|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
222-429 |
5.01e-121 |
|
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: 375.54 E-value: 5.01e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 222 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEV-PLPWLNMKIVYMAPIKALCSQRFDDWKEKFGPVG 300
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERnPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 301 LNCKELTGDTVMDDLFEIQHANIIITTPEKWDSVTRKWRDN-SFIQLVRLFLIDEVHVIKdENRGPTLEVVVSRMKTVqS 379
Cdd:cd18023 81 LSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIK-ENRGATLEVVVSRMKTL-S 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720413913 380 LSRDLESASPVPVRFVAVSATIPNAEDIAEWLSDGerPAVCLKMDESHRP 429
Cdd:cd18023 159 SSSELRGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFGESFRP 206
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
206-762 |
2.55e-104 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 342.65 E-value: 2.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 206 VTEIP-AKFRNIFKEFPY--FNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNMKIVYMAPIK 282
Cdd:COG1204 3 VAELPlEKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN------GGKALYIVPLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 283 ALCSQRFDDWKEKFGPVGLNCKELTGDTVMDDLfEIQHANIIITTPEKWDSVTRKwrDNSFIQLVRLFLIDEVHVIKDEN 362
Cdd:COG1204 77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRN--GPSWLRDVDLVVVDEAHLIDDES 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 363 RGPTLEVVVSRMKTVQSlsrdlesaspvPVRFVAVSATIPNAEDIAEWLsdgERPAVclkmDESHRPVKLQKVV-----L 437
Cdd:COG1204 154 RGPTLEVLLARLRRLNP-----------EAQIVALSATIGNAEEIAEWL---DAELV----KSDWRPVPLNEGVlydgvL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 438 GFPCSSSQTEFKFdLALnykvysVIRTYSDQKPTLVFCSTRKGVQQAASVLVKDAKFIISVEQKLRLQKSAYSIR----- 512
Cdd:COG1204 216 RFDDGSRRSKDPT-LAL------ALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLevsee 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 513 ---DSKLKDTLVYGVGYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKSTmHYSGGVfeEYSETDI 589
Cdd:COG1204 289 thtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-KRGGMV--PIPVLEF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 590 LQMIGRAGRPQFDTTATAVIMTRLST-----REKYVqmLACNDTVESSLH--RHLIEHLNAEIVLHTITDVNIALDWIRS 662
Cdd:COG1204 366 KQMAGRAGRPGYDPYGEAILVAKSSDeadelFERYI--LGEPEPIRSKLAneSALRTHLLALIASGFANSREELLDFLEN 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 663 TMLYIRAlknpshygfssglNKDGIEAKLQElclkNLKDLSSLDLIKMDEDvNFKPTEAGRLMAWYYITFETVKKF---- 738
Cdd:COG1204 444 TFYAYQY-------------DKGDLEEVVDD----ALEFLLENGFIEEDGD-RLRATKLGKLVSRLYIDPLTAAELvdgl 505
|
570 580
....*....|....*....|....
gi 1720413913 739 CAISGKETLLDLISMISSCNEFLD 762
Cdd:COG1204 506 RKADEEFTDLGLLHLILILRDWIN 529
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
718-1031 |
5.55e-69 |
|
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.
Pssm-ID: 460740 Cd Length: 307 Bit Score: 234.40 E-value: 5.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 718 PTEAGRLMAWYYITFETVKKFC-AISGKETLLDLISMISSCNEFLDVQLRISEKRILNTLNKdpnriTIRFPMAERIKTR 796
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNqSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLE-----KVPIPVKGDIEDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 797 EMKVNCLIQAQLGCIPIQDFALTQDTVKIFRNGSRIARWLSDfVAAQEKKFAVLLNSVILTKCFKCKLWeNSKHVSKQLD 876
Cdd:pfam02889 76 HAKVNILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFE-ILLSKGWLSAALTALDLCKMIEQRMW-DSDSPLRQFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 877 KIGISLSNTMVNAGLTSFKKIEEANARELELILNRHPPFGTQIKEAVAHLPKYELEVEqIARYSDIKAEILVTIIlRNFE 956
Cdd:pfam02889 154 GIPPELIKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAE-VQPITRSVLRVEVTIT-PDFP 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720413913 957 qlQTKRTAPDFHYATLIIGDADNQVVFKHKIMdSVLLKSGNWVKKIDVKRALISE---DLSINLISSDYVGLDIHQKF 1031
Cdd:pfam02889 232 --WDKRVHGKSEGFWLVVGDSDGNEILHIERF-TLTKRTLAGEHKLEFTVPPSDPgppQLFVRLISDSWLGADQEVPI 306
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
222-415 |
2.24e-67 |
|
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: 224.83 E-value: 2.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 222 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVplpwlNMKIVYMAPIKALCSQRFDDWKEKFGPVGL 301
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-----GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 302 NCKELTGDTVMDDLfEIQHANIIITTPEKWDSVTRKWRDNsFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMKTVQSls 381
Cdd:cd17921 76 NVGLLTGDPSVNKL-LLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRINK-- 151
|
170 180 190
....*....|....*....|....*....|....
gi 1720413913 382 rdlesaspvPVRFVAVSATIPNAEDIAEWLSDGE 415
Cdd:cd17921 152 ---------NARFVGLSATLPNAEDLAEWLGVED 176
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
718-1033 |
6.93e-61 |
|
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl domain) protein in which it was found. This protein is required for assembly of functional endoplasmic reticulum translocons. Other yeast proteins containing this domain include pre-mRNA splicing helicase BRR2, HFM1 protein and putative helicases.
Pssm-ID: 214946 Cd Length: 314 Bit Score: 211.45 E-value: 6.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 718 PTEAGRLMAWYYITFETVKKFCA-ISGKETLLDLISMISSCNEFLDVQLRISEKRILNTLNKDpnritIRFPMAERIKTR 796
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQsLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-----VPIPVKEGIIDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 797 EM-KVNCLIQAQLGCIPIQDFALTQDTVKIFRNGSRIARWLSDfVAAQEKKFAVLLNSVILTKCFKCKLWENSKHVSKQL 875
Cdd:smart00973 76 PHaKVNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVD-IALSKGWLRTALNALDLSQMVVQRLWEDSDSPLKQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 876 DKIGIS--LSNTMVNAGLTSFKKIEEANARELELILNRHPPFGTQIKEAVAHLPKYELEVEQIARYSDIKAEILVTIIlr 953
Cdd:smart00973 155 PHFLIEdvYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITRDLTLRVELEIT-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 954 NFEQLQTKRTAPDFHYATLIIGDADNQVVFKHKIMDSVLLKSGNWVK-KIDVKR-ALISEDLSINLISSDYVGLDIHQKF 1031
Cdd:smart00973 233 PVFAWDLPRHKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKlDFTVPLsEPGPENYTVYLISDSYLGCDQEVSF 312
|
..
