|
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 ... |
279-486 |
1.06e-120 |
|
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: 1.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 279 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEV-PLPWLNMKIVYMAPIKALCSQRFDDWKEKFGPVG 357
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERnPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 358 LNCKELTGDTVMDDLFEIQHANIIITTPEKWDSVTRKWRDN-SFIQLVRLFLIDEVHVIKdENRGPTLEVVVSRMKTVqS 436
Cdd:cd18023 81 LSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIK-ENRGATLEVVVSRMKTL-S 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568935789 437 LSRDLESASPVPVRFVAVSATIPNAEDIAEWLSDGerPAVCLKMDESHRP 486
Cdd:cd18023 159 SSSELRGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFGESFRP 206
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
263-819 |
4.08e-104 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 342.65 E-value: 4.08e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 263 VTEIP-AKFRNIFKEFPY--FNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNMKIVYMAPIK 339
Cdd:COG1204 3 VAELPlEKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN------GGKALYIVPLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 340 ALCSQRFDDWKEKFGPVGLNCKELTGDTVMDDLfEIQHANIIITTPEKWDSVTRKwrDNSFIQLVRLFLIDEVHVIKDEN 419
Cdd:COG1204 77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRN--GPSWLRDVDLVVVDEAHLIDDES 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 420 RGPTLEVVVSRMKTVQSlsrdlesaspvPVRFVAVSATIPNAEDIAEWLsdgERPAVclkmDESHRPVKLQKVV-----L 494
Cdd:COG1204 154 RGPTLEVLLARLRRLNP-----------EAQIVALSATIGNAEEIAEWL---DAELV----KSDWRPVPLNEGVlydgvL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 495 GFPCSSSQTEFKFdLALnykvysVIRTYSDQKPTLVFCSTRKGVQQAASVLVKDAKFIISVEQKLRLQKSAYSIR----- 569
Cdd:COG1204 216 RFDDGSRRSKDPT-LAL------ALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLevsee 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 570 ---DSKLKDTLVYGVGYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKSTmHYSGGVfeEYSETDI 646
Cdd:COG1204 289 thtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-KRGGMV--PIPVLEF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 647 LQMIGRAGRPQFDTTATAVIMTRLST-----REKYVqmLACNDTVESSLH--RHLIEHLNAEIVLHTITDVNIALDWIRS 719
Cdd:COG1204 366 KQMAGRAGRPGYDPYGEAILVAKSSDeadelFERYI--LGEPEPIRSKLAneSALRTHLLALIASGFANSREELLDFLEN 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 720 TMLYIRAlknpshygfssglNKDGIEAKLQElclkNLKDLSSLDLIKMDEDvNFKPTEAGRLMAWYYITFETVKKF---- 795
Cdd:COG1204 444 TFYAYQY-------------DKGDLEEVVDD----ALEFLLENGFIEEDGD-RLRATKLGKLVSRLYIDPLTAAELvdgl 505
|
570 580
....*....|....*....|....
gi 568935789 796 CAISGKETLLDLISMISSCNEFLD 819
Cdd:COG1204 506 RKADEEFTDLGLLHLILILRDWIN 529
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
775-1088 |
8.90e-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: 234.02 E-value: 8.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 775 PTEAGRLMAWYYITFETVKKFC-AISGKETLLDLISMISSCNEFLDVQLRISEKRILNTLNKdpnriTIRFPMAERIKTR 853
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNqSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLE-----KVPIPVKGDIEDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 854 EMKVNCLIQAQLGCIPIQDFALTQDTVKIFRNGSRIARWLSDfVAAQEKKFAVLLNSVILTKCFKCKLWeNSKHVSKQLD 933
Cdd:pfam02889 76 HAKVNILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFE-ILLSKGWLSAALTALDLCKMIEQRMW-DSDSPLRQFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 934 KIGISLSNTMVNAGLTSFKKIEEANARELELILNRHPPFGTQIKEAVAHLPKYELEVEqIARYSDIKAEILVTIIlRNFE 1013
Cdd:pfam02889 154 GIPPELIKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAE-VQPITRSVLRVEVTIT-PDFP 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568935789 1014 qlQTKRTAPDFHYATLIIGDADNQVVFKHKIMdSVLLKSGNWVKKIDVKRALISE---DLSINLISSDYVGLDIHQKF 1088
Cdd:pfam02889 232 --WDKRVHGKSEGFWLVVGDSDGNEILHIERF-TLTKRTLAGEHKLEFTVPPSDPgppQLFVRLISDSWLGADQEVPI 306
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
279-472 |
2.34e-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: 2.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 279 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVplpwlNMKIVYMAPIKALCSQRFDDWKEKFGPVGL 358
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-----GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 359 NCKELTGDTVMDDLfEIQHANIIITTPEKWDSVTRKWRDNsFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMKTVQSls 438
Cdd:cd17921 76 NVGLLTGDPSVNKL-LLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRINK-- 151
|
170 180 190
....*....|....*....|....*....|....
gi 568935789 439 rdlesaspvPVRFVAVSATIPNAEDIAEWLSDGE 472
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 ... |
775-1090 |
1.01e-60 |
|
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: 211.06 E-value: 1.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 775 PTEAGRLMAWYYITFETVKKFCA-ISGKETLLDLISMISSCNEFLDVQLRISEKRILNTLNKDpnritIRFPMAERIKTR 853
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQsLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-----VPIPVKEGIIDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 854 EM-KVNCLIQAQLGCIPIQDFALTQDTVKIFRNGSRIARWLSDfVAAQEKKFAVLLNSVILTKCFKCKLWENSKHVSKQL 932
Cdd:smart00973 76 PHaKVNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVD-IALSKGWLRTALNALDLSQMVVQRLWEDSDSPLKQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 933 DKIGIS--LSNTMVNAGLTSFKKIEEANARELELILNRHPPFGTQIKEAVAHLPKYELEVEQIARYSDIKAEILVTIIlr 1010
Cdd:smart00973 155 PHFLIEdvYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITRDLTLRVELEIT-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 1011 NFEQLQTKRTAPDFHYATLIIGDADNQVVFKHKIMDSVLLKSGNWVK-KIDVKR-ALISEDLSINLISSDYVGLDIHQKF 1088
Cdd:smart00973 233 PVFAWDLPRHKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKlDFTVPLsEPGPENYTVYLISDSYLGCDQEVSF 312
|
..
