|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1335-1523 |
1.60e-134 |
|
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: 417.93 E-value: 1.60e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1335 HFNPIQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERIEDWKVRIEEKLGKKVV 1414
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1415 ELTGDVTPDMRAIAQADLIVTTPEKWDGVSRSWQNRSYVQKVSILIIDEIHLLGDERGPVLEVIVSRTNFISSHTEKPVR 1494
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*....
gi 764020079 1495 VVGLSTALANARDLADWLNINQMGLFNFR 1523
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
987-1295 |
2.86e-131 |
|
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: 413.91 E-value: 2.86e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 987 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDILAIVSKAEEFEQIKVREEEIEELDTLlNDFCELPAPGGVENNYGKI 1066
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKL-LEKVPIPVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1067 NILLQTYISRGELDSFSLISDSAYVAQNAARIVRALFEIALRKRWPAMTYRLLNLSKVIDKRLWGWVSPLRQFSVLPPSV 1146
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1147 LSKLEEKNLTV--DKMKDMRKDEIGHMLHHVKIGLKVKQCVHQIPSIAMEATIQPITRTVLRVRLNITPDFTWNDQVHGT 1224
Cdd:pfam02889 160 IKKLEKKGVESvrDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764020079 1225 VgEPWWIWVEDPTNDHIYHSEYFIIQKKQVITkePQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIIN 1295
Cdd:pfam02889 240 S-EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
485-682 |
1.93e-126 |
|
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: 395.26 E-value: 1.93e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 485 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHVQH-GVIKKDEFKIVYVAPMKALAAEMTNYFSKRL 563
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 564 EPLGITVKELTGDMQLSKGEILRTQMLVTTPEKWDVVTRKSVGDVALSQLVKLLILDEVHLLHEDRGPVLESIVARTLRQ 643
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 764020079 644 VESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFYFD 682
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
985-1297 |
2.68e-111 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 356.95 E-value: 2.68e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 985 FSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDILAIVSKAEEFEQIKVREEEIEELDTLLNDFCELPAPGGVENNYG 1064
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1065 KINILLQTYISRGELDSFSLISDSAYVAQNAARIVRALFEIALRKRWPAMTYRLLNLSKVIDKRLWGWVSPLRQFSVLPP 1144
Cdd:smart00611 82 KANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1145 SVLSKLEEKN-LTVDKMKDMRKDEIGHMLHH-VKIGLKVKQCVHQIPSIAMEATIQPITRTVLRVRLNITPDFTWNDQVH 1222
Cdd:smart00611 162 EILKRLEKKKvLSLEDLLELEDEERGELLGLlDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEIH 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764020079 1223 GTVgEPWWIWVEDPTNDHIYHSEYFIIQKKQVITKepQLLVFTIPIFEPLPsQYYIRAVSDRWLGAEAVCIINFQ 1297
Cdd:smart00611 242 GKQ-EGWWLVIGDSDGNELLHIERFSLNKKNVSEE--VKLDFTAPATEGNY-QYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
469-1024 |
2.97e-97 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 325.31 E-value: 2.97e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 469 IKDLDE---IGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHvqhgvikkdeFKIVYV 545
Cdd:COG1204 3 VAELPLekvIEFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNG----------GKALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 546 APMKALAAEMTNYFSKRLEPLGITVKELTGDMQLSKGEILRTQMLVTTPEKWDVVTRKSVGdvALSQlVKLLILDEVHLL 625
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRD-VDLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 626 H-EDRGPVLESIVARtLRQVESTqsmIRILGLSATLPNYLDVATFLHVNPyiglfyFDSRFRPVPLgqtFIGIKTTNKVq 704
Cdd:COG1204 150 DdESRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGVL- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 705 qlnHMDEVCYEN-------VLKQIMAGHQVMVFVHARNATVRTAMALREKAKNNGhichfLSPQGSDYGQAEKQVQRSR- 776
Cdd:COG1204 216 ---RFDDGSRRSkdptlalALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRL-----TPEEREELEELAEELLEVSe 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 777 ----NKQLRELFPDGFSIHHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTqiyaaKRGSFVDLGI 852
Cdd:COG1204 288 ethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-----KRGGMVPIPV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 853 LDVMQIFGRAGRPQFDKFGEGIIIT-THDKLSH--YLTLLTQQNPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWIS 927
Cdd:COG1204 363 LEFKQMAGRAGRPGYDPYGEAILVAkSSDEADElfERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLE 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 928 YTYLYVRMRANPLvygishkayqmdpglekhrEQLVIEVGRKLDKARMIrfEERTGFFSSTDLGRTASHYYIKYNTIETF 1007
Cdd:COG1204 443 NTFYAYQYDKGDL-------------------EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAEL 501
|
570
....*....|....*..
gi 764020079 1008 NELFDAHKTEGDILAIV 1024
Cdd:COG1204 502 VDGLRKADEEFTDLGLL 518
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1333-1871 |
3.06e-94 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 316.45 E-value: 3.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1333 FTHFNPIQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERIEDWKVRIEEkLGKK 1412
Cdd:COG1204 20 IEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEE-LGIK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1413 VVELTGDVTPDMRAIAQADLIVTTPEKWDGVSRswQNRSYVQKVSILIIDEIHLLGDE-RGPVLEVIVSRtnfiSSHTEK 1491
Cdd:COG1204 97 VGVSTGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDDEsRGPTLEVLLAR----LRRLNP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1492 PVRVVGLSTALANARDLADWLNINqmglfNFRPSVRPVPLE--VHIQG---FPGQHYCPRmarmnKPAFQAIRSHSPA-K 1565
Cdd:COG1204 171 EAQIVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSK-----DPTLALALDLLEEgG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1566 PVLIFVSSRRQTRLTSLDLIAFLATEDDPKQWLKMDErEMNDII--GTVRDSNLKLT--LAFGIGMHHAGLHERDRKTVE 1641
Cdd:COG1204 241 QVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEE-LAEELLevSEETHTNEKLAdcLEKGVAFHHAGLPSELRRLVE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1642 ELFVNCKIQVLIATSTLAWGVNFPAHLVIVKGTEYYDGKtrryvdyPIT--DVLQMMGRAGRPQFDDQGKAVILVHDIK- 1718
Cdd:COG1204 320 DAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGMV-------PIPvlEFKQMAGRAGRPGYDPYGEAILVAKSSDe 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1719 --KDFYKKFLYEPFPVESSLLD--VLADHLNAEIAAGTITSKQDAMDYITWTYFFRRLIMnptyYNLDNVshdtMNKYLS 1794
Cdd:COG1204 393 adELFERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTFYAYQYDK----GDLEEV----VDDALE 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764020079 1795 SLVEKSLfdlecsycieIGEDNRTIEPLTYGRIASYYYlkhptigmfkdqLKPESSVEELLLILTNADEYTDLPVRH 1871
Cdd:COG1204 465 FLLENGF----------IEEDGDRLRATKLGKLVSRLY------------IDPLTAAELVDGLRKADEEFTDLGLLH 519
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
1821-2186 |
4.07e-83 |
|
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: 276.16 E-value: 4.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1821 PLTYGRIASYYYLKHPTIGMFKDQLKPESSVEELLLILTNADEYTDLPVRHNEDQMNSELAKHLPIEVNPHSFDSSHTKT 1900
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1901 HLLLQAHFSHAILPCPDYATDTKTVLDQAIRICQAMLDVTAHHGWLVAALNITNLVQMVVQGRWIHDSSLLtvpnievqh 1980
Cdd:smart00973 81 NLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEDSDSPL--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1981 lylfqkwsqqkrksvhggYQGPIECLPELMAACEGKEDVFASIVDSELQTAHISQAWNFLSRLPILNVSLSIKGCWDDpa 2060
Cdd:smart00973 152 ------------------KQLPHFLIEDVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIE-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 2061 qpQNEVPVPCltadtrDNKRWIKLHADQEYVLQIHLQRtqmgyqgkqdskavaprfPKVKDEGWFLILGEVDKKELIALK 2140
Cdd:smart00973 212 --VEAEVLPI------TRDLTLRVELEITPVFAWDLPR------------------HKGKSESWWLVVGDSDTNELLAIK 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 764020079 2141 RT----GYVRNRNTVSVAFYTPEtPGKCIYTLYLMSDSYLGMDQQYDIYL 2186
Cdd:smart00973 266 RVtlrkKKKSNEVKLDFTVPLSE-PGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1821-2184 |
8.24e-71 |
|
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.
Pssm-ID: 460740 Cd Length: 307 Bit Score: 240.57 E-value: 8.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1821 PLTYGRIASYYYLKHPTIGMFKDQLKPESSVEELLLILTNADEYTDLPVRHNEDQMNSELAKHLPIEVNPhSFDSSHTKT 1900
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKG-DIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1901 HLLLQAHFSHAILPCPDYATDTKTVLDQAIRICQAMLDVTAHHGWLVAALNITNLVQMVVQGRWIHDSSLLTVPNIEVQH 1980
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1981 LYLFQKWsqqkrksvhggyqgPIECLPELMAACEGKEDVFASIVDSELQTAHisqawNFLSRLPILNVSLSIkgcwddpa 2060
Cdd:pfam02889 160 IKKLEKK--------------GVESVRDILELDDAEELGELIRNPKMGKDIA-----QFVNRFPKIEIEAEV-------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 2061 QPQnevpvpcltadTRDnkrwiklhadqeyVLQIHLQrtqmgyqgkqdskaVAPRFPKVKD-----EGWFLILGEVDKKE 2135
Cdd:pfam02889 213 QPI-----------TRS-------------VLRVEVT--------------ITPDFPWDKRvhgksEGFWLVVGDSDGNE 254
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 764020079 2136 LIALKRTGYVR--NRNTVSVAFYTP-ETPGKCIYTLYLMSDSYLGMDQQYDI 2184
Cdd:pfam02889 255 ILHIERFTLTKrtLAGEHKLEFTVPpSDPGPPQLFVRLISDSWLGADQEVPI 306
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1527-1715 |
1.25e-66 |
|
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: 222.04 E-value: 1.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1527 RPVPLEVHIQGFPGQHYCPRMARMNK-----PAFQAIRSHSPAKPVLIFVSSRRQTRLTSLDLIaflateddpkqwlkmd 1601
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1602 eremndiigtvrdsnlkltlafGIGMHHAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFPAHLVIVKGTEYYDGKT 1681
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 764020079 1682 RRYvdYPITDVLQMMGRAGRPQFDDQGKAVILVH 1715
Cdd:cd18795 123 YRE--LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1353-1881 |
6.33e-56 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 209.29 E-value: 6.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFrvfNKYPTS--KAVYIAPLKALVRER---IEDWkvrieEKLGKKVVELTGDVTPDMRAI 1427
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMV---NKLLREggKAVYLVPLKALAEEKyreFKDW-----EKLGLRVAMTTGDYDSTDEWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1428 AQADLIVTTPEKWDGVSRswQNRSYVQKVSILIIDEIHLLGD-ERGPVLEVIVSrtnfissHTEKPVRVVGLSTALANAR 1506
Cdd:PRK00254 113 GKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSyDRGATLEMILT-------HMLGRAQILGLSATVGNAE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1507 DLADWLNINQMglfnfRPSVRPVPLE--VHIQG-----------FPGQHYcprmarmnKPAFQAIRShspAKPVLIFVSS 1573
Cdd:PRK00254 184 ELAEWLNAELV-----VSDWRPVKLRkgVFYQGflfwedgkierFPNSWE--------SLVYDAVKK---GKGALVFVNT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1574 RRQTRLTSLDL---IAFLATeddpkqwlKMDEREMNDIIGTVRD--SNLKLTLAF--GIGMHHAGLHERDRKTVEELFVN 1646
Cdd:PRK00254 248 RRSAEKEALELakkIKRFLT--------KPELRALKELADSLEEnpTNEKLKKALrgGVAFHHAGLGRTERVLIEDAFRE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1647 CKIQVLIATSTLAWGVNFPAHLVIVKGTEYYDGKTrrYVDYPITDVLQMMGRAGRPQFDDQGKAVILVH-DIKKDFYKKF 1725
Cdd:PRK00254 320 GLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFG--WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1726 LY-EPFPVESSLLD--VLADHLNAEIAAGTITSKQDAMDYITWTYFFRRlimnptyynldnvshdtmNKYLSSLVEKS-- 1800
Cdd:PRK00254 398 IFgKPEKLFSMLSNesAFRSQVLALITNFGVSNFKELVNFLERTFYAHQ------------------RKDLYSLEEKAke 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1801 --LFDLECSYcIEIGEDNRtIEPLTYGRIASYYYLKHPTIGMFKDQL-KPESSVEEL--LLILTNADEYTDLPVRHNEDQ 1875
Cdd:PRK00254 460 ivYFLLENEF-IDIDLEDR-FIPLPLGIRTSQLYIDPLTAKKFKDAFpKIEKNPNPLgiFQLIASTPDMTPLNYSRKEME 537
|
....*.
gi 764020079 1876 MNSELA 1881
Cdd:PRK00254 538 DLLDEA 543
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
502-1052 |
3.94e-54 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 203.90 E-value: 3.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 502 ENMLICAPTGAGKTNIAMLTVLHEIRQhvQHGvikkdefKIVYVAPMKALAAEMTNYFsKRLEPLGITVKELTGDMQlSK 581
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKLLR--EGG-------KAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYD-ST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 582 GEIL-RTQMLVTTPEKWDVVTRKSVGDValsQLVKLLILDEVHLL-HEDRGPVLESIVARTLRQVEstqsmirILGLSAT 659
Cdd:PRK00254 109 DEWLgKYDIIIATAEKFDSLLRHGSSWI---KDVKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ-------ILGLSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 660 LPNYLDVATFLHVNPYIglfyfdSRFRPVPL-----GQTFIGIKTTNKVQQLNHMDEVCYENVLKqimaGHQVMVFVHAR 734
Cdd:PRK00254 179 VGNAEELAEWLNAELVV------SDWRPVKLrkgvfYQGFLFWEDGKIERFPNSWESLVYDAVKK----GKGALVFVNTR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 735 NATVRTAMALREKAKNnghicHFLSPQGSDYGQ-AEKQVQRSRNKQLRELFPDGFSIHHAGMLRQDRSLVENLFSNGHIK 813
Cdd:PRK00254 249 RSAEKEALELAKKIKR-----FLTKPELRALKElADSLEENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 814 VLVCTATLAWGVNLPAHAVVIKGTQIYAakRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDK----LSHYL--- 886
Cdd:PRK00254 324 VITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklMERYIfgk 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 887 -----TLLTQQNPIESQFLesladnlnAEIALGTVTNVEEAVKWISYTYlYVRMRANPlvYGISHKAYQMDPGLekhREQ 961
Cdd:PRK00254 402 peklfSMLSNESAFRSQVL--------ALITNFGVSNFKELVNFLERTF-YAHQRKDL--YSLEEKAKEIVYFL---LEN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 962 LVIEvgrkldkarmIRFEERtgfFSSTDLGRTASHYYIKYNTIETFNELFDahKTEGD-----ILAIVSKAEEFEQIKVR 1036
Cdd:PRK00254 468 EFID----------IDLEDR---FIPLPLGIRTSQLYIDPLTAKKFKDAFP--KIEKNpnplgIFQLIASTPDMTPLNYS 532
|
570
....*....|....*.
gi 764020079 1037 EEEIEELDTLLNDFCE 1052
Cdd:PRK00254 533 RKEMEDLLDEAYEMED 548
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
686-878 |
4.36e-52 |
|
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: 180.44 E-value: 4.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 686 RPVPLGQTFIGIKTTNKVQQLNHM----DEVCYENVLKQIMAGHQVMVFVHARNATVRTAMALRekaknnghichflspq 761
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMnkfdSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 762 gsdygqaekqvqrsrnkqlrelfpdGFSIHHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTQIYA 841
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 764020079 842 AKRgsFVDLGILDVMQIFGRAGRPQFDKFGEGIIITT 878
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1337-1508 |
4.47e-33 |
|
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: 126.59 E-value: 4.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1337 NPIQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFN-KYPTSKAVYIAPLKALVRERIEDWKVRIEEKLGKKVVE 1415
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDkLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1416 LTGDVTPDMR-AIAQADLIVTTPEKWDGVsrsWQNRSYVQKVSILIIDEIHLLGDE-RGPVLEVIVSRTNfisshteKPV 1493
Cdd:pfam00270 80 LGGDSRKEQLeKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHRLLDMgFGPDLEEILRRLP-------KKR 149
|
170
....*....|....*.
gi 764020079 1494 RVVGLS-TALANARDL 1508
Cdd:pfam00270 150 QILLLSaTLPRNLEDL 165
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
487-665 |
5.43e-33 |
|
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: 126.20 E-value: 5.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 487 NRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQhvqhgviKKDEFKIVYVAPMKALAAEMTNYFSKRLEPL 566
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK-------LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 567 GITVKELTGDMQLSK--GEILRTQMLVTTPEKWDVVTRKSvgdVALSQlVKLLILDEVHLLHE-DRGPVLESIVARtlrq 643
Cdd:pfam00270 73 GLKVASLLGGDSRKEqlEKLKGPDILVGTPGRLLDLLQER---KLLKN-LKLLVLDEAHRLLDmGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|..
gi 764020079 644 vesTQSMIRILGLSATLPNYLD 665
Cdd:pfam00270 145 ---LPKKRQILLLSATLPRNLE 163
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1313-1714 |
4.45e-27 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 120.38 E-value: 4.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1313 DLQPLPVTALG-HPEYE--VLYKFTHFNPIQT-QIFHTLYHTDcNVLLGAPTGSGKTVAAELA-IFRVFNKypTSKAVYI 1387
Cdd:COG1202 184 EVDTVPVDDLDlPPELKdlLEGRGEELLPVQSlAVENGLLEGK-DQLVVSATATGKTLIGELAgIKNALEG--KGKMLFL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1388 APLKALVRERIEDWKVRIEEKLgkKVVELTGDV---TPDMRAIAQADLIVTTPEKWDGVSRSwqnRSYVQKVSILIIDEI 1464
Cdd:COG1202 261 VPLVALANQKYEDFKDRYGDGL--DVSIRVGASrirDDGTRFDPNADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1465 HLLGD-ERGPVLEVIVSRTNFISSHTEKpvrvVGLSTALANARDLADWLNinqMGLFNFrpSVRPVPLEVHIQGFPGQHY 1543
Cdd:COG1202 336 HMLEDpERGHRLDGLIARLKYYCPGAQW----IYLSATVGNPEELAKKLG---AKLVEY--EERPVPLERHLTFADGREK 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1544 CPRMARMNKPAFQAIRSHSPAKPVLIFVSSRRQTRltsldliaflateddpkqwlkmderemndiigtvrdsnlKLTLAF 1623
Cdd:COG1202 407 IRIINKLVKREFDTKSSKGYRGQTIIFTNSRRRCH---------------------------------------EIARAL 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1624 GIGM--HHAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFPAHLVIVK----GTEYYDgktrryvdypITDVLQMMG 1697
Cdd:COG1202 448 GYKAapYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDslamGIEWLS----------VQEFHQMLG 517
|
410
....*....|....*..
