|
Name |
Accession |
Description |
Interval |
E-value |
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
4-747 |
0e+00 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 631.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 4 EYQGLKLDQFQMDAIEAINHGHSVIVSAPTGTGKTMVADYLVEKSIREGQRIIYTAPIKALSNQKFKDFSRQFGSKTIGI 83
Cdd:COG4581 20 EERGFELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALARGRRSFYTAPIKALSNQKFFDLVERFGAENVGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 84 MTGDVVINPGAPLLIMTTEIFRNQVITNDPELEHVSYIIFDEIHWLNDEDRGTVWEESIILAPPNIKILGLSATIANAAE 163
Cdd:COG4581 100 LTGDASVNPDAPIVVMTTEILRNMLYREGADLEDVGVVVMDEFHYLADPDRGWVWEEPIIHLPARVQLVLLSATVGNAEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 164 LKGWIEAIRKDTVVLIEEqQRIVPLEYYYFCQDTGIigydDLIRFyyqklkstdrtdNSPLFKPTSHLDLIKTVD-KQYL 242
Cdd:COG4581 180 FAEWLTRVRGETAVVVSE-ERPVPLEFHYLVTPRLF----PLFRV------------NPELLRPPSRHEVIEELDrGGLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 243 PTLYFVFSRKQCADKAHELANIkNYLSSEQSKEVKNIFLEHfgAEDTWSSSTRKLFRVCRKGIAYHHAGLLPLQKSVVED 322
Cdd:COG4581 243 PAIVFIFSRRGCDEAAQQLLSA-RLTTKEERAEIREAIDEF--AEDFSVLFGKTLSRLLRRGIAVHHAGMLPKYRRLVEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 323 LFLAKTISVLYCTETFSVGINYPVKAVCFDSLNKYDGRSFRALANHEFFQMSGRAGRRGIDEIGYSFAIVDlnyfEKEPP 402
Cdd:COG4581 320 LFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDTEGHVVVLAP----EHDDP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 403 VKFD---IAKLEPLTSQFRLSYNTVLNLLATLSPEQIETYFKKSFAAHSYILTAQKTEEEIRLLSEQSAQAKENLCEHVG 479
Cdd:COG4581 396 KKFArlaSARPEPLRSSFRPSYNMVLNLLARPGLERARELLEDSFAQFQADRSVVGLARRARELERALAGVVERLACDLG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 480 TYRCPLNYYPKKKELDRLHK---AYA----------KLDPR----------RRNKIfgRQMHRKIMKWEKIlKTVPQKCT 536
Cdd:COG4581 476 DLQEYFALRQPLSPLEALERespAYAldvvsvpeatLEDPRpvllaqdrraRGEAA--AAMKAAIEYDERM-ERLEEVLR 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 537 RKQNDSCKsfAGNWMNLEKEITDLKNQLFSMPdyNTFNSEFERKKALLQQIGYIGNDKLLPRGELARYIYVqeilVTELI 616
Cdd:COG4581 553 PHPLHECP--LERAFELYRETHPWVRDIELRP--KSVARDFDRFCELLREYGYLDDLTLTSEGLLLRYLYD----AAEAL 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 617 YSGIIEQLDDDQLTALISCIDYESKRNEYFQKF------DQIDFKPVREILNYIQSICgpDAVRFESKAAVLAYYWSKGA 690
Cdd:COG4581 625 RQGVPDDLDPEELAALISWLVEEVRRVDSSEWErlpspaNRRAFVLVNALFRRLELLE--RRHGLPELDPGLAGAWASGA 702
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 504855318 691 ALIELQLLCTLDEGDIIAVLRRTIDllrqmreavTDQSLRERFSVCIKKLDRDEASI 747
Cdd:COG4581 703 DLAEVLDATDLDAGDFVRWVRQVID---------PDPELRRTARAAVDLIRRGVVAY 750
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
13-466 |
1.19e-71 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 243.26 E-value: 1.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 13 FQMDAIEA-INHGHSVIVSAPTGTGKTMVADYLVEKSIREGQRIIYTAPIKALSNQKFKDFSRQFGSK--TIGIMTGDVV 89
Cdd:COG1204 26 PQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNGGKALYIVPLRALASEKYREFKRDFEELgiKVGVSTGDYD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 90 INPGAP----LLIMTTEIFRnQVITNDPE-LEHVSYIIFDEIHWLNDEDRGTVWE---ESIILAPPNIKILGLSATIANA 161
Cdd:COG1204 106 SDDEWLgrydILVATPEKLD-SLLRNGPSwLRDVDLVVVDEAHLIDDESRGPTLEvllARLRRLNPEAQIVALSATIGNA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 162 AELKGWIEAirkdtvVLIEEQQRIVPLEYYYFCQdtGIIGYDDlirfyyQKLKSTDRTdnsplfkptshLDLIKTVDKQY 241
Cdd:COG1204 185 EEIAEWLDA------ELVKSDWRPVPLNEGVLYD--GVLRFDD------GSRRSKDPT-----------LALALDLLEEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 242 LPTLYFVFSRKQCADKAHELAN-IKNYLSSEQSKEVKNIfLEHFGAEDTWSSSTRKLFRVCRKGIAYHHAGLLPLQKSVV 320
Cdd:COG1204 240 GQVLVFVSSRRDAESLAKKLADeLKRRLTPEEREELEEL-AEELLEVSEETHTNEKLADCLEKGVAFHHAGLPSELRRLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 321 EDLFLAKTISVLYCTETFSVGINYPVKAVCFDSLNKYDGRSFRALanhEFFQMSGRAGRRGIDEIGYSFAIVDLNYFEKE 400
Cdd:COG1204 319 EDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGMVPIPVL---EFKQMAGRAGRPGYDPYGEAILVAKSSDEADE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504855318 401 PPVKFDIAKLEPLTSQF---RLSYNTVLNLLAT---LSPEQIETYFKKSFAAHSY--ILTAQKTEEEIRLLSEQ 466
Cdd:COG1204 396 LFERYILGEPEPIRSKLaneSALRTHLLALIASgfaNSREELLDFLENTFYAYQYdkGDLEEVVDDALEFLLEN 469
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
9-173 |
2.52e-65 |
|
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: 215.39 E-value: 2.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 9 KLDQFQMDAIEAINHGHSVIVSAPTGTGKTMVADYLVEKSIREGQRIIYTAPIKALSNQKFKDFSRQFGSktIGIMTGDV 88
Cdd:cd18024 32 TLDPFQKTAIACIERNESVLVSAHTSAGKTVVAEYAIAQSLRDKQRVIYTSPIKALSNQKYRELQEEFGD--VGLMTGDV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 89 VINPGAPLLIMTTEIFRNQVITNDPELEHVSYIIFDEIHWLNDEDRGTVWEESIILAPPNIKILGLSATIANAAELKGWI 168
Cdd:cd18024 110 TINPNASCLVMTTEILRSMLYRGSEIMREVAWVIFDEIHYMRDKERGVVWEETIILLPDKVRYVFLSATIPNARQFAEWI 189
|
....*
gi 504855318 169 EAIRK 173
Cdd:cd18024 190 CKIHK 194
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
8-179 |
9.97e-54 |
|
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: 183.23 E-value: 9.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 8 LKLDQFQMDAIEAINHGHSVIVSAPTGTGKTMVADYLVEKSIREGQRIIYTAPIKALSNQKFKDFSRQFGSktIGIMTGD 87
Cdd:cd18027 7 FELDVFQKQAILHLEAGDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGD--VGLITGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 88 VVINPGAPLLIMTTEIFRNQVITNDPELEHVSYIIFDEIHWLNDEDRGTVWEESIILAPPNIKILGLSATIANAAELKGW 167
Cdd:cd18027 85 VQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDHVSIILLSATVPNTVEFADW 164
|
170
....*....|..
gi 504855318 168 IEAIRKDTVVLI 179
Cdd:cd18027 165 IGRIKKKNIYVI 176
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
10-171 |
4.35e-51 |
|
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: 175.91 E-value: 4.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 10 LDQFQMDAIEAI-NHGHSVIVSAPTGTGKTMVADYLVEKSIRE-GQRIIYTAPIKALSNQKFKDFSRQFGS--KTIGIMT 85
Cdd:cd17921 2 LNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATsGGKAVYIAPTRALVNQKEADLRERFGPlgKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 86 GDVVIN----PGAPLLIMTTEIFRNQVITN-DPELEHVSYIIFDEIHWLNDEDRGTVWEESIILAP---PNIKILGLSAT 157
Cdd:cd17921 82 GDPSVNklllAEADILVATPEKLDLLLRNGgERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrinKNARFVGLSAT 161
|
170
....*....|....
