|
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 ... |
280-488 |
6.93e-125 |
|
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: 386.33 E-value: 6.93e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 280 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEV-PLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIG 358
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERnPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 359 LNCKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDN-SLVQLVRLFLIDEVHIVKdENRGPTLEVVVSRMKTVQS 437
Cdd:cd18023 81 LSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIK-ENRGATLEVVVSRMKTLSS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1804891964 438 VSQTlkNTSTAIPMRFVAVSATIPNAEDIAEWLSDGerPAVCLKMDESHRP 488
Cdd:cd18023 160 SSEL--RGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFGESFRP 206
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
264-798 |
4.27e-103 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 339.18 E-value: 4.27e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 264 VTEIP-AKFRSIFKEFPY--FNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIK 340
Cdd:COG1204 3 VAELPlEKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN------GGKALYIVPLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 341 ALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRK---WRDNslvqlVRLFLIDEVHIVK 417
Cdd:COG1204 77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRNgpsWLRD-----VDLVVVDEAHLID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 418 DENRGPTLEVVVSRMKTVqsvsqtlkntstAIPMRFVAVSATIPNAEDIAEWLsdgERPAVclkmDESHRPVKLQKVVLg 497
Cdd:COG1204 151 DESRGPTLEVLLARLRRL------------NPEAQIVALSATIGNAEEIAEWL---DAELV----KSDWRPVPLNEGVL- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 498 fpcSSNQTEF--KFDLTLNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVR---- 571
Cdd:COG1204 211 ---YDGVLRFddGSRRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLevse 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 572 ----DSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTmHYAGGlfEEYSETD 647
Cdd:COG1204 288 ethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-KRGGM--VPIPVLE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 648 ILQMIGRAGRPQFDTTATAVIMTR-LSTRDKYIQMLACRDT--VESSLH--RHLIEHLNAEIVLHTITDVNIAVEWIRST 722
Cdd:COG1204 365 FKQMAGRAGRPGYDPYGEAILVAKsSDEADELFERYILGEPepIRSKLAneSALRTHLLALIASGFANSREELLDFLENT 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804891964 723 LLYIRAlknpshygfasglNKDGIEAKLQElclkNLNDLSSLDLIKMDEGvNFKPTEAGRLMAWYYITFETVKKFY 798
Cdd:COG1204 445 FYAYQY-------------DKGDLEEVVDD----ALEFLLENGFIEEDGD-RLRATKLGKLVSRLYIDPLTAAELV 502
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
777-1090 |
4.32e-71 |
|
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: 240.57 E-value: 4.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 777 PTEAGRLMAWYYITFETVKKFYT-ISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKdpnriTIRFPMEGRIKTR 855
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQsLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLE-----KVPIPVKGDIEDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 856 EMKVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWeNSLHVSKQLE 935
Cdd:pfam02889 76 HAKVNILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFE-ILLSKGWLSAALTALDLCKMIEQRMW-DSDSPLRQFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 936 KIGITLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEqITRYSDTTAEILVTVIlRNFE 1015
Cdd:pfam02889 154 GIPPELIKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAE-VQPITRSVLRVEVTIT-PDFP 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804891964 1016 qlQTKRTASDSHYVTLIIGDADNQVVYLHKITdSVLLKAGSWAKKIAVKRALKSE---DLSINLISSEFVGLDIQQKL 1090
Cdd:pfam02889 232 --WDKRVHGKSEGFWLVVGDSDGNEILHIERF-TLTKRTLAGEHKLEFTVPPSDPgppQLFVRLISDSWLGADQEVPI 306
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
777-1092 |
7.50e-63 |
|
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: 217.23 E-value: 7.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 777 PTEAGRLMAWYYITFETVKKFYT-ISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKDpnritIRFPMEGRIKTR 855
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQsLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-----VPIPVKEGIIDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 856 EM-KVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWENSLHVSKQL 934
Cdd:smart00973 76 PHaKVNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVD-IALSKGWLRTALNALDLSQMVVQRLWEDSDSPLKQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 935 EKIGI--TLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEQITRYSDTTaeILVTVILR 1012
Cdd:smart00973 155 PHFLIedVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITRDLT--LRVELEIT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 1013 NFEQLQTKRTASDSHYVTLIIGDADNQVVYLHKITDSVLLKAGSWAK-KIAVKR-ALKSEDLSINLISSEFVGLDIQQKL 1090
Cdd:smart00973 233 PVFAWDLPRHKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKlDFTVPLsEPGPENYTVYLISDSYLGCDQEVSF 312
|
..
gi 1804891964 1091 TV 1092
Cdd:smart00973 313 SL 314
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
487-671 |
3.18e-59 |
|
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: 200.47 E-value: 3.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 487 RPVKLQKVVLGFPCSSNQTEFKFDLT--LNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVkdakfimtveqkqrlq 564
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 565 kyaysvrdsklrdilkdGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYS 644
Cdd:cd18795 65 -----------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELS 127
|
170 180
....*....|....*....|....*..
gi 1804891964 645 ETDILQMIGRAGRPQFDTTATAVIMTR 671
Cdd:cd18795 128 PLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
285-669 |
1.57e-50 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 192.48 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 285 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEkFGPIGLNCKEL 364
Cdd:PRK02362 28 QAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIAR------GGKALYIVPLRALASEKFEEFER-FEELGVRVGIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 365 TGDTVMDDLFeIQHAHIIMTTPEKWDSMTRK---W-RDNSLVqlvrlfLIDEVHIVKDENRGPTLEVVVSRMKTVQSVSQ 440
Cdd:PRK02362 101 TGDYDSRDEW-LGDNDIIVATSEKVDSLLRNgapWlDDITCV------VVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 441 TlkntstaipmrfVAVSATIPNAEDIAEWLsDGERpavclkMDESHRPVKLQKVVL---GFPCSSNQTEFKF---DLTLN 514
Cdd:PRK02362 174 V------------VALSATIGNADELADWL-DAEL------VDSEWRPIDLREGVFyggAIHFDDSQREVEVpskDDTLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 515 YkiasVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDS-------KLRDILKDGAAYHH 587
Cdd:PRK02362 235 L----VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVsdtetskDLADCVAKGAAFHH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 588 AGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGL------FEEYSetdilQMIGRAGRPQFD 661
Cdd:PRK02362 311 AGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAgmqpipVLEYH-----QMAGRAGRPGLD 385
|
....*...