gi 764020079 1698 RAGRPQFDDQGKAVILV 1714
Cdd:COG1202 518 RAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1331-1530 |
3.36e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 108.35 E-value: 3.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1331 YKFTHFNPIQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERIEDWKVRIEEKLG 1410
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1411 KKVVELTGDVT-PDMRAIA--QADLIVTTPEKWDGVSRswQNRSYVQKVSILIIDEIH-LLGDERGPVLEVIVSRTNfis 1486
Cdd:smart00487 84 KVVGLYGGDSKrEQLRKLEsgKTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 764020079 1487 shteKPVRVVGLS-TALANARDLADWLNINqmgLFNFRPSVRPVP 1530
Cdd:smart00487 159 ----KNVQLLLLSaTPPEEIENLLELFLND---PVFIDVGFTPLE 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
478-689 |
1.90e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.04 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 478 LAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRqhvqhgviKKDEFKIVYVAPMKALAAEMTN 557
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALK--------RGKGGRVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 558 YFSKRLEPLGITVKELTGDMqlSKGEILR------TQMLVTTPEKWDVVTRKsvgDVALSQLVKLLILDEVH-LLHEDRG 630
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGD--SKREQLRklesgkTDILVTTPGRLLDLLEN---DKLSLSNVDLVILDEAHrLLDGGFG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 764020079 631 PVLESIVARTLRqvestqsMIRILGLSATLPNYLDVATFLHVNpyiGLFYFDSRFRPVP 689
Cdd:smart00487 148 DQLEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
497-865 |
1.14e-17 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 89.92 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 497 AYNTNENMLICAPTGAGKTNIAMLTVLheIRQHVQHGViKKDEFKIVYVAPMKALAAEMTNYFSKRLEPLG--ITVKELT 574
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSL--IDLAGPEAP-KEKGLHTLYITPLRALAVDIARNLQAPIEELGlpIRVETRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 575 GDMQLSKGEILRTQM---LVTTPEKWDVVTrkSVGDVA--LSQLvKLLILDEVH-LLHEDRGPVLESIVARtLRQvesTQ 648
Cdd:TIGR04121 101 GDTSSSERARQRKKPpdiLLTTPESLALLL--SYPDAArlFKDL-RCVVVDEWHeLAGSKRGDQLELALAR-LRR---LA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 649 SMIRILGLSATLPNyLDVA--TFLHVNPYIGLFYFDSRFRPVPLgqTFIGIKTTNKVQQLNHMDEVCYENVLKQIMAGHQ 726
Cdd:TIGR04121 174 PGLRRWGLSATIGN-LEEArrVLLGVGGAPAVLVRGKLPKAIEV--ISLLPESEERFPWAGHLGLRALPEVYAEIDQART 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 727 VMVFVHARNatvrtamalrekaknnghichflspqgsdygQAEKQVQrsrnkQLRELFPDGF---SIHHAGMLRQDRSLV 803
Cdd:TIGR04121 251 TLVFTNTRS-------------------------------QAELWFQ-----ALWEANPEFAlpiALHHGSLDREQRRWV 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764020079 804 ENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtQIYAAKrgsfvdlGILDVMQIFGRAG-RP 865
Cdd:TIGR04121 295 EAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSPK-------GVARLLQRAGRSNhRP 347
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
1355-1670 |
1.50e-17 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 89.53 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1355 LLGAPTGSGKTVAAELAIFRVFNKYPTSK-----AVYIAPLKALVRERIEDWKVRIEEkLGKKV-VEL-TGDVTPDMRAI 1427
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKekglhTLYITPLRALAVDIARNLQAPIEE-LGLPIrVETrTGDTSSSERAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1428 AQA---DLIVTTPEkwdgvsrSWQ-------NRSYVQKVSILIIDEIH-LLGDERGPVLEVIVSRTNFISSHtekpVRVV 1496
Cdd:TIGR04121 111 QRKkppDILLTTPE-------SLAlllsypdAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG----LRRW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1497 GLSTALANARDLADWLninqMGLFNFRPSV------RPVPLEV----HIQGFP-GQHycprMARMNKPA-FQAIRSHspa 1564
Cdd:TIGR04121 180 GLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISllpeSEERFPwAGH----LGLRALPEvYAEIDQA--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1565 KPVLIFVSSRRQTRLTSLDLIAFLATEDDPkqwlkmderemndiigtvrdsnlkltlafgIGMHHAGLHERDRKTVEELF 1644
Cdd:TIGR04121 249 RTTLVFTNTRSQAELWFQALWEANPEFALP------------------------------IALHHGSLDREQRRWVEAAM 298
|
330 340
....*....|....*....|....*..
gi 764020079 1645 VNCKIQVLIATSTLAWGVNF-PAHLVI 1670
Cdd:TIGR04121 299 AAGRLRAVVCTSSLDLGVDFgPVDLVI 325
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1623-1702 |
3.04e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 69.93 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1623 FGIGMHHAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFP-AHLVIvkgteYYDgktrryVDYPITDVLQMMGRAGR 1701
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVI-----IYD------LPWSPASYIQRIGRAGR 80
|
.
gi 764020079 1702 P 1702
Cdd:smart00490 81 A 81
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
778-865 |
1.34e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.93 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 778 KQLRELfPDGFSIHHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVVIKGtqiyaakrgsfVDLGILDVM 856
Cdd:smart00490 5 ELLKEL-GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASYI 72
|
....*....
gi 764020079 857 QIFGRAGRP 865
Cdd:smart00490 73 QRIGRAGRA 81
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
501-828 |
3.32e-11 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 68.76 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 501 NENMLICAPTGAGKTNIAMLTVLHEIRQHVQHGVIkKDEFKIVYVAPMKALAAEMtnyfsKR--LEPL-GItvKELTGDM 577
Cdd:PRK13767 47 GKNVLISSPTGSGKTLAAFLAIIDELFRLGREGEL-EDKVYCLYVSPLRALNNDI-----HRnlEEPLtEI--REIAKER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 578 QLSKGEI---LRT---------QM-------LVTTPEKWDVVT-----RKSVGDvalsqlVKLLILDEVHLLHED-RGPV 632
Cdd:PRK13767 119 GEELPEIrvaIRTgdtssyekqKMlkkpphiLITTPESLAILLnspkfREKLRT------VKWVIVDEIHSLAENkRGVH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 633 LesivARTLRQVES--TQSMIRIlGLSATLPNYLDVATFLhvnpyiGLFYFDSRFRPVPLGQT-F---IGIKTTNKVQQL 706
Cdd:PRK13767 193 L----SLSLERLEElaGGEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDCEIVDArFvkpFDIKVISPVDDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 707 NHMD-----EVCYENVLKQIMAGHQVMVFVHARNATVRTAMalrekaknnghichflspqgsdygqaekqvqrsrnkQLR 781
Cdd:PRK13767 262 IHTPaeeisEALYETLHELIKEHRTTLIFTNTRSGAERVLY------------------------------------NLR 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 764020079 782 ELFPDGFSI-----HHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLP 828
Cdd:PRK13767 306 KRFPEEYDEdnigaHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG 357
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1332-1499 |
1.99e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 62.98 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1332 KFTHFNPIQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAI----FRVFNK-------YptskAVYIAPLKAL---VRER 1397
Cdd:PRK13767 29 KFGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREgeledkvY----CLYVSPLRALnndIHRN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1398 IEDWKVRIEEKLGKKVVEL--------TGDVTPDMRaiaQADL------IVTTPEKWDGVSRSWQNRSYVQKVSILIIDE 1463
Cdd:PRK13767 104 LEEPLTEIREIAKERGEELpeirvairTGDTSSYEK---QKMLkkpphiLITTPESLAILLNSPKFREKLRTVKWVIVDE 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 764020079 1464 IH-LLGDERGPVLEVIVSRTNFISSHteKPVRvVGLS 1499
Cdd:PRK13767 181 IHsLAENKRGVHLSLSLERLEELAGG--EFVR-IGLS 214
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1617-1701 |
4.33e-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: 56.06 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1617 LKLTLAFGIGMHHAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFP-AHLVIVkgteyYDgktrryVDYPITDVLQM 1695
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YD------LPWNPASYIQR 101
|
....*.
gi 764020079 1696 MGRAGR 1701
Cdd:pfam00271 102 IGRAGR 107
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
484-818 |
5.28e-09 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 61.25 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 484 KRLNRIQSIVFETAYNTNEN----MLICAPTGAGKTNIAMLTVLHEIRQHvqhgvikkDEFKIVYVAPMKALAAEMTNYF 559
Cdd:COG1203 126 TPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKH--------GGRRIIYALPFTSIINQTYDRL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 560 SKRLEPlgiTVKELTGDMQLSKGEIL-----RTQMLVTTPEKWD---VVT-----------RKSVGDVALSQLV-KLLIL 619
Cdd:COG1203 198 RDLFGE---DVLLHHSLADLDLLEEEeeyesEARWLKLLKELWDapvVVTtidqlfeslfsNRKGQERRLHNLAnSVIIL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 620 DEVHLL-HEDRGPVLesivaRTLRQVESTQSmiRILGLSATLPNYLDVATF----LHVNPYIGLFYFDSRFRpvplgqtf 694
Cdd:COG1203 275 DEVQAYpPYMLALLL-----RLLEWLKNLGG--SVILMTATLPPLLREELLeayeLIPDEPEELPEYFRAFV-------- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 695 igiKTTNKVQQLNHMDEVCYENVLKQIMAGHQVMVFVharnATVRTAMALREKAKNNG---HICHFlspqgsdygqaekq 771
Cdd:COG1203 340 ---RKRVELKEGPLSDEELAELILEALHKGKSVLVIV----NTVKDAQELYEALKEKLpdeEVYLL-------------- 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 764020079 772 vqrsrnkqlrelfpdgfsihHAGMLRQDRSLVEN----LFSNGHIKVLVCT 818
Cdd:COG1203 399 --------------------HSRFCPADRSEIEKeikeRLERGKPCILVST 429
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
772-864 |
5.70e-07 |
|
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: 49.90 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 772 VQRSRNKQLRELFPDGFSIHHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtqIYAAkrgsfvDLG 851
Cdd:pfam00271 25 KKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVI----NYDL------PWN 94
|
90
....*....|...
gi 764020079 852 ILDVMQIFGRAGR 864
Cdd:pfam00271 95 PASYIQRIGRAGR 107
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
271-299 |
1.07e-03 |
|
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 is required for the assembly of a catalytically active spliceosome on a messenger RNA precursor. The domain is found in the N-terminal region and is non-canonically PWI-like. The PWI-like domain is thought to be involved in protein-protein interactions.
Pssm-ID: 436309 Cd Length: 111 Bit Score: 40.67 E-value: 1.07e-03
10 20
....*....|....*....|....*....
gi 764020079 271 ELQNELFELLGPEGFELIEKLLQNRSVIV 299
Cdd:pfam18149 49 ECENQLVELLDYDKFDLVKLLLKNRDKIV 77
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1335-1523 |
1.60e-134 |
|
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: 417.93 E-value: 1.60e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1335 HFNPIQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERIEDWKVRIEEKLGKKVV 1414
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1415 ELTGDVTPDMRAIAQADLIVTTPEKWDGVSRSWQNRSYVQKVSILIIDEIHLLGDERGPVLEVIVSRTNFISSHTEKPVR 1494
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*....
gi 764020079 1495 VVGLSTALANARDLADWLNINQMGLFNFR 1523
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
987-1295 |
2.86e-131 |
|
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: 413.91 E-value: 2.86e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 987 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDILAIVSKAEEFEQIKVREEEIEELDTLlNDFCELPAPGGVENNYGKI 1066
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKL-LEKVPIPVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1067 NILLQTYISRGELDSFSLISDSAYVAQNAARIVRALFEIALRKRWPAMTYRLLNLSKVIDKRLWGWVSPLRQFSVLPPSV 1146
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1147 LSKLEEKNLTV--DKMKDMRKDEIGHMLHHVKIGLKVKQCVHQIPSIAMEATIQPITRTVLRVRLNITPDFTWNDQVHGT 1224
Cdd:pfam02889 160 IKKLEKKGVESvrDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764020079 1225 VgEPWWIWVEDPTNDHIYHSEYFIIQKKQVITkePQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIIN 1295
Cdd:pfam02889 240 S-EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
485-682 |
1.93e-126 |
|
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: 395.26 E-value: 1.93e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 485 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHVQH-GVIKKDEFKIVYVAPMKALAAEMTNYFSKRL 563
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 564 EPLGITVKELTGDMQLSKGEILRTQMLVTTPEKWDVVTRKSVGDVALSQLVKLLILDEVHLLHEDRGPVLESIVARTLRQ 643
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 764020079 644 VESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFYFD 682
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
469-682 |
1.30e-113 |
|
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: 359.38 E-value: 1.30e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 469 IKDLDEIGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHV-QHGVIKKDEFKIVYVAP 547
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRnPDGTINLDAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 548 MKALAAEMTNYFSKRLEPLGITVKELTGDMQLSKGEILRTQMLVTTPEKWDVVTRKSvGDVALSQLVKLLILDEVHLLHE 627
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKS-GDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 764020079 628 DRGPVLESIVARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFYFD 682
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
985-1297 |
2.68e-111 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 356.95 E-value: 2.68e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 985 FSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDILAIVSKAEEFEQIKVREEEIEELDTLLNDFCELPAPGGVENNYG 1064
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1065 KINILLQTYISRGELDSFSLISDSAYVAQNAARIVRALFEIALRKRWPAMTYRLLNLSKVIDKRLWGWVSPLRQFSVLPP 1144
Cdd:smart00611 82 KANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1145 SVLSKLEEKN-LTVDKMKDMRKDEIGHMLHH-VKIGLKVKQCVHQIPSIAMEATIQPITRTVLRVRLNITPDFTWNDQVH 1222
Cdd:smart00611 162 EILKRLEKKKvLSLEDLLELEDEERGELLGLlDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEIH 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764020079 1223 GTVgEPWWIWVEDPTNDHIYHSEYFIIQKKQVITKepQLLVFTIPIFEPLPsQYYIRAVSDRWLGAEAVCIINFQ 1297
Cdd:smart00611 242 GKQ-EGWWLVIGDSDGNELLHIERFSLNKKNVSEE--VKLDFTAPATEGNY-QYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
987-1296 |
5.70e-99 |
|
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: 321.62 E-value: 5.70e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 987 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDILAIVSKAEEFEQIKVREEEIEELDTlLNDFCELPAPGGVENN-YGK 1065
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNE-LNKRVPIPVKEGIIDSpHAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1066 INILLQTYISRGELDSFSLISDSAYVAQNAARIVRALFEIALRKRWPAMTYRLLNLSKVIDKRLW-GWVSPLRQF-SVLP 1143
Cdd:smart00973 80 VNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWeDSDSPLKQLpHFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1144 PSVLSKLEEKNL--TVDKMKDMRKDEIGHMLH-HVKIGLKVKQCVHQIPSIAMEATIQPITRTV-LRVRLNITPDFTWND 1219
Cdd:smart00973 160 EDVYDKLELKDGsrSFELLLDMNAAELGEFLNrLPPNGRLIYELLRRFPKIEVEAEVLPITRDLtLRVELEITPVFAWDL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764020079 1220 QVHGTVGEPWWIWVEDPTNDHIYHSEYFIIQKKQVitKEPQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIINF 1296
Cdd:smart00973 240 PRHKGKSESWWLVVGDSDTNELLAIKRVTLRKKKK--SNEVKLDFTVPLSEPGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
469-1024 |
2.97e-97 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 325.31 E-value: 2.97e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 469 IKDLDE---IGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHvqhgvikkdeFKIVYV 545
Cdd:COG1204 3 VAELPLekvIEFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNG----------GKALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 546 APMKALAAEMTNYFSKRLEPLGITVKELTGDMQLSKGEILRTQMLVTTPEKWDVVTRKSVGdvALSQlVKLLILDEVHLL 625
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRD-VDLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 626 H-EDRGPVLESIVARtLRQVESTqsmIRILGLSATLPNYLDVATFLHVNPyiglfyFDSRFRPVPLgqtFIGIKTTNKVq 704
Cdd:COG1204 150 DdESRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGVL- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 705 qlnHMDEVCYEN-------VLKQIMAGHQVMVFVHARNATVRTAMALREKAKNNGhichfLSPQGSDYGQAEKQVQRSR- 776
Cdd:COG1204 216 ---RFDDGSRRSkdptlalALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRL-----TPEEREELEELAEELLEVSe 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 777 ----NKQLRELFPDGFSIHHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTqiyaaKRGSFVDLGI 852
Cdd:COG1204 288 ethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-----KRGGMVPIPV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 853 LDVMQIFGRAGRPQFDKFGEGIIIT-THDKLSH--YLTLLTQQNPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWIS 927
Cdd:COG1204 363 LEFKQMAGRAGRPGYDPYGEAILVAkSSDEADElfERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLE 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 928 YTYLYVRMRANPLvygishkayqmdpglekhrEQLVIEVGRKLDKARMIrfEERTGFFSSTDLGRTASHYYIKYNTIETF 1007
Cdd:COG1204 443 NTFYAYQYDKGDL-------------------EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAEL 501
|
570
....*....|....*..