gi 504855318 158 IANAAELKGWIEAI 171
Cdd:cd17921 162 LPNAEDLAEWLGVE 175
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
14-460 |
5.41e-47 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 177.77 E-value: 5.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 14 QMDAIEAINHGHSVIVSAPTGTGKTMVADYLVEKSIREGQRIIYTAPIKALSNQKFKDFS--RQFGSKtIGIMTGDVVIN 91
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELSrlRSLGMR-VKISIGDYDDP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 92 PG----APLLIMTTEIfRNQVITNDPE-LEHVSYIIFDEIHWLNDEDRGTVWEESIILA---PPNIKILGLSATIANAAE 163
Cdd:PRK01172 106 PDfikrYDVVILTSEK-ADSLIHHDPYiINDVGLIVADEIHIIGDEDRGPTLETVLSSAryvNPDARILALSATVSNANE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 164 LKGWIEAirkdtvVLIEEQQRIVPLEyyyfcqdTGIIGYDDLIrfyyqkLKSTDRTDnsplfkpTSHLDLIKTVDKQYLP 243
Cdd:PRK01172 185 LAQWLNA------SLIKSNFRPVPLK-------LGILYRKRLI------LDGYERSQ-------VDINSLIKETVNDGGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 244 TLYFVFSRKQCADKAHELANIKNYLSS-EQSKEVKNIFLEhfgaedtwssstrKLFRVCRKGIAYHHAGLLPLQKSVVED 322
Cdd:PRK01172 239 VLVFVSSRKNAEDYAEMLIQHFPEFNDfKVSSENNNVYDD-------------SLNEMLPHGVAFHHAGLSNEQRRFIEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 323 LFLAKTISVLYCTETFSVGINYPVKAVCFDSLNKYDGRSFRALANHEFFQMSGRAGRRGIDEIGYSfaivdlnYFEKEPP 402
Cdd:PRK01172 306 MFRNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIG-------YIYAASP 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 403 VKFDIAK------LEPLTSQFRLSYNTVLNLLATLS------PEQIETYFKKSFAAhsyiltAQKTEEEI 460
Cdd:PRK01172 379 ASYDAAKkylsgePEPVISYMGSQRKVRFNTLAAISmglassMEDLILFYNETLMA------IQNGVDEI 442
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
14-386 |
2.92e-45 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 173.61 E-value: 2.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 14 QMDAIEA-INHGHSVIVSAPTGTGKTMVADYLVEKSIREGQRIIYTAPIKALSNQKFKDFSR--QFGSKtIGIMTGD--- 87
Cdd:PRK02362 28 QAEAVEAgLLDGKNLLAAIPTASGKTLIAELAMLKAIARGGKALYIVPLRALASEKFEEFERfeELGVR-VGISTGDyds 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 88 ----VVINPgapLLIMTTE----IFRNqvitNDPELEHVSYIIFDEIHWLNDEDRGTVWEesIILAP-----PNIKILGL 154
Cdd:PRK02362 107 rdewLGDND---IIVATSEkvdsLLRN----GAPWLDDITCVVVDEVHLIDSANRGPTLE--VTLAKlrrlnPDLQVVAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 155 SATIANAAELKGWIEAirkdtvVLIEEQQRIVPLEyyyfcqdTGIIgYDDLIRFyyqklKSTDRTDNSPLFKPTSHLdLI 234
Cdd:PRK02362 178 SATIGNADELADWLDA------ELVDSEWRPIDLR-------EGVF-YGGAIHF-----DDSQREVEVPSKDDTLNL-VL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 235 KTVDKQYlPTLYFVFSRKQCADKAHELAN-IKNYLSSEQSKEVKNIFLEHFGAEDTWSSStrKLFRVCRKGIAYHHAGLL 313
Cdd:PRK02362 238 DTLEEGG-QCLVFVSSRRNAEGFAKRAASaLKKTLTAAERAELAELAEEIREVSDTETSK--DLADCVAKGAAFHHAGLS 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504855318 314 PLQKSVVEDLFLAKTISVLYCTETFSVGINYPVKAVCFDSLNKYDGRS-FRALANHEFFQMSGRAGRRGIDEIG 386
Cdd:PRK02362 315 REHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAgMQPIPVLEYHQMAGRAGRPGLDPYG 388
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
14-447 |
2.47e-37 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 149.58 E-value: 2.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 14 QMDAIEA-INHGHSVIVSAPTGTGKTMVADY-LVEKSIREGQRIIYTAPIKALSNQKFKDFS--RQFGSKtIGIMTGDVV 89
Cdd:PRK00254 28 QAEALKSgVLEGKNLVLAIPTASGKTLVAEIvMVNKLLREGGKAVYLVPLKALAEEKYREFKdwEKLGLR-VAMTTGDYD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 90 INP----GAPLLIMTTEIFRNQVITNDPELEHVSYIIFDEIHWLNDEDRGTVWEESIILAPPNIKILGLSATIANAAELK 165
Cdd:PRK00254 107 STDewlgKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQILGLSATVGNAEELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 166 GWIEAirkdtvVLIEEQQRIVPLEYYYFCQdtGIIGYDDlirfyyqklKSTDRTdnsplfkPTSHLDLIKTVDKQYLPTL 245
Cdd:PRK00254 187 EWLNA------ELVVSDWRPVKLRKGVFYQ--GFLFWED---------GKIERF-------PNSWESLVYDAVKKGKGAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 246 YFVFSRKQCADKAHELAN-IKNYLSSEQSKEVKNIflehfgAEDTWSSST-RKLFRVCRKGIAYHHAGLLPLQKSVVEDL 323
Cdd:PRK00254 243 VFVNTRRSAEKEALELAKkIKRFLTKPELRALKEL------ADSLEENPTnEKLKKALRGGVAFHHAGLGRTERVLIEDA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 324 FLAKTISVLYCTETFSVGINYPVKAVCFDSLNKYDGRSFRALANHEFFQMSGRAGRRGIDEIGYSFaIVDLNYFEKEPPV 403
Cdd:PRK00254 317 FREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAI-IVATTEEPSKLME 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 504855318 404 KFDIAKLEPLTSQ------FRlsyNTVLNLLATL---SPEQIETYFKKSFAAH 447
Cdd:PRK00254 396 RYIFGKPEKLFSMlsnesaFR---SQVLALITNFgvsNFKELVNFLERTFYAH 445
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
184-393 |
2.97e-35 |
|
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: 130.75 E-value: 2.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 184 RIVPLE-YYYFCQDTGIIGyddlirfyyQKLKSTDRTDNSPLFKptshldLIKTVdKQYLPTLYFVFSRKQCADKAHELA 262
Cdd:cd18795 1 RPVPLEeYVLGFNGLGIKL---------RVDVMNKFDSDIIVLL------KIETV-SEGKPVLVFCSSRKECEKTAKDLA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 263 niknylsseqskevkniflehfgaedtwssstrklfrvcrkGIAYHHAGLLPLQKSVVEDLFLAKTISVLYCTETFSVGI 342
Cdd:cd18795 65 -----------------------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGV 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504855318 343 NYPVKAVCFDSLNKYDGRSFRALANHEFFQMSGRAGRRGIDEIGYSFAIVD 393
Cdd:cd18795 104 NLPARTVIIKGTQRYDGKGYRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
14-170 |
3.68e-31 |
|
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: 120.13 E-value: 3.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 14 QMDAIEA-INHGHSVIVSAPTGTGKTMVADYLVEKSIREGQRIIYTAPIKALSNQKFKDFSR--QFGSKtIGIMTGDVVI 90
Cdd:cd18028 6 QAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKKleEIGLK-VGISTGDYDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 91 NPG----APLLIMTTEIFrNQVITNDPE-LEHVSYIIFDEIHWLNDEDRGTVWEESIILA---PPNIKILGLSATIANAA 162
Cdd:cd18028 85 DDEwlgdYDIIVATYEKF-DSLLRHSPSwLRDVGVVVVDEIHLISDEERGPTLESIVARLrrlNPNTQIIGLSATIGNPD 163
|
....*...
