|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
480-695 |
1.77e-126 |
|
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: 395.97 E-value: 1.77e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 480 ITSLPDWCQEAFPSseTTSLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHHYNPKTKkLNLSAFKIVY 559
Cdd:cd18019 1 IEELPDWAQPAFEG--FKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGT-INLDAFKIVY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 560 IAPLKALVQEQVREFQRRLAFLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSNNLAIVELVRLLIIDEIHLL 639
Cdd:cd18019 78 IAPMKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6321020 640 HDDRGPVLESIVARTFWASKYGQEYPRIIGLSATLPNYEDVGRFLRV-PKEGLFYFD 695
Cdd:cd18019 158 HDDRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVdPKKGLFYFD 214
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
998-1307 |
2.62e-125 |
|
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: 396.96 E-value: 2.62e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 998 ATDLGNIASSFYINHASMDVYNRELDEHTTQIDLFRIFSMSEEFKYVSVRYEEKRELKQLLEKAPIPIREDIDDPLAKVN 1077
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKGDIEDPHAKVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1078 VLLQSYFSQLKFEGFALNSDIVFIHQNAGRLLRAMFEICLKRGWGHPTRMLLNLCKSATTKMWPTNCPLRQFKTCPVEVI 1157
Cdd:pfam02889 81 ILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPELI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1158 KRLEASTVPW-GDYLQLETPAEVGRAIRSEKYGKQVYDLLKRFPKMSVTCNAQPITRSVMRFNIEIIADWIWDMNVHGSL 1236
Cdd:pfam02889 161 KKLEKKGVESvRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321020 1237 EPFLLMLEDTDGDSILYYDVLFITPDIVGHEFTLSFTYELKQHnqnnLPPNFFLTLISENWWHSEFEIPVS 1307
Cdd:pfam02889 241 EGFWLVVGDSDGNEILHIERFTLTKRTLAGEHKLEFTVPPSDP----GPPQLFVRLISDSWLGADQEVPIS 307
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
995-1309 |
2.27e-107 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 345.78 E-value: 2.27e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 995 VIEATDLGNIASSFYINHASMDVYNRELDEHTTQIDLFRIFSMSEEFKYVSVRYEEKRELKQLLEKAPIPI-REDIDDPL 1073
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLeNPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1074 AKVNVLLQSYFSQLKFEGFALNSDIVFIHQNAGRLLRAMFEICLKRGWGHPTRMLLNLCKSATTKMWPTNCPLRQFKTCP 1153
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1154 VEVIKRLEASTV-PWGDYLQLEtPAEVGRAIRSE-KYGKQVYDLLKRFPKMSVTCNAQPITRSVMRFNIEIIADWIWDMN 1231
Cdd:smart00611 161 EEILKRLEKKKVlSLEDLLELE-DEERGELLGLLdAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDE 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321020 1232 VHGSLEPFLLMLEDTDGDSILYYDVLFITPDIVGHEFTLSFTYELKQHNqnnlpPNFFLTLISENWWHSEFEIPVSFN 1309
Cdd:smart00611 240 IHGKQEGWWLVIGDSDGNELLHIERFSLNKKNVSEEVKLDFTAPATEGN-----YQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
498-1034 |
2.08e-105 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 348.81 E-value: 2.08e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 498 SLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHHYnpktkklnlsafKIVYIAPLKALVQEQVREFQRR 577
Cdd:COG1204 22 ELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------KALYIVPLRALASEKYREFKRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 578 LAFLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSNNlaIVELVRLLIIDEIHLLHD-DRGPVLESIVARtfw 656
Cdd:COG1204 90 FEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDVDLVVVDEAHLIDDeSRGPTLEVLLAR--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 657 ASKYGQEyPRIIGLSATLPNYEDVGRFLRVPKeglfyFDSSFRPCPLSQqfcGIKERNSLK---KLKAMNDACYEKVLES 733
Cdd:COG1204 165 LRRLNPE-AQIVALSATIGNAEEIAEWLDAEL-----VKSDWRPVPLNE---GVLYDGVLRfddGSRRSKDPTLALALDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 734 INEGNQIIVFVHSRKETSRTATWLKNKFAEENITHKLTKNDAGSKQILKTEAANVLDPSLRKLIESGIGTHHAGLTRSDR 813
Cdd:COG1204 236 LEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTNEKLADCLEKGVAFHHAGLPSELR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 814 SLSEDLFADGLLQVLVCTATLAWGVNLPAHTVIIKgtdvySPEKGSWEQLSPQDVLQMLGRAGRPRYDTFGEGIIITDQS 893
Cdd:COG1204 316 RLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-----DTKRGGMVPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSS 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 894 NVQYYL---SVLNQQLPIESQFVSKLVD--NLNAEVVAGNIKCRNDAVNWLAYTYLYVRMLASPMlykvpdissdgqlkk 968
Cdd:COG1204 391 DEADELferYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQYDKGDL--------------- 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321020 969 frESLVHSALCILKEQELVlyDAENDVIEATDLGNIASSFYINHASMDV---YNRELDEHTTQIDLFRI 1034
Cdd:COG1204 456 --EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAElvdGLRKADEEFTDLGLLHL 520
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1345-1536 |
1.23e-101 |
|
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: 323.83 E-value: 1.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1345 FKTFNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHWRQN-KGRAVYINPSGEKIDFLLSDWNKRFSHLAGGK 1423
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNpKGRAVYIAPMQELVDARYKDWRAKFGPLLGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1424 IINKLGnDPSLNLKLLAKSHVLLATPVQFELLSRRWRQRKNIQSLELMIYDDAHEISqGVYGAVYETLISRMIFIATQLE 1503
Cdd:cd18021 81 VVKLTG-ETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIG-GENGPVYEVVVSRMRYISSQLE 158
|
170 180 190
....*....|....*....|....*....|...
gi 6321020 1504 KKIRFVCLSNCLANARDFGEWAGMTKSNIYNFS 1536
Cdd:cd18021 159 KPIRIVGLSSSLANARDVGEWLGASKSTIFNFH 191
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1843-2161 |
6.71e-96 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 312.66 E-value: 6.71e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1843 IISTLSNGLIASHYGVSFFTIQSFVSSLSNTSTLKNMLYVLSTAVEFESVPLRKGDRALLVKLSKRLPLRFPeHTSSGSV 1922
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLE-NPSLDDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1923 SFKVFLLLQAYFSRLELPV-DFQNDLKDILEKVVPLINVVVDILSANGYLN-ATTAMDLAQMLIQGVWDVDNPLRQIPHF 2000
Cdd:smart00611 80 HVKANLLLQAHLSRLKLPSfALESDTVYVLQNAGRLLQAMVDIALERGWLStALNALNLSQMIIQALWPTDSPLLQLPHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 2001 NNKILEKCKEINVETVYDIMALEDEERDEILTLTDSQLAQVAAFVNNYPNVELTYSLNNSDSLISGVKQKITIQLTRDVE 2080
Cdd:smart00611 160 PEEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 2081 PEnlqvtsekypfDKLESWWLVLGEVSKKELYAIKKVTLNKET--QQYELEFDTPTS-GKHNLTIWCVCDSYLDADKELS 2157
Cdd:smart00611 240 IH-----------GKQEGWWLVIGDSDGNELLHIERFSLNKKNvsEEVKLDFTAPATeGNYQYTLRLVSDSYLGCDQEYP 308
|
....
gi 6321020 2158 FEIN 2161
Cdd:smart00611 309 LSFD 312
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1850-2159 |
7.69e-93 |
|
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: 303.74 E-value: 7.69e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1850 GLIASHYGVSFFTIQSFVSSLSNTSTLKNMLYVLSTAVEFESVPLRKGDRALLVKLSKRLPLRFPEHTSSGSvsFKVFLL 1929
Cdd:pfam02889 5 GRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKGDIEDPH--AKVNIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1930 LQAYFSRLELP-VDFQNDLKDILEKVVPLINVVVDILSANGYLNAT-TAMDLAQMLIQGVWDVDNPLRQIPHFNNKILEK 2007
Cdd:pfam02889 83 LQAYISRLKLPgFALVSDMNYILQNAGRILRALFEILLSKGWLSAAlTALDLCKMIEQRMWDSDSPLRQFPGIPPELIKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 2008 CKEINVETVYDIMALEDEERDEILTLTDSQLAQVAAFVNNYPNVELTYSLnnsdSLISGVKQKITIQLTRDvepenlqvt 2087
Cdd:pfam02889 163 LEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEV----QPITRSVLRVEVTITPD--------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 2088 sekYPFDK-----LESWWLVLGEVSKKELYAIKKVTLNKETQQ--YELEFDTPTS--GKHNLTIWCVCDSYLDADKELSF 2158
Cdd:pfam02889 230 ---FPWDKrvhgkSEGFWLVVGDSDGNEILHIERFTLTKRTLAgeHKLEFTVPPSdpGPPQLFVRLISDSWLGADQEVPI 306
|
.
gi 6321020 2159 E 2159
Cdd:pfam02889 307 S 307
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
699-891 |
5.88e-63 |
|
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: 211.64 E-value: 5.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 699 RPCPLSQQFCGIKERNSLKKLKAMN----DACYEKVLESINEGNQIIVFVHSRKETSRTATWLknkfaeenithkltknd 774
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNkfdsDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDL----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 775 agskqilkteaanvldpslrklieSGIGTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLPAHTVIIKGTDVYS 854
Cdd:cd18795 64 ------------------------AGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 6321020 855 PEkgSWEQLSPQDVLQMLGRAGRPRYDTFGEGIIITD 891
Cdd:cd18795 120 GK--GYRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
498-1061 |
5.46e-55 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 206.59 E-value: 5.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 498 SLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKalshhynpktkKLNLSAFKIVYIAPLKALVQEQVREFQRr 577
Cdd:PRK00254 23 ELYPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVN-----------KLLREGGKAVYLVPLKALAEEKYREFKD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 578 LAFLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSNNLaiVELVRLLIIDEIHLLHD-DRGPVLESIVARTFW 656
Cdd:PRK00254 91 WEKLGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRHGSSW--IKDVKLVVADEIHLIGSyDRGATLEMILTHMLG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 657 ASKygqeyprIIGLSATLPNYEDVGRFLRVPkeglfYFDSSFRPCPLSQqfcGIKERNSL----KKLKAMNDACYEKVLE 732
Cdd:PRK00254 169 RAQ-------ILGLSATVGNAEELAEWLNAE-----LVVSDWRPVKLRK---GVFYQGFLfwedGKIERFPNSWESLVYD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 733 SINEGNQIIVFVHSRKETSRTATWLKNKfaeenITHKLTKNDA-GSKQILKTEAANVLDPSLRKLIESGIGTHHAGLTRS 811
Cdd:PRK00254 234 AVKKGKGALVFVNTRRSAEKEALELAKK-----IKRFLTKPELrALKELADSLEENPTNEKLKKALRGGVAFHHAGLGRT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 812 DRSLSEDLFADGLLQVLVCTATLAWGVNLPAHTVIIKGTDVYSpEKGsWEQLSPQDVLQMLGRAGRPRYDTFGEGIII-- 889
Cdd:PRK00254 309 ERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYS-NFG-WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVat 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 890 TDQSN--VQYYL----SVLNQQLPIESQFVSKLVdnlnAEVVAGNIKCRNDAVNWLAYT-YLYVRMLASPMLYKVPDIss 962
Cdd:PRK00254 387 TEEPSklMERYIfgkpEKLFSMLSNESAFRSQVL----ALITNFGVSNFKELVNFLERTfYAHQRKDLYSLEEKAKEI-- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 963 dgqlkkfreslvhsaLCILKEQELVLYDAEnDVIEATDLGNIASSFYINHASMDVYN---RELDEHTTQIDLFRIFSMSE 1039
Cdd:PRK00254 461 ---------------VYFLLENEFIDIDLE-DRFIPLPLGIRTSQLYIDPLTAKKFKdafPKIEKNPNPLGIFQLIASTP 524
|
570 580
....*....|....*....|..
gi 6321020 1040 EFKYVSVRyeeKRELKQLLEKA 1061
Cdd:PRK00254 525 DMTPLNYS---RKEMEDLLDEA 543
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
500-680 |
2.53e-41 |
|
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: 150.09 E-value: 2.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 500 NPIQSKVFHAAFEGDsNMLICAPTGSGKTNIALLTVLKALSHHYNPKtkklnlsafKIVYIAPLKALVQEQVREFQRRLA 579
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDKLDNGP---------QALVLAPTRELAEQIYEELKKLGK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 580 FLGIKV-AELTGDSRLS-RKQIDETQVLVSTPEKWDITTRNSNNLaivELVRLLIIDEIHLLHD-DRGPVLESIVARTfw 656
Cdd:pfam00270 71 GLGLKVaSLLGGDSRKEqLEKLKGPDILVGTPGRLLDLLQERKLL---KNLKLLVLDEAHRLLDmGFGPDLEEILRRL-- 145
|
170 180
....*....|....*....|....*
gi 6321020 657 askygQEYPRIIGLSATLP-NYEDV 680
Cdd:pfam00270 146 -----PKKRQILLLSATLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
491-707 |
2.49e-30 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 119.90 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 491 FPSSETTSLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHHYNPKTkklnlsafkiVYIAPLKALVQEQ 570
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV----------LVLVPTRELAEQW 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 571 VREFQRRLAFLGIKVAELTGDS----RLSRKQIDETQVLVSTPEKWDITTRnsNNLAIVELVRLLIIDEIHLLHD-DRGP 645
Cdd:smart00487 71 AEELKKLGPSLGLKVVGLYGGDskreQLRKLESGKTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHRLLDgGFGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321020 646 VLESIVARTFWAskygqeyPRIIGLSATLPNYEDvgRFLRVPKEGLFYFDSSFRPCPLSQQF 707
Cdd:smart00487 149 QLEKLLKLLPKN-------VQLLLLSATPPEEIE--NLLELFLNDPVFIDVGFTPLEPIEQF 201
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
460-880 |
4.11e-29 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 126.93 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 460 YDEIhipAPSKPVID-YELKEItSLPDWCQEAFpSSETTSLNPIQSK-VFHAAFEGDsNMLICAPTGSGKTNIALLTVLK 537
Cdd:COG1202 175 FDEI---SATTDEVDtVPVDDL-DLPPELKDLL-EGRGEELLPVQSLaVENGLLEGK-DQLVVSATATGKTLIGELAGIK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 538 -ALSHHYnpktkklnlsafKIVYIAPLKALVQEQVREFQRRLAFlGIKVAELTGDSRLSRKQIDET---QVLVSTPEKWD 613
Cdd:COG1202 249 nALEGKG------------KMLFLVPLVALANQKYEDFKDRYGD-GLDVSIRVGASRIRDDGTRFDpnaDIIVGTYEGID 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 614 ITTRNSNNLAIVELVrllIIDEIHLLHD-DRGPVLESIVARTfwasKYGQEYPRIIGLSATLPNYEDVGRFLR---VPKE 689
Cdd:COG1202 316 HALRTGRDLGDIGTV---VIDEVHMLEDpERGHRLDGLIARL----KYYCPGAQWIYLSATVGNPEELAKKLGaklVEYE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 690 GlfyfdssfRPCPLSQQ--FCgiKERNslkKLKAMNDAC---YEKVLESINEGnQIIVFVHSRKEtsrtatwlknkfaee 764
Cdd:COG1202 389 E--------RPVPLERHltFA--DGRE---KIRIINKLVkreFDTKSSKGYRG-QTIIFTNSRRR--------------- 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 765 niTHKLTkndagskqilkteaanvldpslRKLiesGIGT--HHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLPA 842
Cdd:COG1202 440 --CHEIA----------------------RAL---GYKAapYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPA 492
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 6321020 843 HTVIIK----GTDvyspekgsWeqLSPQDVLQMLGRAGRPRY 880
Cdd:COG1202 493 SQVIFDslamGIE--------W--LSVQEFHQMLGRAGRPDY 524
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1349-1521 |
2.34e-26 |
|
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: 107.33 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1349 NKIQSQVFESLYnSNDSVFVGSGKGTGKTAMAELALLNHWR--QNKGRAVYINPSGEKIDFLLSDWNKRFSHLaGGKIIN 1426
Cdd:pfam00270 1 TPIQAEAIPAIL-EGRDVLVQAPTGSGKTLAFLLPALEALDklDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1427 KLGNDP-SLNLKLLAKSHVLLATPvqfELLSRRWRQRKNIQSLELMIYDDAHEISQGVYGAVYETLISRmifiatqLEKK 1505
Cdd:pfam00270 79 LLGGDSrKEQLEKLKGPDILVGTP---GRLLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRR-------LPKK 148
|
170
....*....|....*..
