
Cdd:PRK09751 158 TSAQRIGLSATVRSASDVAAFL-GGDRPVTVV----NPP-----AMRHPQI------------RIVVPVANMDDVSSVAS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 262 DAGKAAGDAlrqasqkpRPGAHSSKASAQLelesasdqapasadpgLAYVFEHsagRKCLVFSNSREECEAVTSTLRE-Y 340
Cdd:PRK09751 216 GTGEDSHAG--------REGSIWPYIETGI----------------LDEVLRH---RSTIVFTNSRGLAEKLTARLNElY 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 341 CRR-AGEP-----------------------ERFLI--HHGNLSTPLRLDAEALMKeENALLTVCTTATLELGIDIGRLE 394
Cdd:PRK09751 269 AARlQRSPsiavdaahfestsgatsnrvqssDVFIArsHHGSVSKEQRAITEQALK-SGELRCVVATSSLELGIDMGAVD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 395 RAFQINAPFTVSAFLQRMGRTGRR--GSPPEMRFV-MREDEVDSREMLPAQLPwelihgiGLVESwredhwVEPPrleRL 471
Cdd:PRK09751 348 LVIQVATPLSVASGLQRIGRAGHQvgGVSKGLFFPrTRRDLVDSAVIVECMFA-------GRLEN------LTPP---HN 411
|
490 500 510
....*....|....*....|....*....|....*
gi 1821503202 472 PFSLLYHQTMATLASEgELTPAELARRVLTLSPFR 506
Cdd:PRK09751 412 PLDVLAQQTVAAAAMD-ALQVDEWYSRVRRAAPWK 445
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
39-192 |
6.63e-21 |
|
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: 89.77 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 39 KHVLLCASTASGKTEAAFFPILTLLSEEPPasvGALYIAPLKALINDQFERLTDLcAEGGIPVWAWHGDVAQSRKRKLIE 118
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKKGK---KVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821503202 119 HPSGILQITPESLEALLLRKHsviPRLFGDLRFIVIDEIHSLMRGDRGGQTMCLIERLARLsgSDPRRIGLSAT 192
Cdd:cd00046 78 GDADIIIATPDMLLNLLLRED---RLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGL--KNAQVILLSAT 146
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
21-203 |
4.62e-19 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350777 [Multi-domain] Cd Length: 214 Bit Score: 86.66 E-value: 4.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 21 EKLRSVQVAAGNAVFNTDKHVLLCASTASGKTEAAffpILTLLSE-----EPPASVGA-----LYIAPLKALINDQF--- 87
Cdd:cd18019 16 KSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVA---LLTILREigkhrNPDGTINLdafkiVYIAPMKALVQEMVgnf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 88 -ERLTDLcaegGIPVWAWHGDVAQSRKRKlieHPSGILQITPEslealllrKHSVIPRLFGDL------RFIVIDEIHsL 160
Cdd:cd18019 93 sKRLAPY----GITVAELTGDQQLTKEQI---SETQIIVTTPE--------KWDIITRKSGDRtytqlvRLIIIDEIH-L 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1821503202 161 MRGDRGGQTMCLIERLAR---LSGSDPRRIGLSATIGDPQKAADFL 203
Cdd:cd18019 157 LHDDRGPVLESIVARTIRqieQTQEYVRLVGLSATLPNYEDVATFL 202
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
22-203 |
1.54e-18 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain] Cd Length: 177 Bit Score: 83.92 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 22 KLRSVQVAAGNAVFNTDKHVLLCASTASGKTEAAFFPILTLLSEeppasvG--ALYIAPLKALINDQFERLTDLcAEGGI 99
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLE------GgkALYLVPLRALASEKYEEFKKL-EEIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 100 PVWAWHGDVaQSRKRKLIEHPsgILQITPESLEALLlrKHSviPRLFGDLRFIVIDEIHSLMRGDRGGQTMCLIERLARL 179
Cdd:cd18028 74 KVGISTGDY-DEDDEWLGDYD--IIVATYEKFDSLL--RHS--PSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRRL 146
|
170 180
....*....|....*....|....
gi 1821503202 180 SGSdPRRIGLSATIGDPQKAADFL 203
Cdd:cd18028 147 NPN-TQIIGLSATIGNPDELAEWL 169
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
22-203 |
1.01e-16 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350778 [Multi-domain] Cd Length: 199 Bit Score: 79.40 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 22 KLRSVQVAAGNAVFNTDKHVLLCASTASGKTEAAFFPILTLLSE--EPPASV-----GALYIAPLKALINDQFERLTDLC 94
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQhvNQGGVIkkddfKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 95 AEGGIPVWAWHGDVaQSRKRKLIEhpSGILQITPESLEaLLLRKHSVIPRLFGDLRFIVIDEIHsLMRGDRGGQTMCLIE 174
Cdd:cd18020 81 APLGIKVKELTGDM-QLTKKEIAE--TQIIVTTPEKWD-VVTRKSSGDVALSQLVRLLIIDEVH-LLHDDRGPVIESLVA 155
|
170 180 190
....*....|....*....|....*....|..
