|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
381-564 |
2.70e-105 |
|
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: 328.79 E-value: 2.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 381 EWQHTCLTLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKISGLSSFGIELGFFVEEYAG 460
Cdd:cd18026 19 DWQKECLSLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRLLERRKKALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 461 SKGRFPPtKRREKKSLYIATIEKGHSLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSK-TTQIIGM 539
Cdd:cd18026 99 NKGRSPP-KRRKSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDGHRGALLELLLTKLLYAAQkNIQIVGM 177
|
170 180
....*....|....*....|....*
gi 119626340 540 SATLNNVEDLQKFLQAEYYTSQFRP 564
Cdd:cd18026 178 SATLPNLEELASWLRAELYTTNFRP 202
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
390-930 |
2.76e-102 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 333.40 E-value: 2.76e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 390 NSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKdVLMILPYVAIVQEKISGLSSFGIELGFfveEYAGSKGRFPPTK 469
Cdd:COG1204 33 AGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK-ALYIVPLRALASEKYREFKRDFEELGI---KVGVSTGDYDSDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 470 RR-EKKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSATLNNVED 548
Cdd:COG1204 109 EWlGRYDILVATPEKLDSLLRN--GPSWLRDVDLVVVDEAHLIDDESRGPTLEVLLARLRRLNPEAQIVALSATIGNAEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 549 LQKFLQAEYYTSQFRPVELKEYLKINDTIYevdskaengmtfsrllnykYSDTLKKMDpDHLVALVTEVIP-NYSCLVFC 627
Cdd:COG1204 187 IAEWLDAELVKSDWRPVPLNEGVLYDGVLR-------------------FDDGSRRSK-DPTLALALDLLEeGGQVLVFV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 628 PSKKNCENVAEMICKFLsKEYLKHKEKEKC-EVIKNLKNIGNGN-LCPVLKRTIPFGVAYHHSGLTSDERKLLEEAYSTG 705
Cdd:COG1204 247 SSRRDAESLAKKLADEL-KRRLTPEEREELeELAEELLEVSEEThTNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 706 VLCLFTCTSTLAAGVNLPARRVILRAPY-VAKEFLKRNQYKQMIGRAGRAGIDTIGESILIlqEKDKQQVLELITKPL-- 782
Cdd:COG1204 326 LIKVLVATPTLAAGVNLPARRVIIRDTKrGGMVPIPVLEFKQMAGRAGRPGYDPYGEAILV--AKSSDEADELFERYIlg 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 783 --ENCYSHLVQEftKGIQTLFLSLIGLKIATNLDDIYHFMNGTFFGVQQkvllKEKSLWEITVESLRYLTEKGLLQKDTI 860
Cdd:COG1204 404 epEPIRSKLANE--SALRTHLLALIASGFANSREELLDFLENTFYAYQY----DKGDLEEVVDDALEFLLENGFIEEDGD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 861 YkseeevqynFHITKLGRASFKGTIDLAYCDILYRDLKKGLEGLVLESLLHLIYLTTpydlvsqcnpDWM 930
Cdd:COG1204 478 R---------LRATKLGKLVSRLYIDPLTAAELVDGLRKADEEFTDLGLLHLILILR----------DWI 528
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
394-1109 |
1.11e-87 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 299.57 E-value: 1.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 394 ERKNLIYSLPTSGGKTLVAEILMLQELLCCRKdVLMILPYVAIVQEK---ISGLSSFGIELGFfveeyagSKGRFpptKR 470
Cdd:PRK02362 38 DGKNLLAAIPTASGKTLIAELAMLKAIARGGK-ALYIVPLRALASEKfeeFERFEELGVRVGI-------STGDY---DS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 471 RE----KKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSATLNNV 546
Cdd:PRK02362 107 RDewlgDNDIIVATSEKVDSLLRN--GAPWLDDITCVVVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQVVALSATIGNA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 547 EDLQKFLQAEYYTSQFRPVELKEYLKINDTIYEVDSKAEngmtfsrllnykysdtLKKMDPDHLVALVTEVI-PNYSCLV 625
Cdd:PRK02362 185 DELADWLDAELVDSEWRPIDLREGVFYGGAIHFDDSQRE----------------VEVPSKDDTLNLVLDTLeEGGQCLV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 626 FCPSKKNCENVAEMICKFLSKEYLKHKEKEKCEVIKNLKNIGNGNLCPVLKRTIPFGVAYHHSGLTSDERKLLEEAYSTG 705
Cdd:PRK02362 249 FVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVSDTETSKDLADCVAKGAAFHHAGLSREHRELVEDAFRDR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 706 VLCLFTCTSTLAAGVNLPARRVILR-----------APYVAKEflkrnqYKQMIGRAGRAGIDTIGESILIlqEKDKQQV 774
Cdd:PRK02362 329 LIKVISSTPTLAAGLNLPARRVIIRdyrrydggagmQPIPVLE------YHQMAGRAGRPGLDPYGEAVLL--AKSYDEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 775 LEL----ITKPLENCYSHLVQEftKGIQTLFLSLIGLKIATNLDDIYHFMNGTFFGVQQKvllKEKSLWEITVESLRYLT 850
Cdd:PRK02362 401 DELferyIWADPEDVRSKLATE--PALRTHVLSTIASGFARTRDGLLEFLEATFYATQTD---DTGRLERVVDDVLDFLE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 851 EKGLLQKDtiyksEEEVqynfHITKLGRasfkgTIDLAYCDILY-RDLKKGLEGLVLES---LLHLIYLTtpydlvsqcn 926
Cdd:PRK02362 476 RNGMIEED-----GETL----EATELGH-----LVSRLYIDPLSaAEIIDGLEAAKKPTdlgLLHLVCST---------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 927 PD-WMIYFRqfsqlSPAEQNVAAILGVSES-FIGKKASgqaigkkVDKNVVNRLYLSFVLYTLLKETNIWTVSE-----K 999
Cdd:PRK02362 532 PDmYELYLR-----SGDYEWLNEYLYEHEDeLLGDVPS-------EFEDDEFEDFLSAVKTALLLEDWIDEVDEeriteR 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 1000 FNMPRGYIQN-------LLTGTASFSScvlhfceELEEFWVYRAllVELTKKLTYCVKAELIPLMEVTGVLEGRAKQLYS 1072
Cdd:PRK02362 600 YGVGPGDIRGkvetaewLLHAAERLAS-------ELDLDLARAA--RELEKRVEYGVREELLDLVGLRGVGRVRARRLYN 670
|
730 740 750
....*....|....*....|....*....|....*..
gi 119626340 1073 AGYKSLMHLANANPEVLVRTidhLSRRQAKQIVSSAK 1109
Cdd:PRK02362 671 AGIESRADLRAADKSVVLAI---LGEKIAENILEQAG 704
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
563-765 |
1.52e-42 |
|
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: 152.32 E-value: 1.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 563 RPVELKEYLKIndtiyevdskaengmtFSRLLNYKYSDTLKKMDPDHLVALVTEVIPNY-SCLVFCPSKKNCENVAEMIc 641
Cdd:cd18795 1 RPVPLEEYVLG----------------FNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGkPVLVFCSSRKECEKTAKDL- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 642 kflskeylkhkekekceviknlknigngnlcpvlkrtipFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVN 721
Cdd:cd18795 64 ---------------------------------------AGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVN 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 119626340 722 LPARRVILRAPYVAK----EFLKRNQYKQMIGRAGRAGIDTIGESILI 765
Cdd:cd18795 105 LPARTVIIKGTQRYDgkgyRELSPLEYLQMIGRAGRPGFDTRGEAIIM 152
|
|
| HTH_61 |
pfam20470 |
Helix-turn-helix domain; This entry represents a presumed helix-turn-helix domain found in DNA ... |
760-856 |
3.23e-30 |
|
Helix-turn-helix domain; This entry represents a presumed helix-turn-helix domain found in DNA polymerase theta.