gi 764020079 1008 NELFDAHKTEGDILAIV 1024
Cdd:COG1204 502 VDGLRKADEEFTDLGLL 518
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1333-1871 |
3.06e-94 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 316.45 E-value: 3.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1333 FTHFNPIQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERIEDWKVRIEEkLGKK 1412
Cdd:COG1204 20 IEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEE-LGIK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1413 VVELTGDVTPDMRAIAQADLIVTTPEKWDGVSRswQNRSYVQKVSILIIDEIHLLGDE-RGPVLEVIVSRtnfiSSHTEK 1491
Cdd:COG1204 97 VGVSTGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDDEsRGPTLEVLLAR----LRRLNP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1492 PVRVVGLSTALANARDLADWLNINqmglfNFRPSVRPVPLE--VHIQG---FPGQHYCPRmarmnKPAFQAIRSHSPA-K 1565
Cdd:COG1204 171 EAQIVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSK-----DPTLALALDLLEEgG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1566 PVLIFVSSRRQTRLTSLDLIAFLATEDDPKQWLKMDErEMNDII--GTVRDSNLKLT--LAFGIGMHHAGLHERDRKTVE 1641
Cdd:COG1204 241 QVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEE-LAEELLevSEETHTNEKLAdcLEKGVAFHHAGLPSELRRLVE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1642 ELFVNCKIQVLIATSTLAWGVNFPAHLVIVKGTEYYDGKtrryvdyPIT--DVLQMMGRAGRPQFDDQGKAVILVHDIK- 1718
Cdd:COG1204 320 DAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGMV-------PIPvlEFKQMAGRAGRPGYDPYGEAILVAKSSDe 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1719 --KDFYKKFLYEPFPVESSLLD--VLADHLNAEIAAGTITSKQDAMDYITWTYFFRRLIMnptyYNLDNVshdtMNKYLS 1794
Cdd:COG1204 393 adELFERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTFYAYQYDK----GDLEEV----VDDALE 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764020079 1795 SLVEKSLfdlecsycieIGEDNRTIEPLTYGRIASYYYlkhptigmfkdqLKPESSVEELLLILTNADEYTDLPVRH 1871
Cdd:COG1204 465 FLLENGF----------IEEDGDRLRATKLGKLVSRLY------------IDPLTAAELVDGLRKADEEFTDLGLLH 519
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1333-1523 |
3.04e-91 |
|
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: 294.17 E-value: 3.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1333 FTHFNPIQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERIEDWKVRIEEKLGKK 1412
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPLLGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1413 VVELTGDVTPDMRAIAQADLIVTTPEKWDGVSRSWQNRSYVQKVSILIIDEIHLLGDERGPVLEVIVSRTNFISSHTEKP 1492
Cdd:cd18021 81 VVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 764020079 1493 VRVVGLSTALANARDLADWLNINQMGLFNFR 1523
Cdd:cd18021 161 IRIVGLSSSLANARDVGEWLGASKSTIFNFH 191
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
1821-2186 |
4.07e-83 |
|
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: 276.16 E-value: 4.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1821 PLTYGRIASYYYLKHPTIGMFKDQLKPESSVEELLLILTNADEYTDLPVRHNEDQMNSELAKHLPIEVNPHSFDSSHTKT 1900
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1901 HLLLQAHFSHAILPCPDYATDTKTVLDQAIRICQAMLDVTAHHGWLVAALNITNLVQMVVQGRWIHDSSLLtvpnievqh 1980
Cdd:smart00973 81 NLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEDSDSPL--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1981 lylfqkwsqqkrksvhggYQGPIECLPELMAACEGKEDVFASIVDSELQTAHISQAWNFLSRLPILNVSLSIKGCWDDpa 2060
Cdd:smart00973 152 ------------------KQLPHFLIEDVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIE-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 2061 qpQNEVPVPCltadtrDNKRWIKLHADQEYVLQIHLQRtqmgyqgkqdskavaprfPKVKDEGWFLILGEVDKKELIALK 2140
Cdd:smart00973 212 --VEAEVLPI------TRDLTLRVELEITPVFAWDLPR------------------HKGKSESWWLVVGDSDTNELLAIK 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 764020079 2141 RT----GYVRNRNTVSVAFYTPEtPGKCIYTLYLMSDSYLGMDQQYDIYL 2186
Cdd:smart00973 266 RVtlrkKKKSNEVKLDFTVPLSE-PGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1818-2184 |
1.23e-79 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 266.05 E-value: 1.23e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1818 TIEPLTYGRIASYYYLKHPTIGMFKDQLKPESSVEELLLILTNADEYTDLPVRHNEDQMNSELAKHLPIEVNPHSFDSSH 1897
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1898 TKTHLLLQAHFSHAILPCPDYATDTKTVLDQAIRICQAMLDVTAHHGWLVAALNITNLVQMVVQGRWIHDSSLLTVPNIE 1977
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1978 VQHLYLFQKWSQQKrksvhggyqgpIECLPELMAacEGKEDVFasivdsELQTAHISQAWNFLSRLPILNVSLSIKGCwd 2057
Cdd:smart00611 161 EEILKRLEKKKVLS-----------LEDLLELED--EERGELL------GLLDAEGERVYKVLSRLPKLNIEISLEPI-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 2058 dpaqpqnevpvpcltadTRDN-KRWIKLHADQEYVLQIHlqrtqmgyqGKQdskavaprfpkvkdEGWFLILGEVDKKEL 2136
Cdd:smart00611 220 -----------------TRTVlGVEVTLTVDLTWDDEIH---------GKQ--------------EGWWLVIGDSDGNEL 259
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 764020079 2137 IALKRTGYVRNRN--TVSVAFYTPETPGKCIYTLYLMSDSYLGMDQQYDI 2184
Cdd:smart00611 260 LHIERFSLNKKNVseEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPL 309
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1821-2184 |
8.24e-71 |
|
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.
Pssm-ID: 460740 Cd Length: 307 Bit Score: 240.57 E-value: 8.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1821 PLTYGRIASYYYLKHPTIGMFKDQLKPESSVEELLLILTNADEYTDLPVRHNEDQMNSELAKHLPIEVNPhSFDSSHTKT 1900
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKG-DIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1901 HLLLQAHFSHAILPCPDYATDTKTVLDQAIRICQAMLDVTAHHGWLVAALNITNLVQMVVQGRWIHDSSLLTVPNIEVQH 1980
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1981 LYLFQKWsqqkrksvhggyqgPIECLPELMAACEGKEDVFASIVDSELQTAHisqawNFLSRLPILNVSLSIkgcwddpa 2060
Cdd:pfam02889 160 IKKLEKK--------------GVESVRDILELDDAEELGELIRNPKMGKDIA-----QFVNRFPKIEIEAEV-------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 2061 QPQnevpvpcltadTRDnkrwiklhadqeyVLQIHLQrtqmgyqgkqdskaVAPRFPKVKD-----EGWFLILGEVDKKE 2135
Cdd:pfam02889 213 QPI-----------TRS-------------VLRVEVT--------------ITPDFPWDKRvhgksEGFWLVVGDSDGNE 254
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 764020079 2136 LIALKRTGYVR--NRNTVSVAFYTP-ETPGKCIYTLYLMSDSYLGMDQQYDI 2184
Cdd:pfam02889 255 ILHIERFTLTKrtLAGEHKLEFTVPpSDPGPPQLFVRLISDSWLGADQEVPI 306
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1527-1715 |
1.25e-66 |
|
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: 222.04 E-value: 1.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1527 RPVPLEVHIQGFPGQHYCPRMARMNK-----PAFQAIRSHSPAKPVLIFVSSRRQTRLTSLDLIaflateddpkqwlkmd 1601
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1602 eremndiigtvrdsnlkltlafGIGMHHAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFPAHLVIVKGTEYYDGKT 1681
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 764020079 1682 RRYvdYPITDVLQMMGRAGRPQFDDQGKAVILVH 1715
Cdd:cd18795 123 YRE--LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
1335-1523 |
1.65e-66 |
|
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: 222.91 E-value: 1.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1335 HFNPIQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERIEDWKVRIEEkLGKKVV 1414
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSG-GKAVYIAPTRALVNQKEADLRERFGP-LGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1415 ELTGDVTPDMRAIAQADLIVTTPEKWDGVSRSWQNRsYVQKVSILIIDEIHLLGDE-RGPVLEVIVSRTNFIsshtEKPV 1493
Cdd:cd17921 79 LLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDGeRGVVLELLLSRLLRI----NKNA 153
|
170 180 190
....*....|....*....|....*....|
gi 764020079 1494 RVVGLSTALANARDLADWLNInqMGLFNFR 1523
Cdd:cd17921 154 RFVGLSATLPNAEDLAEWLGV--EDLIRFD 181
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
1336-1528 |
1.33e-65 |
|
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: 221.46 E-value: 1.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1336 FNPIQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTS-----KAVYIAPLKALVRERIEDWKVRIeEKLG 1410
Cdd:cd18023 2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLpwgnrKVVYIAPIKALCSEKYDDWKEKF-GPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1411 KKVVELTGD-VTPDMRAIAQADLIVTTPEKWDGVSRSW-QNRSYVQKVSILIIDEIHLLGDERGPVLEVIVSRTNFISSH 1488
Cdd:cd18023 81 LSCAELTGDtEMDDTFEIQDADIILTTPEKWDSMTRRWrDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSSS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 764020079 1489 TEK------PVRVVGLSTALANARDLADWLNINQMGLFNFRPSVRP 1528
Cdd:cd18023 161 SELrgstvrPMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
487-687 |
4.14e-57 |
|
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: 197.19 E-value: 4.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 487 NRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHvqhGVIKKDEFKIVYVAPMKALAAEMTNYFSKRLEPL 566
Cdd:cd18023 3 NRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKER---NPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 567 GITVKELTGDMQL-SKGEILRTQMLVTTPEKWDVVTRKSVGDVALSQLVKLLILDEVHLLHEDRGPVLESIVARTLRQVE 645
Cdd:cd18023 80 GLSCAELTGDTEMdDTFEIQDADIILTTPEKWDSMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 764020079 646 STQSM------IRILGLSATLPNYLDVATFLHVNPyIGLFYFDSRFRP 687
Cdd:cd18023 160 SSELRgstvrpMRFVAVSATIPNIEDLAEWLGDNP-AGCFSFGESFRP 206
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
486-682 |
5.50e-57 |
|
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: 195.56 E-value: 5.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 486 LNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHvqhgvikkdEFKIVYVAPMKALAAEMTNYFSKRLEP 565
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS---------GGKAVYIAPTRALVNQKEADLRERFGP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 566 LGITVKELTGDMQLSKGEILRTQMLVTTPEKWDVVTRKSVGDvaLSQLVKLLILDEVHLLH-EDRGPVLESIVARTLRQv 644
Cdd:cd17921 73 LGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER--LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI- 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 764020079 645 estQSMIRILGLSATLPNYLDVATFLHVnpyIGLFYFD 682
Cdd:cd17921 150 ---NKNARFVGLSATLPNAEDLAEWLGV---EDLIRFD 181
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1353-1881 |
6.33e-56 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 209.29 E-value: 6.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFrvfNKYPTS--KAVYIAPLKALVRER---IEDWkvrieEKLGKKVVELTGDVTPDMRAI 1427
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMV---NKLLREggKAVYLVPLKALAEEKyreFKDW-----EKLGLRVAMTTGDYDSTDEWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1428 AQADLIVTTPEKWDGVSRswQNRSYVQKVSILIIDEIHLLGD-ERGPVLEVIVSrtnfissHTEKPVRVVGLSTALANAR 1506
Cdd:PRK00254 113 GKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSyDRGATLEMILT-------HMLGRAQILGLSATVGNAE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1507 DLADWLNINQMglfnfRPSVRPVPLE--VHIQG-----------FPGQHYcprmarmnKPAFQAIRShspAKPVLIFVSS 1573
Cdd:PRK00254 184 ELAEWLNAELV-----VSDWRPVKLRkgVFYQGflfwedgkierFPNSWE--------SLVYDAVKK---GKGALVFVNT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1574 RRQTRLTSLDL---IAFLATeddpkqwlKMDEREMNDIIGTVRD--SNLKLTLAF--GIGMHHAGLHERDRKTVEELFVN 1646
Cdd:PRK00254 248 RRSAEKEALELakkIKRFLT--------KPELRALKELADSLEEnpTNEKLKKALrgGVAFHHAGLGRTERVLIEDAFRE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1647 CKIQVLIATSTLAWGVNFPAHLVIVKGTEYYDGKTrrYVDYPITDVLQMMGRAGRPQFDDQGKAVILVH-DIKKDFYKKF 1725
Cdd:PRK00254 320 GLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFG--WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1726 LY-EPFPVESSLLD--VLADHLNAEIAAGTITSKQDAMDYITWTYFFRRlimnptyynldnvshdtmNKYLSSLVEKS-- 1800
Cdd:PRK00254 398 IFgKPEKLFSMLSNesAFRSQVLALITNFGVSNFKELVNFLERTFYAHQ------------------RKDLYSLEEKAke 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1801 --LFDLECSYcIEIGEDNRtIEPLTYGRIASYYYLKHPTIGMFKDQL-KPESSVEEL--LLILTNADEYTDLPVRHNEDQ 1875
Cdd:PRK00254 460 ivYFLLENEF-IDIDLEDR-FIPLPLGIRTSQLYIDPLTAKKFKDAFpKIEKNPNPLgiFQLIASTPDMTPLNYSRKEME 537
|
....*.
gi 764020079 1876 MNSELA 1881
Cdd:PRK00254 538 DLLDEA 543
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1353-1769 |
2.06e-55 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 207.04 E-value: 2.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERIEDWkVRIEEkLGKKVVELTGDV--TPDMraIAQA 1430
Cdd:PRK01172 39 NVIVSVPTAAGKTLIAYSAIYETFLA--GLKSIYIVPLRSLAMEKYEEL-SRLRS-LGMRVKISIGDYddPPDF--IKRY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1431 DLIVTTPEKWDgvSRSWQNRSYVQKVSILIIDEIHLLGDE-RGPVLEVIVSRTNFISSHTekpvRVVGLSTALANARDLA 1509
Cdd:PRK01172 113 DVVILTSEKAD--SLIHHDPYIINDVGLIVADEIHIIGDEdRGPTLETVLSSARYVNPDA----RILALSATVSNANELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1510 DWLNINQMglfnfRPSVRPVPLEVHIQgFPGQHYCPRMARMNKPAFQAIRSH-SPAKPVLIFVSSRRQTRLTSLDLIAFL 1588
Cdd:PRK01172 187 QWLNASLI-----KSNFRPVPLKLGIL-YRKRLILDGYERSQVDINSLIKETvNDGGQVLVFVSSRKNAEDYAEMLIQHF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1589 ATEDDpkqwLKMDEREMNdiigtVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFPAHL 1668
Cdd:PRK01172 261 PEFND----FKVSSENNN-----VYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1669 VIVKG-TEYYDGKTRryvdyPIT--DVLQMMGRAGRPQFDDQGKAVILV-----HDIKKDFYKKflyEPFPVESSLLDVL 1740
Cdd:PRK01172 332 VIVRDiTRYGNGGIR-----YLSnmEIKQMIGRAGRPGYDQYGIGYIYAaspasYDAAKKYLSG---EPEPVISYMGSQR 403
|
410 420 430
....*....|....*....|....*....|.
gi 764020079 1741 ADHLN--AEIAAGTITSKQDAMDYITWTYFF 1769
Cdd:PRK01172 404 KVRFNtlAAISMGLASSMEDLILFYNETLMA 434
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
502-1052 |
3.94e-54 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 203.90 E-value: 3.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 502 ENMLICAPTGAGKTNIAMLTVLHEIRQhvQHGvikkdefKIVYVAPMKALAAEMTNYFsKRLEPLGITVKELTGDMQlSK 581
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKLLR--EGG-------KAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYD-ST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 582 GEIL-RTQMLVTTPEKWDVVTRKSVGDValsQLVKLLILDEVHLL-HEDRGPVLESIVARTLRQVEstqsmirILGLSAT 659
Cdd:PRK00254 109 DEWLgKYDIIIATAEKFDSLLRHGSSWI---KDVKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ-------ILGLSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 660 LPNYLDVATFLHVNPYIglfyfdSRFRPVPL-----GQTFIGIKTTNKVQQLNHMDEVCYENVLKqimaGHQVMVFVHAR 734
Cdd:PRK00254 179 VGNAEELAEWLNAELVV------SDWRPVKLrkgvfYQGFLFWEDGKIERFPNSWESLVYDAVKK----GKGALVFVNTR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 735 NATVRTAMALREKAKNnghicHFLSPQGSDYGQ-AEKQVQRSRNKQLRELFPDGFSIHHAGMLRQDRSLVENLFSNGHIK 813
Cdd:PRK00254 249 RSAEKEALELAKKIKR-----FLTKPELRALKElADSLEENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 814 VLVCTATLAWGVNLPAHAVVIKGTQIYAakRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDK----LSHYL--- 886
Cdd:PRK00254 324 VITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklMERYIfgk 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 887 -----TLLTQQNPIESQFLesladnlnAEIALGTVTNVEEAVKWISYTYlYVRMRANPlvYGISHKAYQMDPGLekhREQ 961
Cdd:PRK00254 402 peklfSMLSNESAFRSQVL--------ALITNFGVSNFKELVNFLERTF-YAHQRKDL--YSLEEKAKEIVYFL---LEN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 962 LVIEvgrkldkarmIRFEERtgfFSSTDLGRTASHYYIKYNTIETFNELFDahKTEGD-----ILAIVSKAEEFEQIKVR 1036
Cdd:PRK00254 468 EFID----------IDLEDR---FIPLPLGIRTSQLYIDPLTAKKFKDAFP--KIEKNpnplgIFQLIASTPDMTPLNYS 532
|
570
....*....|....*.
