|
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 ... |
238-446 |
3.61e-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: 3.61e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 238 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEV-PLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIG 316
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERnPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 317 LNCKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDN-SLVQLVRLFLIDEVHIVKdENRGPTLEVVVSRMKTVQS 395
Cdd:cd18023 81 LSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIK-ENRGATLEVVVSRMKTLSS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462505394 396 VSQTlkNTSTAIPMRFVAVSATIPNAEDIAEWLSDGerPAVCLKMDESHRP 446
Cdd:cd18023 160 SSEL--RGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFGESFRP 206
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
222-756 |
1.35e-103 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 340.33 E-value: 1.35e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 222 VTEIP-AKFRSIFKEFPY--FNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIK 298
Cdd:COG1204 3 VAELPlEKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN------GGKALYIVPLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 299 ALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRK---WRDNslvqlVRLFLIDEVHIVK 375
Cdd:COG1204 77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRNgpsWLRD-----VDLVVVDEAHLID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 376 DENRGPTLEVVVSRMKTVqsvsqtlkntstAIPMRFVAVSATIPNAEDIAEWLsdgERPAVclkmDESHRPVKLQKVVLg 455
Cdd:COG1204 151 DESRGPTLEVLLARLRRL------------NPEAQIVALSATIGNAEEIAEWL---DAELV----KSDWRPVPLNEGVL- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 456 fpcSSNQTEF--KFDLTLNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVR---- 529
Cdd:COG1204 211 ---YDGVLRFddGSRRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLevse 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 530 ----DSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTmHYAGGlfEEYSETD 605
Cdd:COG1204 288 ethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-KRGGM--VPIPVLE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 606 ILQMIGRAGRPQFDTTATAVIMTR-LSTRDKYIQMLACRDT--VESSLH--RHLIEHLNAEIVLHTITDVNIAVEWIRST 680
Cdd:COG1204 365 FKQMAGRAGRPGYDPYGEAILVAKsSDEADELFERYILGEPepIRSKLAneSALRTHLLALIASGFANSREELLDFLENT 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505394 681 LLYIRAlknpshygfasglNKDGIEAKLQElclkNLNDLSSLDLIKMDEGvNFKPTEAGRLMAWYYITFETVKKFY 756
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 ... |
735-1048 |
2.91e-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: 240.95 E-value: 2.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 735 PTEAGRLMAWYYITFETVKKFYT-ISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKdpnriTIRFPMEGRIKTR 813
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQsLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLE-----KVPIPVKGDIEDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 814 EMKVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWeNSLHVSKQLE 893
Cdd:pfam02889 76 HAKVNILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFE-ILLSKGWLSAALTALDLCKMIEQRMW-DSDSPLRQFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 894 KIGVTLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEqITRYSDTTAEILVTVIlRNFE 973
Cdd:pfam02889 154 GIPPELIKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAE-VQPITRSVLRVEVTIT-PDFP 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462505394 974 qlQTKRTASDSHYVTLIIGDADNQVVYLHKITdSVLLKAGSWAKKIAVKRALKSE---DLSINLISSEFVGLDIQQKL 1048
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 ... |
735-1050 |
1.09e-62 |
|
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: 216.84 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 735 PTEAGRLMAWYYITFETVKKFYT-ISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKDpnritIRFPMEGRIKTR 813
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQsLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-----VPIPVKEGIIDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 814 EM-KVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWENSLHVSKQL 892
Cdd:smart00973 76 PHaKVNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVD-IALSKGWLRTALNALDLSQMVVQRLWEDSDSPLKQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 893 EKIGV--TLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEQITRYSDTTaeILVTVILR 970
Cdd:smart00973 155 PHFLIedVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITRDLT--LRVELEIT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 971 NFEQLQTKRTASDSHYVTLIIGDADNQVVYLHKITDSVLLKAGSWAK-KIAVKR-ALKSEDLSINLISSEFVGLDIQQKL 1048
Cdd:smart00973 233 PVFAWDLPRHKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKlDFTVPLsEPGPENYTVYLISDSYLGCDQEVSF 312
|
..
gi 2462505394 1049 TV 1050
Cdd:smart00973 313 SL 314
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
445-629 |
3.08e-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: 3.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 445 RPVKLQKVVLGFPCSSNQTEFKFDLT--LNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVkdakfimtveqkqrlq 522
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 523 kyaysvrdsklrdilkdGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYS 602
Cdd:cd18795 65 -----------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELS 127
|
170 180
....*....|....*....|....*..
gi 2462505394 603 ETDILQMIGRAGRPQFDTTATAVIMTR 629
Cdd:cd18795 128 PLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
243-755 |
7.22e-51 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 193.11 E-value: 7.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 243 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAIT-RLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEkFGPIGLNCKE 321
Cdd:PRK00254 28 QAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVnKLLRE------GGKAVYLVPLKALAEEKYREFKD-WEKLGLRVAM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 322 LTGDTVMDDLFeIQHAHIIMTTPEKWDSMTRkwRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVQSVsqtlk 401
Cdd:PRK00254 101 TTGDYDSTDEW-LGKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQI----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 402 ntstaipmrfVAVSATIPNAEDIAEWLSdgerpAVCLKMDesHRPVKLQKVV--LGFPCSSNQTEFKFDLTLNykiASVI 479
Cdd:PRK00254 173 ----------LGLSATVGNAEELAEWLN-----AELVVSD--WRPVKLRKGVfyQGFLFWEDGKIERFPNSWE---SLVY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 480 QMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDS----KLRDILKDGAAYHHAGMELSDRKV 555
Cdd:PRK00254 233 DAVKKGKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKELADSLEENptneKLKKALRGGVAFHHAGLGRTERVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 556 VEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVIMTRL----S 631
Cdd:PRK00254 313 IEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTeepsK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 632 TRDKYI----QMLACRDTVESSLHRHLIehlnAEIVLHTITDVNIAVEWIRSTlLYIRALKNPSHygfasglnkdgIEAK 707
Cdd:PRK00254 393 LMERYIfgkpEKLFSMLSNESAFRSQVL----ALITNFGVSNFKELVNFLERT-FYAHQRKDLYS-----------LEEK 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2462505394 708 LQELC---LKNlndlsslDLIKMDEGVNFKPTEAGRLMAWYYITFETVKKF 755
Cdd:PRK00254 457 AKEIVyflLEN-------EFIDIDLEDRFIPLPLGIRTSQLYIDPLTAKKF 500
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
243-627 |
1.49e-50 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 192.48 E-value: 1.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 243 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEkFGPIGLNCKEL 322
Cdd:PRK02362 28 QAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIAR------GGKALYIVPLRALASEKFEEFER-FEELGVRVGIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 323 TGDTVMDDLFeIQHAHIIMTTPEKWDSMTRK---W-RDNSLVqlvrlfLIDEVHIVKDENRGPTLEVVVSRMKTVQSVSQ 398
Cdd:PRK02362 101 TGDYDSRDEW-LGDNDIIVATSEKVDSLLRNgapWlDDITCV------VVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 399 TlkntstaipmrfVAVSATIPNAEDIAEWLsDGERpavclkMDESHRPVKLQKVVL---GFPCSSNQTEFKF---DLTLN 472
Cdd:PRK02362 174 V------------VALSATIGNADELADWL-DAEL------VDSEWRPIDLREGVFyggAIHFDDSQREVEVpskDDTLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 473 YkiasVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDS-------KLRDILKDGAAYHH 545
Cdd:PRK02362 235 L----VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVsdtetskDLADCVAKGAAFHH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 546 AGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGL------FEEYSetdilQMIGRAGRPQFD 619
Cdd:PRK02362 311 AGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAgmqpipVLEYH-----QMAGRAGRPGLD 385
|
....*...
