|
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 ... |
4-167 |
2.50e-93 |
|
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: 296.58 E-value: 2.50e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 4 PLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDN-SLVQ 82
Cdd:cd18023 47 PLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 83 LVRLFLIDEVHIVKdENRGPTLEVVVSRMKTVQSVSQTlkNTSTAIPMRFVAVSATIPNAEDIAEWLSDGerPAVCLKMD 162
Cdd:cd18023 127 LVALVLIDEVHIIK-ENRGATLEVVVSRMKTLSSSSEL--RGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFG 201
|
....*
gi 1034556053 163 ESHRP 167
Cdd:cd18023 202 ESFRP 206
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
11-477 |
2.95e-87 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 291.80 E-value: 2.95e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRK---WRDNslvqlVRLF 87
Cdd:COG1204 68 KALYIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRNgpsWLRD-----VDLV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 88 LIDEVHIVKDENRGPTLEVVVSRMKTVqsvsqtlkntstAIPMRFVAVSATIPNAEDIAEWLsdgERPAVclkmDESHRP 167
Cdd:COG1204 142 VVDEAHLIDDESRGPTLEVLLARLRRL------------NPEAQIVALSATIGNAEEIAEWL---DAELV----KSDWRP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 168 VKLQKVVLgfpcSSNQTEF--KFDLTLNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKY 245
Cdd:COG1204 203 VPLNEGVL----YDGVLRFddGSRRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEEL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 246 AYSVR--------DSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTmHYAGG 317
Cdd:COG1204 279 AEELLevseethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-KRGGM 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 318 lfEEYSETDILQMIGRAGRPQFDTTATAVIMTR-LSTRDKYIQMLACRDT--VESSLH--RHLIEHLNAEIVLHTITDVN 392
Cdd:COG1204 358 --VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKsSDEADELFERYILGEPepIRSKLAneSALRTHLLALIASGFANSRE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 393 IAVEWIRSTLLYIRAlknpshygfasglNKDGIEAKLQElclkNLNDLSSLDLIKMDEGvNFKPTEAGRLMAWYYITFET 472
Cdd:COG1204 436 ELLDFLENTFYAYQY-------------DKGDLEEVVDD----ALEFLLENGFIEEDGD-RLRATKLGKLVSRLYIDPLT 497
|
....*
gi 1034556053 473 VKKFY 477
Cdd:COG1204 498 AAELV 502
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
456-769 |
3.00e-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: 239.79 E-value: 3.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 456 PTEAGRLMAWYYITFETVKKFYT-ISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKdpnriTIRFPMEGRIKTR 534
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQsLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLE-----KVPIPVKGDIEDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 535 EMKVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWeNSLHVSKQLE 614
Cdd:pfam02889 76 HAKVNILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFE-ILLSKGWLSAALTALDLCKMIEQRMW-DSDSPLRQFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 615 KIGITLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEqITRYSDTTAEILVTVIlRNFE 694
Cdd:pfam02889 154 GIPPELIKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAE-VQPITRSVLRVEVTIT-PDFP 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556053 695 qlQTKRTASDSHYVTLIIGDADNQVVYLHKITdSVLLKAGSWAKKIAVKRALKSE---DLSINLISSEFVGLDIQQKL 769
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 ... |
456-771 |
6.21e-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: 216.84 E-value: 6.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 456 PTEAGRLMAWYYITFETVKKFYT-ISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKDpnritIRFPMEGRIKTR 534
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQsLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-----VPIPVKEGIIDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 535 EM-KVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWENSLHVSKQL 613
Cdd:smart00973 76 PHaKVNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVD-IALSKGWLRTALNALDLSQMVVQRLWEDSDSPLKQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 614 EKIGI--TLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEQITRYSDTTaeILVTVILR 691
Cdd:smart00973 155 PHFLIedVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITRDLT--LRVELEIT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 692 NFEQLQTKRTASDSHYVTLIIGDADNQVVYLHKITDSVLLKAGSWAK-KIAVKR-ALKSEDLSINLISSEFVGLDIQQKL 769
Cdd:smart00973 233 PVFAWDLPRHKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKlDFTVPLsEPGPENYTVYLISDSYLGCDQEVSF 312
|
..
gi 1034556053 770 TV 771
Cdd:smart00973 313 SL 314
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
166-350 |
2.20e-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: 2.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 166 RPVKLQKVVLGFPCSSNQTEFKFDLT--LNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVkdakfimtveqkqrlq 243
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 244 kyaysvrdsklrdilkdGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYS 323
Cdd:cd18795 65 -----------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELS 127
|
170 180
....*....|....*....|....*..