gi 1720413913 1032 TV 1033
Cdd:smart00973 313 SL 314
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
220-411 |
1.23e-60 |
|
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: 205.96 E-value: 1.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 220 FPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNMKIVYMAPIKALCSQRFDDWKEKFGPV 299
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNP----KGRAVYIAPMQELVDARYKDWRAKFGPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 300 -GLNCKELTGDTVMdDLFEIQHANIIITTPEKWDSVTRKWRDNSFIQLVRLFLIDEVHVIKDENrGPTLEVVVSRMKTVQ 378
Cdd:cd18021 77 lGKKVVKLTGETST-DLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGEN-GPVYEVVVSRMRYIS 154
|
170 180 190
....*....|....*....|....*....|...
gi 1720413913 379 SlsrDLESaspvPVRFVAVSATIPNAEDIAEWL 411
Cdd:cd18021 155 S---QLEK----PIRIVGLSSSLANARDVGEWL 180
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
428-612 |
4.03e-60 |
|
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: 203.17 E-value: 4.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 428 RPVKLQKVVLGFPCSSSQTEFKFDL--ALNYKVYSVIRTYSDQKPTLVFCSTRKGVQQAASVLVkdakfiisveqklrlq 505
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNkfDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 506 ksaysirdsklkdtlvyGVGYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKSTMHYSGGVFEEYS 585
Cdd:cd18795 65 -----------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELS 127
|
170 180
....*....|....*....|....*..
gi 1720413913 586 ETDILQMIGRAGRPQFDTTATAVIMTR 612
Cdd:cd18795 128 PLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
222-411 |
1.41e-59 |
|
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: 202.99 E-value: 1.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 222 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNMKIVYMAPIKALCSQRFDDWKEKF-GPVG 300
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYP----GSKVVYIAPLKALVRERVDDWKKRFeEKLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 301 LNCKELTGDtVMDDLFEIQHANIIITTPEKWDSVTRKWRDNSFIQLVRLFLIDEVHVIKDEnRGPTLEVVVSRMKTVQSL 380
Cdd:cd18022 77 KKVVELTGD-VTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSD-RGPVLEVIVSRMNYISSQ 154
|
170 180 190
....*....|....*....|....*....|.
gi 1720413913 381 SRdlesaspVPVRFVAVSATIPNAEDIAEWL 411
Cdd:cd18022 155 TE-------KPVRLVGLSTALANAGDLANWL 178
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
227-738 |
1.41e-55 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 207.36 E-value: 1.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 227 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAIT-RLLMEvplpwlNMKIVYMAPIKALCSQRFDDWKEkFGPVGLNCKE 305
Cdd:PRK00254 28 QAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVnKLLRE------GGKAVYLVPLKALAEEKYREFKD-WEKLGLRVAM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 306 LTGDTVMDDLFeIQHANIIITTPEKWDSVTRkwRDNSFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMktvqsLSRdle 385
Cdd:PRK00254 101 TTGDYDSTDEW-LGKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHM-----LGR--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 386 saspvpVRFVAVSATIPNAEDIAEWLSdgerpAVCLKMDesHRPVKLQKVV--LGFPCSSSQTEFKFDLALNYKVYSVIR 463
Cdd:PRK00254 170 ------AQILGLSATVGNAEELAEWLN-----AELVVSD--WRPVKLRKGVfyQGFLFWEDGKIERFPNSWESLVYDAVK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 464 TysdQKPTLVFCSTRKGVQQAASVLVKDAKFIISVEQKLRLQKSAYSIRDS----KLKDTLVYGVGYHHAGMELSDRKLV 539
Cdd:PRK00254 237 K---GKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKELADSLEENptneKLKKALRGGVAFHHAGLGRTERVLI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 540 EGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKSTMHYSGGVFEEYSETDILQMIGRAGRPQFDTTATAVIMTR------- 612
Cdd:PRK00254 314 EDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATteepskl 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 613 -----LSTREKYVQMLACndtvESSLHRHLIehlnAEIVLHTITDVNIALDWIRSTmLYIRALKNPSHygfssglnkdgI 687
Cdd:PRK00254 394 meryiFGKPEKLFSMLSN----ESAFRSQVL----ALITNFGVSNFKELVNFLERT-FYAHQRKDLYS-----------L 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1720413913 688 EAKLQELCLKNLKDlsslDLIKMDEDVNFKPTEAGRLMAWYYITFETVKKF 738
Cdd:PRK00254 454 EEKAKEIVYFLLEN----EFIDIDLEDRFIPLPLGIRTSQLYIDPLTAKKF 500
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
227-610 |
3.47e-53 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 200.55 E-value: 3.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 227 QSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNMKIVYMAPIKALCSQRFDDWKEKFGP--VGLnck 304
Cdd:COG4581 30 QEEAILALE-AGRSVLVAAPTGSGKTLVAEFAIFLALAR------GRRSFYTAPIKALSNQKFFDLVERFGAenVGL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 305 eLTGDTVmddlfEIQHANIIITTPEkwdsVTRKW--RDNSFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMktvqslsr 382
Cdd:COG4581 100 -LTGDAS-----VNPDAPIVVMTTE----ILRNMlyREGADLEDVGVVVMDEFHYLADPDRGWVWEEPIIHL-------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 383 dlesasPVPVRFVAVSATIPNAEDIAEWLSD--GErpavCLKMDESHRPVKL-QKVVLG---FPCSSSQTEFKFDLALNY 456
Cdd:COG4581 162 ------PARVQLVLLSATVGNAEEFAEWLTRvrGE----TAVVVSEERPVPLeFHYLVTprlFPLFRVNPELLRPPSRHE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 457 KVYSVIRTysDQKPTLVFCSTRKGVQQAASVLVkdAKFIISVEQKLRL-------QKSAYSIRDSKLKDTLVYGVGYHHA 529
Cdd:COG4581 232 VIEELDRG--GLLPAIVFIFSRRGCDEAAQQLL--SARLTTKEERAEIreaidefAEDFSVLFGKTLSRLLRRGIAVHHA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 530 GMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKSTMHYSGGVFEEYSETDILQMIGRAGRPQFDTTATAVI 609
Cdd:COG4581 308 GMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDTEGHVVV 387
|
.
