|
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 ... |
319-521 |
1.33e-114 |
|
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: 353.06 E-value: 1.33e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 319 LPSKVRDLYAQfKGIEKLYEWQHTCLTLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKI 398
Cdd:cd18026 1 LPDAVREAYAK-KGIKKLYDWQKECLSLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRLLERRKKALFVLPYVSIVQEKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 399 SGLSSFGIELGFFVEEYAGSKGRFPPtKRREKKSLYIATIEKGHSLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLE 478
Cdd:cd18026 80 DALSPLFEELGFRVEGYAGNKGRSPP-KRRKSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDGHRGALLE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1844083922 479 MTLAKILYTSK-TTQIIGMSATLNNVEDLQKFLQAEYYTSQFRP 521
Cdd:cd18026 159 LLLTKLLYAAQkNIQIVGMSATLPNLEELASWLRAELYTTNFRP 202
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
319-887 |
9.17e-106 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 341.87 E-value: 9.17e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 319 LPSKVRDLYAQFkGIEKLYEWQHTCLTlNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKdVLMILPYVAIVQEKI 398
Cdd:COG1204 7 PLEKVIEFLKER-GIEELYPPQAEALE-AGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK-ALYIVPLRALASEKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 399 SGLSSFGIELGFfveEYAGSKGRFPPTKRR-EKKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGEGSRGATL 477
Cdd:COG1204 84 REFKRDFEELGI---KVGVSTGDYDSDDEWlGRYDILVATPEKLDSLLRN--GPSWLRDVDLVVVDEAHLIDDESRGPTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 478 EMTLAKILYTSKTTQIIGMSATLNNVEDLQKFLQAEYYTSQFRPVELKEYLKINDTIYevdskaengmtfsrllnykYSD 557
Cdd:COG1204 159 EVLLARLRRLNPEAQIVALSATIGNAEEIAEWLDAELVKSDWRPVPLNEGVLYDGVLR-------------------FDD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 558 TLKKMDpDHLVALVTEVIP-NYSCLVFCPSKKNCENVAEMICKFLsKEYLKHKEKEKC-EVIKNLKNIGNGN-LCPVLKR 634
Cdd:COG1204 220 GSRRSK-DPTLALALDLLEeGGQVLVFVSSRRDAESLAKKLADEL-KRRLTPEEREELeELAEELLEVSEEThTNEKLAD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 635 TIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLPARRVILRAPY-VAKEFLKRNQYKQMIGRAGRAGI 713
Cdd:COG1204 298 CLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKrGGMVPIPVLEFKQMAGRAGRPGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 714 DTIGESILIlqEKDKQQVLELITKPL----ENCYSHLVQEftKGIQTLFLSLIGLKIATNLDDIYHFMNGTFFGVQQkvl 789
Cdd:COG1204 378 DPYGEAILV--AKSSDEADELFERYIlgepEPIRSKLANE--SALRTHLLALIASGFANSREELLDFLENTFYAYQY--- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 790 lKEKSLWEITVESLRYLTEKGLLQKDTIYkseeevqynFHITKLGRASFKGTIDLAYCDILYRDLKKGLEGLVLESLLHL 869
Cdd:COG1204 451 -DKGDLEEVVDDALEFLLENGFIEEDGDR---------LRATKLGKLVSRLYIDPLTAAELVDGLRKADEEFTDLGLLHL 520
|
570
....*....|....*...
gi 1844083922 870 IYLTTpydlvsqcnpDWM 887
Cdd:COG1204 521 ILILR----------DWI 528
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
318-1066 |
5.65e-93 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 313.43 E-value: 5.65e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 318 SLPSKVRDLYAQfKGIEKLYEWQHTCLTlNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKdVLMILPYVAIVQEK 397
Cdd:PRK02362 7 PLPEGVIEFYEA-EGIEELYPPQAEAVE-AGLLDGKNLLAAIPTASGKTLIAELAMLKAIARGGK-ALYIVPLRALASEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 398 ---ISGLSSFGIELGFfveeyagSKGRFpptKRRE----KKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGE 470
Cdd:PRK02362 84 feeFERFEELGVRVGI-------STGDY---DSRDewlgDNDIIVATSEKVDSLLRN--GAPWLDDITCVVVDEVHLIDS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 471 GSRGATLEMTLAKILYTSKTTQIIGMSATLNNVEDLQKFLQAEYYTSQFRPVELKEYLKINDTIYEVDSKAEngmtfsrl 550
Cdd:PRK02362 152 ANRGPTLEVTLAKLRRLNPDLQVVALSATIGNADELADWLDAELVDSEWRPIDLREGVFYGGAIHFDDSQRE-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 551 lnykysdtLKKMDPDHLVALVTEVI-PNYSCLVFCPSKKNCENVAEMICKFLSKEYLKHKEKEKCEVIKNLKNIGNGNLC 629
Cdd:PRK02362 224 --------VEVPSKDDTLNLVLDTLeEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVSDTETS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 630 PVLKRTIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLPARRVILR-----------APYVAKEflkr 698
Cdd:PRK02362 296 KDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRdyrrydggagmQPIPVLE---- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 699 nqYKQMIGRAGRAGIDTIGESILIlqEKDKQQVLEL----ITKPLENCYSHLVQEftKGIQTLFLSLIGLKIATNLDDIY 774
Cdd:PRK02362 372 --YHQMAGRAGRPGLDPYGEAVLL--AKSYDELDELferyIWADPEDVRSKLATE--PALRTHVLSTIASGFARTRDGLL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 775 HFMNGTFFGVQQKvllKEKSLWEITVESLRYLTEKGLLQKDtiyksEEEVqynfHITKLGRasfkgTIDLAYCDILY-RD 853
Cdd:PRK02362 446 EFLEATFYATQTD---DTGRLERVVDDVLDFLERNGMIEED-----GETL----EATELGH-----LVSRLYIDPLSaAE 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 854 LKKGLEGLVLES---LLHLIYLTtpydlvsqcnPD-WMIYFRqfsqlSPAEQNVAAILGVSES-FIGKKASgqaigkkVD 928
Cdd:PRK02362 509 IIDGLEAAKKPTdlgLLHLVCST----------PDmYELYLR-----SGDYEWLNEYLYEHEDeLLGDVPS-------EF 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 929 KNVVNRLYLSFVLYTLLKETNIWTVSE-----KFNMPRGYIQN-------LLTGTASFSScvlhfceELEEFWVYRAllV 996
Cdd:PRK02362 567 EDDEFEDFLSAVKTALLLEDWIDEVDEeriteRYGVGPGDIRGkvetaewLLHAAERLAS-------ELDLDLARAA--R 637
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 997 ELTKKLTYCVKAELIPLMEVTGVLEGRAKQLYSAGYKSLMHLANANPEVLVRTidhLSRRQAKQIVSSAK 1066
Cdd:PRK02362 638 ELEKRVEYGVREELLDLVGLRGVGRVRARRLYNAGIESRADLRAADKSVVLAI---LGEKIAENILEQAG 704
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
520-722 |
1.46e-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: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 520 RPVELKEYLKIndtiyevdskaengmtFSRLLNYKYSDTLKKMDPDHLVALVTEVIPNY-SCLVFCPSKKNCENVAEMIc 598
Cdd:cd18795 1 RPVPLEEYVLG----------------FNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGkPVLVFCSSRKECEKTAKDL- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 599 kflskeylkhkekekceviknlknigngnlcpvlkrtipFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVN 678
Cdd:cd18795 64 ---------------------------------------AGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVN 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1844083922 679 LPARRVILRAPYVAK----EFLKRNQYKQMIGRAGRAGIDTIGESILI 722
Cdd:cd18795 105 LPARTVIIKGTQRYDgkgyRELSPLEYLQMIGRAGRPGFDTRGEAIIM 152
|
|
| HTH_61 |
pfam20470 |
Helix-turn-helix domain; This entry represents a presumed helix-turn-helix domain found in DNA ... |
717-813 |
2.93e-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: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 717 GESILILQEKDKQQVLELITKPLENCYSHLVQEfTKGIQTLFLSLIGLKIATNLDDIYHFMNGTFFGVQQKVLLKEKSlw 796
Cdd:pfam20470 1 GESILICKEKDLEKVAELLRAELPPVYSCLLPE-KRGIKRALLEIIALGLATSPEDVDEYMSCTLLSVQQKELDVEKS-- 77
|
90
....*....|....*..