gi 1804891964 662 TTATAVIM 669
Cdd:PRK02362 386 PYGEAVLL 393
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
285-797 |
1.78e-50 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 191.95 E-value: 1.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 285 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAIT-RLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEkFGPIGLNCKE 363
Cdd:PRK00254 28 QAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVnKLLRE------GGKAVYLVPLKALAEEKYREFKD-WEKLGLRVAM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 364 LTGDTVMDDLFeIQHAHIIMTTPEKWDSMTRkwRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVQSVsqtlk 443
Cdd:PRK00254 101 TTGDYDSTDEW-LGKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQI----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 444 ntstaipmrfVAVSATIPNAEDIAEWLSdgerpAVCLKMDesHRPVKLQKVV--LGFPCSSNQTEFKFDLTLNykiASVI 521
Cdd:PRK00254 173 ----------LGLSATVGNAEELAEWLN-----AELVVSD--WRPVKLRKGVfyQGFLFWEDGKIERFPNSWE---SLVY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 522 QMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDS----KLRDILKDGAAYHHAGMELSDRKV 597
Cdd:PRK00254 233 DAVKKGKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKELADSLEENptneKLKKALRGGVAFHHAGLGRTERVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 598 VEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVIMTRL----S 673
Cdd:PRK00254 313 IEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTeepsK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 674 TRDKYI----QMLACRDTVESSLHRHLIehlnAEIVLHTITDVNIAVEWIRSTlLYIRALKNPSHygfasglnkdgIEAK 749
Cdd:PRK00254 393 LMERYIfgkpEKLFSMLSNESAFRSQVL----ALITNFGVSNFKELVNFLERT-FYAHQRKDLYS-----------LEEK 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1804891964 750 LQELC---LKNlndlsslDLIKMDEGVNFKPTEAGRLMAWYYITFETVKKF 797
Cdd:PRK00254 457 AKEIVyflLEN-------EFIDIDLEDRFIPLPLGIRTSQLYIDPLTAKKF 500
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
285-669 |
4.42e-49 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 188.22 E-value: 4.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 285 QSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEKFGP--IGLnck 362
Cdd:COG4581 30 QEEAILALE-AGRSVLVAAPTGSGKTLVAEFAIFLALAR------GRRSFYTAPIKALSNQKFFDLVERFGAenVGL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 363 eLTGDTVmddlfEIQHA-HIIMTTpEKWDSMTrkWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVsrmktvqsvsqt 441
Cdd:COG4581 100 -LTGDAS-----VNPDApIVVMTT-EILRNML--YREGADLEDVGVVVMDEFHYLADPDRGWVWEEPI------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 442 lkntsTAIP--MRFVAVSATIPNAEDIAEWLSD--GErpavCLKMDESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKI 517
Cdd:COG4581 159 -----IHLParVQLVLLSATVGNAEEFAEWLTRvrGE----TAVVVSEERPVPLEFHYLVTPRLFPLFRVNPELLRPPSR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 518 ASVIQM--YSDQKPTLVFCATRKGVQQAASVLVkdAKFIMTVEQKQRLQKYA-------YSVRDSKLRDILKDGAAYHHA 588
Cdd:COG4581 230 HEVIEEldRGGLLPAIVFIFSRRGCDEAAQQLL--SARLTTKEERAEIREAIdefaedfSVLFGKTLSRLLRRGIAVHHA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 589 GMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVI 668
Cdd:COG4581 308 GMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDTEGHVVV 387
|
.
gi 1804891964 669 M 669
Cdd:COG4581 388 L 388
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
284-466 |
1.42e-34 |
|
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: 130.44 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 284 IQSKAFDdLLYTDRNFVICAPTGSGKTVVFELAItrlLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLN-CK 362
Cdd:pfam00270 3 IQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPA---LEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKvAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 363 ELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRdnsLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTvqsvsqtl 442
Cdd:pfam00270 79 LLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-------- 147
|
170 180
....*....|....*....|....*
gi 1804891964 443 kntstaiPMRFVAVSATIP-NAEDI 466
Cdd:pfam00270 148 -------KRQILLLSATLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
276-470 |
1.18e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.04 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 276 KEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQRFDDWKEKFG 355
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK----GGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 356 PIGLN-CKELTGDTVMDDLFEIQH--AHIIMTTPEKWDSMTRKwrDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRM 432
Cdd:smart00487 80 SLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1804891964 433 KTVQsvsqtlkntstaipmRFVAVSATIPNAEDIAEWL 470
Cdd:smart00487 158 PKNV---------------QLLLLSATPPEEIENLLEL 180
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
579-658 |
1.77e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.16 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 579 LKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIKSTmhyagglfeEYSETDILQMIGRAGR 657
Cdd:smart00490 10 LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL---------PWSPASYIQRIGRAGR 80
|
.
gi 1804891964 658 P 658
Cdd:smart00490 81 A 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
516-657 |
1.84e-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: 56.45 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 516 KIASVIQMYSDQKP--TLVFCATRKGVqqaasvlvkDAKFImtveqkqrLQKYAYSVrdsklrdilkdgaAYHHAGMELS 593
Cdd:pfam00271 2 KLEALLELLKKERGgkVLIFSQTKKTL---------EAELL--------LEKEGIKV-------------ARLHGDLSQE 51
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804891964 594 DRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIkstmhyagglFE-EYSETDILQMIGRAGR 657
Cdd:pfam00271 52 EREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN----------YDlPWNPASYIQRIGRAGR 107
|
|
| |
|
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 ... |
280-488 |
6.93e-125 |
|
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: 386.33 E-value: 6.93e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 280 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEV-PLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIG 358
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERnPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 359 LNCKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDN-SLVQLVRLFLIDEVHIVKdENRGPTLEVVVSRMKTVQS 437
Cdd:cd18023 81 LSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIK-ENRGATLEVVVSRMKTLSS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1804891964 438 VSQTlkNTSTAIPMRFVAVSATIPNAEDIAEWLSDGerPAVCLKMDESHRP 488
Cdd:cd18023 160 SSEL--RGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFGESFRP 206
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
264-798 |
4.27e-103 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 339.18 E-value: 4.27e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 264 VTEIP-AKFRSIFKEFPY--FNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIK 340
Cdd:COG1204 3 VAELPlEKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN------GGKALYIVPLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 341 ALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRK---WRDNslvqlVRLFLIDEVHIVK 417
Cdd:COG1204 77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRNgpsWLRD-----VDLVVVDEAHLID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 418 DENRGPTLEVVVSRMKTVqsvsqtlkntstAIPMRFVAVSATIPNAEDIAEWLsdgERPAVclkmDESHRPVKLQKVVLg 497
Cdd:COG1204 151 DESRGPTLEVLLARLRRL------------NPEAQIVALSATIGNAEEIAEWL---DAELV----KSDWRPVPLNEGVL- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 498 fpcSSNQTEF--KFDLTLNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVR---- 571