gi 6321020 1506 IRFVCLSNCLA-NARDF 1521
Cdd:pfam00270 149 RQILLLSATLPrNLEDL 165
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1338-1870 |
2.43e-23 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 106.90 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1338 DFSEVFEFKTFNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHWRqNKGRAVYINPS----GEKidflLSDWN 1413
Cdd:COG1204 13 EFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALL-NGGKALYIVPLralaSEK----YREFK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1414 KRFSHLagGKIINKLGNDPSLNLKLLAKSHVLLATPVQFELLsrrWRQRKN-IQSLELMIYDDAHEISQGVYGAVYETLI 1492
Cdd:COG1204 88 RDFEEL--GIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSL---LRNGPSwLRDVDLVVVDEAHLIDDESRGPTLEVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1493 SRMIfiatQLEKKIRFVCLSNCLANARDFGEW--AGMTKSniyNFSPSERIEPLEI-NIQSFKDVEHISfnfsmLQMAFE 1569
Cdd:COG1204 163 ARLR----RLNPEAQIVALSATIGNAEEIAEWldAELVKS---DWRPVPLNEGVLYdGVLRFDDGSRRS-----KDPTLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1570 ASAAAAGNRNSSSVFLPSRKDCMEVASafmKFSKAIEWDMLNVEEEQIVPYIEKL--------TDGHLRAPLKHGVGILY 1641
Cdd:COG1204 231 LALDLLEEGGQVLVFVSSRRDAESLAK---KLADELKRRLTPEEREELEELAEELlevseethTNEKLADCLEKGVAFHH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1642 KGMASNDERIVKRLYEYGAVSVLliskdcsaFA-----------CKTdeVIIlgTNLYDGAEhkyMPYTINELLEMVGLA 1710
Cdd:COG1204 308 AGLPSELRRLVEDAFREGLIKVL--------VAtptlaagvnlpARR--VII--RDTKRGGM---VPIPVLEFKQMAGRA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1711 --SGNDSMaGKVLIL--TSHNMKAYYKKFLI-EPLPTESYL--QYIIHDTLNNEIANSIIQSKQDCVDWF--TYSYfyrr 1781
Cdd:COG1204 373 grPGYDPY-GEAILVakSSDEADELFERYILgEPEPIRSKLanESALRTHLLALIASGFANSREELLDFLenTFYA---- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1782 ihvnpsYYGVRDTsphgisvfLSNLVETCLNDLVESSFIEIDdteaevtaevnGGDDEATEIistlsnGLIASHYGVSFF 1861
Cdd:COG1204 448 ------YQYDKGD--------LEEVVDDALEFLLENGFIEED-----------GDRLRATKL------GKLVSRLYIDPL 496
|
....*....
gi 6321020 1862 TIQSFVSSL 1870
Cdd:COG1204 497 TAAELVDGL 505
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
281-389 |
6.50e-21 |
|
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: 89.59 E-value: 6.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 281 ESVPIYSIDEFFLQRKLRSElgYKDTSVIQDLSEKILNDIETLEHNPVALEQKLVDLLKFENISLAEFILKNRSTIFWGI 360
Cdd:pfam18149 3 DSLDPHDIDAFWLQRLLSKF--YGDAIEAQKKAEEVLDILESAADDLRECENQLVELLDYDKFDLVKLLLKNRDKIVWCT 80
|
90 100 110
....*....|....*....|....*....|.
gi 6321020 361 RLAKS-TENEIPNLIEKMVAK-GLNDLVEQY 389
Cdd:pfam18149 81 KLARAqSEEEKQAIEEEMRSNpGLAWILDEL 111
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
501-877 |
1.11e-19 |
|
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: 96.47 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 501 PIQSKVFHAAFEGDSNMLIcAPTGSGKTNIALLTVLKALSHHYNPKTKKLnlsafKIVYIAPLKALVQEQVREFQRRLAF 580
Cdd:TIGR04121 16 PFQLEMWAAALEGRSGLLI-APTGSGKTLAGFLPSLIDLAGPEAPKEKGL-----HTLYITPLRALAVDIARNLQAPIEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 581 LG--IKVAELTGDSRLSRKQIDET---QVLVSTPEKWDITTRNSNNLAIVELVRLLIIDEIH-LLHDDRGPVLESIVAR- 653
Cdd:TIGR04121 90 LGlpIRVETRTGDTSSSERARQRKkppDILLTTPESLALLLSYPDAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 654 TFWASKYgqeypRIIGLSATLPNYEDVGRFLrVPKEGlfyfdssfRPCPLSQQFCG--IKERNSLKK------------L 719
Cdd:TIGR04121 170 RRLAPGL-----RRWGLSATIGNLEEARRVL-LGVGG--------APAVLVRGKLPkaIEVISLLPEseerfpwaghlgL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 720 KAMndacyEKVLESINEGNQIIVFVHSRKETSRT--ATWLKNkfAEENIThkltkndagskqilkteaanvldpslrkli 797
Cdd:TIGR04121 236 RAL-----PEVYAEIDQARTTLVFTNTRSQAELWfqALWEAN--PEFALP------------------------------ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 798 esgIGTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVN-LPAHTVIIKGtdvyspekgsweqlSPQDVLQMLGRAG 876
Cdd:TIGR04121 279 ---IALHHGSLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDfGPVDLVIQIG--------------SPKGVARLLQRAG 341
|
.
gi 6321020 877 R 877
Cdd:TIGR04121 342 R 342
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
473-889 |
2.62e-16 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 85.71 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 473 IDYELKEITS------LPDWCQEAFpSSETTSLNPIQSKVFHAAFEGDsNMLICAPTGSGKTNIALLTVLKALSHHynPK 546
Cdd:PRK13767 2 IEYATKEYSDeeildlLRPYVREWF-KEKFGTFTPPQRYAIPLIHEGK-NVLISSPTGSGKTLAAFLAIIDELFRL--GR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 547 TKKLNLSAFkIVYIAPLKAL-------VQEQVREFQRRLAFLG-----IKVAELTGDSRLSRKQ--IDET-QVLVSTPEk 611
Cdd:PRK13767 78 EGELEDKVY-CLYVSPLRALnndihrnLEEPLTEIREIAKERGeelpeIRVAIRTGDTSSYEKQkmLKKPpHILITTPE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 612 wdittrnsnNLAIV----------ELVRLLIIDEIHLLHDD-RG-------PVLESIVartfwaskyGQEYPRiIGLSAT 673
Cdd:PRK13767 156 ---------SLAILlnspkfreklRTVKWVIVDEIHSLAENkRGvhlslslERLEELA---------GGEFVR-IGLSAT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 674 LPNYEDVGRFLrvpkeGLFYFDSSFRPCPlsqqfcgIKERNSLKKL----------------KAMNDACYEKVLESINEG 737
Cdd:PRK13767 217 IEPLEEVAKFL-----VGYEDDGEPRDCE-------IVDARFVKPFdikvispvddlihtpaEEISEALYETLHELIKEH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 738 NQIIVFVHSRKETSRTATWLKNKFAEEnithkltkndagskqilkteaanvldpslrkLIESGIGTHHAGLTRSDRSLSE 817
Cdd:PRK13767 285 RTTLIFTNTRSGAERVLYNLRKRFPEE-------------------------------YDEDNIGAHHSSLSREVRLEVE 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321020 818 DLFADGLLQVLVCTATLAWGVNLPAHTVIIkgtdvyspekgsweQL-SPQDV---LQMLGRAGRpRYDTFGEGIII 889
Cdd:PRK13767 334 EKLKRGELKVVVSSTSLELGIDIGYIDLVV--------------LLgSPKSVsrlLQRIGRAGH-RLGEVSKGRII 394
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1341-1546 |
6.25e-16 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 78.30 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1341 EVFEFKTFNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHW-RQNKGRAVYINPSGEKIDFLLSDWNKRFSHL 1419
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALkRGKGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1420 aGGKIINKLGNDPS---LNLKLLAKSHVLLATPVQFELLSRRWrqRKNIQSLELMIYDDAHEISQGVYGAVYETLISRmi 1496
Cdd:smart00487 82 -GLKVVGLYGGDSKreqLRKLESGKTDILVTTPGRLLDLLEND--KLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKL-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6321020 1497 fiatqLEKKIRFVCLSNCLANARDFGEWAGMtkSNIYNFSPSERI-EPLEI 1546
Cdd:smart00487 157 -----LPKNVQLLLLSATPPEEIENLLELFL--NDPVFIDVGFTPlEPIEQ 200
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
800-878 |
7.90e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 71.47 E-value: 7.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 800 GIGTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLP-AHTVIIKGTDvyspekgsweqLSPQDVLQMLGRAGRP 878
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDLP-----------WSPASYIQRIGRAGRA 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
793-877 |
1.67e-08 |
|
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: 54.14 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 793 LRKLIESGIGTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLP-AHTVIIkgtdvYSPEKgsweqlSPQDVLQM 871
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YDLPW------NPASYIQR 101
|
....*.
gi 6321020 872 LGRAGR 877
Cdd:pfam00271 102 IGRAGR 107
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1543-1724 |
6.73e-06 |
|
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: 47.93 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1543 PLEINIQSFKDVEHISFNFSMLQMAFEASAAAA----GNRNSSSVFLPSRKDCMEVAsafmkfskaiewdmlnveeeqiv 1618
Cdd:cd18795 4 PLEEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKietvSEGKPVLVFCSSRKECEKTA----------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1619 pyiEKLTdghlraplkhGVGILYKGMASNDERIVKRLYEYGAVSVLliskdC--SAFA------CKTdeVIILGTNLYDG 1690
Cdd:cd18795 61 ---KDLA----------GIAFHHAGLTREDRELVEELFREGLIKVL-----VatSTLAagvnlpART--VIIKGTQRYDG 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 6321020 1691 AEHKYMPytINELLEMVGLA--SGNDSMaGKVLILT 1724
Cdd:cd18795 121 KGYRELS--PLEYLQMIGRAgrPGFDTR-GEAIIMT 153
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1374-1531 |
7.98e-06 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 50.97 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1374 TGKTAMAELALLNHWRQNKGRAVYINP----SGEKI-DFllSDWNKrfshlAGGKIINKLGNDPSLNlKLLAKSHVLLAT 1448
Cdd:PRK00254 50 SGKTLVAEIVMVNKLLREGGKAVYLVPlkalAEEKYrEF--KDWEK-----LGLRVAMTTGDYDSTD-EWLGKYDIIIAT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1449 PVQFELLSR---RWrqrknIQSLELMIYDDAHEISQGVYGAVYEtlisrmiFIATQLEKKIRFVCLSNCLANARDFGEW- 1524
Cdd:PRK00254 122 AEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSYDRGATLE-------MILTHMLGRAQILGLSATVGNAEELAEWl 189
|
....*...
gi 6321020 1525 -AGMTKSN 1531
Cdd:PRK00254 190 nAELVVSD 197
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
480-695 |
1.77e-126 |
|
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: 395.97 E-value: 1.77e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 480 ITSLPDWCQEAFPSseTTSLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHHYNPKTKkLNLSAFKIVY 559
Cdd:cd18019 1 IEELPDWAQPAFEG--FKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGT-INLDAFKIVY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 560 IAPLKALVQEQVREFQRRLAFLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSNNLAIVELVRLLIIDEIHLL 639
Cdd:cd18019 78 IAPMKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6321020 640 HDDRGPVLESIVARTFWASKYGQEYPRIIGLSATLPNYEDVGRFLRV-PKEGLFYFD 695
Cdd:cd18019 158 HDDRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVdPKKGLFYFD 214
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
998-1307 |
2.62e-125 |
|
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: 396.96 E-value: 2.62e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 998 ATDLGNIASSFYINHASMDVYNRELDEHTTQIDLFRIFSMSEEFKYVSVRYEEKRELKQLLEKAPIPIREDIDDPLAKVN 1077
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKGDIEDPHAKVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1078 VLLQSYFSQLKFEGFALNSDIVFIHQNAGRLLRAMFEICLKRGWGHPTRMLLNLCKSATTKMWPTNCPLRQFKTCPVEVI 1157
Cdd:pfam02889 81 ILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPELI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1158 KRLEASTVPW-GDYLQLETPAEVGRAIRSEKYGKQVYDLLKRFPKMSVTCNAQPITRSVMRFNIEIIADWIWDMNVHGSL 1236
Cdd:pfam02889 161 KKLEKKGVESvRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321020 1237 EPFLLMLEDTDGDSILYYDVLFITPDIVGHEFTLSFTYELKQHnqnnLPPNFFLTLISENWWHSEFEIPVS 1307
Cdd:pfam02889 241 EGFWLVVGDSDGNEILHIERFTLTKRTLAGEHKLEFTVPPSDP----GPPQLFVRLISDSWLGADQEVPIS 307
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
995-1309 |
2.27e-107 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 345.78 E-value: 2.27e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 995 VIEATDLGNIASSFYINHASMDVYNRELDEHTTQIDLFRIFSMSEEFKYVSVRYEEKRELKQLLEKAPIPI-REDIDDPL 1073
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLeNPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1074 AKVNVLLQSYFSQLKFEGFALNSDIVFIHQNAGRLLRAMFEICLKRGWGHPTRMLLNLCKSATTKMWPTNCPLRQFKTCP 1153
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1154 VEVIKRLEASTV-PWGDYLQLEtPAEVGRAIRSE-KYGKQVYDLLKRFPKMSVTCNAQPITRSVMRFNIEIIADWIWDMN 1231
Cdd:smart00611 161 EEILKRLEKKKVlSLEDLLELE-DEERGELLGLLdAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDE 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321020 1232 VHGSLEPFLLMLEDTDGDSILYYDVLFITPDIVGHEFTLSFTYELKQHNqnnlpPNFFLTLISENWWHSEFEIPVSFN 1309
Cdd:smart00611 240 IHGKQEGWWLVIGDSDGNELLHIERFSLNKKNVSEEVKLDFTAPATEGN-----YQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
498-1034 |
2.08e-105 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 348.81 E-value: 2.08e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 498 SLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHHYnpktkklnlsafKIVYIAPLKALVQEQVREFQRR 577
Cdd:COG1204 22 ELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------KALYIVPLRALASEKYREFKRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 578 LAFLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSNNlaIVELVRLLIIDEIHLLHD-DRGPVLESIVARtfw 656
Cdd:COG1204 90 FEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDVDLVVVDEAHLIDDeSRGPTLEVLLAR--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 657 ASKYGQEyPRIIGLSATLPNYEDVGRFLRVPKeglfyFDSSFRPCPLSQqfcGIKERNSLK---KLKAMNDACYEKVLES 733
Cdd:COG1204 165 LRRLNPE-AQIVALSATIGNAEEIAEWLDAEL-----VKSDWRPVPLNE---GVLYDGVLRfddGSRRSKDPTLALALDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 734 INEGNQIIVFVHSRKETSRTATWLKNKFAEENITHKLTKNDAGSKQILKTEAANVLDPSLRKLIESGIGTHHAGLTRSDR 813
Cdd:COG1204 236 LEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTNEKLADCLEKGVAFHHAGLPSELR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 814 SLSEDLFADGLLQVLVCTATLAWGVNLPAHTVIIKgtdvySPEKGSWEQLSPQDVLQMLGRAGRPRYDTFGEGIIITDQS 893
Cdd:COG1204 316 RLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-----DTKRGGMVPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSS 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 894 NVQYYL---SVLNQQLPIESQFVSKLVD--NLNAEVVAGNIKCRNDAVNWLAYTYLYVRMLASPMlykvpdissdgqlkk 968
Cdd:COG1204 391 DEADELferYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQYDKGDL--------------- 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321020 969 frESLVHSALCILKEQELVlyDAENDVIEATDLGNIASSFYINHASMDV---YNRELDEHTTQIDLFRI 1034
Cdd:COG1204 456 --EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAElvdGLRKADEEFTDLGLLHL 520
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1345-1536 |
1.23e-101 |
|
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: 323.83 E-value: 1.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1345 FKTFNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHWRQN-KGRAVYINPSGEKIDFLLSDWNKRFSHLAGGK 1423
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNpKGRAVYIAPMQELVDARYKDWRAKFGPLLGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1424 IINKLGnDPSLNLKLLAKSHVLLATPVQFELLSRRWRQRKNIQSLELMIYDDAHEISqGVYGAVYETLISRMIFIATQLE 1503
Cdd:cd18021 81 VVKLTG-ETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIG-GENGPVYEVVVSRMRYISSQLE 158
|
170 180 190
....*....|....*....|....*....|...