Pssm-ID: 466619 [Multi-domain] Cd Length: 92 Bit Score: 114.95 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 760 GESILILQEKDKQQVLELITKPLENCYSHLVQEfTKGIQTLFLSLIGLKIATNLDDIYHFMNGTFFGVQQKVLLKEKSlw 839
Cdd:pfam20470 1 GESILICKEKDLEKVAELLRAELPPVYSCLLPE-KRGIKRALLEIIALGLATSPEDVDEYMSCTLLSVQQKELDVEKS-- 77
|
90
....*....|....*..
gi 119626340 840 eiTVESLRYLTEKGLLQ 856
Cdd:pfam20470 78 --IESSLEELVENGLIT 92
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
394-771 |
1.29e-22 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 104.59 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 394 ERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIV-------QEKISGLSSFGIELGffVEEYAGSKGRFP 466
Cdd:COG1202 224 EGKDQLVVSATATGKTLIGELAGIKNALEGKGKMLFLVPLVALAnqkyedfKDRYGDGLDVSIRVG--ASRIRDDGTRFD 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 467 PtkrreKKSLYIATIEkGhslVNSLIETGR-IDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSATLNN 545
Cdd:COG1202 302 P-----NADIIVGTYE-G---IDHALRTGRdLGDIGTVVIDEVHMLEDPERGHRLDGLIARLKYYCPGAQWIYLSATVGN 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 546 VEDLQKFLQAEYYTSQFRPVELKEYLkindtiyevdskaengmTFSRllNYKYSDTLKKmdpdhlvaLVTEVIPNYS--- 622
Cdd:COG1202 373 PEELAKKLGAKLVEYEERPVPLERHL-----------------TFAD--GREKIRIINK--------LVKREFDTKSskg 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 623 ----CLVFCPSKKNCENVAemickflskeylkhkekekceviknlknigngnlcpvlkRTIPFGVAYHHSGLTSDERKLL 698
Cdd:COG1202 426 yrgqTIIFTNSRRRCHEIA---------------------------------------RALGYKAAPYHAGLDYGERKKV 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119626340 699 EEAYSTGVLCLFTCTSTLAAGVNLPARRVILRAPYVAKEFLKRNQYKQMIGRAGRAGIDTIGEsILILQEKDK 771
Cdd:COG1202 467 ERRFADQELAAVVTTAALAAGVDFPASQVIFDSLAMGIEWLSVQEFHQMLGRAGRPDYHDRGK-VYLLVEPGK 538
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
388-549 |
2.54e-19 |
|
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: 86.14 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 388 TLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKD--VLMILPYVAIVQEKISGLSSFGIELGFFVE-EYAGSkgr 464
Cdd:pfam00270 7 AIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGpqALVLAPTRELAEQIYEELKKLGKGLGLKVAsLLGGD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 465 fPPTKRREKKS---LYIATIEKghsLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKIlytSKTTQIIGMSA 541
Cdd:pfam00270 84 -SRKEQLEKLKgpdILVGTPGR---LLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL---PKKRQILLLSA 156
|
....*....
gi 119626340 542 TLN-NVEDL 549
Cdd:pfam00270 157 TLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
392-560 |
1.27e-12 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 67.90 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 392 VQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKD-VLMILPYVAIVQEKISGLSSFGIELGFFVEEYAG--SKGRFPPT 468
Cdd:smart00487 21 LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGrVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGgdSKREQLRK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 469 KRREKKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKIlytSKTTQIIGMSATLNN--V 546
Cdd:smart00487 101 LESGKTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL---PKNVQLLLLSATPPEeiE 175
|
170
....*....|....
gi 119626340 547 EDLQKFLQAEYYTS 560
Cdd:smart00487 176 NLLELFLNDPVFID 189
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
677-755 |
1.42e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.16 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 677 RTIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLP-ARRVILRAPYVAKEflkrnQYKQMIGRAGRAG 755
Cdd:smart00490 8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDLPWSPA-----SYIQRIGRAGRAG 82
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
1056-1109 |
3.52e-03 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 3.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 119626340 1056 LMEVTGVLEGRAKQLYSAGYKSLMHLANANPEVLVRTIDhLSRRQAKQIVSSAK 1109
Cdd:pfam14520 4 LLSISGIGPKTALALLSAGIGTVEDLAEADVDELAEIPG-IGEKTAQRIILELR 56
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
503-567 |
8.89e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 40.25 E-value: 8.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119626340 503 VVVDELHMIGEGSRGATLEMTLAKILY-TSKTTQIIGMSATLNNVEDLQKFLQAEYYTSQFRPVEL 567
Cdd:PRK13767 176 VIVDEIHSLAENKRGVHLSLSLERLEElAGGEFVRIGLSATIEPLEEVAKFLVGYEDDGEPRDCEI 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
381-564 |
2.70e-105 |
|
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: 328.79 E-value: 2.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 381 EWQHTCLTLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKISGLSSFGIELGFFVEEYAG 460