gi 1034556053 324 ETDILQMIGRAGRPQFDTTATAVIMTR 350
Cdd:cd18795 128 PLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
11-348 |
3.54e-46 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 178.61 E-value: 3.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKEkFGPIGLNCKELTGDTVMDDLFeIQHAHIIMTTPEKWDSMTRK---W-RDNSLVqlvrl 86
Cdd:PRK02362 69 KALYIVPLRALASEKFEEFER-FEELGVRVGISTGDYDSRDEW-LGDNDIIVATSEKVDSLLRNgapWlDDITCV----- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 87 fLIDEVHIVKDENRGPTLEVVVSRMKTVQSVSQTlkntstaipmrfVAVSATIPNAEDIAEWLsDGERpavclkMDESHR 166
Cdd:PRK02362 142 -VVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQV------------VALSATIGNADELADWL-DAEL------VDSEWR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 167 PVKLQKVVL---GFPCSSNQTEFKF---DLTLNYkiasVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQ 240
Cdd:PRK02362 202 PIDLREGVFyggAIHFDDSQREVEVpskDDTLNL----VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 241 RLQKYAYSVRDS-------KLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMH 313
Cdd:PRK02362 278 ELAELAEEIREVsdtetskDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRR 357
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034556053 314 YAGGL------FEEYSetdilQMIGRAGRPQFDTTATAVIM 348
Cdd:PRK02362 358 YDGGAgmqpipVLEYH-----QMAGRAGRPGLDPYGEAVLL 393
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
10-145 |
1.93e-20 |
|
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: 89.61 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 10 IKIVYMAPIKALCSQRFDDWKEKFGPIGLN-CKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRdnsLVQLVRLFL 88
Cdd:pfam00270 46 PQALVLAPTRELAEQIYEELKKLGKGLGLKvASLLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLV 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556053 89 IDEVHIVKDENRGPTLEVVVSRMKTvqsvsqtlkntstaiPMRFVAVSATIP-NAEDI 145
Cdd:pfam00270 123 LDEAHRLLDMGFGPDLEEILRRLPK---------------KRQILLLSATLPrNLEDL 165
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
258-337 |
1.96e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 63.77 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 258 LKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIKSTmhyagglfeEYSETDILQMIGRAGR 336
Cdd:smart00490 10 LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL---------PWSPASYIQRIGRAGR 80
|
.
gi 1034556053 337 P 337
Cdd:smart00490 81 A 81
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
9-149 |
5.74e-12 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 65.98 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 9 NIKIVYMAPIKALCSQRFDDWKEKFGPIGLN-CKELTGDTVMDDLFEIQH--AHIIMTTPEKWDSMTRKwrDNSLVQLVR 85
Cdd:smart00487 54 GGRVLVLVPTRELAEQWAEELKKLGPSLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLEN--DKLSLSNVD 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034556053 86 LFLIDEVHIVKDENRGPTLEVVVSRMKTVQsvsqtlkntstaipmRFVAVSATIPNAEDIAEWL 149
Cdd:smart00487 132 LVILDEAHRLLDGGFGDQLEKLLKLLPKNV---------------QLLLLSATPPEEIENLLEL 180
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
195-336 |
2.46e-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: 55.68 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 195 KIASVIQMYSDQKP--TLVFCATRKGVqqaasvlvkDAKFImtveqkqrLQKYAYSVrdsklrdilkdgaAYHHAGMELS 272
Cdd:pfam00271 2 KLEALLELLKKERGgkVLIFSQTKKTL---------EAELL--------LEKEGIKV-------------ARLHGDLSQE 51
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556053 273 DRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIkstmhyagglFE-EYSETDILQMIGRAGR 336
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 ... |
4-167 |
2.50e-93 |
|
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: 296.58 E-value: 2.50e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 4 PLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDN-SLVQ 82
Cdd:cd18023 47 PLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 83 LVRLFLIDEVHIVKdENRGPTLEVVVSRMKTVQSVSQTlkNTSTAIPMRFVAVSATIPNAEDIAEWLSDGerPAVCLKMD 162
Cdd:cd18023 127 LVALVLIDEVHIIK-ENRGATLEVVVSRMKTLSSSSEL--RGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFG 201
|
....*
gi 1034556053 163 ESHRP 167
Cdd:cd18023 202 ESFRP 206
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
11-477 |
2.95e-87 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 291.80 E-value: 2.95e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRK---WRDNslvqlVRLF 87
Cdd:COG1204 68 KALYIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRNgpsWLRD-----VDLV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 88 LIDEVHIVKDENRGPTLEVVVSRMKTVqsvsqtlkntstAIPMRFVAVSATIPNAEDIAEWLsdgERPAVclkmDESHRP 167
Cdd:COG1204 142 VVDEAHLIDDESRGPTLEVLLARLRRL------------NPEAQIVALSATIGNAEEIAEWL---DAELV----KSDWRP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 168 VKLQKVVLgfpcSSNQTEF--KFDLTLNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKY 245
Cdd:COG1204 203 VPLNEGVL----YDGVLRFddGSRRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEEL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 246 AYSVR--------DSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTmHYAGG 317
Cdd:COG1204 279 AEELLevseethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-KRGGM 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 318 lfEEYSETDILQMIGRAGRPQFDTTATAVIMTR-LSTRDKYIQMLACRDT--VESSLH--RHLIEHLNAEIVLHTITDVN 392
Cdd:COG1204 358 --VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKsSDEADELFERYILGEPepIRSKLAneSALRTHLLALIASGFANSRE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 393 IAVEWIRSTLLYIRAlknpshygfasglNKDGIEAKLQElclkNLNDLSSLDLIKMDEGvNFKPTEAGRLMAWYYITFET 472
Cdd:COG1204 436 ELLDFLENTFYAYQY-------------DKGDLEEVVDD----ALEFLLENGFIEEDGD-RLRATKLGKLVSRLYIDPLT 497
|
....*
gi 1034556053 473 VKKFY 477
Cdd:COG1204 498 AAELV 502
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
456-769 |
3.00e-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: 239.79 E-value: 3.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 456 PTEAGRLMAWYYITFETVKKFYT-ISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKdpnriTIRFPMEGRIKTR 534
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQsLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLE-----KVPIPVKGDIEDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 535 EMKVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWeNSLHVSKQLE 614
Cdd:pfam02889 76 HAKVNILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFE-ILLSKGWLSAALTALDLCKMIEQRMW-DSDSPLRQFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 615 KIGITLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEqITRYSDTTAEILVTVIlRNFE 694
Cdd:pfam02889 154 GIPPELIKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAE-VQPITRSVLRVEVTIT-PDFP 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556053 695 qlQTKRTASDSHYVTLIIGDADNQVVYLHKITdSVLLKAGSWAKKIAVKRALKSE---DLSINLISSEFVGLDIQQKL 769
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 ... |
456-771 |
6.21e-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: 216.84 E-value: 6.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 456 PTEAGRLMAWYYITFETVKKFYT-ISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKDpnritIRFPMEGRIKTR 534
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQsLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-----VPIPVKEGIIDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 535 EM-KVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWENSLHVSKQL 613
Cdd:smart00973 76 PHaKVNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVD-IALSKGWLRTALNALDLSQMVVQRLWEDSDSPLKQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 614 EKIGI--TLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEQITRYSDTTaeILVTVILR 691
Cdd:smart00973 155 PHFLIedVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITRDLT--LRVELEIT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 692 NFEQLQTKRTASDSHYVTLIIGDADNQVVYLHKITDSVLLKAGSWAK-KIAVKR-ALKSEDLSINLISSEFVGLDIQQKL 769
Cdd:smart00973 233 PVFAWDLPRHKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKlDFTVPLsEPGPENYTVYLISDSYLGCDQEVSF 312
|
..
gi 1034556053 770 TV 771
Cdd:smart00973 313 SL 314
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
166-350 |
2.20e-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: 2.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 166 RPVKLQKVVLGFPCSSNQTEFKFDLT--LNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVkdakfimtveqkqrlq 243
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 244 kyaysvrdsklrdilkdGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYS 323
Cdd:cd18795 65 -----------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELS 127
|
170 180
....*....|....*....|....*..
gi 1034556053 324 ETDILQMIGRAGRPQFDTTATAVIMTR 350
Cdd:cd18795 128 PLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
11-153 |
6.55e-48 |
|
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: 168.98 E-value: 6.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRKWRDNsLVQLVRLFLID 90
Cdd:cd17921 48 KAVYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSVNKL-LLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVD 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034556053 91 EVHIVKDENRGPTLEVVVSRMKTVQsvsqtlkntstaIPMRFVAVSATIPNAEDIAEWLSDGE 153
Cdd:cd17921 126 EAHLIGDGERGVVLELLLSRLLRIN------------KNARFVGLSATLPNAEDLAEWLGVED 176
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
11-348 |
3.54e-46 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 178.61 E-value: 3.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKEkFGPIGLNCKELTGDTVMDDLFeIQHAHIIMTTPEKWDSMTRK---W-RDNSLVqlvrl 86
Cdd:PRK02362 69 KALYIVPLRALASEKFEEFER-FEELGVRVGISTGDYDSRDEW-LGDNDIIVATSEKVDSLLRNgapWlDDITCV----- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 87 fLIDEVHIVKDENRGPTLEVVVSRMKTVQSVSQTlkntstaipmrfVAVSATIPNAEDIAEWLsDGERpavclkMDESHR 166
Cdd:PRK02362 142 -VVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQV------------VALSATIGNADELADWL-DAEL------VDSEWR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 167 PVKLQKVVL---GFPCSSNQTEFKF---DLTLNYkiasVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQ 240
Cdd:PRK02362 202 PIDLREGVFyggAIHFDDSQREVEVpskDDTLNL----VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 241 RLQKYAYSVRDS-------KLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMH 313
Cdd:PRK02362 278 ELAELAEEIREVsdtetskDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRR 357
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034556053 314 YAGGL------FEEYSetdilQMIGRAGRPQFDTTATAVIM 348
Cdd:PRK02362 358 YDGGAgmqpipVLEYH-----QMAGRAGRPGLDPYGEAVLL 393
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
11-476 |
2.16e-44 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 172.69 E-value: 2.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKEkFGPIGLNCKELTGDTVMDDLFeIQHAHIIMTTPEKWDSMTRkwRDNSLVQLVRLFLID 90
Cdd:PRK00254 70 KAVYLVPLKALAEEKYREFKD-WEKLGLRVAMTTGDYDSTDEW-LGKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVAD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 91 EVHIVKDENRGPTLEVVVSRMKTVQSVsqtlkntstaipmrfVAVSATIPNAEDIAEWLSdgerpAVCLKMDesHRPVKL 170
Cdd:PRK00254 146 EIHLIGSYDRGATLEMILTHMLGRAQI---------------LGLSATVGNAEELAEWLN-----AELVVSD--WRPVKL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 171 QKVV--LGFPCSSNQTEFKFDLTLNykiASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYS 248
Cdd:PRK00254 204 RKGVfyQGFLFWEDGKIERFPNSWE---SLVYDAVKKGKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKELADS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 249 VRDS----KLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSE 324
Cdd:PRK00254 281 LEENptneKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 325 TDILQMIGRAGRPQFDTTATAVIMTRL----STRDKYI----QMLACRDTVESSLHRHLIehlnAEIVLHTITDVNIAVE 396
Cdd:PRK00254 361 LEIQQMMGRAGRPKYDEVGEAIIVATTeepsKLMERYIfgkpEKLFSMLSNESAFRSQVL----ALITNFGVSNFKELVN 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 397 WIRSTlLYIRALKNPSHygfasglnkdgIEAKLQELC---LKNlndlsslDLIKMDEGVNFKPTEAGRLMAWYYITFETV 473
Cdd:PRK00254 437 FLERT-FYAHQRKDLYS-----------LEEKAKEIVyflLEN-------EFIDIDLEDRFIPLPLGIRTSQLYIDPLTA 497
|
...