Cdd:COG1204 211 ---YDGVLRFddGSRRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLevse 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 572 ----DSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTmHYAGGlfEEYSETD 647
Cdd:COG1204 288 ethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-KRGGM--VPIPVLE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 648 ILQMIGRAGRPQFDTTATAVIMTR-LSTRDKYIQMLACRDT--VESSLH--RHLIEHLNAEIVLHTITDVNIAVEWIRST 722
Cdd:COG1204 365 FKQMAGRAGRPGYDPYGEAILVAKsSDEADELFERYILGEPepIRSKLAneSALRTHLLALIASGFANSREELLDFLENT 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804891964 723 LLYIRAlknpshygfasglNKDGIEAKLQElclkNLNDLSSLDLIKMDEGvNFKPTEAGRLMAWYYITFETVKKFY 798
Cdd:COG1204 445 FYAYQY-------------DKGDLEEVVDD----ALEFLLENGFIEEDGD-RLRATKLGKLVSRLYIDPLTAAELV 502
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
777-1090 |
4.32e-71 |
|
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: 240.57 E-value: 4.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 777 PTEAGRLMAWYYITFETVKKFYT-ISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKdpnriTIRFPMEGRIKTR 855
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQsLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLE-----KVPIPVKGDIEDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 856 EMKVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWeNSLHVSKQLE 935
Cdd:pfam02889 76 HAKVNILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFE-ILLSKGWLSAALTALDLCKMIEQRMW-DSDSPLRQFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 936 KIGITLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEqITRYSDTTAEILVTVIlRNFE 1015
Cdd:pfam02889 154 GIPPELIKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAE-VQPITRSVLRVEVTIT-PDFP 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804891964 1016 qlQTKRTASDSHYVTLIIGDADNQVVYLHKITdSVLLKAGSWAKKIAVKRALKSE---DLSINLISSEFVGLDIQQKL 1090
Cdd:pfam02889 232 --WDKRVHGKSEGFWLVVGDSDGNEILHIERF-TLTKRTLAGEHKLEFTVPPSDPgppQLFVRLISDSWLGADQEVPI 306
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
280-474 |
5.51e-68 |
|
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: 226.76 E-value: 5.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 280 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVplpwlNIKIVYMAPIKALCSQRFDDWKEKFGPIGL 359
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-----GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 360 NCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRKWRDNsLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVQsvs 439
Cdd:cd17921 76 NVGLLTGDPSVNKL-LLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRIN--- 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1804891964 440 qtlkntstaIPMRFVAVSATIPNAEDIAEWLSDGE 474
Cdd:cd17921 151 ---------KNARFVGLSATLPNAEDLAEWLGVED 176
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
777-1092 |
7.50e-63 |
|
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: 217.23 E-value: 7.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 777 PTEAGRLMAWYYITFETVKKFYT-ISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKDpnritIRFPMEGRIKTR 855
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQsLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-----VPIPVKEGIIDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 856 EM-KVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWENSLHVSKQL 934
Cdd:smart00973 76 PHaKVNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVD-IALSKGWLRTALNALDLSQMVVQRLWEDSDSPLKQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 935 EKIGI--TLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEQITRYSDTTaeILVTVILR 1012
Cdd:smart00973 155 PHFLIedVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITRDLT--LRVELEIT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 1013 NFEQLQTKRTASDSHYVTLIIGDADNQVVYLHKITDSVLLKAGSWAK-KIAVKR-ALKSEDLSINLISSEFVGLDIQQKL 1090
Cdd:smart00973 233 PVFAWDLPRHKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKlDFTVPLsEPGPENYTVYLISDSYLGCDQEVSF 312
|
..
gi 1804891964 1091 TV 1092
Cdd:smart00973 313 SL 314
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
487-671 |
3.18e-59 |
|
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: 200.47 E-value: 3.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 487 RPVKLQKVVLGFPCSSNQTEFKFDLT--LNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVkdakfimtveqkqrlq 564
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 565 kyaysvrdsklrdilkdGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYS 644
Cdd:cd18795 65 -----------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELS 127
|
170 180
....*....|....*....|....*..
gi 1804891964 645 ETDILQMIGRAGRPQFDTTATAVIMTR 671
Cdd:cd18795 128 PLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
278-470 |
7.52e-59 |
|
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: 200.95 E-value: 7.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 278 FPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQRFDDWKEKFGP- 356
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNP----KGRAVYIAPMQELVDARYKDWRAKFGPl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 357 IGLNCKELTGDTVMdDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDENrGPTLEVVVSRMKTVQ 436
Cdd:cd18021 77 LGKKVVKLTGETST-DLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGEN-GPVYEVVVSRMRYIS 154
|
170 180 190
....*....|....*....|....*....|....
gi 1804891964 437 svSQTLKntstaiPMRFVAVSATIPNAEDIAEWL 470
Cdd:cd18021 155 --SQLEK------PIRIVGLSSSLANARDVGEWL 180
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
280-470 |
2.35e-57 |
|
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: 196.44 E-value: 2.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 280 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQRFDDWKEKF-GPIG 358
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYP----GSKVVYIAPLKALVRERVDDWKKRFeEKLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 359 LNCKELTGDtVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDEnRGPTLEVVVSRMKTVQSV 438
Cdd:cd18022 77 KKVVELTGD-VTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSD-RGPVLEVIVSRMNYISSQ 154
|
170 180 190
....*....|....*....|....*....|..
gi 1804891964 439 sqtlkntsTAIPMRFVAVSATIPNAEDIAEWL 470
Cdd:cd18022 155 --------TEKPVRLVGLSTALANAGDLANWL 178
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
285-669 |
1.57e-50 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 192.48 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 285 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEkFGPIGLNCKEL 364
Cdd:PRK02362 28 QAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIAR------GGKALYIVPLRALASEKFEEFER-FEELGVRVGIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 365 TGDTVMDDLFeIQHAHIIMTTPEKWDSMTRK---W-RDNSLVqlvrlfLIDEVHIVKDENRGPTLEVVVSRMKTVQSVSQ 440
Cdd:PRK02362 101 TGDYDSRDEW-LGDNDIIVATSEKVDSLLRNgapWlDDITCV------VVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 441 TlkntstaipmrfVAVSATIPNAEDIAEWLsDGERpavclkMDESHRPVKLQKVVL---GFPCSSNQTEFKF---DLTLN 514
Cdd:PRK02362 174 V------------VALSATIGNADELADWL-DAEL------VDSEWRPIDLREGVFyggAIHFDDSQREVEVpskDDTLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 515 YkiasVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDS-------KLRDILKDGAAYHH 587
Cdd:PRK02362 235 L----VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVsdtetskDLADCVAKGAAFHH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 588 AGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGL------FEEYSetdilQMIGRAGRPQFD 661
Cdd:PRK02362 311 AGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAgmqpipVLEYH-----QMAGRAGRPGLD 385
|
....*...