gi 1720413913 610 M 610
Cdd:COG4581 388 L 388
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
206-411 |
5.28e-50 |
|
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: 176.41 E-value: 5.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 206 VTEIPAKFRNIFKEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWL-----NMKIVYMAP 280
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGtinldAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 281 IKALCSQRFDDWKEKFGPVGLNCKELTGDTVMDDLfEIQHANIIITTPEKWDSVTRKWRDNSFIQLVRLFLIDEVHVIKD 360
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKE-QISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720413913 361 EnRGPTLEVVVSRmkTVQSLSRDLEsaspvPVRFVAVSATIPNAEDIAEWL 411
Cdd:cd18019 160 D-RGPVLESIVAR--TIRQIEQTQE-----YVRLVGLSATLPNYEDVATFL 202
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
227-610 |
3.58e-49 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 188.24 E-value: 3.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 227 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNMKIVYMAPIKALCSQRFDDWKEkFGPVGLNCKEL 306
Cdd:PRK02362 28 QAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIAR------GGKALYIVPLRALASEKFEEFER-FEELGVRVGIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 307 TGDTVMDDlfEIQHAN-IIITTPEKWDSVTRKwrDNSFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMKtvqSLSRDLE 385
Cdd:PRK02362 101 TGDYDSRD--EWLGDNdIIVATSEKVDSLLRN--GAPWLDDITCVVVDEVHLIDSANRGPTLEVTLAKLR---RLNPDLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 386 saspvpvrFVAVSATIPNAEDIAEWLsDGERpavclkMDESHRPVKLQKVVL---GFPCSSSQTEFKF-----DLALnyk 457
Cdd:PRK02362 174 --------VVALSATIGNADELADWL-DAEL------VDSEWRPIDLREGVFyggAIHFDDSQREVEVpskddTLNL--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 458 vysVIRTYSDQKPTLVFCSTRKGVQQAASVLVKDAKFIISVEQKLRLQKSAYSIRDS-------KLKDTLVYGVGYHHAG 530
Cdd:PRK02362 236 ---VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVsdtetskDLADCVAKGAAFHHAG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 531 MELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKSTMHYSGG-------VFeEYSetdilQMIGRAGRPQFDT 603
Cdd:PRK02362 313 LSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGagmqpipVL-EYH-----QMAGRAGRPGLDP 386
|
....*..
gi 1720413913 604 TATAVIM 610
Cdd:PRK02362 387 YGEAVLL 393
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
210-734 |
4.04e-44 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 171.99 E-value: 4.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 210 PAKFRNIFKEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNMKIVYMAPIKALCSQRF 289
Cdd:PRK01172 9 DDEFLNLFTGNDFELYDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLA------GLKSIYIVPLRSLAMEKY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 290 DDWKeKFGPVGLNCKELTGDtvMDDLFE-IQHANIIITTPEKWDSVTRkwRDNSFIQLVRLFLIDEVHVIKDENRGPTLE 368
Cdd:PRK01172 83 EELS-RLRSLGMRVKISIGD--YDDPPDfIKRYDVVILTSEKADSLIH--HDPYIINDVGLIVADEIHIIGDEDRGPTLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 369 VVVSRMKTVQSlsrdlesaspvPVRFVAVSATIPNAEDIAEWLSdgerpAVCLKmdESHRPVKLQKVVLGFPCSSSQTEF 448
Cdd:PRK01172 158 TVLSSARYVNP-----------DARILALSATVSNANELAQWLN-----ASLIK--SNFRPVPLKLGILYRKRLILDGYE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 449 KFDLALNykvySVIR-TYSDQKPTLVFCSTRKGVQQAASVLVK----DAKFIISVEQKlrlqksaySIRDSKLKDTLVYG 523
Cdd:PRK01172 220 RSQVDIN----SLIKeTVNDGGQVLVFVSSRKNAEDYAEMLIQhfpeFNDFKVSSENN--------NVYDDSLNEMLPHG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 524 VGYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKSTMHYSGGVFEEYSETDILQMIGRAGRPQFDT 603
Cdd:PRK01172 288 VAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGRAGRPGYDQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 604 TATAVImtrlstrekYVQMLACNDTVESSLHRH---LIEHLNAEIVLHTITDVNIALDWIRStMLYIRALKNPSHYGFSS 680
Cdd:PRK01172 368 YGIGYI---------YAASPASYDAAKKYLSGEpepVISYMGSQRKVRFNTLAAISMGLASS-MEDLILFYNETLMAIQN 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1720413913 681 GlnKDGIEAKLQElclkNLKDLSSLDLIKmdEDVNFKPTEAGRLMAWYYITFET 734
Cdd:PRK01172 438 G--VDEIDYYIES----SLKFLKENGFIK--GDVTLRATRLGKLTSDLYIDPES 483
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
224-411 |
2.94e-41 |
|
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: 150.66 E-value: 2.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 224 NYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLME--VPLPWL---NMKIVYMAPIKALCSQRFDDWKEKFGP 298
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQhvNQGGVIkkdDFKIVYIAPMKALAAEMVEKFSKRLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 299 VGLNCKELTGDTVMDDLfEIQHANIIITTPEKWDSVTRKWR-DNSFIQLVRLFLIDEVHVIKDEnRGPTLEVVVSRMKtv 377
Cdd:cd18020 83 LGIKVKELTGDMQLTKK-EIAETQIIVTTPEKWDVVTRKSSgDVALSQLVRLLIIDEVHLLHDD-RGPVIESLVARTL-- 158
|
170 180 190
....*....|....*....|....*....|....
gi 1720413913 378 qslsRDLESASPVpVRFVAVSATIPNAEDIAEWL 411
Cdd:cd18020 159 ----RQVESTQSM-IRIVGLSATLPNYLDVADFL 187
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
222-411 |
1.09e-39 |
|
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: 145.55 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 222 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNMKIVYMAPIKALCSQRFDDWKeKFGPVGL 301
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLE------GGKALYLVPLRALASEKYEEFK-KLEEIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 302 NCKELTGDTVMDDLFeIQHANIIITTPEKWDSVTR-KWrdnSFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMKTVQSl 380
Cdd:cd18028 74 KVGISTGDYDEDDEW-LGDYDIIVATYEKFDSLLRhSP---SWLRDVGVVVVDEIHLISDEERGPTLESIVARLRRLNP- 148
|
170 180 190
....*....|....*....|....*....|.
gi 1720413913 381 srdlesaspvPVRFVAVSATIPNAEDIAEWL 411
Cdd:cd18028 149 ----------NTQIIGLSATIGNPDELAEWL 169
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
226-407 |
3.11e-36 |
|
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: 135.06 E-value: 3.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 226 IQSKAFDdLLYTDRNFVICAPTGSGKTVVFELAItrlLMEVPLPWLNMKIVYMAPIKALCSQRFDDWKEKFGPVGLN-CK 304
Cdd:pfam00270 3 IQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPA---LEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKvAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 305 ELTGDTVMDDLFEIQHANIIITTPEKWDSVTRKWRdnsFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMktvqslsrdl 384
Cdd:pfam00270 79 LLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL---------- 145
|
170 180
....*....|....*....|....