gi 1844083922 797 eiTVESLRYLTEKGLLQ 813
Cdd:pfam20470 78 --IESSLEELVENGLIT 92
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
351-728 |
1.53e-22 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 104.20 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 351 ERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIV-------QEKISGLSSFGIELGffVEEYAGSKGRFP 423
Cdd:COG1202 224 EGKDQLVVSATATGKTLIGELAGIKNALEGKGKMLFLVPLVALAnqkyedfKDRYGDGLDVSIRVG--ASRIRDDGTRFD 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 424 PtkrreKKSLYIATIEkGhslVNSLIETGR-IDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSATLNN 502
Cdd:COG1202 302 P-----NADIIVGTYE-G---IDHALRTGRdLGDIGTVVIDEVHMLEDPERGHRLDGLIARLKYYCPGAQWIYLSATVGN 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 503 VEDLQKFLQAEYYTSQFRPVELKEYLkindtiyevdskaengmTFSRllNYKYSDTLKKmdpdhlvaLVTEVIPNYS--- 579
Cdd:COG1202 373 PEELAKKLGAKLVEYEERPVPLERHL-----------------TFAD--GREKIRIINK--------LVKREFDTKSskg 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 580 ----CLVFCPSKKNCENVAemickflskeylkhkekekceviknlknigngnlcpvlkRTIPFGVAYHHSGLTSDERKLL 655
Cdd:COG1202 426 yrgqTIIFTNSRRRCHEIA---------------------------------------RALGYKAAPYHAGLDYGERKKV 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083922 656 EEAYSTGVLCLFTCTSTLAAGVNLPARRVILRAPYVAKEFLKRNQYKQMIGRAGRAGIDTIGEsILILQEKDK 728
Cdd:COG1202 467 ERRFADQELAAVVTTAALAAGVDFPASQVIFDSLAMGIEWLSVQEFHQMLGRAGRPDYHDRGK-VYLLVEPGK 538
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
345-506 |
3.12e-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: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 345 TLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKD--VLMILPYVAIVQEKISGLSSFGIELGFFVE-EYAGSkgr 421
Cdd:pfam00270 7 AIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGpqALVLAPTRELAEQIYEELKKLGKGLGLKVAsLLGGD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 422 fPPTKRREKKS---LYIATIEKghsLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKIlytSKTTQIIGMSA 498
Cdd:pfam00270 84 -SRKEQLEKLKgpdILVGTPGR---LLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL---PKKRQILLLSA 156
|
....*....
gi 1844083922 499 TLN-NVEDL 506
Cdd:pfam00270 157 TLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
331-517 |
7.13e-14 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 71.75 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 331 KGIEKLYEWQHTCLTLnSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKD-VLMILPYVAIVQEKISGLSSFGIELG 409
Cdd:smart00487 4 FGFEPLRPYQKEAIEA-LLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGrVLVLVPTRELAEQWAEELKKLGPSLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 410 FFVEEYAG--SKGRFPPTKRREKKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKIlyt 487
Cdd:smart00487 83 LKVVGLYGgdSKREQLRKLESGKTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL--- 157
|
170 180 190
....*....|....*....|....*....|..
gi 1844083922 488 SKTTQIIGMSATLNN--VEDLQKFLQAEYYTS 517
Cdd:smart00487 158 PKNVQLLLLSATPPEeiENLLELFLNDPVFID 189
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
634-712 |
1.36e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.16 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 634 RTIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLP-ARRVILRAPYVAKEflkrnQYKQMIGRAGRAG 712
Cdd:smart00490 8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDLPWSPA-----SYIQRIGRAGRAG 82
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
1013-1066 |
3.49e-03 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 3.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1844083922 1013 LMEVTGVLEGRAKQLYSAGYKSLMHLANANPEVLVRTIDhLSRRQAKQIVSSAK 1066
Cdd:pfam14520 4 LLSISGIGPKTALALLSAGIGTVEDLAEADVDELAEIPG-IGEKTAQRIILELR 56
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
460-524 |
9.03e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 40.25 E-value: 9.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844083922 460 VVVDELHMIGEGSRGATLEMTLAKILY-TSKTTQIIGMSATLNNVEDLQKFLQAEYYTSQFRPVEL 524
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 ... |
319-521 |
1.33e-114 |
|
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: 353.06 E-value: 1.33e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 319 LPSKVRDLYAQfKGIEKLYEWQHTCLTLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKI 398
Cdd:cd18026 1 LPDAVREAYAK-KGIKKLYDWQKECLSLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRLLERRKKALFVLPYVSIVQEKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 399 SGLSSFGIELGFFVEEYAGSKGRFPPtKRREKKSLYIATIEKGHSLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLE 478
Cdd:cd18026 80 DALSPLFEELGFRVEGYAGNKGRSPP-KRRKSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDGHRGALLE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1844083922 479 MTLAKILYTSK-TTQIIGMSATLNNVEDLQKFLQAEYYTSQFRP 521
Cdd:cd18026 159 LLLTKLLYAAQkNIQIVGMSATLPNLEELASWLRAELYTTNFRP 202
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
319-887 |
9.17e-106 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 341.87 E-value: 9.17e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 319 LPSKVRDLYAQFkGIEKLYEWQHTCLTlNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKdVLMILPYVAIVQEKI 398
Cdd:COG1204 7 PLEKVIEFLKER-GIEELYPPQAEALE-AGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK-ALYIVPLRALASEKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 399 SGLSSFGIELGFfveEYAGSKGRFPPTKRR-EKKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGEGSRGATL 477
Cdd:COG1204 84 REFKRDFEELGI---KVGVSTGDYDSDDEWlGRYDILVATPEKLDSLLRN--GPSWLRDVDLVVVDEAHLIDDESRGPTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 478 EMTLAKILYTSKTTQIIGMSATLNNVEDLQKFLQAEYYTSQFRPVELKEYLKINDTIYevdskaengmtfsrllnykYSD 557
Cdd:COG1204 159 EVLLARLRRLNPEAQIVALSATIGNAEEIAEWLDAELVKSDWRPVPLNEGVLYDGVLR-------------------FDD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 558 TLKKMDpDHLVALVTEVIP-NYSCLVFCPSKKNCENVAEMICKFLsKEYLKHKEKEKC-EVIKNLKNIGNGN-LCPVLKR 634
Cdd:COG1204 220 GSRRSK-DPTLALALDLLEeGGQVLVFVSSRRDAESLAKKLADEL-KRRLTPEEREELeELAEELLEVSEEThTNEKLAD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 635 TIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLPARRVILRAPY-VAKEFLKRNQYKQMIGRAGRAGI 713
Cdd:COG1204 298 CLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKrGGMVPIPVLEFKQMAGRAGRPGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 714 DTIGESILIlqEKDKQQVLELITKPL----ENCYSHLVQEftKGIQTLFLSLIGLKIATNLDDIYHFMNGTFFGVQQkvl 789
Cdd:COG1204 378 DPYGEAILV--AKSSDEADELFERYIlgepEPIRSKLANE--SALRTHLLALIASGFANSREELLDFLENTFYAYQY--- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 790 lKEKSLWEITVESLRYLTEKGLLQKDTIYkseeevqynFHITKLGRASFKGTIDLAYCDILYRDLKKGLEGLVLESLLHL 869
Cdd:COG1204 451 -DKGDLEEVVDDALEFLLENGFIEEDGDR---------LRATKLGKLVSRLYIDPLTAAELVDGLRKADEEFTDLGLLHL 520
|
570
....*....|....*...