gi 568935789 1089 TV 1090
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 ... |
277-468 |
1.28e-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: 1.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 277 FPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNMKIVYMAPIKALCSQRFDDWKEKFGPV 356
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNP----KGRAVYIAPMQELVDARYKDWRAKFGPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 357 -GLNCKELTGDTVMdDLFEIQHANIIITTPEKWDSVTRKWRDNSFIQLVRLFLIDEVHVIKDENrGPTLEVVVSRMKTVQ 435
Cdd:cd18021 77 lGKKVVKLTGETST-DLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGEN-GPVYEVVVSRMRYIS 154
|
170 180 190
....*....|....*....|....*....|...
gi 568935789 436 SlsrDLESaspvPVRFVAVSATIPNAEDIAEWL 468
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 ... |
485-669 |
4.20e-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: 4.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 485 RPVKLQKVVLGFPCSSSQTEFKFDL--ALNYKVYSVIRTYSDQKPTLVFCSTRKGVQQAASVLVkdakfiisveqklrlq 562
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNkfDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 563 ksaysirdsklkdtlvyGVGYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKSTMHYSGGVFEEYS 642
Cdd:cd18795 65 -----------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELS 127
|
170 180
....*....|....*....|....*..
gi 568935789 643 ETDILQMIGRAGRPQFDTTATAVIMTR 669
Cdd:cd18795 128 PLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
279-468 |
1.47e-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: 1.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 279 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNMKIVYMAPIKALCSQRFDDWKEKF-GPVG 357
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYP----GSKVVYIAPLKALVRERVDDWKKRFeEKLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 358 LNCKELTGDtVMDDLFEIQHANIIITTPEKWDSVTRKWRDNSFIQLVRLFLIDEVHVIKDEnRGPTLEVVVSRMKTVQSL 437
Cdd:cd18022 77 KKVVELTGD-VTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSD-RGPVLEVIVSRMNYISSQ 154
|
170 180 190
....*....|....*....|....*....|.
gi 568935789 438 SRdlesaspVPVRFVAVSATIPNAEDIAEWL 468
Cdd:cd18022 155 TE-------KPVRLVGLSTALANAGDLANWL 178
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
284-795 |
1.51e-55 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 207.36 E-value: 1.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 284 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAIT-RLLMEvplpwlNMKIVYMAPIKALCSQRFDDWKEkFGPVGLNCKE 362
Cdd:PRK00254 28 QAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVnKLLRE------GGKAVYLVPLKALAEEKYREFKD-WEKLGLRVAM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 363 LTGDTVMDDLFeIQHANIIITTPEKWDSVTRkwRDNSFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMktvqsLSRdle 442
Cdd:PRK00254 101 TTGDYDSTDEW-LGKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHM-----LGR--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 443 saspvpVRFVAVSATIPNAEDIAEWLSdgerpAVCLKMDesHRPVKLQKVV--LGFPCSSSQTEFKFDLALNYKVYSVIR 520
Cdd:PRK00254 170 ------AQILGLSATVGNAEELAEWLN-----AELVVSD--WRPVKLRKGVfyQGFLFWEDGKIERFPNSWESLVYDAVK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 521 TysdQKPTLVFCSTRKGVQQAASVLVKDAKFIISVEQKLRLQKSAYSIRDS----KLKDTLVYGVGYHHAGMELSDRKLV 596
Cdd:PRK00254 237 K---GKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKELADSLEENptneKLKKALRGGVAFHHAGLGRTERVLI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 597 EGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKSTMHYSGGVFEEYSETDILQMIGRAGRPQFDTTATAVIMTR------- 669
Cdd:PRK00254 314 EDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATteepskl 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 670 -----LSTREKYVQMLACndtvESSLHRHLIehlnAEIVLHTITDVNIALDWIRSTmLYIRALKNPSHygfssglnkdgI 744
Cdd:PRK00254 394 meryiFGKPEKLFSMLSN----ESAFRSQVL----ALITNFGVSNFKELVNFLERT-FYAHQRKDLYS-----------L 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 568935789 745 EAKLQELCLKNLKDlsslDLIKMDEDVNFKPTEAGRLMAWYYITFETVKKF 795
Cdd:PRK00254 454 EEKAKEIVYFLLEN----EFIDIDLEDRFIPLPLGIRTSQLYIDPLTAKKF 500
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
284-667 |
3.72e-53 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 200.55 E-value: 3.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 284 QSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNMKIVYMAPIKALCSQRFDDWKEKFGP--VGLnck 361
Cdd:COG4581 30 QEEAILALE-AGRSVLVAAPTGSGKTLVAEFAIFLALAR------GRRSFYTAPIKALSNQKFFDLVERFGAenVGL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 362 eLTGDTVmddlfEIQHANIIITTPEkwdsVTRKW--RDNSFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMktvqslsr 439
Cdd:COG4581 100 -LTGDAS-----VNPDAPIVVMTTE----ILRNMlyREGADLEDVGVVVMDEFHYLADPDRGWVWEEPIIHL-------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 440 dlesasPVPVRFVAVSATIPNAEDIAEWLSD--GErpavCLKMDESHRPVKL-QKVVLG---FPCSSSQTEFKFDLALNY 513
Cdd:COG4581 162 ------PARVQLVLLSATVGNAEEFAEWLTRvrGE----TAVVVSEERPVPLeFHYLVTprlFPLFRVNPELLRPPSRHE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 514 KVYSVIRTysDQKPTLVFCSTRKGVQQAASVLVkdAKFIISVEQKLRL-------QKSAYSIRDSKLKDTLVYGVGYHHA 586
Cdd:COG4581 232 VIEELDRG--GLLPAIVFIFSRRGCDEAAQQLL--SARLTTKEERAEIreaidefAEDFSVLFGKTLSRLLRRGIAVHHA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 587 GMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKSTMHYSGGVFEEYSETDILQMIGRAGRPQFDTTATAVI 666
Cdd:COG4581 308 GMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDTEGHVVV 387
|
.