gi 2462505394 620 TTATAVIM 627
Cdd:PRK02362 386 PYGEAVLL 393
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
243-627 |
4.19e-49 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 188.22 E-value: 4.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 243 QSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEKFGP--IGLnck 320
Cdd:COG4581 30 QEEAILALE-AGRSVLVAAPTGSGKTLVAEFAIFLALAR------GRRSFYTAPIKALSNQKFFDLVERFGAenVGL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 321 eLTGDTVmddlfEIQHA-HIIMTTpEKWDSMTrkWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVsrmktvqsvsqt 399
Cdd:COG4581 100 -LTGDAS-----VNPDApIVVMTT-EILRNML--YREGADLEDVGVVVMDEFHYLADPDRGWVWEEPI------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 400 lkntsTAIP--MRFVAVSATIPNAEDIAEWLSD--GErpavCLKMDESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKI 475
Cdd:COG4581 159 -----IHLParVQLVLLSATVGNAEEFAEWLTRvrGE----TAVVVSEERPVPLEFHYLVTPRLFPLFRVNPELLRPPSR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 476 ASVIQM--YSDQKPTLVFCATRKGVQQAASVLVkdAKFIMTVEQKQRLQKYA-------YSVRDSKLRDILKDGAAYHHA 546
Cdd:COG4581 230 HEVIEEldRGGLLPAIVFIFSRRGCDEAAQQLL--SARLTTKEERAEIREAIdefaedfSVLFGKTLSRLLRRGIAVHHA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 547 GMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVI 626
Cdd:COG4581 308 GMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDTEGHVVV 387
|
.
gi 2462505394 627 M 627
Cdd:COG4581 388 L 388
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
242-424 |
1.58e-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: 130.05 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 242 IQSKAFDdLLYTDRNFVICAPTGSGKTVVFELAItrlLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLN-CK 320
Cdd:pfam00270 3 IQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPA---LEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKvAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 321 ELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRdnsLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTvqsvsqtl 400
Cdd:pfam00270 79 LLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-------- 147
|
170 180
....*....|....*....|....*
gi 2462505394 401 kntstaiPMRFVAVSATIP-NAEDI 424
Cdd:pfam00270 148 -------KRQILLLSATLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
234-428 |
1.28e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.04 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 234 KEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQRFDDWKEKFG 313
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK----GGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 314 PIGLN-CKELTGDTVMDDLFEIQH--AHIIMTTPEKWDSMTRKwrDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRM 390
Cdd:smart00487 80 SLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462505394 391 KTVQsvsqtlkntstaipmRFVAVSATIPNAEDIAEWL 428
Cdd:smart00487 158 PKNV---------------QLLLLSATPPEEIENLLEL 180
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
537-616 |
1.72e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.16 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 537 LKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIKSTmhyagglfeEYSETDILQMIGRAGR 615
Cdd:smart00490 10 LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL---------PWSPASYIQRIGRAGR 80
|
.
gi 2462505394 616 P 616
Cdd:smart00490 81 A 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
474-615 |
2.09e-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: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 474 KIASVIQMYSDQKP--TLVFCATRKGVqqaasvlvkDAKFImtveqkqrLQKYAYSVrdsklrdilkdgaAYHHAGMELS 551
Cdd:pfam00271 2 KLEALLELLKKERGgkVLIFSQTKKTL---------EAELL--------LEKEGIKV-------------ARLHGDLSQE 51
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505394 552 DRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIkstmhyagglFE-EYSETDILQMIGRAGR 615
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 ... |
238-446 |
3.61e-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: 3.61e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 238 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEV-PLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIG 316
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERnPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 317 LNCKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDN-SLVQLVRLFLIDEVHIVKdENRGPTLEVVVSRMKTVQS 395
Cdd:cd18023 81 LSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIK-ENRGATLEVVVSRMKTLSS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462505394 396 VSQTlkNTSTAIPMRFVAVSATIPNAEDIAEWLSDGerPAVCLKMDESHRP 446
Cdd:cd18023 160 SSEL--RGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFGESFRP 206
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
222-756 |
1.35e-103 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 340.33 E-value: 1.35e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 222 VTEIP-AKFRSIFKEFPY--FNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIK 298
Cdd:COG1204 3 VAELPlEKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN------GGKALYIVPLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 299 ALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRK---WRDNslvqlVRLFLIDEVHIVK 375
Cdd:COG1204 77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRNgpsWLRD-----VDLVVVDEAHLID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 376 DENRGPTLEVVVSRMKTVqsvsqtlkntstAIPMRFVAVSATIPNAEDIAEWLsdgERPAVclkmDESHRPVKLQKVVLg 455
Cdd:COG1204 151 DESRGPTLEVLLARLRRL------------NPEAQIVALSATIGNAEEIAEWL---DAELV----KSDWRPVPLNEGVL- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 456 fpcSSNQTEF--KFDLTLNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVR---- 529
Cdd:COG1204 211 ---YDGVLRFddGSRRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLevse 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 530 ----DSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTmHYAGGlfEEYSETD 605
Cdd:COG1204 288 ethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-KRGGM--VPIPVLE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 606 ILQMIGRAGRPQFDTTATAVIMTR-LSTRDKYIQMLACRDT--VESSLH--RHLIEHLNAEIVLHTITDVNIAVEWIRST 680
Cdd:COG1204 365 FKQMAGRAGRPGYDPYGEAILVAKsSDEADELFERYILGEPepIRSKLAneSALRTHLLALIASGFANSREELLDFLENT 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505394 681 LLYIRAlknpshygfasglNKDGIEAKLQElclkNLNDLSSLDLIKMDEGvNFKPTEAGRLMAWYYITFETVKKFY 756
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 ... |
735-1048 |
2.91e-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: 240.95 E-value: 2.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 735 PTEAGRLMAWYYITFETVKKFYT-ISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKdpnriTIRFPMEGRIKTR 813
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQsLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLE-----KVPIPVKGDIEDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 814 EMKVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWeNSLHVSKQLE 893
Cdd:pfam02889 76 HAKVNILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFE-ILLSKGWLSAALTALDLCKMIEQRMW-DSDSPLRQFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 894 KIGVTLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEqITRYSDTTAEILVTVIlRNFE 973
Cdd:pfam02889 154 GIPPELIKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAE-VQPITRSVLRVEVTIT-PDFP 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462505394 974 qlQTKRTASDSHYVTLIIGDADNQVVYLHKITdSVLLKAGSWAKKIAVKRALKSE---DLSINLISSEFVGLDIQQKL 1048