gi 504855318 163 ELKGWIEA 170
Cdd:cd18028 164 ELAEWLNA 171
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
14-163 |
1.18e-29 |
|
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: 115.42 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 14 QMDAIEAINHGHSVIVSAPTGTGKTMVADYLVEKSIR---EGQRIIYTAPIKALSNQKFKDFSRQF---GSKTIGIMTGD 87
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDkldNGPQALVLAPTRELAEQIYEELKKLGkglGLKVASLLGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 88 VVIN-----PGAPLLIMTTEIFRNqVITNDPELEHVSYIIFDEIHWLNDEDRGTVWEESIILAPPNIKILGLSATIANAA 162
Cdd:pfam00270 84 SRKEqleklKGPDILVGTPGRLLD-LLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATLPRNL 162
|
.
gi 504855318 163 E 163
Cdd:pfam00270 163 E 163
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
2-163 |
1.58e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 110.66 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 2 ISEYQGLKLDQFQMDAIEAINHG-HSVIVSAPTGTGKTMVADYLVEKSIREGQ--RIIYTAPIKALSNQKFKDFSRQFGS 78
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELKKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 79 ---KTIGIMTGDV-------VINPGAPLLIMTTEIFRNQVITNDPELEHVSYIIFDEIHWLNDEDRGTVWEESIILAPPN 148
Cdd:smart00487 81 lglKVVGLYGGDSkreqlrkLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKN 160
|
170
....*....|....*
gi 504855318 149 IKILGLSATIANAAE 163
Cdd:smart00487 161 VQLLLLSATPPEEIE 175
|
|
| DSHCT |
pfam08148 |
DSHCT (NUC185) domain; This C terminal domain is found in DOB1/SK12/helY-like DEAD box ... |
593-743 |
1.91e-25 |
|
DSHCT (NUC185) domain; This C terminal domain is found in DOB1/SK12/helY-like DEAD box helicases.
Pssm-ID: 462374 Cd Length: 154 Bit Score: 102.91 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 593 DKLLPRGELARYIY-VQEILVTELIYSGIIEQLDDDQLTALISCIDYESKRNEYFQKFDQIDfKPVREILNYIQSICGPD 671
Cdd:pfam08148 1 DVVTLKGRVACEIRsENELLLTELLFSGVFDDLDPEELAALLSAFVFEEKRREPYLPSPELA-EALRLLEEIAHRIAVSR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504855318 672 AVRFEskAAVLAYYWSKGAALIELQLLCTLDEGDIIAVLRRTIDLLRQMREA---VTDQSLRERFSVCIKKLDRD 743
Cdd:pfam08148 80 FLDFG--LMEVVYAWARGASFAEICKLTDLDEGDIVRLIRRLDELLRQIANAakiIGDPELREKAEEAIELIKRD 152
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
11-184 |
3.18e-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: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 11 DQFQMDAIEAINHGHSVIVSAPTGTGKTMVADYLVEKSIREGQR--IIYTAPIKALSNQ-------KFKDFSRQFGSKTI 81
Cdd:cd18025 3 DAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDgvVVYVAPTKALVNQvvaevyaRFSKKYPPSGKSLW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 82 GIMTGDVVINP--GAPLLIMTTEIFRNQVITNDPE--LEHVSYIIFDEIHWLNDEDRGTVWEESIILAP-PnikILGLSA 156
Cdd:cd18025 83 GVFTRDYRHNNpmNCQVLITVPECLEILLLSPHNAswVPRIKYVIFDEIHSIGQSEDGAVWEQLLLLIPcP---FLALSA 159
|
170 180 190
....*....|....*....|....*....|.
gi 504855318 157 TIANAAELKGWIEAI---RKDTVVLIEEQQR 184
Cdd:cd18025 160 TIGNPQKFHEWLQSVqraRKAELKKIEHNHR 190
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
28-396 |
3.20e-22 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 102.28 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 28 IVSApTGTGKTMVADYL-VEKSIREGQRIIYTAPIKALSNQKFKDFSRQFGSK-TIGIMTGDVVIN-------PGAPLLI 98
Cdd:COG1202 230 VVSA-TATGKTLIGELAgIKNALEGKGKMLFLVPLVALANQKYEDFKDRYGDGlDVSIRVGASRIRddgtrfdPNADIIV 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 99 MTTEIFRNQVITNDPeLEHVSYIIFDEIHWLNDEDRGTVWEESI----ILApPNIKILGLSATIANAAELKGWIEAirkd 174
Cdd:COG1202 309 GTYEGIDHALRTGRD-LGDIGTVVIDEVHMLEDPERGHRLDGLIarlkYYC-PGAQWIYLSATVGNPEELAKKLGA---- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 175 tvVLIEEQQRIVPLEYYY-FCQDtgiigyddlirfyYQKLKSTDRtdnsplfkptshldLIK-----TVDKQYL-PTLYF 247
Cdd:COG1202 383 --KLVEYEERPVPLERHLtFADG-------------REKIRIINK--------------LVKrefdtKSSKGYRgQTIIF 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 248 VFSRKQCadkaHELAnikNYLSseqskevkniflehfgaedtwssstrklfrvcrKGIAYHHAGLLPLQKSVVEDLFLAK 327
Cdd:COG1202 434 TNSRRRC----HEIA---RALG---------------------------------YKAAPYHAGLDYGERKKVERRFADQ 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504855318 328 TISVLYCTETFSVGINYPVKAVCFDSL---NKYdgrsfraLANHEFFQMSGRAGRRGIDEIG--YSFAIVDLNY 396
Cdd:COG1202 474 ELAAVVTTAALAAGVDFPASQVIFDSLamgIEW-------LSVQEFHQMLGRAGRPDYHDRGkvYLLVEPGKSY 540
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
26-168 |
2.81e-20 |
|
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: 89.36 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 26 SVIVSAPTGTGKTMVADYLVEKSIRE--GQRIIYTAPIKALSNQKFKD----FSRQFGSKTIGiMTGDVVINP----GAP 95
Cdd:cd18022 19 NVLLGAPTGSGKTIAAELAMFRAFNKypGSKVVYIAPLKALVRERVDDwkkrFEEKLGKKVVE-LTGDVTPDMkalaDAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 96 LLIMTTE----IFRNQviTNDPELEHVSYIIFDEIHWLNdEDRGTVWEesIILAPPN---------IKILGLSATIANAA 162
Cdd:cd18022 98 IIITTPEkwdgISRSW--QTREYVQQVSLIIIDEIHLLG-SDRGPVLE--VIVSRMNyissqtekpVRLVGLSTALANAG 172
|
....*.
gi 504855318 163 ELKGWI 168
Cdd:cd18022 173 DLANWL 178
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
26-168 |
1.09e-16 |
|
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: 79.32 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 26 SVIVSAPTGTGKTMVADYLVEKSIRE-------GQRIIYTAPIKALSNQKFKDFSRQFGSKTIGIM--TGDVVINPgapl 96
Cdd:cd18023 19 NFVVSAPTGSGKTVLFELAILRLLKErnplpwgNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCAelTGDTEMDD---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 97 limTTEIFRNQVITNDPE---------------LEHVSYIIFDEIHWLNDEdRGTVWE-------------ESIILAPPN 148
Cdd:cd18023 95 ---TFEIQDADIILTTPEkwdsmtrrwrdngnlVQLVALVLIDEVHIIKEN-RGATLEvvvsrmktlssssELRGSTVRP 170
|
170 180
....*....|....*....|
gi 504855318 149 IKILGLSATIANAAELKGWI 168
Cdd:cd18023 171 MRFVAVSATIPNIEDLAEWL 190
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
24-157 |
5.87e-16 |
|
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: 75.52 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 24 GHSVIVSAPTGTGKTMVA-----DYLVEKsireGQRIIYTAPIKALSNQKFKDFSRQFG-SKTIGIMTGDV-------VI 90
Cdd:cd00046 1 GENVLITAPTGSGKTLAAllaalLLLLKK----GKKVLVLVPTKALALQTAERLRELFGpGIRVAVLVGGSsaeerekNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 91 NPGAPLLIMTTEIFRNQVITND-PELEHVSYIIFDEIHWLNDEDRGTVWEESII--LAPPNIKILGLSAT 157
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHALLIDSRGALILDLAVrkAGLKNAQVILLSAT 146
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
23-170 |
4.18e-15 |
|
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: 74.56 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 23 HGHSVIVSAPTGTGKTMVADYLVEKSIREGQRI-IYTAPIKALSNQK---FKDFSRQFGSKTIGIMTGDVVINPGAP--- 95
Cdd:cd18026 32 EGRNLVYSLPTSGGKTLVAEILMLKRLLERRKKaLFVLPYVSIVQEKvdaLSPLFEELGFRVEGYAGNKGRSPPKRRksl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 96 -LLIMTTE---IFRNQVITNDpELEHVSYIIFDEIHWLNDEDRGTVWEESII----LAPPNIKILGLSATIANAAELKGW 167
Cdd:cd18026 112 sVAVCTIEkanSLVNSLIEEG-RLDELGLVVVDELHMLGDGHRGALLELLLTkllyAAQKNIQIVGMSATLPNLEELASW 190
|
...
