|
Name |
Accession |
Description |
Interval |
E-value |
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
309-820 |
1.01e-163 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 498.70 E-value: 1.01e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 309 FEPDVFQKQAILHLERHDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFRNTFG--DVGLLTGD 386
Cdd:COG4581 24 FELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALARGRRSFYTAPIKALSNQKFFDLVERFGaeNVGLLTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 387 VQLHPEASCLIMTTEILRSMLYSGSDVIRDLEWVIFDEVHYINDVERGVVWEEVLIMLPDHVSIILLSATVPNALEFADW 466
Cdd:COG4581 104 ASVNPDAPIVVMTTEILRNMLYREGADLEDVGVVVMDEFHYLADPDRGWVWEEPIIHLPARVQLVLLSATVGNAEEFAEW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 467 IGRLkRRQIYVISTVTRPVPLEHYLFTGNssktqgELFLLLdsrgafhtkgyyaAVEAKKERMSKHAQTfgakqpthqgg 546
Cdd:COG4581 184 LTRV-RGETAVVVSEERPVPLEFHYLVTP------RLFPLF-------------RVNPELLRPPSRHEV----------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 547 paqdrgvylslLASLRTRAQLPVVVFTFSRGRCDEQASGLTSLDLTTSSEKSEIHLFLQRclarlRGSDRQLPQVLHMSE 626
Cdd:COG4581 233 -----------IEELDRGGLLPAIVFIFSRRGCDEAAQQLLSARLTTKEERAEIREAIDE-----FAEDFSVLFGKTLSR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 627 LLNRGLGVHHSGILPILKEIVEMLFSRGLVKVLFATETFAMGVNMPARTVVFDSMRKHDGSTFRDLLPGEYVQMAGRAGR 706
Cdd:COG4581 297 LLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 707 RGLDPTGTVILLckgrVPEMAD---LHRMMMGKPSQLQSQFRLTYTMILNLL-RVDALRVEDMMKRSFSEFPSRKDSKAH 782
Cdd:COG4581 377 RGIDTEGHVVVL----APEHDDpkkFARLASARPEPLRSSFRPSYNMVLNLLaRPGLERARELLEDSFAQFQADRSVVGL 452
|
490 500 510
....*....|....*....|....*....|....*...
gi 2217362817 783 EQALAELTKRLGALEEpDMTGQLVDLPEYYSWGEELTE 820
Cdd:COG4581 453 ARRARELERALAGVVE-RLACDLGDLQEYFALRQPLSP 489
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
303-481 |
5.24e-132 |
|
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: 394.71 E-value: 5.24e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 303 PAFQWAFEPDVFQKQAILHLERHDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFRNTFGDVGL 382
Cdd:cd18027 1 PAFKWPFELDVFQKQAILHLEAGDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 383 LTGDVQLHPEASCLIMTTEILRSMLYSGSDVIRDLEWVIFDEVHYINDVERGVVWEEVLIMLPDHVSIILLSATVPNALE 462
Cdd:cd18027 81 ITGDVQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDHVSIILLSATVPNTVE 160
|
170
....*....|....*....
gi 2217362817 463 FADWIGRLKRRQIYVISTV 481
Cdd:cd18027 161 FADWIGRIKKKNIYVISTP 179
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
280-480 |
2.89e-99 |
|
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: 310.14 E-value: 2.89e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 280 QEQWAIPVDATSPvgDFYRLIP--QPAFQWAFEPDVFQKQAILHLERHDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTI 357
Cdd:cd18024 2 THEVALPPDYDYT--PISAHKPpgNPARTYPFTLDPFQKTAIACIERNESVLVSAHTSAGKTVVAEYAIAQSLRDKQRVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 358 YTSPIKALSNQKFRDFRNTFGDVGLLTGDVQLHPEASCLIMTTEILRSMLYSGSDVIRDLEWVIFDEVHYINDVERGVVW 437
Cdd:cd18024 80 YTSPIKALSNQKYRELQEEFGDVGLMTGDVTINPNASCLVMTTEILRSMLYRGSEIMREVAWVIFDEIHYMRDKERGVVW 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217362817 438 EEVLIMLPDHVSIILLSATVPNALEFADWIGRLKRRQIYVIST 480
Cdd:cd18024 160 EETIILLPDKVRYVFLSATIPNARQFAEWICKIHKQPCHVVYT 202
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
314-810 |
8.01e-67 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 233.63 E-value: 8.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 314 FQKQAI-LHLERHDSVFVAAHTSAGKTVVAEYAI--ALAQKHmtRTIYTSPIKALSNQKFRDFRNTFGD----VGLLTGD 386
Cdd:COG1204 26 PQAEALeAGLLEGKNLVVSAPTASGKTLIAELAIlkALLNGG--KALYIVPLRALASEKYREFKRDFEElgikVGVSTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 387 VQLHPE----ASCLIMTTEILRSMLYSGSDVIRDLEWVIFDEVHYINDVERGVVWEEV---LIMLPDHVSIILLSATVPN 459
Cdd:COG1204 104 YDSDDEwlgrYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHLIDDESRGPTLEVLlarLRRLNPEAQIVALSATIGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 460 ALEFADWIGRLkrrqiyVISTVTRPVPLEHYLFTGNSSKTQGELFLLLdsrgafhtkgyyaaveakkermskhaqtfgak 539
Cdd:COG1204 184 AEEIAEWLDAE------LVKSDWRPVPLNEGVLYDGVLRFDDGSRRSK-------------------------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 540 qpthqggpaqDRGVYLsLLASLRTRAQlpVVVFTFSRGRCDEQASGLTSL--DLTTSSEKSEIHLFLQRCL--ARLRGSD 615