gi 1821503202 175 RLARL---SGSDPRRIGLSATIGDPQKAADFL 203
Cdd:cd18020 156 RTLRQvesTQSMIRIVGLSATLPNYLDVADFL 187
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
25-203 |
3.25e-15 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 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: 350781 [Multi-domain] Cd Length: 206 Bit Score: 75.09 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 25 SVQVAAGNAVFNTDKHVLLCASTASGKT---EAAffpILTLLSEEPPASVG---ALYIAPLKALINDQF----ERLTDLc 94
Cdd:cd18023 4 RIQSEVFPDLLYSDKNFVVSAPTGSGKTvlfELA---ILRLLKERNPLPWGnrkVVYIAPIKALCSEKYddwkEKFGPL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 95 aegGIPVWAWHGDVAQSRKRKlIEHPSGILQiTPESLEAlLLRKHSVIPRLFGDLRFIVIDEIHsLMRGDRGG------- 167
Cdd:cd18023 80 ---GLSCAELTGDTEMDDTFE-IQDADIILT-TPEKWDS-MTRRWRDNGNLVQLVALVLIDEVH-IIKENRGAtlevvvs 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1821503202 168 --QTMCLIERLARLSGSDPRRIGLSATIGDPQKAADFL 203
Cdd:cd18023 153 rmKTLSSSSELRGSTVRPMRFVAVSATIPNIEDLAEWL 190
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
308-419 |
5.79e-15 |
|
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: 71.47 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 308 LAYVFEHSAGRKCLVFSNSREECEAvtstlREYCRRAGEpeRFLIHHGNLSTPLRLDAEALMKEENALLTVCTTAtLELG 387
Cdd:pfam00271 6 LLELLKKERGGKVLIFSQTKKTLEA-----ELLLEKEGI--KVARLHGDLSQEEREEILEDFRKGKIDVLVATDV-AERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 1821503202 388 IDIGRLERAFQINAPFTVSAFLQRMGRTGRRG 419
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
296-421 |
2.64e-14 |
|
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: 70.75 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 296 ASDQAPASADPGLAYVFEHS--AGRKCLVFSNSREECEAVTSTLRE-YCRRAGEPERFLIHHGNLSTPLRLDAEALMKEE 372
Cdd:cd18797 12 RKDGERGSARREAARLFADLvrAGVKTIVFCRSRKLAELLLRYLKArLVEEGPLASKVASYRAGYLAEDRREIEAELFNG 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1821503202 373 NaLLTVCTTATLELGIDIGRLERAFQINAPFTVSAFLQRMGRTGRRGSP 421
Cdd:cd18797 92 E-LLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKD 139
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
26-203 |
9.67e-14 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350780 [Multi-domain] Cd Length: 189 Bit Score: 70.48 E-value: 9.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 26 VQVAAGNAVFNTDKHVLLCASTASGKTEAAFFPILTLLSEEPPASVgaLYIAPLKALINdqfERLTDlcaeggipvwaWH 105
Cdd:cd18022 5 IQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKV--VYIAPLKALVR---ERVDD-----------WK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 106 GDVAQSRKRKLIE------------HPSGILQITPESLEALllrKHSVIPRLF-GDLRFIVIDEIHsLMRGDRGGQTMCL 172
Cdd:cd18022 69 KRFEEKLGKKVVEltgdvtpdmkalADADIIITTPEKWDGI---SRSWQTREYvQQVSLIIIDEIH-LLGSDRGPVLEVI 144
|
170 180 190
....*....|....*....|....*....|....
gi 1821503202 173 IER---LARLSGSDPRRIGLSATIGDPQKAADFL 203
Cdd:cd18022 145 VSRmnyISSQTEKPVRLVGLSTALANAGDLANWL 178
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
38-209 |
5.82e-13 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 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: 350783 [Multi-domain] Cd Length: 192 Bit Score: 68.16 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 38 DKHVLLCASTASGKTEAAFFPILTLLSEEPPASVgaLYIAPLKALIN----DQFERLTDLCAEGGIPVWAwhgdvAQSRK 113
Cdd:cd18025 16 RESALIVAPTSSGKTFISYYCMEKVLRESDDGVV--VYVAPTKALVNqvvaEVYARFSKKYPPSGKSLWG-----VFTRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 114 RKLIEHPSGILQIT-PESLEALLLRKH--SVIPRLfgdlRFIVIDEIHSLmrgdrGGQTMCLI-ERLarLSGSDPRRIGL 189
Cdd:cd18025 89 YRHNNPMNCQVLITvPECLEILLLSPHnaSWVPRI----KYVIFDEIHSI-----GQSEDGAVwEQL--LLLIPCPFLAL 157
|
170 180
....*....|....*....|
gi 1821503202 190 SATIGDPQKAADFLCGSSRR 209
Cdd:cd18025 158 SATIGNPQKFHEWLQSVQRA 177
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
336-419 |
9.33e-11 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 58.76 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 336 TLREYCRRAGEpeRFLIHHGNLSTPLRLDAEALMKEENALLtVCTTATLELGIDIGRLERAFQINAPFTVSAFLQRMGRT 415
Cdd:smart00490 2 ELAELLKELGI--KVARLHGGLSQEEREEILDKFNNGKIKV-LVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78
|
....