gi 504855318 168 IEA 170
Cdd:cd18026 191 LRA 193
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
8-173 |
4.73e-15 |
|
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: 74.39 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 8 LKLDQFQMDAIEAINHGHSVIVSAPTGTGKTMVA-----DYLVEKSIREGQRIIYTAPIKALSNQKFKDFSRQF---GSK 79
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTFVAvliceHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFerpGYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 80 TIGImTGDVVINPGAPL-------LIMTTEIFRNQVIT-NDPELEHVSYIIFDEIHWLNDEdrgTVW--------EESII 143
Cdd:cd17927 81 VTGL-SGDTSENVSVEQivessdvIIVTPQILVNDLKSgTIVSLSDFSLLVFDECHNTTKN---HPYneimfrylDQKLG 156
|
170 180 190
....*....|....*....|....*....|..
gi 504855318 144 LAPPNIKILGLSATIAN--AAELKGWIEAIRK 173
Cdd:cd17927 157 SSGPLPQILGLTASPGVggAKNTEEALEHICK 188
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
24-168 |
2.60e-14 |
|
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: 71.46 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 24 GHSVIVSAPTGTGKTMVA------DYLVEKSirEGQRIIYTAPIKALSNQKFK---DFSRQFGSK-TIGIMTGDV----- 88
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAflpalsSLADEPE--KGVQVLYISPLKALINDQERrleEPLDEIDLEiPVAVRHGDTsqsek 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 89 ---VINPgaP-LLIMTTEIFrNQVITN---DPELEHVSYIIFDEIHWLNDEDRGTVWEESII----LAPPNIKILGLSAT 157
Cdd:cd17922 79 akqLKNP--PgILITTPESL-ELLLVNkklRELFAGLRYVVVDEIHALLGSKRGVQLELLLErlrkLTGRPLRRIGLSAT 155
|
170
....*....|.
gi 504855318 158 IANAAELKGWI 168
Cdd:cd17922 156 LGNLEEAAAFL 166
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
13-167 |
2.58e-13 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 73.60 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 13 FQMDAIEAINHGHSVIVSAPTGTGKTMVA-----DYLVEKSI----REGQRIIYTAPIKALSNqkfkDFSR--------- 74
Cdd:COG1201 28 PQREAWPAIAAGESTLLIAPTGSGKTLAAflpalDELARRPRpgelPDGLRVLYISPLKALAN----DIERnlrapleei 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 75 --QFGSK----TIGIMTGD--------VVINPgaPLLIMTTeifrnqvitndPE--------------LEHVSYIIFDEI 126
Cdd:COG1201 104 geAAGLPlpeiRVGVRTGDtpaserqrQRRRP--PHILITT-----------PEslallltspdarelLRGVRTVIVDEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504855318 127 HWLNDEDRGTVWEESI----ILAPPNIKILGLSATIANAAELKGW 167
Cdd:COG1201 171 HALAGSKRGVHLALSLerlrALAPRPLQRIGLSATVGPLEEVARF 215
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
26-168 |
8.50e-13 |
|
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: 67.67 E-value: 8.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 26 SVIVSAPTGTGKTMVADYLVEKSIREG--QRIIYTAPIKALSNQKFKDFSRQFGS---KTIGIMTGDVVINpgAPLLImt 100
Cdd:cd18021 21 NVFVGAPTGSGKTVCAELALLRHWRQNpkGRAVYIAPMQELVDARYKDWRAKFGPllgKKVVKLTGETSTD--LKLLA-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 101 teifRNQVITNDPE--------------LEHVSYIIFDEIHWLNDEDrGTVWEesIILA---------PPNIKILGLSAT 157
Cdd:cd18021 97 ----KSDVILATPEqwdvlsrrwkqrknVQSVELFIADELHLIGGEN-GPVYE--VVVSrmryissqlEKPIRIVGLSSS 169
|
170
....*....|.
gi 504855318 158 IANAAELKGWI 168
Cdd:cd18021 170 LANARDVGEWL 180
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
13-157 |
1.45e-12 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 70.82 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 13 FQMDAIEAI-----NHGHSVIVSAPTGTGKTMVADYLVEKsIREGQRIIYTAPIKALSNQKFKDFSRQFGsktiGIMTGD 87
Cdd:COG1061 84 YQQEALEALlaaleRGGGRGLVVAPTGTGKTVLALALAAE-LLRGKRVLVLVPRRELLEQWAEELRRFLG----DPLAGG 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504855318 88 VVINPGAPLLIMTteifrNQVITNDPELE----HVSYIIFDEIHWLndedRGTVWEESIILAPPNiKILGLSAT 157
Cdd:COG1061 159 GKKDSDAPITVAT-----YQSLARRAHLDelgdRFGLVIIDEAHHA----GAPSYRRILEAFPAA-YRLGLTAT 222
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
27-160 |
1.63e-12 |
|
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: 67.40 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 27 VIVSAPTGTGKTMVADYLVEKSI-----REGQ------RIIYTAPIKALSNQKFKDFSRQFgsKTIGI----MTGDVVIN 91
Cdd:cd18019 36 LLLCAPTGAGKTNVALLTILREIgkhrnPDGTinldafKIVYIAPMKALVQEMVGNFSKRL--APYGItvaeLTGDQQLT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 92 pgapllimTTEIFRNQVITNDPE--------------LEHVSYIIFDEIHWLNDeDRGTVWeESII--------LAPPNI 149
Cdd:cd18019 114 --------KEQISETQIIVTTPEkwdiitrksgdrtyTQLVRLIIIDEIHLLHD-DRGPVL-ESIVartirqieQTQEYV 183
|
170
....*....|.
gi 504855318 150 KILGLSATIAN 160
Cdd:cd18019 184 RLVGLSATLPN 194
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
10-157 |
2.26e-12 |
|
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: 65.02 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 10 LDQFQMDAIEAI---NHGHSVIVSAPTGTGKTMVADYLVEKsIREgQRIIYTAPIKALSNQ---KFKDFsrqFGSKTIGI 83
Cdd:cd17926 1 LRPYQEEALEAWlahKNNRRGILVLPTGSGKTLTALALIAY-LKE-LRTLIVVPTDALLDQwkeRFEDF---LGDSSIGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 84 MTGDVVI-NPGAPLLIMTteifrNQVITNDPE-----LEHVSYIIFDEIHWLNdedrGTVWEESIILAPPNiKILGLSAT 157
Cdd:cd17926 76 IGGGKKKdFDDANVVVAT-----YQSLSNLAEeekdlFDQFGLLIVDEAHHLP----AKTFSEILKELNAK-YRLGLTAT 145
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
12-164 |
1.21e-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: 64.14 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 12 QFQMDAIEAINHGHSVIVSAPTGTGKTMVadYLV---EKSIRE-GQRIIYTAPIKALSN---QKFKDFSRQFGSK-TIGI 83
Cdd:cd17923 3 SHQAEAIEAARAGRSVVVTTGTASGKSLC--YQLpilEALLRDpGSRALYLYPTKALAQdqlRSLRELLEQLGLGiRVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 84 MTGD--------VVINPgAPLLIMTTEIFRNQVITNDPE----LEHVSYIIFDEIHWLndedRGT----VweeSIIL--- 144
Cdd:cd17923 81 YDGDtpreerraIIRNP-PRILLTNPDMLHYALLPHHDRwarfLRNLRYVVLDEAHTY----RGVfgshV---ALLLrrl 152
|
170 180
....*....|....*....|....*.