gi 6321020 1504 KKIRFVCLSNCLANARDFGEWAGMTKSNIYNFS 1536
Cdd:cd18021 159 KPIRIVGLSSSLANARDVGEWLGASKSTIFNFH 191
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1843-2161 |
6.71e-96 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 312.66 E-value: 6.71e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1843 IISTLSNGLIASHYGVSFFTIQSFVSSLSNTSTLKNMLYVLSTAVEFESVPLRKGDRALLVKLSKRLPLRFPeHTSSGSV 1922
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLE-NPSLDDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1923 SFKVFLLLQAYFSRLELPV-DFQNDLKDILEKVVPLINVVVDILSANGYLN-ATTAMDLAQMLIQGVWDVDNPLRQIPHF 2000
Cdd:smart00611 80 HVKANLLLQAHLSRLKLPSfALESDTVYVLQNAGRLLQAMVDIALERGWLStALNALNLSQMIIQALWPTDSPLLQLPHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 2001 NNKILEKCKEINVETVYDIMALEDEERDEILTLTDSQLAQVAAFVNNYPNVELTYSLNNSDSLISGVKQKITIQLTRDVE 2080
Cdd:smart00611 160 PEEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 2081 PEnlqvtsekypfDKLESWWLVLGEVSKKELYAIKKVTLNKET--QQYELEFDTPTS-GKHNLTIWCVCDSYLDADKELS 2157
Cdd:smart00611 240 IH-----------GKQEGWWLVIGDSDGNELLHIERFSLNKKNvsEEVKLDFTAPATeGNYQYTLRLVSDSYLGCDQEYP 308
|
....
gi 6321020 2158 FEIN 2161
Cdd:smart00611 309 LSFD 312
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1850-2159 |
7.69e-93 |
|
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: 303.74 E-value: 7.69e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1850 GLIASHYGVSFFTIQSFVSSLSNTSTLKNMLYVLSTAVEFESVPLRKGDRALLVKLSKRLPLRFPEHTSSGSvsFKVFLL 1929
Cdd:pfam02889 5 GRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKGDIEDPH--AKVNIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1930 LQAYFSRLELP-VDFQNDLKDILEKVVPLINVVVDILSANGYLNAT-TAMDLAQMLIQGVWDVDNPLRQIPHFNNKILEK 2007
Cdd:pfam02889 83 LQAYISRLKLPgFALVSDMNYILQNAGRILRALFEILLSKGWLSAAlTALDLCKMIEQRMWDSDSPLRQFPGIPPELIKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 2008 CKEINVETVYDIMALEDEERDEILTLTDSQLAQVAAFVNNYPNVELTYSLnnsdSLISGVKQKITIQLTRDvepenlqvt 2087
Cdd:pfam02889 163 LEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEV----QPITRSVLRVEVTITPD--------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 2088 sekYPFDK-----LESWWLVLGEVSKKELYAIKKVTLNKETQQ--YELEFDTPTS--GKHNLTIWCVCDSYLDADKELSF 2158
Cdd:pfam02889 230 ---FPWDKrvhgkSEGFWLVVGDSDGNEILHIERFTLTKRTLAgeHKLEFTVPPSdpGPPQLFVRLISDSWLGADQEVPI 306
|
.
gi 6321020 2159 E 2159
Cdd:pfam02889 307 S 307
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
998-1308 |
2.08e-88 |
|
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: 291.18 E-value: 2.08e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 998 ATDLGNIASSFYINHASMDVYNRELDEHTTQIDLFRIFSMSEEFKYVSVRYEEKRELKQLLEKAPIPIRE-DIDDPLAKV 1076
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEgIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1077 NVLLQSYFSQLKFEGFALNSDIVFIHQNAGRLLRAMFEICLKRGWGHPTRMLLNLCKSATTKMWP-TNCPLRQFK-TCPV 1154
Cdd:smart00973 81 NLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEdSDSPLKQLPhFLIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1155 EVIKRLEASTVPWGDYLQLET-PAEVGRAI-RSEKYGKQVYDLLKRFPKMSVTCNAQPITRSV-MRFNIEIIADWIWDMN 1231
Cdd:smart00973 161 DVYDKLELKDGSRSFELLLDMnAAELGEFLnRLPPNGRLIYELLRRFPKIEVEAEVLPITRDLtLRVELEITPVFAWDLP 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321020 1232 V-HGSLEPFLLMLEDTDGDSILYYDVLFITPDIVGHEFTLSFTYELKqhnqNNLPPNFFLTLISENWWHSEFEIPVSF 1308
Cdd:smart00973 241 RhKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKLDFTVPLS----EPGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
498-695 |
2.11e-84 |
|
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: 275.08 E-value: 2.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 498 SLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHHYNPKtKKLNLSAFKIVYIAPLKALVQEQVREFQRR 577
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQG-GVIKKDDFKIVYIAPMKALAAEMVEKFSKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 578 LAFLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSN-NLAIVELVRLLIIDEIHLLHDDRGPVLESIVARTFW 656
Cdd:cd18020 80 LAPLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSgDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6321020 657 ASKYGQEYPRIIGLSATLPNYEDVGRFLRV-PKEGLFYFD 695
Cdd:cd18020 160 QVESTQSMIRIVGLSATLPNYLDVADFLRVnPYKGLFFFD 199
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
1850-2160 |
7.41e-77 |
|
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: 258.06 E-value: 7.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1850 GLIASHYGVSFFTIQSFVSSLSNTSTLKNMLYVLSTAVEFESVPLRKGDRALLVKLSKRLPLRFPEHtSSGSVSFKVFLL 1929
Cdd:smart00973 5 GRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEG-IIDSPHAKVNLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1930 LQAYFSRLELP-VDFQNDLKDILEKVVPLINVVVDILSANGYLN-ATTAMDLAQMLIQGVWDV-DNPLRQIPHFnnkile 2006
Cdd:smart00973 84 LQAHLSRLPLPdFDLVSDLKYILQNAPRILRALVDIALSKGWLRtALNALDLSQMVVQRLWEDsDSPLKQLPHF------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 2007 kckeiNVETVYDIMALEDEERDEILTLtDSQLAQVAAFVNN-YPNVELTYSLNNSDSLIS--GVKQKITIQLTRDVEPEN 2083
Cdd:smart00973 158 -----LIEDVYDKLELKDGSRSFELLL-DMNAAELGEFLNRlPPNGRLIYELLRRFPKIEveAEVLPITRDLTLRVELEI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 2084 LQVTSEKYPF--DKLESWWLVLGEVSKKELYAIKKVTLNK--ETQQYELEFDTPTS--GKHNLTIWCVCDSYLDADKELS 2157
Cdd:smart00973 232 TPVFAWDLPRhkGKSESWWLVVGDSDTNELLAIKRVTLRKkkKSNEVKLDFTVPLSepGPENYTVYLISDSYLGCDQEVS 311
|
...
gi 6321020 2158 FEI 2160
Cdd:smart00973 312 FSL 314
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
498-695 |
8.13e-64 |
|
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: 215.20 E-value: 8.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 498 SLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHHynpktkklnlsAFKIVYIAPLKALVQEQVREFQRR 577
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-----------GGKAVYIAPTRALVNQKEADLRER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 578 LAFLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSNNLaIVELVRLLIIDEIHLLHD-DRGPVLESIVARTFW 656
Cdd:cd17921 70 FGPLGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDgERGVVLELLLSRLLR 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 6321020 657 ASKygqeYPRIIGLSATLPNYEDVGRFLRVpkEGLFYFD 695
Cdd:cd17921 149 INK----NARFVGLSATLPNAEDLAEWLGV--EDLIRFD 181
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
699-891 |
5.88e-63 |
|
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: 211.64 E-value: 5.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 699 RPCPLSQQFCGIKERNSLKKLKAMN----DACYEKVLESINEGNQIIVFVHSRKETSRTATWLknkfaeenithkltknd 774
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNkfdsDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDL----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 775 agskqilkteaanvldpslrklieSGIGTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLPAHTVIIKGTDVYS 854
Cdd:cd18795 64 ------------------------AGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 6321020 855 PEkgSWEQLSPQDVLQMLGRAGRPRYDTFGEGIIITD 891
Cdd:cd18795 120 GK--GYRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
500-700 |
1.42e-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: 198.35 E-value: 1.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 500 NPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALShhynpKTKKLNLSAFKIVYIAPLKALVQEQVREFQRRLA 579
Cdd:cd18023 3 NRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLK-----ERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 580 FLGIKVAELTGDSRLSR-KQIDETQVLVSTPEKWD-ITTRNSNNLAIVELVRLLIIDEIHLLHDDRGPVLESIVARTFWA 657
Cdd:cd18023 78 PLGLSCAELTGDTEMDDtFEIQDADIILTTPEKWDsMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6321020 658 SKYGQEYP------RIIGLSATLPNYEDVGRFLRVPKEGLFYFDSSFRP 700
Cdd:cd18023 158 SSSSELRGstvrpmRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
500-695 |
1.46e-57 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350780 [Multi-domain] Cd Length: 189 Bit Score: 197.60 E-value: 1.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 500 NPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHHynPKtkklnlsaFKIVYIAPLKALVQEQVREFQRRL- 578
Cdd:cd18022 3 NPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKY--PG--------SKVVYIAPLKALVRERVDDWKKRFe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 579 AFLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSNNLAIVELVRLLIIDEIHLLHDDRGPVLESIVARTFWAS 658
Cdd:cd18022 73 EKLGKKVVELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYIS 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 6321020 659 KYGQEYPRIIGLSATLPNYEDVGRFLRVPKEGLFYFD 695
Cdd:cd18022 153 SQTEKPVRLVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
1347-1535 |
4.43e-56 |
|
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: 193.25 E-value: 4.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1347 TFNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHWRQNKGRAVYINPSGEKIDFLLSDWNKRFSHLaGGKIIN 1426
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVYIAPTRALVNQKEADLRERFGPL-GKNVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1427 KLGnDPSLNLKLLAKSHVLLATPVQFELLSRRWRQRkNIQSLELMIYDDAHEISQGVYGAVYETLISRMIFIatqlEKKI 1506
Cdd:cd17921 80 LTG-DPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRI----NKNA 153
|
170 180
....*....|....*....|....*....
gi 6321020 1507 RFVCLSNCLANARDFGEWAGMTksNIYNF 1535
Cdd:cd17921 154 RFVGLSATLPNAEDLAEWLGVE--DLIRF 180
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
498-1061 |
5.46e-55 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 206.59 E-value: 5.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 498 SLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKalshhynpktkKLNLSAFKIVYIAPLKALVQEQVREFQRr 577
Cdd:PRK00254 23 ELYPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVN-----------KLLREGGKAVYLVPLKALAEEKYREFKD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 578 LAFLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSNNLaiVELVRLLIIDEIHLLHD-DRGPVLESIVARTFW 656
Cdd:PRK00254 91 WEKLGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRHGSSW--IKDVKLVVADEIHLIGSyDRGATLEMILTHMLG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 657 ASKygqeyprIIGLSATLPNYEDVGRFLRVPkeglfYFDSSFRPCPLSQqfcGIKERNSL----KKLKAMNDACYEKVLE 732
Cdd:PRK00254 169 RAQ-------ILGLSATVGNAEELAEWLNAE-----LVVSDWRPVKLRK---GVFYQGFLfwedGKIERFPNSWESLVYD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 733 SINEGNQIIVFVHSRKETSRTATWLKNKfaeenITHKLTKNDA-GSKQILKTEAANVLDPSLRKLIESGIGTHHAGLTRS 811
Cdd:PRK00254 234 AVKKGKGALVFVNTRRSAEKEALELAKK-----IKRFLTKPELrALKELADSLEENPTNEKLKKALRGGVAFHHAGLGRT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 812 DRSLSEDLFADGLLQVLVCTATLAWGVNLPAHTVIIKGTDVYSpEKGsWEQLSPQDVLQMLGRAGRPRYDTFGEGIII-- 889
Cdd:PRK00254 309 ERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYS-NFG-WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVat 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 890 TDQSN--VQYYL----SVLNQQLPIESQFVSKLVdnlnAEVVAGNIKCRNDAVNWLAYT-YLYVRMLASPMLYKVPDIss 962
Cdd:PRK00254 387 TEEPSklMERYIfgkpEKLFSMLSNESAFRSQVL----ALITNFGVSNFKELVNFLERTfYAHQRKDLYSLEEKAKEI-- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 963 dgqlkkfreslvhsaLCILKEQELVLYDAEnDVIEATDLGNIASSFYINHASMDVYN---RELDEHTTQIDLFRIFSMSE 1039
Cdd:PRK00254 461 ---------------VYFLLENEFIDIDLE-DRFIPLPLGIRTSQLYIDPLTAKKFKdafPKIEKNPNPLGIFQLIASTP 524
|
570 580
....*....|....*....|..
gi 6321020 1040 EFKYVSVRyeeKRELKQLLEKA 1061
Cdd:PRK00254 525 DMTPLNYS---RKEMEDLLDEA 543
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
482-1011 |
1.91e-54 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 205.19 E-value: 1.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 482 SLPDWCQEAFPSSETTSLNPIQSKVFHA-AFEGDsNMLICAPTGSGKTNIALLTVLKALshhynpktkklnLSAFKIVYI 560
Cdd:PRK02362 7 PLPEGVIEFYEAEGIEELYPPQAEAVEAgLLDGK-NLLAAIPTASGKTLIAELAMLKAI------------ARGGKALYI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 561 APLKALVQEQVREFQRrLAFLGIKVAELTG--DSR---LSRKQIdetqvLVSTPEKWDITTRNSNnlAIVELVRLLIIDE 635
Cdd:PRK02362 74 VPLRALASEKFEEFER-FEELGVRVGISTGdyDSRdewLGDNDI-----IVATSEKVDSLLRNGA--PWLDDITCVVVDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 636 IHLLHD-DRGPVLESIVArtfwasKYGQEYP--RIIGLSATLPNYEDVGRFLRV--------P---KEGLFYfDSSFRpC 701
Cdd:PRK02362 146 VHLIDSaNRGPTLEVTLA------KLRRLNPdlQVVALSATIGNADELADWLDAelvdsewrPidlREGVFY-GGAIH-F 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 702 PLSQQFCGIKERNSLKKLkamndacyekVLESINEGNQIIVFVHSRKETSRTATWLKNKFAEENITHKLTKNDAGSKQIL 781
Cdd:PRK02362 218 DDSQREVEVPSKDDTLNL----------VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 782 K---TEAANVLDPSlrklIESGIGTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLPAHTVIIKGTDVYSPEKG 858
Cdd:PRK02362 288 EvsdTETSKDLADC----VAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 859 sweqLSPQDVL---QMLGRAGRPRYDTFGEGIIITDQSN-----VQYYLSVLNQqlPIESQFVSK--LVDNLNAEVVAGN 928
Cdd:PRK02362 364 ----MQPIPVLeyhQMAGRAGRPGLDPYGEAVLLAKSYDeldelFERYIWADPE--DVRSKLATEpaLRTHVLSTIASGF 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 929 IKCRNDAVNWLAYTyLYVRmlaspmlykvpdissdgQLKKFR--ESLVHSALCILKEQELVLYDAENdvIEATDLGNIAS 1006
Cdd:PRK02362 438 ARTRDGLLEFLEAT-FYAT-----------------QTDDTGrlERVVDDVLDFLERNGMIEEDGET--LEATELGHLVS 497
|
....*
gi 6321020 1007 SFYIN 1011
Cdd:PRK02362 498 RLYID 502
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
511-1090 |
1.73e-50 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 192.02 E-value: 1.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 511 FEGDSNMLICAPTGSGKTNIALLTVLKALshhynpktkklnLSAFKIVYIAPLKALVQEQVREFQRrLAFLGIKVAELTG 590
Cdd:PRK01172 34 LRKGENVIVSVPTAAGKTLIAYSAIYETF------------LAGLKSIYIVPLRSLAMEKYEELSR-LRSLGMRVKISIG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 591 DSRLSRKQIDETQVLVSTPEKWDITTRNSNNlaIVELVRLLIIDEIHLLHD-DRGPVLESIVArtfwASKYGQEYPRIIG 669
Cdd:PRK01172 101 DYDDPPDFIKRYDVVILTSEKADSLIHHDPY--IINDVGLIVADEIHIIGDeDRGPTLETVLS----SARYVNPDARILA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 670 LSATLPNYEDVGRFLRVPkeglfYFDSSFRPCPL-------SQQFCGIKERNSLKKLKAmndacyekVLESINEGNQIIV 742
Cdd:PRK01172 175 LSATVSNANELAQWLNAS-----LIKSNFRPVPLklgilyrKRLILDGYERSQVDINSL--------IKETVNDGGQVLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 743 FVHSRKETSRTATWLKNKFAEENithkltkndagsKQILKTEAANVLDPSLRKLIESGIGTHHAGLTRSDRSLSEDLFAD 822
Cdd:PRK01172 242 FVSSRKNAEDYAEMLIQHFPEFN------------DFKVSSENNNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 823 GLLQVLVCTATLAWGVNLPAHTVIIKGTDVYSPEKGSWeqLSPQDVLQMLGRAGRPRYDTFGEGIIITDQSN----VQYY 898
Cdd:PRK01172 310 RYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRY--LSNMEIKQMIGRAGRPGYDQYGIGYIYAASPAsydaAKKY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 899 LSvlNQQLPIESQFVS--KLVDNLNAEVVAGNIKCRNDAVNWLAYTYLYVRMLASPMLYKvpdissdgqlkkfreslVHS 976
Cdd:PRK01172 388 LS--GEPEPVISYMGSqrKVRFNTLAAISMGLASSMEDLILFYNETLMAIQNGVDEIDYY-----------------IES 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 977 ALCILKEQELVlydAENDVIEATDLGNIASSFYINHASMDVYNRELDeHTTQIDLFrIFSMSEEFKYVSVRYEEKRELKQ 1056
Cdd:PRK01172 449 SLKFLKENGFI---KGDVTLRATRLGKLTSDLYIDPESALILKSAFD-HDYDEDLA-LYYISLCREIIPANTRDDYYAME 523
|
570 580 590
....*....|....*....|....*....|....