Cdd:pfam02889 232 --WDKRVHGKSEGFWLVVGDSDGNEILHIERF-TLTKRTLAGEHKLEFTVPPSDPgppQLFVRLISDSWLGADQEVPI 306
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
238-432 |
5.20e-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: 5.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 238 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVplpwlNIKIVYMAPIKALCSQRFDDWKEKFGPIGL 317
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-----GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 318 NCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRKWRDNsLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVQsvs 397
Cdd:cd17921 76 NVGLLTGDPSVNKL-LLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRIN--- 150
|
170 180 190
....*....|....*....|....*....|....*
gi 2462505394 398 qtlkntstaIPMRFVAVSATIPNAEDIAEWLSDGE 432
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 ... |
735-1050 |
1.09e-62 |
|
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: 216.84 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 735 PTEAGRLMAWYYITFETVKKFYT-ISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKDpnritIRFPMEGRIKTR 813
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQsLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-----VPIPVKEGIIDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 814 EM-KVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWENSLHVSKQL 892
Cdd:smart00973 76 PHaKVNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVD-IALSKGWLRTALNALDLSQMVVQRLWEDSDSPLKQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 893 EKIGV--TLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEQITRYSDTTaeILVTVILR 970
Cdd:smart00973 155 PHFLIedVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITRDLT--LRVELEIT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 971 NFEQLQTKRTASDSHYVTLIIGDADNQVVYLHKITDSVLLKAGSWAK-KIAVKR-ALKSEDLSINLISSEFVGLDIQQKL 1048
Cdd:smart00973 233 PVFAWDLPRHKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKlDFTVPLsEPGPENYTVYLISDSYLGCDQEVSF 312
|
..
gi 2462505394 1049 TV 1050
Cdd:smart00973 313 SL 314
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
445-629 |
3.08e-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: 3.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 445 RPVKLQKVVLGFPCSSNQTEFKFDLT--LNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVkdakfimtveqkqrlq 522
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 523 kyaysvrdsklrdilkdGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYS 602
Cdd:cd18795 65 -----------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELS 127
|
170 180
....*....|....*....|....*..
gi 2462505394 603 ETDILQMIGRAGRPQFDTTATAVIMTR 629
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 ... |
236-428 |
9.35e-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: 200.56 E-value: 9.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 236 FPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQRFDDWKEKFGP- 314
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNP----KGRAVYIAPMQELVDARYKDWRAKFGPl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 315 IGLNCKELTGDTVMdDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDENrGPTLEVVVSRMKTVQ 394
Cdd:cd18021 77 LGKKVVKLTGETST-DLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGEN-GPVYEVVVSRMRYIS 154
|
170 180 190
....*....|....*....|....*....|....
gi 2462505394 395 svSQTLKntstaiPMRFVAVSATIPNAEDIAEWL 428
Cdd:cd18021 155 --SQLEK------PIRIVGLSSSLANARDVGEWL 180
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
238-428 |
2.28e-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: 2.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 238 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQRFDDWKEKF-GPIG 316
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYP----GSKVVYIAPLKALVRERVDDWKKRFeEKLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 317 LNCKELTGDtVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDEnRGPTLEVVVSRMKTVQSV 396
Cdd:cd18022 77 KKVVELTGD-VTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSD-RGPVLEVIVSRMNYISSQ 154
|
170 180 190
....*....|....*....|....*....|..
gi 2462505394 397 sqtlkntsTAIPMRFVAVSATIPNAEDIAEWL 428
Cdd:cd18022 155 --------TEKPVRLVGLSTALANAGDLANWL 178
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
243-755 |
7.22e-51 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 193.11 E-value: 7.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 243 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAIT-RLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEkFGPIGLNCKE 321
Cdd:PRK00254 28 QAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVnKLLRE------GGKAVYLVPLKALAEEKYREFKD-WEKLGLRVAM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 322 LTGDTVMDDLFeIQHAHIIMTTPEKWDSMTRkwRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVQSVsqtlk 401
Cdd:PRK00254 101 TTGDYDSTDEW-LGKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQI----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 402 ntstaipmrfVAVSATIPNAEDIAEWLSdgerpAVCLKMDesHRPVKLQKVV--LGFPCSSNQTEFKFDLTLNykiASVI 479
Cdd:PRK00254 173 ----------LGLSATVGNAEELAEWLN-----AELVVSD--WRPVKLRKGVfyQGFLFWEDGKIERFPNSWE---SLVY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 480 QMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDS----KLRDILKDGAAYHHAGMELSDRKV 555
Cdd:PRK00254 233 DAVKKGKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKELADSLEENptneKLKKALRGGVAFHHAGLGRTERVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 556 VEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVIMTRL----S 631
Cdd:PRK00254 313 IEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTeepsK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 632 TRDKYI----QMLACRDTVESSLHRHLIehlnAEIVLHTITDVNIAVEWIRSTlLYIRALKNPSHygfasglnkdgIEAK 707
Cdd:PRK00254 393 LMERYIfgkpEKLFSMLSNESAFRSQVL----ALITNFGVSNFKELVNFLERT-FYAHQRKDLYS-----------LEEK 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2462505394 708 LQELC---LKNlndlsslDLIKMDEGVNFKPTEAGRLMAWYYITFETVKKF 755
Cdd:PRK00254 457 AKEIVyflLEN-------EFIDIDLEDRFIPLPLGIRTSQLYIDPLTAKKF 500
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
243-627 |
1.49e-50 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 192.48 E-value: 1.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 243 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEkFGPIGLNCKEL 322
Cdd:PRK02362 28 QAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIAR------GGKALYIVPLRALASEKFEEFER-FEELGVRVGIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 323 TGDTVMDDLFeIQHAHIIMTTPEKWDSMTRK---W-RDNSLVqlvrlfLIDEVHIVKDENRGPTLEVVVSRMKTVQSVSQ 398
Cdd:PRK02362 101 TGDYDSRDEW-LGDNDIIVATSEKVDSLLRNgapWlDDITCV------VVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 399 TlkntstaipmrfVAVSATIPNAEDIAEWLsDGERpavclkMDESHRPVKLQKVVL---GFPCSSNQTEFKF---DLTLN 472
Cdd:PRK02362 174 V------------VALSATIGNADELADWL-DAEL------VDSEWRPIDLREGVFyggAIHFDDSQREVEVpskDDTLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 473 YkiasVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDS-------KLRDILKDGAAYHH 545
Cdd:PRK02362 235 L----VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVsdtetskDLADCVAKGAAFHH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 546 AGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGL------FEEYSetdilQMIGRAGRPQFD 619
Cdd:PRK02362 311 AGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAgmqpipVLEYH-----QMAGRAGRPGLD 385
|
....*...