gi 568935789 667 M 667
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 ... |
263-468 |
5.52e-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: 5.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 263 VTEIPAKFRNIFKEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWL-----NMKIVYMAP 337
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGtinldAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 338 IKALCSQRFDDWKEKFGPVGLNCKELTGDTVMDDLfEIQHANIIITTPEKWDSVTRKWRDNSFIQLVRLFLIDEVHVIKD 417
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKE-QISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568935789 418 EnRGPTLEVVVSRmkTVQSLSRDLEsaspvPVRFVAVSATIPNAEDIAEWL 468
Cdd:cd18019 160 D-RGPVLESIVAR--TIRQIEQTQE-----YVRLVGLSATLPNYEDVATFL 202
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
284-667 |
3.83e-49 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 188.24 E-value: 3.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 284 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNMKIVYMAPIKALCSQRFDDWKEkFGPVGLNCKEL 363
Cdd:PRK02362 28 QAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIAR------GGKALYIVPLRALASEKFEEFER-FEELGVRVGIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 364 TGDTVMDDlfEIQHAN-IIITTPEKWDSVTRKwrDNSFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMKtvqSLSRDLE 442
Cdd:PRK02362 101 TGDYDSRD--EWLGDNdIIVATSEKVDSLLRN--GAPWLDDITCVVVDEVHLIDSANRGPTLEVTLAKLR---RLNPDLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 443 saspvpvrFVAVSATIPNAEDIAEWLsDGERpavclkMDESHRPVKLQKVVL---GFPCSSSQTEFKF-----DLALnyk 514
Cdd:PRK02362 174 --------VVALSATIGNADELADWL-DAEL------VDSEWRPIDLREGVFyggAIHFDDSQREVEVpskddTLNL--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 515 vysVIRTYSDQKPTLVFCSTRKGVQQAASVLVKDAKFIISVEQKLRLQKSAYSIRDS-------KLKDTLVYGVGYHHAG 587
Cdd:PRK02362 236 ---VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVsdtetskDLADCVAKGAAFHHAG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 588 MELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKSTMHYSGG-------VFeEYSetdilQMIGRAGRPQFDT 660
Cdd:PRK02362 313 LSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGagmqpipVL-EYH-----QMAGRAGRPGLDP 386
|
....*..
gi 568935789 661 TATAVIM 667
Cdd:PRK02362 387 YGEAVLL 393
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
267-791 |
5.51e-44 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 171.60 E-value: 5.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 267 PAKFRNIFKEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNMKIVYMAPIKALCSQRF 346
Cdd:PRK01172 9 DDEFLNLFTGNDFELYDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLA------GLKSIYIVPLRSLAMEKY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 347 DDWKeKFGPVGLNCKELTGDtvMDDLFE-IQHANIIITTPEKWDSVTRkwRDNSFIQLVRLFLIDEVHVIKDENRGPTLE 425
Cdd:PRK01172 83 EELS-RLRSLGMRVKISIGD--YDDPPDfIKRYDVVILTSEKADSLIH--HDPYIINDVGLIVADEIHIIGDEDRGPTLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 426 VVVSRMKTVQSlsrdlesaspvPVRFVAVSATIPNAEDIAEWLSdgerpAVCLKmdESHRPVKLQKVVLGFPCSSSQTEF 505
Cdd:PRK01172 158 TVLSSARYVNP-----------DARILALSATVSNANELAQWLN-----ASLIK--SNFRPVPLKLGILYRKRLILDGYE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 506 KFDLALNykvySVIR-TYSDQKPTLVFCSTRKGVQQAASVLVK----DAKFIISVEQKlrlqksaySIRDSKLKDTLVYG 580
Cdd:PRK01172 220 RSQVDIN----SLIKeTVNDGGQVLVFVSSRKNAEDYAEMLIQhfpeFNDFKVSSENN--------NVYDDSLNEMLPHG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 581 VGYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKSTMHYSGGVFEEYSETDILQMIGRAGRPQFDT 660
Cdd:PRK01172 288 VAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGRAGRPGYDQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 661 TATAVImtrlstrekYVQMLACNDTVESSLHRH---LIEHLNAEIVLHTITDVNIALDWIRStMLYIRALKNPSHYGFSS 737
Cdd:PRK01172 368 YGIGYI---------YAASPASYDAAKKYLSGEpepVISYMGSQRKVRFNTLAAISMGLASS-MEDLILFYNETLMAIQN 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 568935789 738 GlnKDGIEAKLQElclkNLKDLSSLDLIKmdEDVNFKPTEAGRLMAWYYITFET 791
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; ... |
281-468 |
2.34e-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: 151.04 E-value: 2.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 281 NYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLME--VPLPWL---NMKIVYMAPIKALCSQRFDDWKEKFGP 355
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQhvNQGGVIkkdDFKIVYIAPMKALAAEMVEKFSKRLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 356 VGLNCKELTGDTVMDDLfEIQHANIIITTPEKWDSVTRKWR-DNSFIQLVRLFLIDEVHVIKDEnRGPTLEVVVSRMKtv 434
Cdd:cd18020 83 LGIKVKELTGDMQLTKK-EIAETQIIVTTPEKWDVVTRKSSgDVALSQLVRLLIIDEVHLLHDD-RGPVIESLVARTL-- 158
|
170 180 190
....*....|....*....|....*....|....
gi 568935789 435 qslsRDLESASPVpVRFVAVSATIPNAEDIAEWL 468
Cdd:cd18020 159 ----RQVESTQSM-IRIVGLSATLPNYLDVADFL 187
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
279-468 |
1.13e-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: 1.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 279 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNMKIVYMAPIKALCSQRFDDWKeKFGPVGL 358
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLE------GGKALYLVPLRALASEKYEEFK-KLEEIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 359 NCKELTGDTVMDDLFeIQHANIIITTPEKWDSVTR-KWrdnSFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMKTVQSl 437
Cdd:cd18028 74 KVGISTGDYDEDDEW-LGDYDIIVATYEKFDSLLRhSP---SWLRDVGVVVVDEIHLISDEERGPTLESIVARLRRLNP- 148
|
170 180 190
....*....|....*....|....*....|.
gi 568935789 438 srdlesaspvPVRFVAVSATIPNAEDIAEWL 468
Cdd:cd18028 149 ----------NTQIIGLSATIGNPDELAEWL 169
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
283-464 |
3.24e-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: 3.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 283 IQSKAFDdLLYTDRNFVICAPTGSGKTVVFELAItrlLMEVPLPWLNMKIVYMAPIKALCSQRFDDWKEKFGPVGLN-CK 361
Cdd:pfam00270 3 IQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPA---LEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKvAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 362 ELTGDTVMDDLFEIQHANIIITTPEKWDSVTRKWRdnsFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMktvqslsrdl 441
Cdd:pfam00270 79 LLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL---------- 145
|
170 180
....*....|....*....|....