gi 1034556053 474 KKF 476
Cdd:PRK00254 498 KKF 500
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
11-348 |
7.74e-41 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 162.03 E-value: 7.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKEKFGP--IGLnckeLTGDTVmddlfEIQHA-HIIMTTpEKWDSMTrkWRDNSLVQLVRLF 87
Cdd:COG4581 70 RSFYTAPIKALSNQKFFDLVERFGAenVGL----LTGDAS-----VNPDApIVVMTT-EILRNML--YREGADLEDVGVV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 88 LIDEVHIVKDENRGPTLEVVVsrmktvqsvsqtlkntsTAIP--MRFVAVSATIPNAEDIAEWLSD--GErpavCLKMDE 163
Cdd:COG4581 138 VMDEFHYLADPDRGWVWEEPI-----------------IHLParVQLVLLSATVGNAEEFAEWLTRvrGE----TAVVVS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 164 SHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKIASVIQM--YSDQKPTLVFCATRKGVQQAASVLVkdAKFIMTVEQKQR 241
Cdd:COG4581 197 EERPVPLEFHYLVTPRLFPLFRVNPELLRPPSRHEVIEEldRGGLLPAIVFIFSRRGCDEAAQQLL--SARLTTKEERAE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 242 LQKYA-------YSVRDSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHY 314
Cdd:COG4581 275 IREAIdefaedfSVLFGKTLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKF 354
|
330 340 350
....*....|....*....|....*....|....
gi 1034556053 315 AGGLFEEYSETDILQMIGRAGRPQFDTTATAVIM 348
Cdd:COG4581 355 DGERHRPLTAREFHQIAGRAGRRGIDTEGHVVVL 388
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
11-149 |
1.07e-40 |
|
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: 148.29 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKEKF-GPIGLNCKELTGDtVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLI 89
Cdd:cd18022 49 KVVYIAPLKALVRERVDDWKKRFeEKLGKKVVELTGD-VTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIII 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 90 DEVHIVKDEnRGPTLEVVVSRMKTVQSVsqtlkntsTAIPMRFVAVSATIPNAEDIAEWL 149
Cdd:cd18022 128 DEIHLLGSD-RGPVLEVIVSRMNYISSQ--------TEKPVRLVGLSTALANAGDLANWL 178
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
11-149 |
2.24e-40 |
|
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: 147.40 E-value: 2.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKEKFGP-IGLNCKELTGDTVMDdLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLI 89
Cdd:cd18021 51 RAVYIAPMQELVDARYKDWRAKFGPlLGKKVVKLTGETSTD-LKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIA 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 90 DEVHIVKDENrGPTLEVVVSRMKTVQsvSQTLKntstaiPMRFVAVSATIPNAEDIAEWL 149
Cdd:cd18021 130 DELHLIGGEN-GPVYEVVVSRMRYIS--SQLEK------PIRIVGLSSSLANARDVGEWL 180
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
9-477 |
7.07e-39 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 155.04 E-value: 7.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 9 NIKIVYMAPIKALCSQRFDDWKeKFGPIGLNCKELTGDtvMDDLFE-IQHAHIIMTTPEKWDSMTRkwRDNSLVQLVRLF 87
Cdd:PRK01172 65 GLKSIYIVPLRSLAMEKYEELS-RLRSLGMRVKISIGD--YDDPPDfIKRYDVVILTSEKADSLIH--HDPYIINDVGLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 88 LIDEVHIVKDENRGPTLEVVVSRMKTVqsvsqtlkNTSTaipmRFVAVSATIPNAEDIAEWLSdgerpAVCLKmdESHRP 167
Cdd:PRK01172 140 VADEIHIIGDEDRGPTLETVLSSARYV--------NPDA----RILALSATVSNANELAQWLN-----ASLIK--SNFRP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 168 VKLQKVVLGFPCSSNQTEFKFDLTLNYKIASVIQmysDQKPTLVFCATRKGVQQAASVLVK----DAKFIMTVEQKqrlq 243
Cdd:PRK01172 201 VPLKLGILYRKRLILDGYERSQVDINSLIKETVN---DGGQVLVFVSSRKNAEDYAEMLIQhfpeFNDFKVSSENN---- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 244 kyaySVRDSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYS 323
Cdd:PRK01172 274 ----NVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRYLS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 324 ETDILQMIGRAGRPQFDTTATAVI-MTRLSTRDKYIQMLACR-DTVESSLHRHLIEHLN--AEIVLHTITDVNIAVEWIR 399