gi 1821503202 416 GRRG 419
Cdd:smart00490 79 GRAG 82
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
39-203 |
3.29e-10 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 63.68 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 39 KHVLLCASTASGKTEAAFFPILTLLSEEPPASVgalYIAPLKALINDQFERLTDLcAEGGIPVWAWHGDVaQSRKRKLIE 118
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKLLREGGKAV---YLVPLKALAEEKYREFKDW-EKLGLRVAMTTGDY-DSTDEWLGK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 119 HpsGILQITPESLEALLLRKHSVIPrlfgDLRFIVIDEIHSLMRGDRGGqTMCLIerLARLSGSdPRRIGLSATIGDPQK 198
Cdd:PRK00254 115 Y--DIIIATAEKFDSLLRHGSSWIK----DVKLVVADEIHLIGSYDRGA-TLEMI--LTHMLGR-AQILGLSATVGNAEE 184
|
....*
gi 1821503202 199 AADFL 203
Cdd:PRK00254 185 LAEWL 189
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
20-207 |
3.72e-09 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 57.27 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 20 WEKLRSVQVAAGNAVFNTDKHVLLCASTASGKTEAAFFPILTLLSEEPPASvgALYIAPLKALINDQFERLTDLCAE-GG 98
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGR--AVYIAPMQELVDARYKDWRAKFGPlLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 99 IPVWAWHGDVAQSrkRKLIEHpSGILQITPESLEALLL----RKHsviprlFGDLRFIVIDEIHslMRGDRGGQTM-CLI 173
Cdd:cd18021 79 KKVVKLTGETSTD--LKLLAK-SDVILATPEQWDVLSRrwkqRKN------VQSVELFIADELH--LIGGENGPVYeVVV 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 1821503202 174 ERLARLSG---SDPRRIGLSATIGDPQKAADFL-CGSS 207
Cdd:cd18021 148 SRMRYISSqleKPIRIVGLSSSLANARDVGEWLgASKS 185
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
22-414 |
1.49e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 58.11 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 22 KLRSVQVAAGNAVFNT----DKHVLLCASTASGKTEAAFFPILTLLSEEPpasvgALYIAPLKALINDQFERLTDlcaeg 97
Cdd:COG1061 80 ELRPYQQEALEALLAAlergGGRGLVVAPTGTGKTVLALALAAELLRGKR-----VLVLVPRRELLEQWAEELRR----- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 98 gipvwaWHGDVAQSRKRKLIEHPsgILQITPESLealllRKHSVIPRLFGDLRFIVIDEIHSLmrgdrGGQTmclIERLA 177
Cdd:COG1061 150 ------FLGDPLAGGGKKDSDAP--ITVATYQSL-----ARRAHLDELGDRFGLVIIDEAHHA-----GAPS---YRRIL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 178 RLSgSDPRRIGLSATigdpqkaadflcgssrrgavvpqfeqppvrwrlamehffiakteePHRTDYASVMVDAQ---VSD 254
Cdd:COG1061 209 EAF-PAAYRLGLTAT---------------------------------------------PFRSDGREILLFLFdgiVYE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 255 QRAADASDAGkaagdALRQASQKPRPGAHSSKASAQLELESASDQAPASADPGL-----AYVFEHSAGRKCLVFSNSREE 329
Cdd:COG1061 243 YSLKEAIEDG-----YLAPPEYYGIRVDLTDERAEYDALSERLREALAADAERKdkilrELLREHPDDRKTLVFCSSVDH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 330 CEAVTSTLREycrrAGEPERFLihHGNLSTPLRLDA-EALmkEENALLTVCTTATLELGIDIGRLERAFqINAPF-TVSA 407
Cdd:COG1061 318 AEALAELLNE----AGIRAAVV--TGDTPKKEREEIlEAF--RDGELRILVTVDVLNEGVDVPRLDVAI-LLRPTgSPRE 388
|
....*..