Cdd:cd18026 19 DWQKECLSLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRLLERRKKALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 461 SKGRFPPtKRREKKSLYIATIEKGHSLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSK-TTQIIGM 539
Cdd:cd18026 99 NKGRSPP-KRRKSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDGHRGALLELLLTKLLYAAQkNIQIVGM 177
|
170 180
....*....|....*....|....*
gi 119626340 540 SATLNNVEDLQKFLQAEYYTSQFRP 564
Cdd:cd18026 178 SATLPNLEELASWLRAELYTTNFRP 202
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
390-930 |
2.76e-102 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 333.40 E-value: 2.76e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 390 NSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKdVLMILPYVAIVQEKISGLSSFGIELGFfveEYAGSKGRFPPTK 469
Cdd:COG1204 33 AGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK-ALYIVPLRALASEKYREFKRDFEELGI---KVGVSTGDYDSDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 470 RR-EKKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSATLNNVED 548
Cdd:COG1204 109 EWlGRYDILVATPEKLDSLLRN--GPSWLRDVDLVVVDEAHLIDDESRGPTLEVLLARLRRLNPEAQIVALSATIGNAEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 549 LQKFLQAEYYTSQFRPVELKEYLKINDTIYevdskaengmtfsrllnykYSDTLKKMDpDHLVALVTEVIP-NYSCLVFC 627
Cdd:COG1204 187 IAEWLDAELVKSDWRPVPLNEGVLYDGVLR-------------------FDDGSRRSK-DPTLALALDLLEeGGQVLVFV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 628 PSKKNCENVAEMICKFLsKEYLKHKEKEKC-EVIKNLKNIGNGN-LCPVLKRTIPFGVAYHHSGLTSDERKLLEEAYSTG 705
Cdd:COG1204 247 SSRRDAESLAKKLADEL-KRRLTPEEREELeELAEELLEVSEEThTNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 706 VLCLFTCTSTLAAGVNLPARRVILRAPY-VAKEFLKRNQYKQMIGRAGRAGIDTIGESILIlqEKDKQQVLELITKPL-- 782
Cdd:COG1204 326 LIKVLVATPTLAAGVNLPARRVIIRDTKrGGMVPIPVLEFKQMAGRAGRPGYDPYGEAILV--AKSSDEADELFERYIlg 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 783 --ENCYSHLVQEftKGIQTLFLSLIGLKIATNLDDIYHFMNGTFFGVQQkvllKEKSLWEITVESLRYLTEKGLLQKDTI 860
Cdd:COG1204 404 epEPIRSKLANE--SALRTHLLALIASGFANSREELLDFLENTFYAYQY----DKGDLEEVVDDALEFLLENGFIEEDGD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 861 YkseeevqynFHITKLGRASFKGTIDLAYCDILYRDLKKGLEGLVLESLLHLIYLTTpydlvsqcnpDWM 930
Cdd:COG1204 478 R---------LRATKLGKLVSRLYIDPLTAAELVDGLRKADEEFTDLGLLHLILILR----------DWI 528
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
394-1109 |
1.11e-87 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 299.57 E-value: 1.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 394 ERKNLIYSLPTSGGKTLVAEILMLQELLCCRKdVLMILPYVAIVQEK---ISGLSSFGIELGFfveeyagSKGRFpptKR 470
Cdd:PRK02362 38 DGKNLLAAIPTASGKTLIAELAMLKAIARGGK-ALYIVPLRALASEKfeeFERFEELGVRVGI-------STGDY---DS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 471 RE----KKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSATLNNV 546
Cdd:PRK02362 107 RDewlgDNDIIVATSEKVDSLLRN--GAPWLDDITCVVVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQVVALSATIGNA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 547 EDLQKFLQAEYYTSQFRPVELKEYLKINDTIYEVDSKAEngmtfsrllnykysdtLKKMDPDHLVALVTEVI-PNYSCLV 625
Cdd:PRK02362 185 DELADWLDAELVDSEWRPIDLREGVFYGGAIHFDDSQRE----------------VEVPSKDDTLNLVLDTLeEGGQCLV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 626 FCPSKKNCENVAEMICKFLSKEYLKHKEKEKCEVIKNLKNIGNGNLCPVLKRTIPFGVAYHHSGLTSDERKLLEEAYSTG 705
Cdd:PRK02362 249 FVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVSDTETSKDLADCVAKGAAFHHAGLSREHRELVEDAFRDR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 706 VLCLFTCTSTLAAGVNLPARRVILR-----------APYVAKEflkrnqYKQMIGRAGRAGIDTIGESILIlqEKDKQQV 774
Cdd:PRK02362 329 LIKVISSTPTLAAGLNLPARRVIIRdyrrydggagmQPIPVLE------YHQMAGRAGRPGLDPYGEAVLL--AKSYDEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 775 LEL----ITKPLENCYSHLVQEftKGIQTLFLSLIGLKIATNLDDIYHFMNGTFFGVQQKvllKEKSLWEITVESLRYLT 850
Cdd:PRK02362 401 DELferyIWADPEDVRSKLATE--PALRTHVLSTIASGFARTRDGLLEFLEATFYATQTD---DTGRLERVVDDVLDFLE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 851 EKGLLQKDtiyksEEEVqynfHITKLGRasfkgTIDLAYCDILY-RDLKKGLEGLVLES---LLHLIYLTtpydlvsqcn 926
Cdd:PRK02362 476 RNGMIEED-----GETL----EATELGH-----LVSRLYIDPLSaAEIIDGLEAAKKPTdlgLLHLVCST---------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 927 PD-WMIYFRqfsqlSPAEQNVAAILGVSES-FIGKKASgqaigkkVDKNVVNRLYLSFVLYTLLKETNIWTVSE-----K 999
Cdd:PRK02362 532 PDmYELYLR-----SGDYEWLNEYLYEHEDeLLGDVPS-------EFEDDEFEDFLSAVKTALLLEDWIDEVDEeriteR 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 1000 FNMPRGYIQN-------LLTGTASFSScvlhfceELEEFWVYRAllVELTKKLTYCVKAELIPLMEVTGVLEGRAKQLYS 1072
Cdd:PRK02362 600 YGVGPGDIRGkvetaewLLHAAERLAS-------ELDLDLARAA--RELEKRVEYGVREELLDLVGLRGVGRVRARRLYN 670
|
730 740 750
....*....|....*....|....*....|....*..