gi 764020079 1037 EEEIEELDTLLNDFCE 1052
Cdd:PRK00254 533 RKEMEDLLDEAYEMED 548
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
1333-1522 |
2.00e-53 |
|
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: 186.81 E-value: 2.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1333 FTHFNPIQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKY--PTS-------KAVYIAPLKALVRERIEDWKV 1403
Cdd:cd18019 15 FKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHrnPDGtinldafKIVYIAPMKALVQEMVGNFSK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1404 RIEEkLGKKVVELTGDVTPDMRAIAQADLIVTTPEKWDGVSRSWQNRSYVQKVSILIIDEIHLLGDERGPVLEVIVSRTN 1483
Cdd:cd18019 95 RLAP-YGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDDRGPVLESIVARTI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 764020079 1484 FISSHTEKPVRVVGLSTALANARDLADWLNIN-QMGLFNF 1522
Cdd:cd18019 174 RQIEQTQEYVRLVGLSATLPNYEDVATFLRVDpKKGLFYF 213
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
686-878 |
4.36e-52 |
|
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: 180.44 E-value: 4.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 686 RPVPLGQTFIGIKTTNKVQQLNHM----DEVCYENVLKQIMAGHQVMVFVHARNATVRTAMALRekaknnghichflspq 761
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMnkfdSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 762 gsdygqaekqvqrsrnkqlrelfpdGFSIHHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTQIYA 841
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 764020079 842 AKRgsFVDLGILDVMQIFGRAGRPQFDKFGEGIIITT 878
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1353-1871 |
2.48e-51 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 195.56 E-value: 2.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERIEDWKVRieEKLGKKVVELTGDVTPDMRAIAQADL 1432
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAMLKAIAR--GGKALYIVPLRALASEKFEEFERF--EELGVRVGISTGDYDSRDEWLGDNDI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1433 IVTTPEKWDGVSRswqNR-SYVQKVSILIIDEIHLLGDE-RGPVLEVIVS---RTNfisshtekP-VRVVGLSTALANAR 1506
Cdd:PRK02362 117 IVATSEKVDSLLR---NGaPWLDDITCVVVDEVHLIDSAnRGPTLEVTLAklrRLN--------PdLQVVALSATIGNAD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1507 DLADWLNIN-----------QMGLF-----NFRPSVRPVP-----------LEVHIQGfpGQhyCprmarmnkpafqair 1559
Cdd:PRK02362 186 ELADWLDAElvdsewrpidlREGVFyggaiHFDDSQREVEvpskddtlnlvLDTLEEG--GQ--C--------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1560 shspakpvLIFVSSRRQT-----RLTSldliaflATeddpKQWLKMDER-EMNDIIGTVRDS-------NLKLTLAFGIG 1626
Cdd:PRK02362 247 --------LVFVSSRRNAegfakRAAS-------AL----KKTLTAAERaELAELAEEIREVsdtetskDLADCVAKGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1627 MHHAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFPAHLVIVKGTEYYDGktrryvDY-----PITDVLQMMGRAGR 1701
Cdd:PRK02362 308 FHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDG------GAgmqpiPVLEYHQMAGRAGR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1702 PQFDDQGKAVILV--HDIKKDFYKKFLY-EPFPVESSLLD--VLADHLNAEIAAGTITSKQDAMDYITWTYFFRRlimnp 1776
Cdd:PRK02362 382 PGLDPYGEAVLLAksYDELDELFERYIWaDPEDVRSKLATepALRTHVLSTIASGFARTRDGLLEFLEATFYATQ----- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1777 tyynldnvsHDTmNKYLSSLVEKSLFDLECSYCIEigEDNRTIEPLTYGRIASYYYLkhptigmfkDQLkpesSVEELLL 1856
Cdd:PRK02362 457 ---------TDD-TGRLERVVDDVLDFLERNGMIE--EDGETLEATELGHLVSRLYI---------DPL----SAAEIID 511
|
570
....*....|....*
gi 764020079 1857 ILTNADEYTDLPVRH 1871
Cdd:PRK02362 512 GLEAAKKPTDLGLLH 526
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
487-682 |
1.57e-49 |
|
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: 174.87 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 487 NRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHVQhgvikkdeFKIVYVAPMKALAAEMTNYFSKRL-EP 565
Cdd:cd18022 3 NPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPG--------SKVVYIAPLKALVRERVDDWKKRFeEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 566 LGITVKELTGDMQLSKGEILRTQMLVTTPEKWDVV-----TRKSVgdvalsQLVKLLILDEVHLLHEDRGPVLESIVART 640
Cdd:cd18022 75 LGKKVVELTGDVTPDMKALADADIIITTPEKWDGIsrswqTREYV------QQVSLIIIDEIHLLGSDRGPVLEVIVSRM 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 764020079 641 LRQVESTQSMIRILGLSATLPNYLDVATFLHVNPyIGLFYFD 682
Cdd:cd18022 149 NYISSQTEKPVRLVGLSTALANAGDLANWLGIKK-MGLFNFR 189
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1337-1522 |
4.94e-47 |
|
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: 167.99 E-value: 4.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1337 NPIQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTS---------KAVYIAPLKALVRERIEDWKVRIEe 1407
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQggvikkddfKIVYIAPMKALAAEMVEKFSKRLA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1408 KLGKKVVELTGDVTPDMRAIAQADLIVTTPEKWDGVSR-SWQNRSYVQKVSILIIDEIHLLGDERGPVLEVIVSRTNFIS 1486
Cdd:cd18020 82 PLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRkSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQV 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 764020079 1487 SHTEKPVRVVGLSTALANARDLADWLNINQM-GLFNF 1522
Cdd:cd18020 162 ESTQSMIRIVGLSATLPNYLDVADFLRVNPYkGLFFF 198
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1353-1735 |
5.64e-47 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 182.45 E-value: 5.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERIEDWKvrieEKLGK-KVVELTGDVTpdmraI-AQA 1430
Cdd:COG4581 42 SVLVAAPTGSGKTLVAEFAIFLALAR--GRRSFYTAPIKALSNQKFFDLV----ERFGAeNVGLLTGDAS-----VnPDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1431 DLIVTTPEkwdgVSRswqNRSY-----VQKVSILIIDEIHLLGD-ERGPVLEVIVsrtnfIssHTEKPVRVVGLSTALAN 1504
Cdd:COG4581 111 PIVVMTTE----ILR---NMLYregadLEDVGVVVMDEFHYLADpDRGWVWEEPI-----I--HLPARVQLVLLSATVGN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1505 ARDLADWLNinqmglfnfrpSV-----------RPVPLEvhiqgfpgQHYC--PRMARMNKPAFQAIRSHSPAK------ 1565
Cdd:COG4581 177 AEEFAEWLT-----------RVrgetavvvseeRPVPLE--------FHYLvtPRLFPLFRVNPELLRPPSRHEvieeld 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1566 -----PVLIFVSSRRQ-----TRLTSLDLiaflaTEDDPKQWLKMDEREMNDIIGTVRDSNLKLTLAFGIGMHHAGLHER 1635
Cdd:COG4581 238 rggllPAIVFIFSRRGcdeaaQQLLSARL-----TTKEERAEIREAIDEFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1636 DRKTVEELFVNCKIQVLIATSTLAWGVNFPAHLVIVKGTEYYDGKTRRyvdyPIT--DVLQMMGRAGRPQFDDQGKAVIL 1713
Cdd:COG4581 313 YRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHR----PLTarEFHQIAGRAGRRGIDTEGHVVVL 388
|
410 420
....*....|....*....|....*.
gi 764020079 1714 VHDiKKDFyKKFLY----EPFPVESS 1735
Cdd:COG4581 389 APE-HDDP-KKFARlasaRPEPLRSS 412
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
501-1039 |
5.84e-47 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 181.23 E-value: 5.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 501 NENMLICAPTGAGKTNIAMLTVLHEIrqhvqhgvikKDEFKIVYVAPMKALAAEMTNYFSkRLEPLGITVKELTGDMQLS 580
Cdd:PRK01172 37 GENVIVSVPTAAGKTLIAYSAIYETF----------LAGLKSIYIVPLRSLAMEKYEELS-RLRSLGMRVKISIGDYDDP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 581 KGEILRTQMLVTTPEKWDVVTRKsvgDVALSQLVKLLILDEVHLLH-EDRGPVLESiVARTLRQVESTqsmIRILGLSAT 659
Cdd:PRK01172 106 PDFIKRYDVVILTSEKADSLIHH---DPYIINDVGLIVADEIHIIGdEDRGPTLET-VLSSARYVNPD---ARILALSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 660 LPNYLDVATFLHVNPYIglfyfdSRFRPVPLGqtfIGIKTTNKV----QQLNHMDEVcyeNVLKQIMA-GHQVMVFVHAR 734
Cdd:PRK01172 179 VSNANELAQWLNASLIK------SNFRPVPLK---LGILYRKRLildgYERSQVDIN---SLIKETVNdGGQVLVFVSSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 735 NATVRTAMALREkaknnghicHFLSPQGSDYGQAEKQVQrsrNKQLRELFPDGFSIHHAGMLRQDRSLVENLFSNGHIKV 814
Cdd:PRK01172 247 KNAEDYAEMLIQ---------HFPEFNDFKVSSENNNVY---DDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 815 LVCTATLAWGVNLPAHAVVIKGTQIYAAKRGSFvdLGILDVMQIFGRAGRPQFDKFGEGIII----TTHDKLSHYLTllT 890
Cdd:PRK01172 315 IVATPTLAAGVNLPARLVIVRDITRYGNGGIRY--LSNMEIKQMIGRAGRPGYDQYGIGYIYaaspASYDAAKKYLS--G 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 891 QQNPIESQF--LESLADNLNAEIALGTVTNVEEAVKWISYTYLYVRMRANPLVYGISHKayqmdpglekhreqlvievgr 968
Cdd:PRK01172 391 EPEPVISYMgsQRKVRFNTLAAISMGLASSMEDLILFYNETLMAIQNGVDEIDYYIESS--------------------- 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764020079 969 kldkarmIRFEERTGF------FSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDILAIVSKAEEFEQIKVREEE 1039
Cdd:PRK01172 450 -------LKFLKENGFikgdvtLRATRLGKLTSDLYIDPESALILKSAFDHDYDEDLALYYISLCREIIPANTRDDY 519
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
501-999 |
9.82e-47 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 181.69 E-value: 9.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 501 NENMLICAPTGAGKTNIAMLTVLHEIRQHvqhGvikkdefKIVYVAPMKALAAEMTNYFSkRLEPLGITVKELTGDMQlS 580
Cdd:PRK02362 39 GKNLLAAIPTASGKTLIAELAMLKAIARG---G-------KALYIVPLRALASEKFEEFE-RFEELGVRVGISTGDYD-S 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 581 KGEIL-RTQMLVTTPEKWDVVTRKsvGDVALSQLvKLLILDEVHLL-HEDRGPVLESIVARTLRQVESTQsmirILGLSA 658
Cdd:PRK02362 107 RDEWLgDNDIIVATSEKVDSLLRN--GAPWLDDI-TCVVVDEVHLIdSANRGPTLEVTLAKLRRLNPDLQ----VVALSA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 659 TLPNYLDVATFLHVnpyiGLFyfDSRFRPVPL------GQTFIGIKTTNKVQQLNHMDEVCYenVLKQIMAGHQVMVFVH 732
Cdd:PRK02362 180 TIGNADELADWLDA----ELV--DSEWRPIDLregvfyGGAIHFDDSQREVEVPSKDDTLNL--VLDTLEEGGQCLVFVS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 733 ARnatvRTAMALREKAKNNghichfLSPQGSDYGQAE-----KQVQRSRN----KQLRELFPDGFSIHHAGMLRQDRSLV 803
Cdd:PRK02362 252 SR----RNAEGFAKRAASA------LKKTLTAAERAElaelaEEIREVSDtetsKDLADCVAKGAAFHHAGLSREHRELV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 804 ENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTQIYAAKRGSfVDLGILDVMQIFGRAGRPQFDKFGEGIIIT-THDKL 882
Cdd:PRK02362 322 EDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAGM-QPIPVLEYHQMAGRAGRPGLDPYGEAVLLAkSYDEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 883 S----HYltLLTQQNPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWISYTyLYvrmranplvygishkAYQMDPGle 956
Cdd:PRK02362 401 DelfeRY--IWADPEDVRSKLATepALRTHVLSTIASGFARTRDGLLEFLEAT-FY---------------ATQTDDT-- 460
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 764020079 957 KHREQLVIEVGRKLDKARMIrfEERTGFFSSTDLGRTASHYYI 999
Cdd:PRK02362 461 GRLERVVDDVLDFLERNGMI--EEDGETLEATELGHLVSRLYI 501
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
484-674 |
1.24e-41 |
|
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: 152.03 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 484 KRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQhvqhgvikKDEFKIVYVAPMKALAAEMTNYFSKRL 563
Cdd:cd18021 2 KFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQ--------NPKGRAVYIAPMQELVDARYKDWRAKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 564 EP-LGITVKELTGDMQLSKGEILRTQMLVTTPEKWDVV-----TRKSVgdvalsQLVKLLILDEVHLLHEDRGPVLESIV 637
Cdd:cd18021 74 GPlLGKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLsrrwkQRKNV------QSVELFIADELHLIGGENGPVYEVVV 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 764020079 638 ARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNP 674
Cdd:cd18021 148 SRMRYISSQLEKPIRIVGLSSSLANARDVGEWLGASK 184
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
1336-1513 |
7.44e-38 |
|
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: 140.93 E-value: 7.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1336 FNPIQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIfrVFNKYPTSKAVYIAPLKALVRERIEDWKVRieEKLGKKVVE 1415
Cdd:cd18028 2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAM--VNTLLEGGKALYLVPLRALASEKYEEFKKL--EEIGLKVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1416 LTGDVTPDMRAIAQADLIVTTPEKWDGVsrsWQNR-SYVQKVSILIIDEIHLLGD-ERGPVLEVIVSRTNfissHTEKPV 1493
Cdd:cd18028 78 STGDYDEDDEWLGDYDIIVATYEKFDSL---LRHSpSWLRDVGVVVVDEIHLISDeERGPTLESIVARLR----RLNPNT 150
|
170 180
....*....|....*....|
gi 764020079 1494 RVVGLSTALANARDLADWLN 1513
Cdd:cd18028 151 QIIGLSATIGNPDELAEWLN 170
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
497-972 |
8.91e-37 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 150.86 E-value: 8.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 497 AYNTNENMLICAPTGAGKTNIAMltvlHEIRQHVQHGVikkdefKIVYVAPMKALAAEmtNYF--SKRL--EPLGItvke 572
Cdd:COG4581 36 ALEAGRSVLVAAPTGSGKTLVAE----FAIFLALARGR------RSFYTAPIKALSNQ--KFFdlVERFgaENVGL---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 573 LTGDMQLSKG--------EILRTQMLVTTPEKWDVvtrksvgDVAlsqlvkllILDEVHLLHE-DRGPVLE-SIVARTLR 642
Cdd:COG4581 100 LTGDASVNPDapivvmttEILRNMLYREGADLEDV-------GVV--------VMDEFHYLADpDRGWVWEePIIHLPAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 643 qvestqsmIRILGLSATLPNYLDVATFLH--------VnpyiglfyfDSRFRPVPLGQTFIGIKTTNKVQQLNHMDEVCY 714
Cdd:COG4581 165 --------VQLVLLSATVGNAEEFAEWLTrvrgetavV---------VSEERPVPLEFHYLVTPRLFPLFRVNPELLRPP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 715 E--NVLKQIMAGHQ--VMVFVHARNATVRTAMALR--------EKAKNNGHICHFLSPQGSDYGqaekqvqrsrnKQLRE 782
Cdd:COG4581 228 SrhEVIEELDRGGLlpAIVFIFSRRGCDEAAQQLLsarlttkeERAEIREAIDEFAEDFSVLFG-----------KTLSR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 783 LFPDGFSIHHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGtqiyAAKR--GSFVDLGILDVMQIFG 860
Cdd:COG4581 297 LLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTK----LSKFdgERHRPLTAREFHQIAG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 861 RAGRPQFDKFGEGIIITT-HDKLSHYLTLLTQQ-NPIESQFlesladnlnaEIALGTVTNVeeaVKWISYTylyvRMRAn 938
Cdd:COG4581 373 RAGRRGIDTEGHVVVLAPeHDDPKKFARLASARpEPLRSSF----------RPSYNMVLNL---LARPGLE----RARE- 434
|
490 500 510
....*....|....*....|....*....|....
gi 764020079 939 plVYGISHKAYQMDPGLEKHREQlVIEVGRKLDK 972
Cdd:COG4581 435 --LLEDSFAQFQADRSVVGLARR-ARELERALAG 465
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1337-1508 |
4.47e-33 |
|
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: 126.59 E-value: 4.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1337 NPIQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFN-KYPTSKAVYIAPLKALVRERIEDWKVRIEEKLGKKVVE 1415
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDkLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1416 LTGDVTPDMR-AIAQADLIVTTPEKWDGVsrsWQNRSYVQKVSILIIDEIHLLGDE-RGPVLEVIVSRTNfisshteKPV 1493
Cdd:pfam00270 80 LGGDSRKEQLeKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHRLLDMgFGPDLEEILRRLP-------KKR 149
|
170
....*....|....*.
gi 764020079 1494 RVVGLS-TALANARDL 1508
Cdd:pfam00270 150 QILLLSaTLPRNLEDL 165
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
487-665 |
5.43e-33 |
|
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: 126.20 E-value: 5.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 487 NRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQhvqhgviKKDEFKIVYVAPMKALAAEMTNYFSKRLEPL 566
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK-------LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 567 GITVKELTGDMQLSK--GEILRTQMLVTTPEKWDVVTRKSvgdVALSQlVKLLILDEVHLLHE-DRGPVLESIVARtlrq 643
Cdd:pfam00270 73 GLKVASLLGGDSRKEqlEKLKGPDILVGTPGRLLDLLQER---KLLKN-LKLLVLDEAHRLLDmGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|..
gi 764020079 644 vesTQSMIRILGLSATLPNYLD 665
Cdd:pfam00270 145 ---LPKKRQILLLSATLPRNLE 163
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
485-670 |
8.61e-30 |
|
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: 117.82 E-value: 8.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 485 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIrqhVQHGvikkdefKIVYVAPMKALAAEMTNYFSKrLE 564
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTL---LEGG-------KALYLVPLRALASEKYEEFKK-LE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 565 PLGITVKELTGDMQLSKGEILRTQMLVTTPEKWDVVTRKSvgdVALSQLVKLLILDEVHLLH-EDRGPVLESIVARTLRQ 643
Cdd:cd18028 70 EIGLKVGISTGDYDEDDEWLGDYDIIVATYEKFDSLLRHS---PSWLRDVGVVVVDEIHLISdEERGPTLESIVARLRRL 146
|
170 180
....*....|....*....|....*..
gi 764020079 644 VESTQsmirILGLSATLPNYLDVATFL 670
Cdd:cd18028 147 NPNTQ----IIGLSATIGNPDELAEWL 169
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1313-1714 |
4.45e-27 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 120.38 E-value: 4.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1313 DLQPLPVTALG-HPEYE--VLYKFTHFNPIQT-QIFHTLYHTDcNVLLGAPTGSGKTVAAELA-IFRVFNKypTSKAVYI 1387
Cdd:COG1202 184 EVDTVPVDDLDlPPELKdlLEGRGEELLPVQSlAVENGLLEGK-DQLVVSATATGKTLIGELAgIKNALEG--KGKMLFL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1388 APLKALVRERIEDWKVRIEEKLgkKVVELTGDV---TPDMRAIAQADLIVTTPEKWDGVSRSwqnRSYVQKVSILIIDEI 1464
Cdd:COG1202 261 VPLVALANQKYEDFKDRYGDGL--DVSIRVGASrirDDGTRFDPNADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1465 HLLGD-ERGPVLEVIVSRTNFISSHTEKpvrvVGLSTALANARDLADWLNinqMGLFNFrpSVRPVPLEVHIQGFPGQHY 1543
Cdd:COG1202 336 HMLEDpERGHRLDGLIARLKYYCPGAQW----IYLSATVGNPEELAKKLG---AKLVEY--EERPVPLERHLTFADGREK 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1544 CPRMARMNKPAFQAIRSHSPAKPVLIFVSSRRQTRltsldliaflateddpkqwlkmderemndiigtvrdsnlKLTLAF 1623
Cdd:COG1202 407 IRIINKLVKREFDTKSSKGYRGQTIIFTNSRRRCH---------------------------------------EIARAL 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1624 GIGM--HHAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFPAHLVIVK----GTEYYDgktrryvdypITDVLQMMG 1697
Cdd:COG1202 448 GYKAapYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDslamGIEWLS----------VQEFHQMLG 517
|
410
....*....|....*..