gi 568935789 442 esasPVPVRFVAVSATIP-NAEDI 464
Cdd:pfam00270 146 ----PKKRQILLLSATLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
275-468 |
2.80e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 110.66 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 275 KEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPwlnmKIVYMAPIKALCSQRFDDWKEKFG 354
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGG----RVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 355 PVGLN-CKELTGDTVMDDLFEIQH--ANIIITTPEKWDSVTRKwrDNSFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRM 431
Cdd:smart00487 80 SLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 568935789 432 ktvqslsrdlesasPVPVRFVAVSATIPNAEDIAEWL 468
Cdd:smart00487 158 --------------PKNVQLLLLSATPPEEIENLLEL 180
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
266-658 |
6.67e-27 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 118.84 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 266 IPAKFRNIFK-EFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELA-ITRLLMEvplpwlNMKIVYMAPIKALCS 343
Cdd:COG1202 195 LPPELKDLLEgRGEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAgIKNALEG------KGKMLFLVPLVALAN 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 344 QRFDDWKEKFGP-------VGLN-CKELTGDTVMDdlfeiqhANIIITTPEKWDSVTRKWRDNSFIQLVrlfLIDEVHVI 415
Cdd:COG1202 269 QKYEDFKDRYGDgldvsirVGASrIRDDGTRFDPN-------ADIIVGTYEGIDHALRTGRDLGDIGTV---VIDEVHML 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 416 KDENRGPTLEVVVSRMKTVqslsrdLESAspvpvRFVAVSATIPNAEDIAEWLSdgerpavcLKMDE-SHRPVKLQKVVL 494
Cdd:COG1202 339 EDPERGHRLDGLIARLKYY------CPGA-----QWIYLSATVGNPEELAKKLG--------AKLVEyEERPVPLERHLT 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 495 gFpcssSQTEFKFDLA--LNYKVYSVIRTYSDQKPTLVFCSTRKgvqqaasvlvkdakfiisveqklrlqksaysiRDSK 572
Cdd:COG1202 400 -F----ADGREKIRIInkLVKREFDTKSSKGYRGQTIIFTNSRR--------------------------------RCHE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 573 LKDTLVYGVGYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKS-TMhysGGvfEEYSETDILQMIG 651
Cdd:COG1202 443 IARALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSlAM---GI--EWLSVQEFHQMLG 517
|
....*..
gi 568935789 652 RAGRPQF 658
Cdd:COG1202 518 RAGRPDY 524
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
284-655 |
8.52e-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: 8.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 284 QSKAFDdLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPwlnmKIVYMAPIKALCS---QRFDDWKEKFGPvGLNC 360
Cdd:COG1205 61 QAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA----TALYLYPTKALARdqlRRLRELAEALGL-GVRV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 361 KELTGDTVMDDLFEI-QHANIIITTPEKWDS----VTRKWRdnSFIQLVRLFLIDEVHVIkdenRGptleV-------VV 428
Cdd:COG1205 135 ATYDGDTPPEERRWIrEHPDIVLTNPDMLHYgllpHHTRWA--RFFRNLRYVVIDEAHTY----RG----VfgshvanVL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 429 SRMKTVqslsRDLESASPVpvrFVAVSATIPNAEDIAEWLSDgeRPAVCLkmDESHRPVKLQKVVLGFPC-------SSS 501
Cdd:COG1205 205 RRLRRI----CRHYGSDPQ---FILASATIGNPAEHAERLTG--RPVTVV--DEDGSPRGERTFVLWNPPlvddgirRSA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 502 QTEFKfDLALNYkvysvirTYSDQKpTLVFCSTRKGVQQAASVLvkdakfiisveqKLRLQKSAYSIRdsklkdtlvygV 581
Cdd:COG1205 274 LAEAA-RLLADL-------VREGLR-TLVFTRSRRGAELLARYA------------RRALREPDLADR-----------V 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568935789 582 GYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPA-HLVVIkstMHYSGGVfeeyseTDILQMIGRAGR 655
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 ... |
275-469 |
4.09e-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: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 275 KEFPY-FNYIQSKAFDDLlytDRN--FVICAPTGSGKTVVFELAITRLLMEvplpwlNMKIVYMAPIKALCSQRFDDWKE 351
Cdd:cd18024 27 RTYPFtLDPFQKTAIACI---ERNesVLVSAHTSAGKTVVAEYAIAQSLRD------KQRVIYTSPIKALSNQKYRELQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 352 KFGPVGLnckeLTGDTVMDdlfeiQHANIIITTPEKWDSVTrkWRDNSFIQLVRLFLIDEVHVIKDENRGPTLEvvvsrm 431
Cdd:cd18024 98 EFGDVGL----MTGDVTIN-----PNASCLVMTTEILRSML--YRGSEIMREVAWVIFDEIHYMRDKERGVVWE------ 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 568935789 432 KTVQSLsrdlesasPVPVRFVAVSATIPNAEDIAEWLS 469
Cdd:cd18024 161 ETIILL--------PDKVRYVFLSATIPNARQFAEWIC 190
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
284-468 |
1.42e-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: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 284 QSKAFDDLLYTDRNFViCAPTGSGKTVVFELAITrllmevpLPWLNM-KIVYMAPIKALCSQRFDDWKEKFGPVGLncke 362
Cdd:cd18027 13 QKQAILHLEAGDSVFV-AAHTSAGKTVVAEYAIA-------LAQKHMtRTIYTSPIKALSNQKFRDFKNTFGDVGL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 363 LTGDTVMDdlfeiQHANIIITTPEKWDSVTrkWRDNSFIQLVRLFLIDEVHVIKDENRGPTLEVVVSRMktvqslsrdle 442
Cdd:cd18027 81 ITGDVQLN-----PEASCLIMTTEILRSML--YNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIML----------- 142
|
170 180
....*....|....*....|....*.
