|
Name |
Accession |
Description |
Interval |
E-value |
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1031-1334 |
1.48e-143 |
|
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: 448.57 E-value: 1.48e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1031 TELGRIASHFYITHTSMSTYNQHLKPMMGHIELFRVFALSDEFKYIPVREEEKLELSKLLERVPIPVKEGIEEPTSKINV 1110
Cdd:pfam02889 2 TDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKGDIEDPHAKVNI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1111 LLQAYISQLKLDGFALVSDMVYITQSASRILRAMFEICLKRGWSQLSRRALDLCKMVERRMWLSMSPLRQFKQMPMEVVK 1190
Cdd:pfam02889 82 LLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPELIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1191 KIEKKDFPWER--YFDLNPQEIGELVGIPKVGKLIHKFIHQFPKLELVTYVQPITRSLLRVELKITPDFMWDEKVHGTAE 1268
Cdd:pfam02889 162 KLEKKGVESVRdiLELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGKSE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317352187 1269 AFWVVVEDVDGEVILYHDSFILKQKYAEEDHVITFTVPLFEPLPPNYFISIISDRWLHCETKLPMS 1334
Cdd:pfam02889 242 GFWLVVGDSDGNEILHIERFTLTKRTLAGEHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
512-726 |
2.42e-141 |
|
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: 438.34 E-value: 2.42e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 512 IEELPPWVHGAFKGARILNRIQSKIYPVAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNEETGIiDTDAFKIVYIA 591
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGTI-NLDAFKIVYIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 592 PMKALVQEMVGNFSSRLQQYGIKVSELTGDRQLTKQQISETQIIVTTPEKWDVITRKATDRSYTNLVRLIIIDEVHLLHD 671
Cdd:cd18019 80 PMKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1317352187 672 DRGPVIESIVSRTIRHMEQTQEMIRLVGLSATLPNYGDVATFLRVDPKKGLFHFD 726
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1375-1565 |
4.06e-120 |
|
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: 376.98 E-value: 4.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1375 DKFNPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLWSTPNHGRCVYIAPFQEVVDLQVAQWRQKFGKIqGGKN 1454
Cdd:cd18021 2 KFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPL-LGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1455 IVALTGETSADLRLLESGDVIFATPTQWDVMSRRWKQRKNVQTVALFIADELHLIGSDVGPTYEIIVSRMRYIAHQTKNP 1534
Cdd:cd18021 81 VVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 1317352187 1535 IRIVCLSTSLANAQDLGEWIGSTPHTIFNFH 1565
Cdd:cd18021 161 IRIVGLSSSLANARDVGEWLGASKSTIFNFH 191
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1028-1336 |
4.55e-112 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 359.27 E-value: 4.55e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1028 FQVTELGRIASHFYITHTSMSTYNQHLKPMMGHIELFRVFALSDEFKYIPVREEEKLELSKLLERVPIPVK-EGIEEPTS 1106
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLEnPSLDDPHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1107 KINVLLQAYISQLKLDGFALVSDMVYITQSASRILRAMFEICLKRGWSQLSRRALDLCKMVERRMWLSMSPLRQFKQMPM 1186
Cdd:smart00611 82 KANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1187 EVVKKIEKKD-FPWERYFDLNPQEIGELVGIP-KVGKLIHKFIHQFPKLELVTYVQPITRSLLRVELKITPDFMWDEKVH 1264
Cdd:smart00611 162 EILKRLEKKKvLSLEDLLELEDEERGELLGLLdAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEIH 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317352187 1265 GTAEAFWVVVEDVDGEVILYHDSFILKQKYAEEDHVITFTVPLFEPLpPNYFISIISDRWLHCETKLPMSFR 1336
Cdd:smart00611 242 GKQEGWWLVIGDSDGNELLHIERFSLNKKNVSEEVKLDFTAPATEGN-YQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1862-2178 |
2.78e-108 |
|
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: 348.04 E-value: 2.78e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1862 PLNLGMIAAYYNVSYTTVEMFSMSLNEKTKLKGLLEILSSAAEFESIPVRHHEDTVLKKIYDRLPVKLGnPKFNSPHIKT 1941
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVK-GDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1942 NILLQAHFSRTQLP-PDLQSDQTAVLGKVIPLIQSIVDVISSSGWLKPALASMELAQMCVQALWDSESPLKQIPYFMADV 2020
Cdd:pfam02889 80 NILLQAYISRLKLPgFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 2021 IKRCEEREIDNVFGIMELEDDERNEILQMDGRQLYEVARYVNRYPSIDVKFGIrdedELVAGSQGALDVKLIrevdeddd 2100
Cdd:pfam02889 160 IKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEV----QPITRSVLRVEVTIT-------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 2101 evvgpviaPFFPHKKD-----EGWWIVIGDTEKNSLLGIKRVTLNKSL---SVKLDFTCP-SEAGEHSLKLFFMSDSYSG 2171
Cdd:pfam02889 228 --------PDFPWDKRvhgksEGFWLVVGDSDGNEILHIERFTLTKRTlagEHKLEFTVPpSDPGPPQLFVRLISDSWLG 299
|
....*..
gi 1317352187 2172 CDQEFDL 2178
Cdd:pfam02889 300 ADQEVPI 306
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
512-1043 |
9.02e-104 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 344.19 E-value: 9.02e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 512 IEELPP-WVHGAFKGARI--LNRIQSKIYPVAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRneetgiidtdafKIV 588
Cdd:COG1204 3 VAELPLeKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------KAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 589 YIAPMKALVQEMVGNFSSRLQQYGIKVSELTGDRQLTKQQISETQIIVTTPEKWDVITRKatDRSYTNLVRLIIIDEVHL 668
Cdd:COG1204 71 YIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRN--GPSWLRDVDLVVVDEAHL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 669 LHD-DRGPVIESIVSRtIRHMEQTqemIRLVGLSATLPNYGDVATFLRVDPkkglfhFDSSFRPCPLKQEFIgvteKKAI 747
Cdd:COG1204 149 IDDeSRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPLNEGVL----YDGV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 748 KRFQVMNEVTYQ-------KVVEQAGknQVLIFVHSRKETAKTAKTIKDMALEKDTLRLFLNPSSASREVLQDELPSIKD 820
Cdd:COG1204 215 LRFDDGSRRSKDptlalalDLLEEGG--QVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 821 PNLYELLPFGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPAHTVIIKgtqvySPEKGRWVELSPQDVLQ 900
Cdd:COG1204 293 EKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-----DTKRGGMVPIPVLEFKQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 901 MLGRAGRPQYDTFGEGIIIT-SHNELQ--YYLSLLNQQLPIESQFVSKLAD--NLNAEIVLGTVRNRDEAVQWLGYTYLY 975
Cdd:COG1204 368 MAGRAGRPGYDPYGEAILVAkSSDEADelFERYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYA 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317352187 976 VRMlrnptlygiSTDYLEEdpyLEQKRVDLIHSAGMLldksnlmkyDKKTGRFQVTELGRIASHFYIT 1043
Cdd:COG1204 448 YQY---------DKGDLEE---VVDDALEFLLENGFI---------EEDGDRLRATKLGKLVSRLYID 494
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1859-2181 |
1.03e-98 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 320.75 E-value: 1.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1859 DVTPLNLGMIAAYYNVSYTTVEMFSMSLNEKTKLKGLLEILSSAAEFESIPVRHHEDTVLKKIYDRLPVKLGNPKFNSPH 1938
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1939 IKTNILLQAHFSRTQLPP-DLQSDQTAVLGKVIPLIQSIVDVISSSGWLKPALASMELAQMCVQALWDSESPLKQIPYFM 2017
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSfALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 2018 ADVIKRCEEREIDNVFGIMELEDDERNEILQMDGRQLYEVARYVNRYPSIDVKFGIRDEDELVAGSQGALDVKLIRevde 2097
Cdd:smart00611 161 EEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTW---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 2098 dddevvgpviaPFFPHKKDEGWWIVIGDTEKNSLLGIKRVTLNK---SLSVKLDFTCPSEAGEHSLKLFFMSDSYSGCDQ 2174
Cdd:smart00611 237 -----------DDEIHGKQEGWWLVIGDSDGNELLHIERFSLNKknvSEEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQ 305
|
....*..