gi 6321020 1057 LLEKAPIpIREDIDdpLAKVNVLLQSYFSQLKFE 1090
Cdd:PRK01172 524 FLEDIGV-IDGDIS--AAKTAMVLRGWISEASMQ 554
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
509-884 |
3.42e-47 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 183.22 E-value: 3.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 509 AAFEGDSNMLICAPTGSGKTNIALLTVLKALSHhynpktkklnlsAFKIVYIAPLKALVQEQVREFQRRlaFLGIKVAEL 588
Cdd:COG4581 35 LALEAGRSVLVAAPTGSGKTLVAEFAIFLALAR------------GRRSFYTAPIKALSNQKFFDLVER--FGAENVGLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 589 TGDSRLSRkqidETQVLVSTPEKWD-ITTRNSNNLAIVELVrllIIDEIHLLHD-DRGPVLE-SIV---ARTfwaskygq 662
Cdd:COG4581 101 TGDASVNP----DAPIVVMTTEILRnMLYREGADLEDVGVV---VMDEFHYLADpDRGWVWEePIIhlpARV-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 663 eypRIIGLSATLPNYEDVGRFLR--------VpkeglfyfDSSFRPCPLSQQFCGIKERNSLKKLKAMNDACYE--KVLE 732
Cdd:COG4581 166 ---QLVLLSATVGNAEEFAEWLTrvrgetavV--------VSEERPVPLEFHYLVTPRLFPLFRVNPELLRPPSrhEVIE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 733 SINEGNQ--IIVFVHSRKETSRTATWLKNkfaeenitHKLTkNDAGSKQILKTEAANVLDPS------LRKLIESGIGTH 804
Cdd:COG4581 235 ELDRGGLlpAIVFIFSRRGCDEAAQQLLS--------ARLT-TKEERAEIREAIDEFAEDFSvlfgktLSRLLRRGIAVH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 805 HAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLPAHTVIIKGTDVYSPEKgsWEQLSPQDVLQMLGRAGRPRYDTFG 884
Cdd:COG4581 306 HAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGER--HRPLTAREFHQIAGRAGRRGIDTEG 383
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
499-695 |
3.97e-45 |
|
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: 162.04 E-value: 3.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 499 LNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHhyNPKTkklnlsafKIVYIAPLKALVQEQVREFQRRL 578
Cdd:cd18021 4 FNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQ--NPKG--------RAVYIAPMQELVDARYKDWRAKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 579 A-FLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSNNLAIVELVRLLIIDEIHLLHDDRGPVLESIVARTFWA 657
Cdd:cd18021 74 GpLLGKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYI 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 6321020 658 SKYGQEYPRIIGLSATLPNYEDVGRFLRVPKEGLFYFD 695
Cdd:cd18021 154 SSQLEKPIRIVGLSSSLANARDVGEWLGASKSTIFNFH 191
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1348-1535 |
1.96e-44 |
|
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: 160.23 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1348 FNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHWRQNKG-RAVYINPSGEKIDFLLSDWNKRFSHLAGGKIIn 1426
Cdd:cd18022 2 FNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGsKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1427 KLGNDPSLNLKLLAKSHVLLATPVQFELLSRRWRQRKNIQSLELMIYDDAHEISQGvYGAVYETLISRMIFIATQLEKKI 1506
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSD-RGPVLEVIVSRMNYISSQTEKPV 159
|
170 180
....*....|....*....|....*....
gi 6321020 1507 RFVCLSNCLANARDFGEWAGMTKSNIYNF 1535
Cdd:cd18022 160 RLVGLSTALANAGDLANWLGIKKMGLFNF 188
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
500-680 |
2.53e-41 |
|
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: 150.09 E-value: 2.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 500 NPIQSKVFHAAFEGDsNMLICAPTGSGKTNIALLTVLKALSHHYNPKtkklnlsafKIVYIAPLKALVQEQVREFQRRLA 579
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDKLDNGP---------QALVLAPTRELAEQIYEELKKLGK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 580 FLGIKV-AELTGDSRLS-RKQIDETQVLVSTPEKWDITTRNSNNLaivELVRLLIIDEIHLLHD-DRGPVLESIVARTfw 656
Cdd:pfam00270 71 GLGLKVaSLLGGDSRKEqLEKLKGPDILVGTPGRLLDLLQERKLL---KNLKLLVLDEAHRLLDmGFGPDLEEILRRL-- 145
|
170 180
....*....|....*....|....*
gi 6321020 657 askygQEYPRIIGLSATLP-NYEDV 680
Cdd:pfam00270 146 -----PKKRQILLLSATLPrNLEDL 165
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
498-684 |
1.57e-35 |
|
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: 134.00 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 498 SLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALshhynpktkklnLSAFKIVYIAPLKALVQEQVREFQRR 577
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTL------------LEGGKALYLVPLRALASEKYEEFKKL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 578 LAfLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSNNLaiVELVRLLIIDEIHLLHD-DRGPVLESIVARtfw 656
Cdd:cd18028 69 EE-IGLKVGISTGDYDEDDEWLGDYDIIVATYEKFDSLLRHSPSW--LRDVGVVVVDEIHLISDeERGPTLESIVAR--- 142
|
170 180
....*....|....*....|....*...
gi 6321020 657 ASKYGQEyPRIIGLSATLPNYEDVGRFL 684
Cdd:cd18028 143 LRRLNPN-TQIIGLSATIGNPDELAEWL 169
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
1348-1540 |
5.30e-33 |
|
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: 127.86 E-value: 5.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1348 FNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHWRQ------NKGRAVYINPS----GEKIDfllsDWNKRFS 1417
Cdd:cd18023 2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKErnplpwGNRKVVYIAPIkalcSEKYD----DWKEKFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1418 HLaGGKIINKLGNDPSLNLKLLAKSHVLLATPVQFELLSRRWRQRKN-IQSLELMIYDDAHEISQgVYGAVYETLISRM- 1495
Cdd:cd18023 78 PL-GLSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNGNlVQLVALVLIDEVHIIKE-NRGATLEVVVSRMk 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6321020 1496 -IFIATQLEKK----IRFVCLSNCLANARDFGEWAGMTKSNIYNFSPSER 1540
Cdd:cd18023 156 tLSSSSELRGStvrpMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFR 205
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
491-707 |
2.49e-30 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 119.90 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 491 FPSSETTSLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHHYNPKTkklnlsafkiVYIAPLKALVQEQ 570
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV----------LVLVPTRELAEQW 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 571 VREFQRRLAFLGIKVAELTGDS----RLSRKQIDETQVLVSTPEKWDITTRnsNNLAIVELVRLLIIDEIHLLHD-DRGP 645
Cdd:smart00487 71 AEELKKLGPSLGLKVVGLYGGDskreQLRKLESGKTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHRLLDgGFGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321020 646 VLESIVARTFWAskygqeyPRIIGLSATLPNYEDvgRFLRVPKEGLFYFDSSFRPCPLSQQF 707
Cdd:smart00487 149 QLEKLLKLLPKN-------VQLLLLSATPPEEIE--NLLELFLNDPVFIDVGFTPLEPIEQF 201
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
460-880 |
4.11e-29 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 126.93 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 460 YDEIhipAPSKPVID-YELKEItSLPDWCQEAFpSSETTSLNPIQSK-VFHAAFEGDsNMLICAPTGSGKTNIALLTVLK 537
Cdd:COG1202 175 FDEI---SATTDEVDtVPVDDL-DLPPELKDLL-EGRGEELLPVQSLaVENGLLEGK-DQLVVSATATGKTLIGELAGIK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 538 -ALSHHYnpktkklnlsafKIVYIAPLKALVQEQVREFQRRLAFlGIKVAELTGDSRLSRKQIDET---QVLVSTPEKWD 613
Cdd:COG1202 249 nALEGKG------------KMLFLVPLVALANQKYEDFKDRYGD-GLDVSIRVGASRIRDDGTRFDpnaDIIVGTYEGID 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 614 ITTRNSNNLAIVELVrllIIDEIHLLHD-DRGPVLESIVARTfwasKYGQEYPRIIGLSATLPNYEDVGRFLR---VPKE 689
Cdd:COG1202 316 HALRTGRDLGDIGTV---VIDEVHMLEDpERGHRLDGLIARL----KYYCPGAQWIYLSATVGNPEELAKKLGaklVEYE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 690 GlfyfdssfRPCPLSQQ--FCgiKERNslkKLKAMNDAC---YEKVLESINEGnQIIVFVHSRKEtsrtatwlknkfaee 764
Cdd:COG1202 389 E--------RPVPLERHltFA--DGRE---KIRIINKLVkreFDTKSSKGYRG-QTIIFTNSRRR--------------- 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 765 niTHKLTkndagskqilkteaanvldpslRKLiesGIGT--HHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLPA 842
Cdd:COG1202 440 --CHEIA----------------------RAL---GYKAapYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPA 492
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 6321020 843 HTVIIK----GTDvyspekgsWeqLSPQDVLQMLGRAGRPRY 880
Cdd:COG1202 493 SQVIFDslamGIE--------W--LSVQEFHQMLGRAGRPDY 524
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
514-684 |
5.40e-28 |
|
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: 111.91 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 514 DSNMLICAPTGSGKTNIALLTVLKALshhynpktKKLNLSAFKIVYIAPLKALVQEQVREFQRRLA--FLGIKVAELTGD 591
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSL--------ADEPEKGVQVLYISPLKALINDQERRLEEPLDeiDLEIPVAVRHGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 592 --SRLSRKQIDET-QVLVSTPEKWDI---TTRNSNNLAIVELVrllIIDEIH-LLHDDRGPVLESIVARTfwaSKYGQEY 664
Cdd:cd17922 73 tsQSEKAKQLKNPpGILITTPESLELllvNKKLRELFAGLRYV---VVDEIHaLLGSKRGVQLELLLERL---RKLTGRP 146
|
170 180
....*....|....*....|
gi 6321020 665 PRIIGLSATLPNYEDVGRFL 684
Cdd:cd17922 147 LRRIGLSATLGNLEEAAAFL 166
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1349-1521 |
2.34e-26 |
|
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: 107.33 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1349 NKIQSQVFESLYnSNDSVFVGSGKGTGKTAMAELALLNHWR--QNKGRAVYINPSGEKIDFLLSDWNKRFSHLaGGKIIN 1426
Cdd:pfam00270 1 TPIQAEAIPAIL-EGRDVLVQAPTGSGKTLAFLLPALEALDklDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1427 KLGNDP-SLNLKLLAKSHVLLATPvqfELLSRRWRQRKNIQSLELMIYDDAHEISQGVYGAVYETLISRmifiatqLEKK 1505
Cdd:pfam00270 79 LLGGDSrKEQLEKLKGPDILVGTP---GRLLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRR-------LPKK 148
|
170
....*....|....*..
gi 6321020 1506 IRFVCLSNCLA-NARDF 1521
Cdd:pfam00270 149 RQILLLSATLPrNLEDL 165
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
483-700 |
5.05e-26 |
|
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: 107.69 E-value: 5.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 483 LPDWCQEAFPSSETTSLNPIQSK-VFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALShhynpKTKKlnlsafKIVYIA 561
Cdd:cd18026 1 LPDAVREAYAKKGIKKLYDWQKEcLSLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRLL-----ERRK------KALFVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 562 PLKALVQEQVREFQRRLAFLGIKVAELTGDS-RLSRKQIDETQVLVSTPEKWD------ITTRNSNNLAIVelvrllIID 634
Cdd:cd18026 70 PYVSIVQEKVDALSPLFEELGFRVEGYAGNKgRSPPKRRKSLSVAVCTIEKANslvnslIEEGRLDELGLV------VVD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321020 635 EIHLLHD-DRGPVLESIVARTFWASKYGqeyPRIIGLSATLPNYEDVGRFLRVpkeglFYFDSSFRP 700
Cdd:cd18026 144 ELHMLGDgHRGALLELLLTKLLYAAQKN---IQIVGMSATLPNLEELASWLRA-----ELYTTNFRP 202
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
503-877 |
1.14e-23 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 109.15 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 503 QSKVFHAAFEGDsNMLICAPTGSGKTNIALLTVLKALSHHYNPKTkklnlsafkiVYIAPLKALVQEQVREFQR--RLAF 580
Cdd:COG1205 61 QAEAIEAARAGK-NVVIATPTASGKSLAYLLPVLEALLEDPGATA----------LYLYPTKALARDQLRRLRElaEALG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 581 LGIKVAELTGDSRLS-RKQI-DETQVLVSTP-----------EKWDITTRNsnnlaivelVRLLIIDEIHLLhddRGpVL 647
Cdd:COG1205 130 LGVRVATYDGDTPPEeRRWIrEHPDIVLTNPdmlhygllphhTRWARFFRN---------LRYVVIDEAHTY---RG-VF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 648 ESIVARTF-----WASKYGQEyPRIIGLSATLPNYED-----VGRFLRV---------PKEGLFYfdssfRPCPLSQQfc 708
Cdd:COG1205 197 GSHVANVLrrlrrICRHYGSD-PQFILASATIGNPAEhaerlTGRPVTVvdedgsprgERTFVLW-----NPPLVDDG-- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 709 gikERNSlkklkAMNDACYekVLES-INEGNQIIVFVHSRKETSRTATWLKNKFAEenithkltkndagskqilkteaan 787
Cdd:COG1205 269 ---IRRS-----ALAEAAR--LLADlVREGLRTLVFTRSRRGAELLARYARRALRE------------------------ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 788 vldPSLRKLIESgigtHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLPA-HTVIIKGtdvYSPekgsweqlSPQ 866
Cdd:COG1205 315 ---PDLADRVAA----YRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVVLAG---YPG--------TRA 376
|
410
....*....|.