gi 1821503202 408 FLQRMGR 414
Cdd:COG1061 389 FIQRLGR 395
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
8-419 |
1.56e-08 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 58.41 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 8 APFVQDFIYAH--RWEKLRSV-----QVAAGNAVfNTDKHVLLCASTASGKTEAAFFPILTLLSEeppaSVGALYIAPLK 80
Cdd:COG4581 4 SPARADARLEAlaDFAEERGFeldpfQEEAILAL-EAGRSVLVAAPTGSGKTLVAEFAIFLALAR----GRRSFYTAPIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 81 ALINDQFErltDLCAE-GGIPVWAWHGDVAqsrkrklIEHPSGILQITPESLEALLLRKhsviPRLFGDLRFIVIDEIHS 159
Cdd:COG4581 79 ALSNQKFF---DLVERfGAENVGLLTGDAS-------VNPDAPIVVMTTEILRNMLYRE----GADLEDVGVVVMDEFHY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 160 LMRGDRGG---QTMCLIERLARLsgsdprrIGLSATIGDPQKAADFLcgSSRRG--AVVPQFEQP-PVRWrlameHFFia 233
Cdd:COG4581 145 LADPDRGWvweEPIIHLPARVQL-------VLLSATVGNAEEFAEWL--TRVRGetAVVVSEERPvPLEF-----HYL-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 234 ktEEPHRTDYASVMVDAQVSDQRAADASDagkaagdaLRQASQKP-------RPGAHsskASAQlELESASDQAPASADp 306
Cdd:COG4581 209 --VTPRLFPLFRVNPELLRPPSRHEVIEE--------LDRGGLLPaivfifsRRGCD---EAAQ-QLLSARLTTKEERA- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 307 GLAYVFEHSAGRKCLVFsnsreeceavTSTLREYCRRagepeRFLIHHGNLSTPLRLDAEALMKEenALLTV-CTTATLE 385
Cdd:COG4581 274 EIREAIDEFAEDFSVLF----------GKTLSRLLRR-----GIAVHHAGMLPKYRRLVEELFQA--GLLKVvFATDTLA 336
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1821503202 386 LGID-------IGRLERaF--QINAPFTVSAFLQRMGRTGRRG 419
Cdd:COG4581 337 VGINmpartvvFTKLSK-FdgERHRPLTAREFHQIAGRAGRRG 378
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
308-419 |
3.13e-08 |
|
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: 52.89 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 308 LAYVFEHSAGRKCLVFSNSREECEAVTSTLREycrragEPERFLIHHGNLSTPLRLDA-EALMKEENALLtVCTtatlEL 386
Cdd:cd18787 18 LLLLLEKLKPGKAIIFVNTKKRVDRLAELLEE------LGIKVAALHGDLSQEERERAlKKFRSGKVRVL-VAT----DV 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 1821503202 387 ---GIDIGRLERAFQINAPFTVSAFLQRMGRTGRRG 419
Cdd:cd18787 87 aarGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAG 122
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
35-222 |
4.49e-08 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 56.82 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 35 FNTDKHVLLCASTASGKTEAAFFPILtllsEEPPASVGALYIAPLKALINDQFERLTDLcAEGGIPVWAWHGDVAQSRKr 114
Cdd:PRK01172 34 LRKGENVIVSVPTAAGKTLIAYSAIY----ETFLAGLKSIYIVPLRSLAMEKYEELSRL-RSLGMRVKISIGDYDDPPD- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 115 kLIEHPSGILqITPESLEALLlrKHSviPRLFGDLRFIVIDEIHSLMRGDRgGQTMCLIERLARLSGSDPRRIGLSATIG 194
Cdd:PRK01172 108 -FIKRYDVVI-LTSEKADSLI--HHD--PYIINDVGLIVADEIHIIGDEDR-GPTLETVLSSARYVNPDARILALSATVS 180
|
170 180
....*....|....*....|....*...
gi 1821503202 195 DPQKAADFLCGSSrrgaVVPQFEQPPVR 222
Cdd:PRK01172 181 NANELAQWLNASL----IKSNFRPVPLK 204
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
20-158 |
5.35e-08 |
|
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: 53.69 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 20 WEKLRSVQVAAGNAVFNtDKHVLLCASTASGKT-----EAAFFPILTLLseeppasvgalyIAPLKALINDQFERLTDLc 94
Cdd:cd17920 10 YDEFRPGQLEAINAVLA-GRDVLVVMPTGGGKSlcyqlPALLLDGVTLV------------VSPLISLMQDQVDRLQQL- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821503202 95 aegGIPVWAWHGDVAQSRKRK-LIEHPSG---ILQITPESLE-----ALLLRKHSviprlFGDLRFIVIDEIH 158
Cdd:cd17920 76 ---GIRAAALNSTLSPEEKREvLLRIKNGqykLLYVTPERLLspdflELLQRLPE-----RKRLALIVVDEAH 140
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
313-419 |
1.98e-07 |
|
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: 51.01 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 313 EHSAGRKCLVFSNSREECEAVTSTLreycrrAGeperFLIHHGNLSTPLRLDAEALMKeENALLTVCTTATLELGID--- 389
Cdd:cd18795 39 TVSEGKPVLVFCSSRKECEKTAKDL------AG----IAFHHAGLTREDRELVEELFR-EGLIKVLVATSTLAAGVNlpa 107
|
90 100 110
....*....|....*....|....*....|....*
gi 1821503202 390 ----IGRLER-AFQINAPFTVSAFLQRMGRTGRRG 419