gi 119626340 1073 AGYKSLMHLANANPEVLVRTidhLSRRQAKQIVSSAK 1109
Cdd:PRK02362 671 AGIESRADLRAADKSVVLAI---LGEKIAENILEQAG 704
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
392-1091 |
2.45e-58 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 215.07 E-value: 2.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 392 VQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKISGLSSFGiELGFFVeeyAGSKGRFPPTKR- 470
Cdd:PRK00254 36 VLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGGKAVYLVPLKALAEEKYREFKDWE-KLGLRV---AMTTGDYDSTDEw 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 471 REKKSLYIATIEKghslVNSLIETGR--IDSLGLVVVDELHMIGEGSRGATLEMTLAKILytsKTTQIIGMSATLNNVED 548
Cdd:PRK00254 112 LGKYDIIIATAEK----FDSLLRHGSswIKDVKLVVADEIHLIGSYDRGATLEMILTHML---GRAQILGLSATVGNAEE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 549 LQKFLQAEYYTSQFRPVELKEYLKINDTIYEVDSKAENGMTFSRLLNYkysDTLKKmdpdhlvalvtevipNYSCLVFCP 628
Cdd:PRK00254 185 LAEWLNAELVVSDWRPVKLRKGVFYQGFLFWEDGKIERFPNSWESLVY---DAVKK---------------GKGALVFVN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 629 SKKNCENVAEMICKFLSKEYLKHKEKEKCEVIKNLK-NIGNGNLcpvlKRTIPFGVAYHHSGLTSDERKLLEEAYSTGVL 707
Cdd:PRK00254 247 TRRSAEKEALELAKKIKRFLTKPELRALKELADSLEeNPTNEKL----KKALRGGVAFHHAGLGRTERVLIEDAFREGLI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 708 CLFTCTSTLAAGVNLPARRVILRAPYVAKEF----LKRNQYKQMIGRAGRAGIDTIGESILILQEKDKQQVLE--LITKP 781
Cdd:PRK00254 323 KVITATPTLSAGINLPAFRVIIRDTKRYSNFgwedIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEPSKLMEryIFGKP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 782 lENCYSHLVQEftKGIQTLFLSLIGLKIATNLDDIYHFMNGTFFGVQQkvllKEKSLWEITVESLRYLtekgLLQKDTIy 861
Cdd:PRK00254 403 -EKLFSMLSNE--SAFRSQVLALITNFGVSNFKELVNFLERTFYAHQR----KDLYSLEEKAKEIVYF----LLENEFI- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 862 ksEEEVQYNFHITKLGRASFKGTIDlaycDILYRDLKKGLEGLVLE----SLLHLIYLT---TPYDLVSQCNPDWMIYFR 934
Cdd:PRK00254 471 --DIDLEDRFIPLPLGIRTSQLYID----PLTAKKFKDAFPKIEKNpnplGIFQLIASTpdmTPLNYSRKEMEDLLDEAY 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 935 QFsqlspaEQNVAAILGVSESFIGKKASGQAIGKKvdknvvnrlylsfVLYTLLKETNIWTVSEKFNMPRGYIQNLLtgt 1014
Cdd:PRK00254 545 EM------EDRLYFNIPYWEDYKFQKFLRAFKTAK-------------VLLDWINEVPEGEIVETYNIDPGDLYRIL--- 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 1015 asfsscvlhfceELEEFWVYRalLVELTK-----------------KLTYCVKAELIPLMEVTGVLEGRAKQLYSAGYKS 1077
Cdd:PRK00254 603 ------------ELADWLMYS--LIELYKlfepkqevldyletlhlRVKHGVREELLELMRLPMIGRKRARALYNAGFRS 668
|
730
....*....|....
gi 119626340 1078 LMHLANANPEVLVR 1091
Cdd:PRK00254 669 IEDIVNAKPSELLK 682
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
382-1115 |
1.56e-56 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 208.58 E-value: 1.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 382 WQHTCLTLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVlMILPYVAIVQEKISGLSSFGiELGFFVEEYAGS 461
Cdd:PRK01172 24 YDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSI-YIVPLRSLAMEKYEELSRLR-SLGMRVKISIGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 462 KGRFPPTKRRekKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSA 541
Cdd:PRK01172 102 YDDPPDFIKR--YDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSARYVNPDARILALSA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 542 TLNNVEDLQKFLQAEYYTSQFRPVELKEYLKINDTIYeVDSKAENGMTFSRLLNYKYSDtlkkmdpdhlvalvtevipNY 621
Cdd:PRK01172 178 TVSNANELAQWLNASLIKSNFRPVPLKLGILYRKRLI-LDGYERSQVDINSLIKETVND-------------------GG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 622 SCLVFCPSKKNCENVAEMICKFLSKeylkhkekekcevIKNLK-NIGNGNLCP-VLKRTIPFGVAYHHSGLTSDERKLLE 699
Cdd:PRK01172 238 QVLVFVSSRKNAEDYAEMLIQHFPE-------------FNDFKvSSENNNVYDdSLNEMLPHGVAFHHAGLSNEQRRFIE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 700 EAYSTGVLCLFTCTSTLAAGVNLPARRVIL----RAPYVAKEFLKRNQYKQMIGRAGRAGIDTIGESILILQEKDKQQVL 775
Cdd:PRK01172 305 EMFRNRYIKVIVATPTLAAGVNLPARLVIVrditRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYIYAASPASYDAA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 776 -ELITKPLENCYSHLVQEFTKGIQTlfLSLIGLKIATNLDDIYHFMNGTFFGVQQKVLLKEKSLweitVESLRYLTEKGL 854
Cdd:PRK01172 385 kKYLSGEPEPVISYMGSQRKVRFNT--LAAISMGLASSMEDLILFYNETLMAIQNGVDEIDYYI----ESSLKFLKENGF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 855 LQKDTIYKSeeevqynfhiTKLGRAsfkgTIDLaYCDIlyrdlkkgleglvlESLLHLI-YLTTPYDLvsqcnpDWMIYF 933
Cdd:PRK01172 459 IKGDVTLRA----------TRLGKL----TSDL-YIDP--------------ESALILKsAFDHDYDE------DLALYY 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 934 RQFS-QLSPAE-QNVAAILGVSESfIGkkasgqaigkKVDKNvVNRLYLSFVLYTLLKETNIWTVSEKFNMPRGYIQNLL 1011
Cdd:PRK01172 504 ISLCrEIIPANtRDDYYAMEFLED-IG----------VIDGD-ISAAKTAMVLRGWISEASMQKITDTYGIAPGDVQARA 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 1012 TGTASFSSCVLHFCEeleefwVY----RALLVELTKKLTYCVKAELIPLMEVTGVLEGRAKQLYSAGYKSLMHLANANPE 1087
Cdd:PRK01172 572 SSADWISYSLARLSS------IYkpemRRKLEILNIRIKEGIREDLIDLVLIPKVGRVRARRLYDAGFKTVDDIARSSPE 645
|
730 740
....*....|....*....|....*...
gi 119626340 1088 vLVRTIDHLSRRQAKQIVSSAKMLLHEK 1115
Cdd:PRK01172 646 -RIKKIYGFSDTLANAIVNRAMKISSMY 672
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
563-765 |
1.52e-42 |
|
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: 152.32 E-value: 1.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 563 RPVELKEYLKIndtiyevdskaengmtFSRLLNYKYSDTLKKMDPDHLVALVTEVIPNY-SCLVFCPSKKNCENVAEMIc 641
Cdd:cd18795 1 RPVPLEEYVLG----------------FNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGkPVLVFCSSRKECEKTAKDL- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 642 kflskeylkhkekekceviknlknigngnlcpvlkrtipFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVN 721
Cdd:cd18795 64 ---------------------------------------AGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVN 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 119626340 722 LPARRVILRAPYVAK----EFLKRNQYKQMIGRAGRAGIDTIGESILI 765
Cdd:cd18795 105 LPARTVIIKGTQRYDgkgyRELSPLEYLQMIGRAGRPGFDTRGEAIIM 152
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
380-557 |
2.48e-35 |
|
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: 132.77 E-value: 2.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 380 NEWQHTCLTLnSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKISGLSSFGIELGFFVEEYA 459
Cdd:cd17921 3 NPIQREALRA-LYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 460 GSKGRFPptKRREKKSLYIATIEKGHSLVNSLIETGrIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGM 539
Cdd:cd17921 82 GDPSVNK--LLLAEADILVATPEKLDLLLRNGGERL-IQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRINKNARFVGL 158
|
170
....*....|....*...