gi 6321020 867 DVLQMLGRAGR 877
Cdd:COG1205 377 SFWQQAGRAGR 387
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1338-1870 |
2.43e-23 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 106.90 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1338 DFSEVFEFKTFNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHWRqNKGRAVYINPS----GEKidflLSDWN 1413
Cdd:COG1204 13 EFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALL-NGGKALYIVPLralaSEK----YREFK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1414 KRFSHLagGKIINKLGNDPSLNLKLLAKSHVLLATPVQFELLsrrWRQRKN-IQSLELMIYDDAHEISQGVYGAVYETLI 1492
Cdd:COG1204 88 RDFEEL--GIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSL---LRNGPSwLRDVDLVVVDEAHLIDDESRGPTLEVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1493 SRMIfiatQLEKKIRFVCLSNCLANARDFGEW--AGMTKSniyNFSPSERIEPLEI-NIQSFKDVEHISfnfsmLQMAFE 1569
Cdd:COG1204 163 ARLR----RLNPEAQIVALSATIGNAEEIAEWldAELVKS---DWRPVPLNEGVLYdGVLRFDDGSRRS-----KDPTLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1570 ASAAAAGNRNSSSVFLPSRKDCMEVASafmKFSKAIEWDMLNVEEEQIVPYIEKL--------TDGHLRAPLKHGVGILY 1641
Cdd:COG1204 231 LALDLLEEGGQVLVFVSSRRDAESLAK---KLADELKRRLTPEEREELEELAEELlevseethTNEKLADCLEKGVAFHH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1642 KGMASNDERIVKRLYEYGAVSVLliskdcsaFA-----------CKTdeVIIlgTNLYDGAEhkyMPYTINELLEMVGLA 1710
Cdd:COG1204 308 AGLPSELRRLVEDAFREGLIKVL--------VAtptlaagvnlpARR--VII--RDTKRGGM---VPIPVLEFKQMAGRA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1711 --SGNDSMaGKVLIL--TSHNMKAYYKKFLI-EPLPTESYL--QYIIHDTLNNEIANSIIQSKQDCVDWF--TYSYfyrr 1781
Cdd:COG1204 373 grPGYDPY-GEAILVakSSDEADELFERYILgEPEPIRSKLanESALRTHLLALIASGFANSREELLDFLenTFYA---- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1782 ihvnpsYYGVRDTsphgisvfLSNLVETCLNDLVESSFIEIDdteaevtaevnGGDDEATEIistlsnGLIASHYGVSFF 1861
Cdd:COG1204 448 ------YQYDKGD--------LEEVVDDALEFLLENGFIEED-----------GDRLRATKL------GKLVSRLYIDPL 496
|
....*....
gi 6321020 1862 TIQSFVSSL 1870
Cdd:COG1204 497 TAAELVDGL 505
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
485-876 |
1.29e-21 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 102.87 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 485 DWCQEAFpssetTSLNPIQSKVFHAAFEGDsNMLICAPTGSGKTNIALLTVLKALSHHYNPKTKKLNLsafKIVYIAPLK 564
Cdd:COG1201 16 AWFAARF-----GAPTPPQREAWPAIAAGE-STLLIAPTGSGKTLAAFLPALDELARRPRPGELPDGL---RVLYISPLK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 565 AL-------VQEQVREFQRR--LAFLGIKVAELTGD--SRLSRKQIDET-QVLVSTPEkwdittrnSnnLAIV------- 625
Cdd:COG1201 87 ALandiernLRAPLEEIGEAagLPLPEIRVGVRTGDtpASERQRQRRRPpHILITTPE--------S--LALLltspdar 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 626 EL---VRLLIIDEIHLLHDD-RGpV--------LESIVARTFwaskygqeypRIIGLSATLPNYEDVGRFLrVPKEGlfy 693
Cdd:COG1201 157 ELlrgVRTVIVDEIHALAGSkRG-VhlalslerLRALAPRPL----------QRIGLSATVGPLEEVARFL-VGYED--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 694 fdssFRPCPlsqqfcgIKERNSLKKLK------------------AMNDACYEKVLESINEGNQIIVFVHSRketsRTAt 755
Cdd:COG1201 222 ----PRPVT-------IVDAGAGKKPDlevlvpvedlierfpwagHLWPHLYPRVLDLIEAHRTTLVFTNTR----SQA- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 756 wlknkfaeENITHKLtkndagsKQILKTEAANvldpslrkliesgIGTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLA 835
Cdd:COG1201 286 --------ERLFQRL-------NELNPEDALP-------------IAAHHGSLSREQRLEVEEALKAGELRAVVATSSLE 337
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 6321020 836 WGVNLPA-HTVIikgtdvyspekgsweQL-SPQDV---LQMLGRAG 876
Cdd:COG1201 338 LGIDIGDvDLVI---------------QVgSPKSVarlLQRIGRAG 368
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
281-389 |
6.50e-21 |
|
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: 89.59 E-value: 6.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 281 ESVPIYSIDEFFLQRKLRSElgYKDTSVIQDLSEKILNDIETLEHNPVALEQKLVDLLKFENISLAEFILKNRSTIFWGI 360
Cdd:pfam18149 3 DSLDPHDIDAFWLQRLLSKF--YGDAIEAQKKAEEVLDILESAADDLRECENQLVELLDYDKFDLVKLLLKNRDKIVWCT 80
|
90 100 110
....*....|....*....|....*....|.
gi 6321020 361 RLAKS-TENEIPNLIEKMVAK-GLNDLVEQY 389
Cdd:pfam18149 81 KLARAqSEEEKQAIEEEMRSNpGLAWILDEL 111
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
501-877 |
1.11e-19 |
|
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: 96.47 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 501 PIQSKVFHAAFEGDSNMLIcAPTGSGKTNIALLTVLKALSHHYNPKTKKLnlsafKIVYIAPLKALVQEQVREFQRRLAF 580
Cdd:TIGR04121 16 PFQLEMWAAALEGRSGLLI-APTGSGKTLAGFLPSLIDLAGPEAPKEKGL-----HTLYITPLRALAVDIARNLQAPIEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 581 LG--IKVAELTGDSRLSRKQIDET---QVLVSTPEKWDITTRNSNNLAIVELVRLLIIDEIH-LLHDDRGPVLESIVAR- 653
Cdd:TIGR04121 90 LGlpIRVETRTGDTSSSERARQRKkppDILLTTPESLALLLSYPDAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 654 TFWASKYgqeypRIIGLSATLPNYEDVGRFLrVPKEGlfyfdssfRPCPLSQQFCG--IKERNSLKK------------L 719
Cdd:TIGR04121 170 RRLAPGL-----RRWGLSATIGNLEEARRVL-LGVGG--------APAVLVRGKLPkaIEVISLLPEseerfpwaghlgL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 720 KAMndacyEKVLESINEGNQIIVFVHSRKETSRT--ATWLKNkfAEENIThkltkndagskqilkteaanvldpslrkli 797
Cdd:TIGR04121 236 RAL-----PEVYAEIDQARTTLVFTNTRSQAELWfqALWEAN--PEFALP------------------------------ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 798 esgIGTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVN-LPAHTVIIKGtdvyspekgsweqlSPQDVLQMLGRAG 876
Cdd:TIGR04121 279 ---IALHHGSLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDfGPVDLVIQIG--------------SPKGVARLLQRAG 341
|
.
gi 6321020 877 R 877
Cdd:TIGR04121 342 R 342
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
515-673 |
1.42e-19 |
|
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: 87.07 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 515 SNMLICAPTGSGKTNIALLTVLKAlshhynpktkkLNLSAFKIVYIAPLKALVQEQVREFqRRLAFLGIKVAELTGDS-- 592
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLL-----------LLKKGKKVLVLVPTKALALQTAERL-RELFGPGIRVAVLVGGSsa 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 593 -RLSRKQIDETQVLVSTPEKwdITTRNSNNLAIVEL-VRLLIIDEIH-LLHDDRGPVLESIVARtfwasKYGQEYPRIIG 669
Cdd:cd00046 70 eEREKNKLGDADIIIATPDM--LLNLLLREDRLFLKdLKLIIVDEAHaLLIDSRGALILDLAVR-----KAGLKNAQVIL 142
|
....
gi 6321020 670 LSAT 673
Cdd:cd00046 143 LSAT 146
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
490-768 |
9.60e-18 |
|
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: 89.37 E-value: 9.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 490 AFPSSETTSLNPIQSKVFHAAFEGDSN----MLICAPTGSGKTNIALLTVLKALSHHYNPktkklnlsafKIVYIAPLKA 565
Cdd:COG1203 119 PKKSKPRTPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKHGGR----------RIIYALPFTS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 566 LVqEQVreFQRRLAFLGIKVAELTGDSRLSRKQIDE-----TQVLVSTPEKWD----ITT-----------RNSNNLAIV 625
Cdd:COG1203 189 II-NQT--YDRLRDLFGEDVLLHHSLADLDLLEEEEeyeseARWLKLLKELWDapvvVTTidqlfeslfsnRKGQERRLH 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 626 ELVR-LLIIDEIHLLHDDRGPVLESIVArtfWASKYGQeypRIIGLSATLPNYEdvgrflrvpKEGLFYF-----DSSFR 699
Cdd:COG1203 266 NLANsVIILDEVQAYPPYMLALLLRLLE---WLKNLGG---SVILMTATLPPLL---------REELLEAyelipDEPEE 330
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321020 700 PCPLSQQFcgIKERNSLKKLKAMNDACYEKVLESINEGNQIIVFVHSRKETSRTATWLKNKFAEENITH 768
Cdd:COG1203 331 LPEYFRAF--VRKRVELKEGPLSDEELAELILEALHKGKSVLVIVNTVKDAQELYEALKEKLPDEEVYL 397
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
498-673 |
5.03e-17 |
|
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: 81.71 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 498 SLNPIQSKVFHAAFEGdSNMLICAPTGSGKTNIALLtvlkaLSHHYNPKTKKLNLSafKIVYIAPLKALVQEQVREFQRR 577
Cdd:cd17927 2 KPRNYQLELAQPALKG-KNTIICLPTGSGKTFVAVL-----ICEHHLKKFPAGRKG--KVVFLANKVPLVEQQKEVFRKH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 578 LAFLGIKVAELTGDSRL---SRKQIDETQVLVSTPEkwdITTRNSNNLAIVEL--VRLLIIDEIHLLHDDrGPVLEsiVA 652
Cdd:cd17927 74 FERPGYKVTGLSGDTSEnvsVEQIVESSDVIIVTPQ---ILVNDLKSGTIVSLsdFSLLVFDECHNTTKN-HPYNE--IM 147
|
170 180
....*....|....*....|...
gi 6321020 653 RTFWASKYG--QEYPRIIGLSAT 673
Cdd:cd17927 148 FRYLDQKLGssGPLPQILGLTAS 170
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
473-889 |
2.62e-16 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 85.71 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 473 IDYELKEITS------LPDWCQEAFpSSETTSLNPIQSKVFHAAFEGDsNMLICAPTGSGKTNIALLTVLKALSHHynPK 546
Cdd:PRK13767 2 IEYATKEYSDeeildlLRPYVREWF-KEKFGTFTPPQRYAIPLIHEGK-NVLISSPTGSGKTLAAFLAIIDELFRL--GR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 547 TKKLNLSAFkIVYIAPLKAL-------VQEQVREFQRRLAFLG-----IKVAELTGDSRLSRKQ--IDET-QVLVSTPEk 611
Cdd:PRK13767 78 EGELEDKVY-CLYVSPLRALnndihrnLEEPLTEIREIAKERGeelpeIRVAIRTGDTSSYEKQkmLKKPpHILITTPE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 612 wdittrnsnNLAIV----------ELVRLLIIDEIHLLHDD-RG-------PVLESIVartfwaskyGQEYPRiIGLSAT 673
Cdd:PRK13767 156 ---------SLAILlnspkfreklRTVKWVIVDEIHSLAENkRGvhlslslERLEELA---------GGEFVR-IGLSAT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 674 LPNYEDVGRFLrvpkeGLFYFDSSFRPCPlsqqfcgIKERNSLKKL----------------KAMNDACYEKVLESINEG 737
Cdd:PRK13767 217 IEPLEEVAKFL-----VGYEDDGEPRDCE-------IVDARFVKPFdikvispvddlihtpaEEISEALYETLHELIKEH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 738 NQIIVFVHSRKETSRTATWLKNKFAEEnithkltkndagskqilkteaanvldpslrkLIESGIGTHHAGLTRSDRSLSE 817
Cdd:PRK13767 285 RTTLIFTNTRSGAERVLYNLRKRFPEE-------------------------------YDEDNIGAHHSSLSREVRLEVE 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321020 818 DLFADGLLQVLVCTATLAWGVNLPAHTVIIkgtdvyspekgsweQL-SPQDV---LQMLGRAGRpRYDTFGEGIII 889
Cdd:PRK13767 334 EKLKRGELKVVVSSTSLELGIDIGYIDLVV--------------LLgSPKSVsrlLQRIGRAGH-RLGEVSKGRII 394
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1341-1546 |
6.25e-16 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 78.30 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1341 EVFEFKTFNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHW-RQNKGRAVYINPSGEKIDFLLSDWNKRFSHL 1419
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALkRGKGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1420 aGGKIINKLGNDPS---LNLKLLAKSHVLLATPVQFELLSRRWrqRKNIQSLELMIYDDAHEISQGVYGAVYETLISRmi 1496
Cdd:smart00487 82 -GLKVVGLYGGDSKreqLRKLESGKTDILVTTPGRLLDLLEND--KLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKL-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6321020 1497 fiatqLEKKIRFVCLSNCLANARDFGEWAGMtkSNIYNFSPSERI-EPLEI 1546
Cdd:smart00487 157 -----LPKNVQLLLLSATPPEEIENLLELFL--NDPVFIDVGFTPlEPIEQ 200
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
503-676 |
6.44e-16 |
|
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: 78.01 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 503 QSKVFHAAFEGdSNMLICAPTGSGKTNIALLTVLKALSHHYNPKTkklnlsafkiVYIAPLKALVQEQVREFQRRLA--F 580
Cdd:cd17923 5 QAEAIEAARAG-RSVVVTTGTASGKSLCYQLPILEALLRDPGSRA----------LYLYPTKALAQDQLRSLRELLEqlG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 581 LGIKVAELTGDSRLSRKQ---IDETQVLVSTPEKWDIT-TRNSNNLA-IVELVRLLIIDEIHLLhddRGpVLESIVA--- 652
Cdd:cd17923 74 LGIRVATYDGDTPREERRaiiRNPPRILLTNPDMLHYAlLPHHDRWArFLRNLRYVVLDEAHTY---RG-VFGSHVAlll 149
|
170 180
....*....|....*....|....*
gi 6321020 653 -RTFWASKYGQEYPRIIGLSATLPN 676
Cdd:cd17923 150 rRLRRLCRRYGADPQFILTSATIGN 174
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
800-878 |
7.90e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 71.47 E-value: 7.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 800 GIGTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLP-AHTVIIKGTDvyspekgsweqLSPQDVLQMLGRAGRP 878
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDLP-----------WSPASYIQRIGRAGRA 81
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
503-672 |
1.30e-14 |
|
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: 74.61 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 503 QSKVFHAAFegDSNMLICAPTGSGKTNIALLtVLKALSH--HYNPKTKKLnlsafkIVYIAPLKALVQEQVREFQRrlaF 580
Cdd:cd18034 7 QLELFEAAL--KRNTIVVLPTGSGKTLIAVM-LIKEMGElnRKEKNPKKR------AVFLVPTVPLVAQQAEAIRS---H 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 581 LGIKVAELTGDSRLS--RKQ-----IDETQVLVSTPEkwdiTTRN--SNNLAIVELVRLLIIDEIHL---LHDDRGpvle 648
Cdd:cd18034 75 TDLKVGEYSGEMGVDkwTKErwkeeLEKYDVLVMTAQ----ILLDalRHGFLSLSDINLLIFDECHHatgDHPYAR---- 146
|
170 180
....*....|....*....|....
gi 6321020 649 siVARTFWASKYGQEYPRIIGLSA 672
Cdd:cd18034 147 --IMKEFYHLEGRTSRPRILGLTA 168
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
1347-1527 |
1.94e-14 |
|
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: 73.52 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1347 TFNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHWRQNkGRAVYINP----SGEKI-DFllSDWNKRfshlaG 1421
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEG-GKALYLVPlralASEKYeEF--KKLEEI-----G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1422 GKIINKLGNDPSlNLKLLAKSHVLLATpvqFELLSRRWRQRKN-IQSLELMIYDDAHEISQGVYGAVYETLISRMifiaT 1500
Cdd:cd18028 73 LKVGISTGDYDE-DDEWLGDYDIIVAT---YEKFDSLLRHSPSwLRDVGVVVVDEIHLISDEERGPTLESIVARL----R 144
|
170 180
....*....|....*....|....*..