gi 504855318 145 ------APPNIKILGLSATIANAAEL 164
Cdd:cd17923 153 rrlcrrYGADPQFILTSATIGNPAEH 178
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
15-162 |
1.89e-11 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to 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: 438711 [Multi-domain] Cd Length: 174 Bit Score: 63.12 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 15 MDAI-EAINHGHSVIVSAPTGTGK-TMVADYLVEKSIREGQRIIYTAPIKALSNQKFKDFSRQFGSK---TIGI-MTGDV 88
Cdd:cd17990 7 LPALrAALDAGGQVVLEAPPGAGKtTRVPLALLAELWIAGGKIIVLEPRRVAARAAARRLATLLGEApgeTVGYrVRGES 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504855318 89 VINPGAPLLIMTTEIFRNQvITNDPELEHVSYIIFDEIH--WLN-DEDRGTVWEESIILAPPnIKILGLSATIANAA 162
Cdd:cd17990 87 RVGRRTRVEVVTEGVLLRR-LQRDPELSGVGAVILDEFHerSLDaDLALALLLEVQQLLRDD-LRLLAMSATLDGDG 161
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
27-160 |
1.92e-11 |
|
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: 63.99 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 27 VIVSAPTGTGKTMVADYLVEKSIREGQR-----------IIYTAPIKALSNQKFKDFSRQFGSKTIGI--MTGDVVINpg 93
Cdd:cd18020 20 MLICAPTGAGKTNIAMLTILHEIRQHVNqggvikkddfkIVYIAPMKALAAEMVEKFSKRLAPLGIKVkeLTGDMQLT-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 94 apllimTTEIFRNQVITNDPE---------------LEHVSYIIFDEIHWLNDeDRGTVWE-------ESIILAPPNIKI 151
Cdd:cd18020 98 ------KKEIAETQIIVTTPEkwdvvtrkssgdvalSQLVRLLIIDEVHLLHD-DRGPVIEslvartlRQVESTQSMIRI 170
|
....*....
gi 504855318 152 LGLSATIAN 160
Cdd:cd18020 171 VGLSATLPN 179
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
6-183 |
4.18e-11 |
|
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: 66.42 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 6 QGLKLDQFQMDAIEAINHGHSVIVSAPTGTGKTM------VADYLVEKSIRE-GQRIIYTAPIKALSnqkfKDFSR---- 74
Cdd:TIGR04121 10 RGWTPRPFQLEMWAAALEGRSGLLIAPTGSGKTLagflpsLIDLAGPEAPKEkGLHTLYITPLRALA----VDIARnlqa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 75 ---QFG-SKTIGIMTGDvvinpgapllimTTEIFRNQVITNDPEL---------------------EHVSYIIFDEIHWL 129
Cdd:TIGR04121 86 pieELGlPIRVETRTGD------------TSSSERARQRKKPPDIllttpeslalllsypdaarlfKDLRCVVVDEWHEL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504855318 130 NDEDRGTVWEESII----LApPNIKILGLSATIANAAELKGWIEAIRKDTVVLIEEQQ 183
Cdd:TIGR04121 154 AGSKRGDQLELALArlrrLA-PGLRRWGLSATIGNLEEARRVLLGVGGAPAVLVRGKL 210
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
13-164 |
4.64e-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: 66.40 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 13 FQMDAIEAINHGHSVIVSAPTGTGKTMVadYLV---EKSIREGQ-RIIYTAPIKALSN---QKFKDFSRQFGSK-TIGIM 84
Cdd:COG1205 60 HQAEAIEAARAGKNVVIATPTASGKSLA--YLLpvlEALLEDPGaTALYLYPTKALARdqlRRLRELAEALGLGvRVATY 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 85 TGDVvinPGAplliMTTEIFRNQ--VITNdPE----------------LEHVSYIIFDEIH-----------WLND---- 131
Cdd:COG1205 138 DGDT---PPE----ERRWIREHPdiVLTN-PDmlhygllphhtrwarfFRNLRYVVIDEAHtyrgvfgshvaNVLRrlrr 209
|
170 180 190
....*....|....*....|....*....|....*
gi 504855318 132 --EDRGTvweesiilappNIKILGLSATIANAAEL 164
Cdd:COG1205 210 icRHYGS-----------DPQFILASATIGNPAEH 233
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
8-127 |
5.40e-11 |
|
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: 62.49 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 8 LKLDQFQMDAIEAINHGHSVIVSAPTGTGKTMVADYLVEKSIRE------GQRIIYTAPIKALSNQKFKDFSRQF----- 76
Cdd:cd18036 1 LELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKrrsageKGRVVVLVNKVPLVEQQLEKFFKYFrkgyk 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 77 -----GSKTIGIMTGDVVINpgAPLLIMTTEIFRNQV----ITNDPELEHVSYIIFDEIH 127
Cdd:cd18036 81 vtglsGDSSHKVSFGQIVKA--SDVIICTPQILINNLlsgrEEERVYLSDFSLLIFDECH 138
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
13-157 |
2.09e-09 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain] Cd Length: 163 Bit Score: 57.19 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 13 FQMDAI----EAINHGHS-VIVSAPTGTGKTMVADYLVEKSIREG--QRIIYTAPIKALSNQKFKDFSRQFGSKTIGIMT 85
Cdd:cd18032 4 YQQEAIealeEAREKGQRrALLVMATGTGKTYTAAFLIKRLLEANrkKRILFLAHREELLEQAERSFKEVLPDGSFGNLK 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504855318 86 GDVVINPGAPLLIMTTEIFRNQVITNDPELEHVSYIIFDEIHwlndedRGT--VWEEsiILA--PPNIkILGLSAT 157
Cdd:cd18032 84 GGKKKPDDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAH------HAIasSYRK--ILEyfEPAF-LLGLTAT 150
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
8-157 |
2.86e-09 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 56.53 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 8 LKLDQFQMDAIEAI-----NHGHSVIVSAPTGTGKTMVADYLVEKSIREG--QRIIYTAPIKALSNQKFKDFSRQFGSKT 80
Cdd:pfam04851 2 LELRPYQIEAIENLlesikNGQKRGLIVMATGSGKTLTAAKLIARLFKKGpiKKVLFLVPRKDLLEQALEEFKKFLPNYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 81 --IGIMTGD--VVINPGAPLLIMTTEIFRNQVITNDPEL--EHVSYIIFDEIHWLNDEdrgtVWEEsIILAPPNIKILGL 154
Cdd:pfam04851 82 eiGEIISGDkkDESVDDNKIVVTTIQSLYKALELASLELlpDFFDVIIIDEAHRSGAS----SYRN-ILEYFKPAFLLGL 156
|
...
gi 504855318 155 SAT 157
Cdd:pfam04851 157 TAT 159
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
14-159 |
6.82e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 59.51 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 14 QMDAIEAINHGHSVIVSAPTGTGKTMVA-----DYLVEKSiREGQ-----RIIYTAPIKALSN--------------QKF 69
Cdd:PRK13767 37 QRYAIPLIHEGKNVLISSPTGSGKTLAAflaiiDELFRLG-REGEledkvYCLYVSPLRALNNdihrnleeplteirEIA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 70 KDFSRQFGSKTIGIMTGDV--------VINPgaP-LLIMTTEIFrnQVITNDPE----LEHVSYIIFDEIHWLNDEDRGT 136
Cdd:PRK13767 116 KERGEELPEIRVAIRTGDTssyekqkmLKKP--PhILITTPESL--AILLNSPKfrekLRTVKWVIVDEIHSLAENKRGV 191
|
170 180
....*....|....*....|....*....
gi 504855318 137 ----VWE--ESIILAPPnIKIlGLSATIA 159
Cdd:PRK13767 192 hlslSLErlEELAGGEF-VRI-GLSATIE 218
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
331-387 |
5.08e-08 |
|
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: 52.18 E-value: 5.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 504855318 331 VLYCTETFSVGINYPVKAVCFDSLNKYDGRSFRALANHEFFQMSGRAGRRGID-EIGY 387
Cdd:cd18805 73 VLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMRPLSPSEVKQIAGRAGRFGSHfPEGE 130
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
12-157 |
8.74e-08 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.89 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 12 QFQMDAIEAINHGHSVIVsAPTGTGKTMVA-----DYLVEKsireGQRIIYTAPIKALSNQKFKDFSR--QFGSKTIGIM 84
Cdd:COG1111 6 LYQLNLAASALRKNTLVV-LPTGLGKTAVAllviaERLHKK----GGKVLFLAPTKPLVEQHAEFFKEalNIPEDEIVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 85 TGDVVINPGAPL------LIMTTEIFRNQVITNDPELEHVSYIIFDEIHwlndedRGT-------VWEESIILApPNIKI 151
Cdd:COG1111 81 TGEVSPEKRKELwekariIVATPQVIENDLIAGRIDLDDVSLLIFDEAH------RAVgnyayvyIAERYHEDA-KDPLI 153
|
....*.