Cdd:cd18795 108 rtviIKGTQRyDGKGYRELSPLEYLQMIGRAGRPG 142
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
17-202 |
3.95e-07 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It 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: 350714 [Multi-domain] Cd Length: 231 Bit Score: 51.86 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 17 AHRWEKLRSVQVAAGNAVFNTDKH--------VLLCASTASGKTEAAFFPILTLLSEEPPASVGALYIAPLKALIN---D 85
Cdd:cd17956 7 NNGITSAFPVQAAVIPWLLPSSKStppyrpgdLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKELVQqvyK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 86 QFERltdLCAEGGIPVWAWHGDVAQSRKRKLI--------EHPSGILQITPESLEALLLRKHSVIprlFGDLRFIVIDE- 156
Cdd:cd17956 87 VFES---LCKGTGLKVVSLSGQKSFKKEQKLLlvdtsgryLSRVDILVATPGRLVDHLNSTPGFT---LKHLRFLVIDEa 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821503202 157 ---------------IHSLMRGDRGGQTMCLIERLARLSGSDPRRIGLSATIG-DPQKAADF 202
Cdd:cd17956 161 drllnqsfqdwletvMKALGRPTAPDLGSFGDANLLERSVRPLQKLLFSATLTrDPEKLSSL 222
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
47-422 |
4.26e-07 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 53.81 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 47 TASGKTEAAffpILTLLSEeppASVG--ALYIAPLKALINDQFERLTDLcAEGGIPVWAWHGDVaQSRKRKLIEHpsGIL 124
Cdd:PRK02362 48 TASGKTLIA---ELAMLKA---IARGgkALYIVPLRALASEKFEEFERF-EELGVRVGISTGDY-DSRDEWLGDN--DII 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 125 QITPESLEALLLRKHSVIPrlfgDLRFIVIDEIHSLMRGDRGGQTMCLIERLARLSgSDPRRIGLSATIGDPQKAADFLc 204
Cdd:PRK02362 118 VATSEKVDSLLRNGAPWLD----DITCVVVDEVHLIDSANRGPTLEVTLAKLRRLN-PDLQVVALSATIGNADELADWL- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 205 gssrrgavvpqfeqppvrwrlamehffiakteephrtdyasvmvDAQ--VSDQRAADASDaGKAAGDALRQA-SQKPRPG 281
Cdd:PRK02362 192 --------------------------------------------DAElvDSEWRPIDLRE-GVFYGGAIHFDdSQREVEV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 282 AHSSKASAqLELESASDqapasadpglayvfehsaGRKCLVFSNSREECEA----VTSTLREYCRRAGEP------ERFL 351
Cdd:PRK02362 227 PSKDDTLN-LVLDTLEE------------------GGQCLVFVSSRRNAEGfakrAASALKKTLTAAERAelaelaEEIR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 352 --------------------IHHGNLSTPLRldaeALMKE---ENALLTVCTTATLELGID------IGRLERAFQINA- 401
Cdd:PRK02362 288 evsdtetskdladcvakgaaFHHAGLSREHR----ELVEDafrDRLIKVISSTPTLAAGLNlparrvIIRDYRRYDGGAg 363
|
410 420
....*....|....*....|...
gi 1821503202 402 --PFTVSAFLQRMGRTGRRGSPP 422
Cdd:PRK02362 364 mqPIPVLEYHQMAGRAGRPGLDP 386
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
15-221 |
1.06e-06 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 52.59 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 15 IYAHRWEKLRSVQVAAGNAVFNTDKHVLLCASTASGKT---EAAffPILTLLSEEppasvGA-LYIAPLKALINDQFERL 90
Cdd:COG1202 202 LLEGRGEELLPVQSLAVENGLLEGKDQLVVSATATGKTligELA--GIKNALEGK-----GKmLFLVPLVALANQKYEDF 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 91 TDLCAEG---GIPVWAwhGDVAQSRKRKLIEhpSGILQITPESLEALLLRKHSViprlfGDLRFIVIDEIHSLMRGDRGG 167
Cdd:COG1202 275 KDRYGDGldvSIRVGA--SRIRDDGTRFDPN--ADIIVGTYEGIDHALRTGRDL-----GDIGTVVIDEVHMLEDPERGH 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1821503202 168 QTMCLIERLARLSgSDPRRIGLSATIGDPQKAADFLcgssrrGAVVPQFEQPPV 221
Cdd:COG1202 346 RLDGLIARLKYYC-PGAQWIYLSATVGNPEELAKKL------GAKLVEYEERPV 392
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
38-203 |
1.48e-06 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 49.52 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 38 DKHVLLCASTASGKTEAAFFPIL-TLLSEEPPAsvgaLYIAPLKALINDQFERLTDLCAEGGIPVWAWHGDvaQSRKRKL 116
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLkRLLERRKKA----LFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGN--KGRSPPK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 117 IEHPSGILQITPEslealllRKHSVIPRLF-----GDLRFIVIDEIHSLMRGDRGGQTMCLIERLARLSGSDPRRIGLSA 191
Cdd:cd18026 107 RRKSLSVAVCTIE-------KANSLVNSLIeegrlDELGLVVVDELHMLGDGHRGALLELLLTKLLYAAQKNIQIVGMSA 179
|
170
....*....|..