gi 6321020 1501 QLEKKIRFVCLSNCLANARDFGEWAGM 1527
Cdd:cd18028 145 RLNPNTQIIGLSATIGNPDELAEWLNA 171
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
493-1052 |
3.42e-14 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.14 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 493 SSETTSLNPIQSKVFHAAFE----GDSNMLICAPTGSGKTNIAlltvLKALSHHYNPKtkklnlsafKIVYIAPLKALVQ 568
Cdd:COG1061 75 SGTSFELRPYQQEALEALLAalerGGGRGLVVAPTGTGKTVLA----LALAAELLRGK---------RVLVLVPRRELLE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 569 EQVREFQRRLaflgiKVAELTGDsrlsRKQIDEtQVLVSTpekWDITTRNSNNLAIVELVRLLIIDEIHLLhddRGPVLE 648
Cdd:COG1061 142 QWAEELRRFL-----GDPLAGGG----KKDSDA-PITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHA---GAPSYR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 649 SIVARTfwaskygqEYPRIIGLSATlPNYEDVGRflrvpkeglfyfdssfrpcPLSQQFCGIKERNSLKKLkamndacye 728
Cdd:COG1061 206 RILEAF--------PAAYRLGLTAT-PFRSDGRE-------------------ILLFLFDGIVYEYSLKEA--------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 729 kvlesINEGN--QIIVFVHSRKETSRTATWLKnkfAEENITHKLTKNDAGSKQILKTEAANVLDPS-------------- 792
Cdd:COG1061 249 -----IEDGYlaPPEYYGIRVDLTDERAEYDA---LSERLREALAADAERKDKILRELLREHPDDRktlvfcssvdhaea 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 793 -LRKLIESGIGTH--HAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLPAHTVIIkgtdVYSPEKgsweqlSPQDVL 869
Cdd:COG1061 321 lAELLNEAGIRAAvvTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI----LLRPTG------SPREFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 870 QMLGRAGRPRYDtfGEGIIITDqsnvqyylsVLNQQLPIESQFVSKLVDNLNAEVVAGNIKCRNDAVNwlAYTYLYVRML 949
Cdd:COG1061 391 QRLGRGLRPAPG--KEDALVYD---------FVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELAL--LIAVKPALEV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 950 ASPMLYKVPDISSDGQLKKFRESLVHSALCILKEQELVLYDAENDVIEATDLGNIASSFYINHASMDVYNRELDEHTTQI 1029
Cdd:COG1061 458 KGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLE 537
|
570 580
....*....|....*....|...
gi 6321020 1030 DLFRIFSMSEEFKYVSVRYEEKR 1052
Cdd:COG1061 538 LLELLAALLRLEELAALLLKELL 560
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
499-675 |
5.43e-14 |
|
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: 72.89 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 499 LNPIQSKVFHAAFEGdSNMLICAPTGSGKTNIALLTVLkalsHHYNPKTKKLNLSafKIVYIAPLKALVQEQVREFQRRL 578
Cdd:cd18036 3 LRNYQLELVLPALRG-KNTIICAPTGSGKTRVAVYICR----HHLEKRRSAGEKG--RVVVLVNKVPLVEQQLEKFFKYF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 579 AfLGIKVAELTGDSRLS---RKQIDETQVLVSTPEkwdITTRNSNNLAIVELVR-----LLIIDEIHllHDDRGPVLESI 650
Cdd:cd18036 76 R-KGYKVTGLSGDSSHKvsfGQIVKASDVIICTPQ---ILINNLLSGREEERVYlsdfsLLIFDECH--HTQKEHPYNKI 149
|
170 180
....*....|....*....|....*.
gi 6321020 651 VARTF-WASKYGQEYPRIIGLSATLP 675
Cdd:cd18036 150 MRMYLdKKLSSQGPLPQILGLTASPG 175
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1347-1520 |
6.06e-13 |
|
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: 69.77 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1347 TFNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHWRQNKGRAVYINPSGEKIDF----------LLSDWNKRF 1416
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQGGVIKKDDFKIVYiapmkalaaeMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1417 SHLagGKIINKLGNDPSLNLKLLAKSHVLLATPVQFELLSRRWRQRKNIQSL-ELMIYDDAHeISQGVYGAVYETLISRM 1495
Cdd:cd18020 81 APL--GIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLvRLLIIDEVH-LLHDDRGPVIESLVART 157
|
170 180
....*....|....*....|....*
gi 6321020 1496 IFIATQLEKKIRFVCLSNCLANARD 1520
Cdd:cd18020 158 LRQVESTQSMIRIVGLSATLPNYLD 182
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
1341-1522 |
9.92e-13 |
|
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: 69.32 E-value: 9.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1341 EVFE-FKTFNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLN----HWRQNKG------RAVYINPSGEKIDFLL 1409
Cdd:cd18019 10 PAFEgFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILReigkHRNPDGTinldafKIVYIAPMKALVQEMV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1410 SDWNKRFSHLagGKIINKLGNDPSLNLKLLAKSHVLLATPVQFELLSRRWRQRKNIQSLELMIYDDAHEISQGvYGAVYE 1489
Cdd:cd18019 90 GNFSKRLAPY--GITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDD-RGPVLE 166
|
170 180 190
....*....|....*....|....*....|...
gi 6321020 1490 TLISRMIFIATQLEKKIRFVCLSNCLANARDFG 1522
Cdd:cd18019 167 SIVARTIRQIEQTQEYVRLVGLSATLPNYEDVA 199
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
519-876 |
2.30e-11 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 69.57 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 519 ICAPTGSGKTNIALLTVLKALSHHYNPKTKKLN-LSAFKIVYIAPLKAL---VQEQVR--------EFQRR-LAFLGIKV 585
Cdd:PRK09751 1 VIAPTGSGKTLAAFLYALDRLFREGGEDTREAHkRKTSRILYISPIKALgtdVQRNLQiplkgiadERRRRgETEVNLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 586 AELTGD------SRLSRKQIDetqVLVSTPEK--WDITTRNSNNLAIVELVrllIIDEIHllhddrgpvlesIVARTFWA 657
Cdd:PRK09751 81 GIRTGDtpaqerSKLTRNPPD---ILITTPESlyLMLTSRARETLRGVETV---IIDEVH------------AVAGSKRG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 658 SKYGQEYPRI----------IGLSATLPNYEDVGRFLRVPKEGLFYFDSSFR--------PCP----LSQQFCGIKERNS 715
Cdd:PRK09751 143 AHLALSLERLdallhtsaqrIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRhpqirivvPVAnmddVSSVASGTGEDSH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 716 LKKLKAMNDACYEKVLESINEGNQIIVFVHSRKETSRTATWLKNKFAE---------ENITHklTKNDAGSKQILKTEAa 786
Cdd:PRK09751 223 AGREGSIWPYIETGILDEVLRHRSTIVFTNSRGLAEKLTARLNELYAArlqrspsiaVDAAH--FESTSGATSNRVQSS- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 787 nvlDPSLRKliesgigTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLPAHTVIIKgtdVYSPekgsweqLSPQ 866
Cdd:PRK09751 300 ---DVFIAR-------SHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQ---VATP-------LSVA 359
|
410
....*....|
gi 6321020 867 DVLQMLGRAG 876
Cdd:PRK09751 360 SGLQRIGRAG 369
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
497-689 |
3.38e-11 |
|
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: 64.39 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 497 TSLNPIQSKVFHAAFEGdSNMLICAPTGSGKTnIA-LLTVLKALShhynpKTKKLNLSAFKIVYIAPLKALVQeQV-REF 574
Cdd:cd00268 11 EKPTPIQAQAIPLILSG-RDVIGQAQTGSGKT-LAfLLPILEKLL-----PEPKKKGRGPQALVLAPTRELAM-QIaEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 575 QRRLAFLGIKVAELTGDSRLsRKQIDE----TQVLVSTPEK-WDITTRNSNNLaivELVRLLIIDEI-HLLHDDRGPVLE 648
Cdd:cd00268 83 RKLGKGTGLKVAAIYGGAPI-KKQIEAlkkgPDIVVGTPGRlLDLIERGKLDL---SNVKYLVLDEAdRMLDMGFEEDVE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6321020 649 SIVARTfwaskygQEYPRIIGLSATLPNY--EDVGRFLRVPKE 689
Cdd:cd00268 159 KILSAL-------PKDRQTLLFSATLPEEvkELAKKFLKNPVR 194
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
514-677 |
4.08e-11 |
|
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: 64.23 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 514 DSNMLICAPTGSGKTNIALLTVLKALSHHYNPktkklnlsafKIVYIAPLKALVQEQVREFQRRLAFLGI--KVAELTGD 591
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWALKLAARGGKR----------RIIYALPTRATINQMYERIREILGRLDDedKVLLLHSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 592 SRLSRKQIDE---------TQVLVSTPEKWD----ITT----------RNSNNLAIVELVR-LLIIDEIHLLhDDR--GP 645
Cdd:cd17930 71 AALELLESDEepdddpveaVDWALLLKRSWLapivVTTidqllesllkYKHFERRLHGLANsVVVLDEVQAY-DPEymAL 149
|
170 180 190
....*....|....*....|....*....|..
gi 6321020 646 VLESIVartFWASKYGQeypRIIGLSATLPNY 677
Cdd:cd17930 150 LLKALL---ELLGELGG---PVVLMTATLPAL 175
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
514-679 |
6.71e-11 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 67.83 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 514 DSNMLICAPTGSGKTNIALLTVLKALShhynpKTKKlnlsafKIVYIAPLKALVQEQVREFQRRLAFLGIKVAELTGDSR 593
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAERLH-----KKGG------KVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 594 LS-RKQI-DETQVLVSTPEkwdiTTRNSNNLAIVEL--VRLLIIDEIHllhddRGpvlesiV---ARTFWASKYGQEY-- 664
Cdd:COG1111 86 PEkRKELwEKARIIVATPQ----VIENDLIAGRIDLddVSLLIFDEAH-----RA------VgnyAYVYIAERYHEDAkd 150
|
170
....*....|....*
gi 6321020 665 PRIIGLSATLPNYED 679
Cdd:COG1111 151 PLILGMTASPGSDEE 165
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1339-1536 |
3.94e-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: 61.13 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1339 FSEVFEFKTFNKIQSQVFESlynsNDSVFVGSGKGTGKTAMAELAL-LNHwrQNKGRAVYINPSGEKIDFLLSDWNKRFS 1417
Cdd:cd18027 3 FKWPFELDVFQKQAILHLEA----GDSVFVAAHTSAGKTVVAEYAIaLAQ--KHMTRTIYTSPIKALSNQKFRDFKNTFG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1418 HlaggkiINKLGNDPSLNLKllaKSHVLLATPVqfeLLSRRWRQRKNIQSLELMIYDDAHEISQGVYGAVYETLIsrmif 1497
Cdd:cd18027 77 D------VGLITGDVQLNPE---ASCLIMTTEI---LRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVL----- 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6321020 1498 iaTQLEKKIRFVCLSNCLANARDFGEWAGMTKS-NIYNFS 1536
Cdd:cd18027 140 --IMLPDHVSIILLSATVPNTVEFADWIGRIKKkNIYVIS 177
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
499-676 |
2.32e-09 |
|
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: 58.82 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 499 LNPIQSKVFHAAFEGDSnMLICAPTGSGKTNIALLTVlkALSHHYNPKTkklnlsafkiVYIAPLKALVQEQVREFQRRL 578
Cdd:cd18027 9 LDVFQKQAILHLEAGDS-VFVAAHTSAGKTVVAEYAI--ALAQKHMTRT----------IYTSPIKALSNQKFRDFKNTF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 579 AFLGIkvaeLTGDSRLSrkqiDETQVLVSTPEKWDITTRNSNNLaiVELVRLLIIDEIHLLHD-DRGPVLESIVARTfwa 657
Cdd:cd18027 76 GDVGL----ITGDVQLN----PEASCLIMTTEILRSMLYNGSDV--IRDLEWVIFDEVHYINDaERGVVWEEVLIML--- 142
|
170
....*....|....*....
gi 6321020 658 skygQEYPRIIGLSATLPN 676
Cdd:cd18027 143 ----PDHVSIILLSATVPN 157
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
514-684 |
3.04e-09 |
|
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: 58.92 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 514 DSNMLICAPTGSGKTNI---ALLTVLKALSHHYnpktkklnlsafkIVYIAPLKALVQEQVRE----FQRRLAFLGIKV- 585
Cdd:cd18025 16 RESALIVAPTSSGKTFIsyyCMEKVLRESDDGV-------------VVYVAPTKALVNQVVAEvyarFSKKYPPSGKSLw 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 586 AELTGDSRLsrKQIDETQVLVSTPEKWDITTRNSNNLAIVELVRLLIIDEIHLL-HDDRGPVLESIVARTfwaskygqEY 664
Cdd:cd18025 83 GVFTRDYRH--NNPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIgQSEDGAVWEQLLLLI--------PC 152
|
170 180
....*....|....*....|
gi 6321020 665 PrIIGLSATLPNYEDVGRFL 684
Cdd:cd18025 153 P-FLALSATIGNPQKFHEWL 171
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
514-672 |
4.49e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 61.81 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 514 DSNMLICAPTGSGKTNIALLTVLKALshHYNPKtkklnlsafKIVYIAPLKALVQEQVREFQRRLAFLGIKVAELTGD-S 592
Cdd:PRK13766 29 KKNTLVVLPTGLGKTAIALLVIAERL--HKKGG---------KVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEvS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 593 RLSRKQI-DETQVLVSTPE--KWDI-TTRNSnnlaiVELVRLLIIDEIHllhddRGpvlesiV---ARTFWASKYGQE-- 663
Cdd:PRK13766 98 PEKRAELwEKAKVIVATPQviENDLiAGRIS-----LEDVSLLIFDEAH-----RA------VgnyAYVYIAERYHEDak 161
|
....*....
gi 6321020 664 YPRIIGLSA 672
Cdd:PRK13766 162 NPLVLGLTA 170
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
512-673 |
1.23e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 56.14 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 512 EGDSNMLICAPTGSGKTNIALLTVLKALSHHYnpktkklnlsAFKIVYIAPLKALVQEQVREFQRRLAFLGIKVAELTGD 591
Cdd:pfam04851 21 NGQKRGLIVMATGSGKTLTAAKLIARLFKKGP----------IKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 592 SRLSRKqiDETQVLVSTPEKWDITTRNSNNLAIVELVRLLIIDEIHllhddRGPvlesivartfwASKYGQ-----EYPR 666
Cdd:pfam04851 91 KKDESV--DDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH-----RSG-----------ASSYRNileyfKPAF 152
|
....*..
gi 6321020 667 IIGLSAT 673
Cdd:pfam04851 153 LLGLTAT 159
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
727-877 |
1.54e-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: 55.73 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 727 YEKVLESINEGNQIIVFVHSRKETSRTATWLKNKFAEENITHKltkndagskqilkteaanvldpslrkliesgIGTHHA 806
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRVPPDF-------------------------------IALHHG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321020 807 GLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLPA-HTVIikgtdvyspekgsweQL-SPQDV---LQMLGRAGR 877
Cdd:cd18796 77 SLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDvDLVI---------------QIgSPKSVarlLQRLGRSGH 137
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
497-635 |
1.57e-08 |
|
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: 57.26 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 497 TSLNPIQSKVFHAA----------FEGDsnMLICAPTGSGKTNIALLTVLKALSHHYNPKTKKLnlsafkIVyiAPLKAL 566
Cdd:cd17956 11 TSAFPVQAAVIPWLlpsskstppyRPGD--LCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRAL------IV--VPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 567 VQEQVREFQRRLAFLGIKVAELTGDSRLSRKQ-----------IDETQVLVSTPekwditTR-----NSNNLAIVELVRL 630
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQklllvdtsgryLSRVDILVATP------GRlvdhlNSTPGFTLKHLRF 154
|
....*
gi 6321020 631 LIIDE 635
Cdd:cd17956 155 LVIDE 159
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
793-877 |
1.67e-08 |
|
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: 54.14 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 793 LRKLIESGIGTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLP-AHTVIIkgtdvYSPEKgsweqlSPQDVLQM 871
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YDLPW------NPASYIQR 101
|
....*.