Cdd:PRK01172 350 NMEIKQMIGRAGRPGYDQYGIGYIyAASPASYDAAKKYLSGEpEPVISYMGSQRKVRFNtlAAISMGLASSMEDLILFYN 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 400 STLLYIRAlknpshygfasglNKDGIEAKLQElclknlndlsSLDLIK----MDEGVNFKPTEAGRLMAWYYITFET--- 472
Cdd:PRK01172 430 ETLMAIQN-------------GVDEIDYYIES----------SLKFLKengfIKGDVTLRATRLGKLTSDLYIDPESali 486
|
....*
gi 1034556053 473 VKKFY 477
Cdd:PRK01172 487 LKSAF 491
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
9-149 |
5.27e-33 |
|
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: 127.10 E-value: 5.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 9 NIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFL 88
Cdd:cd18019 72 AFKIVYIAPMKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKE-QISETQIIVTTPEKWDIITRKSGDRTYTQLVRLII 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034556053 89 IDEVHIVKDEnRGPTLEVVVSRmkTVQSVSQTLKntstaiPMRFVAVSATIPNAEDIAEWL 149
Cdd:cd18019 151 IDEIHLLHDD-RGPVLESIVAR--TIRQIEQTQE------YVRLVGLSATLPNYEDVATFL 202
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
9-149 |
1.57e-31 |
|
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: 122.54 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 9 NIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRKWR-DNSLVQLVRLF 87
Cdd:cd18020 56 DFKIVYIAPMKALAAEMVEKFSKRLAPLGIKVKELTGDMQLTKK-EIAETQIIVTTPEKWDVVTRKSSgDVALSQLVRLL 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034556053 88 LIDEVHIVKDEnRGPTLEVVVSR-MKTVQSvSQTLkntstaipMRFVAVSATIPNAEDIAEWL 149
Cdd:cd18020 135 IIDEVHLLHDD-RGPVIESLVARtLRQVES-TQSM--------IRIVGLSATLPNYLDVADFL 187
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
11-149 |
1.44e-27 |
|
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: 110.50 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKeKFGPIGLNCKELTGDTVMDDLFeIQHAHIIMTTPEKWDSMTR-KWrdnSLVQLVRLFLI 89
Cdd:cd18028 47 KALYLVPLRALASEKYEEFK-KLEEIGLKVGISTGDYDEDDEW-LGDYDIIVATYEKFDSLLRhSP---SWLRDVGVVVV 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 90 DEVHIVKDENRGPTLEVVVSRMKTVqsvsqtlkNTSTaipmRFVAVSATIPNAEDIAEWL 149
Cdd:cd18028 122 DEIHLISDEERGPTLESIVARLRRL--------NPNT----QIIGLSATIGNPDELAEWL 169
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
10-145 |
1.93e-20 |
|
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: 89.61 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 10 IKIVYMAPIKALCSQRFDDWKEKFGPIGLN-CKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRdnsLVQLVRLFL 88
Cdd:pfam00270 46 PQALVLAPTRELAEQIYEELKKLGKGLGLKvASLLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLV 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556053 89 IDEVHIVKDENRGPTLEVVVSRMKTvqsvsqtlkntstaiPMRFVAVSATIP-NAEDI 145
Cdd:pfam00270 123 LDEAHRLLDMGFGPDLEEILRRLPK---------------KRQILLLSATLPrNLEDL 165
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
11-339 |
4.46e-20 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 96.50 E-value: 4.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKEKFGPiGLNCKELTG---------DTVMDdlfeiqhAHIIMTTPEKWDSMTRKWRDNSLV 81
Cdd:COG1202 256 KMLFLVPLVALANQKYEDFKDRYGD-GLDVSIRVGasrirddgtRFDPN-------ADIIVGTYEGIDHALRTGRDLGDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 82 QLVrlfLIDEVHIVKDENRGPTLEVVVSRMKTVQSVSQtlkntstaipmrFVAVSATIPNAEDIAEWLSdgerpavcLKM 161
Cdd:COG1202 328 GTV---VIDEVHMLEDPERGHRLDGLIARLKYYCPGAQ------------WIYLSATVGNPEELAKKLG--------AKL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 162 DE-SHRPVKLQKVVLgFpcssNQTEFKFDLtlnykIASVIQMYSDQKP-------TLVFCATRKgvqqaasvlvkdakfi 233
Cdd:COG1202 385 VEyEERPVPLERHLT-F----ADGREKIRI-----INKLVKREFDTKSskgyrgqTIIFTNSRR---------------- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 234 mtveqkqrlqkyaysvRDSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKS-TM 312
Cdd:COG1202 439 ----------------RCHEIARALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSlAM 502
|
330 340
....*....|....*....|....*..