gi 1804891964 662 TTATAVIM 669
Cdd:PRK02362 386 PYGEAVLL 393
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
285-797 |
1.78e-50 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 191.95 E-value: 1.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 285 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAIT-RLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEkFGPIGLNCKE 363
Cdd:PRK00254 28 QAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVnKLLRE------GGKAVYLVPLKALAEEKYREFKD-WEKLGLRVAM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 364 LTGDTVMDDLFeIQHAHIIMTTPEKWDSMTRkwRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVQSVsqtlk 443
Cdd:PRK00254 101 TTGDYDSTDEW-LGKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQI----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 444 ntstaipmrfVAVSATIPNAEDIAEWLSdgerpAVCLKMDesHRPVKLQKVV--LGFPCSSNQTEFKFDLTLNykiASVI 521
Cdd:PRK00254 173 ----------LGLSATVGNAEELAEWLN-----AELVVSD--WRPVKLRKGVfyQGFLFWEDGKIERFPNSWE---SLVY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 522 QMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDS----KLRDILKDGAAYHHAGMELSDRKV 597
Cdd:PRK00254 233 DAVKKGKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKELADSLEENptneKLKKALRGGVAFHHAGLGRTERVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 598 VEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVIMTRL----S 673
Cdd:PRK00254 313 IEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTeepsK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 674 TRDKYI----QMLACRDTVESSLHRHLIehlnAEIVLHTITDVNIAVEWIRSTlLYIRALKNPSHygfasglnkdgIEAK 749
Cdd:PRK00254 393 LMERYIfgkpEKLFSMLSNESAFRSQVL----ALITNFGVSNFKELVNFLERT-FYAHQRKDLYS-----------LEEK 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1804891964 750 LQELC---LKNlndlsslDLIKMDEGVNFKPTEAGRLMAWYYITFETVKKF 797
Cdd:PRK00254 457 AKEIVyflLEN-------EFIDIDLEDRFIPLPLGIRTSQLYIDPLTAKKF 500
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
285-669 |
4.42e-49 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 188.22 E-value: 4.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 285 QSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEKFGP--IGLnck 362
Cdd:COG4581 30 QEEAILALE-AGRSVLVAAPTGSGKTLVAEFAIFLALAR------GRRSFYTAPIKALSNQKFFDLVERFGAenVGL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 363 eLTGDTVmddlfEIQHA-HIIMTTpEKWDSMTrkWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVsrmktvqsvsqt 441
Cdd:COG4581 100 -LTGDAS-----VNPDApIVVMTT-EILRNML--YREGADLEDVGVVVMDEFHYLADPDRGWVWEEPI------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 442 lkntsTAIP--MRFVAVSATIPNAEDIAEWLSD--GErpavCLKMDESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKI 517
Cdd:COG4581 159 -----IHLParVQLVLLSATVGNAEEFAEWLTRvrGE----TAVVVSEERPVPLEFHYLVTPRLFPLFRVNPELLRPPSR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 518 ASVIQM--YSDQKPTLVFCATRKGVQQAASVLVkdAKFIMTVEQKQRLQKYA-------YSVRDSKLRDILKDGAAYHHA 588
Cdd:COG4581 230 HEVIEEldRGGLLPAIVFIFSRRGCDEAAQQLL--SARLTTKEERAEIREAIdefaedfSVLFGKTLSRLLRRGIAVHHA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 589 GMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVI 668
Cdd:COG4581 308 GMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDTEGHVVV 387
|
.
gi 1804891964 669 M 669
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 ... |
264-470 |
1.35e-48 |
|
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: 172.55 E-value: 1.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 264 VTEIPAKFRSIFKEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNI-----KIVYMAP 338
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGTInldafKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 339 IKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKD 418
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKE-QISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1804891964 419 EnRGPTLEVVVSRmkTVQSVSQTLKntstaiPMRFVAVSATIPNAEDIAEWL 470
Cdd:cd18019 160 D-RGPVLESIVAR--TIRQIEQTQE------YVRLVGLSATLPNYEDVATFL 202
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
297-798 |
2.49e-42 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 166.60 E-value: 2.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 297 RNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKeKFGPIGLNCKELTGDtvMDDLFE- 375
Cdd:PRK01172 38 ENVIVSVPTAAGKTLIAYSAIYETFLA------GLKSIYIVPLRSLAMEKYEELS-RLRSLGMRVKISIGD--YDDPPDf 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 376 IQHAHIIMTTPEKWDSMTRkwRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVqsvsqtlkNTSTaipmRFVA 455
Cdd:PRK01172 109 IKRYDVVILTSEKADSLIH--HDPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSARYV--------NPDA----RILA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 456 VSATIPNAEDIAEWLSdgerpAVCLKmdESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKIASVIQmysDQKPTLVFCA 535
Cdd:PRK01172 175 LSATVSNANELAQWLN-----ASLIK--SNFRPVPLKLGILYRKRLILDGYERSQVDINSLIKETVN---DGGQVLVFVS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 536 TRKGVQQAASVLVK----DAKFIMTVEQKqrlqkyaySVRDSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLF 611
Cdd:PRK01172 245 SRKNAEDYAEMLIQhfpeFNDFKVSSENN--------NVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 612 TTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVI-MTRLSTRDKYIQMLACR-DTVE 689
Cdd:PRK01172 317 ATPTLAAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYIyAASPASYDAAKKYLSGEpEPVI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 690 SSLHRHLIEHLN--AEIVLHTITDVNIAVEWIRSTLLYIRAlknpshygfasglNKDGIEAKLQElclknlndlsSLDLI 767
Cdd:PRK01172 397 SYMGSQRKVRFNtlAAISMGLASSMEDLILFYNETLMAIQN-------------GVDEIDYYIES----------SLKFL 453
|
490 500 510
....*....|....*....|....*....|....*...
gi 1804891964 768 K----MDEGVNFKPTEAGRLMAWYYITFET---VKKFY 798
Cdd:PRK01172 454 KengfIKGDVTLRATRLGKLTSDLYIDPESaliLKSAF 491
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
282-470 |
2.53e-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: 2.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 282 NYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLME--VPLPWL---NIKIVYMAPIKALCSQRFDDWKEKFGP 356
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQhvNQGGVIkkdDFKIVYIAPMKALAAEMVEKFSKRLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 357 IGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRKWR-DNSLVQLVRLFLIDEVHIVKDEnRGPTLEVVVSR-MKT 434
Cdd:cd18020 83 LGIKVKELTGDMQLTKK-EIAETQIIVTTPEKWDVVTRKSSgDVALSQLVRLLIIDEVHLLHDD-RGPVIESLVARtLRQ 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1804891964 435 VQSvSQTLkntstaipMRFVAVSATIPNAEDIAEWL 470
Cdd:cd18020 161 VES-TQSM--------IRIVGLSATLPNYLDVADFL 187
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
280-470 |
2.60e-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: 144.40 E-value: 2.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 280 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKeKFGPIGL 359
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLE------GGKALYLVPLRALASEKYEEFK-KLEEIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 360 NCKELTGDTVMDDLFeIQHAHIIMTTPEKWDSMTR-KWrdnSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVqsv 438
Cdd:cd18028 74 KVGISTGDYDEDDEW-LGDYDIIVATYEKFDSLLRhSP---SWLRDVGVVVVDEIHLISDEERGPTLESIVARLRRL--- 146
|
170 180 190
....*....|....*....|....*....|..