gi 1844083922 870 IYLTTpydlvsqcnpDWM 887
Cdd:COG1204 521 ILILR----------DWI 528
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
318-1066 |
5.65e-93 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 313.43 E-value: 5.65e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 318 SLPSKVRDLYAQfKGIEKLYEWQHTCLTlNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKdVLMILPYVAIVQEK 397
Cdd:PRK02362 7 PLPEGVIEFYEA-EGIEELYPPQAEAVE-AGLLDGKNLLAAIPTASGKTLIAELAMLKAIARGGK-ALYIVPLRALASEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 398 ---ISGLSSFGIELGFfveeyagSKGRFpptKRRE----KKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGE 470
Cdd:PRK02362 84 feeFERFEELGVRVGI-------STGDY---DSRDewlgDNDIIVATSEKVDSLLRN--GAPWLDDITCVVVDEVHLIDS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 471 GSRGATLEMTLAKILYTSKTTQIIGMSATLNNVEDLQKFLQAEYYTSQFRPVELKEYLKINDTIYEVDSKAEngmtfsrl 550
Cdd:PRK02362 152 ANRGPTLEVTLAKLRRLNPDLQVVALSATIGNADELADWLDAELVDSEWRPIDLREGVFYGGAIHFDDSQRE-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 551 lnykysdtLKKMDPDHLVALVTEVI-PNYSCLVFCPSKKNCENVAEMICKFLSKEYLKHKEKEKCEVIKNLKNIGNGNLC 629
Cdd:PRK02362 224 --------VEVPSKDDTLNLVLDTLeEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVSDTETS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 630 PVLKRTIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLPARRVILR-----------APYVAKEflkr 698
Cdd:PRK02362 296 KDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRdyrrydggagmQPIPVLE---- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 699 nqYKQMIGRAGRAGIDTIGESILIlqEKDKQQVLEL----ITKPLENCYSHLVQEftKGIQTLFLSLIGLKIATNLDDIY 774
Cdd:PRK02362 372 --YHQMAGRAGRPGLDPYGEAVLL--AKSYDELDELferyIWADPEDVRSKLATE--PALRTHVLSTIASGFARTRDGLL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 775 HFMNGTFFGVQQKvllKEKSLWEITVESLRYLTEKGLLQKDtiyksEEEVqynfHITKLGRasfkgTIDLAYCDILY-RD 853
Cdd:PRK02362 446 EFLEATFYATQTD---DTGRLERVVDDVLDFLERNGMIEED-----GETL----EATELGH-----LVSRLYIDPLSaAE 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 854 LKKGLEGLVLES---LLHLIYLTtpydlvsqcnPD-WMIYFRqfsqlSPAEQNVAAILGVSES-FIGKKASgqaigkkVD 928
Cdd:PRK02362 509 IIDGLEAAKKPTdlgLLHLVCST----------PDmYELYLR-----SGDYEWLNEYLYEHEDeLLGDVPS-------EF 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 929 KNVVNRLYLSFVLYTLLKETNIWTVSE-----KFNMPRGYIQN-------LLTGTASFSScvlhfceELEEFWVYRAllV 996
Cdd:PRK02362 567 EDDEFEDFLSAVKTALLLEDWIDEVDEeriteRYGVGPGDIRGkvetaewLLHAAERLAS-------ELDLDLARAA--R 637
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 997 ELTKKLTYCVKAELIPLMEVTGVLEGRAKQLYSAGYKSLMHLANANPEVLVRTidhLSRRQAKQIVSSAK 1066
Cdd:PRK02362 638 ELEKRVEYGVREELLDLVGLRGVGRVRARRLYNAGIESRADLRAADKSVVLAI---LGEKIAENILEQAG 704
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
331-1048 |
2.81e-61 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 223.54 E-value: 2.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 331 KGIEKLYEWQHTCLTlNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKISGLSSFGiELGF 410
Cdd:PRK00254 19 RGIEELYPPQAEALK-SGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGGKAVYLVPLKALAEEKYREFKDWE-KLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 411 FVeeyAGSKGRFPPTKR-REKKSLYIATIEKghslVNSLIETGR--IDSLGLVVVDELHMIGEGSRGATLEMTLAKILyt 487
Cdd:PRK00254 97 RV---AMTTGDYDSTDEwLGKYDIIIATAEK----FDSLLRHGSswIKDVKLVVADEIHLIGSYDRGATLEMILTHML-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 488 sKTTQIIGMSATLNNVEDLQKFLQAEYYTSQFRPVELKEYLKINDTIYEVDSKAENGMTFSRLLNYkysDTLKKmdpdhl 567
Cdd:PRK00254 168 -GRAQILGLSATVGNAEELAEWLNAELVVSDWRPVKLRKGVFYQGFLFWEDGKIERFPNSWESLVY---DAVKK------ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 568 valvtevipNYSCLVFCPSKKNCENVAEMICKFLSKEYLKHKEKEKCEVIKNLK-NIGNGNLcpvlKRTIPFGVAYHHSG 646
Cdd:PRK00254 238 ---------GKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKELADSLEeNPTNEKL----KKALRGGVAFHHAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 647 LTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLPARRVILRAPYVAKEF----LKRNQYKQMIGRAGRAGIDTIGESILI 722
Cdd:PRK00254 305 LGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFgwedIPVLEIQQMMGRAGRPKYDEVGEAIIV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 723 LQEKDKQQVLE--LITKPlENCYSHLVQEftKGIQTLFLSLIGLKIATNLDDIYHFMNGTFFGVQQkvllKEKSLWEITV 800
Cdd:PRK00254 385 ATTEEPSKLMEryIFGKP-EKLFSMLSNE--SAFRSQVLALITNFGVSNFKELVNFLERTFYAHQR----KDLYSLEEKA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 801 ESLRYLtekgLLQKDTIyksEEEVQYNFHITKLGRASFKGTIDlaycDILYRDLKKGLEGLVLE----SLLHLIYLT--- 873
Cdd:PRK00254 458 KEIVYF----LLENEFI---DIDLEDRFIPLPLGIRTSQLYID----PLTAKKFKDAFPKIEKNpnplGIFQLIASTpdm 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 874 TPYDLVSQCNPDWMIYFRQFsqlspaEQNVAAILGVSESFIGKKASGQAIGKKvdknvvnrlylsfVLYTLLKETNIWTV 953
Cdd:PRK00254 527 TPLNYSRKEMEDLLDEAYEM------EDRLYFNIPYWEDYKFQKFLRAFKTAK-------------VLLDWINEVPEGEI 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 954 SEKFNMPRGYIQNLLtgtasfsscvlhfceELEEFWVYRalLVELTK-----------------KLTYCVKAELIPLMEV 1016
Cdd:PRK00254 588 VETYNIDPGDLYRIL---------------ELADWLMYS--LIELYKlfepkqevldyletlhlRVKHGVREELLELMRL 650
|
730 740 750
....*....|....*....|....*....|..