gi 1720413913 385 esasPVPVRFVAVSATIP-NAEDI 407
Cdd:pfam00270 146 ----PKKRQILLLSATLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
218-411 |
3.15e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 110.66 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 218 KEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPwlnmKIVYMAPIKALCSQRFDDWKEKFG 297
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGG----RVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 298 PVGLN-CKELTGDTVMDDLFEIQH--ANIIITTPEKWDSVTRKwrDNSFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRM 374
Cdd:smart00487 80 SLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720413913 375 ktvqslsrdlesasPVPVRFVAVSATIPNAEDIAEWL 411
Cdd:smart00487 158 --------------PKNVQLLLLSATPPEEIENLLEL 180
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
209-601 |
6.68e-27 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 118.84 E-value: 6.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 209 IPAKFRNIFK-EFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELA-ITRLLMEvplpwlNMKIVYMAPIKALCS 286
Cdd:COG1202 195 LPPELKDLLEgRGEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAgIKNALEG------KGKMLFLVPLVALAN 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 287 QRFDDWKEKFGP-------VGLN-CKELTGDTVMDdlfeiqhANIIITTPEKWDSVTRKWRDNSFIQLVrlfLIDEVHVI 358
Cdd:COG1202 269 QKYEDFKDRYGDgldvsirVGASrIRDDGTRFDPN-------ADIIVGTYEGIDHALRTGRDLGDIGTV---VIDEVHML 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 359 KDENRGPTLEVVVSRMKTVqslsrdLESAspvpvRFVAVSATIPNAEDIAEWLSdgerpavcLKMDE-SHRPVKLQKVVL 437
Cdd:COG1202 339 EDPERGHRLDGLIARLKYY------CPGA-----QWIYLSATVGNPEELAKKLG--------AKLVEyEERPVPLERHLT 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 438 gFpcssSQTEFKFDLA--LNYKVYSVIRTYSDQKPTLVFCSTRKgvqqaasvlvkdakfiisveqklrlqksaysiRDSK 515
Cdd:COG1202 400 -F----ADGREKIRIInkLVKREFDTKSSKGYRGQTIIFTNSRR--------------------------------RCHE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 516 LKDTLVYGVGYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKS-TMhysGGvfEEYSETDILQMIG 594
Cdd:COG1202 443 IARALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSlAM---GI--EWLSVQEFHQMLG 517
|
....*..
gi 1720413913 595 RAGRPQF 601
Cdd:COG1202 518 RAGRPDY 524
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
227-598 |
8.05e-23 |
|
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: 105.69 E-value: 8.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 227 QSKAFDdLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPwlnmKIVYMAPIKALCS---QRFDDWKEKFGPvGLNC 303
Cdd:COG1205 61 QAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA----TALYLYPTKALARdqlRRLRELAEALGL-GVRV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 304 KELTGDTVMDDLFEI-QHANIIITTPEKWDS----VTRKWRdnSFIQLVRLFLIDEVHVIkdenRGptleV-------VV 371
Cdd:COG1205 135 ATYDGDTPPEERRWIrEHPDIVLTNPDMLHYgllpHHTRWA--RFFRNLRYVVIDEAHTY----RG----VfgshvanVL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 372 SRMKTVqslsRDLESASPVpvrFVAVSATIPNAEDIAEWLSDgeRPAVCLkmDESHRPVKLQKVVLGFPC-------SSS 444
Cdd:COG1205 205 RRLRRI----CRHYGSDPQ---FILASATIGNPAEHAERLTG--RPVTVV--DEDGSPRGERTFVLWNPPlvddgirRSA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 445 QTEFKfDLALNYkvysvirTYSDQKpTLVFCSTRKGVQQAASVLvkdakfiisveqKLRLQKSAYSIRdsklkdtlvygV 524
Cdd:COG1205 274 LAEAA-RLLADL-------VREGLR-TLVFTRSRRGAELLARYA------------RRALREPDLADR-----------V 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720413913 525 GYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPA-HLVVIkstMHYSGGVfeeyseTDILQMIGRAGR 598
Cdd:COG1205 322 AAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVVL---AGYPGTR------ASFWQQAGRAGR 387
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
218-412 |
3.91e-20 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350782 [Multi-domain] Cd Length: 205 Bit Score: 90.20 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 218 KEFPY-FNYIQSKAFDDLlytDRN--FVICAPTGSGKTVVFELAITRLLMEvplpwlNMKIVYMAPIKALCSQRFDDWKE 294
Cdd:cd18024 27 RTYPFtLDPFQKTAIACI---ERNesVLVSAHTSAGKTVVAEYAIAQSLRD------KQRVIYTSPIKALSNQKYRELQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 295 KFGPVGLnckeLTGDTVMDdlfeiQHANIIITTPEKWDSVTrkWRDNSFIQLVRLFLIDEVHVIKDENRGPTLEvvvsrm 374
Cdd:cd18024 98 EFGDVGL----MTGDVTIN-----PNASCLVMTTEILRSML--YRGSEIMREVAWVIFDEIHYMRDKERGVVWE------ 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720413913 375 KTVQSLsrdlesasPVPVRFVAVSATIPNAEDIAEWLS 412
Cdd:cd18024 161 ETIILL--------PDKVRYVFLSATIPNARQFAEWIC 190
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
227-411 |
1.36e-19 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 87.71 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 227 QSKAFDDLLYTDRNFViCAPTGSGKTVVFELAITrllmevpLPWLNM-KIVYMAPIKALCSQRFDDWKEKFGPVGLncke 305
Cdd:cd18027 13 QKQAILHLEAGDSVFV-AAHTSAGKTVVAEYAIA-------LAQKHMtRTIYTSPIKALSNQKFRDFKNTFGDVGL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 306 LTGDTVMDdlfeiQHANIIITTPEKWDSVTrkWRDNSFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMktvqslsrdle 385
Cdd:cd18027 81 ITGDVQLN-----PEASCLIMTTEILRSML--YNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIML----------- 142
|
170 180
....*....|....*....|....*.