gi 568935789 443 sasPVPVRFVAVSATIPNAEDIAEWL 468
Cdd:cd18027 143 ---PDHVSIILLSATVPNTVEFADWI 165
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
773-993 |
3.89e-18 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 86.93 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 773 FKPTEAGRLMAWYYITFETVKKFC-AISGKETLLDLISMISSCNEFLDVQLRISEKRILNTLNKDpNRITIRFPMAERIK 851
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNeLLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEK-LPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 852 TremKVNCLIQAQLGCIPIQDFALTQDTVKIFRNGSRIARWLSDfVAAQEKKFAVLLNSVILTKCFKCKLWEnSKHVSKQ 931
Cdd:smart00611 81 V---KANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVD-IALERGWLSTALNALNLSQMIIQALWP-TDSPLLQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568935789 932 LDKIGISLSNTMVNAGLTSFKKIEEANARELELILNRHPPFGTQIKEAVAHLPKYELEVEQI 993
Cdd:smart00611 156 LPHLPEEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLE 217
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
284-656 |
9.19e-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: 9.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 284 QSKAFDDLLYT----DRNFVICAPTGSGKTVVFELAITRLLmevplpwLNMKIVYMAPIKALCSQrfddWKEKFgpvgln 359
Cdd:COG1061 85 QQEALEALLAAlergGGRGLVVAPTGTGKTVLALALAAELL-------RGKRVLVLVPRRELLEQ----WAEEL------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 360 cKELTGDTVMDDLFEIQHANIIITTpekWDSVTRKWRDNSFIQLVRLFLIDEVHVIkdenRGPTLEVVVSRMKtvqslsr 439
Cdd:COG1061 148 -RRFLGDPLAGGGKKDSDAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHA----GAPSYRRILEAFP------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 440 dlesaspvPVRFVAVSATiPNAED---IAEWLSDGERPAVCLK--MDESH--------RPVKLQKVVLGFPCSSSQTEFK 506
Cdd:COG1061 213 --------AAYRLGLTAT-PFRSDgreILLFLFDGIVYEYSLKeaIEDGYlappeyygIRVDLTDERAEYDALSERLREA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 507 FDL---ALNYKVYSVIRTYSDQKPTLVFCSTrkgvqqaasvlVKDAKFIISveqklRLQKSAYSIrdsklkdTLVYGvgy 583
Cdd:COG1061 284 LAAdaeRKDKILRELLREHPDDRKTLVFCSS-----------VDHAEALAE-----LLNEAGIRA-------AVVTG--- 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568935789 584 hhaGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPA--HLVVIKSTMhysggvfeeySETDILQMIGRAGRP 656
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 ... |
288-468 |
1.36e-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: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 288 FDDLLYTDRNFVICAPTGSGKTVVFELAITRLLmevplpWLNMKIV-YMAPIKALCSQRFDDWKEKFGPVGLNCKELTGD 366
Cdd:cd18026 26 SLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRL------LERRKKAlFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 367 --TVMDDLFEIQHanIIITTPEKWDSVTrkwrdNSFIQLVRLFLI-----DEVHVIKDENRGPTLEVVVSRmktvqslsr 439
Cdd:cd18026 100 kgRSPPKRRKSLS--VAVCTIEKANSLV-----NSLIEEGRLDELglvvvDELHMLGDGHRGALLELLLTK--------- 163
|
170 180
....*....|....*....|....*....
gi 568935789 440 dLESASPVPVRFVAVSATIPNAEDIAEWL 468
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 ... |
284-466 |
4.80e-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: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 284 QSKAFDdLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNMKIVYMAPIKALC-SQ--RFDDWKEKFGPvGLNC 360
Cdd:cd17923 5 QAEAIE-AARAGRSVVVTTGTASGKSLCYQLPILEALLRDP----GSRALYLYPTKALAqDQlrSLRELLEQLGL-GIRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 361 KELTGDTVMDDLFEI--QHANIIITTPEKWD-SVTR---KWRdnSFIQLVRLFLIDEVHVIkdenRGP---TLEVVVSRM 431
Cdd:cd17923 79 ATYDGDTPREERRAIirNPPRILLTNPDMLHyALLPhhdRWA--RFLRNLRYVVLDEAHTY----RGVfgsHVALLLRRL 152
|
170 180 190
....*....|....*....|....*....|....*
gi 568935789 432 ktvqslsRDLESASPVPVRFVAVSATIPNAEDIAE 466
Cdd:cd17923 153 -------RRLCRRYGADPQFILTSATIGNPAEHAR 180
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
300-654 |
1.17e-14 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 79.97 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 300 ICAPTGSGKTVV-FELAITRLLME------VPLPWLNMKIVYMAPIKALCS--QR--------FDDWKEKFG--PVGLNC 360
Cdd:PRK09751 1 VIAPTGSGKTLAaFLYALDRLFREggedtrEAHKRKTSRILYISPIKALGTdvQRnlqiplkgIADERRRRGetEVNLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 361 KELTGDTVMDDLFEI--QHANIIITTPEK-WDSVTRKWRDNsfIQLVRLFLIDEVHVIKDENRGPTLEVvvsrmktvqSL 437
Cdd:PRK09751 81 GIRTGDTPAQERSKLtrNPPDILITTPESlYLMLTSRARET--LRGVETVIIDEVHAVAGSKRGAHLAL---------SL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 438 SRdLESASPVPVRFVAVSATIPNAEDIAEWLSdGERPAVCLKMDESHRPvKLQKVV-----LGFPCSSSQTEFKFDLALN 512
Cdd:PRK09751 150 ER-LDALLHTSAQRIGLSATVRSASDVAAFLG-GDRPVTVVNPPAMRHP-QIRIVVpvanmDDVSSVASGTGEDSHAGRE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 513 YKVY-----SVIRTYSDQKPTLVFCSTRkGV----------------QQAASVLVKDAKF-IISVEQKLRLQKSAYSIRD 570
Cdd:PRK09751 227 GSIWpyietGILDEVLRHRSTIVFTNSR-GLaekltarlnelyaarlQRSPSIAVDAAHFeSTSGATSNRVQSSDVFIAR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 571 SklkdtlvygvgyHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIKstmhysggVFEEYSETDILQMI 650
Cdd:PRK09751 306 S------------HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQ--------VATPLSVASGLQRI 365
|
....
gi 568935789 651 GRAG 654
Cdd:PRK09751 366 GRAG 369
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
295-468 |
1.09e-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: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 295 DRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLnmKIVYMAPIKALCS---QRFDDWKEKFG---PVGLNckelTGDT- 367
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV--QVLYISPLKALINdqeRRLEEPLDEIDleiPVAVR----HGDTs 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 368 ------VMDDLfeiqhANIIITTPEkwdSV----TRKWRDNSFiQLVRLFLIDEVHVIKDENRGPTLEVvvsrmktvqSL 437
Cdd:cd17922 75 qsekakQLKNP-----PGILITTPE---SLelllVNKKLRELF-AGLRYVVVDEIHALLGSKRGVQLEL---------LL 136
|
170 180 190
....*....|....*....|....*....|.
gi 568935789 438 SRdLESASPVPVRFVAVSATIPNAEDIAEWL 468
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 ... |
290-473 |
1.42e-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: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 290 DLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNMKIVYMAPIKALCSQ-------RFDdwkEKFGPVGLN-CK 361
Cdd:cd18025 11 DIVDRRESALIVAPTSSGKTFISYYCMEKVLRESD----DGVVVYVAPTKALVNQvvaevyaRFS---KKYPPSGKSlWG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 362 ELTGDTVMDDlfeIQHANIIITTPEKWDSVTRKWRDNSFIQLVRLFLIDEVHVIKDENRGPTLEvvvsrmktvqslsrDL 441
Cdd:cd18025 84 VFTRDYRHNN---PMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWE--------------QL 146
|
170 180 190
....*....|....*....|....*....|..