Cdd:COG1204 226 ----------DPTLAL-ALDLLEEGGQ--VLVFVSSRRDAESLAKKLADElkRRLTPEEREELEELAEELLevSEETHTN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 616 RQLpqvlhmSELLNRGLGVHHSGILPILKEIVEMLFSRGLVKVLFATETFAMGVNMPARTVVfdsMRKHDGSTFRDLLPG 695
Cdd:COG1204 293 EKL------ADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVI---IRDTKRGGMVPIPVL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 696 EYVQMAGRAGRRGLDPTGTVILLCKGRVPEMADLHRMMMGKPSQLQSQFRLTYTMILNLLRV----DALRVEDMMKRSFS 771
Cdd:COG1204 364 EFKQMAGRAGRPGYDPYGEAILVAKSSDEADELFERYILGEPEPIRSKLANESALRTHLLALiasgFANSREELLDFLEN 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2217362817 772 EFPSRKDSKAH-----EQALAELTKRlGALEEPDMTGQLVDLPE 810
Cdd:COG1204 444 TFYAYQYDKGDleevvDDALEFLLEN-GFIEEDGDRLRATKLGK 486
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
314-469 |
3.10e-55 |
|
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: 189.39 E-value: 3.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 314 FQKQAILHL-ERHDSVFVAAHTSAGKTVVAEYAIALA-QKHMTRTIYTSPIKALSNQKFRDFRNTFG----DVGLLTGDV 387
Cdd:cd17921 5 IQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRAlATSGGKAVYIAPTRALVNQKEADLRERFGplgkNVGLLTGDP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 388 ----QLHPEASCLIMTTEILRSMLY-SGSDVIRDLEWVIFDEVHYINDVERGVVWEEVLIMLP---DHVSIILLSATVPN 459
Cdd:cd17921 85 svnkLLLAEADILVATPEKLDLLLRnGGERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrinKNARFVGLSATLPN 164
|
170
....*....|
gi 2217362817 460 ALEFADWIGR 469
Cdd:cd17921 165 AEDLAEWLGV 174
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
483-720 |
4.31e-45 |
|
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: 159.64 E-value: 4.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 483 RPVPLEHYLFTGNSSKTqgelFLLLDSRGAFhtkgyyaaveakkermskhaqtfgakqpthqggpaqdRGVYLSLLASLR 562
Cdd:cd18795 1 RPVPLEEYVLGFNGLGI----KLRVDVMNKF-------------------------------------DSDIIVLLKIET 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 563 TRAQLPVVVFTFSRGRCDEQASGLtsldlttssekseihlflqrclarlrgsdrqlpqvlhmsellnRGLGVHHSGILPI 642
Cdd:cd18795 40 VSEGKPVLVFCSSRKECEKTAKDL-------------------------------------------AGIAFHHAGLTRE 76
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217362817 643 LKEIVEMLFSRGLVKVLFATETFAMGVNMPARTVVFDSMRKHDGSTFRDLLPGEYVQMAGRAGRRGLDPTGTVILLCK 720
Cdd:cd18795 77 DRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
327-720 |
2.43e-36 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 147.41 E-value: 2.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 327 SVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFRN--TFG-DVGLLTGDVQLHPEA----SCLIMT 399
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAMLKAIARGGKALYIVPLRALASEKFEEFERfeELGvRVGISTGDYDSRDEWlgdnDIIVAT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 400 TEILRSMLYSGSDVIRDLEWVIFDEVHYINDVERGVVWEEVLIML----PDhVSIILLSATVPNALEFADWIGrlkrrqI 475
Cdd:PRK02362 121 SEKVDSLLRNGAPWLDDITCVVVDEVHLIDSANRGPTLEVTLAKLrrlnPD-LQVVALSATIGNADELADWLD------A 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 476 YVISTVTRPVPLEhylftgnssktQGELFllldsRGAFHTKGyyaaveakkermskhaqtfgAKQPTHQGGPAQDrgvyL 555
Cdd:PRK02362 194 ELVDSEWRPIDLR-----------EGVFY-----GGAIHFDD--------------------SQREVEVPSKDDT----L 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 556 SL-LASLRTRAQlpVVVFTFSRGRCDEQASGLTSL--DLTTSSEKSEihlfLQRCLARLR-GSDRQLPQVLHMSelLNRG 631
Cdd:PRK02362 234 NLvLDTLEEGGQ--CLVFVSSRRNAEGFAKRAASAlkKTLTAAERAE----LAELAEEIReVSDTETSKDLADC--VAKG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 632 LGVHHSGILPILKEIVEMLFSRGLVKVLFATETFAMGVNMPARTVVFDSMRKHDGSTFRDLLP-GEYVQMAGRAGRRGLD 710
Cdd:PRK02362 306 AAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAGMQPIPvLEYHQMAGRAGRPGLD 385
|
410
....*....|
gi 2217362817 711 PTGTVILLCK 720
Cdd:PRK02362 386 PYGEAVLLAK 395
|
|
| Ski2_N |
pfam17911 |
Ski2 N-terminal region; This region is the N-terminal extended region found in the Ski2 ... |
79-201 |
1.51e-35 |
|
Ski2 N-terminal region; This region is the N-terminal extended region found in the Ski2 protein. The Ski complex is a conserved multiprotein assembly required for the cytoplasmic functions of the exosome, including RNA turnover, surveillance, and interference. Ski2, Ski3, and Ski8 assemble in a tetramer with 1:1:2 stoichiometry.