gi 119626340 540 SATLNNVEDLQKFLQAEY 557
Cdd:cd17921 159 SATLPNAEDLAEWLGVED 176
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
487-783 |
1.25e-31 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 133.14 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 487 LVNSLIETGR-IDSLGLVVVDELHMIGEGSRGATLEmtlAKILYTSKTTQIIGMSATLNNVEDLQKFLQA-----EYYTS 560
Cdd:COG4581 120 LRNMLYREGAdLEDVGVVVMDEFHYLADPDRGWVWE---EPIIHLPARVQLVLLSATVGNAEEFAEWLTRvrgetAVVVS 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 561 QFRPVELKEYLKINDTIYEVDSKAENGMTFSRLlnykySDTLKKMDPDHLValvteviPNYsclVFCPSKKNCENVAEMI 640
Cdd:COG4581 197 EERPVPLEFHYLVTPRLFPLFRVNPELLRPPSR-----HEVIEELDRGGLL-------PAI---VFIFSRRGCDEAAQQL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 641 ckfLSKEYLKHKEKEK-CEVIKNLKNIGNGNLCPVLKRTIPFGVAYHHSGLTSDERKLLEEAYSTG---VLClftCTSTL 716
Cdd:COG4581 262 ---LSARLTTKEERAEiREAIDEFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGllkVVF---ATDTL 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119626340 717 AAGVNLPARRVIL----------RAPYVAKEFLkrnqykQMIGRAGRAGIDTIGESILILQE-KDKQQVLELITKPLE 783
Cdd:COG4581 336 AVGINMPARTVVFtklskfdgerHRPLTAREFH------QIAGRAGRRGIDTEGHVVVLAPEhDDPKKFARLASARPE 407
|
|
| HTH_61 |
pfam20470 |
Helix-turn-helix domain; This entry represents a presumed helix-turn-helix domain found in DNA ... |
760-856 |
3.23e-30 |
|
Helix-turn-helix domain; This entry represents a presumed helix-turn-helix domain found in DNA polymerase theta.
Pssm-ID: 466619 [Multi-domain] Cd Length: 92 Bit Score: 114.95 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 760 GESILILQEKDKQQVLELITKPLENCYSHLVQEfTKGIQTLFLSLIGLKIATNLDDIYHFMNGTFFGVQQKVLLKEKSlw 839
Cdd:pfam20470 1 GESILICKEKDLEKVAELLRAELPPVYSCLLPE-KRGIKRALLEIIALGLATSPEDVDEYMSCTLLSVQQKELDVEKS-- 77
|
90
....*....|....*..
gi 119626340 840 eiTVESLRYLTEKGLLQ 856
Cdd:pfam20470 78 --IESSLEELVENGLIT 92
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
396-560 |
2.07e-28 |
|
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: 112.81 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 396 KNLIYSLPTSGGKTLVAEILMLQELLCCRKdVLMILPYVAIVQEKISGLSSFGiELGFFVeeyAGSKGRFPPTKRREKKS 475
Cdd:cd18028 18 ENLLISIPTASGKTLIAEMAMVNTLLEGGK-ALYLVPLRALASEKYEEFKKLE-EIGLKV---GISTGDYDEDDEWLGDY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 476 -LYIATIEKGHSLVNSLIETgrIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSATLNNVEDLQKFLQ 554
Cdd:cd18028 93 dIIVATYEKFDSLLRHSPSW--LRDVGVVVVDEIHLISDEERGPTLESIVARLRRLNPNTQIIGLSATIGNPDELAEWLN 170
|
....*.
gi 119626340 555 AEYYTS 560
Cdd:cd18028 171 AELVES 176
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
394-771 |
1.29e-22 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 104.59 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 394 ERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIV-------QEKISGLSSFGIELGffVEEYAGSKGRFP 466
Cdd:COG1202 224 EGKDQLVVSATATGKTLIGELAGIKNALEGKGKMLFLVPLVALAnqkyedfKDRYGDGLDVSIRVG--ASRIRDDGTRFD 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 467 PtkrreKKSLYIATIEkGhslVNSLIETGR-IDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSATLNN 545
Cdd:COG1202 302 P-----NADIIVGTYE-G---IDHALRTGRdLGDIGTVVIDEVHMLEDPERGHRLDGLIARLKYYCPGAQWIYLSATVGN 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 546 VEDLQKFLQAEYYTSQFRPVELKEYLkindtiyevdskaengmTFSRllNYKYSDTLKKmdpdhlvaLVTEVIPNYS--- 622
Cdd:COG1202 373 PEELAKKLGAKLVEYEERPVPLERHL-----------------TFAD--GREKIRIINK--------LVKREFDTKSskg 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 623 ----CLVFCPSKKNCENVAemickflskeylkhkekekceviknlknigngnlcpvlkRTIPFGVAYHHSGLTSDERKLL 698
Cdd:COG1202 426 yrgqTIIFTNSRRRCHEIA---------------------------------------RALGYKAAPYHAGLDYGERKKV 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119626340 699 EEAYSTGVLCLFTCTSTLAAGVNLPARRVILRAPYVAKEFLKRNQYKQMIGRAGRAGIDTIGEsILILQEKDK 771
Cdd:COG1202 467 ERRFADQELAAVVTTAALAAGVDFPASQVIFDSLAMGIEWLSVQEFHQMLGRAGRPDYHDRGK-VYLLVEPGK 538
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
388-549 |
2.54e-19 |
|
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: 86.14 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 388 TLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKD--VLMILPYVAIVQEKISGLSSFGIELGFFVE-EYAGSkgr 464
Cdd:pfam00270 7 AIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGpqALVLAPTRELAEQIYEELKKLGKGLGLKVAsLLGGD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 465 fPPTKRREKKS---LYIATIEKghsLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKIlytSKTTQIIGMSA 541
Cdd:pfam00270 84 -SRKEQLEKLKgpdILVGTPGR---LLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL---PKKRQILLLSA 156
|
....*....
gi 119626340 542 TLN-NVEDL 549
Cdd:pfam00270 157 TLPrNLEDL 165
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
396-542 |
1.18e-14 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 72.44 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 396 KNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKISGLSSF---GIELGFFVEEYAgSKGRFPPTKRRE 472
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSS-AEEREKNKLGDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 473 KksLYIATIEKGHSLVNSLiETGRIDSLGLVVVDELHMIGEGSRGAtLEMTLAKILYTSKTTQIIGMSAT 542
Cdd:cd00046 81 D--IIIATPDMLLNLLLRE-DRLFLKDLKLIIVDEAHALLIDSRGA-LILDLAVRKAGLKNAQVILLSAT 146
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
390-564 |
1.51e-14 |
|
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: 73.54 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 390 NSVQER---------KNLIYSLPTSGGKTLVAEILMLQeLLCCRKD-------VLMILPYVAIVQEKISGL-SSFGiELG 452
Cdd:cd18023 3 NRIQSEvfpdllysdKNFVVSAPTGSGKTVLFELAILR-LLKERNPlpwgnrkVVYIAPIKALCSEKYDDWkEKFG-PLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 453 FFVEEYAGSKGrFPPTKRREKKSLYIATIEKGHSLVNSLIETGR-IDSLGLVVVDELHMIGEgSRGATLEMTLA--KILY 529
Cdd:cd18023 81 LSCAELTGDTE-MDDTFEIQDADIILTTPEKWDSMTRRWRDNGNlVQLVALVLIDEVHIIKE-NRGATLEVVVSrmKTLS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 119626340 530 TSKTT--------QIIGMSATLNNVEDLQKFLQAEY-----YTSQFRP 564
Cdd:cd18023 159 SSSELrgstvrpmRFVAVSATIPNIEDLAEWLGDNPagcfsFGESFRP 206
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
392-560 |
1.27e-12 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 67.90 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 392 VQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKD-VLMILPYVAIVQEKISGLSSFGIELGFFVEEYAG--SKGRFPPT 468
Cdd:smart00487 21 LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGrVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGgdSKREQLRK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 469 KRREKKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKIlytSKTTQIIGMSATLNN--V 546
Cdd:smart00487 101 LESGKTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL---PKNVQLLLLSATPPEeiE 175
|
170
....*....|....