gi 1844083922 1017 TGVLEGRAKQLYSAGYKSLMHLANANPEVLVR 1048
Cdd:PRK00254 651 PMIGRKRARALYNAGFRSIEDIVNAKPSELLK 682
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
339-1072 |
2.72e-56 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 207.81 E-value: 2.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 339 WQHTCLTLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVlMILPYVAIVQEKISGLSSFGiELGFFVEEYAGS 418
Cdd:PRK01172 24 YDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSI-YIVPLRSLAMEKYEELSRLR-SLGMRVKISIGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 419 KGRFPPTKRRekKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSA 498
Cdd:PRK01172 102 YDDPPDFIKR--YDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSARYVNPDARILALSA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 499 TLNNVEDLQKFLQAEYYTSQFRPVELKEYLKINDTIYeVDSKAENGMTFSRLLNYKYSDtlkkmdpdhlvalvtevipNY 578
Cdd:PRK01172 178 TVSNANELAQWLNASLIKSNFRPVPLKLGILYRKRLI-LDGYERSQVDINSLIKETVND-------------------GG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 579 SCLVFCPSKKNCENVAEMICKFLSKeylkhkekekcevIKNLK-NIGNGNLCP-VLKRTIPFGVAYHHSGLTSDERKLLE 656
Cdd:PRK01172 238 QVLVFVSSRKNAEDYAEMLIQHFPE-------------FNDFKvSSENNNVYDdSLNEMLPHGVAFHHAGLSNEQRRFIE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 657 EAYSTGVLCLFTCTSTLAAGVNLPARRVIL----RAPYVAKEFLKRNQYKQMIGRAGRAGIDTIGESILILQEKDKQQVL 732
Cdd:PRK01172 305 EMFRNRYIKVIVATPTLAAGVNLPARLVIVrditRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYIYAASPASYDAA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 733 -ELITKPLENCYSHLVQEFTKGIQTlfLSLIGLKIATNLDDIYHFMNGTFFGVQQKVLLKEKSLweitVESLRYLTEKGL 811
Cdd:PRK01172 385 kKYLSGEPEPVISYMGSQRKVRFNT--LAAISMGLASSMEDLILFYNETLMAIQNGVDEIDYYI----ESSLKFLKENGF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 812 LQKDTIYKSeeevqynfhiTKLGRAsfkgTIDLaYCDIlyrdlkkgleglvlESLLHLI-YLTTPYDLvsqcnpDWMIYF 890
Cdd:PRK01172 459 IKGDVTLRA----------TRLGKL----TSDL-YIDP--------------ESALILKsAFDHDYDE------DLALYY 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 891 RQFS-QLSPAE-QNVAAILGVSESfIGkkasgqaigkKVDKNvVNRLYLSFVLYTLLKETNIWTVSEKFNMPRGYIQNLL 968
Cdd:PRK01172 504 ISLCrEIIPANtRDDYYAMEFLED-IG----------VIDGD-ISAAKTAMVLRGWISEASMQKITDTYGIAPGDVQARA 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 969 TGTASFSSCVLHFCEeleefwVY----RALLVELTKKLTYCVKAELIPLMEVTGVLEGRAKQLYSAGYKSLMHLANANPE 1044
Cdd:PRK01172 572 SSADWISYSLARLSS------IYkpemRRKLEILNIRIKEGIREDLIDLVLIPKVGRVRARRLYDAGFKTVDDIARSSPE 645
|
730 740
....*....|....*....|....*...
gi 1844083922 1045 vLVRTIDHLSRRQAKQIVSSAKMLLHEK 1072
Cdd:PRK01172 646 -RIKKIYGFSDTLANAIVNRAMKISSMY 672
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
520-722 |
1.46e-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: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 520 RPVELKEYLKIndtiyevdskaengmtFSRLLNYKYSDTLKKMDPDHLVALVTEVIPNY-SCLVFCPSKKNCENVAEMIc 598
Cdd:cd18795 1 RPVPLEEYVLG----------------FNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGkPVLVFCSSRKECEKTAKDL- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 599 kflskeylkhkekekceviknlknigngnlcpvlkrtipFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVN 678
Cdd:cd18795 64 ---------------------------------------AGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVN 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1844083922 679 LPARRVILRAPYVAK----EFLKRNQYKQMIGRAGRAGIDTIGESILI 722
Cdd:cd18795 105 LPARTVIIKGTQRYDgkgyRELSPLEYLQMIGRAGRPGFDTRGEAIIM 152
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
336-514 |
2.52e-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: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 336 LYEWQHTCLTLnSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKISGLSSFGIELGFFVEEY 415
Cdd:cd17921 2 LNPIQREALRA-LYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 416 AGSKGRFPptKRREKKSLYIATIEKGHSLVNSLIETGrIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIG 495
Cdd:cd17921 81 TGDPSVNK--LLLAEADILVATPEKLDLLLRNGGERL-IQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRINKNARFVG 157
|
170
....*....|....*....