Pssm-ID: 465562 Cd Length: 134 Bit Score: 131.24 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 79 RKWQRKTDPWSLLAVLGAPVPSDLQAQRHPTTGQILGYKEV-LLENTNLSATTSLSLRRPPGPASQSLWGNPTQYPFWPG 157
Cdd:pfam17911 5 RHWDRDKDYKSLLKIPPSPSRTTLRFKRDGLEGKIVGYKEVsLVEISNATAKNSLSLNRKPGPKSDFVRGSSSNLPFAPG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2217362817 158 GMDEPTITDLN-TREEAEEEIDFEKDLLTIPPGFKKGMDFAPKDC 201
Cdd:pfam17911 85 GLDEEVLKDSEgVDSGLKRLHRDEGGLLDVPPGFSRGLDFGEDEE 129
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
330-743 |
3.92e-35 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 143.80 E-value: 3.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 330 VAAHTSAGKTVVAEyaIALAQKHMT---RTIYTSPIKALSNQKFRDFRN--TFG-DVGLLTGDVQLHPE----ASCLIMT 399
Cdd:PRK00254 44 LAIPTASGKTLVAE--IVMVNKLLReggKAVYLVPLKALAEEKYREFKDweKLGlRVAMTTGDYDSTDEwlgkYDIIIAT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 400 TEILRSMLYSGSDVIRDLEWVIFDEVHYINDVERGVVWEEVLIMLPDHVSIILLSATVPNALEFADWIgrlkrrQIYVIS 479
Cdd:PRK00254 122 AEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQILGLSATVGNAEELAEWL------NAELVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 480 TVTRPVPLEHYLFtgnsskTQGELFLLLDSRGAFHTKGYYAAVEAKKErmSKHAqtfgakqpthqggpaqdrgvylslla 559
Cdd:PRK00254 196 SDWRPVKLRKGVF------YQGFLFWEDGKIERFPNSWESLVYDAVKK--GKGA-------------------------- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 560 slrtraqlpvVVFTFSRGRCDEQASGLTSL--DLTTSSEkseihlflQRCLARLRGSDRQLPQVLHMSELLNRGLGVHHS 637
Cdd:PRK00254 242 ----------LVFVNTRRSAEKEALELAKKikRFLTKPE--------LRALKELADSLEENPTNEKLKKALRGGVAFHHA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 638 GILPILKEIVEMLFSRGLVKVLFATETFAMGVNMPARTVVFDSMRKHDGSTFRDLLPGEYVQMAGRAGRRGLDPTGTVIL 717
Cdd:PRK00254 304 GLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAII 383
|
410 420
....*....|....*....|....*.
gi 2217362817 718 LCKGRVPEMAdLHRMMMGKPSQLQSQ 743
Cdd:PRK00254 384 VATTEEPSKL-MERYIFGKPEKLFSM 408
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
315-713 |
1.00e-32 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 135.78 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 315 QKQAILHLERHDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRD---FRNTFGDVGLLTGDVQLHP 391
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEElsrLRSLGMRVKISIGDYDDPP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 392 E----ASCLIMTTEILRSMLYSGSDVIRDLEWVIFDEVHYINDVERGVVWEEVL----IMLPDhVSIILLSATVPNALEF 463
Cdd:PRK01172 107 DfikrYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTLETVLssarYVNPD-ARILALSATVSNANEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 464 ADWIgrlkrrQIYVISTVTRPVPLEhylfTGNSSKTQgelfLLLDSrgafhtkgyyaaveakKERmSKHAQTFGAKQPTH 543
Cdd:PRK01172 186 AQWL------NASLIKSNFRPVPLK----LGILYRKR----LILDG----------------YER-SQVDINSLIKETVN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 544 QGGpaqdrgvylsllaslrtraqlPVVVFTFSRGRCDEQASGLTSL-----DLTTSSEKSEIHlflqrclarlrgsdrql 618
Cdd:PRK01172 235 DGG---------------------QVLVFVSSRKNAEDYAEMLIQHfpefnDFKVSSENNNVY----------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 619 PQVLhmSELLNRGLGVHHSGILPILKEIVEMLFSRGLVKVLFATETFAMGVNMPARTVVFDSMRKHDGSTFRDLLPGEYV 698
Cdd:PRK01172 277 DDSL--NEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRYLSNMEIK 354
|
410
....*....|....*
gi 2217362817 699 QMAGRAGRRGLDPTG 713
Cdd:PRK01172 355 QMIGRAGRPGYDQYG 369
|
|
| rRNA_proc-arch |
pfam13234 |
rRNA-processing arch domain; Mtr4 is the essential RNA helicase, and is an exosome-activating ... |
763-943 |
2.35e-30 |
|
rRNA-processing arch domain; Mtr4 is the essential RNA helicase, and is an exosome-activating cofactor. This arch domain is carried in Mtr4 and Ski2 (the cytosolic homolog of Mtr4). The arch domain is required for proper 5.8S rRNA processing, and appears to function independently of canonical helicase activity.