gi 119626340 547 EDLQKFLQAEYYTS 560
Cdd:smart00487 176 NLLELFLNDPVFID 189
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
388-553 |
1.27e-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: 68.17 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 388 TLNSVQER---------KNLIYSLPTSGGKTLVAEILMLQELLCCRKD----------VLMILPYVAIVQEKISGLSSFG 448
Cdd:cd18019 17 SLNRIQSKlfpaafetdENLLLCAPTGAGKTNVALLTILREIGKHRNPdgtinldafkIVYIAPMKALVQEMVGNFSKRL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 449 IELGFFVEEYAG----SKGRFPPTKrrekksLYIATIEKGHSLVNSLIETGRIDSLGLVVVDELHMIGEgSRGATLEMTL 524
Cdd:cd18019 97 APYGITVAELTGdqqlTKEQISETQ------IIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD-DRGPVLESIV 169
|
170 180 190
....*....|....*....|....*....|...
gi 119626340 525 AKILYTSKTTQ----IIGMSATLNNVEDLQKFL 553
Cdd:cd18019 170 ARTIRQIEQTQeyvrLVGLSATLPNYEDVATFL 202
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
677-755 |
1.42e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.16 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 677 RTIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLP-ARRVILRAPYVAKEflkrnQYKQMIGRAGRAG 755
Cdd:smart00490 8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDLPWSPA-----SYIQRIGRAGRAG 82
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
396-553 |
4.57e-11 |
|
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: 63.16 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 396 KNLIYSLPTSGGKTLVAEILMLQELlccRK----DVLMILPYVAIVQEKISGLSS-FGIELGFFVEEYAGSKGrfPPTKR 470
Cdd:cd18022 18 NNVLLGAPTGSGKTIAAELAMFRAF---NKypgsKVVYIAPLKALVRERVDDWKKrFEEKLGKKVVELTGDVT--PDMKA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 471 REKKSLYIATIEKGHSLVNSLIETGRIDSLGLVVVDELHMIGEgSRGATLEMTLAKILY----TSKTTQIIGMSATLNNV 546
Cdd:cd18022 93 LADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGS-DRGPVLEVIVSRMNYissqTEKPVRLVGLSTALANA 171
|
....*..
gi 119626340 547 EDLQKFL 553
Cdd:cd18022 172 GDLANWL 178
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
646-755 |
4.36e-10 |
|
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: 57.99 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 646 KEYLKHKEKEKCEVIKNLKNIGNGNLcpvLKRTIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLP-A 724
Cdd:pfam00271 7 LELLKKERGGKVLIFSQTKKTLEAEL---LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdV 83
|
90 100 110
....*....|....*....|....*....|..
gi 119626340 725 RRVI-LRAPYvakeflKRNQYKQMIGRAGRAG 755
Cdd:pfam00271 84 DLVInYDLPW------NPASYIQRIGRAGRAG 109
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
388-562 |
5.11e-10 |
|
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: 60.14 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 388 TLNSVQER---------KNLIYSLPTSGGKTLVAEILMLQELLC-------CRKD---VLMILPYVAIVQEKISGLSSFG 448
Cdd:cd18020 1 RLNRIQSLvfpvayktnENMLICAPTGAGKTNIAMLTILHEIRQhvnqggvIKKDdfkIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 449 IELGFFVEEYAGSkgrFPPTKRREKKSLYIAT-------IEKGHSLVNSLIETGRidslgLVVVDELHMIGEgSRGATLE 521
Cdd:cd18020 81 APLGIKVKELTGD---MQLTKKEIAETQIIVTtpekwdvVTRKSSGDVALSQLVR-----LLIIDEVHLLHD-DRGPVIE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 119626340 522 MTLAKILYTSKTTQ----IIGMSATLNNVEDLQKFLQAEYYTSQF 562
Cdd:cd18020 152 SLVARTLRQVESTQsmirIVGLSATLPNYLDVADFLRVNPYKGLF 196
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
376-768 |
2.58e-09 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 61.19 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 376 GLRAneWQHTCLT---LNSVQERKNLIYSLPTSGGKTLVAeILMLQELLCCRKdVLMILPYVAIV---QEKIsglssfgi 449
Cdd:COG1061 80 ELRP--YQQEALEallAALERGGGRGLVVAPTGTGKTVLA-LALAAELLRGKR-VLVLVPRRELLeqwAEEL-------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 450 elgffvEEYAGSKGRFPPTKRREKKsLYIATIekgHSLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKIly 529
Cdd:COG1061 148 ------RRFLGDPLAGGGKKDSDAP-ITVATY---QSLARRAHLDELGDRFGLVIIDEAHHAGAPSYRRILEAFPAAY-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 530 tskttqIIGMSATLnnvedlqkflqaeYYTSQfRPVELKEYLKIndtIYEVDSK--AENGM-------------TFSRLL 594
Cdd:COG1061 216 ------RLGLTATP-------------FRSDG-REILLFLFDGI---VYEYSLKeaIEDGYlappeyygirvdlTDERAE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 595 NYKYSDTLKK---MDPDHLVALVTEVIPNYS----CLVFCPSKKNCENVAEMIckflskeylkHKEKEKCEVIknlknig 667
Cdd:COG1061 273 YDALSERLREalaADAERKDKILRELLREHPddrkTLVFCSSVDHAEALAELL----------NEAGIRAAVV------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 668 ngnlcpvlkrtipfgvayhHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLP-ARRVILRAPYVAkeflkRNQYKQ 746
Cdd:COG1061 336 -------------------TGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPrLDVAILLRPTGS-----PREFIQ 391
|
410 420 430
....*....|....*....|....*....|
gi 119626340 747 MIGRAGRAG--------IDTIGESILILQE 768
Cdd:COG1061 392 RLGRGLRPApgkedalvYDFVGNDVPVLEE 421
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
397-549 |
4.29e-09 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 57.27 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 397 NLIYSLPTSGGKTLVAEILMLQellCCRKDVLMILPYVAIVQEKISGL-----SSFGIELGFFVEEYAGSKGRfpPTKRR 471
Cdd:cd18021 21 NVFVGAPTGSGKTVCAELALLR---HWRQNPKGRAVYIAPMQELVDARykdwrAKFGPLLGKKVVKLTGETST--DLKLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 472 EKKSLYIATIEKGHSLVNSLIETGRIDSLGLVVVDELHMIGeGSRGATLEMTLAKILY----TSKTTQIIGMSATLNNVE 547
Cdd:cd18021 96 AKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIG-GENGPVYEVVVSRMRYissqLEKPIRIVGLSSSLANAR 174
|
..