gi 1844083922 496 MSATLNNVEDLQKFLQAEY 514
Cdd:cd17921 158 LSATLPNAEDLAEWLGVED 176
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
320-740 |
7.58e-32 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 133.91 E-value: 7.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 320 PSKVRDLYAQFKGIE-----KLYEWQHT-CLTLNSvqeRKNLIYSLPTSGGKTLVAEI---LMLQEllccRKDVLMILPY 390
Cdd:COG4581 5 PARADARLEALADFAeergfELDPFQEEaILALEA---GRSVLVAAPTGSGKTLVAEFaifLALAR----GRRSFYTAPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 391 VAIVQEKisglssfgielgFF--VEEYAGSK-----GRfppTKRREKKSLYIATIEkghSLVNSLIETGR-IDSLGLVVV 462
Cdd:COG4581 78 KALSNQK------------FFdlVERFGAENvglltGD---ASVNPDAPIVVMTTE---ILRNMLYREGAdLEDVGVVVM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 463 DELHMIGEGSRGATLEmtlAKILYTSKTTQIIGMSATLNNVEDLQKFLQA-----EYYTSQFRPVELKEYLKINDTIYEV 537
Cdd:COG4581 140 DEFHYLADPDRGWVWE---EPIIHLPARVQLVLLSATVGNAEEFAEWLTRvrgetAVVVSEERPVPLEFHYLVTPRLFPL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 538 DSKAENGMTFSRLlnykySDTLKKMDPDHLValvteviPNYsclVFCPSKKNCENVAEMIckfLSKEYLKHKEKEK-CEV 616
Cdd:COG4581 217 FRVNPELLRPPSR-----HEVIEELDRGGLL-------PAI---VFIFSRRGCDEAAQQL---LSARLTTKEERAEiREA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 617 IKNLKNIGNGNLCPVLKRTIPFGVAYHHSGLTSDERKLLEEAYSTG---VLClftCTSTLAAGVNLPARRVIL------- 686
Cdd:COG4581 279 IDEFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGllkVVF---ATDTLAVGINMPARTVVFtklskfd 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083922 687 ---RAPYVAKEFLkrnqykQMIGRAGRAGIDTIGESILILQE-KDKQQVLELITKPLE 740
Cdd:COG4581 356 gerHRPLTAREFH------QIAGRAGRRGIDTEGHVVVLAPEhDDPKKFARLASARPE 407
|
|
| HTH_61 |
pfam20470 |
Helix-turn-helix domain; This entry represents a presumed helix-turn-helix domain found in DNA ... |
717-813 |
2.93e-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: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 717 GESILILQEKDKQQVLELITKPLENCYSHLVQEfTKGIQTLFLSLIGLKIATNLDDIYHFMNGTFFGVQQKVLLKEKSlw 796
Cdd:pfam20470 1 GESILICKEKDLEKVAELLRAELPPVYSCLLPE-KRGIKRALLEIIALGLATSPEDVDEYMSCTLLSVQQKELDVEKS-- 77
|
90
....*....|....*..
gi 1844083922 797 eiTVESLRYLTEKGLLQ 813
Cdd:pfam20470 78 --IESSLEELVENGLIT 92
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
353-517 |
2.23e-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: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 353 KNLIYSLPTSGGKTLVAEILMLQELLCCRKdVLMILPYVAIVQEKISGLSSFGiELGFFVeeyAGSKGRFPPTKRREKKS 432
Cdd:cd18028 18 ENLLISIPTASGKTLIAEMAMVNTLLEGGK-ALYLVPLRALASEKYEEFKKLE-EIGLKV---GISTGDYDEDDEWLGDY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 433 -LYIATIEKGHSLVNSLIEtgRIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSATLNNVEDLQKFLQ 511
Cdd:cd18028 93 dIIVATYEKFDSLLRHSPS--WLRDVGVVVVDEIHLISDEERGPTLESIVARLRRLNPNTQIIGLSATIGNPDELAEWLN 170
|
....*.
gi 1844083922 512 AEYYTS 517
Cdd:cd18028 171 AELVES 176
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
351-728 |
1.53e-22 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 104.20 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 351 ERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIV-------QEKISGLSSFGIELGffVEEYAGSKGRFP 423
Cdd:COG1202 224 EGKDQLVVSATATGKTLIGELAGIKNALEGKGKMLFLVPLVALAnqkyedfKDRYGDGLDVSIRVG--ASRIRDDGTRFD 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 424 PtkrreKKSLYIATIEkGhslVNSLIETGR-IDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSATLNN 502
Cdd:COG1202 302 P-----NADIIVGTYE-G---IDHALRTGRdLGDIGTVVIDEVHMLEDPERGHRLDGLIARLKYYCPGAQWIYLSATVGN 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 503 VEDLQKFLQAEYYTSQFRPVELKEYLkindtiyevdskaengmTFSRllNYKYSDTLKKmdpdhlvaLVTEVIPNYS--- 579
Cdd:COG1202 373 PEELAKKLGAKLVEYEERPVPLERHL-----------------TFAD--GREKIRIINK--------LVKREFDTKSskg 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 580 ----CLVFCPSKKNCENVAemickflskeylkhkekekceviknlknigngnlcpvlkRTIPFGVAYHHSGLTSDERKLL 655
Cdd:COG1202 426 yrgqTIIFTNSRRRCHEIA---------------------------------------RALGYKAAPYHAGLDYGERKKV 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083922 656 EEAYSTGVLCLFTCTSTLAAGVNLPARRVILRAPYVAKEFLKRNQYKQMIGRAGRAGIDTIGEsILILQEKDK 728
Cdd:COG1202 467 ERRFADQELAAVVTTAALAAGVDFPASQVIFDSLAMGIEWLSVQEFHQMLGRAGRPDYHDRGK-VYLLVEPGK 538
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
345-506 |
3.12e-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: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 345 TLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKD--VLMILPYVAIVQEKISGLSSFGIELGFFVE-EYAGSkgr 421
Cdd:pfam00270 7 AIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGpqALVLAPTRELAEQIYEELKKLGKGLGLKVAsLLGGD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 422 fPPTKRREKKS---LYIATIEKghsLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKIlytSKTTQIIGMSA 498
Cdd:pfam00270 84 -SRKEQLEKLKgpdILVGTPGR---LLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL---PKKRQILLLSA 156
|
....*....