gi 1720413913 386 sasPVPVRFVAVSATIPNAEDIAEWL 411
Cdd:cd18027 143 ---PDHVSIILLSATVPNTVEFADWI 165
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
716-936 |
3.23e-18 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 87.31 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 716 FKPTEAGRLMAWYYITFETVKKFC-AISGKETLLDLISMISSCNEFLDVQLRISEKRILNTLNKDpNRITIRFPMAERIK 794
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNeLLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEK-LPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 795 TremKVNCLIQAQLGCIPIQDFALTQDTVKIFRNGSRIARWLSDfVAAQEKKFAVLLNSVILTKCFKCKLWEnSKHVSKQ 874
Cdd:smart00611 81 V---KANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVD-IALERGWLSTALNALNLSQMIIQALWP-TDSPLLQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720413913 875 LDKIGISLSNTMVNAGLTSFKKIEEANARELELILNRHPPFGTQIKEAVAHLPKYELEVEQI 936
Cdd:smart00611 156 LPHLPEEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLE 217
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
227-599 |
8.73e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 85.46 E-value: 8.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 227 QSKAFDDLLYT----DRNFVICAPTGSGKTVVFELAITRLLmevplpwLNMKIVYMAPIKALCSQrfddWKEKFgpvgln 302
Cdd:COG1061 85 QQEALEALLAAlergGGRGLVVAPTGTGKTVLALALAAELL-------RGKRVLVLVPRRELLEQ----WAEEL------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 303 cKELTGDTVMDDLFEIQHANIIITTpekWDSVTRKWRDNSFIQLVRLFLIDEVHVIkdenRGPTLEVVVSRMKtvqslsr 382
Cdd:COG1061 148 -RRFLGDPLAGGGKKDSDAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHA----GAPSYRRILEAFP------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 383 dlesaspvPVRFVAVSATiPNAED---IAEWLSDGERPAVCLK--MDESH--------RPVKLQKVVLGFPCSSSQTEFK 449
Cdd:COG1061 213 --------AAYRLGLTAT-PFRSDgreILLFLFDGIVYEYSLKeaIEDGYlappeyygIRVDLTDERAEYDALSERLREA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 450 FDL---ALNYKVYSVIRTYSDQKPTLVFCSTrkgvqqaasvlVKDAKFIISveqklRLQKSAYSIrdsklkdTLVYGvgy 526
Cdd:COG1061 284 LAAdaeRKDKILRELLREHPDDRKTLVFCSS-----------VDHAEALAE-----LLNEAGIRA-------AVVTG--- 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720413913 527 hhaGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPA--HLVVIKSTMhysggvfeeySETDILQMIGRAGRP 599
Cdd:COG1061 338 ---DTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPTG----------SPREFIQRLGRGLRP 399
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
231-411 |
1.30e-15 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 76.87 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 231 FDDLLYTDRNFVICAPTGSGKTVVFELAITRLLmevplpWLNMKIV-YMAPIKALCSQRFDDWKEKFGPVGLNCKELTGD 309
Cdd:cd18026 26 SLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRL------LERRKKAlFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 310 --TVMDDLFEIQHanIIITTPEKWDSVTrkwrdNSFIQLVRLFLI-----DEVHVIKDENRGPTLEVVVSRmktvqslsr 382
Cdd:cd18026 100 kgRSPPKRRKSLS--VAVCTIEKANSLV-----NSLIEEGRLDELglvvvDELHMLGDGHRGALLELLLTK--------- 163
|
170 180
....*....|....*....|....*....
gi 1720413913 383 dLESASPVPVRFVAVSATIPNAEDIAEWL 411
Cdd:cd18026 164 -LLYAAQKNIQIVGMSATLPNLEELASWL 191
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
227-409 |
4.60e-15 |
|
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: 74.93 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 227 QSKAFDdLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNMKIVYMAPIKALC-SQ--RFDDWKEKFGPvGLNC 303
Cdd:cd17923 5 QAEAIE-AARAGRSVVVTTGTASGKSLCYQLPILEALLRDP----GSRALYLYPTKALAqDQlrSLRELLEQLGL-GIRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 304 KELTGDTVMDDLFEI--QHANIIITTPEKWD-SVTR---KWRdnSFIQLVRLFLIDEVHVIkdenRGP---TLEVVVSRM 374
Cdd:cd17923 79 ATYDGDTPREERRAIirNPPRILLTNPDMLHyALLPhhdRWA--RFLRNLRYVVLDEAHTY----RGVfgsHVALLLRRL 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1720413913 375 ktvqslsRDLESASPVPVRFVAVSATIPNAEDIAE 409
Cdd:cd17923 153 -------RRLCRRYGADPQFILTSATIGNPAEHAR 180
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
243-597 |
1.11e-14 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 79.97 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 243 ICAPTGSGKTVV-FELAITRLLME------VPLPWLNMKIVYMAPIKALCS--QR--------FDDWKEKFG--PVGLNC 303
Cdd:PRK09751 1 VIAPTGSGKTLAaFLYALDRLFREggedtrEAHKRKTSRILYISPIKALGTdvQRnlqiplkgIADERRRRGetEVNLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 304 KELTGDTVMDDLFEI--QHANIIITTPEK-WDSVTRKWRDNsfIQLVRLFLIDEVHVIKDENRGPTLEVvvsrmktvqSL 380
Cdd:PRK09751 81 GIRTGDTPAQERSKLtrNPPDILITTPESlYLMLTSRARET--LRGVETVIIDEVHAVAGSKRGAHLAL---------SL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 381 SRdLESASPVPVRFVAVSATIPNAEDIAEWLSdGERPAVCLKMDESHRPvKLQKVV-----LGFPCSSSQTEFKFDLALN 455
Cdd:PRK09751 150 ER-LDALLHTSAQRIGLSATVRSASDVAAFLG-GDRPVTVVNPPAMRHP-QIRIVVpvanmDDVSSVASGTGEDSHAGRE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 456 YKVY-----SVIRTYSDQKPTLVFCSTRkGV----------------QQAASVLVKDAKF-IISVEQKLRLQKSAYSIRD 513
Cdd:PRK09751 227 GSIWpyietGILDEVLRHRSTIVFTNSR-GLaekltarlnelyaarlQRSPSIAVDAAHFeSTSGATSNRVQSSDVFIAR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 514 SklkdtlvygvgyHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKstmhysggVFEEYSETDILQMI 593
Cdd:PRK09751 306 S------------HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQ--------VATPLSVASGLQRI 365
|
....
gi 1720413913 594 GRAG 597
Cdd:PRK09751 366 GRAG 369
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
238-411 |
1.04e-13 |
|
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: 70.30 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 238 DRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLnmKIVYMAPIKALCS---QRFDDWKEKFG---PVGLNckelTGDT- 310
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV--QVLYISPLKALINdqeRRLEEPLDEIDleiPVAVR----HGDTs 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 311 ------VMDDLfeiqhANIIITTPEkwdSV----TRKWRDNSFiQLVRLFLIDEVHVIKDENRGPTLEVvvsrmktvqSL 380
Cdd:cd17922 75 qsekakQLKNP-----PGILITTPE---SLelllVNKKLRELF-AGLRYVVVDEIHALLGSKRGVQLEL---------LL 136
|
170 180 190
....*....|....*....|....*....|.
gi 1720413913 381 SRdLESASPVPVRFVAVSATIPNAEDIAEWL 411
Cdd:cd17922 137 ER-LRKLTGRPLRRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
233-416 |
1.36e-13 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350783 [Multi-domain] Cd Length: 192 Bit Score: 70.86 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 233 DLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNMKIVYMAPIKALCSQ-------RFDdwkEKFGPVGLN-CK 304
Cdd:cd18025 11 DIVDRRESALIVAPTSSGKTFISYYCMEKVLRESD----DGVVVYVAPTKALVNQvvaevyaRFS---KKYPPSGKSlWG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 305 ELTGDTVMDDlfeIQHANIIITTPEKWDSVTRKWRDNSFIQLVRLFLIDEVHVIKDENRGPTLEvvvsrmktvqslsrDL 384
Cdd:cd18025 84 VFTRDYRHNN---PMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWE--------------QL 146
|
170 180 190
....*....|....*....|....*....|..