gi 119626340 548 DL 549
Cdd:cd18021 175 DV 176
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
382-768 |
1.77e-08 |
|
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: 58.69 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 382 WQHTCLTLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLccrKD----VLMILPYVAIVQEKISGLSSF--GIELGFFV 455
Cdd:COG1205 58 YSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL---EDpgatALYLYPTKALARDQLRRLRELaeALGLGVRV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 456 EEYAGSKgrfPPTKRRE--KKSLYIAT--------IEKGHSLVNSLIEtgridSLGLVVVDELHMIgEGSRGATLEMTLA 525
Cdd:COG1205 135 ATYDGDT---PPEERRWirEHPDIVLTnpdmlhygLLPHHTRWARFFR-----NLRYVVIDEAHTY-RGVFGSHVANVLR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 526 KIL-----YTSKTtQIIGMSATLNNvedlqkflqaeyytsqfrPVELKEYLkINDTIYEVDskaENG-----MTFSrLLN 595
Cdd:COG1205 206 RLRricrhYGSDP-QFILASATIGN------------------PAEHAERL-TGRPVTVVD---EDGsprgeRTFV-LWN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 596 YKYSDTLKKMDPDHLVA-LVTE-VIPNYSCLVFCPSKKNCENVAEMICKFLSKEYLKHKekekceviknlknigngnlcp 673
Cdd:COG1205 262 PPLVDDGIRRSALAEAArLLADlVREGLRTLVFTRSRRGAELLARYARRALREPDLADR--------------------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 674 vlkrtipfgVAYHHSGLTSDERKLLEEAYSTG-VLCLFTcTSTLAAGVNLP---ArrVILRA-PYvakeflKRNQYKQMI 748
Cdd:COG1205 321 ---------VAAYRAGYLPEERREIERGLRSGeLLGVVS-TNALELGIDIGgldA--VVLAGyPG------TRASFWQQA 382
|
410 420
....*....|....*....|
gi 119626340 749 GRAGRAGIDtiGESILILQE 768
Cdd:COG1205 383 GRAGRRGQD--SLVVLVAGD 400
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
396-553 |
2.89e-08 |
|
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: 54.51 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 396 KNLIYSLPTSGGKTLVAEILMLQELLCCRKD---VLMILPYVAI---VQEKISGLSSfGIELGFFVEEYAG--SKGRfpp 467
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALSSLADEPEKgvqVLYISPLKALindQERRLEEPLD-EIDLEIPVAVRHGdtSQSE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 468 tKRREKKS---LYIATIEkghSLVNSLIETGR---IDSLGLVVVDELHMIGEGSRGATLEMTLAKI-LYTSKTTQIIGMS 540
Cdd:cd17922 78 -KAKQLKNppgILITTPE---SLELLLVNKKLrelFAGLRYVVVDEIHALLGSKRGVQLELLLERLrKLTGRPLRRIGLS 153
|
170
....*....|...
gi 119626340 541 ATLNNVEDLQKFL 553
Cdd:cd17922 154 ATLGNLEEAAAFL 166
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
382-549 |
5.73e-08 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 53.74 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 382 WQHTCLTLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLccrKDV----LMILPYVAIVQEKISGLSSF--GIELGFFV 455
Cdd:cd17923 2 YSHQAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL---RDPgsraLYLYPTKALAQDQLRSLRELleQLGLGIRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 456 EEYAGSkgrfppTKRREKKSLYI--------------ATIEKGHSLVNSLIEtgridSLGLVVVDELHMIgEGSRGATLE 521
Cdd:cd17923 79 ATYDGD------TPREERRAIIRnpprilltnpdmlhYALLPHHDRWARFLR-----NLRYVVLDEAHTY-RGVFGSHVA 146
|
170 180 190
....*....|....*....|....*....|..
gi 119626340 522 MTLAKIL----YTSKTTQIIGMSATLNNVEDL 549
Cdd:cd17923 147 LLLRRLRrlcrRYGADPQFILTSATIGNPAEH 178
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
503-752 |
7.80e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 50.31 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 503 VVVDELHMIGEGSRGATLEMTLAK---ILYTSktTQIIGMSATLNNVEDLQKFLQAEYYTSQFRPVELKEY-LKINDTIY 578
Cdd:PRK09751 128 VIIDEVHAVAGSKRGAHLALSLERldaLLHTS--AQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRHPqIRIVVPVA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 579 EVDSKAENGmtfSRLLNYKYSDTLKKMDPDHLVALVTEVIPNYSCLVFcpskKNCENVAEMICKFLSKEYLKH--KEKEK 656
Cdd:PRK09751 206 NMDDVSSVA---SGTGEDSHAGREGSIWPYIETGILDEVLRHRSTIVF----TNSRGLAEKLTARLNELYAARlqRSPSI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 657 CEVIKNLKNIgNGNLCPVLKRTIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLPARRVILRA---PY 733
Cdd:PRK09751 279 AVDAAHFEST-SGATSNRVQSSDVFIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVatpLS 357
|
250
....*....|....*....
gi 119626340 734 VAKEFlkrnqykQMIGRAG 752
Cdd:PRK09751 358 VASGL-------QRIGRAG 369
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
622-753 |
7.89e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 46.87 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 622 SCLVFCPSKKNCENVAEmickflskeylkhkekekcevikNLKNigngnLCPvlKRTIPFGVAYHHSGLTSDERKLLEEA 701
Cdd:cd18796 40 STLVFTNTRSQAERLAQ-----------------------RLRE-----LCP--DRVPPDFIALHHGSLSRELREEVEAA 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 119626340 702 YSTGVLCLFTCTSTLAAGVNLPA-RRVI-LRAPYVAKEFLKRnqykqmIGRAGR 753
Cdd:cd18796 90 LKRGDLKVVVATSSLELGIDIGDvDLVIqIGSPKSVARLLQR------LGRSGH 137
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
503-553 |
1.58e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 49.33 E-value: 1.58e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 119626340 503 VVVDELHMIGEGSRGATLEMTLAKI-LYTSKTTQIIGMSATLNNVEDLQKFL 553
Cdd:COG1201 165 VIVDEIHALAGSKRGVHLALSLERLrALAPRPLQRIGLSATVGPLEEVARFL 216
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
389-554 |
1.93e-05 |
|
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: 46.76 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 389 LNSVQERKNLIYSLPTSGGKTLVAEIlmlqELLCCRKDVLMILPYVAIVQEKISGLSSFGIELGFFveeyAGSKGRFPPT 468
Cdd:cd17920 21 INAVLAGRDVLVVMPTGGGKSLCYQL----PALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAAL----NSTLSPEEKR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 469 KRREK------KSLYIA--TIEKGH--SLVNSLIETGRIDslgLVVVDELHMI---GEGSRGATLEmtLAKILYTSKTTQ 535
Cdd:cd17920 93 EVLLRikngqyKLLYVTpeRLLSPDflELLQRLPERKRLA---LIVVDEAHCVsqwGHDFRPDYLR--LGRLRRALPGVP 167
|
170 180
....*....|....*....|.