gi 504855318 152 LGLSAT 157
Cdd:COG1111 154 LGMTAS 159
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
25-161 |
1.18e-07 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain] Cd Length: 200 Bit Score: 52.65 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 25 HSVIVSAPTGTGKTMVA-------DYLVEKSIREGQRIIYTAPIKALSNQKFKDFSRQFGSKTiGIMTGDVVINPGAPL- 96
Cdd:cd18034 17 RNTIVVLPTGSGKTLIAvmlikemGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHTDLKV-GEYSGEMGVDKWTKEr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 97 ----------LIMTTEIFRNQVITNDPELEHVSYIIFDEIH--------------WLNDEDRGTVweesiilaPpniKIL 152
Cdd:cd18034 96 wkeelekydvLVMTAQILLDALRHGFLSLSDINLLIFDECHhatgdhpyarimkeFYHLEGRTSR--------P---RIL 164
|
....*....
gi 504855318 153 GLSATIANA 161
Cdd:cd18034 165 GLTASPVNG 173
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
296-381 |
2.19e-07 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 48.75 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 296 KLFRVCRKGIAYHHAGLLPLQKSVVEDLFLAKTISVLYCTETFSVGINYP-VKAVCFdslnkYDGRSFRALANheffQMS 374
Cdd:smart00490 5 ELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVII-----YDLPWSPASYI----QRI 75
|
....*..
gi 504855318 375 GRAGRRG 381
Cdd:smart00490 76 GRAGRAG 82
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
27-127 |
3.80e-07 |
|
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to 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: 438707 [Multi-domain] Cd Length: 159 Bit Score: 50.54 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 27 VIVSAPTGTGK-TMVADYLVEKSIREGQ--RIIYTAP--IKALSNQKFkdFSRQFGSK---TIGIMT-GDVVINPGAPLL 97
Cdd:cd17917 4 VVIVGETGSGKtTQVPQFLLEDGLAKGGkgRIVCTQPrrIAAISVAER--VAEERGEKlgeEVGYQIrFESKTSSKTRIK 81
|
90 100 110
....*....|....*....|....*....|
gi 504855318 98 IMTTEIFRnQVITNDPELEHVSYIIFDEIH 127
Cdd:cd17917 82 FCTDGILL-RELLSDPLLSGYSHVILDEAH 110
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
14-125 |
4.37e-07 |
|
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: 51.05 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 14 QMDAIEAINHGHSVIVSAPTGTGKTM-----VADYLVEKSIREGQRIIYTAPIKALSNQ---KFKDFSRQFGSKTIGIMT 85
Cdd:cd17957 17 QMQAIPILLHGRDLLACAPTGSGKTLaflipILQKLGKPRKKKGLRALILAPTRELASQiyrELLKLSKGTGLRIVLLSK 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 504855318 86 GDVVINPGAPLLIMTTEIFRN------QVITNDPE-LEHVSYIIFDE 125
Cdd:cd17957 97 SLEAKAKDGPKSITKYDILVStplrlvFLLKQGPIdLSSVEYLVLDE 143
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
29-177 |
5.69e-07 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 53.39 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 29 VSAPTGTGKTMVA-DYLVEKSIREG------------QRIIYTAPIKALSN----------QKFKDFSRQFGSK----TI 81
Cdd:PRK09751 1 VIAPTGSGKTLAAfLYALDRLFREGgedtreahkrktSRILYISPIKALGTdvqrnlqiplKGIADERRRRGETevnlRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 82 GIMTGD--------VVINPgAPLLIMTTEIFRNQVITNDPE-LEHVSYIIFDEIHWLNDEDRGTVWEESI----ILAPPN 148
Cdd:PRK09751 81 GIRTGDtpaqerskLTRNP-PDILITTPESLYLMLTSRAREtLRGVETVIIDEVHAVAGSKRGAHLALSLerldALLHTS 159
|
170 180
....*....|....*....|....*....
gi 504855318 149 IKILGLSATIANAAELKGWIEAIRKDTVV 177
Cdd:PRK09751 160 AQRIGLSATVRSASDVAAFLGGDRPVTVV 188
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
16-192 |
1.62e-06 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 51.85 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 16 DAIEAINHGHSVIVSAPTGTGK-TMVADYLVEKSIREGqRIIYTAPIK-ALSNQKFKdFSRQFGSK---TIGI-MTGDVV 89
Cdd:PRK11664 12 ELLTALKTAPQVLLKAPTGAGKsTWLPLQLLQHGGING-KIIMLEPRRlAARNVAQR-LAEQLGEKpgeTVGYrMRAESK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 90 INPGAPLLIMTTEIFrNQVITNDPELEHVSYIIFDEIHwlndedrgtvwEESI----ILA---------PPNIKILGLSA 156
Cdd:PRK11664 90 VGPNTRLEVVTEGIL-TRMIQRDPELSGVGLVILDEFH-----------ERSLqadlALAllldvqqglRDDLKLLIMSA 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 504855318 157 TIANAAeLKGWI-EAIrkdtvvLIEEQQRIVPLEYYY 192
Cdd:PRK11664 158 TLDNDR-LQQLLpDAP------VIVSEGRSFPVERRY 187
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
8-127 |
1.78e-06 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain] Cd Length: 202 Bit Score: 49.43 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 8 LKLDQFQMDAIEAINHGHSVIVSAPTGTGKTMVADYLVE---KSIREGQ--RIIYTAPIKALSNQKFKDFSRQFGSKTIG 82
Cdd:cd18073 1 FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEhhlKKFPQGQkgKVVFFATKVPVYEQQKSVFSKYFERHGYR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 504855318 83 I--MTGDVVINPGAPLLIMTTEI--FRNQVITND------PELEHVSYIIFDEIH 127
Cdd:cd18073 81 VtgISGATAENVPVEQIIENNDIiiLTPQILVNNlkkgtiPSLSIFTLMIFDECH 135
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
299-381 |
1.99e-06 |
|
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: 47.59 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 299 RVCRKGI--AYHHAGLLPLQKSVVEDLFLAKTISVLYCTETFSVGINYP-VKAVCFDSLNKydgrSFRAlanheFFQMSG 375
Cdd:cd18794 49 RLQSKGIsaAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPdVRFVIHYSLPK----SMES-----YYQESG 119
|
....*.
gi 504855318 376 RAGRRG 381
Cdd:cd18794 120 RAGRDG 125
|
|
| DEXHc_RLR-3 |
cd18075 |
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ... |
8-171 |
2.24e-06 |
|
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 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: 350833 [Multi-domain] Cd Length: 200 Bit Score: 49.09 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 8 LKLDQFQMDAIEAINHGHSVIVSAPTGTGKTMVADYLVEKSI--REGQRIIYTAPIKALSNQKF-KDFSRQFGSKTIGIM 84
Cdd:cd18075 1 MELHGYQWEVVAPALRGKNSIIWLPTGAGKTRAAVYVARRHLetKRGAKVAVLVNKVHLVDQHLeKEFHVLLDKYTVTAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 85 TGDVV-------INPGAPLLIMTTEIFRNqVITNDPELEHV-----SYIIFDEIHWLNDEdrgTVW--------EESIIL 144
Cdd:cd18075 81 SGDSShkcffgqLARGSDVVICTAQILQN-ALLSGEEEAHVeltdfSLLVIDECHHTHKE---AVYnkimlsylEKKLSR 156
|
170 180
....*....|....*....|....*....