gi 1317352187 2175 EFDLPIK 2181
Cdd:smart00611 306 EYPLSFD 312
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
730-920 |
2.93e-66 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 221.27 E-value: 2.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 730 RPCPLKQEFIGVTEKKAIKRFQVMNE-----VTYQKVVEQAGKNQVLIFVHSRKETAKTAKTIKdmalekdtlrlflnps 804
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 805 sasrevlqdelpsikdpnlyellpfGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPAHTVIIKGTQVYS 884
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 1317352187 885 PEkgRWVELSPQDVLQMLGRAGRPQYDTFGEGIIIT 920
Cdd:cd18795 120 GK--GYRELSPLEYLQMIGRAGRPGFDTRGEAIIMT 153
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1374-1899 |
4.28e-64 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 228.63 E-value: 4.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1374 VDKFNPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLWStpNHGRCVYIAPF----QEVVDlqvaQWRQKFGKI 1449
Cdd:COG1204 20 IEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALL--NGGKALYIVPLralaSEKYR----EFKRDFEEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1450 qgGKNIVALTGETSADLRLLESGDVIFATPTQWDVMSRR---WKQRknvqtVALFIADELHLIGSDV-GPTYEIIVSRMR 1525
Cdd:COG1204 94 --GIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNgpsWLRD-----VDLVVVDEAHLIDDESrGPTLEVLLARLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1526 YIAHqtknPIRIVCLSTSLANAQDLGEWIGSTPhTIFNFhpsvRPVPLEI---------HIQSYSIPHFASLmmAMAKPT 1596
Cdd:COG1204 167 RLNP----EAQIVALSATIGNAEEIAEWLDAEL-VKSDW----RPVPLNEgvlydgvlrFDDGSRRSKDPTL--ALALDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1597 YvaitnySSDRPAIVFVPSRKQCRFTAVDLltfcaADGTTDRFLHAHASDIEDHLKQI--------NDKALAETLQHGVG 1668
Cdd:COG1204 236 L------EEGGQVLVFVSSRRDAESLAKKL-----ADELKRRLTPEEREELEELAEELlevseethTNEKLADCLEKGVA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1669 FYHEALSKQDKRIVEELFESGAIQVVVAsrdT---CWGINLSCHMVIVMGTqffegkeHRYADYPIT--DVLQMMGRACR 1743
Cdd:COG1204 305 FHHAGLPSELRRLVEDAFREGLIKVLVA---TptlAAGVNLPARRVIIRDT-------KRGGMVPIPvlEFKQMAGRAGR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1744 PQHDDTGRCVLMCQAIK---KDFYKKFLYEALPVESHL--DHFLHDHFNAEVVTKTIENKQDAVDYLTWTFLYrrmvenp 1818
Cdd:COG1204 375 PGYDPYGEAILVAKSSDeadELFERYILGEPEPIRSKLanESALRTHLLALIASGFANSREELLDFLENTFYA------- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1819 nyygmqgsdHRHLSDHLSELVETTVNDLSASKCIALEDELdVTPLNLGMIAAYYNVSYTTVEMFSMSLNEKTKLKGLLEI 1898
Cdd:COG1204 448 ---------YQYDKGDLEEVVDDALEFLLENGFIEEDGDR-LRATKLGKLVSRLYIDPLTAAELVDGLRKADEEFTDLGL 517
|
.
gi 1317352187 1899 L 1899
Cdd:COG1204 518 L 518
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
541-1042 |
1.05e-54 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 204.73 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 541 FEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRneetgiidtdafKIVYIAPMKALVQEMVGNFSsRLQQYGIKVSELTG 620
Cdd:PRK01172 34 LRKGENVIVSVPTAAGKTLIAYSAIYETFLAGL------------KSIYIVPLRSLAMEKYEELS-RLRSLGMRVKISIG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 621 DRQLTKQQISETQIIVTTPEKWDVITRKatDRSYTNLVRLIIIDEVHLLHD-DRGPVIESIVSrTIRHMEQTqemIRLVG 699
Cdd:PRK01172 101 DYDDPPDFIKRYDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDeDRGPTLETVLS-SARYVNPD---ARILA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 700 LSATLPNYGDVATFLRVDPKKglfhfdSSFRPCPLKqefIGVTEKKAI-----KRFQVMNEVTYQKVVEQAGknQVLIFV 774
Cdd:PRK01172 175 LSATVSNANELAQWLNASLIK------SNFRPVPLK---LGILYRKRLildgyERSQVDINSLIKETVNDGG--QVLVFV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 775 HSRKETAKTAKtikdmalekDTLRLFlnPSSASREVLQDElPSIKDPNLYELLPFGFAIHHAGMSRTDRTTVEDLFADGH 854
Cdd:PRK01172 244 SSRKNAEDYAE---------MLIQHF--PEFNDFKVSSEN-NNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 855 IQVLVSTATLAWGVNLPAHTVIIKGTQVYSPEKGRWveLSPQDVLQMLGRAGRPQYDTFGEGIII----TSHNELQYYLS 930
Cdd:PRK01172 312 IKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRY--LSNMEIKQMIGRAGRPGYDQYGIGYIYaaspASYDAAKKYLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 931 llNQQLPIESQFVS--KLADNLNAEIVLGTVRNRDEAVQWLgytylyvrmlrNPTLYGISTDYLEEDPYleqkrvdlIHS 1008
Cdd:PRK01172 390 --GEPEPVISYMGSqrKVRFNTLAAISMGLASSMEDLILFY-----------NETLMAIQNGVDEIDYY--------IES 448
|
490 500 510
....*....|....*....|....*....|....
gi 1317352187 1009 AGMLLDKSNLMKYDKKtgrFQVTELGRIASHFYI 1042
Cdd:PRK01172 449 SLKFLKENGFIKGDVT---LRATRLGKLTSDLYI 479
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
295-403 |
1.09e-50 |
|
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: 174.72 E-value: 1.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 295 EQKISPHDIDAFWLQRLVANYYSDPHTAQEKTSSTMQILASDVN-TRDCENELMALFEYDKFDLVKILTRNRELIVWCTK 373
Cdd:pfam18149 2 KDSLDPHDIDAFWLQRLLSKFYGDAIEAQKKAEEVLDILESAADdLRECENQLVELLDYDKFDLVKLLLKNRDKIVWCTK 81
|
90 100 110
....*....|....*....|....*....|.
gi 1317352187 374 LARAGTDgAERQNIEREMREH-GLEWILRDL 403
Cdd:pfam18149 82 LARAQSE-EEKQAIEEEMRSNpGLAWILDEL 111
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1569-1757 |
7.47e-47 |
|
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: 165.42 E-value: 7.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1569 RPVPLEIHIQSYSIPHFASLMMAMAK-----PTYVAITNYSSDRPAIVFVPSRKQCRFTAVDLLtfcaadgttdrflhah 1643
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1644 asdiedhlkqindkalaetlqhGVGFYHEALSKQDKRIVEELFESGAIQVVVASRDTCWGINLSCHMVIVMGTQFFEGKE 1723
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 1317352187 1724 HRYadYPITDVLQMMGRACRPQHDDTGRCVLMCQ 1757
Cdd:cd18795 123 YRE--LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1359-1929 |
3.96e-37 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 151.89 E-value: 3.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1359 SALRNREYEAVYngwvdkfnPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLWSTPNhGRCVYIAPFQEVVDlq 1438
Cdd:PRK00254 14 RVLKERGIEELY--------PPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREG-GKAVYLVPLKALAE-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1439 vaqwrQKFGKIQG----GKNIVALTGETSADLRLLESGDVIFATPTQWDVMSR---RWkqrknVQTVALFIADELHLIGS 1511
Cdd:PRK00254 83 -----EKYREFKDweklGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1512 -DVGPTYEIIVSRMryiahqtKNPIRIVCLSTSLANAQDLGEWIGSTPhtifnFHPSVRPVPL--------EIHIQSYSI 1582
Cdd:PRK00254 153 yDRGATLEMILTHM-------LGRAQILGLSATVGNAEELAEWLNAEL-----VVSDWRPVKLrkgvfyqgFLFWEDGKI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1583 PHFASLMMAMAkptYVAItnySSDRPAIVFVPSRKQCRFTAVDLLTFCAA--DGTTDRFLHAHASDIEDHlkQINDKaLA 1660
Cdd:PRK00254 221 ERFPNSWESLV---YDAV---KKGKGALVFVNTRRSAEKEALELAKKIKRflTKPELRALKELADSLEEN--PTNEK-LK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1661 ETLQHGVGFYHEALSKQDKRIVEELFESGAIQVVVASRDTCWGINLSCHMVIVMGTQffegkehRYADY-----PITDVL 1735
Cdd:PRK00254 292 KALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTK-------RYSNFgwediPVLEIQ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1736 QMMGRACRPQHDDTGRCVLMCQAIK-KDFYKKF-------LYEALPVESHldhfLHDHFNAEVVTKTIENKQDAVDYLTW 1807
Cdd:PRK00254 365 QMMGRAGRPKYDEVGEAIIVATTEEpSKLMERYifgkpekLFSMLSNESA----FRSQVLALITNFGVSNFKELVNFLER 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1808 TFlyrrmvenpnyYGMQGSDHRHLSDHLSE----LVETTVNDLSaskciaLEDEldVTPLNLGMIAAYYNVSYTTVEMFS 1883
Cdd:PRK00254 441 TF-----------YAHQRKDLYSLEEKAKEivyfLLENEFIDID------LEDR--FIPLPLGIRTSQLYIDPLTAKKFK 501
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1317352187 1884 MSLNEKTKLK---GLLEILSSAAEFESIPVRHHEDTVLKKIYDRLPVKL 1929
Cdd:PRK00254 502 DAFPKIEKNPnplGIFQLIASTPDMTPLNYSRKEMEDLLDEAYEMEDRL 550
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
530-705 |
3.39e-36 |
|
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: 135.45 E-value: 3.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 530 NRIQSKIYPvAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNeetgiidtdAFKIVYIAPMKALVQEMVGNFSSRLQ 609
Cdd:pfam00270 1 TPIQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN---------GPQALVLAPTRELAEQIYEELKKLGK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 610 QYGIKVSELTG--DRQLTKQQISETQIIVTTPEKWDVITRKatdRSYTNLVRLIIIDEVHLLHD-DRGPVIESIVSRtir 686
Cdd:pfam00270 71 GLGLKVASLLGgdSRKEQLEKLKGPDILVGTPGRLLDLLQE---RKLLKNLKLLVLDEAHRLLDmGFGPDLEEILRR--- 144
|
170
....*....|....*....