gi 1844083922 499 TLN-NVEDL 506
Cdd:pfam00270 157 TLPrNLEDL 165
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
353-499 |
1.14e-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: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 353 KNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKISGLSSF---GIELGFFVEEYAgSKGRFPPTKRRE 429
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSS-AEEREKNKLGDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 430 KksLYIATIEKGHSLVNSLiETGRIDSLGLVVVDELHMIGEGSRGAtLEMTLAKILYTSKTTQIIGMSAT 499
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 ... |
347-521 |
1.45e-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: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 347 NSVQER---------KNLIYSLPTSGGKTLVAEILMLQeLLCCRKD-------VLMILPYVAIVQEKISGL-SSFGiELG 409
Cdd:cd18023 3 NRIQSEvfpdllysdKNFVVSAPTGSGKTVLFELAILR-LLKERNPlpwgnrkVVYIAPIKALCSEKYDDWkEKFG-PLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 410 FFVEEYAGSKGrFPPTKRREKKSLYIATIEKGHSLVNSLIETGR-IDSLGLVVVDELHMIGEgSRGATLEMTLA--KILY 486
Cdd:cd18023 81 LSCAELTGDTE-MDDTFEIQDADIILTTPEKWDSMTRRWRDNGNlVQLVALVLIDEVHIIKE-NRGATLEVVVSrmKTLS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1844083922 487 TSKTT--------QIIGMSATLNNVEDLQKFLQAEY-----YTSQFRP 521
Cdd:cd18023 159 SSSELrgstvrpmRFVAVSATIPNIEDLAEWLGDNPagcfsFGESFRP 206
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
331-517 |
7.13e-14 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 71.75 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 331 KGIEKLYEWQHTCLTLnSVQERKNLIYSLPTSGGKTLVAEILMLQELLCCRKD-VLMILPYVAIVQEKISGLSSFGIELG 409
Cdd:smart00487 4 FGFEPLRPYQKEAIEA-LLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGrVLVLVPTRELAEQWAEELKKLGPSLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 410 FFVEEYAG--SKGRFPPTKRREKKSLYIATIEKGHSLVNSliETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKIlyt 487
Cdd:smart00487 83 LKVVGLYGgdSKREQLRKLESGKTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL--- 157
|
170 180 190
....*....|....*....|....*....|..
gi 1844083922 488 SKTTQIIGMSATLNN--VEDLQKFLQAEYYTS 517
Cdd:smart00487 158 PKNVQLLLLSATPPEeiENLLELFLNDPVFID 189
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
333-510 |
9.14e-14 |
|
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: 71.63 E-value: 9.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 333 IEKLYEWQHTCL----TLNSVQER---------KNLIYSLPTSGGKTLVAEILMLQELLCCRKD----------VLMILP 389
Cdd:cd18019 1 IEELPDWAQPAFegfkSLNRIQSKlfpaafetdENLLLCAPTGAGKTNVALLTILREIGKHRNPdgtinldafkIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 390 YVAIVQEKISGLSSFGIELGFFVEEYAG----SKGRFPPTKrrekksLYIATIEKGHSLVNSLIETGRIDSLGLVVVDEL 465
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGdqqlTKEQISETQ------IIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1844083922 466 HMIGEgSRGATLEMTLAKILYTSKTTQ----IIGMSATLNNVEDLQKFL 510
Cdd:cd18019 155 HLLHD-DRGPVLESIVARTIRQIEQTQeyvrLVGLSATLPNYEDVATFL 202
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
634-712 |
1.36e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.16 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 634 RTIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLP-ARRVILRAPYVAKEflkrnQYKQMIGRAGRAG 712
Cdd:smart00490 8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDLPWSPA-----SYIQRIGRAGRAG 82
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
319-725 |
1.05e-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: 69.09 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 319 LPSKVRDLYAQfKGIEKLYEwqHTCLTLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLccrKD----VLMILPYVAIV 394
Cdd:COG1205 41 LPPELRAALKK-RGIERLYS--HQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL---EDpgatALYLYPTKALA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 395 QEKISGLSSF--GIELGFFVEEYAGSKgrfPPTKRRE--KKSLYIAT--------IEKGHSLVNSLIEtgridSLGLVVV 462
Cdd:COG1205 115 RDQLRRLRELaeALGLGVRVATYDGDT---PPEERRWirEHPDIVLTnpdmlhygLLPHHTRWARFFR-----NLRYVVI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 463 DELHMIgEGSRGATLEMTLAKIL-----YTSKTtQIIGMSATLNNvedlqkflqaeyytsqfrPVELKEYLkINDTIYEV 537
Cdd:COG1205 187 DEAHTY-RGVFGSHVANVLRRLRricrhYGSDP-QFILASATIGN------------------PAEHAERL-TGRPVTVV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 538 DskaENG-----MTFSrLLNYKYSDTLKKMDPDHLVA-LVTE-VIPNYSCLVFCPSKKNCENVAEMICKFLSKEYLKHKe 610
Cdd:COG1205 246 D---EDGsprgeRTFV-LWNPPLVDDGIRRSALAEAArLLADlVREGLRTLVFTRSRRGAELLARYARRALREPDLADR- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 611 kekceviknlknigngnlcpvlkrtipfgVAYHHSGLTSDERKLLEEAYSTG-VLCLFTcTSTLAAGVNLP---ArrVIL 686
Cdd:COG1205 321 -----------------------------VAAYRAGYLPEERREIERGLRSGeLLGVVS-TNALELGIDIGgldA--VVL 368
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1844083922 687 RA-PYvakeflKRNQYKQMIGRAGRAGIDtiGESILILQE 725
Cdd:COG1205 369 AGyPG------TRASFWQQAGRAGRRGQD--SLVVLVAGD 400
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
353-510 |
4.38e-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: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 353 KNLIYSLPTSGGKTLVAEILMLQELlccRK----DVLMILPYVAIVQEKISGLSS-FGIELGFFVEEYAGSKGrfPPTKR 427
Cdd:cd18022 18 NNVLLGAPTGSGKTIAAELAMFRAF---NKypgsKVVYIAPLKALVRERVDDWKKrFEEKLGKKVVELTGDVT--PDMKA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 428 REKKSLYIATIEKGHSLVNSLIETGRIDSLGLVVVDELHMIGEgSRGATLEMTLAKILY----TSKTTQIIGMSATLNNV 503
Cdd:cd18022 93 LADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGS-DRGPVLEVIVSRMNYissqTEKPVRLVGLSTALANA 171
|
....*..
gi 1844083922 504 EDLQKFL 510
Cdd:cd18022 172 GDLANWL 178
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
335-725 |
1.57e-10 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 65.05 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 335 KLYEWQHTCLT---LNSVQERKNLIYSLPTSGGKTLVAeILMLQELLCCRKdVLMILPYVAIV---QEKIsglssfgiel 408
Cdd:COG1061 80 ELRPYQQEALEallAALERGGGRGLVVAPTGTGKTVLA-LALAAELLRGKR-VLVLVPRRELLeqwAEEL---------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 409 gffvEEYAGSKGRFPPTKRREKKsLYIATIekgHSLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKIlyts 488
Cdd:COG1061 148 ----RRFLGDPLAGGGKKDSDAP-ITVATY---QSLARRAHLDELGDRFGLVIIDEAHHAGAPSYRRILEAFPAAY---- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 489 kttqIIGMSATLnnvedlqkflqaeYYTSQfRPVELKEYLKIndtIYEVDSK--AENGM-------------TFSRLLNY 553
Cdd:COG1061 216 ----RLGLTATP-------------FRSDG-REILLFLFDGI---VYEYSLKeaIEDGYlappeyygirvdlTDERAEYD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 554 KYSDTLKK---MDPDHLVALVTEVIPNYS----CLVFCPSKKNCENVAEMIckflskeylkHKEKEKCEVIknlknigng 626
Cdd:COG1061 275 ALSERLREalaADAERKDKILRELLREHPddrkTLVFCSSVDHAEALAELL----------NEAGIRAAVV--------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 627 nlcpvlkrtipfgvayhHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLP-ARRVILRAPYVAkeflkRNQYKQMI 705
Cdd:COG1061 336 -----------------TGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPrLDVAILLRPTGS-----PREFIQRL 393
|
410 420
....*....|....*....|....*...