gi 764020079 1698 RAGRPQFDDQGKAVILV 1714
Cdd:COG1202 518 RAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1331-1530 |
3.36e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 108.35 E-value: 3.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1331 YKFTHFNPIQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERIEDWKVRIEEKLG 1410
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1411 KKVVELTGDVT-PDMRAIA--QADLIVTTPEKWDGVSRswQNRSYVQKVSILIIDEIH-LLGDERGPVLEVIVSRTNfis 1486
Cdd:smart00487 84 KVVGLYGGDSKrEQLRKLEsgKTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 764020079 1487 shteKPVRVVGLS-TALANARDLADWLNINqmgLFNFRPSVRPVP 1530
Cdd:smart00487 159 ----KNVQLLLLSaTPPEEIENLLELFLND---PVFIDVGFTPLE 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
478-689 |
1.90e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.04 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 478 LAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRqhvqhgviKKDEFKIVYVAPMKALAAEMTN 557
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALK--------RGKGGRVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 558 YFSKRLEPLGITVKELTGDMqlSKGEILR------TQMLVTTPEKWDVVTRKsvgDVALSQLVKLLILDEVH-LLHEDRG 630
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGD--SKREQLRklesgkTDILVTTPGRLLDLLEN---DKLSLSNVDLVILDEAHrLLDGGFG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 764020079 631 PVLESIVARTLRqvestqsMIRILGLSATLPNYLDVATFLHVNpyiGLFYFDSRFRPVP 689
Cdd:smart00487 148 DQLEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1332-1772 |
1.03e-22 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 106.34 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1332 KFTHFNPIQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAIF-RVFNKYPTSKA------VYIAPLKAL---VRERIEDW 1401
Cdd:COG1201 21 RFGAPTPPQREAW-PAIAAGESTLLIAPTGSGKTLAAFLPALdELARRPRPGELpdglrvLYISPLKALandIERNLRAP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1402 KVRIEEKLGKKVVEL-----TGDVTPDMRAiAQA----DLIVTTPE---------KWdgvsrswqnRSYVQKVSILIIDE 1463
Cdd:COG1201 100 LEEIGEAAGLPLPEIrvgvrTGDTPASERQ-RQRrrppHILITTPEslallltspDA---------RELLRGVRTVIVDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1464 IH-LLGDERGPVLEVIVSRtnfISSHTEKPVRVVGLSTALANARDLADWLninqMGLFNFRPS--VRP-----------V 1529
Cdd:COG1201 170 IHaLAGSKRGVHLALSLER---LRALAPRPLQRIGLSATVGPLEEVARFL----VGYEDPRPVtiVDAgagkkpdlevlV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1530 PLEVHIQGFP-----GQHYCPRMArmnkpafQAIRSHspaKPVLIFVSSRRQT-RLTsldliaflateddpkqwlkmdeR 1603
Cdd:COG1201 243 PVEDLIERFPwaghlWPHLYPRVL-------DLIEAH---RTTLVFTNTRSQAeRLF----------------------Q 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1604 EMNDIIGtvrDSNLKltlafgIGMHHAGL-HERdRKTVEELFVNCKIQVLIATSTLAWGVNFPA-HLVI-V---KGteyy 1677
Cdd:COG1201 291 RLNELNP---EDALP------IAAHHGSLsREQ-RLEVEEALKAGELRAVVATSSLELGIDIGDvDLVIqVgspKS---- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1678 dgktrryvdypITDVLQMMGRAGRpQFDDQGKAVILVHD---------IKKDFYKKFLYEPFPVESSlLDVLADHLNAEI 1748
Cdd:COG1201 357 -----------VARLLQRIGRAGH-RVGEVSKGRLVPTHrdelvecaaALEAARAGEIEARRPPRNP-LDVLAQHIVAMA 423
|
490 500
....*....|....*....|....
gi 764020079 1749 AAGTITSkQDAMDYITWTYFFRRL 1772
Cdd:COG1201 424 AGGPFDV-DELYAEVRRAYPYRDL 446
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
1353-1512 |
2.46e-22 |
|
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: 95.73 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKYPTS--KAVYIAPLKALVRerieDWKVRIEEKLGKKVVEL-----TGDVTPDMR 1425
Cdd:cd17922 3 NVLIAAPTGSGKTEAAFLPALSSLADEPEKgvQVLYISPLKALIN----DQERRLEEPLDEIDLEIpvavrHGDTSQSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1426 AIAQA---DLIVTTPEKWDGVSRSWQNRSYVQKVSILIIDEIH-LLGDERGPVLEVIVSRtnfISSHTEKPVRVVGLSTA 1501
Cdd:cd17922 79 AKQLKnppGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHaLLGSKRGVQLELLLER---LRKLTGRPLRRIGLSAT 155
|
170
....*....|.
gi 764020079 1502 LANARDLADWL 1512
Cdd:cd17922 156 LGNLEEAAAFL 166
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
501-670 |
2.85e-21 |
|
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: 92.65 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 501 NENMLICAPTGAGKTNIAMLTVLHEIRQHvqhgviKKDEFKIVYVAPMKALAAEMTnyfsKRLE------PLGITVKELT 574
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADE------PEKGVQVLYISPLKALINDQE----RRLEepldeiDLEIPVAVRH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 575 GDM-QLSKGEILRT--QMLVTTPEKWDVV-TRKsvgdvALSQL---VKLLILDEVH-LLHEDRGPVLESIVARtLRQVES 646
Cdd:cd17922 71 GDTsQSEKAKQLKNppGILITTPESLELLlVNK-----KLRELfagLRYVVVDEIHaLLGSKRGVQLELLLER-LRKLTG 144
|
170 180
....*....|....*....|....
gi 764020079 647 TQsmIRILGLSATLPNYLDVATFL 670
Cdd:cd17922 145 RP--LRRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
501-687 |
4.07e-21 |
|
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: 93.43 E-value: 4.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 501 NENMLICAPTGAGKTNIAMLTVLHEIRQHvqhgviKKdefKIVYVAPMKALAAEMTNYFSKRLEPLGITVKELTGdmqlS 580
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLLER------RK---KALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAG----N 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 581 KGEIL-----RTQMLVTTPEKWDVVTRKSVGDVALSQLvKLLILDEVHLLHE-DRGPVLESIVARTLRqveSTQSMIRIL 654
Cdd:cd18026 100 KGRSPpkrrkSLSVAVCTIEKANSLVNSLIEEGRLDEL-GLVVVDELHMLGDgHRGALLELLLTKLLY---AAQKNIQIV 175
|
170 180 190
....*....|....*....|....*....|...
gi 764020079 655 GLSATLPNYLDVATFLHVnpyiglFYFDSRFRP 687
Cdd:cd18026 176 GMSATLPNLEELASWLRA------ELYTTNFRP 202
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
1351-1524 |
8.27e-21 |
|
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: 92.66 E-value: 8.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1351 DCNVLLGAPTGSGKTVAAELAIFRVF--NKyptSKAVYIAPLKALVRERIeDWKVRIEEKLGKKVVELTGDVTPDMRA-I 1427
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLleRR---KKALFVLPYVSIVQEKV-DALSPLFEELGFRVEGYAGNKGRSPPKrR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1428 AQADLIVTTPEKWDG-VSRSWQNRSyVQKVSILIIDEIHLLGDE-RGPVLEVIVSRtnfISSHTEKPVRVVGLSTALANA 1505
Cdd:cd18026 109 KSLSVAVCTIEKANSlVNSLIEEGR-LDELGLVVVDELHMLGDGhRGALLELLLTK---LLYAAQKNIQIVGMSATLPNL 184
|
170 180
....*....|....*....|.
gi 764020079 1506 RDLADWLNinqMGLF--NFRP 1524
Cdd:cd18026 185 EELASWLR---AELYttNFRP 202
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
502-879 |
1.14e-17 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 89.78 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 502 ENMLICAPTGAGKTNIAMLTVLHE-IRQHVQHGviKKDEFKIVYVAPMKALA-----------AEMTNYFSKRLEPlgIT 569
Cdd:COG1201 40 ESTLLIAPTGSGKTLAAFLPALDElARRPRPGE--LPDGLRVLYISPLKALAndiernlraplEEIGEAAGLPLPE--IR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 570 VKELTGDMqlSKGEilRTQM-------LVTTPE---------KWdvvtRKSVGDvalsqlVKLLILDEVHLLHED-RGPV 632
Cdd:COG1201 116 VGVRTGDT--PASE--RQRQrrrpphiLITTPEslallltspDA----RELLRG------VRTVIVDEIHALAGSkRGVH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 633 LESIVARtLRQVeSTQSMIRIlGLSATLPNYLDVATFLhvnpyIGlfyfDSRFRPV-----PLGQTF-IGI-----KTTN 701
Cdd:COG1201 182 LALSLER-LRAL-APRPLQRI-GLSATVGPLEEVARFL-----VG----YEDPRPVtivdaGAGKKPdLEVlvpveDLIE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 702 KVQQLNHMDEVCYENVLKQIMAGHQVMVFVHARnatvrtamalrekaknnghichflspqgsdyGQAEKQVQRsrnkqLR 781
Cdd:COG1201 250 RFPWAGHLWPHLYPRVLDLIEAHRTTLVFTNTR-------------------------------SQAERLFQR-----LN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 782 ELFPDGFS---IHHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtQIYAAK---RGsfvdlgildv 855
Cdd:COG1201 294 ELNPEDALpiaAHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVI---QVGSPKsvaRL---------- 360
|
410 420
....*....|....*....|....
gi 764020079 856 MQIFGRAGRpQFDKFGEGIIITTH 879
Cdd:COG1201 361 LQRIGRAGH-RVGEVSKGRLVPTH 383
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
497-865 |
1.14e-17 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 89.92 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 497 AYNTNENMLICAPTGAGKTNIAMLTVLheIRQHVQHGViKKDEFKIVYVAPMKALAAEMTNYFSKRLEPLG--ITVKELT 574
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSL--IDLAGPEAP-KEKGLHTLYITPLRALAVDIARNLQAPIEELGlpIRVETRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 575 GDMQLSKGEILRTQM---LVTTPEKWDVVTrkSVGDVA--LSQLvKLLILDEVH-LLHEDRGPVLESIVARtLRQvesTQ 648
Cdd:TIGR04121 101 GDTSSSERARQRKKPpdiLLTTPESLALLL--SYPDAArlFKDL-RCVVVDEWHeLAGSKRGDQLELALAR-LRR---LA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 649 SMIRILGLSATLPNyLDVA--TFLHVNPYIGLFYFDSRFRPVPLgqTFIGIKTTNKVQQLNHMDEVCYENVLKQIMAGHQ 726
Cdd:TIGR04121 174 PGLRRWGLSATIGN-LEEArrVLLGVGGAPAVLVRGKLPKAIEV--ISLLPESEERFPWAGHLGLRALPEVYAEIDQART 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 727 VMVFVHARNatvrtamalrekaknnghichflspqgsdygQAEKQVQrsrnkQLRELFPDGF---SIHHAGMLRQDRSLV 803
Cdd:TIGR04121 251 TLVFTNTRS-------------------------------QAELWFQ-----ALWEANPEFAlpiALHHGSLDREQRRWV 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764020079 804 ENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtQIYAAKrgsfvdlGILDVMQIFGRAG-RP 865
Cdd:TIGR04121 295 EAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSPK-------GVARLLQRAGRSNhRP 347
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
1353-1499 |
1.22e-17 |
|
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: 81.68 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERIEdwKVRIEEKLGKKVVELTGDVTPDMR---AIAQ 1429
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKG-KKVLVLVPTKALALQTAE--RLRELFGPGIRVAVLVGGSSAEEReknKLGD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764020079 1430 ADLIVTTPEKWDGVSRSwQNRSYVQKVSILIIDEIH-LLGDERGPVLEVIVSRTnfissHTEKPVRVVGLS 1499
Cdd:cd00046 80 ADIIIATPDMLLNLLLR-EDRLFLKDLKLIIVDEAHaLLIDSRGALILDLAVRK-----AGLKNAQVILLS 144
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
1355-1670 |
1.50e-17 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 89.53 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1355 LLGAPTGSGKTVAAELAIFRVFNKYPTSK-----AVYIAPLKALVRERIEDWKVRIEEkLGKKV-VEL-TGDVTPDMRAI 1427
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKekglhTLYITPLRALAVDIARNLQAPIEE-LGLPIrVETrTGDTSSSERAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1428 AQA---DLIVTTPEkwdgvsrSWQ-------NRSYVQKVSILIIDEIH-LLGDERGPVLEVIVSRTNFISSHtekpVRVV 1496
Cdd:TIGR04121 111 QRKkppDILLTTPE-------SLAlllsypdAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG----LRRW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1497 GLSTALANARDLADWLninqMGLFNFRPSV------RPVPLEV----HIQGFP-GQHycprMARMNKPA-FQAIRSHspa 1564
Cdd:TIGR04121 180 GLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISllpeSEERFPwAGH----LGLRALPEvYAEIDQA--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1565 KPVLIFVSSRRQTRLTSLDLIAFLATEDDPkqwlkmderemndiigtvrdsnlkltlafgIGMHHAGLHERDRKTVEELF 1644
Cdd:TIGR04121 249 RTTLVFTNTRSQAELWFQALWEANPEFALP------------------------------IALHHGSLDREQRRWVEAAM 298
|
330 340
....*....|....*....|....*..
gi 764020079 1645 VNCKIQVLIATSTLAWGVNF-PAHLVI 1670
Cdd:TIGR04121 299 AAGRLRAVVCTSSLDLGVDFgPVDLVI 325
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
456-886 |
9.00e-17 |
|
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: 86.81 E-value: 9.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 456 EPMPIGIEEKIVYIkdldeigqLAFKGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQHvqhgvi 535
Cdd:COG1205 35 APWPDWLPPELRAA--------LKKRGIERLYSHQAEAIEAARA-GKNVVIATPTASGKSLAYLLPVLEALLED------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 536 kkDEFKIVYVAPMKALAA----EMTNYFSKRlePLGITVKELTGDMQLSKGEILRT--QMLVTTP-----------EKWD 598
Cdd:COG1205 100 --PGATALYLYPTKALARdqlrRLRELAEAL--GLGVRVATYDGDTPPEERRWIREhpDIVLTNPdmlhygllphhTRWA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 599 VVtrksvgdvaLSQLvKLLILDEVHLLhedRGpVLESIVA----RTLRQVESTQSMIRILGLSATLPNYLDVA------- 667
Cdd:COG1205 176 RF---------FRNL-RYVVIDEAHTY---RG-VFGSHVAnvlrRLRRICRHYGSDPQFILASATIGNPAEHAerltgrp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 668 --------------TFLHVNPYIglfYFDSRFRPVPLgqtfigikttnkvqqlnhmdEVCYenVLKQIM-AGHQVMVFVH 732
Cdd:COG1205 242 vtvvdedgsprgerTFVLWNPPL---VDDGIRRSALA--------------------EAAR--LLADLVrEGLRTLVFTR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 733 ARNATVRTAMALREKAKNNGhichflspqgsdygqaekqvqrsrnkqlrelFPDGFSIHHAGMLRQDRSLVENLFSNGHI 812
Cdd:COG1205 297 SRRGAELLARYARRALREPD-------------------------------LADRVAAYRAGYLPEERREIERGLRSGEL 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764020079 813 KVLVCTATLAWGVNLPA-HAVVIKGtqiYAAKRGSFVdlgildvmQIFGRAGRPQFDkfGEGIIITTHDKLSHYL 886
Cdd:COG1205 346 LGVVSTNALELGIDIGGlDAVVLAG---YPGTRASFW--------QQAGRAGRRGQD--SLVVLVAGDDPLDQYY 407
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1353-1744 |
1.01e-16 |
|
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: 86.81 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVR---ERIEDWKVRIEEKLgkKVVELTGDVTPDMR--AI 1427
Cdd:COG1205 73 NVVIATPTASGKSLAYLLPVLEALLEDPGATALYLYPTKALARdqlRRLRELAEALGLGV--RVATYDGDTPPEERrwIR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1428 AQADLIVTTP-----------EKWdgvSRSWQNRSYVqkvsilIIDEIH----------------LLgdeRgpVLEVIVS 1480
Cdd:COG1205 151 EHPDIVLTNPdmlhygllphhTRW---ARFFRNLRYV------VIDEAHtyrgvfgshvanvlrrLR---R--ICRHYGS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1481 RTNFI-SS--------HTEK----PVRVVGLSTALANARDLAdwlninqmgLFN----FRPSVRPVPLEVhiqgfpgqhy 1543
Cdd:COG1205 217 DPQFIlASatignpaeHAERltgrPVTVVDEDGSPRGERTFV---------LWNpplvDDGIRRSALAEA---------- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1544 cPRMARMnkpafqAIRSHSpakPVLIFVSSRRQTRLTSLDLIAFLATEDDPKQwlkmderemndiigtvrdsnlkltlaf 1623
Cdd:COG1205 278 -ARLLAD------LVREGL---RTLVFTRSRRGAELLARYARRALREPDLADR--------------------------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1624 gIGMHHAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFPA-HLVIVKGteyydgktrryvdYP--ITDVLQMMGRAG 1700
Cdd:COG1205 321 -VAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVVLAG-------------YPgtRASFWQQAGRAG 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 764020079 1701 RpqfDDQGKAVILV--HDIKKDFYKK---FLYEPfPVESSLLD-----VLADHL 1744
Cdd:COG1205 387 R---RGQDSLVVLVagDDPLDQYYVRhpeELFER-PPEAAVIDpdnpyVLAPHL 436
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
463-867 |
4.84e-15 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 81.48 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 463 EEKIVYIKDLDEIGQlaFKGM-----KRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIrqhvqhgviKK 537
Cdd:COG1202 184 EVDTVPVDDLDLPPE--LKDLlegrgEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAGIKNA---------LE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 538 DEFKIVYVAPMKALAAEMTNYFSKRLEPlGITVKELTGDMQLSKGE---ILRTQMLVTTPEKWDVVTR--KSVGDVALsq 612
Cdd:COG1202 253 GKGKMLFLVPLVALANQKYEDFKDRYGD-GLDVSIRVGASRIRDDGtrfDPNADIIVGTYEGIDHALRtgRDLGDIGT-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 613 lvklLILDEVHLLHE-DRGPVLESIVARtLRQV-ESTQsmirILGLSATLPNYLDVATFLHVNpyigLFYFDSRfrPVPL 690
Cdd:COG1202 330 ----VVIDEVHMLEDpERGHRLDGLIAR-LKYYcPGAQ----WIYLSATVGNPEELAKKLGAK----LVEYEER--PVPL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 691 GQTFIGIKTTNKVQQLNHMDEVCYENVLKQimaGH--QVMVFVHARNATVRTAMALREKAknnghichflSPqgsdygqa 768
Cdd:COG1202 395 ERHLTFADGREKIRIINKLVKREFDTKSSK---GYrgQTIIFTNSRRRCHEIARALGYKA----------AP-------- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 769 ekqvqrsrnkqlrelfpdgfsiHHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVikgtqiyaakrgsFV 848
Cdd:COG1202 454 ----------------------YHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVI-------------FD 498
|
410 420
....*....|....*....|....*.