gi 1317352187 687 hmeqTQEMIRLVGLSATLP 705
Cdd:pfam00270 145 ----LPKKRQILLLSATLP 159
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
503-910 |
3.24e-28 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 123.85 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 503 HAENERLISIEELPpwVHGAFKgaRILNRIQSKIYPV---AFE----QDENLLVCAPTGSGKTNVA-MLCILNEMEKNRn 574
Cdd:COG1202 181 TTDEVDTVPVDDLD--LPPELK--DLLEGRGEELLPVqslAVEngllEGKDQLVVSATATGKTLIGeLAGIKNALEGKG- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 575 eetgiidtdafKIVYIAPMKALVQEMVGNFSSRlqqY--GIKVSELTGDRQLT---KQQISETQIIVTTPEKWDVITRka 649
Cdd:COG1202 256 -----------KMLFLVPLVALANQKYEDFKDR---YgdGLDVSIRVGASRIRddgTRFDPNADIIVGTYEGIDHALR-- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 650 TDRSYTNlVRLIIIDEVHLLHD-DRGPVIESIVSRtIRHM-EQTQemirLVGLSATLPNYGDVATFLRVDpkkgLFHFDS 727
Cdd:COG1202 320 TGRDLGD-IGTVVIDEVHMLEDpERGHRLDGLIAR-LKYYcPGAQ----WIYLSATVGNPEELAKKLGAK----LVEYEE 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 728 sfRPCPLKQEFIGVTEKKAIKRFQVMNEVTYQKVVEQAGKNQVLIFVHSRKETAKTAktikdmalekdtlrlflnpssas 807
Cdd:COG1202 390 --RPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFTNSRRRCHEIA----------------------- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 808 revlqdelpsikdpnlyELLPFGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPAHTVI-------IKgt 880
Cdd:COG1202 445 -----------------RALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIfdslamgIE-- 505
|
410 420 430
....*....|....*....|....*....|
gi 1317352187 881 qvyspekgrWveLSPQDVLQMLGRAGRPQY 910
Cdd:COG1202 506 ---------W--LSVQEFHQMLGRAGRPDY 524
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
524-738 |
6.81e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 107.19 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 524 KGARILNRIQSKIYPVAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNeetgiidtdaFKIVYIAPMKALVQEMVGN 603
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKG----------GRVLVLVPTRELAEQWAEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 604 FSSRLQQYGIKVSELTGD----RQLTKQQISETQIIVTTPEKWdvITRKATDRSYTNLVRLIIIDEVHLLHD-DRGPVIE 678
Cdd:smart00487 74 LKKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRL--LDLLENDKLSLSNVDLVILDEAHRLLDgGFGDQLE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 679 SIVSRTIRhmeqtqeMIRLVGLSATLPNYGDVATFLRVdpkKGLFHFDSSFRPCPLKQEF 738
Cdd:smart00487 152 KLLKLLPK-------NVQLLLLSATPPEEIENLLELFL---NDPVFIDVGFTPLEPIEQF 201
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1378-1550 |
4.32e-25 |
|
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: 103.86 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1378 NPIQTQVFNALYNmNDNVFVGAPTGSGKTVCAEFALL-RLWSTPNHGRCVYIAPFQEVVDLQVAQWRqKFGKIQGGKNIV 1456
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALeALDKLDNGPQALVLAPTRELAEQIYEELK-KLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1457 ALTG-ETSADLRLLESGDVIFATPTQWDVMSRrwkQRKNVQTVALFIADELHLIGSDV-GPTYEIIVSRMRYiahqtknP 1534
Cdd:pfam00270 79 LLGGdSRKEQLEKLKGPDILVGTPGRLLDLLQ---ERKLLKNLKLLVLDEAHRLLDMGfGPDLEEILRRLPK-------K 148
|
170
....*....|....*..
gi 1317352187 1535 IRIVCLSTSLA-NAQDL 1550
Cdd:pfam00270 149 RQILLLSATLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1376-1561 |
6.13e-20 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 90.24 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1376 KFNPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLWSTPNHGRCVYIAPFQEVVDlQVAQWRQKFGKIQGGKNI 1455
Cdd:smart00487 8 PLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAE-QWAEELKKLGPSLGLKVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1456 VALTGETS-ADLRLLESG--DVIFATPTQWDVMSRRWKqrKNVQTVALFIADELH-LIGSDVGPTYEIIVSRMRyiahqt 1531
Cdd:smart00487 87 GLYGGDSKrEQLRKLESGktDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP------ 158
|
170 180 190
....*....|....*....|....*....|.
gi 1317352187 1532 kNPIRIVCLS-TSLANAQDLGEWIGSTPHTI 1561
Cdd:smart00487 159 -KNVQLLLLSaTPPEEIENLLELFLNDPVFI 188
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
540-908 |
2.88e-18 |
|
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: 91.84 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 540 AFEQDENLLVCAPTGSGKTNVAMLCILNEME-KNRNEETGIidtdafKIVYIAPMKALVQEMVGNFSSRLQQYG--IKVS 616
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSLIDLAgPEAPKEKGL------HTLYITPLRALAVDIARNLQAPIEELGlpIRVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 617 ELTGD---RQLTKQQISETQIIVTTPEKWDV-ITRKATDRSYTNLvRLIIIDEVH-LLHDDRGPVIESIVSRtirhMEQT 691
Cdd:TIGR04121 98 TRTGDtssSERARQRKKPPDILLTTPESLALlLSYPDAARLFKDL-RCVVVDEWHeLAGSKRGDQLELALAR----LRRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 692 QEMIRLVGLSATLpnyGDVATFLRVdpkkgLFHFDSSfrPCPLkqefIGVTEKKAIKRFQVMNEVT-------------Y 758
Cdd:TIGR04121 173 APGLRRWGLSATI---GNLEEARRV-----LLGVGGA--PAVL----VRGKLPKAIEVISLLPESEerfpwaghlglraL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 759 QKVVEQAGKNQ-VLIFVHSRketaktaktikdmalekdtlrlflnpSSASR--EVLQDELPSIKDPnlyellpfgFAIHH 835
Cdd:TIGR04121 239 PEVYAEIDQARtTLVFTNTR--------------------------SQAELwfQALWEANPEFALP---------IALHH 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317352187 836 AGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVN-LPAHTVIikgtQVYSPeKG--RwvelspqdVLQMLGRAG-RP 908
Cdd:TIGR04121 284 GSLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDfGPVDLVI----QIGSP-KGvaR--------LLQRAGRSNhRP 347
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
823-908 |
4.46e-17 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 77.64 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 823 LYELL---PFGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLP-AHTVIIKGtqvyspekgrwVELSPQDV 898
Cdd:smart00490 3 LAELLkelGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASY 71
|
90
....*....|
gi 1317352187 899 LQMLGRAGRP 908
Cdd:smart00490 72 IQRIGRAGRA 81
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
545-906 |
2.26e-14 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 79.16 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 545 ENLLVCAPTGSGKTNVAMLCILNEM-EKNRNEETgiidTDAFKIVYIAPMKALVQEMVGNFSSRLQQ-------YGIKVS 616
Cdd:PRK13767 48 KNVLISSPTGSGKTLAAFLAIIDELfRLGREGEL----EDKVYCLYVSPLRALNNDIHRNLEEPLTEireiakeRGEELP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 617 EL-----TGD-----RQltkQQISET-QIIVTTPEKWDVITRKATDRSYTNLVRLIIIDEVHLLHDD-RGpvieSIVSRT 684
Cdd:PRK13767 124 EIrvairTGDtssyeKQ---KMLKKPpHILITTPESLAILLNSPKFREKLRTVKWVIVDEIHSLAENkRG----VHLSLS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 685 IRHME--QTQEMIRlVGLSATLPNYGDVATFLrvdpkkGLFHFDSSFRPCplkqEFIGVTEKKAIKrFQVMNEVtyqkvv 762
Cdd:PRK13767 197 LERLEelAGGEFVR-IGLSATIEPLEEVAKFL------VGYEDDGEPRDC----EIVDARFVKPFD-IKVISPV------ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 763 eqagKNqvliFVHSRKE--TAKTAKTIKDMALEKDTLRLFLNPSSASREVLQdelpsikdpNLYELLPFGFAI-----HH 835
Cdd:PRK13767 259 ----DD----LIHTPAEeiSEALYETLHELIKEHRTTLIFTNTRSGAERVLY---------NLRKRFPEEYDEdnigaHH 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317352187 836 AGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPAHTVIIkgtQVYSPEkgrwvelSPQDVLQMLGRAG 906
Cdd:PRK13767 322 SSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVV---LLGSPK-------SVSRLLQRIGRAG 382
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
823-907 |
1.99e-11 |
|
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: 62.61 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 823 LYELLPFGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLP-AHTVIIkgtqvYSPEKgrwvelSPQDVLQM 901
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YDLPW------NPASYIQR 101
|
....*.