gi 2462505394 620 TTATAVIM 627
Cdd:PRK02362 386 PYGEAVLL 393
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
243-627 |
4.19e-49 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 188.22 E-value: 4.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 243 QSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEKFGP--IGLnck 320
Cdd:COG4581 30 QEEAILALE-AGRSVLVAAPTGSGKTLVAEFAIFLALAR------GRRSFYTAPIKALSNQKFFDLVERFGAenVGL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 321 eLTGDTVmddlfEIQHA-HIIMTTpEKWDSMTrkWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVsrmktvqsvsqt 399
Cdd:COG4581 100 -LTGDAS-----VNPDApIVVMTT-EILRNML--YREGADLEDVGVVVMDEFHYLADPDRGWVWEEPI------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 400 lkntsTAIP--MRFVAVSATIPNAEDIAEWLSD--GErpavCLKMDESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKI 475
Cdd:COG4581 159 -----IHLParVQLVLLSATVGNAEEFAEWLTRvrGE----TAVVVSEERPVPLEFHYLVTPRLFPLFRVNPELLRPPSR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 476 ASVIQM--YSDQKPTLVFCATRKGVQQAASVLVkdAKFIMTVEQKQRLQKYA-------YSVRDSKLRDILKDGAAYHHA 546
Cdd:COG4581 230 HEVIEEldRGGLLPAIVFIFSRRGCDEAAQQLL--SARLTTKEERAEIREAIdefaedfSVLFGKTLSRLLRRGIAVHHA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 547 GMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVI 626
Cdd:COG4581 308 GMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDTEGHVVV 387
|
.
gi 2462505394 627 M 627
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 ... |
222-428 |
1.21e-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: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 222 VTEIPAKFRSIFKEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNI-----KIVYMAP 296
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGTInldafKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 297 IKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKD 376
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKE-QISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462505394 377 EnRGPTLEVVVSRmkTVQSVSQTLKntstaiPMRFVAVSATIPNAEDIAEWL 428
Cdd:cd18019 160 D-RGPVLESIVAR--TIRQIEQTQE------YVRLVGLSATLPNYEDVATFL 202
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
255-756 |
1.51e-42 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 166.98 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 255 RNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKeKFGPIGLNCKELTGDtvMDDLFE- 333
Cdd:PRK01172 38 ENVIVSVPTAAGKTLIAYSAIYETFLA------GLKSIYIVPLRSLAMEKYEELS-RLRSLGMRVKISIGD--YDDPPDf 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 334 IQHAHIIMTTPEKWDSMTRkwRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVqsvsqtlkNTSTaipmRFVA 413
Cdd:PRK01172 109 IKRYDVVILTSEKADSLIH--HDPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSARYV--------NPDA----RILA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 414 VSATIPNAEDIAEWLSdgerpAVCLKmdESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKIASVIQmysDQKPTLVFCA 493
Cdd:PRK01172 175 LSATVSNANELAQWLN-----ASLIK--SNFRPVPLKLGILYRKRLILDGYERSQVDINSLIKETVN---DGGQVLVFVS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 494 TRKGVQQAASVLVK----DAKFIMTVEQKqrlqkyaySVRDSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLF 569
Cdd:PRK01172 245 SRKNAEDYAEMLIQhfpeFNDFKVSSENN--------NVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 570 TTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVI-MTRLSTRDKYIQMLACR-DTVE 647
Cdd:PRK01172 317 ATPTLAAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYIyAASPASYDAAKKYLSGEpEPVI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 648 SSLHRHLIEHLN--AEIVLHTITDVNIAVEWIRSTLLYIRAlknpshygfasglNKDGIEAKLQElclknlndlsSLDLI 725
Cdd:PRK01172 397 SYMGSQRKVRFNtlAAISMGLASSMEDLILFYNETLMAIQN-------------GVDEIDYYIES----------SLKFL 453
|
490 500 510
....*....|....*....|....*....|....*...
gi 2462505394 726 K----MDEGVNFKPTEAGRLMAWYYITFET---VKKFY 756
Cdd:PRK01172 454 KengfIKGDVTLRATRLGKLTSDLYIDPESaliLKSAF 491
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
240-428 |
2.64e-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: 2.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 240 NYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLME--VPLPWL---NIKIVYMAPIKALCSQRFDDWKEKFGP 314
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQhvNQGGVIkkdDFKIVYIAPMKALAAEMVEKFSKRLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 315 IGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRKWR-DNSLVQLVRLFLIDEVHIVKDEnRGPTLEVVVSR-MKT 392
Cdd:cd18020 83 LGIKVKELTGDMQLTKK-EIAETQIIVTTPEKWDVVTRKSSgDVALSQLVRLLIIDEVHLLHDD-RGPVIESLVARtLRQ 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462505394 393 VQSvSQTLkntstaipMRFVAVSATIPNAEDIAEWL 428
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 ... |
238-428 |
2.52e-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: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 238 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKeKFGPIGL 317
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLE------GGKALYLVPLRALASEKYEEFK-KLEEIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 318 NCKELTGDTVMDDLFeIQHAHIIMTTPEKWDSMTR-KWrdnSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVqsv 396
Cdd:cd18028 74 KVGISTGDYDEDDEW-LGDYDIIVATYEKFDSLLRhSP---SWLRDVGVVVVDEIHLISDEERGPTLESIVARLRRL--- 146
|
170 180 190
....*....|....*....|....*....|..