gi 1034556053 313 hyaGGlfEEYSETDILQMIGRAGRPQF 339
Cdd:COG1202 503 ---GI--EWLSVQEFHQMLGRAGRPDY 524
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
454-724 |
1.59e-17 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 84.62 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 454 FKPTEAGRLMAWYYITFETVKKFY-TISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKdpnRITIRFPMEGrIK 532
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNeLLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAE---KLPIRLENPS-LD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 533 TREMKVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDfVAAQEKKFAVLLNSLILAKCFRCKLWEnSLHVSKQ 612
Cdd:smart00611 78 DPHVKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVD-IALERGWLSTALNALNLSQMIIQALWP-TDSPLLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 613 LEKIGITLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYEL--KVEQITRysdTTAEILVTV-- 688
Cdd:smart00611 156 LPHLPEEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIeiSLEPITR---TVLGVEVTLtv 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 1034556053 689 -ILRNFEQLQTkrtasdSHYVTLIIGDADNQVVYLHK 724
Cdd:smart00611 233 dLTWDDEIHGK------QEGWWLVIGDSDGNELLHIE 263
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
11-150 |
4.84e-15 |
|
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: 75.17 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKEKFGPIGLnckeLTGDTVMDDLFEIqhahIIMTTpEKWDSMTrkWRDNSLVQLVRLFLID 90
Cdd:cd18024 77 RVIYTSPIKALSNQKYRELQEEFGDVGL----MTGDVTINPNASC----LVMTT-EILRSML--YRGSEIMREVAWVIFD 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 91 EVHIVKDENRGPTLEvvvsrmKTVQSVSQTlkntstaipMRFVAVSATIPNAEDIAEWLS 150
Cdd:cd18024 146 EIHYMRDKERGVVWE------ETIILLPDK---------VRYVFLSATIPNARQFAEWIC 190
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
11-149 |
7.04e-14 |
|
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: 71.14 E-value: 7.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQRFDDWKEKFGPIGLnckeLTGDTVMDDlfeiQHAHIIMTTpEKWDSMTrkWRDNSLVQLVRLFLID 90
Cdd:cd18027 53 RTIYTSPIKALSNQKFRDFKNTFGDVGL----ITGDVQLNP----EASCLIMTT-EILRSML--YNGSDVIRDLEWVIFD 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556053 91 EVHIVKDENRGPTLEVVVSRMKtvQSVSqtlkntstaipmrFVAVSATIPNAEDIAEWL 149
Cdd:cd18027 122 EVHYINDAERGVVWEEVLIMLP--DHVS-------------IILLSATVPNTVEFADWI 165
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
258-337 |
1.96e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 63.77 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 258 LKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIKSTmhyagglfeEYSETDILQMIGRAGR 336
Cdd:smart00490 10 LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL---------PWSPASYIQRIGRAGR 80
|
.
gi 1034556053 337 P 337
Cdd:smart00490 81 A 81
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
11-336 |
2.04e-12 |
|
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: 71.41 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCS---QRFDDWKEKFGPiGLNCKELTGDTVMDDLFEI-QHAHIIMTTPEKWD-SM---TRKWRdnSLVQ 82
Cdd:COG1205 103 TALYLYPTKALARdqlRRLRELAEALGL-GVRVATYDGDTPPEERRWIrEHPDIVLTNPDMLHyGLlphHTRWA--RFFR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 83 LVRLFLIDEVHIVkdenRGptleV-------VVSRMKTVqsvsqtLKNTSTAipMRFVAVSATIPNAEDIAEWLSDgeRP 155
Cdd:COG1205 180 NLRYVVIDEAHTY----RG----VfgshvanVLRRLRRI------CRHYGSD--PQFILASATIGNPAEHAERLTG--RP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 156 AVCLkmDESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKIASVIqMYSDQKpTLVFCATRKGVQQAASVLvkdakfimt 235
Cdd:COG1205 242 VTVV--DEDGSPRGERTFVLWNPPLVDDGIRRSALAEAARLLADL-VREGLR-TLVFTRSRRGAELLARYA--------- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 236 veqKQRLQKYAYSVRdsklrdIlkdgAAYHhAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPA-HLVVIkstMHY 314
Cdd:COG1205 309 ---RRALREPDLADR------V----AAYR-AGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVVL---AGY 371
|
330 340
....*....|....*....|..