gi 1804891964 439 sqtlkNTSTaipmRFVAVSATIPNAEDIAEWL 470
Cdd:cd18028 147 -----NPNT----QIIGLSATIGNPDELAEWL 169
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
284-466 |
1.42e-34 |
|
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: 130.44 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 284 IQSKAFDdLLYTDRNFVICAPTGSGKTVVFELAItrlLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLN-CK 362
Cdd:pfam00270 3 IQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPA---LEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKvAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 363 ELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRdnsLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTvqsvsqtl 442
Cdd:pfam00270 79 LLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-------- 147
|
170 180
....*....|....*....|....*
gi 1804891964 443 kntstaiPMRFVAVSATIP-NAEDI 466
Cdd:pfam00270 148 -------KRQILLLSATLPrNLEDL 165
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
267-660 |
3.07e-26 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 116.91 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 267 IPAKFRSIFK-EFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELA-ITRLLMEvplpwlNIKIVYMAPIKALCS 344
Cdd:COG1202 195 LPPELKDLLEgRGEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAgIKNALEG------KGKMLFLVPLVALAN 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 345 QRFDDWKEKFGPiGLNCKELTG---------DTVMDdlfeiqhAHIIMTTPEKWDSMTRKWRDNSLVQLVrlfLIDEVHI 415
Cdd:COG1202 269 QKYEDFKDRYGD-GLDVSIRVGasrirddgtRFDPN-------ADIIVGTYEGIDHALRTGRDLGDIGTV---VIDEVHM 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 416 VKDENRGPTLEVVVSRMKTVQSVSQtlkntstaipmrFVAVSATIPNAEDIAEWLSdgerpavcLKMDE-SHRPVKLQKV 494
Cdd:COG1202 338 LEDPERGHRLDGLIARLKYYCPGAQ------------WIYLSATVGNPEELAKKLG--------AKLVEyEERPVPLERH 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 495 VLgFpcssNQTEFKFDLtlnykIASVIQMYSDQKP-------TLVFCATRKgvqqaasvlvkdakfimtveqkqrlqkya 567
Cdd:COG1202 398 LT-F----ADGREKIRI-----INKLVKREFDTKSskgyrgqTIIFTNSRR----------------------------- 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 568 ysvRDSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKS-TMhyaGGlfEEYSET 646
Cdd:COG1202 439 ---RCHEIARALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSlAM---GI--EWLSVQ 510
|
410
....*....|....
gi 1804891964 647 DILQMIGRAGRPQF 660
Cdd:COG1202 511 EFHQMLGRAGRPDY 524
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
276-470 |
1.18e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.04 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 276 KEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQRFDDWKEKFG 355
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK----GGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 356 PIGLN-CKELTGDTVMDDLFEIQH--AHIIMTTPEKWDSMTRKwrDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRM 432
Cdd:smart00487 80 SLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1804891964 433 KTVQsvsqtlkntstaipmRFVAVSATIPNAEDIAEWL 470
Cdd:smart00487 158 PKNV---------------QLLLLSATPPEEIENLLEL 180
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
285-657 |
7.45e-22 |
|
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: 102.61 E-value: 7.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 285 QSKAFDdLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCS---QRFDDWKEKFGPiGLNC 361
Cdd:COG1205 61 QAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEALLEDP----GATALYLYPTKALARdqlRRLRELAEALGL-GVRV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 362 KELTGDTVMDDLFEI-QHAHIIMTTPEKWD-SM---TRKWRdnSLVQLVRLFLIDEVHIVkdenRGptleV-------VV 429
Cdd:COG1205 135 ATYDGDTPPEERRWIrEHPDIVLTNPDMLHyGLlphHTRWA--RFFRNLRYVVIDEAHTY----RG----VfgshvanVL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 430 SRMKTVqsvsqtLKNTSTAipMRFVAVSATIPNAEDIAEWLSDgeRPAVCLkmDESHRPVKLQKVVLGFPCSSNQTEFKF 509
Cdd:COG1205 205 RRLRRI------CRHYGSD--PQFILASATIGNPAEHAERLTG--RPVTVV--DEDGSPRGERTFVLWNPPLVDDGIRRS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 510 DLTLNYKIASVIqMYSDQKpTLVFCATRKGVQQAASVLvkdakfimtveqKQRLQKYAYSVRdsklrdIlkdgAAYhHAG 589
Cdd:COG1205 273 ALAEAARLLADL-VREGLR-TLVFTRSRRGAELLARYA------------RRALREPDLADR------V----AAY-RAG 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1804891964 590 MELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPA-HLVVIkstMHYAGglfeeySETDILQMIGRAGR 657
Cdd:COG1205 328 YLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVVL---AGYPG------TRASFWQQAGRAGR 387
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
276-471 |
1.15e-19 |
|
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: 89.04 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 276 KEFPY-FNYIQSKAFDDLlytDRN--FVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKE 352
Cdd:cd18024 27 RTYPFtLDPFQKTAIACI---ERNesVLVSAHTSAGKTVVAEYAIAQSLRD------KQRVIYTSPIKALSNQKYRELQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 353 KFGPIGLnckeLTGDTVMDDLFEIqhahIIMTTpEKWDSMTrkWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEvvvsrm 432
Cdd:cd18024 98 EFGDVGL----MTGDVTINPNASC----LVMTT-EILRSML--YRGSEIMREVAWVIFDEIHYMRDKERGVVWE------ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1804891964 433 KTVQSVSQTlkntstaipMRFVAVSATIPNAEDIAEWLS 471
Cdd:cd18024 161 ETIILLPDK---------VRYVFLSATIPNARQFAEWIC 190
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
285-470 |
9.79e-18 |
|
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: 82.70 E-value: 9.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 285 QSKAFDDLLYTDRNFViCAPTGSGKTVVFELAITRLLMEVplpwlnIKIVYMAPIKALCSQRFDDWKEKFGPIGLnckeL 364
Cdd:cd18027 13 QKQAILHLEAGDSVFV-AAHTSAGKTVVAEYAIALAQKHM------TRTIYTSPIKALSNQKFRDFKNTFGDVGL----I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 365 TGDTVMDDlfeiQHAHIIMTTpEKWDSMTrkWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKtvQSVSqtlkn 444
Cdd:cd18027 82 TGDVQLNP----EASCLIMTT-EILRSML--YNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLP--DHVS----- 147
|
170 180
....*....|....*....|....*.