gi 1844083922 706 GRAGRAG--------IDTIGESILILQE 725
Cdd:COG1061 394 GRGLRPApgkedalvYDFVGNDVPVLEE 421
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
603-712 |
4.94e-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: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 603 KEYLKHKEKEKCEVIKNLKNIGNGNLcpvLKRTIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLP-A 681
Cdd:pfam00271 7 LELLKKERGGKVLIFSQTKKTLEAEL---LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdV 83
|
90 100 110
....*....|....*....|....*....|..
gi 1844083922 682 RRVI-LRAPYvakeflKRNQYKQMIGRAGRAG 712
Cdd:pfam00271 84 DLVInYDLPW------NPASYIQRIGRAGRAG 109
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
345-519 |
5.14e-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: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 345 TLNSVQER---------KNLIYSLPTSGGKTLVAEILMLQELLC-------CRKD---VLMILPYVAIVQEKISGLSSFG 405
Cdd:cd18020 1 RLNRIQSLvfpvayktnENMLICAPTGAGKTNIAMLTILHEIRQhvnqggvIKKDdfkIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 406 IELGFFVEEYAGSkgrFPPTKRREKKSLYIAT-------IEKGHSLVNSLIETGRidslgLVVVDELHMIGEgSRGATLE 478
Cdd:cd18020 81 APLGIKVKELTGD---MQLTKKEIAETQIIVTtpekwdvVTRKSSGDVALSQLVR-----LLIIDEVHLLHD-DRGPVIE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1844083922 479 MTLAKILYTSKTTQ----IIGMSATLNNVEDLQKFLQAEYYTSQF 519
Cdd:cd18020 152 SLVARTLRQVESTQsmirIVGLSATLPNYLDVADFLRVNPYKGLF 196
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
354-506 |
4.11e-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: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 354 NLIYSLPTSGGKTLVAEILMLQellCCRKDVLMILPYVAIVQEKISGL-----SSFGIELGFFVEEYAGSKGRfpPTKRR 428
Cdd:cd18021 21 NVFVGAPTGSGKTVCAELALLR---HWRQNPKGRAVYIAPMQELVDARykdwrAKFGPLLGKKVVKLTGETST--DLKLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 429 EKKSLYIATIEKGHSLVNSLIETGRIDSLGLVVVDELHMIGeGSRGATLEMTLAKILY----TSKTTQIIGMSATLNNVE 504
Cdd:cd18021 96 AKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIG-GENGPVYEVVVSRMRYissqLEKPIRIVGLSSSLANAR 174
|
..
gi 1844083922 505 DL 506
Cdd:cd18021 175 DV 176
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
353-510 |
2.77e-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: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 353 KNLIYSLPTSGGKTLVAEILMLQELLCCRKD---VLMILPYVAI---VQEKISGLSSfGIELGFFVEEYAG--SKGRfpp 424
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALSSLADEPEKgvqVLYISPLKALindQERRLEEPLD-EIDLEIPVAVRHGdtSQSE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 425 tKRREKKS---LYIATIEkghSLVNSLIETGR---IDSLGLVVVDELHMIGEGSRGATLEMTLAKI-LYTSKTTQIIGMS 497
Cdd:cd17922 78 -KAKQLKNppgILITTPE---SLELLLVNKKLrelFAGLRYVVVDEIHALLGSKRGVQLELLLERLrKLTGRPLRRIGLS 153
|
170
....*....|...
gi 1844083922 498 ATLNNVEDLQKFL 510
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 ... |
339-506 |
5.49e-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: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 339 WQHTCLTLNSVQERKNLIYSLPTSGGKTLVAEILMLQELLccrKDV----LMILPYVAIVQEKISGLSSF--GIELGFFV 412
Cdd:cd17923 2 YSHQAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL---RDPgsraLYLYPTKALAQDQLRSLRELleQLGLGIRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 413 EEYAGSkgrfppTKRREKKSLYI--------------ATIEKGHSLVNSLIEtgridSLGLVVVDELHMIgEGSRGATLE 478
Cdd:cd17923 79 ATYDGD------TPREERRAIIRnpprilltnpdmlhYALLPHHDRWARFLR-----NLRYVVLDEAHTY-RGVFGSHVA 146
|
170 180 190
....*....|....*....|....*....|..
gi 1844083922 479 MTLAKIL----YTSKTTQIIGMSATLNNVEDL 506
Cdd:cd17923 147 LLLRRLRrlcrRYGADPQFILTSATIGNPAEH 178
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
460-709 |
7.45e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 50.31 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 460 VVVDELHMIGEGSRGATLEMTLAK---ILYTSktTQIIGMSATLNNVEDLQKFLQAEYYTSQFRPVELKEY-LKINDTIY 535
Cdd:PRK09751 128 VIIDEVHAVAGSKRGAHLALSLERldaLLHTS--AQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRHPqIRIVVPVA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 536 EVDSKAENGmtfSRLLNYKYSDTLKKMDPDHLVALVTEVIPNYSCLVFcpskKNCENVAEMICKFLSKEYLKH--KEKEK 613
Cdd:PRK09751 206 NMDDVSSVA---SGTGEDSHAGREGSIWPYIETGILDEVLRHRSTIVF----TNSRGLAEKLTARLNELYAARlqRSPSI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 614 CEVIKNLKNIgNGNLCPVLKRTIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLPARRVILRA---PY 690
Cdd:PRK09751 279 AVDAAHFEST-SGATSNRVQSSDVFIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVatpLS 357
|
250
....*....|....*....
gi 1844083922 691 VAKEFlkrnqykQMIGRAG 709
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 ... |
579-710 |
7.57e-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: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 579 SCLVFCPSKKNCENVAEmickflskeylkhkekekcevikNLKNigngnLCPvlKRTIPFGVAYHHSGLTSDERKLLEEA 658
Cdd:cd18796 40 STLVFTNTRSQAERLAQ-----------------------RLRE-----LCP--DRVPPDFIALHHGSLSRELREEVEAA 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1844083922 659 YSTGVLCLFTCTSTLAAGVNLPA-RRVI-LRAPYVAKEFLKRnqykqmIGRAGR 710
Cdd:cd18796 90 LKRGDLKVVVATSSLELGIDIGDvDLVIqIGSPKSVARLLQR------LGRSGH 137
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
335-499 |
1.06e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.90 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 335 KLYEWQHTCL--TLNSV--QERKNLIySLPTSGGKTLVAEILM--LQELLCCRKdVLMILPYVAIVQEKISGLSSFGIEL 408
Cdd:pfam04851 3 ELRPYQIEAIenLLESIknGQKRGLI-VMATGSGKTLTAAKLIarLFKKGPIKK-VLFLVPRKDLLEQALEEFKKFLPNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 409 GFFVEEYAGSKGRFPptkrREKKSLYIATIEKGHSLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLEMtlakilytS 488
Cdd:pfam04851 81 VEIGEIISGDKKDES----VDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAHRSGASSYRNILEY--------F 148
|
170
....*....|.