gi 2462505394 397 sqtlkNTSTaipmRFVAVSATIPNAEDIAEWL 428
Cdd:cd18028 147 -----NPNT----QIIGLSATIGNPDELAEWL 169
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
242-424 |
1.58e-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: 130.05 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 242 IQSKAFDdLLYTDRNFVICAPTGSGKTVVFELAItrlLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLN-CK 320
Cdd:pfam00270 3 IQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPA---LEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKvAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 321 ELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRdnsLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTvqsvsqtl 400
Cdd:pfam00270 79 LLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-------- 147
|
170 180
....*....|....*....|....*
gi 2462505394 401 kntstaiPMRFVAVSATIP-NAEDI 424
Cdd:pfam00270 148 -------KRQILLLSATLPrNLEDL 165
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
225-618 |
2.10e-26 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 117.30 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 225 IPAKFRSIFK-EFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELA-ITRLLMEvplpwlNIKIVYMAPIKALCS 302
Cdd:COG1202 195 LPPELKDLLEgRGEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAgIKNALEG------KGKMLFLVPLVALAN 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 303 QRFDDWKEKFGPiGLNCKELTG---------DTVMDdlfeiqhAHIIMTTPEKWDSMTRKWRDNSLVQLVrlfLIDEVHI 373
Cdd:COG1202 269 QKYEDFKDRYGD-GLDVSIRVGasrirddgtRFDPN-------ADIIVGTYEGIDHALRTGRDLGDIGTV---VIDEVHM 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 374 VKDENRGPTLEVVVSRMKTVQSVSQtlkntstaipmrFVAVSATIPNAEDIAEWLSdgerpavcLKMDE-SHRPVKLQKV 452
Cdd:COG1202 338 LEDPERGHRLDGLIARLKYYCPGAQ------------WIYLSATVGNPEELAKKLG--------AKLVEyEERPVPLERH 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 453 VLgFpcssNQTEFKFDLtlnykIASVIQMYSDQKP-------TLVFCATRKgvqqaasvlvkdakfimtveqkqrlqkya 525
Cdd:COG1202 398 LT-F----ADGREKIRI-----INKLVKREFDTKSskgyrgqTIIFTNSRR----------------------------- 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 526 ysvRDSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKS-TMhyaGGlfEEYSET 604
Cdd:COG1202 439 ---RCHEIARALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSlAM---GI--EWLSVQ 510
|
410
....*....|....
gi 2462505394 605 DILQMIGRAGRPQF 618
Cdd:COG1202 511 EFHQMLGRAGRPDY 524
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
234-428 |
1.28e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.04 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 234 KEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQRFDDWKEKFG 313
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK----GGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 314 PIGLN-CKELTGDTVMDDLFEIQH--AHIIMTTPEKWDSMTRKwrDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRM 390
Cdd:smart00487 80 SLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462505394 391 KTVQsvsqtlkntstaipmRFVAVSATIPNAEDIAEWL 428
Cdd:smart00487 158 PKNV---------------QLLLLSATPPEEIENLLEL 180
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
243-615 |
7.14e-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: 7.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 243 QSKAFDdLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCS---QRFDDWKEKFGPiGLNC 319
Cdd:COG1205 61 QAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEALLEDP----GATALYLYPTKALARdqlRRLRELAEALGL-GVRV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 320 KELTGDTVMDDLFEI-QHAHIIMTTPEKWD-SM---TRKWRdnSLVQLVRLFLIDEVHIVkdenRGptleV-------VV 387
Cdd:COG1205 135 ATYDGDTPPEERRWIrEHPDIVLTNPDMLHyGLlphHTRWA--RFFRNLRYVVIDEAHTY----RG----VfgshvanVL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 388 SRMKTVqsvsqtLKNTSTAipMRFVAVSATIPNAEDIAEWLSDgeRPAVCLkmDESHRPVKLQKVVLGFPCSSNQTEFKF 467
Cdd:COG1205 205 RRLRRI------CRHYGSD--PQFILASATIGNPAEHAERLTG--RPVTVV--DEDGSPRGERTFVLWNPPLVDDGIRRS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 468 DLTLNYKIASVIqMYSDQKpTLVFCATRKGVQQAASVLvkdakfimtveqKQRLQKYAYSVRdsklrdIlkdgAAYhHAG 547
Cdd:COG1205 273 ALAEAARLLADL-VREGLR-TLVFTRSRRGAELLARYA------------RRALREPDLADR------V----AAY-RAG 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462505394 548 MELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPA-HLVVIkstMHYAGglfeeySETDILQMIGRAGR 615
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 ... |
234-429 |
1.11e-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: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 234 KEFPY-FNYIQSKAFDDLlytDRN--FVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKE 310
Cdd:cd18024 27 RTYPFtLDPFQKTAIACI---ERNesVLVSAHTSAGKTVVAEYAIAQSLRD------KQRVIYTSPIKALSNQKYRELQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 311 KFGPIGLnckeLTGDTVMDDLFEIqhahIIMTTpEKWDSMTrkWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEvvvsrm 390
Cdd:cd18024 98 EFGDVGL----MTGDVTINPNASC----LVMTT-EILRSML--YRGSEIMREVAWVIFDEIHYMRDKERGVVWE------ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462505394 391 KTVQSVSQTlkntstaipMRFVAVSATIPNAEDIAEWLS 429
Cdd:cd18024 161 ETIILLPDK---------VRYVFLSATIPNARQFAEWIC 190
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
243-428 |
9.48e-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: 9.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 243 QSKAFDDLLYTDRNFViCAPTGSGKTVVFELAITRLLMEVplpwlnIKIVYMAPIKALCSQRFDDWKEKFGPIGLnckeL 322
Cdd:cd18027 13 QKQAILHLEAGDSVFV-AAHTSAGKTVVAEYAIALAQKHM------TRTIYTSPIKALSNQKFRDFKNTFGDVGL----I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 323 TGDTVMDDlfeiQHAHIIMTTpEKWDSMTrkWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKtvQSVSqtlkn 402
Cdd:cd18027 82 TGDVQLNP----EASCLIMTT-EILRSML--YNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLP--DHVS----- 147
|
170 180
....*....|....*....|....*.