gi 1720413913 385 ESASPVPvrFVAVSATIPNAEDIAEWLSDGER 416
Cdd:cd18025 147 LLLIPCP--FLALSATIGNPQKFHEWLQSVQR 176
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
522-599 |
2.97e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 66.47 E-value: 2.97e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720413913 522 YGVGYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMP-AHLVVIKSTmhysggvfeEYSETDILQMIGRAGRP 599
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL---------PWSPASYIQRIGRAGRA 81
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
240-400 |
4.46e-11 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 62.42 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 240 NFVICAPTGSGKTVVFELAITRLLMEVPLpwlnmKIVYMAPIKALCSQRFDDWKEKFGPvGLNCKELTGDTVM--DDLFE 317
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKGK-----KVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAeeREKNK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 318 IQHANIIITTPEK-WDSVTRKWRdnSFIQLVRLFLIDEVHVIKDENRGptlevvvsrmkTVQSLSRDLESASPvPVRFVA 396
Cdd:cd00046 77 LGDADIIIATPDMlLNLLLREDR--LFLKDLKLIIVDEAHALLIDSRG-----------ALILDLAVRKAGLK-NAQVIL 142
|
....
gi 1720413913 397 VSAT 400
Cdd:cd00046 143 LSAT 146
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
216-356 |
1.58e-10 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 61.15 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 216 IFKEFPYfnyiQSKAFDDLL----YTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPwlnmKIVYMAPIKALCSQRFDD 291
Cdd:pfam04851 1 KLELRPY----QIEAIENLLesikNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK----KVLFLVPRKDLLEQALEE 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720413913 292 WKEKFGPVGLNCKELTGDTvmdDLFEIQHANIIITTPEKWDSVTRKWRDNSFIQLVRLFLIDEVH 356
Cdd:pfam04851 73 FKKFLPNYVEIGEIISGDK---KDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
514-598 |
1.40e-09 |
|
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: 56.84 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 514 SKLKDTLVYGVGYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMP-AHLVVIkstmhYSGgvfeEYSETDILQM 592
Cdd:pfam00271 31 ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YDL----PWNPASYIQR 101
|
....*.
gi 1720413913 593 IGRAGR 598
Cdd:pfam00271 102 IGRAGR 107
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
239-597 |
6.79e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 60.67 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 239 RNFVICAPTGSGKTVVFELAI----TRLLMEVPLPwlnMKI--VYMAPIKAL-------CSQRFDDWKEKFGPVGLNCKE 305
Cdd:PRK13767 48 KNVLISSPTGSGKTLAAFLAIidelFRLGREGELE---DKVycLYVSPLRALnndihrnLEEPLTEIREIAKERGEELPE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 306 L-----TGDTVMDD----LFEIQHanIIITTPEkwdS-----VTRKWRDnsFIQLVRLFLIDEVHVIKDENRGPTLEVvv 371
Cdd:PRK13767 125 IrvairTGDTSSYEkqkmLKKPPH--ILITTPE---SlaillNSPKFRE--KLRTVKWVIVDEIHSLAENKRGVHLSL-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 372 srmktvqSLSRDLESASPVPVRfVAVSATIPNAEDIAEWL---SDGERPAVCLKMDESH-RP--VKLQKVVLGFPCSSSQ 445
Cdd:PRK13767 196 -------SLERLEELAGGEFVR-IGLSATIEPLEEVAKFLvgyEDDGEPRDCEIVDARFvKPfdIKVISPVDDLIHTPAE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 446 TefkfdlaLNYKVYSVI-RTYSDQKPTLVFCSTRKGvqqAASVLVKdakfiisveqklrLQKSAYSIRDSKLkdtlvygV 524
Cdd:PRK13767 268 E-------ISEALYETLhELIKEHRTTLIFTNTRSG---AERVLYN-------------LRKRFPEEYDEDN-------I 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720413913 525 GYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPaH--LVVIKSTmhysggvfeEYSETDILQMIGRAG 597
Cdd:PRK13767 318 GAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG-YidLVVLLGS---------PKSVSRLLQRIGRAG 382
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
238-403 |
3.33e-08 |
|
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: 55.52 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 238 DRNFVICAPTGSGKTVVfelAItrLLMEVPLPWLNM----KIVYMAPIKALCSQRFDDWKEKFGPVGLNCKELTGDTVMD 313
Cdd:cd17927 17 GKNTIICLPTGSGKTFV---AV--LICEHHLKKFPAgrkgKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSEN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 314 DLFE--IQHANIIITTPEKWDSVTRKWRDNSfIQLVRLFLIDEVH-VIKDenrGPTLEVVVSrmktvqSLSRDLESASPV 390
Cdd:cd17927 92 VSVEqiVESSDVIIVTPQILVNDLKSGTIVS-LSDFSLLVFDECHnTTKN---HPYNEIMFR------YLDQKLGSSGPL 161
|
170
....*....|...
gi 1720413913 391 PvRFVAVSATIPN 403
Cdd:cd17927 162 P-QILGLTASPGV 173
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
226-411 |
1.13e-07 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 53.60 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 226 IQSKAFDDLLyTDRNFVICAPTGSGKTVVFEL-AITRLLMEVPLPWLNMKIVYMAPIKALCSQRFDDWKEKFGPVGLNCK 304
Cdd:cd00268 16 IQAQAIPLIL-SGRDVIGQAQTGSGKTLAFLLpILEKLLPEPKKKGRGPQALVLAPTRELAMQIAEVARKLGKGTGLKVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 305 ELTGDTVMDDLFEI--QHANIIITTPEK-WDSVTRKwrdnsFIQL--VRLFLIDEVHVIKDENRGPTLEVVVSRM-KTVQ 378
Cdd:cd00268 95 AIYGGAPIKKQIEAlkKGPDIVVGTPGRlLDLIERG-----KLDLsnVKYLVLDEADRMLDMGFEEDVEKILSALpKDRQ 169
|
170 180 190
....*....|....*....|....*....|....
gi 1720413913 379 SLsrdlesaspvpvrfvAVSATIPNA-EDIAEWL 411
Cdd:cd00268 170 TL---------------LFSATLPEEvKELAKKF 188
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
227-356 |
6.09e-07 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 51.50 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 227 QSKAFDDLLytDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNMKI-VYMAPIKALCSQRFDDWKEKfgpVGLNCKE 305
Cdd:cd18034 7 QLELFEAAL--KRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNPKKRaVFLVPTVPLVAQQAEAIRSH---TDLKVGE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720413913 306 LTGDTVMDD------LFEIQHANIIITTPEkwdsVTRKWRDNSFIQL--VRLFLIDEVH 356
Cdd:cd18034 82 YSGEMGVDKwtkerwKEELEKYDVLVMTAQ----ILLDALRHGFLSLsdINLLIFDECH 136
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
239-328 |
9.15e-07 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 51.05 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 239 RNFVICAPTGSGKTVVFELAItrlLMEVPLPWLNMKI--VYMAPIKALCSQRFDDWKEKFGPVGLNCKELTG---DTVMD 313
Cdd:cd17957 28 RDLLACAPTGSGKTLAFLIPI---LQKLGKPRKKKGLraLILAPTRELASQIYRELLKLSKGTGLRIVLLSKsleAKAKD 104
|
90
....*....|....*
gi 1720413913 314 DLFEIQHANIIITTP 328
Cdd:cd17957 105 GPKSITKYDILVSTP 119
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
237-329 |
3.79e-06 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350831 [Multi-domain] Cd Length: 202 Bit Score: 49.43 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 237 TDRNFVICAPTGSGKTVVfELAITRLLMEVPLPWLNMKIVYMAPIKALCSQRFDDWKEKFGPVGLNCKELTGDTvmDDLF 316
Cdd:cd18073 16 KGKNTIICAPTGCGKTFV-SLLICEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGAT--AENV 92
|
90
....*....|....*..