gi 6321020 872 LGRAGR 877
Cdd:pfam00271 102 IGRAGR 107
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
516-635 |
1.72e-08 |
|
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: 56.83 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 516 NMLICAPTGSGKTnIALLtvLKALSHHYNPKTKKlnlsAFKIVYIAPLKALVQEQVREFQRRLAFLGIKVAELTG----- 590
Cdd:cd17957 29 DLLACAPTGSGKT-LAFL--IPILQKLGKPRKKK----GLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKsleak 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 6321020 591 --DSRLSRKQIDetqVLVSTPEKwdITTRNSNNLAIVELVRLLIIDE 635
Cdd:cd17957 102 akDGPKSITKYD---ILVSTPLR--LVFLLKQGPIDLSSVEYLVLDE 143
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
503-637 |
2.76e-08 |
|
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: 56.37 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 503 QSKVFHAAFEGdSNMLICAPTGSGKTNIALLTVlkalSHHYN--PKTKKLnlsafKIVYIAPLKALVQEQVREFQRRLAF 580
Cdd:cd18073 7 QLELALPAMKG-KNTIICAPTGCGKTFVSLLIC----EHHLKkfPQGQKG-----KVVFFATKVPVYEQQKSVFSKYFER 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321020 581 LGIKVAELTGD--SRLSRKQ-IDETQVLVSTPEkwdITTRNSNNLAI--VELVRLLIIDEIH 637
Cdd:cd18073 77 HGYRVTGISGAtaENVPVEQiIENNDIIILTPQ---ILVNNLKKGTIpsLSIFTLMIFDECH 135
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
515-673 |
5.13e-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: 55.02 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 515 SNMLICAPTGSGKTNIAlLTVLkalshhYN-----PKTkklnlsafKIVYIAPLKALVQEQVREFQRrlaFLGI---KVA 586
Cdd:cd18033 17 QNTLVALPTGLGKTFIA-AVVM------LNyyrwfPKG--------KIVFMAPTKPLVSQQIEACYK---ITGIpssQTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 587 ELTG-DSRLSRKQIDET-QVLVSTPEkwdiTTRN--SNNLAIVELVRLLIIDEIHllhddRGP-------VLESIVARTF 655
Cdd:cd18033 79 ELTGsVPPTKRAELWASkRVFFLTPQ----TLENdlKEGDCDPKSIVCLVIDEAH-----RATgnyaycqVVRELMRYNS 149
|
170
....*....|....*...
gi 6321020 656 WAskygqeypRIIGLSAT 673
Cdd:cd18033 150 HF--------RILALTAT 159
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
499-676 |
1.01e-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: 54.76 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 499 LNPIQSKVFhAAFEGDSNMLICAPTGSGKTNIALLTVLKALshhynpKTKKlnlsafKIVYIAPLKALVQEQVREFQRRL 578
Cdd:cd18024 33 LDPFQKTAI-ACIERNESVLVSAHTSAGKTVVAEYAIAQSL------RDKQ------RVIYTSPIKALSNQKYRELQEEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 579 AFLGIkvaeLTGDSRLSrkqiDETQVLVSTPEKW-DITTRNSNnlaIVELVRLLIIDEIHLLHD-DRGPVL-ESIVArtf 655
Cdd:cd18024 100 GDVGL----MTGDVTIN----PNASCLVMTTEILrSMLYRGSE---IMREVAWVIFDEIHYMRDkERGVVWeETIIL--- 165
|
170 180
....*....|....*....|....
gi 6321020 656 waskygqeYP---RIIGLSATLPN 676
Cdd:cd18024 166 --------LPdkvRYVFLSATIPN 181
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
518-674 |
3.03e-07 |
|
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: 51.92 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 518 LICAPTGSGKTNIALltvlkALShhynpktkkLNLSAFKIVYIAPLKALVQEQVREFQRrlAFLGIKVAELTGDsrlSRK 597
Cdd:cd17926 22 ILVLPTGSGKTLTAL-----ALI---------AYLKELRTLIVVPTDALLDQWKERFED--FLGDSSIGLIGGG---KKK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321020 598 QIDETQVLVSTPEKwdITTRNSNNLAIVELVRLLIIDEIHllhddRGPvlesivARTFWASKYGQEYPRIIGLSATL 674
Cdd:cd17926 83 DFDDANVVVATYQS--LSNLAEEEKDLFDQFGLLIVDEAH-----HLP------AKTFSEILKELNAKYRLGLTATP 146
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
499-673 |
4.44e-07 |
|
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: 52.13 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 499 LNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALshhynpkTKKlnlsAFKIVYIAPLKALVqEQVREFQRRL 578
Cdd:cd18035 1 EERRLYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRL-------TKK----GGKVLILAPSRPLV-EQHAENLKRV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 579 AFLGIKVAELTGDSRL-SRKQI-DETQVLVSTPEkwdiTTRNS--NNLAIVELVRLLIIDEIHLLHDDRgpvlesivART 654
Cdd:cd18035 69 LNIPDKITSLTGEVKPeERAERwDASKIIVATPQ----VIENDllAGRITLDDVSLLIFDEAHHAVGNY--------AYV 136
|
170 180
....*....|....*....|.
gi 6321020 655 FWASKYGQEY--PRIIGLSAT 673
Cdd:cd18035 137 YIAHRYKREAnnPLILGLTAS 157
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
498-675 |
3.10e-06 |
|
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: 50.23 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 498 SLNPIQSKVFHAAFEGdSNMLICAPTGSGKTniaLLTVLKALshhYNPKTKklnlsafkIVyIAPLKALVQEQVREFQRr 577
Cdd:cd17920 12 EFRPGQLEAINAVLAG-RDVLVVMPTGGGKS---LCYQLPAL---LLDGVT--------LV-VSPLISLMQDQVDRLQQ- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 578 lafLGIKVAELTgdSRLSRKQIDETQ----------VLVsTPEK-WDITTRNS-NNLAIVELVRLLIIDEIHLL----HD 641
Cdd:cd17920 75 ---LGIRAAALN--STLSPEEKREVLlrikngqyklLYV-TPERlLSPDFLELlQRLPERKRLALIVVDEAHCVsqwgHD 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6321020 642 DRgpvlesivartfwaSKYGQ------EYPR--IIGLSATLP 675
Cdd:cd17920 149 FR--------------PDYLRlgrlrrALPGvpILALTATAT 176
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
499-673 |
6.47e-06 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain] Cd Length: 163 Bit Score: 48.33 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 499 LNPIQ----SKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHHYNPktkklnlsafKIVYIAPLKALVQEQVREF 574
Cdd:cd18032 1 PRYYQqeaiEALEEAREKGQRRALLVMATGTGKTYTAAFLIKRLLEANRKK----------RILFLAHREELLEQAERSF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 575 QRrlAFLGIKVAELTGDsrlsRKQIDETQVLVSTpekwdITTRNSNNLAI---VELVRLLIIDEIHllhddRGPvlesiv 651
Cdd:cd18032 71 KE--VLPDGSFGNLKGG----KKKPDDARVVFAT-----VQTLNKRKRLEkfpPDYFDLIIIDEAH-----HAI------ 128
|
170 180
....*....|....*....|....*..
gi 6321020 652 artfwASKYGQ--EY---PRIIGLSAT 673
Cdd:cd18032 129 -----ASSYRKilEYfepAFLLGLTAT 150
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1543-1724 |
6.73e-06 |
|
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: 47.93 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1543 PLEINIQSFKDVEHISFNFSMLQMAFEASAAAA----GNRNSSSVFLPSRKDCMEVAsafmkfskaiewdmlnveeeqiv 1618
Cdd:cd18795 4 PLEEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKietvSEGKPVLVFCSSRKECEKTA----------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1619 pyiEKLTdghlraplkhGVGILYKGMASNDERIVKRLYEYGAVSVLliskdC--SAFA------CKTdeVIILGTNLYDG 1690
Cdd:cd18795 61 ---KDLA----------GIAFHHAGLTREDRELVEELFREGLIKVL-----VatSTLAagvnlpART--VIIKGTQRYDG 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 6321020 1691 AEHKYMPytINELLEMVGLA--SGNDSMaGKVLILT 1724
Cdd:cd18795 121 KGYRELS--PLEYLQMIGRAgrPGFDTR-GEAIIMT 153
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1374-1531 |
7.98e-06 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 50.97 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1374 TGKTAMAELALLNHWRQNKGRAVYINP----SGEKI-DFllSDWNKrfshlAGGKIINKLGNDPSLNlKLLAKSHVLLAT 1448
Cdd:PRK00254 50 SGKTLVAEIVMVNKLLREGGKAVYLVPlkalAEEKYrEF--KDWEK-----LGLRVAMTTGDYDSTD-EWLGKYDIIIAT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1449 PVQFELLSR---RWrqrknIQSLELMIYDDAHEISQGVYGAVYEtlisrmiFIATQLEKKIRFVCLSNCLANARDFGEW- 1524
Cdd:PRK00254 122 AEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSYDRGATLE-------MILTHMLGRAQILGLSATVGNAEELAEWl 189
|
....*...
gi 6321020 1525 -AGMTKSN 1531
Cdd:PRK00254 190 nAELVVSD 197
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
501-639 |
1.09e-05 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 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: 350719 [Multi-domain] Cd Length: 206 Bit Score: 48.35 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 501 PIQSKVFHAAFEGdSNMLICAPTGSGKTNIALLTVLKALSHHynpKTKKLNLSAFKIVYIAPLKALVQeQVREFQRRL-A 579
Cdd:cd17961 19 LIQSKAIPLALEG-KDILARARTGSGKTAAYALPIIQKILKA---KAESGEEQGTRALILVPTRELAQ-QVSKVLEQLtA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321020 580 FLG--IKVAELTG---DSRLSRKQIDETQVLVSTPEK-WDITtrNSNNLAIVELVRLLIIDEIHLL 639
Cdd:cd17961 94 YCRkdVRVVNLSAsssDSVQRALLAEKPDIVVSTPARlLSHL--ESGSLLLLSTLKYLVIDEADLV 157
|
|
| DEXHc_RLR-2 |
cd18074 |
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma ... |
498-673 |
1.55e-05 |
|
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma differentiation-associated protein 5 or Mda5 and IFIH1) is a viral double-stranded RNA (dsRNA) receptor that shares sequence similarity and signaling pathways with RIG-I, yet plays essential functions in antiviral immunity through distinct specificity for viral RNA. RLR-2 recognizes the internal duplex structure, whereas RIG-I recognizes the terminus of dsRNA. RLR-2 uses direct protein-protein contacts to stack along dsRNA in a head-to-tail arrangement. The signaling domain (tandem CARD), which decorates the outside of the core RLR-2 filament, also has an intrinsic propensity to oligomerize into an elongated structure that activates the signaling adaptor, MAVS. RLR-2 uses long dsRNA as a signaling platform to cooperatively assemble the core filament, which in turn promotes stochastic assembly of the tandem CARD oligomers for signaling. LGP2 appears to positively and negatively regulate RLR-2 and RIG-I signaling, respectively. RLR-2 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: 350832 [Multi-domain] Cd Length: 216 Bit Score: 48.32 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 498 SLNPIQSKVFHAAFEGDsNMLICAPTGSGKTNIALLTVLKALShhynpKTKKLNLSAFKIVYIAPLKALVQEQVREFQrr 577
Cdd:cd18074 2 TLRDYQMEVAKPALEGK-NIIICLPTGSGKTRVAVYITKDHLD-----KKRKASEPGKVIVLVNKVPLVEQHYRKEFN-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 578 lAFLG--IKVAELTGDSRLS---RKQIDETQVLVSTPEKWDITTRNSNN--LAIVEL--VRLLIIDEIHllHDDRGPVLE 648
Cdd:cd18074 74 -PFLKhwYQVIGLSGDSQLKisfPEVVKRYDVIICTAQILENSLLNATEeeDEGVQLsdFSLIIIDECH--HTQKEAVYN 150
|
170 180 190
....*....|....*....|....*....|....*
gi 6321020 649 SIVARTF--------WA--SKYGQEYPRIIGLSAT 673
Cdd:cd18074 151 NIMRRYLkqkiknrkQKkeNKPLIPLPQILGLTAS 185
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
498-653 |
2.36e-05 |
|
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: 47.58 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 498 SLNPIQSKVFHAAFEGDSNMLICAPTGSGKTnIALLtvLKALSHHYNPKtKKLNLSAFKIVYIAPLKALVQEQVREFQRR 577
Cdd:cd17964 16 TMTPVQQKTLKPILSTGDDVLARAKTGTGKT-LAFL--LPAIQSLLNTK-PAGRRSGVSALIISPTRELALQIAAEAKKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 578 LAFL-GIKVAELTGDSRLSRKQIDETQ----VLVSTPEKWDITTRNSNNLAIVELVRLLIIDEI-HLLhdDRG--PVLES 649
Cdd:cd17964 92 LQGLrKLRVQSAVGGTSRRAELNRLRRgrpdILVATPGRLIDHLENPGVAKAFTDLDYLVLDEAdRLL--DMGfrPDLEQ 169
|
....
gi 6321020 650 IVAR 653
Cdd:cd17964 170 ILRH 173
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
488-637 |
3.97e-05 |
|
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350749 [Multi-domain] Cd Length: 193 Bit Score: 46.80 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 488 QEAFPSSETtslnPIQSKVFHAA---FEGDSNM--LICAPTGSGKTNIALLTVLKALSHHYnpktkklnlsafKIVYIAP 562
Cdd:cd17991 9 EASFPYEET----PDQLKAIEEIlkdMESGKPMdrLICGDVGFGKTEVAMRAAFKAVLSGK------------QVAVLVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 563 LKALVQEQVREFQRRLAFLGIKVAELTG-----DSRLSRKQIDE--------TQVLVSTpekwDITTRNsnnlaivelVR 629
Cdd:cd17991 73 TTLLAQQHYETFKERFANFPVNVELLSRfttaaEQREILEGLKEgkvdivigTHRLLSK----DVEFKN---------LG 139
|
....*...
gi 6321020 630 LLIIDEIH 637
Cdd:cd17991 140 LLIIDEEQ 147
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
497-831 |
5.06e-05 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 48.22 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 497 TSLNPIQSKVFHAAFEGdSNMLICAPTGSGKTnIA-LLTVLKALSHHYNPKTKKLnlsafkIvyIAPLKALVQeQV-REF 574
Cdd:COG0513 23 TTPTPIQAQAIPLILAG-RDVLGQAQTGTGKT-AAfLLPLLQRLDPSRPRAPQAL------I--LAPTRELAL-QVaEEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 575 QRRLAFLGIKVAELTGDSRLSRkQIDE----TQVLVSTPekwditTR-----NSNNLAIvELVRLLIIDEI-HLLhdDRG 644
Cdd:COG0513 92 RKLAKYLGLRVATVYGGVSIGR-QIRAlkrgVDIVVATP------GRlldliERGALDL-SGVETLVLDEAdRML--DMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 645 --PVLESIVARTfwaskygqeyP--RIIGL-SATLPnyEDV----GRFLRVPKEglFYFDSSFRPCP-LSQQFCGIKERN 714
Cdd:COG0513 162 fiEDIERILKLL----------PkeRQTLLfSATMP--PEIrklaKRYLKNPVR--IEVAPENATAEtIEQRYYLVDKRD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 715 slkKLKAMNdacyeKVLESINEGnQIIVFVHSRKETSRTATWLKNKfaeeNIthkltkndagskqilkteAANVLdpslr 794
Cdd:COG0513 228 ---KLELLR-----RLLRDEDPE-RAIVFCNTKRGADRLAEKLQKR----GI------------------SAAAL----- 271
|
330 340 350
....*....|....*....|....*....|....*..