gi 1804891964 445 tstaipmrFVAVSATIPNAEDIAEWL 470
Cdd:cd18027 148 --------IILLSATVPNTVEFADWI 165
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
775-1045 |
1.57e-17 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 85.39 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 775 FKPTEAGRLMAWYYITFETVKKFY-TISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKdpnRITIRFPMEGrIK 853
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNeLLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAE---KLPIRLENPS-LD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 854 TREMKVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWEnSLHVSKQ 933
Cdd:smart00611 78 DPHVKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVD-IALERGWLSTALNALNLSQMIIQALWP-TDSPLLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 934 LEKIGITLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYEL--KVEQITRysdTTAEILVTV-- 1009
Cdd:smart00611 156 LPHLPEEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIeiSLEPITR---TVLGVEVTLtv 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 1804891964 1010 -ILRNFEQLQTkrtasdSHYVTLIIGDADNQVVYLHK 1045
Cdd:smart00611 233 dLTWDDEIHGK------QEGWWLVIGDSDGNELLHIE 263
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
285-658 |
2.06e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 87.77 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 285 QSKAFDDLLYT----DRNFVICAPTGSGKTVVFELAITRLLmevplpwLNIKIVYMAPIKALCSQrfddWKEKFgpigln 360
Cdd:COG1061 85 QQEALEALLAAlergGGRGLVVAPTGTGKTVLALALAAELL-------RGKRVLVLVPRRELLEQ----WAEEL------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 361 cKELTGDTVMDDLFEIQHAHIIMTTpekWDSMTRKWRDNSLVQLVRLFLIDEVHIVkdenRGPTLEVVVSRMKtvqsvsq 440
Cdd:COG1061 148 -RRFLGDPLAGGGKKDSDAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHA----GAPSYRRILEAFP------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 441 tlkntstaiPMRFVAVSATiPNAED---IAEWLSDGERPAVCLK--MDESH-RPVKLQKVVLGFpcSSNQTEF-KFDLTL 513
Cdd:COG1061 213 ---------AAYRLGLTAT-PFRSDgreILLFLFDGIVYEYSLKeaIEDGYlAPPEYYGIRVDL--TDERAEYdALSERL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 514 NYKIAS-----------VIQMYSDQKPTLVFCATrkgvqqaasvlVKDAKFIMtveqkQRLQKYAYSvrdsklrdilkdg 582
Cdd:COG1061 281 REALAAdaerkdkilreLLREHPDDRKTLVFCSS-----------VDHAEALA-----ELLNEAGIR------------- 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804891964 583 AAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPA--HLVVIKSTMhyagglfeeySETDILQMIGRAGRP 658
Cdd:COG1061 332 AAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPTG----------SPREFIQRLGRGLRP 399
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
296-470 |
1.24e-14 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 73.00 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 296 DRNFVICAPTGSGKTVVFELAITRLLMEVPLPwlNIKIVYMAPIKALCSQRFDDWKEKfgpigLNCKEL-------TGDT 368
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEK--GVQVLYISPLKALINDQERRLEEP-----LDEIDLeipvavrHGDT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 369 -------VMDDLfeiqhAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVqsvsqt 441
Cdd:cd17922 74 sqsekakQLKNP-----PGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKL------ 142
|
170 180
....*....|....*....|....*....
gi 1804891964 442 lkntsTAIPMRFVAVSATIPNAEDIAEWL 470
Cdd:cd17922 143 -----TGRPLRRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
289-470 |
1.14e-13 |
|
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: 71.48 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 289 FDDLLYTDRNFVICAPTGSGKTVVFELAITRLLmevplpWLNIKIV-YMAPIKALCSQRFDDWKEKFGPIGLNCKELTGD 367
Cdd:cd18026 26 SLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRL------LERRKKAlFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 368 --TVMDDLFEiqHAHIIMTTPEKWDSMTrkwrdNSLVQLVRLFLI-----DEVHIVKDENRGPTLEVVVSRMktvqsvsq 440
Cdd:cd18026 100 kgRSPPKRRK--SLSVAVCTIEKANSLV-----NSLIEEGRLDELglvvvDELHMLGDGHRGALLELLLTKL-------- 164
|
170 180 190
....*....|....*....|....*....|
gi 1804891964 441 TLKNTSTaipMRFVAVSATIPNAEDIAEWL 470
Cdd:cd18026 165 LYAAQKN---IQIVGMSATLPNLEELASWL 191
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
291-475 |
3.02e-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: 69.70 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 291 DLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQ-------RFDdwkEKFGPIGLN-CK 362
Cdd:cd18025 11 DIVDRRESALIVAPTSSGKTFISYYCMEKVLRESD----DGVVVYVAPTKALVNQvvaevyaRFS---KKYPPSGKSlWG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 363 ELTGDTVMDDlfeIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEvvvsrmktvqsvsQTL 442
Cdd:cd18025 84 VFTRDYRHNN---PMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWE-------------QLL 147
|
170 180 190
....*....|....*....|....*....|...
gi 1804891964 443 kntsTAIPMRFVAVSATIPNAEDIAEWLSDGER 475
Cdd:cd18025 148 ----LLIPCPFLALSATIGNPQKFHEWLQSVQR 176
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
285-468 |
3.60e-13 |
|
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: 69.54 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 285 QSKAFDdLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALC-SQ--RFDDWKEKFGPiGLNC 361
Cdd:cd17923 5 QAEAIE-AARAGRSVVVTTGTASGKSLCYQLPILEALLRDP----GSRALYLYPTKALAqDQlrSLRELLEQLGL-GIRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 362 KELTGDTVMDDLFEI--QHAHIIMTTPEKWD-SMTR---KWRdnSLVQLVRLFLIDEVHIVkdenRGP---TLEVVVSRM 432
Cdd:cd17923 79 ATYDGDTPREERRAIirNPPRILLTNPDMLHyALLPhhdRWA--RFLRNLRYVVLDEAHTY----RGVfgsHVALLLRRL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1804891964 433 KtvqsvsQTLKNTSTAIpmRFVAVSATIPNAEDIAE 468
Cdd:cd17923 153 R------RLCRRYGADP--QFILTSATIGNPAEHAR 180
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
301-676 |
4.36e-13 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 74.58 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 301 ICAPTGSGKTVV-FELAITRLLME------VPLPWLNIKIVYMAPIKALCS--QR--------FDDWKEKFGPIGLNCKE 363
Cdd:PRK09751 1 VIAPTGSGKTLAaFLYALDRLFREggedtrEAHKRKTSRILYISPIKALGTdvQRnlqiplkgIADERRRRGETEVNLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 364 --LTGDTVMDDLFEI--QHAHIIMTTPEKWDSM-TRKWRDNslVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMktvqsv 438
Cdd:PRK09751 81 giRTGDTPAQERSKLtrNPPDILITTPESLYLMlTSRARET--LRGVETVIIDEVHAVAGSKRGAHLALSLERL------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 439 sQTLKNTstaiPMRFVAVSATIPNAEDIAEWLSdGERPAVCLKMDESHRPvKLQKVV-----LGFPCSSNQTEFKFDLTL 513
Cdd:PRK09751 153 -DALLHT----SAQRIGLSATVRSASDVAAFLG-GDRPVTVVNPPAMRHP-QIRIVVpvanmDDVSSVASGTGEDSHAGR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 514 NYKI-----ASVIQMYSDQKPTLVFCATRkGVQQAASVLVKD---AKFIMTVEQKQRLQKYAYSVRDSKLRDILKDG--A 583
Cdd:PRK09751 226 EGSIwpyieTGILDEVLRHRSTIVFTNSR-GLAEKLTARLNElyaARLQRSPSIAVDAAHFESTSGATSNRVQSSDVfiA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 584 AYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIK--STMHYAGGlfeeysetdiLQMIGRAGRpQFD 661
Cdd:PRK09751 305 RSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQvaTPLSVASG----------LQRIGRAGH-QVG 373
|
410
....*....|....*
gi 1804891964 662 TTATAVIMTRlSTRD 676
Cdd:PRK09751 374 GVSKGLFFPR-TRRD 387
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
579-658 |
1.77e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.16 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 579 LKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIKSTmhyagglfeEYSETDILQMIGRAGR 657
Cdd:smart00490 10 LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL---------PWSPASYIQRIGRAGR 80
|
.