gi 1034556053 315 AGglfeeySETDILQMIGRAGR 336
Cdd:COG1205 372 PG------TRASFWQQAGRAGR 387
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
9-149 |
5.74e-12 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 65.98 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 9 NIKIVYMAPIKALCSQRFDDWKEKFGPIGLN-CKELTGDTVMDDLFEIQH--AHIIMTTPEKWDSMTRKwrDNSLVQLVR 85
Cdd:smart00487 54 GGRVLVLVPTRELAEQWAEELKKLGPSLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLEN--DKLSLSNVD 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034556053 86 LFLIDEVHIVKDENRGPTLEVVVSRMKTVQsvsqtlkntstaipmRFVAVSATIPNAEDIAEWL 149
Cdd:smart00487 132 LVILDEAHRLLDGGFGDQLEKLLKLLPKNV---------------QLLLLSATPPEEIENLLEL 180
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
195-336 |
2.46e-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: 55.68 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 195 KIASVIQMYSDQKP--TLVFCATRKGVqqaasvlvkDAKFImtveqkqrLQKYAYSVrdsklrdilkdgaAYHHAGMELS 272
Cdd:pfam00271 2 KLEALLELLKKERGgkVLIFSQTKKTL---------EAELL--------LEKEGIKV-------------ARLHGDLSQE 51
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556053 273 DRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIkstmhyagglFE-EYSETDILQMIGRAGR 336
Cdd:pfam00271 52 EREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN----------YDlPWNPASYIQRIGRAGR 107
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
12-154 |
1.90e-08 |
|
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: 55.45 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 12 IVYMAPIKALCSQ-------RFDdwkEKFGPIGLN-CKELTGDTVMDDlfeIQHAHIIMTTPEKWDSMTRKWRDNSLVQL 83
Cdd:cd18025 49 VVYVAPTKALVNQvvaevyaRFS---KKYPPSGKSlWGVFTRDYRHNN---PMNCQVLITVPECLEILLLSPHNASWVPR 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034556053 84 VRLFLIDEVHIVKDENRGPTLEvvvsrmktvqsvsQTLkntsTAIPMRFVAVSATIPNAEDIAEWLSDGER 154
Cdd:cd18025 123 IKYVIFDEIHSIGQSEDGAVWE-------------QLL----LLIPCPFLALSATIGNPQKFHEWLQSVQR 176
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
11-337 |
2.17e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 58.11 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 11 KIVYMAPIKALCSQrfddWKEKFgpiglncKELTGDTVMDDLFEIQHAHIIMTTpekWDSMTRKWRDNSLVQLVRLFLID 90
Cdd:COG1061 129 RVLVLVPRRELLEQ----WAEEL-------RRFLGDPLAGGGKKDSDAPITVAT---YQSLARRAHLDELGDRFGLVIID 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 91 EVHIVkdenRGPTLEVVVSRMKtvqsvsqtlkntstaiPMRFVAVSATiPNAED---IAEWLSDGERPAVCLK--MDESH 165
Cdd:COG1061 195 EAHHA----GAPSYRRILEAFP----------------AAYRLGLTAT-PFRSDgreILLFLFDGIVYEYSLKeaIEDGY 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 166 -RPVKLQKVVLGFpcSSNQTEF-KFDLTLNYKIAS-----------VIQMYSDQKPTLVFCATrkgvqqaasvlVKDAKF 232
Cdd:COG1061 254 lAPPEYYGIRVDL--TDERAEYdALSERLREALAAdaerkdkilreLLREHPDDRKTLVFCSS-----------VDHAEA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 233 IMtveqkQRLQKYAYSvrdsklrdilkdgAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPA--HLVVIKS 310
Cdd:COG1061 321 LA-----ELLNEAGIR-------------AAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRP 382
|
330 340
....*....|....*....|....*..
gi 1034556053 311 TMhyagglfeeySETDILQMIGRAGRP 337
Cdd:COG1061 383 TG----------SPREFIQRLGRGLRP 399
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
4-355 |
5.19e-08 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 57.63 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 4 PLPWLNIKIVYMAPIKALCS--QR--------FDDWKEKFGPIGLNCKE--LTGDTVMDDLFEI--QHAHIIMTTPEKWD 69
Cdd:PRK09751 32 AHKRKTSRILYISPIKALGTdvQRnlqiplkgIADERRRRGETEVNLRVgiRTGDTPAQERSKLtrNPPDILITTPESLY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 70 SM-TRKWRDNslVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMktvqsvsQTLKNTstaiPMRFVAVSATIPNAEDIAEW 148
Cdd:PRK09751 112 LMlTSRARET--LRGVETVIIDEVHAVAGSKRGAHLALSLERL-------DALLHT----SAQRIGLSATVRSASDVAAF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 149 LSdGERPAVCLKMDESHRPvKLQKVV-----LGFPCSSNQTEFKFDLTLNYKI-----ASVIQMYSDQKPTLVFCATRkG 218
Cdd:PRK09751 179 LG-GDRPVTVVNPPAMRHP-QIRIVVpvanmDDVSSVASGTGEDSHAGREGSIwpyieTGILDEVLRHRSTIVFTNSR-G 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 219 VQQAASVLVKD---AKFIMTVEQKQRLQKYAYSVRDSKLRDILKDG--AAYHHAGMELSDRKVVEGAFTVGDLPVLFTTS 293
Cdd:PRK09751 256 LAEKLTARLNElyaARLQRSPSIAVDAAHFESTSGATSNRVQSSDVfiARSHHGSVSKEQRAITEQALKSGELRCVVATS 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034556053 294 TLAMGVNLPAHLVVIK--STMHYAGGlfeeysetdiLQMIGRAGRpQFDTTATAVIMTRlSTRD 355