gi 2462505394 403 tstaipmrFVAVSATIPNAEDIAEWL 428
Cdd:cd18027 148 --------IILLSATVPNTVEFADWI 165
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
733-1003 |
1.61e-17 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 85.00 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 733 FKPTEAGRLMAWYYITFETVKKFY-TISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKdpnRITIRFPMEGrIK 811
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNeLLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAE---KLPIRLENPS-LD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 812 TREMKVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWEnSLHVSKQ 891
Cdd:smart00611 78 DPHVKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVD-IALERGWLSTALNALNLSQMIIQALWP-TDSPLLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 892 LEKIGVTLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYEL--KVEQITRysdTTAEILVTV-- 967
Cdd:smart00611 156 LPHLPEEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIeiSLEPITR---TVLGVEVTLtv 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462505394 968 -ILRNFEQLQTkrtasdSHYVTLIIGDADNQVVYLHK 1003
Cdd:smart00611 233 dLTWDDEIHGK------QEGWWLVIGDSDGNELLHIE 263
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
243-616 |
1.98e-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: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 243 QSKAFDDLLYT----DRNFVICAPTGSGKTVVFELAITRLLmevplpwLNIKIVYMAPIKALCSQrfddWKEKFgpigln 318
Cdd:COG1061 85 QQEALEALLAAlergGGRGLVVAPTGTGKTVLALALAAELL-------RGKRVLVLVPRRELLEQ----WAEEL------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 319 cKELTGDTVMDDLFEIQHAHIIMTTpekWDSMTRKWRDNSLVQLVRLFLIDEVHIVkdenRGPTLEVVVSRMKtvqsvsq 398
Cdd:COG1061 148 -RRFLGDPLAGGGKKDSDAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHA----GAPSYRRILEAFP------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 399 tlkntstaiPMRFVAVSATiPNAED---IAEWLSDGERPAVCLK--MDESH-RPVKLQKVVLGFpcSSNQTEF-KFDLTL 471
Cdd:COG1061 213 ---------AAYRLGLTAT-PFRSDgreILLFLFDGIVYEYSLKeaIEDGYlAPPEYYGIRVDL--TDERAEYdALSERL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 472 NYKIAS-----------VIQMYSDQKPTLVFCATrkgvqqaasvlVKDAKFIMtveqkQRLQKYAYSvrdsklrdilkdg 540
Cdd:COG1061 281 REALAAdaerkdkilreLLREHPDDRKTLVFCSS-----------VDHAEALA-----ELLNEAGIR------------- 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462505394 541 AAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPA--HLVVIKSTMhyagglfeeySETDILQMIGRAGRP 616
Cdd:COG1061 332 AAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPTG----------SPREFIQRLGRGLRP 399
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
254-428 |
1.20e-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: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 254 DRNFVICAPTGSGKTVVFELAITRLLMEVPLPwlNIKIVYMAPIKALCSQRFDDWKEKfgpigLNCKEL-------TGDT 326
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEK--GVQVLYISPLKALINDQERRLEEP-----LDEIDLeipvavrHGDT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 327 -------VMDDLfeiqhAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVqsvsqt 399
Cdd:cd17922 74 sqsekakQLKNP-----PGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKL------ 142
|
170 180
....*....|....*....|....*....
gi 2462505394 400 lkntsTAIPMRFVAVSATIPNAEDIAEWL 428
Cdd:cd17922 143 -----TGRPLRRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
247-428 |
1.10e-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: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 247 FDDLLYTDRNFVICAPTGSGKTVVFELAITRLLmevplpWLNIKIV-YMAPIKALCSQRFDDWKEKFGPIGLNCKELTGD 325
Cdd:cd18026 26 SLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRL------LERRKKAlFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 326 --TVMDDLFEiqHAHIIMTTPEKWDSMTrkwrdNSLVQLVRLFLI-----DEVHIVKDENRGPTLEVVVSRMktvqsvsq 398
Cdd:cd18026 100 kgRSPPKRRK--SLSVAVCTIEKANSLV-----NSLIEEGRLDELglvvvDELHMLGDGHRGALLELLLTKL-------- 164
|
170 180 190
....*....|....*....|....*....|
gi 2462505394 399 TLKNTSTaipMRFVAVSATIPNAEDIAEWL 428
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 ... |
249-433 |
2.92e-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: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 249 DLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQ-------RFDdwkEKFGPIGLN-CK 320
Cdd:cd18025 11 DIVDRRESALIVAPTSSGKTFISYYCMEKVLRESD----DGVVVYVAPTKALVNQvvaevyaRFS---KKYPPSGKSlWG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 321 ELTGDTVMDDlfeIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEvvvsrmktvqsvsQTL 400
Cdd:cd18025 84 VFTRDYRHNN---PMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWE-------------QLL 147
|
170 180 190
....*....|....*....|....*....|...
gi 2462505394 401 kntsTAIPMRFVAVSATIPNAEDIAEWLSDGER 433
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 ... |
243-426 |
3.49e-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: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 243 QSKAFDdLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALC-SQ--RFDDWKEKFGPiGLNC 319
Cdd:cd17923 5 QAEAIE-AARAGRSVVVTTGTASGKSLCYQLPILEALLRDP----GSRALYLYPTKALAqDQlrSLRELLEQLGL-GIRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 320 KELTGDTVMDDLFEI--QHAHIIMTTPEKWD-SMTR---KWRdnSLVQLVRLFLIDEVHIVkdenRGP---TLEVVVSRM 390
Cdd:cd17923 79 ATYDGDTPREERRAIirNPPRILLTNPDMLHyALLPhhdRWA--RFLRNLRYVVLDEAHTY----RGVfgsHVALLLRRL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462505394 391 KtvqsvsQTLKNTSTAIpmRFVAVSATIPNAEDIAE 426
Cdd:cd17923 153 R------RLCRRYGADP--QFILTSATIGNPAEHAR 180
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
259-634 |
4.20e-13 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 74.58 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 259 ICAPTGSGKTVV-FELAITRLLME------VPLPWLNIKIVYMAPIKALCS--QR--------FDDWKEKFGPIGLNCKE 321
Cdd:PRK09751 1 VIAPTGSGKTLAaFLYALDRLFREggedtrEAHKRKTSRILYISPIKALGTdvQRnlqiplkgIADERRRRGETEVNLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 322 --LTGDTVMDDLFEI--QHAHIIMTTPEKWDSM-TRKWRDNslVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMktvqsv 396
Cdd:PRK09751 81 giRTGDTPAQERSKLtrNPPDILITTPESLYLMlTSRARET--LRGVETVIIDEVHAVAGSKRGAHLALSLERL------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 397 sQTLKNTstaiPMRFVAVSATIPNAEDIAEWLSdGERPAVCLKMDESHRPvKLQKVV-----LGFPCSSNQTEFKFDLTL 471
Cdd:PRK09751 153 -DALLHT----SAQRIGLSATVRSASDVAAFLG-GDRPVTVVNPPAMRHP-QIRIVVpvanmDDVSSVASGTGEDSHAGR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 472 NYKI-----ASVIQMYSDQKPTLVFCATRkGVQQAASVLVKD---AKFIMTVEQKQRLQKYAYSVRDSKLRDILKDG--A 541
Cdd:PRK09751 226 EGSIwpyieTGILDEVLRHRSTIVFTNSR-GLAEKLTARLNElyaARLQRSPSIAVDAAHFESTSGATSNRVQSSDVfiA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 542 AYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIK--STMHYAGGlfeeysetdiLQMIGRAGRpQFD 619
Cdd:PRK09751 305 RSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQvaTPLSVASG----------LQRIGRAGH-QVG 373
|
410
....*....|....*
gi 2462505394 620 TTATAVIMTRlSTRD 634
Cdd:PRK09751 374 GVSKGLFFPR-TRRD 387
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
537-616 |
1.72e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.16 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 537 LKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIKSTmhyagglfeEYSETDILQMIGRAGR 615
Cdd:smart00490 10 LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL---------PWSPASYIQRIGRAGR 80
|
.