Pssm-ID: 463813 Cd Length: 267 Bit Score: 121.23 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 763 EDMMKRSFSEFPSRKDSKAHEQALAELTKRLGALEEPDMTgqlvDLPEYYSWGEELTETQHMIQRRIMESVNGLKSLSAG 842
Cdd:pfam13234 1 EYMLKRSFSQFQNQASLPELEKKLKELEKELASIKIPDEE----DIKEYYDLRQQLEKLNEDIREVILHPPYGLPFLQPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 843 RVVVVK-NQEHHNALGVILQVSSN---------STSRVFTTLVLCDKPLSQDPQDrgpataevpyPDDLVGFKLFLPEGP 912
Cdd:pfam13234 77 RLVVVKdNGDQDFGWGVVVNFKKRkkngkaeppQESYIVDVLLVLALVSSPEDLD----------KFNDVNPEGFRPAPP 146
|
170 180 190
....*....|....*....|....*....|....
gi 2217362817 913 ---CDHTVVKLQPGDMAAITTKVLRVNGEKILED 943
Cdd:pfam13234 147 gekGEMEVVPVPLSDIEAISSVRLKLPKDLRPAE 180
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
315-462 |
4.65e-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: 116.96 E-value: 4.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 315 QKQAILHLERHDSVFVAAHTSAGKTVVAEYAIALAQKHM---TRTIYTSPIKALSNQKFRDFRNTFGDVGL----LTGDV 387
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLdngPQALVLAPTRELAEQIYEELKKLGKGLGLkvasLLGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 388 QLHPEAS------CLIMTTEILRSMLYSgSDVIRDLEWVIFDEVHYINDVERGVVWEEVLIMLPDHVSIILLSATVPNAL 461
Cdd:pfam00270 84 SRKEQLEklkgpdILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATLPRNL 162
|
.
gi 2217362817 462 E 462
Cdd:pfam00270 163 E 163
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
309-486 |
4.00e-28 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 112.59 E-value: 4.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 309 FEPDVFQKQAILHLERHD-SVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFRNTFGD-----V 380
Cdd:smart00487 7 EPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPAleALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSlglkvV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 381 GLLTGDV-------QLHPEASCLIMTTEILRSMLYSGSDVIRDLEWVIFDEVHYINDVERGVVWEEVLIMLPDHVSIILL 453
Cdd:smart00487 87 GLYGGDSkreqlrkLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLLL 166
|
170 180 190
....*....|....*....|....*....|...
gi 2217362817 454 SATVPNALEFADWIGRLKRRQIYVISTVTRPVP 486
Cdd:smart00487 167 SATPPEEIENLLELFLNDPVFIDVGFTPLEPIE 199
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
322-468 |
8.37e-27 |
|
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: 107.81 E-value: 8.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 322 LERHDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFR--NTFG-DVGLLTGD----VQLHPEAS 394
Cdd:cd18028 14 LLKGENLLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKklEEIGlKVGISTGDydedDEWLGDYD 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217362817 395 CLIMTTEILRSMLYSGSDVIRDLEWVIFDEVHYINDVERGVVWEEVLI---MLPDHVSIILLSATVPNALEFADWIG 468
Cdd:cd18028 94 IIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVArlrRLNPNTQIIGLSATIGNPDELAEWLN 170
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
311-473 |
4.78e-25 |
|
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: 103.60 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 311 PDVFQKQAILHLERHDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTI--YTSPIKALSNQKFRDFRNTFGD--------- 379
Cdd:cd18025 2 PDAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDGVvvYVAPTKALVNQVVAEVYARFSKkyppsgksl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 380 VGLLTGDVQLHPEASCLIMTT--EILRSMLYSGSDV--IRDLEWVIFDEVHYINDVERGVVWEEVLIMLPdhVSIILLSA 455
Cdd:cd18025 82 WGVFTRDYRHNNPMNCQVLITvpECLEILLLSPHNAswVPRIKYVIFDEIHSIGQSEDGAVWEQLLLLIP--CPFLALSA 159
|
170
....*....|....*...
gi 2217362817 456 TVPNALEFADWIGRLKRR 473
Cdd:cd18025 160 TIGNPQKFHEWLQSVQRA 177
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
322-468 |
2.31e-21 |
|
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: 93.19 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 322 LERHDSVFVAAHTSAGKTVVAEYAIA-------LAQKHMTRTIYTSPIKALSNQKFRDFRNTFGDVGL----LTGDVQLH 390
Cdd:cd18023 14 LYSDKNFVVSAPTGSGKTVLFELAILrllkernPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLscaeLTGDTEMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 391 PE---ASC-LIMTT-EILRSMLYSGSD---VIRDLEWVIFDEVHYINDvERGVVWEEVL-----------IMLPDH--VS 449
Cdd:cd18023 94 DTfeiQDAdIILTTpEKWDSMTRRWRDngnLVQLVALVLIDEVHIIKE-NRGATLEVVVsrmktlsssseLRGSTVrpMR 172
|
170
....*....|....*....