gi 764020079 849 DL--GI--LDV---MQIFGRAGRPQF 867
Cdd:COG1202 499 SLamGIewLSVqefHQMLGRAGRPDY 524
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
501-662 |
5.04e-15 |
|
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: 75.48 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 501 NENMLICAPTGAGKTNI---AMLTVLHEirqhvqhgvikKDEFKIVYVAPMKAL----AAEMTNYFSKRLEPLGITV-KE 572
Cdd:cd18025 16 RESALIVAPTSSGKTFIsyyCMEKVLRE-----------SDDGVVVYVAPTKALvnqvVAEVYARFSKKYPPSGKSLwGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 573 LTGDMQLSkgEILRTQMLVTTPEKWDVVTRkSVGDVALSQLVKLLILDEVHLL-HEDRGPVLESIVArtlrqvestqsMI 651
Cdd:cd18025 85 FTRDYRHN--NPMNCQVLITVPECLEILLL-SPHNASWVPRIKYVIFDEIHSIgQSEDGAVWEQLLL-----------LI 150
|
170
....*....|...
gi 764020079 652 R--ILGLSATLPN 662
Cdd:cd18025 151 PcpFLALSATIGN 163
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1623-1702 |
3.04e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 69.93 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1623 FGIGMHHAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFP-AHLVIvkgteYYDgktrryVDYPITDVLQMMGRAGR 1701
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVI-----IYD------LPWSPASYIQRIGRAGR 80
|
.
gi 764020079 1702 P 1702
Cdd:smart00490 81 A 81
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
501-659 |
1.05e-13 |
|
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: 70.51 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 501 NENMLICAPTGAGKTNIAMLTVLHEIRqhvqhgvikKDEFKIVYVAPMKALAAEMTNYFsKRLEPLGITVKELTGDM--- 577
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLL---------KKGKKVLVLVPTKALALQTAERL-RELFGPGIRVAVLVGGSsae 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 578 QLSKGEILRTQMLVTTPEKwdvVTRKSVGDVALSQL-VKLLILDEVH-LLHEDRGPVLESIVARTLRQVEStqsmiRILG 655
Cdd:cd00046 71 EREKNKLGDADIIIATPDM---LLNLLLREDRLFLKdLKLIIVDEAHaLLIDSRGALILDLAVRKAGLKNA-----QVIL 142
|
....
gi 764020079 656 LSAT 659
Cdd:cd00046 143 LSAT 146
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
1331-1512 |
9.97e-13 |
|
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: 69.39 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1331 YKFThFNPIQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERIEDwkvrIEEKLG 1410
Cdd:cd18024 29 YPFT-LDPFQKTAIACIERNE-SVLVSAHTSAGKTVVAEYAIAQSLRD--KQRVIYTSPIKALSNQKYRE----LQEEFG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1411 KkVVELTGDVT--PDmraiaqADLIVTTPEkwdgVSRS--WQNRSYVQKVSILIIDEIHLLGD-ERGPVLEvivsRTNFI 1485
Cdd:cd18024 101 D-VGLMTGDVTinPN------ASCLVMTTE----ILRSmlYRGSEIMREVAWVIFDEIHYMRDkERGVVWE----ETIIL 165
|
170 180
....*....|....*....|....*..
gi 764020079 1486 SSHTekpVRVVGLSTALANARDLADWL 1512
Cdd:cd18024 166 LPDK---VRYVFLSATIPNARQFAEWI 189
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
778-865 |
1.34e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.93 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 778 KQLRELfPDGFSIHHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVVIKGtqiyaakrgsfVDLGILDVM 856
Cdd:smart00490 5 ELLKEL-GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASYI 72
|
....*....
gi 764020079 857 QIFGRAGRP 865
Cdd:smart00490 73 QRIGRAGRA 81
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
501-828 |
3.32e-11 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 68.76 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 501 NENMLICAPTGAGKTNIAMLTVLHEIRQHVQHGVIkKDEFKIVYVAPMKALAAEMtnyfsKR--LEPL-GItvKELTGDM 577
Cdd:PRK13767 47 GKNVLISSPTGSGKTLAAFLAIIDELFRLGREGEL-EDKVYCLYVSPLRALNNDI-----HRnlEEPLtEI--REIAKER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 578 QLSKGEI---LRT---------QM-------LVTTPEKWDVVT-----RKSVGDvalsqlVKLLILDEVHLLHED-RGPV 632
Cdd:PRK13767 119 GEELPEIrvaIRTgdtssyekqKMlkkpphiLITTPESLAILLnspkfREKLRT------VKWVIVDEIHSLAENkRGVH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 633 LesivARTLRQVES--TQSMIRIlGLSATLPNYLDVATFLhvnpyiGLFYFDSRFRPVPLGQT-F---IGIKTTNKVQQL 706
Cdd:PRK13767 193 L----SLSLERLEElaGGEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDCEIVDArFvkpFDIKVISPVDDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 707 NHMD-----EVCYENVLKQIMAGHQVMVFVHARNATVRTAMalrekaknnghichflspqgsdygqaekqvqrsrnkQLR 781
Cdd:PRK13767 262 IHTPaeeisEALYETLHELIKEHRTTLIFTNTRSGAERVLY------------------------------------NLR 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 764020079 782 ELFPDGFSI-----HHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLP 828
Cdd:PRK13767 306 KRFPEEYDEdnigaHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG 357
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
502-659 |
3.55e-11 |
|
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: 64.76 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 502 ENMLICAPTGAGKTNIAMLTVLHEIRQHVQhgvikKDEFKIVYVAPMKALAAEMTNYFSKRLEPLGITVKELTGDMQL-- 579
Cdd:cd17927 18 KNTIICLPTGSGKTFVAVLICEHHLKKFPA-----GRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSEnv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 580 -SKGEILRTQMLVTTPEKWdVVTRKSVGDVALSQlVKLLILDEVHllHEDRGPVLESIVARTLRQ-VESTQSMIRILGLS 657
Cdd:cd17927 93 sVEQIVESSDVIIVTPQIL-VNDLKSGTIVSLSD-FSLLVFDECH--NTTKNHPYNEIMFRYLDQkLGSSGPLPQILGLT 168
|
..
gi 764020079 658 AT 659
Cdd:cd17927 169 AS 170
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
1342-1717 |
6.51e-11 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 67.36 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1342 QIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTskaVYIAPLKALVreriEDWKVRIEEKLGKKvvELTGDVT 1421
Cdd:COG1061 91 ALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV---LVLVPRRELL----EQWAEELRRFLGDP--LAGGGKK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1422 PDmraiaQADLIVTTpekWDGVSRSWQNRSYVQKVSILIIDEIHLLGderGPVLEVIVSRTNfisshtekPVRVVGLS-T 1500
Cdd:COG1061 162 DS-----DAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHAG---APSYRRILEAFP--------AAYRLGLTaT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1501 AlanardladwlninqmglfnFRPSVRPVPLEVhiqgFPGQHYcprmarmNKPAFQAIRSHSPAKPVLIfvssRRQTRLT 1580
Cdd:COG1061 223 P--------------------FRSDGREILLFL----FDGIVY-------EYSLKEAIEDGYLAPPEYY----GIRVDLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1581 SlDLIAFLATEDDPKQWLKMDEREMNDIIGTVRDSNLKL--TLAFGIGMHHA-------------------GLHERDRKT 1639
Cdd:COG1061 268 D-ERAEYDALSERLREALAADAERKDKILRELLREHPDDrkTLVFCSSVDHAealaellneagiraavvtgDTPKKEREE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1640 VEELFVNCKIQVLIATSTLAWGVNFPA--HLVIVKGTeyydgKTRRYvdypitdVLQMMGRAGRPqfdDQGKAVILVHDI 1717
Cdd:COG1061 347 ILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPT-----GSPRE-------FIQRLGRGLRP---APGKEDALVYDF 411
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1337-1512 |
1.74e-10 |
|
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: 62.28 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1337 NPIQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIfrVFNKYPTSKAVYIAPLKALVRERIEDWKVRIEEklgkkVVEL 1416
Cdd:cd18027 10 DVFQKQAILHLEAGD-SVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGD-----VGLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1417 TGDVTPDMRAiaqADLIVTTPekwdgVSRS--WQNRSYVQKVSILIIDEIHLLGD-ERGPVLEVIVSrtnFISSHtekpV 1493
Cdd:cd18027 82 TGDVQLNPEA---SCLIMTTE-----ILRSmlYNGSDVIRDLEWVIFDEVHYINDaERGVVWEEVLI---MLPDH----V 146
|
170
....*....|....*....
gi 764020079 1494 RVVGLSTALANARDLADWL 1512
Cdd:cd18027 147 SIILLSATVPNTVEFADWI 165
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
1353-1509 |
1.81e-10 |
|
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: 62.22 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVR---ERIEDWKVRIEEKLgkKVVELTGDVTPDMR---A 1426
Cdd:cd17923 17 SVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQdqlRSLRELLEQLGLGI--RVATYDGDTPREERraiI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1427 IAQADLIVTTP-----------EKWDGVSRSWQnrsYVqkvsilIIDEIH----LLGDERGPVLEVIVSRTNFISSHtek 1491
Cdd:cd17923 95 RNPPRILLTNPdmlhyallphhDRWARFLRNLR---YV------VLDEAHtyrgVFGSHVALLLRRLRRLCRRYGAD--- 162
|
170
....*....|....*...
gi 764020079 1492 pVRVVGLSTALANARDLA 1509
Cdd:cd17923 163 -PQFILTSATIGNPAEHA 179
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1358-1700 |
2.35e-10 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 66.49 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1358 APTGSGKTVAAEL-AIFRVF----------NKYPTSKAVYIAPLKALVRERIEDWKVRIE------EKLGKKVVEL---- 1416
Cdd:PRK09751 3 APTGSGKTLAAFLyALDRLFreggedtreaHKRKTSRILYISPIKALGTDVQRNLQIPLKgiaderRRRGETEVNLrvgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1417 -TGDVTPDMRA---IAQADLIVTTPEKWDGVSRSwQNRSYVQKVSILIIDEIH-LLGDERGPVLEVIVSRTNFIsSHTek 1491
Cdd:PRK09751 83 rTGDTPAQERSkltRNPPDILITTPESLYLMLTS-RARETLRGVETVIIDEVHaVAGSKRGAHLALSLERLDAL-LHT-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1492 PVRVVGLSTALANARDLADWLNINQMGLFNFRPSVR--------PVPLEVHIQGFPGQHycPRMARMNKPAfqAIRSHS- 1562
Cdd:PRK09751 159 SAQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRhpqirivvPVANMDDVSSVASGT--GEDSHAGREG--SIWPYIe 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1563 --------PAKPVLIFVSSRRQT-----RLTSLDLIAFLATEDDPKqwlkmDEREMNDIIGTV--RDSNLKLTLAFGigm 1627
Cdd:PRK09751 235 tgildevlRHRSTIVFTNSRGLAekltaRLNELYAARLQRSPSIAV-----DAAHFESTSGATsnRVQSSDVFIARS--- 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764020079 1628 HHAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFPA-HLVIvkgteyydgktrrYVDYP--ITDVLQMMGRAG 1700
Cdd:PRK09751 307 HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAvDLVI-------------QVATPlsVASGLQRIGRAG 369
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1354-1513 |
2.72e-10 |
|
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: 62.00 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1354 VLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERIEDWKVRIEEKLGKKVVELTGDVTPDMR--AIAQAD 1431
Cdd:cd18025 19 ALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYPPSGKSLWGVFTRDYRhnNPMNCQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1432 LIVTTPEKWDGVSRSWQNRSYVQKVSILIIDEIHLLG-DERGPVLEVIVsrtnfisshTEKPVRVVGLSTALANARDLAD 1510
Cdd:cd18025 99 VLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGqSEDGAVWEQLL---------LLIPCPFLALSATIGNPQKFHE 169
|
...
gi 764020079 1511 WLN 1513
Cdd:cd18025 170 WLQ 172
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1332-1499 |
1.99e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 62.98 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1332 KFTHFNPIQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAI----FRVFNK-------YptskAVYIAPLKAL---VRER 1397
Cdd:PRK13767 29 KFGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREgeledkvY----CLYVSPLRALnndIHRN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1398 IEDWKVRIEEKLGKKVVEL--------TGDVTPDMRaiaQADL------IVTTPEKWDGVSRSWQNRSYVQKVSILIIDE 1463
Cdd:PRK13767 104 LEEPLTEIREIAKERGEELpeirvairTGDTSSYEK---QKMLkkpphiLITTPESLAILLNSPKFREKLRTVKWVIVDE 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 764020079 1464 IH-LLGDERGPVLEVIVSRTNFISSHteKPVRvVGLS 1499
Cdd:PRK13767 181 IHsLAENKRGVHLSLSLERLEELAGG--EFVR-IGLS 214
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
1353-1479 |
2.64e-09 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 58.84 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVR---ERIEDW--KVRIEEklgkKVVELTGDVTPDM--R 1425
Cdd:cd17930 3 LVILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINqmyERIREIlgRLDDED----KVLLLHSKAALELleS 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764020079 1426 AIAQADLIVTTPEKWDGVSRSW-----------------QNRSYVQKV-----SILIIDEIHLLGDER-GPVLEVIV 1479
Cdd:cd17930 79 DEEPDDDPVEAVDWALLLKRSWlapivvttidqllesllKYKHFERRLhglanSVVVLDEVQAYDPEYmALLLKALL 155
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1617-1701 |
4.33e-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: 56.06 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1617 LKLTLAFGIGMHHAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFP-AHLVIVkgteyYDgktrryVDYPITDVLQM 1695
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YD------LPWNPASYIQR 101
|
....*.
gi 764020079 1696 MGRAGR 1701
Cdd:pfam00271 102 IGRAGR 107
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
484-818 |
5.28e-09 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 61.25 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 484 KRLNRIQSIVFETAYNTNEN----MLICAPTGAGKTNIAMLTVLHEIRQHvqhgvikkDEFKIVYVAPMKALAAEMTNYF 559
Cdd:COG1203 126 TPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKH--------GGRRIIYALPFTSIINQTYDRL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 560 SKRLEPlgiTVKELTGDMQLSKGEIL-----RTQMLVTTPEKWD---VVT-----------RKSVGDVALSQLV-KLLIL 619
Cdd:COG1203 198 RDLFGE---DVLLHHSLADLDLLEEEeeyesEARWLKLLKELWDapvVVTtidqlfeslfsNRKGQERRLHNLAnSVIIL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 620 DEVHLL-HEDRGPVLesivaRTLRQVESTQSmiRILGLSATLPNYLDVATF----LHVNPYIGLFYFDSRFRpvplgqtf 694
Cdd:COG1203 275 DEVQAYpPYMLALLL-----RLLEWLKNLGG--SVILMTATLPPLLREELLeayeLIPDEPEELPEYFRAFV-------- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 695 igiKTTNKVQQLNHMDEVCYENVLKQIMAGHQVMVFVharnATVRTAMALREKAKNNG---HICHFlspqgsdygqaekq 771
Cdd:COG1203 340 ---RKRVELKEGPLSDEELAELILEALHKGKSVLVIV----NTVKDAQELYEALKEKLpdeEVYLL-------------- 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 764020079 772 vqrsrnkqlrelfpdgfsihHAGMLRQDRSLVEN----LFSNGHIKVLVCT 818
Cdd:COG1203 399 --------------------HSRFCPADRSEIEKeikeRLERGKPCILVST 429
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
502-667 |
7.08e-09 |
|
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: 57.59 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 502 ENMLICAPTGAGKTNIAMLTVLHEIRQhvQHGVikkdefKIVYVAPMKALAAEMTNYFSKRLEPL--GITVKELTGDMQL 579
Cdd:cd17923 16 RSVVVTTGTASGKSLCYQLPILEALLR--DPGS------RALYLYPTKALAQDQLRSLRELLEQLglGIRVATYDGDTPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 580 SKGEILRTQ---MLVTTPEKWDV-VTRKSVGDVALSQLVKLLILDEVHLLhedRGpVLESIVA----RTLRQVESTQSMI 651
Cdd:cd17923 88 EERRAIIRNpprILLTNPDMLHYaLLPHHDRWARFLRNLRYVVLDEAHTY---RG-VFGSHVAlllrRLRRLCRRYGADP 163
|
170
....*....|....*.