gi 1720413913 317 E----IQHANIIITTPE 329
Cdd:cd18073 93 PveqiIENNDIIILTPQ 109
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
239-356 |
6.99e-06 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 48.63 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 239 RNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNMKIVYMAPIKALCSQRfddwKEKFGPV---GLNCKELTGDTVMDDL 315
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQQ----LEKFFKYfrkGYKVTGLSGDSSHKVS 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1720413913 316 F--EIQHANIIITTPEKWDSVTRKWRDNSFIQL--VRLFLIDEVH 356
Cdd:cd18036 94 FgqIVKASDVIICTPQILINNLLSGREEERVYLsdFSLLIFDECH 138
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
201-328 |
1.51e-05 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 47.68 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 201 GSLKAVTEIPAKFRNIFKE-FPYFNYIQSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLmEVPLPWLNMKIVYMA 279
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKgYKVPTPIQRKTIPLIL-DGRDVVAMARTGSGKTAAFLIPMIEKL-KAHSPTVGARALILS 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1720413913 280 PIKALCSQRFDDWKE--KFgpVGLNCKELTGDTVMDDLFEIQHAN--IIITTP 328
Cdd:cd17959 79 PTRELALQTLKVTKElgKF--TDLRTALLVGGDSLEEQFEALASNpdIIIATP 129
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
459-598 |
1.65e-05 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 48.98 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 459 YSVIRTYSDQK--------------PTLVFCSTRKGVQQAASvlvkdakfiisveqklRLQKSAYSirdsklkdtlvygV 524
Cdd:COG0514 207 LEVVPKPPDDKlaqlldflkehpggSGIVYCLSRKKVEELAE----------------WLREAGIR-------------A 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 525 GYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMG-----------MNMPAHLvvikstmhysggvfEEYsetdiLQMI 593
Cdd:COG0514 258 AAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGidkpdvrfvihYDLPKSI--------------EAY-----YQEI 318
|
....*
gi 1720413913 594 GRAGR 598
Cdd:COG0514 319 GRAGR 323
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
242-356 |
2.35e-05 |
|
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: 45.76 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 242 VICAPTGSGKTVVfELAITRLLMEvplpwlnMKIVYMAPIKALCSQrfddWKEKFGpvglncKELTGDTVM----DDLFE 317
Cdd:cd17926 22 ILVLPTGSGKTLT-ALALIAYLKE-------LRTLIVVPTDALLDQ----WKERFE------DFLGDSSIGliggGKKKD 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1720413913 318 IQHANIIITTpekWDSVTRKWRDNSFIQLVRLFLI-DEVH 356
Cdd:cd17926 84 FDDANVVVAT---YQSLSNLAEEEKDLFDQFGLLIvDEAH 120
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
446-598 |
3.40e-05 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 44.89 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 446 TEFKFDLALNYKVYSvirtysDQKPTLVFCSTRKGVQQAASVLvkdakfiisveQKLRLQKSAYsirdsklkdtlvygvg 525
Cdd:cd18794 14 KDEKLDLLKRIKVEH------LGGSGIIYCLSRKECEQVAARL-----------QSKGISAAAY---------------- 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720413913 526 yhHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIkstmHYS-GGVFEEYsetdiLQMIGRAGR 598
Cdd:cd18794 61 --HAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVI----HYSlPKSMESY-----YQESGRAGR 123
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
238-361 |
3.56e-05 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 48.19 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 238 DRNFVICAPTGSGKTVVFELAITRLLMEVplpwlNMKIVYMAPIKALCSQRFDDWKEKFGPVGLNCKELTGDTVMDDLFE 317
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAERLHKK-----GGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKRKE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1720413913 318 I-QHANIIITTPE--KWDSVTRkwrdnsfiqlvRLFLIDEVHVIKDE 361
Cdd:COG1111 92 LwEKARIIVATPQviENDLIAG-----------RIDLDDVSLLIFDE 127
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
238-404 |
6.90e-04 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 42.28 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 238 DRNFVICAPTGSGKTvvfELAITRLLmEVPLPWLNMKIVYMAPIKALCSQRFDDWKEKFGPVGLNCK--ELTGDT--VMD 313
Cdd:cd17930 1 PGLVILEAPTGSGKT---EAALLWAL-KLAARGGKRRIIYALPTRATINQMYERIREILGRLDDEDKvlLLHSKAalELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 314 DLFEIQHANIIITTpEKWDSVTRKWrDNSFI----------------QLVRLFL-------IDEVHVIKDENRGPTLEVv 370
Cdd:cd17930 77 ESDEEPDDDPVEAV-DWALLLKRSW-LAPIVvttidqllesllkykhFERRLHGlansvvvLDEVQAYDPEYMALLLKA- 153
|
170 180 190
....*....|....*....|....*....|....
gi 1720413913 371 vsrmktvqsLSRDLESASpvpVRFVAVSATIPNA 404
Cdd:cd17930 154 ---------LLELLGELG---GPVVLMTATLPAL 175
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
235-413 |
1.14e-03 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 42.35 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 235 LYTDRNFVICAPTGSGKTVVFELAIT-RLL---MEVPLPWLNMKIVYMAPIKALCSQrFDDWKEKFG-PVGLNCKELTGD 309
Cdd:cd17948 24 ILRGRNTLCAAETGSGKTLTYLLPIIqRLLrykLLAEGPFNAPRGLVITPSRELAEQ-IGSVAQSLTeGLGLKVKVITGG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 310 TVMDDL--FEIQHANIIITTPekwdSVTRKWRDNSFIQL--VRLFLIDEVHVIKDENRGPTLEVVVSRMKtVQSLSRDLE 385
Cdd:cd17948 103 RTKRQIrnPHFEEVDILVATP----GALSKLLTSRIYSLeqLRHLVLDEADTLLDDSFNEKLSHFLRRFP-LASRRSENT 177
|
170 180
....*....|....*....|....*...