gi 1804891964 658 P 658
Cdd:smart00490 81 A 81
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
298-438 |
3.58e-10 |
|
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: 59.72 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 298 NFVICAPTGSGKTVVFELAITRLLMEVPLpwlniKIVYMAPIKALCSQRFDDWKEKFGPiGLNCKELTGDTVM--DDLFE 375
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKGK-----KVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAeeREKNK 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804891964 376 IQHAHIIMTTPEK-WDSMTRKWRdnsLVQL-VRLFLIDEVHIVKDENRGPTLE---VVVSRMKTVQSV 438
Cdd:cd00046 77 LGDADIIIATPDMlLNLLLREDR---LFLKdLKLIIVDEAHALLIDSRGALILdlaVRKAGLKNAQVI 141
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
516-657 |
1.84e-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: 56.45 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 516 KIASVIQMYSDQKP--TLVFCATRKGVqqaasvlvkDAKFImtveqkqrLQKYAYSVrdsklrdilkdgaAYHHAGMELS 593
Cdd:pfam00271 2 KLEALLELLKKERGgkVLIFSQTKKTL---------EAELL--------LEKEGIKV-------------ARLHGDLSQE 51
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804891964 594 DRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIkstmhyagglFE-EYSETDILQMIGRAGR 657
Cdd:pfam00271 52 EREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN----------YDlPWNPASYIQRIGRAGR 107
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
274-414 |
5.52e-09 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 56.53 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 274 IFKEFPYfnyiQSKAFDDLL----YTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPwlniKIVYMAPIKALCSQRFDD 349
Cdd:pfam04851 1 KLELRPY----QIEAIENLLesikNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK----KVLFLVPRKDLLEQALEE 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1804891964 350 WKEKFGPIGLNCKELTGDTvmdDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVH 414
Cdd:pfam04851 73 FKKFLPNYVEIGEIISGDK---KDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
297-656 |
5.53e-07 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 54.51 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 297 RNFVICAPTGSGKTVVFELAI----TRLLMEVPLPwLNIKIVYMAPIKALCSqrfDDWKEKFGPIGLNCKELTGDTVmdD 372
Cdd:PRK13767 48 KNVLISSPTGSGKTLAAFLAIidelFRLGREGELE-DKVYCLYVSPLRALNN---DIHRNLEEPLTEIREIAKERGE--E 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 373 LFEIQHA-------------------HIIMTTPE---------KWdsmTRKWRDnslvqlVRLFLIDEVHIVKDENRGPT 424
Cdd:PRK13767 122 LPEIRVAirtgdtssyekqkmlkkppHILITTPEslaillnspKF---REKLRT------VKWVIVDEIHSLAENKRGVH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 425 LEVVVSRmktvqsvsqtLKNTSTAIPMRfVAVSATIPNAEDIAEWL---SDGERPAVCLKMDESH-RPVKLqKVVLGFPC 500
Cdd:PRK13767 193 LSLSLER----------LEELAGGEFVR-IGLSATIEPLEEVAKFLvgyEDDGEPRDCEIVDARFvKPFDI-KVISPVDD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 501 SSNQTEFKFDLTLNYKIASVIQmysDQKPTLVFCATRKGvqqAASVLVKdakfimtveQKQRLQKYAYSvrdsklrdilk 580
Cdd:PRK13767 261 LIHTPAEEISEALYETLHELIK---EHRTTLIFTNTRSG---AERVLYN---------LRKRFPEEYDE----------- 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804891964 581 DGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPaH--LVVIKSTmhyagglfeEYSETDILQMIGRAG 656
Cdd:PRK13767 315 DNIGAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG-YidLVVLLGS---------PKSVSRLLQRIGRAG 382
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
527-657 |
7.08e-07 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 53.61 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 527 QKPTLVFCATRKGVQQAAsvlvkdakfimtveqkQRLQKYAYSVrdsklrdilkdgAAYHhAGMELSDRKVVEGAFTVGD 606
Cdd:COG0514 230 GGSGIVYCLSRKKVEELA----------------EWLREAGIRA------------AAYH-AGLDAEEREANQDRFLRDE 280
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1804891964 607 LPVLFTTSTLAMGVNLP-----AHLVVIKSTmhyagglfEEYsetdiLQMIGRAGR 657
Cdd:COG0514 281 VDVIVATIAFGMGIDKPdvrfvIHYDLPKSI--------EAY-----YQEIGRAGR 323
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
527-657 |
1.05e-06 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 49.51 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 527 QKPTLVFCATRKGVQQAAsvlvkdakfimtveqkQRLQKyaysvrdsklrdiLKDGAAYHHAGMELSDRKVVEGAFTVGD 606
Cdd:cd18794 30 GGSGIIYCLSRKECEQVA----------------ARLQS-------------KGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1804891964 607 LPVLFTTSTLAMGVNLP-----AHLVVIKSTMHYagglfeeysetdiLQMIGRAGR 657
Cdd:cd18794 81 IQVIVATVAFGMGIDKPdvrfvIHYSLPKSMESY-------------YQESGRAGR 123
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
297-414 |
1.48e-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: 50.55 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 297 RNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNIKIVYMAPIKALCSQ---RFDDWKEKfgpiGLNCKELTGDTVMDDL 373
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQqleKFFKYFRK----GYKVTGLSGDSSHKVS 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1804891964 374 F--EIQHAHIIMTTPEKWDSMTRKWRDNSLVQL--VRLFLIDEVH 414
Cdd:cd18036 94 FgqIVKASDVIICTPQILINNLLSGREEERVYLsdFSLLIFDECH 138
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
284-470 |
1.49e-06 |
|
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: 50.52 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 284 IQSKAFDDLLyTDRNFVICAPTGSGKTVVFEL-AITRLLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCK 362
Cdd:cd00268 16 IQAQAIPLIL-SGRDVIGQAQTGSGKTLAFLLpILEKLLPEPKKKGRGPQALVLAPTRELAMQIAEVARKLGKGTGLKVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 363 ELTGDTVMDDLFEI--QHAHIIMTTPEK-WDSMTRKWRDnslVQLVRLFLIDEVhivkDE--NRG--PTLEVVVSRM-KT 434
Cdd:cd00268 95 AIYGGAPIKKQIEAlkKGPDIVVGTPGRlLDLIERGKLD---LSNVKYLVLDEA----DRmlDMGfeEDVEKILSALpKD 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1804891964 435 VQSvsqtlkntstaipmrfVAVSATIPNA-EDIAEWL 470
Cdd:cd00268 168 RQT----------------LLFSATLPEEvKELAKKF 188
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
296-414 |
2.12e-06 |
|
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: 50.12 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 296 DRNFVICAPTGSGKTVVfelAItrLLMEVPLPWLNI----KIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMD 371
Cdd:cd17927 17 GKNTIICLPTGSGKTFV---AV--LICEHHLKKFPAgrkgKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSEN 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1804891964 372 DLFE--IQHAHIIMTTPEKWDSMTRKWRDNSLvQLVRLFLIDEVH 414
Cdd:cd17927 92 VSVEqiVESSDVIIVTPQILVNDLKSGTIVSL-SDFSLLVFDECH 135
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
297-386 |
1.07e-05 |
|
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: 47.97 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 297 RNFVICAPTGSGKTVVFELAItrlLMEVPLPWLN--IKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTG---DTVMD 371
Cdd:cd17957 28 RDLLACAPTGSGKTLAFLIPI---LQKLGKPRKKkgLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKsleAKAKD 104
|
90
....*....|....*
gi 1804891964 372 DLFEIQHAHIIMTTP 386
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 ... |
295-387 |
5.54e-05 |
|
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: 45.97 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 295 TDRNFVICAPTGSGKTVVfELAITRLLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTvmDDLF 374
Cdd:cd18073 16 KGKNTIICAPTGCGKTFV-SLLICEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGAT--AENV 92
|
90
....*....|....*..