gi 1317352187 902 LGRAGR 907
Cdd:pfam00271 102 IGRAGR 107
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1659-1744 |
2.21e-07 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 50.29 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1659 LAETLQ---HGVGFYHEALSKQDKRIVEELFESGAIQVVVASRDTCWGINLSC-HMVIVMGtqffegkehryADYPITDV 1734
Cdd:smart00490 3 LAELLKelgIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGvDLVIIYD-----------LPWSPASY 71
|
90
....*....|
gi 1317352187 1735 LQMMGRACRP 1744
Cdd:smart00490 72 IQRIGRAGRA 81
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1399-1706 |
4.57e-07 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 55.70 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1399 APTGSGKTVCA-EFALLRLWS-------TPNHG---RCVYIAPFQEV-VDLQ---------VAQWRQKFGKIQGGKNIVA 1457
Cdd:PRK09751 3 APTGSGKTLAAfLYALDRLFReggedtrEAHKRktsRILYISPIKALgTDVQrnlqiplkgIADERRRRGETEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1458 LTGETSADLR---LLESGDVIFATPTQWDVM--SRRWKQRKNVQTValfIADELHLI-GSDVGPTYEIIVSRMRYIAHqt 1531
Cdd:PRK09751 83 RTGDTPAQERsklTRNPPDILITTPESLYLMltSRARETLRGVETV---IIDEVHAVaGSKRGAHLALSLERLDALLH-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1532 kNPIRIVCLSTSLANAQDLGEWI-GSTPHTIFNfHPSVRPVPLEIHIQSYSIPHFASLMMAMAKPTYVA----------- 1599
Cdd:PRK09751 158 -TSAQRIGLSATVRSASDVAAFLgGDRPVTVVN-PPAMRHPQIRIVVPVANMDDVSSVASGTGEDSHAGregsiwpyiet 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1600 --ITNYSSDRPAIVFVPSRKqcrftavdlltfcAADGTTDRFLHAHASDIEDHLKQINDKALAETLQHGVG--------- 1668
Cdd:PRK09751 236 giLDEVLRHRSTIVFTNSRG-------------LAEKLTARLNELYAARLQRSPSIAVDAAHFESTSGATSnrvqssdvf 302
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1317352187 1669 ---FYHEALSKQDKRIVEELFESGAIQVVVASRDTCWGINL 1706
Cdd:PRK09751 303 iarSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDM 343
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
1391-1507 |
5.60e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.12 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1391 MNDNVFVGAPTGSGKTVCAEFALLRLWSTPNhGRCVYIAPFQEVVDlQVAQWRQKFGKIQGGKnIVALTGETSADLR--L 1468
Cdd:COG1111 16 LRKNTLVVLPTGLGKTAVALLVIAERLHKKG-GKVLFLAPTKPLVE-QHAEFFKEALNIPEDE-IVVFTGEVSPEKRkeL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1317352187 1469 LESGDVIFATP--TQWDVMSRRWkqrkNVQTVALFIADELH 1507
Cdd:COG1111 93 WEKARIIVATPqvIENDLIAGRI----DLDDVSLLIFDEAH 129
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1031-1334 |
1.48e-143 |
|
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: 448.57 E-value: 1.48e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1031 TELGRIASHFYITHTSMSTYNQHLKPMMGHIELFRVFALSDEFKYIPVREEEKLELSKLLERVPIPVKEGIEEPTSKINV 1110
Cdd:pfam02889 2 TDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKGDIEDPHAKVNI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1111 LLQAYISQLKLDGFALVSDMVYITQSASRILRAMFEICLKRGWSQLSRRALDLCKMVERRMWLSMSPLRQFKQMPMEVVK 1190
Cdd:pfam02889 82 LLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPELIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1191 KIEKKDFPWER--YFDLNPQEIGELVGIPKVGKLIHKFIHQFPKLELVTYVQPITRSLLRVELKITPDFMWDEKVHGTAE 1268
Cdd:pfam02889 162 KLEKKGVESVRdiLELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGKSE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317352187 1269 AFWVVVEDVDGEVILYHDSFILKQKYAEEDHVITFTVPLFEPLPPNYFISIISDRWLHCETKLPMS 1334
Cdd:pfam02889 242 GFWLVVGDSDGNEILHIERFTLTKRTLAGEHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
512-726 |
2.42e-141 |
|
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: 438.34 E-value: 2.42e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 512 IEELPPWVHGAFKGARILNRIQSKIYPVAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNEETGIiDTDAFKIVYIA 591
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGTI-NLDAFKIVYIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 592 PMKALVQEMVGNFSSRLQQYGIKVSELTGDRQLTKQQISETQIIVTTPEKWDVITRKATDRSYTNLVRLIIIDEVHLLHD 671
Cdd:cd18019 80 PMKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1317352187 672 DRGPVIESIVSRTIRHMEQTQEMIRLVGLSATLPNYGDVATFLRVDPKKGLFHFD 726
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1375-1565 |
4.06e-120 |
|
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: 376.98 E-value: 4.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1375 DKFNPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLWSTPNHGRCVYIAPFQEVVDLQVAQWRQKFGKIqGGKN 1454
Cdd:cd18021 2 KFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPL-LGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1455 IVALTGETSADLRLLESGDVIFATPTQWDVMSRRWKQRKNVQTVALFIADELHLIGSDVGPTYEIIVSRMRYIAHQTKNP 1534
Cdd:cd18021 81 VVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 1317352187 1535 IRIVCLSTSLANAQDLGEWIGSTPHTIFNFH 1565
Cdd:cd18021 161 IRIVGLSSSLANARDVGEWLGASKSTIFNFH 191
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1028-1336 |
4.55e-112 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 359.27 E-value: 4.55e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1028 FQVTELGRIASHFYITHTSMSTYNQHLKPMMGHIELFRVFALSDEFKYIPVREEEKLELSKLLERVPIPVK-EGIEEPTS 1106
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLEnPSLDDPHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1107 KINVLLQAYISQLKLDGFALVSDMVYITQSASRILRAMFEICLKRGWSQLSRRALDLCKMVERRMWLSMSPLRQFKQMPM 1186
Cdd:smart00611 82 KANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1187 EVVKKIEKKD-FPWERYFDLNPQEIGELVGIP-KVGKLIHKFIHQFPKLELVTYVQPITRSLLRVELKITPDFMWDEKVH 1264
Cdd:smart00611 162 EILKRLEKKKvLSLEDLLELEDEERGELLGLLdAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEIH 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317352187 1265 GTAEAFWVVVEDVDGEVILYHDSFILKQKYAEEDHVITFTVPLFEPLpPNYFISIISDRWLHCETKLPMSFR 1336
Cdd:smart00611 242 GKQEGWWLVIGDSDGNELLHIERFSLNKKNVSEEVKLDFTAPATEGN-YQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1862-2178 |
2.78e-108 |
|
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: 348.04 E-value: 2.78e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1862 PLNLGMIAAYYNVSYTTVEMFSMSLNEKTKLKGLLEILSSAAEFESIPVRHHEDTVLKKIYDRLPVKLGnPKFNSPHIKT 1941
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVK-GDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1942 NILLQAHFSRTQLP-PDLQSDQTAVLGKVIPLIQSIVDVISSSGWLKPALASMELAQMCVQALWDSESPLKQIPYFMADV 2020
Cdd:pfam02889 80 NILLQAYISRLKLPgFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 2021 IKRCEEREIDNVFGIMELEDDERNEILQMDGRQLYEVARYVNRYPSIDVKFGIrdedELVAGSQGALDVKLIrevdeddd 2100
Cdd:pfam02889 160 IKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEV----QPITRSVLRVEVTIT-------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 2101 evvgpviaPFFPHKKD-----EGWWIVIGDTEKNSLLGIKRVTLNKSL---SVKLDFTCP-SEAGEHSLKLFFMSDSYSG 2171
Cdd:pfam02889 228 --------PDFPWDKRvhgksEGFWLVVGDSDGNEILHIERFTLTKRTlagEHKLEFTVPpSDPGPPQLFVRLISDSWLG 299
|
....*..