gi 504855318 145 APPNIKILGLSAT--IANAAELKGWIEAI 171
Cdd:cd18075 157 QGDLPQILGLTASpgTGGATSFDGAVEHI 185
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
16-193 |
4.50e-06 |
|
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273901 [Multi-domain] Cd Length: 819 Bit Score: 50.15 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 16 DAIEAINhghSVIVSAPTGTGKTMVADYLVEKSIREGQRIIYTAPIKALSNQKFKDFSRQFGSK---TIGI-MTGDVVIN 91
Cdd:TIGR01970 12 DALAAHP---QVVLEAPPGAGKSTAVPLALLDAPGIGGKIIMLEPRRLAARSAAQRLASQLGEAvgqTVGYrVRGENKVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 92 PGAPLLIMTTEIFrNQVITNDPELEHVSYIIFDEIHwlndeDRGTVWEESIILA-------PPNIKILGLSATIANAAel 164
Cdd:TIGR01970 89 RRTRLEVVTEGIL-TRMIQDDPELDGVGALIFDEFH-----ERSLDADLGLALAldvqsslREDLKILAMSATLDGER-- 160
|
170 180
....*....|....*....|....*....
gi 504855318 165 kgwIEAIRKDTVVLiEEQQRIVPLEYYYF 193
Cdd:TIGR01970 161 ---LSSLLPDAPVV-ESEGRSFPVEIRYL 185
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
1-158 |
8.28e-06 |
|
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to 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: 350730 [Multi-domain] Cd Length: 234 Bit Score: 47.91 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 1 MISEYQGLKLDQFQMDAIEAINHGHSVIVSAPTGTGK-TMVADYLVEKSIREGQ----RIIYTAP--IKALSNQKFKDFS 73
Cdd:cd17972 52 ILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKtTQVPQYILDDFIQNDRaaecNIVVTQPrrISAVSVAERVAFE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 74 R--QFGsKTIG--IMTGDVVINPGAPLLIMTTEIFRNQVitnDPELEHVSYIIFDEIHWLN-DEDRGTVWEESIILAPPN 148
Cdd:cd17972 132 RgeEVG-KSCGysVRFESVLPRPHASILFCTVGVLLRKL---EAGIRGISHVIVDEIHERDiNTDFLLVVLRDVVQAYPD 207
|
170
....*....|
gi 504855318 149 IKILGLSATI 158
Cdd:cd17972 208 LRVILMSATI 217
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
13-127 |
1.81e-05 |
|
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: 45.97 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 13 FQMDAIEAINHGHSVIVsAPTGTGKT----MVADYLVEKsirEGQRIIYTAPIKALSNQKFKDFSRQFGSK-TIGIMTGD 87
Cdd:cd18035 6 YQVLIAAVALNGNTLIV-LPTGLGKTiiaiLVAADRLTK---KGGKVLILAPSRPLVEQHAENLKRVLNIPdKITSLTGE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 504855318 88 VV------INPGAPLLIMTTEIFRNQVITNDPELEHVSYIIFDEIH 127
Cdd:cd18035 82 VKpeeraeRWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAH 127
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
14-158 |
2.33e-05 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 45.90 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 14 QMDAIEAINHGHSVIVSAPTGTGKTM-----VADYLVEKSIREGQ--RIIYTAPIKALSNQ---KFKDFSRQFGSKTIGI 83
Cdd:cd00268 17 QAQAIPLILSGRDVIGQAQTGSGKTLafllpILEKLLPEPKKKGRgpQALVLAPTRELAMQiaeVARKLGKGTGLKVAAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 84 MTG--------------DVVI-NPGaPLLimttEIFRNQVITndpeLEHVSYIIFDEIhwlnDE--DRGtvWEESI--IL 144
Cdd:cd00268 97 YGGapikkqiealkkgpDIVVgTPG-RLL----DLIERGKLD----LSNVKYLVLDEA----DRmlDMG--FEEDVekIL 161
|
170
....*....|....*.
gi 504855318 145 A--PPNIKILGLSATI 158
Cdd:cd00268 162 SalPKDRQTLLFSATL 177
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
27-160 |
2.74e-05 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 47.06 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 27 VIVSAPTGTGKTMVADYLVEKSI--REGQRIIYTAPIKALSNQKFKDFSRQFGSKTIGIMTGDVVIN----PGAPLLImt 100
Cdd:TIGR01587 2 LVIEAPTGYGKTEAALLWALHSIksQKADRVIIALPTRATINAMYRRAKELFGSELVGLHHSSSFSRikemGDSEEFE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 101 tEIFRNQVITND--------------------PELEH---------VSYIIFDEIHWLNDEDRGTVWEESIILAPPNIKI 151
Cdd:TIGR01587 80 -HLFPLYIHSNDklfldpitvctidqvlksvfGEFGHyeftlasiaNSLLIFDEVHFYDEYTLALILAVLEVLKDNDVPI 158
|
....*....
gi 504855318 152 LGLSATIAN 160
Cdd:TIGR01587 159 LLMSATLPK 167
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
27-157 |
4.24e-05 |
|
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: 44.97 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 27 VIVSAPTGTGKT----MVADYLVEKSIRegQRIIYTAPIKALSNQKF----KDFSRQFGSKTIGIMTGDVVINPGA---- 94
Cdd:cd17930 4 VILEAPTGSGKTeaalLWALKLAARGGK--RRIIYALPTRATINQMYerirEILGRLDDEDKVLLLHSKAALELLEsdee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 95 --PLLIMTTEIFRNQ---------VITNDPELEHV---------------SYIIFDEIHWLNDEdrgtVWEESI-----I 143
Cdd:cd17930 82 pdDDPVEAVDWALLLkrswlapivVTTIDQLLESLlkykhferrlhglanSVVVLDEVQAYDPE----YMALLLkalleL 157
|
170
....*....|....
gi 504855318 144 LAPPNIKILGLSAT 157
Cdd:cd17930 158 LGELGGPVVLMTAT 171
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
12-67 |
5.14e-05 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 46.84 E-value: 5.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504855318 12 QFQM-DAI-EAINHGHSVIVSAPTGTGKTMVadYLV---EKSIREGQRIIYTAPIKALSNQ 67
Cdd:COG1199 19 QREMaEAVaRALAEGRHLLIEAGTGTGKTLA--YLVpalLAARETGKKVVISTATKALQEQ 77
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
24-127 |
1.26e-04 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 45.63 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 24 GHSVIVsAPTGTGKT----MVADYLVEKsirEGQRIIYTAPIKALSNQKFKDFSRQFGSKTIGIM--TGDvvINPG---- 93
Cdd:PRK13766 30 KNTLVV-LPTGLGKTaialLVIAERLHK---KGGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVvfTGE--VSPEkrae 103
|
90 100 110
....*....|....*....|....*....|....*...
gi 504855318 94 ----APLLIMTTEIFRNQVITNDPELEHVSYIIFDEIH 127
Cdd:PRK13766 104 lwekAKVIVATPQVIENDLIAGRISLEDVSLLIFDEAH 141
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
11-127 |
1.92e-04 |
|
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: 44.69 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 11 DQFQMDAIEAINHGHS-VIVSAPTGTGKTMVADYLVEKSIRE--GQRIIYTAPIKALSNQKFKDFsRQFGSKTIGIMTGD 87
Cdd:COG1203 133 NEALELALEAAEEEPGlFILTAPTGGGKTEAALLFALRLAAKhgGRRIIYALPFTSIINQTYDRL-RDLFGEDVLLHHSL 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504855318 88 VVINP---------GAPLLIMTTEIFRNQVI--TNDPELEHV----------------SYIIFDEIH 127
Cdd:COG1203 212 ADLDLleeeeeyesEARWLKLLKELWDAPVVvtTIDQLFESLfsnrkgqerrlhnlanSVIILDEVQ 278
|
|
| DEXDc_ComFA |
cd17925 |
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ... |
17-101 |
2.58e-04 |
|
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon protein 1) is part of the complex mediating the binding and uptake of single-stranded DNA. ComFA is required for DNA uptake but not for binding. It 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: 350683 [Multi-domain] Cd Length: 143 Bit Score: 41.90 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 17 AIEAINHGHSVIVSAPTGTGKTMVADYLVEKSIREGQRIIYTAPIKALSNQKFKDFSRQFGSKTIGIMTGDVVINPG-AP 95
Cdd:cd17925 9 LVETIDAKEDLLVWAVTGAGKTEMLFPAIAQALRQGGRVAIASPRIDVCLELAPRLKAAFPGAAIVLLHGGSEDQYQrSP 88
|
....*.