gi 1720413913 386 SASPVPVRFVAVSATIPnaEDIAEWLSD 413
Cdd:cd17948 178 DGLDPGTQLVLVSATMP--SGVGEVLSK 203
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
542-598 |
1.16e-03 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350192 [Multi-domain] Cd Length: 135 Bit Score: 40.62 E-value: 1.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720413913 542 LFTSGDLP--VLFTTSTLAMGMNMPAHLVVIKSTMHYSGGVFEEYSETDILQMIGRAGR 598
Cdd:cd18805 63 LFNDPESGydVLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMRPLSPSEVKQIAGRAGR 121
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
240-356 |
1.18e-03 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 41.54 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 240 NFVICAPTGSGKTVvfelaITRLLMEVPLPWL-NMKIVYMAPIKALCSQRFDDWKEKFGPVGLNCKELTGDTVMDD-LFE 317
Cdd:cd18033 18 NTLVALPTGLGKTF-----IAAVVMLNYYRWFpKGKIVFMAPTKPLVSQQIEACYKITGIPSSQTAELTGSVPPTKrAEL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1720413913 318 IQHANIIITTPEKWDS-VTRKWRDNSFIQLVrlfLIDEVH 356
Cdd:cd18033 93 WASKRVFFLTPQTLENdLKEGDCDPKSIVCL---VIDEAH 129
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
237-402 |
1.63e-03 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 41.38 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 237 TDRNFVICAPTGSGKTVVFEL-AITRLLMEVPLPwlnmKIVYMAPIKALCSQRFDDWKEkFGPVGLNCKE---LTGDTVM 312
Cdd:cd17962 26 LGRDILASADTGSGKTAAFLLpVIIRCLTEHRNP----SALILTPTRELAVQIEDQAKE-LMKGLPPMKTallVGGLPLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 313 DDLFEI-QHANIIITTPEKWDSVTRKwrdnSFIQL--VRLFLIDEVHVIKdeNRGPTLEVvvsrMKTVQSLSRDLESasp 389
Cdd:cd17962 101 PQLYRLqQGVKVIIATPGRLLDILKQ----SSVELdnIKIVVVDEADTML--KMGFQQQV----LDILENISHDHQT--- 167
|
170
....*....|...
gi 1720413913 390 vpvrfVAVSATIP 402
Cdd:cd17962 168 -----ILVSATIP 175
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
243-410 |
2.02e-03 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 41.46 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 243 ICAPTGSGKTVVFELAITRLLMEVPLPWLNMKIVymAPIKALCSQRFDDWKEKFGPVGLNCKELTGDTV----MDDLFEI 318
Cdd:cd17956 41 VSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIV--VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSfkkeQKLLLVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 319 QH------ANIIITTPEKW-DSVTRKwrdNSFI-QLVRLFLIDEVHVIKDENRGPTLEVVVSRMKTVQSLSRDLESA--- 387
Cdd:cd17956 119 TSgrylsrVDILVATPGRLvDHLNST---PGFTlKHLRFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLGSFGDanl 195
|
170 180
....*....|....*....|....*..
gi 1720413913 388 ---SPVPVRFVAVSATIP-NAEDIAEW 410
Cdd:cd17956 196 lerSVRPLQKLLFSATLTrDPEKLSSL 222
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
245-328 |
2.36e-03 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 40.76 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 245 APTGSGKTVVFELAITRLLMEVPLPwlnMKIVYMAPIKALCSQRFDDWKEKFGPVGLNCKELTG--DTVMDDLFEIQHAN 322
Cdd:cd17954 44 AETGSGKTAAFALPILQALLENPQR---FFALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGgmDMMAQAIALAKKPH 120
|
....*.
gi 1720413913 323 IIITTP 328
Cdd:cd17954 121 VIVATP 126
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
471-598 |
2.63e-03 |
|
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: 39.94 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 471 TLVFCSTRKGVQqaasvlvkdakfiiSVEQKLRLqksaysiRDSKLKDTLVYGVgyHHAGMELSDRKLVEGLFTSGDLPV 550
Cdd:cd18796 41 TLVFTNTRSQAE--------------RLAQRLRE-------LCPDRVPPDFIAL--HHGSLSRELREEVEAALKRGDLKV 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1720413913 551 LFTTSTLAMGMNMPA-HLVV-IKSTmhysggvfeeYSETDILQMIGRAGR 598
Cdd:cd18796 98 VVATSSLELGIDIGDvDLVIqIGSP----------KSVARLLQRLGRSGH 137
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
461-598 |
2.67e-03 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 42.01 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 461 VIRTYSDQ--KPTLVFCSTRKGVQQAASvlvkdakfiisveqklRLQKSAYSirdsklkdtlvygVGYHHAGMELSDRKL 538
Cdd:PRK11057 227 LMRYVQEQrgKSGIIYCNSRAKVEDTAA----------------RLQSRGIS-------------AAAYHAGLDNDVRAD 277
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720413913 539 VEGLFTSGDLPVLFTTSTLAMGMNMP-----AHLVVIKSTMHYsggvfeeYSETdilqmiGRAGR 598
Cdd:PRK11057 278 VQEAFQRDDLQIVVATVAFGMGINKPnvrfvVHFDIPRNIESY-------YQET------GRAGR 329
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
471-598 |
2.86e-03 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 39.55 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 471 TLVFCSTRKgvqqAASVLVKDAKFIISVEQKLrlqksaysirdsklkdtlVYGVGYHHAGMELSDRKLVEGLFTSGDLPV 550
Cdd:cd18797 38 TIVFCRSRK----LAELLLRYLKARLVEEGPL------------------ASKVASYRAGYLAEDRREIEAELFNGELLG 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1720413913 551 LFTTSTLAMGMNMPAHLVVIKSTmhYSGGVFEeysetdILQMIGRAGR 598
Cdd:cd18797 96 VVATNALELGIDIGGLDAVVLAG--YPGSLAS------LWQQAGRAGR 135
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
211-495 |
4.23e-03 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 41.61 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 211 AKFRNIFKEFPYFNYIQSKAFDDLLYTDRN----FVICAPTGSGKTvvfeLAITRLLMEVPLPWLNMKIVYMAPIKALCS 286
Cdd:COG1203 116 RLLPKKSKPRTPINPLQNEALELALEAAEEepglFILTAPTGGGKT----EAALLFALRLAAKHGGRRIIYALPFTSIIN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 287 QRFDDWKEKFGP-VGlnckELTGDTVM-----DDLFEIQH-----------ANIIITTPEK-WDSVTRKWRdNSFIQLVR 348
Cdd:COG1203 192 QTYDRLRDLFGEdVL----LHHSLADLdlleeEEEYESEArwlkllkelwdAPVVVTTIDQlFESLFSNRK-GQERRLHN 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413913 349 L----FLIDEVHVIkDENRGPTLEVVVSRMKTVQSlsrdlesaspvpvRFVAVSATIPNA-----EDIAEWLSDGERPAV 419
Cdd:COG1203 267 LansvIILDEVQAY-PPYMLALLLRLLEWLKNLGG-------------SVILMTATLPPLlreelLEAYELIPDEPEELP 332
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720413913 420 CLKMDESHRPVKLQKVVLgfpcssSQTEFkfdlalnykVYSVIRTYSDQKPTLVFCSTRKGVQQAASVLVKDAKFI 495
Cdd:COG1203 333 EYFRAFVRKRVELKEGPL------SDEEL---------AELILEALHKGKSVLVIVNTVKDAQELYEALKEKLPDE 393
|
|
| |