gi 2217362817 450 IILLSATVPNALEFADWIG 468
Cdd:cd18023 173 FVAVSATIPNIEDLAEWLG 191
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
322-718 |
7.31e-19 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 92.26 E-value: 7.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 322 LERHDSVFVAAhTSAGKTVVAEYA-IALAQKHMTRTIYTSPIKALSNQKFRDFRNTFG---DVGLLTG-------DVQLH 390
Cdd:COG1202 223 LEGKDQLVVSA-TATGKTLIGELAgIKNALEGKGKMLFLVPLVALANQKYEDFKDRYGdglDVSIRVGasrirddGTRFD 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 391 PEASCLIMTTEILRSMLYSGSDvIRDLEWVIFDEVHYINDVERGVVWEEV---LIMLPDHVSIILLSATVPNALEFAdwi 467
Cdd:COG1202 302 PNADIIVGTYEGIDHALRTGRD-LGDIGTVVIDEVHMLEDPERGHRLDGLiarLKYYCPGAQWIYLSATVGNPEELA--- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 468 grlKRRQIYVISTVTRPVPLE-HYLFTGNSSKTQGELFLlldSRGAFHT---KGYyaaveakkermskHAQTfgakqpth 543
Cdd:COG1202 378 ---KKLGAKLVEYEERPVPLErHLTFADGREKIRIINKL---VKREFDTkssKGY-------------RGQT-------- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 544 qggpaqdrgvylsllaslrtraqlpvVVFTFSRGRCDEQASGLtsldlttssekseihlflqrclarlrgsdrqlpqvlh 623
Cdd:COG1202 431 --------------------------IIFTNSRRRCHEIARAL------------------------------------- 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 624 msellnrGLGV--HHSGILPILKEIVEMLFSRGLVKVLFATETFAMGVNMPARTVVFDS--MrkhdGSTFrdLLPGEYVQ 699
Cdd:COG1202 448 -------GYKAapYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSlaM----GIEW--LSVQEFHQ 514
|
410
....*....|....*....
gi 2217362817 700 MAGRAGRRGLDPTGTVILL 718
Cdd:COG1202 515 MLGRAGRPDYHDRGKVYLL 533
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
326-468 |
4.41e-17 |
|
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: 80.38 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 326 DSVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFRNTFGDVG-----LLTGDVQL---HPEASC 395
Cdd:cd18021 20 DNVFVGAPTGSGKTVCAELALlrHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPLLgkkvvKLTGETSTdlkLLAKSD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 396 LIMTT----EILrSMLYSGSDVIRDLEWVIFDEVHYINDVErGVVWEEVL-------IMLPDHVSIILLSATVPNALEFA 464
Cdd:cd18021 100 VILATpeqwDVL-SRRWKQRKNVQSVELFIADELHLIGGEN-GPVYEVVVsrmryisSQLEKPIRIVGLSSSLANARDVG 177
|
....
gi 2217362817 465 DWIG 468
Cdd:cd18021 178 EWLG 181
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
626-708 |
4.39e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 68.39 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 626 ELLNRGLGV--HHSGILPILKEIVEMLFSRGLVKVLFATETFAMGVNMP-ARTVVFDSMRKHdgstfrdllPGEYVQMAG 702
Cdd:smart00490 6 LLKELGIKVarLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDLPWS---------PASYIQRIG 76
|
....*.
gi 2217362817 703 RAGRRG 708
Cdd:smart00490 77 RAGRAG 82
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
326-468 |
9.34e-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: 70.87 E-value: 9.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 326 DSVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFRNTFGDV-GL----LTGDVQLHPE----AS 394
Cdd:cd18022 18 NNVLLGAPTGSGKTIAAELAMfrAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKlGKkvveLTGDVTPDMKaladAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 395 CLIMTTE----ILRSmlYSGSDVIRDLEWVIFDEVHYINDvERGVVWEEV---LIMLPDH----VSIILLSATVPNALEF 463
Cdd:cd18022 98 IIITTPEkwdgISRS--WQTREYVQQVSLIIIDEIHLLGS-DRGPVLEVIvsrMNYISSQtekpVRLVGLSTALANAGDL 174
|
....*
gi 2217362817 464 ADWIG 468
Cdd:cd18022 175 ANWLG 179
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
657-715 |
3.75e-12 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 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: 350192 [Multi-domain] Cd Length: 135 Bit Score: 64.50 E-value: 3.75e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 657 KVLFATETFAMGVNMPARTVVFDSMRKHDGSTFRDLLPGEYVQMAGRAGRRGLD-PTGTV 715
Cdd:cd18805 72 DVLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMRPLSPSEVKQIAGRAGRFGSHfPEGEV 131
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
328-456 |
1.02e-11 |
|
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: 63.58 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 328 VFVAAHTSAGKTVVAEYAI--ALAQKHmTRTIYTSPIKALSNQKFRDFRNTFG---DVGLLTGDVQLH-------PEASC 395
Cdd:cd00046 4 VLITAPTGSGKTLAALLAAllLLLKKG-KKVLVLVPTKALALQTAERLRELFGpgiRVAVLVGGSSAEereknklGDADI 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217362817 396 LIMTTE-ILRSMLYSGSDVIRDLEWVIFDEVHYINDVERGVVWEEVLI---MLPDhVSIILLSAT 456
Cdd:cd00046 83 IIATPDmLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVrkaGLKN-AQVILLSAT 146
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
326-467 |
1.64e-11 |
|
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: 63.76 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 326 DSVFVAAHTSAGKTVVAE----YAIALAQKHMTRTIYTSPIKALSNQKFRDFR---NTFG---DVGLLTGDV-------Q 388
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFlpalSSLADEPEKGVQVLYISPLKALINDQERRLEeplDEIDleiPVAVRHGDTsqsekakQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 389 LHPEASCLIMTTEILRSMLYS--GSDVIRDLEWVIFDEVHYINDVERGVVWEEVLIMLpDHVSI-----ILLSATVPNAL 461
Cdd:cd17922 82 LKNPPGILITTPESLELLLVNkkLRELFAGLRYVVVDEIHALLGSKRGVQLELLLERL-RKLTGrplrrIGLSATLGNLE 160
|
....*.