gi 1317352187 2172 CDQEFDL 2178
Cdd:pfam02889 300 ADQEVPI 306
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
1031-1335 |
1.70e-105 |
|
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: 340.49 E-value: 1.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1031 TELGRIASHFYITHTSMSTYNQHLKPMMGHIELFRVFALSDEFKYIPVREEEKLELSKLLERVPIPVKEGIEEPTS-KIN 1109
Cdd:smart00973 2 TELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHaKVN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1110 VLLQAYISQLKLDGFALVSDMVYITQSASRILRAMFEICLKRGWSQLSRRALDLCKMVERRMWL-SMSPLRQFKQM-PME 1187
Cdd:smart00973 82 LLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEdSDSPLKQLPHFlIED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1188 VVKKIEKKDFPW--ERYFDLNPQEIGELVGI-PKVGKLIHKFIHQFPKLELVTYVQPITRSL-LRVELKITPDFMWDEKV 1263
Cdd:smart00973 162 VYDKLELKDGSRsfELLLDMNAAELGEFLNRlPPNGRLIYELLRRFPKIEVEAEVLPITRDLtLRVELEITPVFAWDLPR 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317352187 1264 -HGTAEAFWVVVEDVDGEVILYHDSFILKQKYAEEDHVITFTVPLFEPLPPNYFISIISDRWLHCETKLPMSF 1335
Cdd:smart00973 242 hKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKLDFTVPLSEPGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
512-1043 |
9.02e-104 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 344.19 E-value: 9.02e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 512 IEELPP-WVHGAFKGARI--LNRIQSKIYPVAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRneetgiidtdafKIV 588
Cdd:COG1204 3 VAELPLeKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------KAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 589 YIAPMKALVQEMVGNFSSRLQQYGIKVSELTGDRQLTKQQISETQIIVTTPEKWDVITRKatDRSYTNLVRLIIIDEVHL 668
Cdd:COG1204 71 YIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRN--GPSWLRDVDLVVVDEAHL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 669 LHD-DRGPVIESIVSRtIRHMEQTqemIRLVGLSATLPNYGDVATFLRVDPkkglfhFDSSFRPCPLKQEFIgvteKKAI 747
Cdd:COG1204 149 IDDeSRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPLNEGVL----YDGV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 748 KRFQVMNEVTYQ-------KVVEQAGknQVLIFVHSRKETAKTAKTIKDMALEKDTLRLFLNPSSASREVLQDELPSIKD 820
Cdd:COG1204 215 LRFDDGSRRSKDptlalalDLLEEGG--QVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 821 PNLYELLPFGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPAHTVIIKgtqvySPEKGRWVELSPQDVLQ 900
Cdd:COG1204 293 EKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-----DTKRGGMVPIPVLEFKQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 901 MLGRAGRPQYDTFGEGIIIT-SHNELQ--YYLSLLNQQLPIESQFVSKLAD--NLNAEIVLGTVRNRDEAVQWLGYTYLY 975
Cdd:COG1204 368 MAGRAGRPGYDPYGEAILVAkSSDEADelFERYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYA 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317352187 976 VRMlrnptlygiSTDYLEEdpyLEQKRVDLIHSAGMLldksnlmkyDKKTGRFQVTELGRIASHFYIT 1043
Cdd:COG1204 448 YQY---------DKGDLEE---VVDDALEFLLENGFI---------EEDGDRLRATKLGKLVSRLYID 494
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
529-726 |
4.56e-99 |
|
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: 317.06 E-value: 4.56e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 529 LNRIQSKIYPVAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNEEtGIIDTDAFKIVYIAPMKALVQEMVGNFSSRL 608
Cdd:cd18020 2 LNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQG-GVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 609 QQYGIKVSELTGDRQLTKQQISETQIIVTTPEKWDVITRKAT-DRSYTNLVRLIIIDEVHLLHDDRGPVIESIVSRTIRH 687
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSgDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1317352187 688 MEQTQEMIRLVGLSATLPNYGDVATFLRVDPKKGLFHFD 726
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1859-2181 |
1.03e-98 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 320.75 E-value: 1.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1859 DVTPLNLGMIAAYYNVSYTTVEMFSMSLNEKTKLKGLLEILSSAAEFESIPVRHHEDTVLKKIYDRLPVKLGNPKFNSPH 1938
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1939 IKTNILLQAHFSRTQLPP-DLQSDQTAVLGKVIPLIQSIVDVISSSGWLKPALASMELAQMCVQALWDSESPLKQIPYFM 2017
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSfALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 2018 ADVIKRCEEREIDNVFGIMELEDDERNEILQMDGRQLYEVARYVNRYPSIDVKFGIRDEDELVAGSQGALDVKLIRevde 2097
Cdd:smart00611 161 EEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTW---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 2098 dddevvgpviaPFFPHKKDEGWWIVIGDTEKNSLLGIKRVTLNK---SLSVKLDFTCPSEAGEHSLKLFFMSDSYSGCDQ 2174
Cdd:smart00611 237 -----------DDEIHGKQEGWWLVIGDSDGNELLHIERFSLNKknvSEEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQ 305
|
....*..
gi 1317352187 2175 EFDLPIK 2181
Cdd:smart00611 306 EYPLSFD 312
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
1862-2180 |
1.39e-87 |
|
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: 288.87 E-value: 1.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1862 PLNLGMIAAYYNVSYTTVEMFSMSLNEKTKLKGLLEILSSAAEFESIPVRHHEDTVLKKIYDRLPVKLGNPKFNSPHIKT 1941
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1942 NILLQAHFSRTQLPP-DLQSDQTAVLGKVIPLIQSIVDVISSSGWLKPALASMELAQMCVQALW-DSESPLKQIPYFmad 2019
Cdd:smart00973 81 NLLLQAHLSRLPLPDfDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWeDSDSPLKQLPHF--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 2020 vikrceerEIDNVFGIMELEDDERNEILQMDgRQLYEVARYVNR-YPSIDVKFGIRDEDEL--VAGSQGALDVKLIRevd 2096
Cdd:smart00973 158 --------LIEDVYDKLELKDGSRSFELLLD-MNAAELGEFLNRlPPNGRLIYELLRRFPKieVEAEVLPITRDLTL--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 2097 eDDDEVVGPVIAPFFP--HKKDEGWWIVIGDTEKNSLLGIKRVTLNK---SLSVKLDFTCP-SEAGEHSLKLFFMSDSYS 2170
Cdd:smart00973 226 -RVELEITPVFAWDLPrhKGKSESWWLVVGDSDTNELLAIKRVTLRKkkkSNEVKLDFTVPlSEPGPENYTVYLISDSYL 304
|
330
....*....|
gi 1317352187 2171 GCDQEFDLPI 2180
Cdd:smart00973 305 GCDQEVSFSL 314
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1377-1564 |
1.19e-73 |
|
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: 243.82 E-value: 1.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1377 FNPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLWSTPNHGRCVYIAPFQEVVDLQVAQWRQKFgKIQGGKNIV 1456
Cdd:cd18022 2 FNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRF-EEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1457 ALTGETSADLRLLESGDVIFATPTQWDVMSRRWKQRKNVQTVALFIADELHLIGSDVGPTYEIIVSRMRYIAHQTKNPIR 1536
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*...