gi 568935789 442 ESASPVPvrFVAVSATIPNAEDIAEWLSDGER 473
Cdd:cd18025 147 LLLIPCP--FLALSATIGNPQKFHEWLQSVQR 176
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
579-656 |
2.72e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 66.47 E-value: 2.72e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568935789 579 YGVGYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMP-AHLVVIKSTmhysggvfeEYSETDILQMIGRAGRP 656
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 ... |
297-457 |
4.65e-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: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 297 NFVICAPTGSGKTVVFELAITRLLMEVPLpwlnmKIVYMAPIKALCSQRFDDWKEKFGPvGLNCKELTGDTVM--DDLFE 374
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKGK-----KVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAeeREKNK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 375 IQHANIIITTPEK-WDSVTRKWRdnSFIQLVRLFLIDEVHVIKDENRGptlevvvsrmkTVQSLSRDLESASPvPVRFVA 453
Cdd:cd00046 77 LGDADIIIATPDMlLNLLLREDR--LFLKDLKLIIVDEAHALLIDSRG-----------ALILDLAVRKAGLK-NAQVIL 142
|
....
gi 568935789 454 VSAT 457
Cdd:cd00046 143 LSAT 146
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
273-413 |
1.55e-10 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 61.15 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 273 IFKEFPYfnyiQSKAFDDLL----YTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPwlnmKIVYMAPIKALCSQRFDD 348
Cdd:pfam04851 1 KLELRPY----QIEAIENLLesikNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK----KVLFLVPRKDLLEQALEE 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568935789 349 WKEKFGPVGLNCKELTGDTvmdDLFEIQHANIIITTPEKWDSVTRKWRDNSFIQLVRLFLIDEVH 413
Cdd:pfam04851 73 FKKFLPNYVEIGEIISGDK---KDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
571-655 |
1.16e-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: 57.22 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 571 SKLKDTLVYGVGYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMP-AHLVVIkstmhYSGgvfeEYSETDILQM 649
Cdd:pfam00271 31 ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YDL----PWNPASYIQR 101
|
....*.
gi 568935789 650 IGRAGR 655
Cdd:pfam00271 102 IGRAGR 107
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
296-654 |
7.49e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 60.67 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 296 RNFVICAPTGSGKTVVFELAI----TRLLMEVPLPwlnMKI--VYMAPIKAL-------CSQRFDDWKEKFGPVGLNCKE 362
Cdd:PRK13767 48 KNVLISSPTGSGKTLAAFLAIidelFRLGREGELE---DKVycLYVSPLRALnndihrnLEEPLTEIREIAKERGEELPE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 363 L-----TGDTVMDD----LFEIQHanIIITTPEkwdS-----VTRKWRDnsFIQLVRLFLIDEVHVIKDENRGPTLEVvv 428
Cdd:PRK13767 125 IrvairTGDTSSYEkqkmLKKPPH--ILITTPE---SlaillNSPKFRE--KLRTVKWVIVDEIHSLAENKRGVHLSL-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 429 srmktvqSLSRDLESASPVPVRfVAVSATIPNAEDIAEWL---SDGERPAVCLKMDESH-RP--VKLQKVVLGFPCSSSQ 502
Cdd:PRK13767 196 -------SLERLEELAGGEFVR-IGLSATIEPLEEVAKFLvgyEDDGEPRDCEIVDARFvKPfdIKVISPVDDLIHTPAE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 503 TefkfdlaLNYKVYSVI-RTYSDQKPTLVFCSTRKGvqqAASVLVKdakfiisveqklrLQKSAYSIRDSKLkdtlvygV 581
Cdd:PRK13767 268 E-------ISEALYETLhELIKEHRTTLIFTNTRSG---AERVLYN-------------LRKRFPEEYDEDN-------I 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568935789 582 GYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPaH--LVVIKSTmhysggvfeEYSETDILQMIGRAG 654
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 ... |
295-460 |
3.02e-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: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 295 DRNFVICAPTGSGKTVVfelAItrLLMEVPLPWLNM----KIVYMAPIKALCSQRFDDWKEKFGPVGLNCKELTGDTVMD 370
Cdd:cd17927 17 GKNTIICLPTGSGKTFV---AV--LICEHHLKKFPAgrkgKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSEN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 371 DLFE--IQHANIIITTPEKWDSVTRKWRDNSfIQLVRLFLIDEVH-VIKDenrGPTLEVVVSrmktvqSLSRDLESASPV 447
Cdd:cd17927 92 VSVEqiVESSDVIIVTPQILVNDLKSGTIVS-LSDFSLLVFDECHnTTKN---HPYNEIMFR------YLDQKLGSSGPL 161
|
170
....*....|...
gi 568935789 448 PvRFVAVSATIPN 460
Cdd:cd17927 162 P-QILGLTASPGV 173
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
283-468 |
1.18e-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: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 283 IQSKAFDDLLyTDRNFVICAPTGSGKTVVFEL-AITRLLMEVPLPWLNMKIVYMAPIKALCSQRFDDWKEKFGPVGLNCK 361
Cdd:cd00268 16 IQAQAIPLIL-SGRDVIGQAQTGSGKTLAFLLpILEKLLPEPKKKGRGPQALVLAPTRELAMQIAEVARKLGKGTGLKVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 362 ELTGDTVMDDLFEI--QHANIIITTPEK-WDSVTRKwrdnsFIQL--VRLFLIDEVHVIKDENRGPTLEVVVSRM-KTVQ 435
Cdd:cd00268 95 AIYGGAPIKKQIEAlkKGPDIVVGTPGRlLDLIERG-----KLDLsnVKYLVLDEADRMLDMGFEEDVEKILSALpKDRQ 169
|
170 180 190
....*....|....*....|....*....|....
gi 568935789 436 SLsrdlesaspvpvrfvAVSATIPNA-EDIAEWL 468
Cdd:cd00268 170 TL---------------LFSATLPEEvKELAKKF 188
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
284-413 |
5.95e-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: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 284 QSKAFDDLLytDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNMKI-VYMAPIKALCSQRFDDWKEKfgpVGLNCKE 362
Cdd:cd18034 7 QLELFEAAL--KRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNPKKRaVFLVPTVPLVAQQAEAIRSH---TDLKVGE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568935789 363 LTGDTVMDD------LFEIQHANIIITTPEkwdsVTRKWRDNSFIQL--VRLFLIDEVH 413
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 ... |
296-385 |
9.55e-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: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 296 RNFVICAPTGSGKTVVFELAItrlLMEVPLPWLNMKI--VYMAPIKALCSQRFDDWKEKFGPVGLNCKELTG---DTVMD 370
Cdd:cd17957 28 RDLLACAPTGSGKTLAFLIPI---LQKLGKPRKKKGLraLILAPTRELASQIYRELLKLSKGTGLRIVLLSKsleAKAKD 104
|
90
....*....|....*
gi 568935789 371 DLFEIQHANIIITTP 385
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 ... |
294-386 |
3.74e-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: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 294 TDRNFVICAPTGSGKTVVfELAITRLLMEVPLPWLNMKIVYMAPIKALCSQRFDDWKEKFGPVGLNCKELTGDTvmDDLF 373
Cdd:cd18073 16 KGKNTIICAPTGCGKTFV-SLLICEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGAT--AENV 92
|
90
....*....|....*..