Cdd:PRK09751 336 SLELGIDMGAVDLVIQvaTPLSVASG----------LQRIGRAGH-QVGGVSKGLFFPR-TRRD 387
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
206-336 |
5.24e-07 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 53.61 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 206 QKPTLVFCATRKGVQQAAsvlvkdakfimtveqkQRLQKYAYSVrdsklrdilkdgAAYHhAGMELSDRKVVEGAFTVGD 285
Cdd:COG0514 230 GGSGIVYCLSRKKVEELA----------------EWLREAGIRA------------AAYH-AGLDAEEREANQDRFLRDE 280
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556053 286 LPVLFTTSTLAMGVNLP-----AHLVVIKSTmhyagglfEEYsetdiLQMIGRAGR 336
Cdd:COG0514 281 VDVIVATIAFGMGIDKPdvrfvIHYDLPKSI--------EAY-----YQEIGRAGR 323
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
10-149 |
7.66e-07 |
|
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: 50.27 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 10 IKIVYMAPIKALCSQRFDDWKEKfgpigLNCKEL-------TGDT-------VMDDLfeiqhAHIIMTTPEKWDSMTRKW 75
Cdd:cd17922 34 VQVLYISPLKALINDQERRLEEP-----LDEIDLeipvavrHGDTsqsekakQLKNP-----PGILITTPESLELLLVNK 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034556053 76 RDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVqsvsqtlkntsTAIPMRFVAVSATIPNAEDIAEWL 149
Cdd:cd17922 104 KLRELFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKL-----------TGRPLRRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
59-149 |
1.07e-06 |
|
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: 50.68 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 59 HIIMTTPEKWDSMTrkwrdNSLVQLVRLFLI-----DEVHIVKDENRGPTLEVVVSRMktvqsvsqTLKNTSTaipMRFV 133
Cdd:cd18026 112 SVAVCTIEKANSLV-----NSLIEEGRLDELglvvvDELHMLGDGHRGALLELLLTKL--------LYAAQKN---IQIV 175
|
90
....*....|....*.
gi 1034556053 134 AVSATIPNAEDIAEWL 149
Cdd:cd18026 176 GMSATLPNLEELASWL 191
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
206-336 |
1.08e-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: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 206 QKPTLVFCATRKGVQQAAsvlvkdakfimtveqkQRLQKyaysvrdsklrdiLKDGAAYHHAGMELSDRKVVEGAFTVGD 285
Cdd:cd18794 30 GGSGIIYCLSRKECEQVA----------------ARLQS-------------KGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556053 286 LPVLFTTSTLAMGVNLP-----AHLVVIKSTMHYagglfeeysetdiLQMIGRAGR 336
Cdd:cd18794 81 IQVIVATVAFGMGIDKPdvrfvIHYSLPKSMESY-------------YQESGRAGR 123
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
196-336 |
2.54e-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: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 196 IASVIQMYSDQKPTLVFCATRKGVqqaasvlvkdakfimtveqkqrlQKYAYSVRDskLRDILKDG--AAYHHAGMELSD 273
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQA-----------------------ERLAQRLRE--LCPDRVPPdfIALHHGSLSREL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034556053 274 RKVVEGAFTVGDLPVLFTTSTLAMGVNLPA-HLVV-IKSTmhyagglfeeYSETDILQMIGRAGR 336
Cdd:cd18796 83 REEVEAALKRGDLKVVVATSSLELGIDIGDvDLVIqIGSP----------KSVARLLQRLGRSGH 137
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
207-336 |
3.56e-04 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 44.70 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 207 KPTLVFCATRKGVQQAASvlvkdakfimtveqkqRLQKYAYSVrdsklrdilkdgAAYHhAGMELSDRKVVEGAFTVGDL 286
Cdd:PRK11057 237 KSGIIYCNSRAKVEDTAA----------------RLQSRGISA------------AAYH-AGLDNDVRADVQEAFQRDDL 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034556053 287 PVLFTTSTLAMGVNLP-----AHLVVIKSTMHYagglfeeYSETdilqmiGRAGR 336
Cdd:PRK11057 288 QIVVATVAFGMGINKPnvrfvVHFDIPRNIESY-------YQET------GRAGR 329
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
209-336 |
1.29e-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: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556053 209 TLVFCATRKgvqqAASVLVKDAKfimtveqkQRLQKYAYSVrdSKLrdilkdgAAYHhAGMELSDRKVVEGAFTVGDLPV 288
Cdd:cd18797 38 TIVFCRSRK----LAELLLRYLK--------ARLVEEGPLA--SKV-------ASYR-AGYLAEDRREIEAELFNGELLG 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034556053 289 LFTTSTLAMGVNLPAHLVVIKSTmhYAGGLFEeysetdILQMIGRAGR 336
Cdd:cd18797 96 VVATNALELGIDIGGLDAVVLAG--YPGSLAS------LWQQAGRAGR 135
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
288-336 |
2.72e-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: 2.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1034556053 288 VLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGR 336
Cdd:cd18805 73 VLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMRPLSPSEVKQIAGRAGR 121
|
|
| |