gi 504855318 96 LLIMTT 101
Cdd:cd17925 89 LVIATT 94
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
14-60 |
3.34e-04 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain] Cd Length: 155 Bit Score: 41.77 E-value: 3.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 504855318 14 QMDAIEAINHGHSVIVSAPTGTGKTMVADYLVEKSIREGQRIIYTAP 60
Cdd:cd17933 2 QKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAP 48
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
14-161 |
4.10e-04 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 42.29 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 14 QMDAIEAINHGHSVIVSAPTGTGKTmvADYLV---EK----SIREGQRIIYTAPIKALSNQKF---KDFSRQFGSKTIGI 83
Cdd:cd17959 28 QRKTIPLILDGRDVVAMARTGSGKT--AAFLIpmiEKlkahSPTVGARALILSPTRELALQTLkvtKELGKFTDLRTALL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 84 MTGD--------VVINPGapLLIMTTEIFRNQVITNDPELEHVSYIIFDEIHWLNDEDRGTVWEESIILAPPNIKILGLS 155
Cdd:cd17959 106 VGGDsleeqfeaLASNPD--IIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAEQLHEILSRLPENRQTLLFS 183
|
....*.
gi 504855318 156 ATIANA 161
Cdd:cd17959 184 ATLPKL 189
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
14-163 |
1.16e-03 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 42.08 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 14 QMDAIEAINHGHSVIVSAPTGTGKTmvADYLV------------EKSIREGQRIIYTAPIKALSNQ---KFKDFSRQFGS 78
Cdd:PLN00206 148 QMQAIPAALSGRSLLVSADTGSGKT--ASFLVpiisrcctirsgHPSEQRNPLAMVLTPTRELCVQvedQAKVLGKGLPF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 79 KTIGIMTGDVV------INPGAPLLIMTTEIFRNQVITNDPELEHVSYIIFDEIHWLNDED-RGTVWEesIILAPPNIKI 151
Cdd:PLN00206 226 KTALVVGGDAMpqqlyrIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGfRDQVMQ--IFQALSQPQV 303
|
170
....*....|..
gi 504855318 152 LGLSATIANAAE 163
Cdd:PLN00206 304 LLFSATVSPEVE 315
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
14-84 |
1.21e-03 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350687 [Multi-domain] Cd Length: 178 Bit Score: 40.65 E-value: 1.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504855318 14 QMDAIEAINHG----HSVIVSAPTGTGKTMVADYLVEKSIREGQRIIYTAPIKALSNQKFKDFSRQFGSKtIGIM 84
Cdd:cd17929 1 QRKAYEAIVSSlggfKTFLLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTPQLIKRFKKRFGDK-VAVL 74
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
14-131 |
2.00e-03 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 40.22 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 14 QMDAIEAINHGHSVIVSAPTGTGKTM-VADYLVEKSIREGQ--------RIIYTAPIKALSNQKFKDFSRQFGSKTIGIM 84
Cdd:cd17944 17 QVKTFHPVYSGKDLIAQARTGTGKTFsFAIPLIEKLQEDQQprkrgrapKVLVLAPTRELANQVTKDFKDITRKLSVACF 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504855318 85 TGDVVINP-------GAPLLIMTTEIFRNQVITNDPELEHVSYIIFDEIHWLND 131
Cdd:cd17944 97 YGGTPYQQqifairnGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLD 150
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
25-157 |
2.12e-03 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 40.00 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 25 HSVIVSAPTGTGKTMVADYLVEKSIR---EGqRIIYTAPIKALSNQKFKDFSRQFG--SKTIGIMTGDVVINPGAPL--- 96
Cdd:cd18033 17 QNTLVALPTGLGKTFIAAVVMLNYYRwfpKG-KIVFMAPTKPLVSQQIEACYKITGipSSQTAELTGSVPPTKRAELwas 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 97 ---LIMTTEIFRNQVITNDPELEHVSYIIFDEIHwlndedRGT------VWEESIILAPPNIKILGLSAT 157
Cdd:cd18033 96 krvFFLTPQTLENDLKEGDCDPKSIVCLVIDEAH------RATgnyaycQVVRELMRYNSHFRILALTAT 159
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
24-59 |
2.41e-03 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 41.02 E-value: 2.41e-03
10 20 30
....*....|....*....|....*....|....*.
gi 504855318 24 GHSVIVSAPTGTGKTMVADYLVEKSIREGQRIIYTA 59
Cdd:PRK09302 273 GSIILVSGATGTGKTLLASKFAEAACRRGERCLLFA 308
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
6-60 |
2.89e-03 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 40.73 E-value: 2.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 504855318 6 QGLKLDQFQMDAIEAINHGHSV-IVSAPTGTGKTMVADYLVEKSIREGQRIIYTAP 60
Cdd:COG0507 121 AGITLSDEQREAVALALTTRRVsVLTGGAGTGKTTTLRALLAALEALGLRVALAAP 176
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
16-134 |
4.03e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 38.64 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 16 DAIEAINHG--HSVIVSAPTGTGKTMVADYLVEKSIREGqriIYTAPIKALSNQKFKDFSRQFGSKTI------------ 81
Cdd:pfam13191 14 DALDRVRSGrpPSVLLTGEAGTGKTTLLRELLRALERDG---GYFLRGKCDENLPYSPLLEALTREGLlrqlldelessl 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 504855318 82 ---GIMTGDVVINPGAPLLIMTTEIFRN---QVITNDPELEHVSYIIFDEIHWLNDEDR 134
Cdd:pfam13191 91 leaWRAALLEALAPVPELPGDLAERLLDlllRLLDLLARGERPLVLVLDDLQWADEASL 149
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
302-382 |
4.04e-03 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129701 [Multi-domain] Cd Length: 470 Bit Score: 40.52 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 302 RKGIA--YHHAGLLPLQKSVVEDLFLAKTISVLYCTETFSVGINYP-VKAVCFDSLNKydgrsfralaNHE-FFQMSGRA 377
Cdd:TIGR00614 248 KLGLAagAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPdVRFVIHYSLPK----------SMEsYYQESGRA 317
|
....*
gi 504855318 378 GRRGI 382
Cdd:TIGR00614 318 GRDGL 322
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
14-39 |
4.76e-03 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 40.13 E-value: 4.76e-03
10 20
....*....|....*....|....*.
gi 504855318 14 QMDAIEAINHGHSVIVSAPTGTGKTM 39
Cdd:COG0513 29 QAQAIPLILAGRDVLGQAQTGTGKTA 54
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
27-162 |
4.83e-03 |
|
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to 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: 350743 [Multi-domain] Cd Length: 177 Bit Score: 38.67 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 27 VIVSAPTGTGK-TMVADYLVEKSIREGQ----RIIYTAPiKALSNQKFKDFSRQFGSKTIGIMTG-----DVVINPGAPL 96
Cdd:cd17985 20 LVISGMTGCGKtTQIPQFILDNSLQGPPlpvaNIICTQP-RRISAISVAERVAQERAERVGQSVGyqirlESVKSSATRL 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504855318 97 LIMTTEIFRNQvITNDPELEHVSYIIFDEIHWLNDE-DRGTVWEESIILAPPNIKILGLSATIaNAA 162
Cdd:cd17985 99 LYCTTGVLLRR-LEGDPTLQGVTHVIVDEVHERTEEsDFLLLVLKDLMVQRPDLKVILMSATL-NAE 163
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
28-157 |
5.46e-03 |
|
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: 38.55 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504855318 28 IVSAPTGTGKTMVADYLVEKSIREGQRIIYTAPIKALSNQKFKDFSRQFGSKTIGIMTGDVV--INPGAPLLIMTTEIfr 105
Cdd:cd17918 40 LLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARKFLPFINVELVTGGTKaqILSGISLLVGTHAL-- 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 504855318 106 nqvITNDPELEHVSYIIFDEIHWLndedrGTVWEESiILAPPNIKILGLSAT 157
Cdd:cd17918 118 ---LHLDVKFKNLDLVIVDEQHRF-----GVAQREA-LYNLGATHFLEATAT 160
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
9-40 |
8.97e-03 |
|
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: 38.28 E-value: 8.97e-03
10 20 30
....*....|....*....|....*....|....*
gi 504855318 9 KLDQF---QMDAIEAINHGHSVIVSAPTGTGKTMV 40
Cdd:cd17920 9 GYDEFrpgQLEAINAVLAGRDVLVVMPTGGGKSLC 43
|
|
| |