gi 2217362817 462 EFADWI 467
Cdd:cd17922 161 EAAAFL 166
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
315-464 |
2.23e-11 |
|
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: 63.76 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 315 QKQAILHLERHDSVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSN---QKFRDFRNTFG---DVGLLTGD 386
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPIleALLRDPGSRALYLYPTKALAQdqlRSLRELLEQLGlgiRVATYDGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 387 VQLHP-------EASCLIMTTEIL-RSMLYSGS---DVIRDLEWVIFDEVHYIndveRGVVWEEVLIML----------P 445
Cdd:cd17923 85 TPREErraiirnPPRILLTNPDMLhYALLPHHDrwaRFLRNLRYVVLDEAHTY----RGVFGSHVALLLrrlrrlcrryG 160
|
170
....*....|....*....
gi 2217362817 446 DHVSIILLSATVPNALEFA 464
Cdd:cd17923 161 ADPQFILTSATIGNPAEHA 179
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
314-718 |
3.73e-11 |
|
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: 67.17 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 314 FQKQAILHLERHDSVFVAAHTSAGKTVVaeYAI----ALAQKHMTRTIYTSPIKALSN---QKFRDFRNTFG---DVGLL 383
Cdd:COG1205 60 HQAEAIEAARAGKNVVIATPTASGKSLA--YLLpvleALLEDPGATALYLYPTKALARdqlRRLRELAEALGlgvRVATY 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 384 TGD--------VQLHPeaSCLIMTTEIL-RSMLYSG---SDVIRDLEWVIFDEVH-YindveRGVvweevlimLPDHVS- 449
Cdd:COG1205 138 DGDtppeerrwIREHP--DIVLTNPDMLhYGLLPHHtrwARFFRNLRYVVIDEAHtY-----RGV--------FGSHVAn 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 450 -----------------IILLSATVPNALEFAdwiGRLKRRQIYVISTVTRPvplehylftgnssktQGELFLLLdsrga 512
Cdd:COG1205 203 vlrrlrricrhygsdpqFILASATIGNPAEHA---ERLTGRPVTVVDEDGSP---------------RGERTFVL----- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 513 fhtkgYYAAVEAKKERMSKHAQTfgakqpthqggpAQdrgvylsLLASLrTRAQLPVVVFTFSRgrcdeqasgltsldlt 592
Cdd:COG1205 260 -----WNPPLVDDGIRRSALAEA------------AR-------LLADL-VREGLRTLVFTRSR---------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 593 TSSEKseIHLFLQRCLARLRGSDRqlpqvlhmsellnrgLGVHHSGILPILKEIVEMLFSRGLVKVLFATETFAMGVNMP 672
Cdd:COG1205 299 RGAEL--LARYARRALREPDLADR---------------VAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIG 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217362817 673 artvvfdsmrkhdgstfrDL-------LPGE---YVQMAGRAGRRGldPTGTVILL 718
Cdd:COG1205 362 ------------------GLdavvlagYPGTrasFWQQAGRAGRRG--QDSLVVLV 397
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
326-468 |
2.44e-09 |
|
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: 58.21 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 326 DSVFVAAHTSAGKTVVAEYAI-----------ALAQKHMTRTIYTSPIKALSNQKFRDFRNTFGDVGL----LTGDVQLH 390
Cdd:cd18020 18 ENMLICAPTGAGKTNIAMLTIlheirqhvnqgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRLAPLGIkvkeLTGDMQLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 391 P---EASCLIMTT----EILRSMLYSGSDVIRDLEWVIFDEVHYINDvERGVVWEEVLI-------MLPDHVSIILLSAT 456
Cdd:cd18020 98 KkeiAETQIIVTTpekwDVVTRKSSGDVALSQLVRLLIIDEVHLLHD-DRGPVIESLVArtlrqveSTQSMIRIVGLSAT 176
|
170
....*....|..
gi 2217362817 457 VPNALEFADWIG 468
Cdd:cd18020 177 LPNYLDVADFLR 188
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
314-456 |
3.76e-09 |
|
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: 56.16 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 314 FQKQAI----LHLERHDSVFVAAhTSAGKTVVAEYAIALAQKHmtRTIYTSPIKALSNQKFRDFRNTFGD--VGLLTGDV 387
Cdd:cd17926 4 YQEEALeawlAHKNNRRGILVLP-TGSGKTLTALALIAYLKEL--RTLIVVPTDALLDQWKERFEDFLGDssIGLIGGGK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 388 QLHPEASCLIMTT-EILRSMLYSGSDVIRDLEWVIFDEVHYINdverGVVWEEVLIMLPDHVsIILLSAT 456
Cdd:cd17926 81 KKDFDDANVVVATyQSLSNLAEEEKDLFDQFGLLIVDEAHHLP----AKTFSEILKELNAKY-RLGLTAT 145
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
322-459 |
1.15e-08 |
|
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: 56.22 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 322 LERHDSVFVAAHTSAGKTVVAEYAIALA-QKHMTR----------TIYTSPIKALSNQKFRDFRN---TFG-DVGLLTGD 386
Cdd:cd18019 30 FETDENLLLCAPTGAGKTNVALLTILREiGKHRNPdgtinldafkIVYIAPMKALVQEMVGNFSKrlaPYGiTVAELTGD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 387 VQLHPE---ASCLIMTTE-----ILRSmlySGSDVIRDL-EWVIFDEVHYINDvERGVVWEEVLI-------MLPDHVSI 450
Cdd:cd18019 110 QQLTKEqisETQIIVTTPekwdiITRK---SGDRTYTQLvRLIIIDEIHLLHD-DRGPVLESIVArtirqieQTQEYVRL 185
|
....*....