gi 1821503202 192 TIGDPQKAADFL 203
Cdd:cd18026 180 TLPNLEELASWL 191
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
38-160 |
1.84e-06 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 49.21 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 38 DKHVLLCASTASGKTEAAFFPILTLLSEEPPASVgaLYIAPLKALINDQFERLTDLCAEGGIP--VWAWHGDVAQSRKRK 115
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWALKLAARGGKRRI--IYALPTRATINQMYERIREILGRLDDEdkVLLLHSKAALELLES 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821503202 116 LIEHPSGILqitpESLEALLLRKHS------------VIPRLFGDLRF-----------IVIDEIHSL 160
Cdd:cd17930 79 DEEPDDDPV----EAVDWALLLKRSwlapivvttidqLLESLLKYKHFerrlhglansvVVLDEVQAY 142
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
41-204 |
4.37e-05 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 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: 350782 [Multi-domain] Cd Length: 205 Bit Score: 45.51 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 41 VLLCASTASGKTEAAFFPILTLLSEEPPAsvgaLYIAPLKALINDQFERLTDLCAEGGIPVwawhGDVAqsrkrklIEHP 120
Cdd:cd18024 50 VLVSAHTSAGKTVVAEYAIAQSLRDKQRV----IYTSPIKALSNQKYRELQEEFGDVGLMT----GDVT-------INPN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 121 SGILQITPESLEALLLRKHSVIPrlfgDLRFIVIDEIHSLMRGDRG---GQTMCLIERLARLsgsdprrIGLSATIGDPQ 197
Cdd:cd18024 115 ASCLVMTTEILRSMLYRGSEIMR----EVAWVIFDEIHYMRDKERGvvwEETIILLPDKVRY-------VFLSATIPNAR 183
|
....*..
gi 1821503202 198 KAADFLC 204
Cdd:cd18024 184 QFAEWIC 190
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
41-160 |
6.26e-05 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 46.61 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 41 VLLCASTASGKTEAAFFPILTLLSEEPPASVgaLYIAPLKALINDQFERLTDLcaeGGIPVWAWHG--DVAQSRKRKLIE 118
Cdd:COG1203 150 FILTAPTGGGKTEAALLFALRLAAKHGGRRI--IYALPFTSIINQTYDRLRDL---FGEDVLLHHSlaDLDLLEEEEEYE 224
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1821503202 119 HPSGILQITPES-------------LEALLLRKHSVIPRLFGDLR-FIVIDEIHSL 160
Cdd:COG1203 225 SEARWLKLLKELwdapvvvttidqlFESLFSNRKGQERRLHNLANsVIILDEVQAY 280
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
22-204 |
8.16e-05 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain] Cd Length: 204 Bit Score: 44.39 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 22 KLRSVQVAAGNAVFNtDKHVLLCASTASGKTEAAFFPILTLLSEEPPASVGA--LYIAPLKALINDQFERLTDLCaEGGI 99
Cdd:cd18036 2 ELRNYQLELVLPALR-GKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGrvVVLVNKVPLVEQQLEKFFKYF-RKGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 100 PVWAWHGDVAQSRKRKLIEHPSGILQITPESLEALLLRKHSVIPRLFGDLRFIVIDEIHSLMRGDRGGQTM-CLIERLAR 178
Cdd:cd18036 80 KVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEERVYLSDFSLLIFDECHHTQKEHPYNKIMrMYLDKKLS 159
|
170 180 190
....*....|....*....|....*....|.
gi 1821503202 179 LSGSDPRRIGLSATIG-----DPQKAADFLC 204
Cdd:cd18036 160 SQGPLPQILGLTASPGvggarSFEEALEHIL 190
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
33-166 |
8.51e-05 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L 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: 350785 [Multi-domain] Cd Length: 179 Bit Score: 44.18 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 33 AVFNTDKH--VLLCASTASGKTEAAFFPILTLLSEeppaSVGALYIAPLKALINDQFERLTDLCAEGGIPVwawhGDVAQ 110
Cdd:cd18027 16 AILHLEAGdsVFVAAHTSAGKTVVAEYAIALAQKH----MTRTIYTSPIKALSNQKFRDFKNTFGDVGLIT----GDVQL 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821503202 111 srkrklieHPSG-ILQITPESLEALLLRKHSVIPrlfgDLRFIVIDEIHSLMRGDRG 166
Cdd:cd18027 88 --------NPEAsCLIMTTEILRSMLYNGSDVIR----DLEWVIFDEVHYINDAERG 132
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
22-204 |
1.35e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 43.96 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 22 KLRSVQVAAGNAVFNtDKHVLLCASTASGKTEAAFFpILTLLSEEPPASVGA--LYIAPLKALINDQFERLTDLCAEGGI 99
Cdd:cd17927 2 KPRNYQLELAQPALK-GKNTIICLPTGSGKTFVAVL-ICEHHLKKFPAGRKGkvVFLANKVPLVEQQKEVFRKHFERPGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 100 PVWAWHGDVA-QSRKRKLIEHpSGILQITPESLEALLlrKHSVIPRLfGDLRFIVIDEIH---------SLMRgdrggqt 169
Cdd:cd17927 80 KVTGLSGDTSeNVSVEQIVES-SDVIIVTPQILVNDL--KSGTIVSL-SDFSLLVFDECHnttknhpynEIMF------- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1821503202 170 MCLIERLARlSGSDPRRIGLSATIG-----DPQKAADFLC 204
Cdd:cd17927 149 RYLDQKLGS-SGPLPQILGLTASPGvggakNTEEALEHIC 187
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
26-195 |
1.52e-04 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 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: 350718 [Multi-domain] Cd Length: 202 Bit Score: 43.72 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 26 VQVAAgNAVFNTDKHVLLCASTASGKTEAAFFPILTLLS----EEPPASVGALYIAP-----------LKALINDQFERL 90
Cdd:cd17960 16 VQAAT-IPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLkrkaNLKKGQVGALIISPtrelatqiyevLQSFLEHHLPKL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 91 TDLCAEGGIPVwawhgdvaQSRKRKLIEHPSGILQITPESLEALLLRKHSVIPrlFGDLRFIVIDEIHSLMrgDRG-GQT 169
Cdd:cd17960 95 KCQLLIGGTNV--------EEDVKKFKRNGPNILVGTPGRLEELLSRKADKVK--VKSLEVLVLDEADRLL--DLGfEAD 162
|
170 180
....*....|....*....|....*....