gi 1317352187 1537 IVCLSTSLANAQDLGEWIGSTPHTIFNF 1564
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNF 188
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
730-920 |
2.93e-66 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 221.27 E-value: 2.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 730 RPCPLKQEFIGVTEKKAIKRFQVMNE-----VTYQKVVEQAGKNQVLIFVHSRKETAKTAKTIKdmalekdtlrlflnps 804
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 805 sasrevlqdelpsikdpnlyellpfGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPAHTVIIKGTQVYS 884
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 1317352187 885 PEkgRWVELSPQDVLQMLGRAGRPQYDTFGEGIIIT 920
Cdd:cd18795 120 GK--GYRELSPLEYLQMIGRAGRPGFDTRGEAIIMT 153
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1374-1899 |
4.28e-64 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 228.63 E-value: 4.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1374 VDKFNPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLWStpNHGRCVYIAPF----QEVVDlqvaQWRQKFGKI 1449
Cdd:COG1204 20 IEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALL--NGGKALYIVPLralaSEKYR----EFKRDFEEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1450 qgGKNIVALTGETSADLRLLESGDVIFATPTQWDVMSRR---WKQRknvqtVALFIADELHLIGSDV-GPTYEIIVSRMR 1525
Cdd:COG1204 94 --GIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNgpsWLRD-----VDLVVVDEAHLIDDESrGPTLEVLLARLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1526 YIAHqtknPIRIVCLSTSLANAQDLGEWIGSTPhTIFNFhpsvRPVPLEI---------HIQSYSIPHFASLmmAMAKPT 1596
Cdd:COG1204 167 RLNP----EAQIVALSATIGNAEEIAEWLDAEL-VKSDW----RPVPLNEgvlydgvlrFDDGSRRSKDPTL--ALALDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1597 YvaitnySSDRPAIVFVPSRKQCRFTAVDLltfcaADGTTDRFLHAHASDIEDHLKQI--------NDKALAETLQHGVG 1668
Cdd:COG1204 236 L------EEGGQVLVFVSSRRDAESLAKKL-----ADELKRRLTPEEREELEELAEELlevseethTNEKLADCLEKGVA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1669 FYHEALSKQDKRIVEELFESGAIQVVVAsrdT---CWGINLSCHMVIVMGTqffegkeHRYADYPIT--DVLQMMGRACR 1743
Cdd:COG1204 305 FHHAGLPSELRRLVEDAFREGLIKVLVA---TptlAAGVNLPARRVIIRDT-------KRGGMVPIPvlEFKQMAGRAGR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1744 PQHDDTGRCVLMCQAIK---KDFYKKFLYEALPVESHL--DHFLHDHFNAEVVTKTIENKQDAVDYLTWTFLYrrmvenp 1818
Cdd:COG1204 375 PGYDPYGEAILVAKSSDeadELFERYILGEPEPIRSKLanESALRTHLLALIASGFANSREELLDFLENTFYA------- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1819 nyygmqgsdHRHLSDHLSELVETTVNDLSASKCIALEDELdVTPLNLGMIAAYYNVSYTTVEMFSMSLNEKTKLKGLLEI 1898
Cdd:COG1204 448 ---------YQYDKGDLEEVVDDALEFLLENGFIEEDGDR-LRATKLGKLVSRLYIDPLTAAELVDGLRKADEEFTDLGL 517
|
.
gi 1317352187 1899 L 1899
Cdd:COG1204 518 L 518
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
529-726 |
5.01e-60 |
|
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: 204.42 E-value: 5.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 529 LNRIQSKIYPVAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNeetgiidtdafKIVYIAPMKALVQEMVGNFSSRL 608
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGG-----------KAVYIAPTRALVNQKEADLRERF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 609 QQYGIKVSELTGDRQLTKQQISETQIIVTTPEKWDVITRKATDRsYTNLVRLIIIDEVHLLHD-DRGPVIESIVSRTIRh 687
Cdd:cd17921 71 GPLGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDgERGVVLELLLSRLLR- 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1317352187 688 meqTQEMIRLVGLSATLPNYGDVATFLRVdpkKGLFHFD 726
Cdd:cd17921 149 ---INKNARFVGLSATLPNAEDLAEWLGV---EDLIRFD 181
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
530-731 |
2.04e-58 |
|
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: 200.66 E-value: 2.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 530 NRIQSKIYPVAFEQDENLLVCAPTGSGKTNVAMLCILnemeknRN-EETGIIDTDAFKIVYIAPMKALVQEMVGNFSSRL 608
Cdd:cd18023 3 NRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAIL------RLlKERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 609 QQYGIKVSELTGDRQLTK-QQISETQIIVTTPEKWDVITRKATDR-SYTNLVRLIIIDEVHLLHDDRGPVIESIVSR--T 684
Cdd:cd18023 77 GPLGLSCAELTGDTEMDDtFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIKENRGATLEVVVSRmkT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1317352187 685 I-RHMEQTQEM---IRLVGLSATLPNYGDVATFLRVDPkKGLFHFDSSFRP 731
Cdd:cd18023 157 LsSSSELRGSTvrpMRFVAVSATIPNIEDLAEWLGDNP-AGCFSFGESFRP 206
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
1377-1570 |
1.83e-57 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 197.96 E-value: 1.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1377 FNPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLWS-----TPNHGRCVYIAPFQEVVDLQVAQWRQKFGKIqg 1451
Cdd:cd18023 2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKernplPWGNRKVVYIAPIKALCSEKYDDWKEKFGPL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1452 GKNIVALTGETSA-DLRLLESGDVIFATPTQWDVMSRRWKQRKN-VQTVALFIADELHLIGSDVGPTYEIIVSRMRYIAH 1529
Cdd:cd18023 80 GLSCAELTGDTEMdDTFEIQDADIILTTPEKWDSMTRRWRDNGNlVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1317352187 1530 ------QTKNPIRIVCLSTSLANAQDLGEWIGSTPHTIFNFHPSVRP 1570
Cdd:cd18023 160 sselrgSTVRPMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
530-726 |
8.21e-55 |
|
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: 189.89 E-value: 8.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 530 NRIQSKIYPVAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNrneetgiidtDAFKIVYIAPMKALVQEMVGNFSSRLQ 609
Cdd:cd18022 3 NPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKY----------PGSKVVYIAPLKALVRERVDDWKKRFE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 610 Q-YGIKVSELTGDRQLTKQQISETQIIVTTPEKWDVITRKATDRSYTNLVRLIIIDEVHLLHDDRGPVIESIVSRTIRHM 688
Cdd:cd18022 73 EkLGKKVVELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYIS 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1317352187 689 EQTQEMIRLVGLSATLPNYGDVATFLRVdPKKGLFHFD 726
Cdd:cd18022 153 SQTEKPVRLVGLSTALANAGDLANWLGI-KKMGLFNFR 189
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
541-1042 |
1.05e-54 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 204.73 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 541 FEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRneetgiidtdafKIVYIAPMKALVQEMVGNFSsRLQQYGIKVSELTG 620
Cdd:PRK01172 34 LRKGENVIVSVPTAAGKTLIAYSAIYETFLAGL------------KSIYIVPLRSLAMEKYEELS-RLRSLGMRVKISIG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 621 DRQLTKQQISETQIIVTTPEKWDVITRKatDRSYTNLVRLIIIDEVHLLHD-DRGPVIESIVSrTIRHMEQTqemIRLVG 699
Cdd:PRK01172 101 DYDDPPDFIKRYDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDeDRGPTLETVLS-SARYVNPD---ARILA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 700 LSATLPNYGDVATFLRVDPKKglfhfdSSFRPCPLKqefIGVTEKKAI-----KRFQVMNEVTYQKVVEQAGknQVLIFV 774
Cdd:PRK01172 175 LSATVSNANELAQWLNASLIK------SNFRPVPLK---LGILYRKRLildgyERSQVDINSLIKETVNDGG--QVLVFV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 775 HSRKETAKTAKtikdmalekDTLRLFlnPSSASREVLQDElPSIKDPNLYELLPFGFAIHHAGMSRTDRTTVEDLFADGH 854
Cdd:PRK01172 244 SSRKNAEDYAE---------MLIQHF--PEFNDFKVSSEN-NNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 855 IQVLVSTATLAWGVNLPAHTVIIKGTQVYSPEKGRWveLSPQDVLQMLGRAGRPQYDTFGEGIII----TSHNELQYYLS 930
Cdd:PRK01172 312 IKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRY--LSNMEIKQMIGRAGRPGYDQYGIGYIYaaspASYDAAKKYLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 931 llNQQLPIESQFVS--KLADNLNAEIVLGTVRNRDEAVQWLgytylyvrmlrNPTLYGISTDYLEEDPYleqkrvdlIHS 1008
Cdd:PRK01172 390 --GEPEPVISYMGSqrKVRFNTLAAISMGLASSMEDLILFY-----------NETLMAIQNGVDEIDYY--------IES 448
|
490 500 510
....*....|....*....|....*....|....