gi 1844083922 489 KTTQIIGMSAT 499
Cdd:pfam04851 149 KPAFLLGLTAT 159
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
460-510 |
1.51e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 49.33 E-value: 1.51e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1844083922 460 VVVDELHMIGEGSRGATLEMTLAKI-LYTSKTTQIIGMSATLNNVEDLQKFL 510
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 ... |
346-511 |
1.85e-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: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 346 LNSVQERKNLIYSLPTSGGKTLVAEIlmlqELLCCRKDVLMILPYVAIVQEKISGLSSFGIELGFFveeyAGSKGRFPPT 425
Cdd:cd17920 21 INAVLAGRDVLVVMPTGGGKSLCYQL----PALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAAL----NSTLSPEEKR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 426 KRREK------KSLYIA--TIEKGH--SLVNSLIETGRIDslgLVVVDELHMI---GEGSRGATLEmtLAKILYTSKTTQ 492
Cdd:cd17920 93 EVLLRikngqyKLLYVTpeRLLSPDflELLQRLPERKRLA---LIVVDEAHCVsqwGHDFRPDYLR--LGRLRRALPGVP 167
|
170 180
....*....|....*....|.
gi 1844083922 493 IIGMSATLNNV--EDLQKFLQ 511
Cdd:cd17920 168 ILALTATATPEvrEDILKRLG 188
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
353-502 |
2.79e-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: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 353 KNLIYSLPTSGGKTLVAEILM---LQELLCCRKD-VLMILPYVAIVQEKISGLSSFGIELGFFVEEYAG---SKGRFPpt 425
Cdd:cd17927 18 KNTIICLPTGSGKTFVAVLICehhLKKFPAGRKGkVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGdtsENVSVE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 426 KRREKKSLYIATiekGHSLVNSLiETGRIDSL---GLVVVDELHM-IGEGS-RGATLEMTLAKILYTSKTTQIIGMSATL 500
Cdd:cd17927 96 QIVESSDVIIVT---PQILVNDL-KSGTIVSLsdfSLLVFDECHNtTKNHPyNEIMFRYLDQKLGSSGPLPQILGLTASP 171
|
..
gi 1844083922 501 NN 502
Cdd:cd17927 172 GV 173
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
352-466 |
4.36e-04 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 44.34 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 352 RKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKISGLSSFgieLGFFVEEYAGSKGRFPPTKRR--- 428
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAERLHKKGGKVLFLAPTKPLVEQHAEFFKEA---LNIPEDEIVVFTGEVSPEKRKelw 93
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1844083922 429 EKKSLYIATIEkghsLVNSLIETGRID--SLGLVVVDELH 466
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 ... |
353-508 |
4.61e-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: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 353 KNLIYSLPTSGGKTLVAEILMLQELlccR-----KDVLMIlPYVAIVQEKISGLSSFGielGFFVEEYAGSKGRFPPTKR 427
Cdd:cd18033 17 QNTLVALPTGLGKTFIAAVVMLNYY---RwfpkgKIVFMA-PTKPLVSQQIEACYKIT---GIPSSQTAELTGSVPPTKR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 428 RE---KKSLYIATiekGHSLVNSLIEtGRID--SLGLVVVDELHMiGEGSRGATleMTLAKILYTSKTTQIIGMSATL-N 501
Cdd:cd18033 90 AElwaSKRVFFLT---PQTLENDLKE-GDCDpkSIVCLVIDEAHR-ATGNYAYC--QVVRELMRYNSHFRILALTATPgS 162
|
....*..
gi 1844083922 502 NVEDLQK 508
Cdd:cd18033 163 KLEAVQQ 169
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
352-516 |
9.02e-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: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 352 RKNLIYSLPTSGGKTLVAEILMLQELLCCRKD------VLMILPYVAIVQEKIsglSSFGIELGFFVEEYAGSKGrfPPT 425
Cdd:cd18034 16 KRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEknpkkrAVFLVPTVPLVAQQA---EAIRSHTDLKVGEYSGEMG--VDK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 426 KRREKKSLYIATIE----KGHSLVNSLIETG-RIDSLGLVVVDELHMIGEGSRGAtlemTLAKILYTSKTTQ----IIGM 496
Cdd:cd18034 91 WTKERWKEELEKYDvlvmTAQILLDALRHGFlSLSDINLLIFDECHHATGDHPYA----RIMKEFYHLEGRTsrprILGL 166
|
170 180 190
....*....|....*....|....*....|.
gi 1844083922 497 SA-----------TLNNVEDLQKFLQAEYYT 516
Cdd:cd18034 167 TAspvngkgdpksVEKKIQQLEELLNSTIKT 197
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
336-500 |
1.11e-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: 40.75 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 336 LYEWQHTCL--TLNSVQERKNLIySLPTSGGKTLVAeILMLQELLCCRkdVLMILPYVAIV---QEKISGLSSfGIELGF 410
Cdd:cd17926 1 LRPYQEEALeaWLAHKNNRRGIL-VLPTGSGKTLTA-LALIAYLKELR--TLIVVPTDALLdqwKERFEDFLG-DSSIGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083922 411 FveeyagskgRFPPTKRREKKSLYIATIEkghSLVNSLIETGRI-DSLGLVVVDELHMIGEGSRGATLEMTLAKILytsk 489
Cdd:cd17926 76 I---------GGGKKKDFDDANVVVATYQ---SLSNLAEEEKDLfDQFGLLIVDEAHHLPAKTFSEILKELNAKYR---- 139
|
170
....*....|.
gi 1844083922 490 ttqiIGMSATL 500
Cdd:cd17926 140 ----LGLTATP 146
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
1013-1066 |
3.49e-03 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 3.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1844083922 1013 LMEVTGVLEGRAKQLYSAGYKSLMHLANANPEVLVRTIDhLSRRQAKQIVSSAK 1066
Cdd:pfam14520 4 LLSISGIGPKTALALLSAGIGTVEDLAEADVDELAEIPG-IGEKTAQRIILELR 56
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
652-722 |
8.20e-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: 8.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083922 652 RKLLEEAYStgVLCLFTCTSTLAAGVNLP-ARRVILRAPYVAKeflkrNQYKQMIGRAGRAGiDTIGESILI 722
Cdd:cd18785 13 IEHAEEIAS--SLEILVATNVLGEGIDVPsLDTVIFFDPPSSA-----ASYIQRVGRAGRGG-KDEGEVILF 76
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
460-524 |
9.03e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 40.25 E-value: 9.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844083922 460 VVVDELHMIGEGSRGATLEMTLAKILY-TSKTTQIIGMSATLNNVEDLQKFLQAEYYTSQFRPVEL 524
Cdd:PRK13767 176 VIVDEIHSLAENKRGVHLSLSLERLEElAGGEFVRIGLSATIEPLEEVAKFLVGYEDDGEPRDCEI 241
|
|
| |