gi 6321020 795 kliesgigthHAGLTRSDRSLSEDLFADGLLQVLVCT 831
Cdd:COG0513 272 ----------HGDLSQGQRERALDAFRNGKIRVLVAT 298
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
501-635 |
5.64e-05 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 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: 350704 [Multi-domain] Cd Length: 235 Bit Score: 46.85 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 501 PIQSKVFHAAFEGDSNMLICAPTGSGKT---NIALL-TVLKALSHHYNPKTKKlnlsAFKIVYIAPLKALVQEQVREFQR 576
Cdd:cd17946 15 PIQALALPAAIRDGKDVIGAAETGSGKTlafGIPILeRLLSQKSSNGVGGKQK----PLRALILTPTRELAVQVKDHLKA 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321020 577 RLAFLGIKVAELTG-------DSRLSRKqideTQVLVSTPEK-WDITTRNSNNLAIVELVRLLIIDE 635
Cdd:cd17946 91 IAKYTNIKIASIVGglavqkqERLLKKR----PEIVVATPGRlWELIQEGNEHLANLKSLRFLVLDE 153
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
516-668 |
1.18e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 516 NMLICAPTGSGKTniallTVLKALSHHYNPKTKKlnlsafkIVYIAPLKALvqeQVREFQRRLAFLGIKVAELTGDSRLs 595
Cdd:smart00382 4 VILIVGPPGSGKT-----TLARALARELGPPGGG-------VIYIDGEDIL---EEVLDQLLLIIVGGKKASGSGELRL- 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321020 596 rkqidetqvlvstpekwdittRNSNNLAIVELVRLLIIDEIHLLHDDRGPVLESIVARTFWASKYGQEYPRII 668
Cdd:smart00382 68 ---------------------RLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV 119
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
730-877 |
1.23e-04 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 44.17 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 730 VLESINEGNQIIVFVHSRKETSRTATWLKNKFAEENithKLTKNdagskqilkteaanvldpslrkliesgIGTHHAGLT 809
Cdd:cd18797 28 FADLVRAGVKTIVFCRSRKLAELLLRYLKARLVEEG---PLASK---------------------------VASYRAGYL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321020 810 RSDRSLSEDLFADGLLQVLVCTATLAWGVN---LPAhtVIIKGtdvYSPekgsweqlSPQDVLQMLGRAGR 877
Cdd:cd18797 78 AEDRREIEAELFNGELLGVVATNALELGIDiggLDA--VVLAG---YPG--------SLASLWQQAGRAGR 135
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
515-675 |
1.46e-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: 45.44 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 515 SNMLICAPTGSGKTNIALLTVLKALSHHYNPKTKKLNlsAFKIVYIAPLKALVQeQVREFQRRL-AFLGIKVAELTGDSr 593
Cdd:cd17948 28 RNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFN--APRGLVITPSRELAE-QIGSVAQSLtEGLGLKVKVITGGR- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 594 lSRKQI-----DETQVLVSTPEK-WDITTRNSNNLaivELVRLLIIDEIH-LLHDDRGPVLESIVARTFWAS----KYGQ 662
Cdd:cd17948 104 -TKRQIrnphfEEVDILVATPGAlSKLLTSRIYSL---EQLRHLVLDEADtLLDDSFNEKLSHFLRRFPLASrrseNTDG 179
|
170
....*....|....*
gi 6321020 663 EYP--RIIGLSATLP 675
Cdd:cd17948 180 LDPgtQLVLVSATMP 194
|
|
| DEXQc_Suv3 |
cd17913 |
DEXQ-box helicase domain of Suv3; Suppressor of var1 3-like protein (Suv3) is a DNA/RNA ... |
522-644 |
2.57e-04 |
|
DEXQ-box helicase domain of Suv3; Suppressor of var1 3-like protein (Suv3) is a DNA/RNA unwinding enzyme belonging to the class of DexH-box helicases. It localizes predominantly in the mitochondria, where it forms an RNA-degrading complex called mitochondrial degradosome (mtEXO) with exonuclease PNP (polynucleotide phosphorylase), that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Suv3 plays a role in the RNA surveillance system in mitochondria; it regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. It also confers salinity and drought stress tolerance by maintaining both photosynthesis and antioxidant machinery, probably via an increase in plant hormone levels such as gibberellic acid (GA3), the cytokinin zeatin (Z), and indole-3-acetic acid (IAA). Suv3 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: 350671 [Multi-domain] Cd Length: 142 Bit Score: 43.32 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 522 PTGSGKTNIAlltvLKALshhynpktkklnLSAFKIVYIAPLKALVQEQvrefQRRLAFLGIKVAELTGDSRLSRkqiDE 601
Cdd:cd17913 9 PTNSGKTYHA----LQRL------------KSAKSGVYCGPLRLLAWEV----YERLNAEGVPCDLVTGQERREV---EG 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 6321020 602 TQVLVSTPEKWDITTRnsnnlaiVELVrllIIDEIHLLHD-DRG 644
Cdd:cd17913 66 ATHVSCTVEMASISEP-------YDVA---VIDEIQMIGDpQRG 99
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
501-635 |
3.20e-04 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 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: 350711 [Multi-domain] Cd Length: 222 Bit Score: 44.29 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 501 PIQSKVFHAAFEGdSNMLICAPTGSGKTNIALLTVLKALSHHYNPKTKKLNLSafkiVYIAPLKALVQEQVREFQRRLAF 580
Cdd:cd17953 37 PIQAQALPAIMSG-RDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEGPIG----LIMAPTRELALQIYVECKKFSKA 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 581 LGIKVAELTGDSRLSrKQIDE----TQVLVSTPEKW-DITTRNSNNLAIVELVRLLIIDE 635
Cdd:cd17953 112 LGLRVVCVYGGSGIS-EQIAElkrgAEIVVCTPGRMiDILTANNGRVTNLRRVTYVVLDE 170
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
501-637 |
3.78e-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: 43.47 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 501 PIQSKV--FHAAFEGDSNMLICAPTGSGKTNIALLTVLKALShhynpktkklnLSAFKIVYIAPLKAlvqeQVREFQRRL 578
Cdd:cd17990 2 PIAAVLpaLRAALDAGGQVVLEAPPGAGKTTRVPLALLAELW-----------IAGGKIIVLEPRRV----AARAAARRL 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321020 579 AF-LGIKVAELTG-----DSRLSRKqideTQVLVSTPekwDITTR---NSNNLAIVELVrllIIDEIH 637
Cdd:cd17990 67 ATlLGEAPGETVGyrvrgESRVGRR----TRVEVVTE---GVLLRrlqRDPELSGVGAV---ILDEFH 124
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
516-637 |
3.92e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 43.56 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 516 NMLICAPTGSGKTNIALLTVLKALSHHynpktkklnlsaFKIVYIAPLKALVQEQVREFQRRLAFlgIKVAELTGDSRLS 595
Cdd:cd17918 38 DRLLSGDVGSGKTLVALGAALLAYKNG------------KQVAILVPTEILAHQHYEEARKFLPF--INVELVTGGTKAQ 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 6321020 596 RKQidETQVLVSTPE--KWDITTRNSNnlaivelvrLLIIDEIH 637
Cdd:cd17918 104 ILS--GISLLVGTHAllHLDVKFKNLD---------LVIVDEQH 136
|
|
| DEXHc_RLR-3 |
cd18075 |
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ... |
499-673 |
3.99e-04 |
|
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: 43.69 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 499 LNPIQSKVFHAAFEGDsNMLICAPTGSGKTNIALLTVLKALSHHYNPktkklnlsafKIVYIAPLKALVQEQVREFqRRL 578
Cdd:cd18075 3 LHGYQWEVVAPALRGK-NSIIWLPTGAGKTRAAVYVARRHLETKRGA----------KVAVLVNKVHLVDQHLEKE-FHV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 579 AFLGIKVAELTGDS-------RLSRkqidETQVLVSTPEKWDITTRNSNNLAIVELV--RLLIIDEIHLLHDDR--GPVL 647
Cdd:cd18075 71 LLDKYTVTAISGDSshkcffgQLAR----GSDVVICTAQILQNALLSGEEEAHVELTdfSLLVIDECHHTHKEAvyNKIM 146
|
170 180
....*....|....*....|....*.
gi 6321020 648 ESIVARTFwasKYGQEYPRIIGLSAT 673
Cdd:cd18075 147 LSYLEKKL---SRQGDLPQILGLTAS 169
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
501-651 |
8.83e-04 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 42.69 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 501 PIQSKVFHAAFEGdSNMLICAPTGSGKTNIALLTVLKALSHHYNPktkklnlsaFKIVYIAPLKALVQEQVREFQRRLAF 580
Cdd:cd17954 25 KIQEEAIPVALQG-RDIIGLAETGSGKTAAFALPILQALLENPQR---------FFALVLAPTRELAQQISEQFEALGSS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321020 581 LGIKVAELTG--DS-----RLSRKqideTQVLVSTPEKWDITTRNSNNLAIVELvRLLIIDEI-HLLHDDRGPVLESIV 651
Cdd:cd17954 95 IGLKSAVLVGgmDMmaqaiALAKK----PHVIVATPGRLVDHLENTKGFSLKSL-KFLVMDEAdRLLNMDFEPEIDKIL 168
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
501-698 |
1.20e-03 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350773 [Multi-domain] Cd Length: 209 Bit Score: 42.35 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 501 PIQSKVFHAAFEGDSNMLIcAPTGSGKTniaLLTVLKALSHhynpktkklnlSAFKIVyIAPLKALVQEQVREFQRrlaf 580
Cdd:cd18015 21 PLQLETINATMAGRDVFLV-MPTGGGKS---LCYQLPALCS-----------DGFTLV-VSPLISLMEDQLMALKK---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 581 LGIKVAELTGDS----------RLSRKQiDETQVLVSTPEKWDITTRNSNNLAIVELVRLL---IIDEIH----LLHDDR 643
Cdd:cd18015 81 LGISATMLNASSskehvkwvhaALTDKN-SELKLLYVTPEKIAKSKRFMSKLEKAYNAGRLariAIDEVHccsqWGHDFR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 644 GPVLE-SIVARTFwaskygqeyPR--IIGLSATLPNY--EDVGRFLRVPKegLFYFDSSF 698
Cdd:cd18015 160 PDYKKlGILKRQF---------PNvpILGLTATATSKvlKDVQKILCIQK--CLTFTASF 208
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
497-677 |
1.23e-03 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members 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. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 42.53 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 497 TSLNPIQSKVFHAAFEGdSNMLICAPTGSGKTNIALLTVLKALSHHYNPKTKKlnlSAFKIVYIAPLKALVQEQVREFQ- 575
Cdd:cd17944 11 TYLFPIQVKTFHPVYSG-KDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRG---RAPKVLVLAPTRELANQVTKDFKd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 576 --RRLaflgiKVAELTGDSRLSrKQIDETQ----VLVSTPEKwdITTRNSNNLAIVELVRLLIIDEIHLLHD-DRGPVLE 648
Cdd:cd17944 87 itRKL-----SVACFYGGTPYQ-QQIFAIRngidILVGTPGR--IKDHLQNGRLDLTKLKHVVLDEVDQMLDmGFAEQVE 158
|
170 180
....*....|....*....|....*....
gi 6321020 649 SIVARTFwaSKYGQEYPRIIGLSATLPNY 677
Cdd:cd17944 159 EILSVSY--KKDSEDNPQTLLFSATCPDW 185
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
502-683 |
1.37e-03 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 43.39 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 502 IQSKVFHAAFEGdSNMLICAPTGSGKTNIALLTVLKALSHHynPKTKklnLSAFKIVYIAPLKALVQeQVREFQRRLA-F 580
Cdd:PRK11192 27 IQAEAIPPALDG-RDVLGSAPTGTGKTAAFLLPALQHLLDF--PRRK---SGPPRILILTPTRELAM-QVADQARELAkH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 581 LGIKVAELTGD-SRLSRKQI-DETQ-VLVSTP---------EKWDittrnsnnlaiVELVRLLIIDEIhllhdDR----- 643
Cdd:PRK11192 100 THLDIATITGGvAYMNHAEVfSENQdIVVATPgrllqyikeENFD-----------CRAVETLILDEA-----DRmldmg 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6321020 644 -GPVLESIVARTFWASKygqeyprIIGLSATLpNYEDVGRF 683
Cdd:PRK11192 164 fAQDIETIAAETRWRKQ-------TLLFSATL-EGDAVQDF 196
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
501-635 |
1.91e-03 |
|
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 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: 350705 [Multi-domain] Cd Length: 196 Bit Score: 41.86 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 501 PIQSKVFHAAFEGdSNMLICAPTGSGKTNIALLTVLKALShhYNPKTKKlnlsAFKIVYIAPLKALVQeQVREFQRRLA- 579
Cdd:cd17947 15 PIQAAAIPLALLG-KDICASAVTGSGKTAAFLLPILERLL--YRPKKKA----ATRVLVLVPTRELAM-QCFSVLQQLAq 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321020 580 FLGIKVAELTGDSRLS------RKQIDetqVLVSTPEKWDITTRNSNNLAIvELVRLLIIDE 635
Cdd:cd17947 87 FTDITFALAVGGLSLKaqeaalRARPD---IVIATPGRLIDHLRNSPSFDL-DSIEILVLDE 144
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1363-1524 |
2.03e-03 |
|
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: 41.58 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1363 NDSVFVGSGKGTGKTAMAELALLNHWRQ-NKGRAVYINPSGEKIDFLLSDWNKRFS---HLAGGKIINKLGNDPSLNLKL 1438
Cdd:cd18025 16 RESALIVAPTSSGKTFISYYCMEKVLREsDDGVVVYVAPTKALVNQVVAEVYARFSkkyPPSGKSLWGVFTRDYRHNNPM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1439 laKSHVLLATPVQFE--LLSR---RWRQRkniqsLELMIYDDAHEISQGVYGAVYETLisrMIFIATQlekkirFVCLSN 1513
Cdd:cd18025 96 --NCQVLITVPECLEilLLSPhnaSWVPR-----IKYVIFDEIHSIGQSEDGAVWEQL---LLLIPCP------FLALSA 159
|
170
....*....|.
gi 6321020 1514 CLANARDFGEW 1524
Cdd:cd18025 160 TIGNPQKFHEW 170
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
500-637 |
2.21e-03 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350772 [Multi-domain] Cd Length: 205 Bit Score: 41.69 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 500 NPIQSKVFHAAFEGDSNMLICAPTGSGKTniaLLTVLKALSHhynpktkklnlSAFKIVyIAPLKALVQEQVREFQRrla 579
Cdd:cd18014 15 SPLQEKATMAVVKGNKDVFVCMPTGAGKS---LCYQLPALLA-----------KGITIV-ISPLIALIQDQVDHLKT--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321020 580 fLGIKVAELTgdSRLS---RKQI--------DETQVLVSTPEKWDITT--RNSNNLAIVELVRLLIIDEIH 637
Cdd:cd18014 77 -LKIRVDSLN--SKLSaqeRKRIiadlesekPQTKFLYITPEMAATSSfqPLLSSLVSRNLLSYLVVDEAH 144
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
827-890 |
3.68e-03 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350192 [Multi-domain] Cd Length: 135 Bit Score: 39.85 E-value: 3.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321020 827 VLVCTATLAWGVNLPAHTVIIkgTDVYSPEKGSWEQLSPQDVLQMLGRAGRPRYDtFGEGIIIT 890
Cdd:cd18805 73 VLVASDAIGMGLNLNIRRVIF--SSLSKFDGNEMRPLSPSEVKQIAGRAGRFGSH-FPEGEVTT 133
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
518-679 |
5.72e-03 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 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: 350723 [Multi-domain] Cd Length: 251 Bit Score: 40.82 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 518 LICAPTGSGKTNIALLTVLKAL-----------SHHYNPKTkklNLSAFKIVYIAPLKALVqEQVREFQRRLA-FLGIKV 585
Cdd:cd17965 65 LLAAETGSGKTLAYLAPLLDYLkrqeqepfeeaEEEYESAK---DTGRPRSVILVPTHELV-EQVYSVLKKLShTVKLGI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 586 AELTGDSRLSRKQIDE-----TQVLVSTPEKwdITTRNSNNLAIVELVRLLIIDEIHLLHDDrgpvleSIVARTFWASKY 660
Cdd:cd17965 141 KTFSSGFGPSYQRLQLafkgrIDILVTTPGK--LASLAKSRPKILSRVTHLVVDEADTLFDR------SFLQDTTSIIKR 212
|
170
....*....|....*....
gi 6321020 661 GQEYPRIIGLSATLPNYED 679
Cdd:cd17965 213 APKLKHLILCSATIPKEFD 231
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
825-890 |
7.97e-03 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The 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: 350172 [Multi-domain] Cd Length: 77 Bit Score: 37.30 E-value: 7.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321020 825 LQVLVCTATLAWGVNLP-AHTVIIkgtdvYSPEKgsweqlSPQDVLQMLGRAGRPRYDtfgEGIIIT 890
Cdd:cd18785 23 LEILVATNVLGEGIDVPsLDTVIF-----FDPPS------SAASYIQRVGRAGRGGKD---EGEVIL 75
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
1375-1524 |
8.43e-03 |
|
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: 39.89 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321020 1375 GKTAMAELALLNHWRQNKGRAVYINP----SGEKIDFLlsdwnKRFSHLAGGKIINKLGNDPSLNLKLLAKSHVLLATPV 1450
Cdd:cd18026 45 GKTLVAEILMLKRLLERRKKALFVLPyvsiVQEKVDAL-----SPLFEELGFRVEGYAGNKGRSPPKRRKSLSVAVCTIE 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321020 1451 QFELLSRRWRQRKNIQSLELMIYDDAHEISQGVYGAVYETLISRMIFIAtqlEKKIRFVCLSNCLANARDFGEW 1524
Cdd:cd18026 120 KANSLVNSLIEEGRLDELGLVVVDELHMLGDGHRGALLELLLTKLLYAA---QKNIQIVGMSATLPNLEELASW 190
|
|
| |