gi 1317352187 1009 AGMLLDKSNLMKYDKKtgrFQVTELGRIASHFYI 1042
Cdd:PRK01172 449 SLKFLKENGFIKGDVT---LRATRLGKLTSDLYI 479
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
545-1042 |
6.96e-54 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 203.12 E-value: 6.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 545 ENLLVCAPTGSGKTNVAMLCILNEMEKnrneETGiidtdafKIVYIAPMKALVQEMVGNFSSrLQQYGIKVSELTGDRQL 624
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKLLR----EGG-------KAVYLVPLKALAEEKYREFKD-WEKLGLRVAMTTGDYDS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 625 TKQQISETQIIVTTPEKWDVITRKATdrSYTNLVRLIIIDEVHLLHD-DRGPVIESIVSrtirHMEQTQEMIrlvGLSAT 703
Cdd:PRK00254 108 TDEWLGKYDIIIATAEKFDSLLRHGS--SWIKDVKLVVADEIHLIGSyDRGATLEMILT----HMLGRAQIL---GLSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 704 LPNYGDVATFLRVDPKKglfhfdSSFRPCPLK-----QEFIgVTEKKAIKRFQV-MNEVTYQKVveQAGKnQVLIFVHSR 777
Cdd:PRK00254 179 VGNAEELAEWLNAELVV------SDWRPVKLRkgvfyQGFL-FWEDGKIERFPNsWESLVYDAV--KKGK-GALVFVNTR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 778 KETAKTAktikdMALEKDTLRLFLNPSSASREVLQDELPSI-KDPNLYELLPFGFAIHHAGMSRTDRTTVEDLFADGHIQ 856
Cdd:PRK00254 249 RSAEKEA-----LELAKKIKRFLTKPELRALKELADSLEENpTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 857 VLVSTATLAWGVNLPAHTVIIKGTQVYSpEKGrWVELSPQDVLQMLGRAGRPQYDTFGEGIIITSHNE----LQYYL--- 929
Cdd:PRK00254 324 VITATPTLSAGINLPAFRVIIRDTKRYS-NFG-WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklMERYIfgk 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 930 -SLLNQQLPIESQFVSKLAdnlnAEIVLGTVRNRDEAVQWLGYTYLYvrmlrnptlygistdYLEEDPY-LEQKRVDLIH 1007
Cdd:PRK00254 402 pEKLFSMLSNESAFRSQVL----ALITNFGVSNFKELVNFLERTFYA---------------HQRKDLYsLEEKAKEIVY 462
|
490 500 510
....*....|....*....|....*....|....*
gi 1317352187 1008 sagmLLDKSNLMKYDKKTgRFQVTELGRIASHFYI 1042
Cdd:PRK00254 463 ----FLLENEFIDIDLED-RFIPLPLGIRTSQLYI 492
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
1377-1565 |
2.02e-52 |
|
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: 182.46 E-value: 2.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1377 FNPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLWSTPNhGRCVYIAPFQEVVDLQVAQWRQKFGkiQGGKNIV 1456
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSG-GKAVYIAPTRALVNQKEADLRERFG--PLGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1457 ALTGETSADLRLLESGDVIFATPTQWDVMSRRWKQRkNVQTVALFIADELHLIGSDV-GPTYEIIVSRMRYIAhqtkNPI 1535
Cdd:cd17921 79 LLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDGErGVVLELLLSRLLRIN----KNA 153
|
170 180 190
....*....|....*....|....*....|
gi 1317352187 1536 RIVCLSTSLANAQDLGEWIGSTPHtiFNFH 1565
Cdd:cd17921 154 RFVGLSATLPNAEDLAEWLGVEDL--IRFD 181
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
512-1042 |
7.33e-51 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 194.41 E-value: 7.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 512 IEEL--PPWVHGAFKGARIlnriqSKIYPVAFE-------QDENLLVCAPTGSGKTNVAMLCILNEMEKNRneetgiidt 582
Cdd:PRK02362 3 IAELplPEGVIEFYEAEGI-----EELYPPQAEaveagllDGKNLLAAIPTASGKTLIAELAMLKAIARGG--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 583 dafKIVYIAPMKALVQEMVGNFSsRLQQYGIKVSELTGDRQLTKQQISETQIIVTTPEKWDVITRKATdrSYTNLVRLII 662
Cdd:PRK02362 69 ---KALYIVPLRALASEKFEEFE-RFEELGVRVGISTGDYDSRDEWLGDNDIIVATSEKVDSLLRNGA--PWLDDITCVV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 663 IDEVHLLHD-DRGPVIESivsrTIRHMEQTQEMIRLVGLSATLPNYGDVATFLrvdpKKGLFhfDSSFRPCPLKQefiGV 741
Cdd:PRK02362 143 VDEVHLIDSaNRGPTLEV----TLAKLRRLNPDLQVVALSATIGNADELADWL----DAELV--DSEWRPIDLRE---GV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 742 TEKKAIkRF-----QVMNEVTYQKV------VEQAGknQVLIFVHSRKETAKTAKTIKDmALeKDTLRLFLNPSSASrev 810
Cdd:PRK02362 210 FYGGAI-HFddsqrEVEVPSKDDTLnlvldtLEEGG--QCLVFVSSRRNAEGFAKRAAS-AL-KKTLTAAERAELAE--- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 811 LQDELPSIKDP----NLYELLPFGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPAHTVIIKGTQVYSPE 886
Cdd:PRK02362 282 LAEEIREVSDTetskDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 887 KGrwveLSPQDVL---QMLGRAGRPQYDTFGEGIIIT-SHNELQ----YYLSLLNQqlPIESQFVSK--LADNLNAEIVL 956
Cdd:PRK02362 362 AG----MQPIPVLeyhQMAGRAGRPGLDPYGEAVLLAkSYDELDelfeRYIWADPE--DVRSKLATEpaLRTHVLSTIAS 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 957 GTVRNRDEAVQWLGYTyLYVRMLRNPTLYGISTD----YLEEdpyleqkrvdlihsAGMLldksnlmkyDKKTGRFQVTE 1032
Cdd:PRK02362 436 GFARTRDGLLEFLEAT-FYATQTDDTGRLERVVDdvldFLER--------------NGMI---------EEDGETLEATE 491
|
570
....*....|
gi 1317352187 1033 LGRIASHFYI 1042
Cdd:PRK02362 492 LGHLVSRLYI 501
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
295-403 |
1.09e-50 |
|
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: 174.72 E-value: 1.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 295 EQKISPHDIDAFWLQRLVANYYSDPHTAQEKTSSTMQILASDVN-TRDCENELMALFEYDKFDLVKILTRNRELIVWCTK 373
Cdd:pfam18149 2 KDSLDPHDIDAFWLQRLLSKFYGDAIEAQKKAEEVLDILESAADdLRECENQLVELLDYDKFDLVKLLLKNRDKIVWCTK 81
|
90 100 110
....*....|....*....|....*....|.
gi 1317352187 374 LARAGTDgAERQNIEREMREH-GLEWILRDL 403
Cdd:pfam18149 82 LARAQSE-EEKQAIEEEMRSNpGLAWILDEL 111
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1569-1757 |
7.47e-47 |
|
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: 165.42 E-value: 7.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1569 RPVPLEIHIQSYSIPHFASLMMAMAK-----PTYVAITNYSSDRPAIVFVPSRKQCRFTAVDLLtfcaadgttdrflhah 1643
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1644 asdiedhlkqindkalaetlqhGVGFYHEALSKQDKRIVEELFESGAIQVVVASRDTCWGINLSCHMVIVMGTQFFEGKE 1723
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 1317352187 1724 HRYadYPITDVLQMMGRACRPQHDDTGRCVLMCQ 1757
Cdd:cd18795 123 YRE--LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
540-942 |
4.25e-46 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 179.75 E-value: 4.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 540 AFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRneetgiidtdafKIVYIAPMKALVQEmvgNFSSRLQQYG-IKVSEL 618
Cdd:COG4581 36 ALEAGRSVLVAAPTGSGKTLVAEFAIFLALARGR------------RSFYTAPIKALSNQ---KFFDLVERFGaENVGLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 619 TGDRQLtkqqISETQIIVTTPEkwdvITRKATDRSYTNLVRL--IIIDEVHLLHD-DRGPVIE-SIVsrtirHMEQTqem 694
Cdd:COG4581 101 TGDASV----NPDAPIVVMTTE----ILRNMLYREGADLEDVgvVVMDEFHYLADpDRGWVWEePII-----HLPAR--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 695 IRLVGLSATLPNYGDVATFLR--------VDpkkglfhfdSSFRPCPLKQEFigVTEKKAIKRFQVMNEVTY----QKVV 762
Cdd:COG4581 165 VQLVLLSATVGNAEEFAEWLTrvrgetavVV---------SEERPVPLEFHY--LVTPRLFPLFRVNPELLRppsrHEVI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 763 EQAGKNQVL--IFVH-SRKETAKTAKTIKDMAL----EKDTLRLFLNPSSASREVLQDelpsikdPNLYELLPFGFAIHH 835
Cdd:COG4581 234 EELDRGGLLpaIVFIfSRRGCDEAAQQLLSARLttkeERAEIREAIDEFAEDFSVLFG-------KTLSRLLRRGIAVHH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 836 AGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPAHTVIIKGTQVYSPEKGRwvELSPQDVLQMLGRAGRPQYDTFGE 915
Cdd:COG4581 307 AGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHR--PLTAREFHQIAGRAGRRGIDTEGH 384
|
410 420
....*....|....*....|....*....