gi 1804891964 375 E----IQHAHIIMTTPE 387
Cdd:cd18073 93 PveqiIENNDIIILTPQ 109
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
303-386 |
1.95e-04 |
|
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: 44.23 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 303 APTGSGKTVVFELAITRLLMEVPLPWLnikIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTG--DTVMDDLFEIQHAH 380
Cdd:cd17954 44 AETGSGKTAAFALPILQALLENPQRFF---ALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGgmDMMAQAIALAKKPH 120
|
....*.
gi 1804891964 381 IIMTTP 386
Cdd:cd17954 121 VIVATP 126
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
259-386 |
2.15e-04 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 44.22 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 259 GSLKAVTEIPAKFRSIFKE-FPYFNYIQSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLmEVPLPWLNIKIVYMA 337
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKgYKVPTPIQRKTIPLIL-DGRDVVAMARTGSGKTAAFLIPMIEKL-KAHSPTVGARALILS 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1804891964 338 PIKALCSQRFDDWKE--KFgpIGLNCKELTGDTVMDDLFEIQHAH--IIMTTP 386
Cdd:cd17959 79 PTRELALQTLKVTKElgKF--TDLRTALLVGGDSLEEQFEALASNpdIIIATP 129
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
517-657 |
3.33e-04 |
|
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: 42.64 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 517 IASVIQMYSDQKPTLVFCATRKGVqqaasvlvkdakfimtveqkqrlQKYAYSVRDskLRDILKDG--AAYHHAGMELSD 594
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQA-----------------------ERLAQRLRE--LCPDRVPPdfIALHHGSLSREL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1804891964 595 RKVVEGAFTVGDLPVLFTTSTLAMGVNLPA-HLVV-IKSTmhyagglfeeYSETDILQMIGRAGR 657
Cdd:cd18796 83 REEVEAALKRGDLKVVVATSSLELGIDIGDvDLVIqIGSP----------KSVARLLQRLGRSGH 137
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
528-657 |
4.76e-04 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 44.70 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 528 KPTLVFCATRKGVQQAASvlvkdakfimtveqkqRLQKYAYSVrdsklrdilkdgAAYHhAGMELSDRKVVEGAFTVGDL 607
Cdd:PRK11057 237 KSGIIYCNSRAKVEDTAA----------------RLQSRGISA------------AAYH-AGLDNDVRADVQEAFQRDDL 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1804891964 608 PVLFTTSTLAMGVNLP-----AHLVVIKSTMHYagglfeeYSETdilqmiGRAGR 657
Cdd:PRK11057 288 QIVVATVAFGMGINKPnvrfvVHFDIPRNIESY-------YQET------GRAGR 329
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
296-387 |
6.02e-04 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 44.34 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 296 DRNFVICAPTGSGKTVVFELAITRLLMEVplpwlNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLFE 375
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAERLHKK-----GGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKRKE 91
|
90
....*....|...
gi 1804891964 376 I-QHAHIIMTTPE 387
Cdd:COG1111 92 LwEKARIIVATPQ 104
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
530-657 |
1.68e-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: 40.32 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 530 TLVFCATRKgvqqAASVLVKDAKfimtveqkQRLQKYAYSVrdSKLrdilkdgAAYHhAGMELSDRKVVEGAFTVGDLPV 609
Cdd:cd18797 38 TIVFCRSRK----LAELLLRYLK--------ARLVEEGPLA--SKV-------ASYR-AGYLAEDRREIEAELFNGELLG 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1804891964 610 LFTTSTLAMGVNLPAHLVVIKSTmhYAGGLFEeysetdILQMIGRAGR 657
Cdd:cd18797 96 VVATNALELGIDIGGLDAVVLAG--YPGSLAS------LWQQAGRAGR 135
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
285-414 |
1.73e-03 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 41.10 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 285 QSKAFDDLLytDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNIKI-VYMAPIKALCSQRFDDWKEKFgpiGLNCKE 363
Cdd:cd18034 7 QLELFEAAL--KRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNPKKRaVFLVPTVPLVAQQAEAIRSHT---DLKVGE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1804891964 364 LTGDTVMDD------LFEIQHAHIIMTTPEkwdsMTRKWRDNSLVQL--VRLFLIDEVH 414
Cdd:cd18034 82 YSGEMGVDKwtkerwKEELEKYDVLVMTAQ----ILLDALRHGFLSLsdINLLIFDECH 136
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
298-414 |
2.48e-03 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 40.38 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 298 NFVICAPTGSGKTVvfelaITRLLMEVPLPWL-NIKIVYMAPIKALCSQRFDDWKeKFGPIGLN-CKELTGDTVMDD-LF 374
Cdd:cd18033 18 NTLVALPTGLGKTF-----IAAVVMLNYYRWFpKGKIVFMAPTKPLVSQQIEACY-KITGIPSSqTAELTGSVPPTKrAE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1804891964 375 EIQHAHIIMTTPEKWDS-MTRKWRD-NSLVQLVrlflIDEVH 414
Cdd:cd18033 92 LWASKRVFFLTPQTLENdLKEGDCDpKSIVCLV----IDEAH 129
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
609-657 |
3.29e-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: 39.46 E-value: 3.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1804891964 609 VLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGR 657
Cdd:cd18805 73 VLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMRPLSPSEVKQIAGRAGR 121
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
300-472 |
9.79e-03 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 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: 350701 [Multi-domain] Cd Length: 192 Bit Score: 38.78 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 300 VICAPTGSGKTVVFE-LAITRLLMEVplpwLNIKIVYMAPIKALCSQRFDDWKE--KFGPiGLNCKELTGDT-VMDDLFE 375
Cdd:cd17943 31 IVQAKSGTGKTLVFVvIALESLDLER----RHPQVLILAPTREIAVQIHDVFKKigKKLE-GLKCEVFIGGTpVKEDKKK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891964 376 IQHAHIIMTTPEKWDSMTRKwrdNSL-VQLVRLFLIDEVHIVKDENRGPTLEVVVSRMktvQSVSQTLkntstaipmrfv 454
Cdd:cd17943 106 LKGCHIAVGTPGRIKQLIEL---GALnVSHVRLFVLDEADKLMEGSFQKDVNWIFSSL---PKNKQVI------------ 167
|
170 180
....*....|....*....|
gi 1804891964 455 AVSATIPN--AEDIAEWLSD 472
Cdd:cd17943 168 AFSATYPKnlDNLLARYMRK 187
|
|
| |