gi 1821503202 170 MCLIerLARLsgsdP--RRIGL-SATIGD 195
Cdd:cd17960 163 LNRI--LSKL----PkqRRTGLfSATQTD 185
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
351-422 |
1.67e-04 |
|
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: 40.77 E-value: 1.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821503202 351 LIHHGNLSTPLRLDAEALMKEENALLTvctTATLELGIDIGRLERAFQINAPFTVSAFLQRMGRTGRRGSPP 422
Cdd:cd18785 2 MVVKIIVFTNSIEHAEEIASSLEILVA---TNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
41-196 |
2.08e-04 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 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: 350715 [Multi-domain] Cd Length: 198 Bit Score: 43.35 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 41 VLLCASTASGKTEAAFFPILTLLsEEPPASVG--ALYIAPLKAL---INDQFERLTDlcaegGIPVWaWH-----GDVAQ 110
Cdd:cd17957 30 LLACAPTGSGKTLAFLIPILQKL-GKPRKKKGlrALILAPTRELasqIYRELLKLSK-----GTGLR-IVllsksLEAKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 111 SRKRKLIEHPSgILQITPESLEALLLRKHSVIPRlfgdLRFIVIDEIHSLMrgDRG--GQTMCLierLARLSGSDPRRIG 188
Cdd:cd17957 103 KDGPKSITKYD-ILVSTPLRLVFLLKQGPIDLSS----VEYLVLDEADKLF--EPGfrEQTDEI---LAACTNPNLQRSL 172
|
....*...
gi 1821503202 189 LSATIGDP 196
Cdd:cd17957 173 FSATIPSE 180
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
41-204 |
3.31e-04 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 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: 350696 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 41 VLLCASTASGKTEAAFFPILTLlseeppasVGALYIAPLKAL---INDQFER----LTDLCAEGGIPVwawhGDVAQSRK 113
Cdd:cd17938 39 VLMAAETGSGKTGAFCLPVLQI--------VVALILEPSRELaeqTYNCIENfkkyLDNPKLRVALLI----GGVKAREQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 114 RKLIEHPSGILQITPESLEAlLLRKHSVIPRlfgDLRFIVIDEIHSLMRGDRGGQTMCLIERLARLSGSDPR--RIGLSA 191
Cdd:cd17938 107 LKRLESGVDIVVGTPGRLED-LIKTGKLDLS---SVRFFVLDEADRLLSQGNLETINRIYNRIPKITSDGKRlqVIVCSA 182
|
170
....*....|....*
gi 1821503202 192 TIGDPQ--KAADFLC 204
Cdd:cd17938 183 TLHSFEvkKLADKIM 197
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
39-429 |
5.94e-04 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 43.21 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 39 KHVLLCASTASGKTeAAF-FPILTLLSEEPPASVGALYIAP---LKALINDQFERLTD------LCAEGGipvwawhgdV 108
Cdd:COG0513 40 RDVLGQAQTGTGKT-AAFlLPLLQRLDPSRPRAPQALILAPtreLALQVAEELRKLAKylglrvATVYGG---------V 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 109 AQSRKRKLIEHPSGILQITPESLEALLLRKHsviprL-FGDLRFIVIDE---------------IHSLMRGDRggQTMCL 172
Cdd:COG0513 110 SIGRQIRALKRGVDIVVATPGRLLDLIERGA-----LdLSGVETLVLDEadrmldmgfiedierILKLLPKER--QTLLF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 173 -------IERLARLSGSDPRRIglsaTIGDPQKAADflcgssrrgavvpqfeqppvrwrlAMEHFFIakteephrtdyas 245
Cdd:COG0513 183 satmppeIRKLAKRYLKNPVRI----EVAPENATAE------------------------TIEQRYY------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 246 vMVDaqvsdqraadasdagkaagdalrqasqkprpgaHSSKASAqlelesasdqapasadpgLAYVFEHSAGRKCLVFSN 325
Cdd:COG0513 222 -LVD---------------------------------KRDKLEL------------------LRRLLRDEDPERAIVFCN 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 326 SREECEAVTSTLREYCRRAGEperflIhHGNLSTPLRLDAEALMKEENALLTVCTtatlEL---GIDIGRLERAFQINAP 402
Cdd:COG0513 250 TKRGADRLAEKLQKRGISAAA-----L-HGDLSQGQRERALDAFRNGKIRVLVAT----DVaarGIDIDDVSHVINYDLP 319
|
410 420 430
....*....|....*....|....*....|....*.