gi 568935789 374 E----IQHANIIITTPE 386
Cdd:cd18073 93 PveqiIENNDIIILTPQ 109
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
296-413 |
7.30e-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: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 296 RNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNMKIVYMAPIKALCSQRfddwKEKFGPV---GLNCKELTGDTVMDDL 372
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQQ----LEKFFKYfrkGYKVTGLSGDSSHKVS 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568935789 373 F--EIQHANIIITTPEKWDSVTRKWRDNSFIQL--VRLFLIDEVH 413
Cdd:cd18036 94 FgqIVKASDVIICTPQILINNLLSGREEERVYLsdFSLLIFDECH 138
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
258-385 |
1.58e-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: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 258 GSLKAVTEIPAKFRNIFKE-FPYFNYIQSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLmEVPLPWLNMKIVYMA 336
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKgYKVPTPIQRKTIPLIL-DGRDVVAMARTGSGKTAAFLIPMIEKL-KAHSPTVGARALILS 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568935789 337 PIKALCSQRFDDWKE--KFgpVGLNCKELTGDTVMDDLFEIQHAN--IIITTP 385
Cdd:cd17959 79 PTRELALQTLKVTKElgKF--TDLRTALLVGGDSLEEQFEALASNpdIIIATP 129
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
516-655 |
1.73e-05 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 48.98 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 516 YSVIRTYSDQK--------------PTLVFCSTRKGVQQAASvlvkdakfiisveqklRLQKSAYSirdsklkdtlvygV 581
Cdd:COG0514 207 LEVVPKPPDDKlaqlldflkehpggSGIVYCLSRKKVEELAE----------------WLREAGIR-------------A 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 582 GYHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMG-----------MNMPAHLvvikstmhysggvfEEYsetdiLQMI 650
Cdd:COG0514 258 AAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGidkpdvrfvihYDLPKSI--------------EAY-----YQEI 318
|
....*
gi 568935789 651 GRAGR 655
Cdd:COG0514 319 GRAGR 323
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
299-413 |
2.45e-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: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 299 VICAPTGSGKTVVfELAITRLLMEvplpwlnMKIVYMAPIKALCSQrfddWKEKFGpvglncKELTGDTVM----DDLFE 374
Cdd:cd17926 22 ILVLPTGSGKTLT-ALALIAYLKE-------LRTLIVVPTDALLDQ----WKERFE------DFLGDSSIGliggGKKKD 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568935789 375 IQHANIIITTpekWDSVTRKWRDNSFIQLVRLFLI-DEVH 413
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 ... |
503-655 |
2.76e-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: 45.28 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 503 TEFKFDLALNYKVYSvirtysDQKPTLVFCSTRKGVQQAASvlvkdakfiisveqklRLQKSAYSirdsklkdtlvygVG 582
Cdd:cd18794 14 KDEKLDLLKRIKVEH------LGGSGIIYCLSRKECEQVAA----------------RLQSKGIS-------------AA 58
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568935789 583 YHHAGMELSDRKLVEGLFTSGDLPVLFTTSTLAMGMNMPAHLVVIkstmHYS-GGVFEEYsetdiLQMIGRAGR 655
Cdd:cd18794 59 AYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVI----HYSlPKSMESY-----YQESGRAGR 123
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
295-418 |
3.63e-05 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 48.57 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 295 DRNFVICAPTGSGKTVVFELAITRLLMEVplpwlNMKIVYMAPIKALCSQRFDDWKEKFGPVGLNCKELTGDTVMDDLFE 374
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAERLHKK-----GGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKRKE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568935789 375 I-QHANIIITTPE--KWDSVTRkwrdnsfiqlvRLFLIDEVHVIKDE 418
Cdd:COG1111 92 LwEKARIIVATPQviENDLIAG-----------RIDLDDVSLLIFDE 127
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
295-461 |
7.20e-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: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 295 DRNFVICAPTGSGKTvvfELAITRLLmEVPLPWLNMKIVYMAPIKALCSQRFDDWKEKFGPVGLNCK--ELTGDT--VMD 370
Cdd:cd17930 1 PGLVILEAPTGSGKT---EAALLWAL-KLAARGGKRRIIYALPTRATINQMYERIREILGRLDDEDKvlLLHSKAalELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 371 DLFEIQHANIIITTpEKWDSVTRKWrDNSFI----------------QLVRLFL-------IDEVHVIKDENRGPTLEVv 427
Cdd:cd17930 77 ESDEEPDDDPVEAV-DWALLLKRSW-LAPIVvttidqllesllkykhFERRLHGlansvvvLDEVQAYDPEYMALLLKA- 153
|
170 180 190
....*....|....*....|....*....|....
gi 568935789 428 vsrmktvqsLSRDLESASpvpVRFVAVSATIPNA 461
Cdd:cd17930 154 ---------LLELLGELG---GPVVLMTATLPAL 175
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
599-655 |
1.14e-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: 1.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568935789 599 LFTSGDLP--VLFTTSTLAMGMNMPAHLVVIKSTMHYSGGVFEEYSETDILQMIGRAGR 655
Cdd:cd18805 63 LFNDPESGydVLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMRPLSPSEVKQIAGRAGR 121
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
292-470 |
1.19e-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: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 292 LYTDRNFVICAPTGSGKTVVFELAIT-RLL---MEVPLPWLNMKIVYMAPIKALCSQrFDDWKEKFG-PVGLNCKELTGD 366
Cdd:cd17948 24 ILRGRNTLCAAETGSGKTLTYLLPIIqRLLrykLLAEGPFNAPRGLVITPSRELAEQ-IGSVAQSLTeGLGLKVKVITGG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 367 TVMDDL--FEIQHANIIITTPekwdSVTRKWRDNSFIQL--VRLFLIDEVHVIKDENRGPTLEVVVSRMKtVQSLSRDLE 442
Cdd:cd17948 103 RTKRQIrnPHFEEVDILVATP----GALSKLLTSRIYSLeqLRHLVLDEADTLLDDSFNEKLSHFLRRFP-LASRRSENT 177
|
170 180
....*....|....*....|....*...