gi 2462505394 616 P 616
Cdd:smart00490 81 A 81
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
256-396 |
3.47e-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: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 256 NFVICAPTGSGKTVVFELAITRLLMEVPLpwlniKIVYMAPIKALCSQRFDDWKEKFGPiGLNCKELTGDTVM--DDLFE 333
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKGK-----KVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAeeREKNK 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462505394 334 IQHAHIIMTTPEK-WDSMTRKWRdnsLVQL-VRLFLIDEVHIVKDENRGPTLE---VVVSRMKTVQSV 396
Cdd:cd00046 77 LGDADIIIATPDMlLNLLLREDR---LFLKdLKLIIVDEAHALLIDSRGALILdlaVRKAGLKNAQVI 141
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
474-615 |
2.09e-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: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 474 KIASVIQMYSDQKP--TLVFCATRKGVqqaasvlvkDAKFImtveqkqrLQKYAYSVrdsklrdilkdgaAYHHAGMELS 551
Cdd:pfam00271 2 KLEALLELLKKERGgkVLIFSQTKKTL---------EAELL--------LEKEGIKV-------------ARLHGDLSQE 51
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505394 552 DRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIkstmhyagglFE-EYSETDILQMIGRAGR 615
Cdd:pfam00271 52 EREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN----------YDlPWNPASYIQRIGRAGR 107
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
232-372 |
5.25e-09 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 56.91 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 232 IFKEFPYfnyiQSKAFDDLL----YTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPwlniKIVYMAPIKALCSQRFDD 307
Cdd:pfam04851 1 KLELRPY----QIEAIENLLesikNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK----KVLFLVPRKDLLEQALEE 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462505394 308 WKEKFGPIGLNCKELTGDTvmdDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVH 372
Cdd:pfam04851 73 FKKFLPNYVEIGEIISGDK---KDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
255-614 |
4.25e-07 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 54.51 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 255 RNFVICAPTGSGKTVVFELAI----TRLLMEVPLPwLNIKIVYMAPIKALCSqrfDDWKEKFGPIGLNCKELTGDTVmdD 330
Cdd:PRK13767 48 KNVLISSPTGSGKTLAAFLAIidelFRLGREGELE-DKVYCLYVSPLRALNN---DIHRNLEEPLTEIREIAKERGE--E 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 331 LFEIQHA-------------------HIIMTTPE---------KWdsmTRKWRDnslvqlVRLFLIDEVHIVKDENRGPT 382
Cdd:PRK13767 122 LPEIRVAirtgdtssyekqkmlkkppHILITTPEslaillnspKF---REKLRT------VKWVIVDEIHSLAENKRGVH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 383 LEVVVSRmktvqsvsqtLKNTSTAIPMRfVAVSATIPNAEDIAEWL---SDGERPAVCLKMDESH-RPVKLqKVVLGFPC 458
Cdd:PRK13767 193 LSLSLER----------LEELAGGEFVR-IGLSATIEPLEEVAKFLvgyEDDGEPRDCEIVDARFvKPFDI-KVISPVDD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 459 SSNQTEFKFDLTLNYKIASVIQmysDQKPTLVFCATRKGvqqAASVLVKdakfimtveQKQRLQKYAYSvrdsklrdilk 538
Cdd:PRK13767 261 LIHTPAEEISEALYETLHELIK---EHRTTLIFTNTRSG---AERVLYN---------LRKRFPEEYDE----------- 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462505394 539 DGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPaH--LVVIKSTmhyagglfeEYSETDILQMIGRAG 614
Cdd:PRK13767 315 DNIGAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG-YidLVVLLGS---------PKSVSRLLQRIGRAG 382
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
485-615 |
6.84e-07 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 53.61 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 485 QKPTLVFCATRKGVQQAAsvlvkdakfimtveqkQRLQKYAYSVrdsklrdilkdgAAYHhAGMELSDRKVVEGAFTVGD 564
Cdd:COG0514 230 GGSGIVYCLSRKKVEELA----------------EWLREAGIRA------------AAYH-AGLDAEEREANQDRFLRDE 280
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505394 565 LPVLFTTSTLAMGVNLP-----AHLVVIKSTmhyagglfEEYsetdiLQMIGRAGR 615
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 ... |
485-615 |
1.21e-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: 49.13 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 485 QKPTLVFCATRKGVQQAAsvlvkdakfimtveqkQRLQKyaysvrdsklrdiLKDGAAYHHAGMELSDRKVVEGAFTVGD 564
Cdd:cd18794 30 GGSGIIYCLSRKECEQVA----------------ARLQS-------------KGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505394 565 LPVLFTTSTLAMGVNLP-----AHLVVIKSTMHYagglfeeysetdiLQMIGRAGR 615
Cdd:cd18794 81 IQVIVATVAFGMGIDKPdvrfvIHYSLPKSMESY-------------YQESGRAGR 123
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
242-428 |
1.43e-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: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 242 IQSKAFDDLLyTDRNFVICAPTGSGKTVVFEL-AITRLLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCK 320
Cdd:cd00268 16 IQAQAIPLIL-SGRDVIGQAQTGSGKTLAFLLpILEKLLPEPKKKGRGPQALVLAPTRELAMQIAEVARKLGKGTGLKVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 321 ELTGDTVMDDLFEI--QHAHIIMTTPEK-WDSMTRKWRDnslVQLVRLFLIDEVhivkDE--NRG--PTLEVVVSRM-KT 392
Cdd:cd00268 95 AIYGGAPIKKQIEAlkKGPDIVVGTPGRlLDLIERGKLD---LSNVKYLVLDEA----DRmlDMGfeEDVEKILSALpKD 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462505394 393 VQSvsqtlkntstaipmrfVAVSATIPNA-EDIAEWL 428
Cdd:cd00268 168 RQT----------------LLFSATLPEEvKELAKKF 188
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
255-372 |
1.43e-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: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 255 RNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNIKIVYMAPIKALCSQ---RFDDWKEKfgpiGLNCKELTGDTVMDDL 331
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQqleKFFKYFRK----GYKVTGLSGDSSHKVS 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462505394 332 F--EIQHAHIIMTTPEKWDSMTRKWRDNSLVQL--VRLFLIDEVH 372
Cdd:cd18036 94 FgqIVKASDVIICTPQILINNLLSGREEERVYLsdFSLLIFDECH 138
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
254-372 |
2.09e-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: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 254 DRNFVICAPTGSGKTVVfelAItrLLMEVPLPWLNI----KIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMD 329
Cdd:cd17927 17 GKNTIICLPTGSGKTFV---AV--LICEHHLKKFPAgrkgKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSEN 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462505394 330 DLFE--IQHAHIIMTTPEKWDSMTRKWRDNSLvQLVRLFLIDEVH 372
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 ... |
255-344 |
1.04e-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: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 255 RNFVICAPTGSGKTVVFELAItrlLMEVPLPWLN--IKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTG---DTVMD 329
Cdd:cd17957 28 RDLLACAPTGSGKTLAFLIPI---LQKLGKPRKKkgLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKsleAKAKD 104
|
90
....*....|....*
gi 2462505394 330 DLFEIQHAHIIMTTP 344
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 ... |
253-345 |
5.78e-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: 45.58 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 253 TDRNFVICAPTGSGKTVVfELAITRLLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTvmDDLF 332
Cdd:cd18073 16 KGKNTIICAPTGCGKTFV-SLLICEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGAT--AENV 92
|
90
....*....|....*..