gi 764020079 652 RILGLSATLPNYLDVA 667
Cdd:cd17923 164 QFILTSATIGNPAEHA 179
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
501-621 |
7.59e-09 |
|
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: 57.60 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 501 NENMLICAPTGAGKTNIAMLTVLHEIRQHVqhgviKKDEFKIVYVAPMKALAAEMTNYFSKRLEPLGITVKELTGDM--Q 578
Cdd:cd17957 27 GRDLLACAPTGSGKTLAFLIPILQKLGKPR-----KKKGLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLeaK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 764020079 579 LSKGEILRTQ--MLVTTPEKwdVVTRKSVGDVALSQlVKLLILDE 621
Cdd:cd17957 102 AKDGPKSITKydILVSTPLR--LVFLLKQGPIDLSS-VEYLVLDE 143
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
1353-1466 |
9.76e-09 |
|
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: 57.44 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKYP---TSKAVYIAPLKALVRERIEDWKvRIEEKLGKKVVELTGDVTPDMRA--- 1426
Cdd:cd17927 19 NTIICLPTGSGKTFVAVLICEHHLKKFPagrKGKVVFLANKVPLVEQQKEVFR-KHFERPGYKVTGLSGDTSENVSVeqi 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 764020079 1427 IAQADLIVTTP-------EKWDGVSRSwqnrsyvqKVSILIIDEIHL 1466
Cdd:cd17927 98 VESSDVIIVTPqilvndlKSGTIVSLS--------DFSLLVFDECHN 136
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
714-864 |
2.13e-08 |
|
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: 55.35 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 714 YENVLKQIMAGHQVMVFVHARNATVRTAMALREKAKNNGHichflspqgsdygqaekqvqrsrnkqlrelfPDGFSIHHA 793
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRVP-------------------------------PDFIALHHG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764020079 794 GMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtQIYAAKrgsfvdlGILDVMQIFGRAGR 864
Cdd:cd18796 77 SLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVI---QIGSPK-------SVARLLQRLGRSGH 137
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1353-1465 |
2.86e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 55.37 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERIEDWKvrieeKLGKKVVELTGDVTPD--MRAIAQA 1430
Cdd:pfam04851 25 RGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFK-----KFLPNYVEIGEIISGDkkDESVDDN 99
|
90 100 110
....*....|....*....|....*....|....*
gi 764020079 1431 DLIVTTPEKWDGVSRSWQNRSYVQKVSILIIDEIH 1465
Cdd:pfam04851 100 KIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
506-863 |
6.46e-08 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 58.40 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 506 ICAPTGAGKTNIAMltvLHEIRQHVQHGVI------KKDEFKIVYVAPMKALAAEMTNYFSKRLEPLG------------ 567
Cdd:PRK09751 1 VIAPTGSGKTLAAF---LYALDRLFREGGEdtreahKRKTSRILYISPIKALGTDVQRNLQIPLKGIAderrrrgetevn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 568 ITVKELTGDMQLS-KGEILRT--QMLVTTPEKWDVV----TRKSVGDvalsqlVKLLILDEVHLLH-EDRGPVLesivAR 639
Cdd:PRK09751 78 LRVGIRTGDTPAQeRSKLTRNppDILITTPESLYLMltsrARETLRG------VETVIIDEVHAVAgSKRGAHL----AL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 640 TLRQVEST--QSMIRIlGLSATLPNYLDVATFLHVNpyiglfyfdsrfRPV----PLGQTFIGIKTTNKVQQLNHMDEVC 713
Cdd:PRK09751 148 SLERLDALlhTSAQRI-GLSATVRSASDVAAFLGGD------------RPVtvvnPPAMRHPQIRIVVPVANMDDVSSVA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 714 YE-------------------NVLKQIMAGHQVMVFVHARNATVRTAMALRE--------KAKNNGHICHFLSPQGSdyg 766
Cdd:PRK09751 215 SGtgedshagregsiwpyietGILDEVLRHRSTIVFTNSRGLAEKLTARLNElyaarlqrSPSIAVDAAHFESTSGA--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 767 qAEKQVQRSRNKQLRElfpdgfsiHHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtQIYAAkrgs 846
Cdd:PRK09751 292 -TSNRVQSSDVFIARS--------HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVI---QVATP---- 355
|
410
....*....|....*..
gi 764020079 847 fvdLGILDVMQIFGRAG 863
Cdd:PRK09751 356 ---LSVASGLQRIGRAG 369
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
1345-1465 |
6.52e-08 |
|
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: 54.64 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1345 HTLYHtdcNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERIEDWKvRIEEKLGKKVVELTGDVTPDM 1424
Cdd:cd18033 13 KALFQ---NTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACY-KITGIPSSQTAELTGSVPPTK 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 764020079 1425 RAI--AQADLIVTTPEKWDGVSRSwqNRSYVQKVSILIIDEIH 1465
Cdd:cd18033 89 RAElwASKRVFFLTPQTLENDLKE--GDCDPKSIVCLVIDEAH 129
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
490-658 |
6.57e-08 |
|
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: 54.97 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 490 QSIVFETAynTNENMLICAPTGAGKTNIAMLTVLHEIRQHVQHGVIKKdefKIVYVAPMKALAAEMTNYFSkrlEPLGIT 569
Cdd:cd18034 7 QLELFEAA--LKRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNPKK---RAVFLVPTVPLVAQQAEAIR---SHTDLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 570 VKELTGDMQLS-------KGEILRTQMLVTTPEKW-DVVTRksvGDVALSQlVKLLILDEVHL---LHEDRGpvlesiVA 638
Cdd:cd18034 79 VGEYSGEMGVDkwtkerwKEELEKYDVLVMTAQILlDALRH---GFLSLSD-INLLIFDECHHatgDHPYAR------IM 148
|
170 180
....*....|....*....|
gi 764020079 639 RTLRQVESTQSMIRILGLSA 658
Cdd:cd18034 149 KEFYHLEGRTSRPRILGLTA 168
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
505-753 |
8.78e-08 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 56.67 E-value: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 505 LICAPTGAGKTNIAMLTVLHEIRQHVqhgvikkdEFKIVYVAPMKALAAEMTNYFSKRL-EPLGITVKELTGD--MQLSK 581
Cdd:cd09639 3 VIEAPTGYGKTEAALLWALHSLKSQK--------ADRVIIALPTRATINAMYRRAKEAFgETGLYHSSILSSRikEMGDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 582 GEILR--------------TQMLVTTPEKWDVVTRKSVGDVALSQL---VKLLILDEVHLLHEDrgpVLESIVA--RTLR 642
Cdd:cd09639 75 EEFEHlfplyihsndtlflDPITVCTIDQVLKSVFGEFGHYEFTLAsiaNSLLIFDEVHFYDEY---TLALILAvlEVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 643 QVEstqsmIRILGLSATLPNYLDvatflHVNPYIGLFYFDSRFRPVPLGQTFIGIKTTNKVQQLNHMDEvcyenVLKQIM 722
Cdd:cd09639 152 DND-----VPILLMSATLPKFLK-----EYAEKIGYVEENEPLDLKPNERAPFIKIESDKVGEISSLER-----LLEFIK 216
|
250 260 270
....*....|....*....|....*....|.
gi 764020079 723 AGHQVMVFVHarnaTVRTAMALREKAKNNGH 753
Cdd:cd09639 217 KGGSVAIIVN----TVDRAQEFYQQLKEKGP 243
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
463-869 |
8.97e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 57.34 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 463 EEKIVYIKDLDEIGQLAFKGMKRLNRIQSIVFETAYNT----NENMLICAPTGAGKTNIAMLTvlheIRQHVQHGvikkd 538
Cdd:COG1061 58 TERELAEAEALEAGDEASGTSFELRPYQQEALEALLAAlergGGRGLVVAPTGTGKTVLALAL----AAELLRGK----- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 539 efKIVYVAPMKAL----AAEMTNYFSKRLEPLGitVKELTGDmqlskgeilrtqMLVTTpekWDVVTRKSVGDvALSQLV 614
Cdd:COG1061 129 --RVLVLVPRRELleqwAEELRRFLGDPLAGGG--KKDSDAP------------ITVAT---YQSLARRAHLD-ELGDRF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 615 KLLILDEVHLLhedrgpvlesiVARTLRQVESTQSMIRILGLSATlPNYLD-----VATFLHVNPYIGL-------FYFD 682
Cdd:COG1061 189 GLVIIDEAHHA-----------GAPSYRRILEAFPAAYRLGLTAT-PFRSDgreilLFLFDGIVYEYSLkeaiedgYLAP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 683 SRFRPVPLGQTFIGIKTTNKVQQLNH--------MDEVCyENVLKQIMAGHQVMVFVharnATVRTAMALREKAKNNGHI 754
Cdd:COG1061 257 PEYYGIRVDLTDERAEYDALSERLREalaadaerKDKIL-RELLREHPDDRKTLVFC----SSVDHAEALAELLNEAGIR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 755 CHFLspqgsdygqaekqvqrsrnkqlrelfpdgfsihHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVi 834
Cdd:COG1061 332 AAVV---------------------------------TGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVA- 377
|
410 420 430
....*....|....*....|....*....|....*
gi 764020079 835 kgtqIYAAKRGSfvdLGILdvMQIFGRAGRPQFDK 869
Cdd:COG1061 378 ----ILLRPTGS---PREF--IQRLGRGLRPAPGK 403
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
501-623 |
1.90e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 56.66 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 501 NENMLICAPTGAGKTNIAMLTVLHeirqhvqhgVIKKDEFKIVYVAPMKALAAEMTNYFSKRLEPLGITVKELTGDMQLS 580
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE---------RLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 764020079 581 KGEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqlvkLLILDEVH 623
Cdd:COG1111 88 KRKELweKARIIVATPQviENDLIAgRIDLDDVS------LLIFDEAH 129
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
452-667 |
2.71e-07 |
|
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: 53.22 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 452 IPHSEPMPIGIEEKiVYIKDLDEIGQLAFKGMKRlnriqsivfetayntNENMLICAPTGAGKTNIAMLTVLHEIRqhvq 531
Cdd:cd18024 14 TPISAHKPPGNPAR-TYPFTLDPFQKTAIACIER---------------NESVLVSAHTSAGKTVVAEYAIAQSLR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 532 hgvikkDEFKIVYVAPMKALAAEMTNYFSKRLEPLGItvkeLTGDMQLSKG--------EILRTqMLVTTPEkwdvVTRK 603
Cdd:cd18024 74 ------DKQRVIYTSPIKALSNQKYRELQEEFGDVGL----MTGDVTINPNasclvmttEILRS-MLYRGSE----IMRE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764020079 604 svgdvalsqlVKLLILDEVHLLHE-DRGPVLE-SIVArtlrqvesTQSMIRILGLSATLPNYLDVA 667
Cdd:cd18024 139 ----------VAWVIFDEIHYMRDkERGVVWEeTIIL--------LPDKVRYVFLSATIPNARQFA 186
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1334-1527 |
4.84e-07 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 55.09 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1334 THFNPIQTQIFHTLYHTDCN----VLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVrERIEDwkvRIEEKL 1409
Cdd:COG1203 126 TPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKHGGRRIIYALPFTSII-NQTYD---RLRDLF 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1410 GKKVVELTGDVTPDMRAIA-----------------QADLIVTTPekwDGVSRS--WQNRSYVQKV-----SILIIDEIH 1465
Cdd:COG1203 202 GEDVLLHHSLADLDLLEEEeeyesearwlkllkelwDAPVVVTTI---DQLFESlfSNRKGQERRLhnlanSVIILDEVQ 278
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764020079 1466 LLGDERGPVLEvivsrtNFISSHTEKPVRVVgLSTA---------LANARDLADWLNINQMGLFNFRPSVR 1527
Cdd:COG1203 279 AYPPYMLALLL------RLLEWLKNLGGSVI-LMTAtlppllreeLLEAYELIPDEPEELPEYFRAFVRKR 342
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
772-864 |
5.70e-07 |
|
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: 49.90 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 772 VQRSRNKQLRELFPDGFSIHHAGMLRQDRSLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtqIYAAkrgsfvDLG 851
Cdd:pfam00271 25 KKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVI----NYDL------PWN 94
|
90
....*....|...
gi 764020079 852 ILDVMQIFGRAGR 864
Cdd:pfam00271 95 PASYIQRIGRAGR 107
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
1353-1465 |
9.98e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 54.11 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERIEDWK--VRIEEklgKKVVELTGDVTPDMRAIA-- 1428
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIAERLHKKG-GKVLILAPTKPLVEQHAEFFRkfLNIPE---EKIVVFTGEVSPEKRAELwe 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 764020079 1429 QADLIVTTPE--KWDGVSrswqNRSYVQKVSILIIDEIH 1465
Cdd:PRK13766 107 KAKVIVATPQviENDLIA----GRISLEDVSLLIFDEAH 141
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
500-660 |
1.02e-06 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350831 [Multi-domain] Cd Length: 202 Bit Score: 51.75 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 500 TNENMLICAPTGAGKTNIAMLTVLHEIRQHVQhgvikKDEFKIVYVAPMKALAAEMTNYFSKRLEPLGITVKELTGDM-- 577
Cdd:cd18073 16 KGKNTIICAPTGCGKTFVSLLICEHHLKKFPQ-----GQKGKVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGATae 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 578 QLSKGEILR-TQMLVTTPEKwdVVTRKSVGDVALSQLVKLLILDEVHllHEDRGPVLESIVARTLRQ--VESTQSMIRIL 654
Cdd:cd18073 91 NVPVEQIIEnNDIIILTPQI--LVNNLKKGTIPSLSIFTLMIFDECH--NTSGNHPYNMIMFRYLDQklGGSSGPLPQII 166
|
....*.
gi 764020079 655 GLSATL 660
Cdd:cd18073 167 GLTASV 172
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
1353-1465 |
1.48e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 53.58 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKyPTSKAVYIAPLKALVRERIEDWKvRIEEKLGKKVVELTGDVTPDMRAI--AQA 1430
Cdd:COG1111 19 NTLVVLPTGLGKTAVALLVIAERLHK-KGGKVLFLAPTKPLVEQHAEFFK-EALNIPEDEIVVFTGEVSPEKRKElwEKA 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 764020079 1431 DLIVTTPE--KWDGVSrswqNRSYVQKVSILIIDEIH 1465
Cdd:COG1111 97 RIIVATPQviENDLIA----GRIDLDDVSLLIFDEAH 129
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
502-661 |
1.49e-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: 50.94 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 502 ENMLICAPTGAGKTNIAMLTVLHEIRQHVQHGvikkDEFKIVYVAPMKALAAEMTNYFSKRLEPlGITVKELTGDMQLSK 581
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAG----EKGRVVVLVNKVPLVEQQLEKFFKYFRK-GYKVTGLSGDSSHKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 582 G---EILRTQMLVTTPE-------KWDVVTRKSVGDVAlsqlvkLLILDEVHllHEDRGPVLESIVARTLRQ-VESTQSM 650
Cdd:cd18036 93 SfgqIVKASDVIICTPQilinnllSGREEERVYLSDFS------LLIFDECH--HTQKEHPYNKIMRMYLDKkLSSQGPL 164
|
170
....*....|.
gi 764020079 651 IRILGLSATLP 661
Cdd:cd18036 165 PQILGLTASPG 175
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
502-665 |
1.68e-06 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 50.75 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 502 ENMLICAPTGAGKTNIAMLTVLHeirQHVQHGVikkdeFKIVYVAPMKALA----AEMTNYFSKRLEPLGIT-------V 570
Cdd:cd17930 2 GLVILEAPTGSGKTEAALLWALK---LAARGGK-----RRIIYALPTRATInqmyERIREILGRLDDEDKVLllhskaaL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 571 KELTGDMQLSKGEILRTQMLVTTPEKWD---VVT----------------RKSVGdvaLSQlvKLLILDEVHLLhedrGP 631
Cdd:cd17930 74 ELLESDEEPDDDPVEAVDWALLLKRSWLapiVVTtidqllesllkykhfeRRLHG---LAN--SVVVLDEVQAY----DP 144
|
170 180 190
....*....|....*....|....*....|....
gi 764020079 632 VLESIVARTLRQVESTQSmIRILGLSATLPNYLD 665
Cdd:cd17930 145 EYMALLLKALLELLGELG-GPVVLMTATLPALLR 177
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
490-659 |
1.82e-06 |
|
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: 50.40 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 490 QSIVFETAYNtneNMLICAPTGAGKTNIAMLTVLHEIRQHVQHgvikkdefKIVYVAPMKALAAEMTNYFSKRLE-PLGI 568
Cdd:cd18033 8 FTIVQKALFQ---NTLVALPTGLGKTFIAAVVMLNYYRWFPKG--------KIVFMAPTKPLVSQQIEACYKITGiPSSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 569 TVkELTGDMQLSK-GEILRT-QMLVTTPEkwdVVTRKSVGDVALSQLVKLLILDEVhllHEDRGPVLESIVARTLRQVES 646
Cdd:cd18033 77 TA-ELTGSVPPTKrAELWASkRVFFLTPQ---TLENDLKEGDCDPKSIVCLVIDEA---HRATGNYAYCQVVRELMRYNS 149
|
170
....*....|...
gi 764020079 647 TqsmIRILGLSAT 659
Cdd:cd18033 150 H---FRILALTAT 159
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
1358-1499 |
1.94e-06 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 49.61 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1358 APTGSGKTVAAELAIFRVFNKyptsKAVYIAPLKALVreriEDWKVRIEEKLGKKVV-ELTGDVTpdmRAIAQADLIVTT 1436
Cdd:cd17926 25 LPTGSGKTLTALALIAYLKEL----RTLIVVPTDALL----DQWKERFEDFLGDSSIgLIGGGKK---KDFDDANVVVAT 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764020079 1437 PEkwdgvSRSWQN---RSYVQKVSILIIDEIHLLGderGPVLEVIVSRTNFIsshtekpvRVVGLS 1499
Cdd:cd17926 94 YQ-----SLSNLAeeeKDLFDQFGLLIVDEAHHLP---AKTFSEILKELNAK--------YRLGLT 143
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
1353-1465 |
2.06e-06 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 50.21 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKYpTSKAVYIAPLKALVRERIEDWKVRIEEKLgkKVVELTGDVTPDMRA--IAQA 1430
Cdd:cd18035 18 NTLIVLPTGLGKTIIAILVAADRLTKK-GGKVLILAPSRPLVEQHAENLKRVLNIPD--KITSLTGEVKPEERAerWDAS 94
|
90 100 110
....*....|....*....|....*....|....*
gi 764020079 1431 DLIVTTPEKWDgvSRSWQNRSYVQKVSILIIDEIH 1465
Cdd:cd18035 95 KIIVATPQVIE--NDLLAGRITLDDVSLLIFDEAH 127
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
502-670 |
2.78e-06 |
|
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: 49.96 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 502 ENMLICAPTGAGKTNIAMLTVlheirqhvqhGVIKKDEFKIVYVAPMKALAAEMTNYFSKRLEPLGItvkeLTGDMQLSK 581
Cdd:cd18027 24 DSVFVAAHTSAGKTVVAEYAI----------ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGL----ITGDVQLNP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 582 G--------EILRTqMLVTTPEkwdvVTRKsvgdvalsqlVKLLILDEVHLLHE-DRGPVLESIVARTLRQVestqsmiR 652
Cdd:cd18027 90 EasclimttEILRS-MLYNGSD----VIRD----------LEWVIFDEVHYINDaERGVVWEEVLIMLPDHV-------S 147
|
170
....*....|....*...