gi 568935789 443 SASPVPVRFVAVSATIPnaEDIAEWLSD 470
Cdd:cd17948 178 DGLDPGTQLVLVSATMP--SGVGEVLSK 203
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
297-413 |
1.23e-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: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 297 NFVICAPTGSGKTVvfelaITRLLMEVPLPWL-NMKIVYMAPIKALCSQRFDDWKEKFGPVGLNCKELTGDTVMDD-LFE 374
Cdd:cd18033 18 NTLVALPTGLGKTF-----IAAVVMLNYYRWFpKGKIVFMAPTKPLVSQQIEACYKITGIPSSQTAELTGSVPPTKrAEL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568935789 375 IQHANIIITTPEKWDS-VTRKWRDNSFIQLVrlfLIDEVH 413
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 ... |
294-459 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 294 TDRNFVICAPTGSGKTVVFEL-AITRLLMEVPLPwlnmKIVYMAPIKALCSQRFDDWKEkFGPVGLNCKE---LTGDTVM 369
Cdd:cd17962 26 LGRDILASADTGSGKTAAFLLpVIIRCLTEHRNP----SALILTPTRELAVQIEDQAKE-LMKGLPPMKTallVGGLPLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 370 DDLFEI-QHANIIITTPEKWDSVTRKwrdnSFIQL--VRLFLIDEVHVIKdeNRGPTLEVvvsrMKTVQSLSRDLESasp 446
Cdd:cd17962 101 PQLYRLqQGVKVIIATPGRLLDILKQ----SSVELdnIKIVVVDEADTML--KMGFQQQV----LDILENISHDHQT--- 167
|
170
....*....|...
gi 568935789 447 vpvrfVAVSATIP 459
Cdd:cd17962 168 -----ILVSATIP 175
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
300-467 |
2.10e-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: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 300 ICAPTGSGKTVVFELAITRLLMEVPLPWLNMKIVymAPIKALCSQRFDDWKEKFGPVGLNCKELTGDTV----MDDLFEI 375
Cdd:cd17956 41 VSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIV--VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSfkkeQKLLLVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 376 QH------ANIIITTPEKW-DSVTRKwrdNSFI-QLVRLFLIDEVHVIKDENRGPTLEVVVSRMKTVQSLSRDLESA--- 444
Cdd:cd17956 119 TSgrylsrVDILVATPGRLvDHLNST---PGFTlKHLRFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLGSFGDanl 195
|
170 180
....*....|....*....|....*..
gi 568935789 445 ---SPVPVRFVAVSATIP-NAEDIAEW 467
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 ... |
302-385 |
2.47e-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: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 302 APTGSGKTVVFELAITRLLMEVPLPwlnMKIVYMAPIKALCSQRFDDWKEKFGPVGLNCKELTG--DTVMDDLFEIQHAN 379
Cdd:cd17954 44 AETGSGKTAAFALPILQALLENPQR---FFALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGgmDMMAQAIALAKKPH 120
|
....*.
gi 568935789 380 IIITTP 385
Cdd:cd17954 121 VIVATP 126
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
528-655 |
2.75e-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: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 528 TLVFCSTRKGVQqaasvlvkdakfiiSVEQKLRLqksaysiRDSKLKDTLVYGVgyHHAGMELSDRKLVEGLFTSGDLPV 607
Cdd:cd18796 41 TLVFTNTRSQAE--------------RLAQRLRE-------LCPDRVPPDFIAL--HHGSLSRELREEVEAALKRGDLKV 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 568935789 608 LFTTSTLAMGMNMPA-HLVV-IKSTmhysggvfeeYSETDILQMIGRAGR 655
Cdd:cd18796 98 VVATSSLELGIDIGDvDLVIqIGSP----------KSVARLLQRLGRSGH 137
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
518-655 |
2.79e-03 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 42.01 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 518 VIRTYSDQ--KPTLVFCSTRKGVQQAASvlvkdakfiisveqklRLQKSAYSirdsklkdtlvygVGYHHAGMELSDRKL 595
Cdd:PRK11057 227 LMRYVQEQrgKSGIIYCNSRAKVEDTAA----------------RLQSRGIS-------------AAAYHAGLDNDVRAD 277
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568935789 596 VEGLFTSGDLPVLFTTSTLAMGMNMP-----AHLVVIKSTMHYsggvfeeYSETdilqmiGRAGR 655
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 ... |
528-655 |
2.98e-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: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 528 TLVFCSTRKgvqqAASVLVKDAKFIISVEQKLrlqksaysirdsklkdtlVYGVGYHHAGMELSDRKLVEGLFTSGDLPV 607
Cdd:cd18797 38 TIVFCRSRK----LAELLLRYLKARLVEEGPL------------------ASKVASYRAGYLAEDRREIEAELFNGELLG 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568935789 608 LFTTSTLAMGMNMPAHLVVIKSTmhYSGGVFEeysetdILQMIGRAGR 655
Cdd:cd18797 96 VVATNALELGIDIGGLDAVVLAG--YPGSLAS------LWQQAGRAGR 135
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
268-552 |
4.06e-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: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 268 AKFRNIFKEFPYFNYIQSKAFDDLLYTDRN----FVICAPTGSGKTvvfeLAITRLLMEVPLPWLNMKIVYMAPIKALCS 343
Cdd:COG1203 116 RLLPKKSKPRTPINPLQNEALELALEAAEEepglFILTAPTGGGKT----EAALLFALRLAAKHGGRRIIYALPFTSIIN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 344 QRFDDWKEKFGP-VGlnckELTGDTVM-----DDLFEIQH-----------ANIIITTPEK-WDSVTRKWRdNSFIQLVR 405
Cdd:COG1203 192 QTYDRLRDLFGEdVL----LHHSLADLdlleeEEEYESEArwlkllkelwdAPVVVTTIDQlFESLFSNRK-GQERRLHN 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935789 406 L----FLIDEVHVIkDENRGPTLEVVVSRMKTVQSlsrdlesaspvpvRFVAVSATIPNA-----EDIAEWLSDGERPAV 476
Cdd:COG1203 267 LansvIILDEVQAY-PPYMLALLLRLLEWLKNLGG-------------SVILMTATLPPLlreelLEAYELIPDEPEELP 332
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568935789 477 CLKMDESHRPVKLQKVVLgfpcssSQTEFkfdlalnykVYSVIRTYSDQKPTLVFCSTRKGVQQAASVLVKDAKFI 552
Cdd:COG1203 333 EYFRAFVRKRVELKEGPL------SDEEL---------AELILEALHKGKSVLVIVNTVKDAQELYEALKEKLPDE 393
|
|
| |