gi 2217362817 451 ILLSATVPN 459
Cdd:cd18019 186 VGLSATLPN 194
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
331-484 |
1.28e-08 |
|
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: 56.07 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 331 AAHTSAGKTVVAEyaiALAQKHMTRT----IYTSPIKALSNQKFRDFRNTFGDVGLL---------TGDVQLHPEASCLI 397
Cdd:cd18026 39 SLPTSGGKTLVAE---ILMLKRLLERrkkaLFVLPYVSIVQEKVDALSPLFEELGFRvegyagnkgRSPPKRRKSLSVAV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 398 MTTEILRSMLYSG--SDVIRDLEWVIFDEVHYINDVERGVVWE----EVLIMLPDHVSIILLSATVPNALEFADWIgrlk 471
Cdd:cd18026 116 CTIEKANSLVNSLieEGRLDELGLVVVDELHMLGDGHRGALLEllltKLLYAAQKNIQIVGMSATLPNLEELASWL---- 191
|
170
....*....|...
gi 2217362817 472 RRQIYviSTVTRP 484
Cdd:cd18026 192 RAELY--TTNFRP 202
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
305-468 |
2.09e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 58.19 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 305 FQWAF-EPDVFQKQAILHLERHDSVFVAAHTSAGKTvvaeYA------IALAQKHM-------TRTIYTSPIKALSNQKF 370
Cdd:COG1201 18 FAARFgAPTPPQREAWPAIAAGESTLLIAPTGSGKT----LAaflpalDELARRPRpgelpdgLRVLYISPLKALANDIE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 371 R-------DFRNTFGD------VGLLTGDV-------QL-HPeASCLIMTTEILRSMLYS--GSDVIRDLEWVIFDEVHY 427
Cdd:COG1201 94 RnlrapleEIGEAAGLplpeirVGVRTGDTpaserqrQRrRP-PHILITTPESLALLLTSpdARELLRGVRTVIVDEIHA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217362817 428 INDVERGvvweeVLIML---------PDHVSIILLSATVPNALEFADWIG 468
Cdd:COG1201 173 LAGSKRG-----VHLALslerlralaPRPLQRIGLSATVGPLEEVARFLV 217
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
634-708 |
4.01e-08 |
|
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: 52.21 E-value: 4.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217362817 634 VHHSGILPILKEIVEMLFSRGLVKVLFATETFAMGVNMP-ARTVVFDSMrkhdgstfrDLLPGEYVQMAGRAGRRG 708
Cdd:pfam00271 43 RLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVINYDL---------PWNPASYIQRIGRAGRAG 109
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
314-482 |
1.31e-07 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 55.42 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 314 FQKQAI------LHLERHDSVFVAAhTSAGKTVVAEYAIALAQKHMtRTIYTSPIKALSNQKFRDFRNTFGDVGLLTGDV 387
Cdd:COG1061 84 YQQEALeallaaLERGGGRGLVVAP-TGTGKTVLALALAAELLRGK-RVLVLVPRRELLEQWAEELRRFLGDPLAGGGKK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 388 QlhPEASCLIMTTEILRSMLYSgsDVIRDlEW--VIFDEVHYIndveRGVVWEEVLIMLPDHVsIILLSATvpnaLEFAD 465
Cdd:COG1061 162 D--SDAPITVATYQSLARRAHL--DELGD-RFglVIIDEAHHA----GAPSYRRILEAFPAAY-RLGLTAT----PFRSD 227
|
170
....*....|....*..
gi 2217362817 466 WIGRLKRRQIYVISTVT 482
Cdd:COG1061 228 GREILLFLFDGIVYEYS 244
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
332-462 |
1.01e-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: 49.98 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 332 AHTSAGKTvvaEYAIALAQKH-----MTRTIYTSPIKALSNQKFRDFRNTFG------DVGLLTGDVQLHPE-------- 392
Cdd:cd17930 8 APTGSGKT---EAALLWALKLaarggKRRIIYALPTRATINQMYERIREILGrlddedKVLLLHSKAALELLesdeepdd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 393 ----------------ASCLIMTT--EILRSMLYSGSDVIRDLEW----VIFDEVHYInDVERGVVWEEVLIMLPDH--V 448
Cdd:cd17930 85 dpveavdwalllkrswLAPIVVTTidQLLESLLKYKHFERRLHGLansvVVLDEVQAY-DPEYMALLLKALLELLGElgG 163
|
170
....*....|....
gi 2217362817 449 SIILLSATVPNALE 462
Cdd:cd17930 164 PVVLMTATLPALLR 177
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
330-468 |
2.12e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 51.85 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 330 VAAHTSAGKTVVA-EYAI------------ALAQKHMTRTIYTSPIKALSNQKFRDF----------RNTFGD------V 380
Cdd:PRK09751 1 VIAPTGSGKTLAAfLYALdrlfreggedtrEAHKRKTSRILYISPIKALGTDVQRNLqiplkgiadeRRRRGEtevnlrV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 381 GLLTGDVQLHPEA-------SCLIMTTEILRSMLYS-GSDVIRDLEWVIFDEVHYINDVERG----VVWEEVLIMLPDHV 448
Cdd:PRK09751 81 GIRTGDTPAQERSkltrnppDILITTPESLYLMLTSrARETLRGVETVIIDEVHAVAGSKRGahlaLSLERLDALLHTSA 160
|
170 180
....*....|....*....|
gi 2217362817 449 SIILLSATVPNALEFADWIG 468
Cdd:PRK09751 161 QRIGLSATVRSASDVAAFLG 180
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
309-464 |
3.79e-05 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the 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: 350676 [Multi-domain] Cd Length: 180 Bit Score: 45.48 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 309 FEPDVFQKQAI------LHLERHDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFRNTFGD--V 380
Cdd:cd17918 14 FSLTKDQAQAIkdiekdLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARKFLPFinV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 381 GLLTGDV--QLHPEASCLIMTTEILRSMLYSgsdviRDLEWVIFDEVHYIndverGVVWEEVLIMLpDHVSIILLSAT-V 457
Cdd:cd17918 94 ELVTGGTkaQILSGISLLVGTHALLHLDVKF-----KNLDLVIVDEQHRF-----GVAQREALYNL-GATHFLEATATpI 162
|
....*..