gi 1821503202 403 FTVSAFLQRMGRTGRRG---------SPPEMRFVMR 429
Cdd:COG0513 320 EDPEDYVHRIGRTGRAGaegtaislvTPDERRLLRA 355
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
39-164 |
6.57e-04 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) 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: 350713 [Multi-domain] Cd Length: 204 Bit Score: 41.83 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 39 KHVLLCASTASGKTeAAF-FPILTLLSEEpPASVGALYIAPLKAL---INDQFE------RLTDLCAEGGIPVwawhgdV 108
Cdd:cd17955 37 RDVIGGAKTGSGKT-AAFaLPILQRLSED-PYGIFALVLTPTRELayqIAEQFRalgaplGLRCCVIVGGMDM------V 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1821503202 109 AQSRKRKLIEHpsgILQITPESLeALLLRKHSVIPRLFGDLRFIVIDEIHSLMRGD 164
Cdd:cd17955 109 KQALELSKRPH---IVVATPGRL-ADHLRSSDDTTKVLSRVKFLVLDEADRLLTGS 160
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
39-156 |
8.82e-04 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 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: 350719 [Multi-domain] Cd Length: 206 Bit Score: 41.42 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 39 KHVLLCASTASGKTEAAFFPILTLL-----SEEPPASVGALYIAPLKAL---INDQFERLTDLCaEGGIPVWAWHGDVAQ 110
Cdd:cd17961 32 KDILARARTGSGKTAAYALPIIQKIlkakaESGEEQGTRALILVPTRELaqqVSKVLEQLTAYC-RKDVRVVNLSASSSD 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1821503202 111 SRKR-KLIEHPSgILQITPESLEALLLRKHSVIPRlfgDLRFIVIDE 156
Cdd:cd17961 111 SVQRaLLAEKPD-IVVSTPARLLSHLESGSLLLLS---TLKYLVIDE 153
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
21-158 |
9.35e-04 |
|
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: 41.20 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 21 EKLRSVQVAAGNAVFnTDKHVLLCASTASGKTeaaffpiltlLSEEPPASVG---ALYIAPLKALINDQFERLTDLcaeg 97
Cdd:cd18015 17 EKFRPLQLETINATM-AGRDVFLVMPTGGGKS----------LCYQLPALCSdgfTLVVSPLISLMEDQLMALKKL---- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821503202 98 GIPVWAWHGDVA-QSRKR---KLIEHPSG--ILQITPESLE------ALLLRKHSViprlfGDLRFIVIDEIH 158
Cdd:cd18015 82 GISATMLNASSSkEHVKWvhaALTDKNSElkLLYVTPEKIAkskrfmSKLEKAYNA-----GRLARIAIDEVH 149
|
|
| PRK11447 |
PRK11447 |
cellulose synthase subunit BcsC; Provisional |
185-262 |
5.17e-03 |
|
cellulose synthase subunit BcsC; Provisional
Pssm-ID: 183140 [Multi-domain] Cd Length: 1157 Bit Score: 40.45 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 185 RRIGLS-ATIGDPQKAADFLcgssrrGAVVPQFEQPPVRWRLAM----EHFFIAKTEEPHR--TDYASVMVDAQVSDQRA 257
Cdd:PRK11447 675 RRVALAwAALGDTAAAQRTF------NRLIPQAKSQPPSMESALvlrdAARFEAQTGQPQQalETYKDAMVASGITPTRP 748
|
....*
gi 1821503202 258 ADASD 262
Cdd:PRK11447 749 QDNDT 753
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
39-156 |
7.35e-03 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 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: 350704 [Multi-domain] Cd Length: 235 Bit Score: 38.76 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821503202 39 KHVLLCASTASGKTEAAFFPIL-TLLSEEPPASVG-------ALYIAPLKAL---INDQFERltdLCAEGGIPVWAWHGD 107
Cdd:cd17946 29 KDVIGAAETGSGKTLAFGIPILeRLLSQKSSNGVGgkqkplrALILTPTRELavqVKDHLKA---IAKYTNIKIASIVGG 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1821503202 108 VAQSRKRKLIEHPSGILQITPESLEALLLRKHSVIPRLfGDLRFIVIDE 156
Cdd:cd17946 106 LAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANL-KSLRFLVLDE 153
|
|
| |