gi 119626340 536 IIGMSATLNNV--EDLQKFLQ 554
Cdd:cd17920 168 ILALTATATPEvrEDILKRLG 188
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
393-542 |
6.92e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.59 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 393 QERKNLIySLPTSGGKTLVAEILM--LQELLCCRKdVLMILPYVAIVQEKISGLSSFGIELGFFVEEYAGSKGRFPptkr 470
Cdd:pfam04851 22 GQKRGLI-VMATGSGKTLTAAKLIarLFKKGPIKK-VLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDES---- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119626340 471 REKKSLYIATIEKGHSLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLEMtlakilytSKTTQIIGMSAT 542
Cdd:pfam04851 96 VDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAHRSGASSYRNILEY--------FKPAFLLGLTAT 159
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
396-545 |
3.16e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 43.19 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 396 KNLIYSLPTSGGKTLVAEILM---LQELLCCRKD-VLMILPYVAIVQEKISGLSSFGIELGFFVEEYAG---SKGRFPpt 468
Cdd:cd17927 18 KNTIICLPTGSGKTFVAVLICehhLKKFPAGRKGkVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGdtsENVSVE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 469 KRREKKSLYIATiekGHSLVNSLiETGRIDSL---GLVVVDELHM-IGEGS-RGATLEMTLAKILYTSKTTQIIGMSATL 543
Cdd:cd17927 96 QIVESSDVIIVT---PQILVNDL-KSGTIVSLsdfSLLVFDECHNtTKNHPyNEIMFRYLDQKLGSSGPLPQILGLTASP 171
|
..
gi 119626340 544 NN 545
Cdd:cd17927 172 GV 173
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
395-509 |
4.19e-04 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 44.34 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 395 RKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKISGLSSFgieLGFFVEEYAGSKGRFPPTKRR--- 471
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAERLHKKGGKVLFLAPTKPLVEQHAEFFKEA---LNIPEDEIVVFTGEVSPEKRKelw 93
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 119626340 472 EKKSLYIATIEkghsLVNSLIETGRID--SLGLVVVDELH 509
Cdd:COG1111 94 EKARIIVATPQ----VIENDLIAGRIDldDVSLLIFDEAH 129
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
396-551 |
4.81e-04 |
|
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: 42.31 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 396 KNLIYSLPTSGGKTLVAEILMLQELlccR-----KDVLMIlPYVAIVQEKISGLSSFGielGFFVEEYAGSKGRFPPTKR 470
Cdd:cd18033 17 QNTLVALPTGLGKTFIAAVVMLNYY---RwfpkgKIVFMA-PTKPLVSQQIEACYKIT---GIPSSQTAELTGSVPPTKR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 471 RE---KKSLYIATiekGHSLVNSLIEtGRID--SLGLVVVDELHMiGEGSRGATleMTLAKILYTSKTTQIIGMSATL-N 544
Cdd:cd18033 90 AElwaSKRVFFLT---PQTLENDLKE-GDCDpkSIVCLVIDEAHR-ATGNYAYC--QVVRELMRYNSHFRILALTATPgS 162
|
....*..
gi 119626340 545 NVEDLQK 551
Cdd:cd18033 163 KLEAVQQ 169
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
395-559 |
9.16e-04 |
|
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: 41.87 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 395 RKNLIYSLPTSGGKTLVAEILMLQELLCCRKD------VLMILPYVAIVQEKIsglSSFGIELGFFVEEYAGSKGrfPPT 468
Cdd:cd18034 16 KRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEknpkkrAVFLVPTVPLVAQQA---EAIRSHTDLKVGEYSGEMG--VDK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 469 KRREKKSLYIATIE----KGHSLVNSLIETG-RIDSLGLVVVDELHMIGEGSRGAtlemTLAKILYTSKTTQ----IIGM 539
Cdd:cd18034 91 WTKERWKEELEKYDvlvmTAQILLDALRHGFlSLSDINLLIFDECHHATGDHPYA----RIMKEFYHLEGRTsrprILGL 166
|
170 180 190
....*....|....*....|....*....|.
gi 119626340 540 SA-----------TLNNVEDLQKFLQAEYYT 559
Cdd:cd18034 167 TAspvngkgdpksVEKKIQQLEELLNSTIKT 197
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
399-543 |
2.98e-03 |
|
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: 39.21 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626340 399 IYSLPTSGGKTLVAeILMLQELLCCRkdVLMILPYVAIV---QEKISGLSSfGIELGFFveeyagskgRFPPTKRREKKS 475
Cdd:cd17926 22 ILVLPTGSGKTLTA-LALIAYLKELR--TLIVVPTDALLdqwKERFEDFLG-DSSIGLI---------GGGKKKDFDDAN 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119626340 476 LYIATIEkghSLVNSLIETGRI-DSLGLVVVDELHMIGEGSRGATLEMTLAKILytskttqiIGMSATL 543
Cdd:cd17926 89 VVVATYQ---SLSNLAEEEKDLfDQFGLLIVDEAHHLPAKTFSEILKELNAKYR--------LGLTATP 146
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
1056-1109 |
3.52e-03 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 3.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 119626340 1056 LMEVTGVLEGRAKQLYSAGYKSLMHLANANPEVLVRTIDhLSRRQAKQIVSSAK 1109
Cdd:pfam14520 4 LLSISGIGPKTALALLSAGIGTVEDLAEADVDELAEIPG-IGEKTAQRIILELR 56
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
695-765 |
8.53e-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: 36.14 E-value: 8.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119626340 695 RKLLEEAYStgVLCLFTCTSTLAAGVNLP-ARRVILRAPYVAKeflkrNQYKQMIGRAGRAGiDTIGESILI 765
Cdd:cd18785 13 IEHAEEIAS--SLEILVATNVLGEGIDVPsLDTVIFFDPPSSA-----ASYIQRVGRAGRGG-KDEGEVILF 76
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
503-567 |
8.89e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 40.25 E-value: 8.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119626340 503 VVVDELHMIGEGSRGATLEMTLAKILY-TSKTTQIIGMSATLNNVEDLQKFLQAEYYTSQFRPVEL 567
Cdd:PRK13767 176 VIVDEIHSLAENKRGVHLSLSLERLEElAGGEFVRIGLSATIEPLEEVAKFLVGYEDDGEPRDCEI 241
|
|
| |