gi 2217362817 458 PNALEFA 464
Cdd:cd17918 163 PRTLALA 169
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
627-743 |
1.68e-04 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 45.47 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 627 LLNRGLGV--HHSGILPILKEIVEMLFSRGLVKVLFATETFAMGVNMP-ARTVV-FDSMRKHDgstfrdllpgEYVQMAG 702
Cdd:PRK11057 256 LQSRGISAaaYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPnVRFVVhFDIPRNIE----------SYYQETG 325
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2217362817 703 RAGRRGLdPTGTVILLCKGrvpEMADLHRMMMGKPSQLQSQ 743
Cdd:PRK11057 326 RAGRDGL-PAEAMLFYDPA---DMAWLRRCLEEKPAGQQQD 362
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
626-709 |
1.72e-04 |
|
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: 42.58 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 626 ELLNRGL--GVHHSGILPILKEIVEMLFSRGLVKVLFATETFAMGVNMP-ARTVVfdsmrkHDGstfrdlLPG---EYVQ 699
Cdd:cd18794 49 RLQSKGIsaAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPdVRFVI------HYS------LPKsmeSYYQ 116
|
90
....*....|
gi 2217362817 700 MAGRAGRRGL 709
Cdd:cd18794 117 ESGRAGRDGL 126
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
334-426 |
1.95e-04 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 45.49 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 334 TSAGKTVVAEYAIA-LAQKHMTRTIYTSPIKALSNQKFRDFRNTFG----DVGLLTGDVQ------LHPEASCLIMTTEI 402
Cdd:COG1111 26 TGLGKTAVALLVIAeRLHKKGGKVLFLAPTKPLVEQHAEFFKEALNipedEIVVFTGEVSpekrkeLWEKARIIVATPQV 105
|
90 100
....*....|....*....|....
gi 2217362817 403 LRSMLYSGSDVIRDLEWVIFDEVH 426
Cdd:COG1111 106 IENDLIAGRIDLDDVSLLIFDEAH 129
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
698-726 |
5.08e-04 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 43.71 E-value: 5.08e-04
10 20
....*....|....*....|....*....
gi 2217362817 698 VQMAGRAGRRGLDPTGTVILLCKGRVPEM 726
Cdd:COG4098 406 VQIAGRVGRSADYPTGEVIFFHHGKTRAM 434
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
310-426 |
1.19e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 40.96 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 310 EPDVFQKQAILHLERHDSVFVAAhTSAGKTVVAEYAIA-LAQKHMTRTIYTSPIKALSNQ---KFRDFRNTFGDVGLLTG 385
Cdd:cd18035 2 ERRLYQVLIAAVALNGNTLIVLP-TGLGKTIIAILVAAdRLTKKGGKVLILAPSRPLVEQhaeNLKRVLNIPDKITSLTG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2217362817 386 DVQ------LHPEASCLIMTTEILRSMLYSGSDVIRDLEWVIFDEVH 426
Cdd:cd18035 81 EVKpeeraeRWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAH 127
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
315-456 |
2.20e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 39.96 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 315 QKQAI-----LHLERHDSVFVAAHTSAGKTVVAEYAIALAQK--HMTRTIYTSPIKALSNQKFRDFRNTFGD----VGLL 383
Cdd:pfam04851 8 QIEAIenlleSIKNGQKRGLIVMATGSGKTLTAAKLIARLFKkgPIKKVLFLVPRKDLLEQALEEFKKFLPNyveiGEII 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217362817 384 TGDVQLHPEASC--LIMTTEILRSMLYSGSDVIRDLEW--VIFDEVHYINDVErgvvWEEVLIMLPDhvSIIL-LSAT 456
Cdd:pfam04851 88 SGDKKDESVDDNkiVVTTIQSLYKALELASLELLPDFFdvIIIDEAHRSGASS----YRNILEYFKP--AFLLgLTAT 159
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
643-719 |
2.86e-03 |
|
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: 37.30 E-value: 2.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217362817 643 LKEIVEMLfsrglvKVLFATETFAMGVNMP-ARTVVFDSMRKHdgstfrdllPGEYVQMAGRAGRRGLDPtGTVILLC 719
Cdd:cd18785 16 AEEIASSL------EILVATNVLGEGIDVPsLDTVIFFDPPSS---------AASYIQRVGRAGRGGKDE-GEVILFV 77
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
636-718 |
7.99e-03 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 39.74 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362817 636 HSGILPILKEIVEMLFSRGLVKVLFATETFAMGVNMP-ARTVVfdsmrkHDGstfrdlLPG---EYVQMAGRAGRRGLDp 711
Cdd:COG0514 261 HAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPdVRFVI------HYD------LPKsieAYYQEIGRAGRDGLP- 327
|
....*..
gi 2217362817 712 tGTVILL 718
Cdd:COG0514 328 -AEALLL 333
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