gi 2462505394 333 E----IQHAHIIMTTPE 345
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 ... |
261-344 |
1.89e-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: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 261 APTGSGKTVVFELAITRLLMEVPLPWLnikIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTG--DTVMDDLFEIQHAH 338
Cdd:cd17954 44 AETGSGKTAAFALPILQALLENPQRFF---ALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGgmDMMAQAIALAKKPH 120
|
....*.
gi 2462505394 339 IIMTTP 344
Cdd:cd17954 121 VIVATP 126
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
217-344 |
2.08e-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: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 217 GSLKAVTEIPAKFRSIFKE-FPYFNYIQSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLmEVPLPWLNIKIVYMA 295
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKgYKVPTPIQRKTIPLIL-DGRDVVAMARTGSGKTAAFLIPMIEKL-KAHSPTVGARALILS 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462505394 296 PIKALCSQRFDDWKE--KFgpIGLNCKELTGDTVMDDLFEIQHAH--IIMTTP 344
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 ... |
475-615 |
3.22e-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: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 475 IASVIQMYSDQKPTLVFCATRKGVqqaasvlvkdakfimtveqkqrlQKYAYSVRDskLRDILKDG--AAYHHAGMELSD 552
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQA-----------------------ERLAQRLRE--LCPDRVPPdfIALHHGSLSREL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462505394 553 RKVVEGAFTVGDLPVLFTTSTLAMGVNLPA-HLVV-IKSTmhyagglfeeYSETDILQMIGRAGR 615
Cdd:cd18796 83 REEVEAALKRGDLKVVVATSSLELGIDIGDvDLVIqIGSP----------KSVARLLQRLGRSGH 137
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
486-615 |
4.60e-04 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 44.70 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 486 KPTLVFCATRKGVQQAASvlvkdakfimtveqkqRLQKYAYSVrdsklrdilkdgAAYHhAGMELSDRKVVEGAFTVGDL 565
Cdd:PRK11057 237 KSGIIYCNSRAKVEDTAA----------------RLQSRGISA------------AAYH-AGLDNDVRADVQEAFQRDDL 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462505394 566 PVLFTTSTLAMGVNLP-----AHLVVIKSTMHYagglfeeYSETdilqmiGRAGR 615
Cdd:PRK11057 288 QIVVATVAFGMGINKPnvrfvVHFDIPRNIESY-------YQET------GRAGR 329
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
254-345 |
5.30e-04 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 44.34 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 254 DRNFVICAPTGSGKTVVFELAITRLLMEVplpwlNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLFE 333
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAERLHKK-----GGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKRKE 91
|
90
....*....|...
gi 2462505394 334 I-QHAHIIMTTPE 345
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 ... |
488-615 |
1.63e-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: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 488 TLVFCATRKgvqqAASVLVKDAKfimtveqkQRLQKYAYSVrdSKLrdilkdgAAYHhAGMELSDRKVVEGAFTVGDLPV 567
Cdd:cd18797 38 TIVFCRSRK----LAELLLRYLK--------ARLVEEGPLA--SKV-------ASYR-AGYLAEDRREIEAELFNGELLG 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462505394 568 LFTTSTLAMGVNLPAHLVVIKSTmhYAGGLFEeysetdILQMIGRAGR 615
Cdd:cd18797 96 VVATNALELGIDIGGLDAVVLAG--YPGSLAS------LWQQAGRAGR 135
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
243-372 |
1.92e-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: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 243 QSKAFDDLLytDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNIKI-VYMAPIKALCSQRFDDWKEKFgpiGLNCKE 321
Cdd:cd18034 7 QLELFEAAL--KRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNPKKRaVFLVPTVPLVAQQAEAIRSHT---DLKVGE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462505394 322 LTGDTVMDD------LFEIQHAHIIMTTPEkwdsMTRKWRDNSLVQL--VRLFLIDEVH 372
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 ... |
256-372 |
2.41e-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: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505394 256 NFVICAPTGSGKTVvfelaITRLLMEVPLPWL-NIKIVYMAPIKALCSQRFDDWKeKFGPIGLN-CKELTGDTVMDD-LF 332
Cdd:cd18033 18 NTLVALPTGLGKTF-----IAAVVMLNYYRWFpKGKIVFMAPTKPLVSQQIEACY-KITGIPSSqTAELTGSVPPTKrAE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462505394 333 EIQHAHIIMTTPEKWDS-MTRKWRD-NSLVQLVrlflIDEVH 372
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 ... |
567-615 |
3.41e-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: 39.08 E-value: 3.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462505394 567 VLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGR 615
Cdd:cd18805 73 VLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMRPLSPSEVKQIAGRAGR 121
|
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| |