gi 764020079 653 ILGLSATLPNYLDVATFL 670
Cdd:cd18027 148 IILLSATVPNTVEFADWI 165
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
478-674 |
2.99e-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: 50.13 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 478 LAFKGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTnIA-MLTVLHEIRqhvQHGVIKKDEFKIVYVAPMKALA---A 553
Cdd:cd00268 5 LKKLGFEKPTPIQAQAIPLILS-GRDVIGQAQTGSGKT-LAfLLPILEKLL---PEPKKKGRGPQALVLAPTRELAmqiA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 554 EMTNYFSKrlePLGITVKELTGDMQLSKGEIL---RTQMLVTTPEK-WDVVTRksvGDVALSQlVKLLILDEV-HLLHED 628
Cdd:cd00268 80 EVARKLGK---GTGLKVAAIYGGAPIKKQIEAlkkGPDIVVGTPGRlLDLIER---GKLDLSN-VKYLVLDEAdRMLDMG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 764020079 629 RGPVLESIVARTLRQvesTQSMIrilgLSATLPNYLD--VATFLHvNP 674
Cdd:cd00268 153 FEEDVEKILSALPKD---RQTLL----FSATLPEEVKelAKKFLK-NP 192
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
505-753 |
3.31e-06 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 51.69 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 505 LICAPTGAGKTNIAMLTVLHEIRQHVqhgvikkdEFKIVYVAPMKALAAEMTNYFSKRL--EPLGITVKELTGD--MQLS 580
Cdd:TIGR01587 3 VIEAPTGYGKTEAALLWALHSIKSQK--------ADRVIIALPTRATINAMYRRAKELFgsELVGLHHSSSFSRikEMGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 581 KGEILR--------------TQMLVTTPEKWDVVTRKSVGDVALSQL---VKLLILDEVHLLHEDrgpVLESIVA--RTL 641
Cdd:TIGR01587 75 SEEFEHlfplyihsndklflDPITVCTIDQVLKSVFGEFGHYEFTLAsiaNSLLIFDEVHFYDEY---TLALILAvlEVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 642 RQVEstqsmIRILGLSATLPNYLDvATFLHVNPYIGLFYFDSRFRPVPLGQTFIGI--KTTNKVQQLNHMdevcyenvLK 719
Cdd:TIGR01587 152 KDND-----VPILLMSATLPKFLK-EYAEKIGYVEFNEPLDLKEERRFENHRFILIesDKVGEISSLERL--------LE 217
|
250 260 270
....*....|....*....|....*....|....
gi 764020079 720 QIMAGHQVMVFVHarnaTVRTAMALREKAKNNGH 753
Cdd:TIGR01587 218 FIKKGGSIAIIVN----TVDRAQEFYQQLKEKAP 247
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
503-623 |
4.36e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 52.18 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 503 NMLICAPTGAGKTNIAMLtvlheirqhVQHGVIKKDEFKIVYVAPMKALAAEMTNYFSK--RLEPLGITVkeLTGDMQLS 580
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALL---------VIAERLHKKGGKVLILAPTKPLVEQHAEFFRKflNIPEEKIVV--FTGEVSPE 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 764020079 581 KGEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqlvkLLILDEVH 623
Cdd:PRK13766 100 KRAELweKAKVIVATPQviENDLIAgRISLEDVS------LLIFDEAH 141
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
1353-1505 |
8.11e-06 |
|
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: 48.80 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRV-----FNKYPTSKAVYIAPLKALVRERIEdwkvRIEEKLGKKVVELTGDVTPDM--- 1424
Cdd:cd18034 18 NTIVVLPTGSGKTLIAVMLIKEMgelnrKEKNPKKRAVFLVPTVPLVAQQAE----AIRSHTDLKVGEYSGEMGVDKwtk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1425 ----RAIAQADLIVTTPEkwdgVSRSWQNRSYVQ--KVSILIIDEIHLLGDERgpVLEVIVSRTNFISSHTEKPvRVVGL 1498
Cdd:cd18034 94 erwkEELEKYDVLVMTAQ----ILLDALRHGFLSlsDINLLIFDECHHATGDH--PYARIMKEFYHLEGRTSRP-RILGL 166
|
....*..
gi 764020079 1499 STALANA 1505
Cdd:cd18034 167 TASPVNG 173
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
481-672 |
8.21e-06 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 49.29 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 481 KGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQHVQHGVIKKDEFKIVYVAPMKALAAEMTNYFS 560
Cdd:cd17948 8 QGITKPTTVQKQGIPSILR-GRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNAPRGLVITPSRELAEQIGSVAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 561 KRLEPLGITVKELTGDMqlSKGEILRTQM-----LVTTPEK-WDVVTRksvGDVALSQlVKLLILDEVH-LLHEDRGPVL 633
Cdd:cd17948 87 SLTEGLGLKVKVITGGR--TKRQIRNPHFeevdiLVATPGAlSKLLTS---RIYSLEQ-LRHLVLDEADtLLDDSFNEKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 764020079 634 ESIVART---LRQVESTQSMIR---ILGLSATLPNYL--------DVATFLHV 672
Cdd:cd17948 161 SHFLRRFplaSRRSENTDGLDPgtqLVLVSATMPSGVgevlskviDVDSIETV 213
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
501-623 |
3.78e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 46.35 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 501 NENMLICAPTGAGKTNIAMLtvlheirqhVQHGVIKKDEFKIVYVAPMKALAAEMTNYFsKRLEPLGITVKELTGDMQLS 580
Cdd:cd18035 16 NGNTLIVLPTGLGKTIIAIL---------VAADRLTKKGGKVLILAPSRPLVEQHAENL-KRVLNIPDKITSLTGEVKPE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 764020079 581 KGEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqlvkLLILDEVH 623
Cdd:cd18035 86 ERAERwdASKIIVATPQviENDLLAgRITLDDVS------LLIFDEAH 127
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
495-660 |
1.69e-04 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to 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: 438711 [Multi-domain] Cd Length: 174 Bit Score: 44.63 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 495 ETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHVQhgvikkdefKIVYVAP----MKALAAEMTnyfSKRLEPLGITV 570
Cdd:cd17990 11 RAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGG---------KIIVLEPrrvaARAAARRLA---TLLGEAPGETV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 571 K-ELTGDMQLSKgeilRTQMLVTTPekwDVVTRKSVGDVALSQlVKLLILDEVHllheDRGPVLESIVARTLRQVESTQS 649
Cdd:cd17990 79 GyRVRGESRVGR----RTRVEVVTE---GVLLRRLQRDPELSG-VGAVILDEFH----ERSLDADLALALLLEVQQLLRD 146
|
170
....*....|.
gi 764020079 650 MIRILGLSATL 660
Cdd:cd17990 147 DLRLLAMSATL 157
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
1334-1490 |
4.37e-04 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 44.28 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1334 THFNPIQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFR--------VFNKYPTSKAVYIAPLKALVrERIEDWKVRI 1405
Cdd:cd17948 11 TKPTTVQKQGIPSILRGR-NTLCAAETGSGKTLTYLLPIIQrllrykllAEGPFNAPRGLVITPSRELA-EQIGSVAQSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1406 EEKLGKKVVELTGDVTP-DMRAIA--QADLIVTTPekwDGVSRSWQNRSY-VQKVSILIIDEIH-LLGDERGPVLEVIVS 1480
Cdd:cd17948 89 TEGLGLKVKVITGGRTKrQIRNPHfeEVDILVATP---GALSKLLTSRIYsLEQLRHLVLDEADtLLDDSFNEKLSHFLR 165
|
170
....*....|
gi 764020079 1481 RTNFISSHTE 1490
Cdd:cd17948 166 RFPLASRRSE 175
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
1629-1701 |
5.26e-04 |
|
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: 42.20 E-value: 5.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764020079 1629 HAGLHERDRKTVEELFVNCKIQVLIATSTLAWGVNFP-----AHLVIVKGTE-YYdgktrryvdypitdvlQMMGRAGR 1701
Cdd:cd18794 61 HAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPdvrfvIHYSLPKSMEsYY----------------QESGRAGR 123
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
490-624 |
9.02e-04 |
|
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D
Pssm-ID: 187841 [Multi-domain] Cd Length: 353 Bit Score: 44.09 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 490 QSIVFETAYNTNEN-MLICAPTGAGKTNIAMLTVLHEirqhvqhgvikkdEFKIVYVAPMKALA-------AEMTNYFSK 561
Cdd:cd09710 2 QVATFEALQSKDADiIFNTAPTGAGKTLAWLTPLLHG-------------ENKAIALYPTNALIedqteaiKEFVDDANP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 562 RLEPLGITVKELT-----GDMQLSKGEIL-----------RTQMLVTTPEKWDVVTR-----KSVGDVALSQLVKLLILD 620
Cdd:cd09710 69 RHQVKSLSASDITlwpndKNVGSSKGEKLynllrndigtsTPIILLTNPDIFVYLTRfayidRGDIAAGFYTKFSTVIFD 148
|
....
gi 764020079 621 EVHL 624
Cdd:cd09710 149 EFHL 152
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
271-299 |
1.07e-03 |
|
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 is required for the assembly of a catalytically active spliceosome on a messenger RNA precursor. The domain is found in the N-terminal region and is non-canonically PWI-like. The PWI-like domain is thought to be involved in protein-protein interactions.
Pssm-ID: 436309 Cd Length: 111 Bit Score: 40.67 E-value: 1.07e-03
10 20
....*....|....*....|....*....
gi 764020079 271 ELQNELFELLGPEGFELIEKLLQNRSVIV 299
Cdd:pfam18149 49 ECENQLVELLDYDKFDLVKLLLKNRDKIV 77
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
1558-1701 |
1.19e-03 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 41.48 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1558 IRSHSPAKPVLIFVSSRRQT-RLTSLdliaflateddpkqwLKM--DEREMNDIIGTvrdsnlkltlafgigmHHAGLHE 1634
Cdd:cd18796 32 IFLLERHKSTLVFTNTRSQAeRLAQR---------------LRElcPDRVPPDFIAL----------------HHGSLSR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 764020079 1635 RDRKTVEELFVNCKIQVLIATSTLAWGVNFPA-HLVIVKGTEyydgktrryvdYPITDVLQMMGRAGR 1701
Cdd:cd18796 81 ELREEVEAALKRGDLKVVVATSSLELGIDIGDvDLVIQIGSP-----------KSVARLLQRLGRSGH 137
|
|
| cas3_cyano |
TIGR03158 |
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short ... |
490-624 |
1.29e-03 |
|
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. It contains helicase motifs and appears to represent the Cas3 protein of the Cyano subtype of CRISPR/Cas system.
Pssm-ID: 274457 [Multi-domain] Cd Length: 357 Bit Score: 43.35 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 490 QSIVFETAYNTNEN-MLICAPTGAGKTNIAMLTVLHEirqhvqhgvikkdEFKIVYVAPMKALAAEMTNYFSKRLEPL-- 566
Cdd:TIGR03158 2 QVATFEALQSKDADiIFNTAPTGAGKTLAWLTPLLHG-------------ENDTIALYPTNALIEDQTEAIKEFVDVFkp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 567 ----------GITVKEL----TGDMQLSKGEIL-----------RTQMLVTTPEKWDVVTR-----KSVGDVALSQLVKL 616
Cdd:TIGR03158 69 erdvnllhvsKATLKDIkeyaNDKVGSSKGEKLynllrnpigtsTPIILLTNPDIFVYLTRfayidRGDIAAGFYTKFST 148
|
....*...
gi 764020079 617 LILDEVHL 624
Cdd:TIGR03158 149 VIFDEFHL 156
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
499-659 |
1.57e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 41.50 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 499 NTNENMLICAPTGAGKTNIAMLTVLHEIRQHvqhgvikkDEFKIVYVAPMKALAAEMTNYFSKRLEPLGITVKELTGDMQ 578
Cdd:pfam04851 21 NGQKRGLIVMATGSGKTLTAAKLIARLFKKG--------PIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 579 LSKGEilRTQMLVTTPEKWDvVTRKSVGDVALSQLVKLLILDEVHllhedRGPvlesivARTLRQVESTQSMIRILGLSA 658
Cdd:pfam04851 93 DESVD--DNKIVVTTIQSLY-KALELASLELLPDFFDVIIIDEAH-----RSG------ASSYRNILEYFKPAFLLGLTA 158
|
.
gi 764020079 659 T 659
Cdd:pfam04851 159 T 159
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
1332-1465 |
1.60e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 42.14 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1332 KFTHFNPIQTQ-IFHTLYHTDCNVLLgaPTGSGKTVAAELAIFrVFNKyPTskaVYIAPLKALvrerIEDwKVRIEEKLG 1410
Cdd:cd17920 9 GYDEFRPGQLEaINAVLAGRDVLVVM--PTGGGKSLCYQLPAL-LLDG-VT---LVVSPLISL----MQD-QVDRLQQLG 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764020079 1411 KKVVELTGDVTPDMRAIA-------QADLIVTTPEK--WDGVSRSWQNRSYVQKVSILIIDEIH 1465
Cdd:cd17920 77 IRAAALNSTLSPEEKREVllrikngQYKLLYVTPERllSPDFLELLQRLPERKRLALIVVDEAH 140
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1333-1437 |
3.50e-03 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 42.06 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1333 FTHFNPIQTQ-IFHTLYHTDcnVLLGAPTGSGKTVAAELAIF-RVfnKYPTSKAVyiaplKALV----RERIedwkVRIE 1406
Cdd:COG0513 22 YTTPTPIQAQaIPLILAGRD--VLGQAQTGTGKTAAFLLPLLqRL--DPSRPRAP-----QALIlaptRELA----LQVA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 764020079 1407 E---KLGK----KVVELTG--DVTPDMRAIAQ-ADLIVTTP 1437
Cdd:COG0513 89 EelrKLAKylglRVATVYGgvSIGRQIRALKRgVDIVVATP 129
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
482-661 |
3.73e-03 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 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: 350722 [Multi-domain] Cd Length: 211 Bit Score: 41.03 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 482 GMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTnIAML-----TVLHEIRQHVQHGVikkdefKIVYVAPMKALAAEMT 556
Cdd:cd17964 13 GFETMTPVQQKTLKPILSTGDDVLARAKTGTGKT-LAFLlpaiqSLLNTKPAGRRSGV------SALIISPTRELALQIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 557 NYFSKRLEPL-GITVKELTG----DMQLSKGEILRTQMLVTTPEKWDVVTRKSVGDVALSQLvKLLILDEV-HLLheDRG 630
Cdd:cd17964 86 AEAKKLLQGLrKLRVQSAVGgtsrRAELNRLRRGRPDILVATPGRLIDHLENPGVAKAFTDL-DYLVLDEAdRLL--DMG 162
|
170 180 190
....*....|....*....|....*....|...
gi 764020079 631 --PVLESIVaRTLRQVESTQsmIRILGLSATLP 661
Cdd:cd17964 163 frPDLEQIL-RHLPEKNADP--RQTLLFSATVP 192
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
1332-1463 |
3.86e-03 |
|
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: 40.65 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1332 KFTHFNPIQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIF---RVFNKYPTSKAVYIAPLKALVrERIEDWKVRIEEK 1408
Cdd:cd17957 9 GYREPTPIQMQAIPILLHGR-DLLACAPTGSGKTLAFLIPILqklGKPRKKKGLRALILAPTRELA-SQIYRELLKLSKG 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 764020079 1409 LGKKVVELTGDVTP----DMRAIAQADLIVTTPEKWdgVSRSWQNRSYVQKVSILIIDE 1463
Cdd:cd17957 87 TGLRIVLLSKSLEAkakdGPKSITKYDILVSTPLRL--VFLLKQGPIDLSSVEYLVLDE 143
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
497-660 |
4.79e-03 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 39.60 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 497 AYNTNENMLICAPTGAGKTnIAMLTVLHEIRqhvqhgvikkdEFKIVYVAPMKAL----AAEMTNYFSKRleplgiTVKE 572
Cdd:cd17926 14 AHKNNRRGILVLPTGSGKT-LTALALIAYLK-----------ELRTLIVVPTDALldqwKERFEDFLGDS------SIGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 573 LTGDmqlSKGEILRTQMLVTTPEK--WDVVTRKSVGDVALsqlvkLLILDEVHllhedRGPvlesivARTLRQVESTQSM 650
Cdd:cd17926 76 IGGG---KKKDFDDANVVVATYQSlsNLAEEEKDLFDQFG-----LLIVDEAH-----HLP------AKTFSEILKELNA 136
|
170
....*....|
gi 764020079 651 IRILGLSATL 660
Cdd:cd17926 137 KYRLGLTATP 146
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
1353-1465 |
5.58e-03 |
|
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: 40.54 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1353 NVLLGAPTGSGKTVAAELAIFRVFNKYP----TSKAVYIAPLKALVrERIEDWKVRIEEKlGKKVVELTGD--VTPDMRA 1426
Cdd:cd18036 19 NTIICAPTGSGKTRVAVYICRHHLEKRRsageKGRVVVLVNKVPLV-EQQLEKFFKYFRK-GYKVTGLSGDssHKVSFGQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 764020079 1427 IAQA-DLIVTTPEKWDGVSRS--WQNRSYVQKVSILIIDEIH 1465
Cdd:cd18036 97 IVKAsDVIICTPQILINNLLSgrEEERVYLSDFSLLIFDECH 138
|
|
| DEXHc_RLR-3 |
cd18075 |
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ... |
502-659 |
6.71e-03 |
|
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 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: 350833 [Multi-domain] Cd Length: 200 Bit Score: 40.23 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 502 ENMLICAPTGAGKTNIAmltvLHEIRQHVQhgviKKDEFKIVYVAPMKALaaeMTNYFSKRLEPL--GITVKELTGDM-- 577
Cdd:cd18075 18 KNSIIWLPTGAGKTRAA----VYVARRHLE----TKRGAKVAVLVNKVHL---VDQHLEKEFHVLldKYTVTAISGDSsh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 578 -----QLSKG--------EILrtQMLVTTPEKWDvvtrksvgDVALSQLvKLLILDEVHLLHEDrgPVLESIVARTL-RQ 643
Cdd:cd18075 87 kcffgQLARGsdvvictaQIL--QNALLSGEEEA--------HVELTDF-SLLVIDECHHTHKE--AVYNKIMLSYLeKK 153
|
170
....*....|....*.
gi 764020079 644 VESTQSMIRILGLSAT 659
Cdd:cd18075 154 LSRQGDLPQILGLTAS 169
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
1332-1437 |
7.51e-03 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 40.31 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764020079 1332 KFTHFNPIQTQIFHTLYHTD--------CNVLLGAPTGSGKTVAAELAIFRVFNKYPTSK--AVYIAPLKALVRErIEDW 1401
Cdd:cd17956 9 GITSAFPVQAAVIPWLLPSSkstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRlrALIVVPTKELVQQ-VYKV 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 764020079 1402 KVRIEEKLGKKVVELTG--DVTPDMRAIAQ---------ADLIVTTP 1437
Cdd:cd17956 88 FESLCKGTGLKVVSLSGqkSFKKEQKLLLVdtsgrylsrVDILVATP 134
|
|
| |