gi 1317352187 916 GIII-TSHNELQYYLSLLNQQL-PIESQF 942
Cdd:COG4581 385 VVVLaPEHDDPKKFARLASARPePLRSSF 413
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
527-726 |
7.76e-43 |
|
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: 155.49 E-value: 7.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 527 RILNRIQSKIYPVAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNEetgiidtdafKIVYIAPMKALVQEMVGNFSS 606
Cdd:cd18021 2 KFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKG----------RAVYIAPMQELVDARYKDWRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 607 RLQQY-GIKVSELTGDRQLTKQQISETQIIVTTPEKWDVITRKATDRSYTNLVRLIIIDEVHLLHDDRGPVIESIVSRTi 685
Cdd:cd18021 72 KFGPLlGKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRM- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1317352187 686 RHME-QTQEMIRLVGLSATLPNYGDVATFLRVDPkKGLFHFD 726
Cdd:cd18021 151 RYISsQLEKPIRIVGLSSSLANARDVGEWLGASK-STIFNFH 191
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1359-1929 |
3.96e-37 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 151.89 E-value: 3.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1359 SALRNREYEAVYngwvdkfnPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLWSTPNhGRCVYIAPFQEVVDlq 1438
Cdd:PRK00254 14 RVLKERGIEELY--------PPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREG-GKAVYLVPLKALAE-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1439 vaqwrQKFGKIQG----GKNIVALTGETSADLRLLESGDVIFATPTQWDVMSR---RWkqrknVQTVALFIADELHLIGS 1511
Cdd:PRK00254 83 -----EKYREFKDweklGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1512 -DVGPTYEIIVSRMryiahqtKNPIRIVCLSTSLANAQDLGEWIGSTPhtifnFHPSVRPVPL--------EIHIQSYSI 1582
Cdd:PRK00254 153 yDRGATLEMILTHM-------LGRAQILGLSATVGNAEELAEWLNAEL-----VVSDWRPVKLrkgvfyqgFLFWEDGKI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1583 PHFASLMMAMAkptYVAItnySSDRPAIVFVPSRKQCRFTAVDLLTFCAA--DGTTDRFLHAHASDIEDHlkQINDKaLA 1660
Cdd:PRK00254 221 ERFPNSWESLV---YDAV---KKGKGALVFVNTRRSAEKEALELAKKIKRflTKPELRALKELADSLEEN--PTNEK-LK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1661 ETLQHGVGFYHEALSKQDKRIVEELFESGAIQVVVASRDTCWGINLSCHMVIVMGTQffegkehRYADY-----PITDVL 1735
Cdd:PRK00254 292 KALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTK-------RYSNFgwediPVLEIQ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1736 QMMGRACRPQHDDTGRCVLMCQAIK-KDFYKKF-------LYEALPVESHldhfLHDHFNAEVVTKTIENKQDAVDYLTW 1807
Cdd:PRK00254 365 QMMGRAGRPKYDEVGEAIIVATTEEpSKLMERYifgkpekLFSMLSNESA----FRSQVLALITNFGVSNFKELVNFLER 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1808 TFlyrrmvenpnyYGMQGSDHRHLSDHLSE----LVETTVNDLSaskciaLEDEldVTPLNLGMIAAYYNVSYTTVEMFS 1883
Cdd:PRK00254 441 TF-----------YAHQRKDLYSLEEKAKEivyfLLENEFIDID------LEDR--FIPLPLGIRTSQLYIDPLTAKKFK 501
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1317352187 1884 MSLNEKTKLK---GLLEILSSAAEFESIPVRHHEDTVLKKIYDRLPVKL 1929
Cdd:PRK00254 502 DAFPKIEKNPnplGIFQLIASTPDMTPLNYSRKEMEDLLDEAYEMEDRL 550
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
530-705 |
3.39e-36 |
|
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: 135.45 E-value: 3.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 530 NRIQSKIYPvAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNeetgiidtdAFKIVYIAPMKALVQEMVGNFSSRLQ 609
Cdd:pfam00270 1 TPIQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN---------GPQALVLAPTRELAEQIYEELKKLGK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 610 QYGIKVSELTG--DRQLTKQQISETQIIVTTPEKWDVITRKatdRSYTNLVRLIIIDEVHLLHD-DRGPVIESIVSRtir 686
Cdd:pfam00270 71 GLGLKVASLLGgdSRKEQLEKLKGPDILVGTPGRLLDLLQE---RKLLKNLKLLVLDEAHRLLDmGFGPDLEEILRR--- 144
|
170
....*....|....*....
gi 1317352187 687 hmeqTQEMIRLVGLSATLP 705
Cdd:pfam00270 145 ----LPKKRQILLLSATLP 159
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
541-714 |
1.99e-34 |
|
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: 130.92 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 541 FEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRneetgiidtdafKIVYIAPMKALVQEMVGNFsSRLQQYGIKVSELTG 620
Cdd:cd18028 14 LLKGENLLISIPTASGKTLIAEMAMVNTLLEGG------------KALYLVPLRALASEKYEEF-KKLEEIGLKVGISTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 621 DRQLTKQQISETQIIVTTPEKWDVITRKATdrSYTNLVRLIIIDEVHLLHD-DRGPVIESIVSRtIRHMEQTqemIRLVG 699
Cdd:cd18028 81 DYDEDDEWLGDYDIIVATYEKFDSLLRHSP--SWLRDVGVVVVDEIHLISDeERGPTLESIVAR-LRRLNPN---TQIIG 154
|
170
....*....|....*
gi 1317352187 700 LSATLPNYGDVATFL 714
Cdd:cd18028 155 LSATIGNPDELAEWL 169
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1393-1753 |
6.43e-29 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 126.21 E-value: 6.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1393 DNVFVGAPTGSGKTVCAEFALLRLWSTpnHGRCVYIAPFQEVVDlqvaqwrQKF---GKIQGGKNIVALTGETS--AD-- 1465
Cdd:COG4581 41 RSVLVAAPTGSGKTLVAEFAIFLALAR--GRRSFYTAPIKALSN-------QKFfdlVERFGAENVGLLTGDASvnPDap 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1466 --------LR--LLESGDVIfatptqwdvmsrrwkqrKNVQTValfIADELHLIG-SDVGPTYE--IIvsrmrYIAHQtk 1532
Cdd:COG4581 112 ivvmtteiLRnmLYREGADL-----------------EDVGVV---VMDEFHYLAdPDRGWVWEepII-----HLPAR-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1533 npIRIVCLSTSLANAQDLGEWI----GSTpHTIFNFHpsvRPVPLEIH--IQSYSIPHFASLMMAMAKPTYVAITNYSSD 1606
Cdd:COG4581 165 --VQLVLLSATVGNAEEFAEWLtrvrGET-AVVVSEE---RPVPLEFHylVTPRLFPLFRVNPELLRPPSRHEVIEELDR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1607 R---PAIVFVPSRKQCRfTAVDLLTfcAADGTTD---RFLHAHASDIEDHLKQINDKALAETLQHGVGFYHEALSKQDKR 1680
Cdd:COG4581 239 GgllPAIVFIFSRRGCD-EAAQQLL--SARLTTKeerAEIREAIDEFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPKYRR 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317352187 1681 IVEELFESGAIQVVVASrDT-CWGINLSCHMVIVMGTQFFEGKEHRyadyPIT--DVLQMMGRACRPQHDDTGRCV 1753
Cdd:COG4581 316 LVEELFQAGLLKVVFAT-DTlAVGINMPARTVVFTKLSKFDGERHR----PLTarEFHQIAGRAGRRGIDTEGHVV 386
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1392-1787 |
2.36e-28 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 123.84 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1392 NDNVFVGAPTGSGKTVCAEFALLRLWSTpnHGRCVYIAPFQEvvdLQVAQWRQKFGKIQGGKNIVALTGETSADLRLLES 1471
Cdd:PRK01172 37 GENVIVSVPTAAGKTLIAYSAIYETFLA--GLKSIYIVPLRS---LAMEKYEELSRLRSLGMRVKISIGDYDDPPDFIKR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1472 GDVIFATPTQWDVMSRRwkQRKNVQTVALFIADELHLIG-SDVGPTYEIIVSRMRYIahqtkNP-IRIVCLSTSLANAQD 1549
Cdd:PRK01172 112 YDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGdEDRGPTLETVLSSARYV-----NPdARILALSATVSNANE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1550 LGEWIGSTphTIFNfhpSVRPVPLEIhiqsySIPHFASLMMAMAKPTYVAITNYSSDR-----PAIVFVPSRKQCRFTAV 1624
Cdd:PRK01172 185 LAQWLNAS--LIKS---NFRPVPLKL-----GILYRKRLILDGYERSQVDINSLIKETvndggQVLVFVSSRKNAEDYAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1625 DLLTFCAADgttdrflhahaSDIEDHLKQIN--DKALAETLQHGVGFYHEALSKQDKRIVEELFESGAIQVVVASRDTCW 1702
Cdd:PRK01172 255 MLIQHFPEF-----------NDFKVSSENNNvyDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1703 GINLSCHMVIVMGTQffegkehRYADYPIT-----DVLQMMGRACRPQHDDTGRCVL-MCQAIKKDFYKKFLY-EALPVE 1775
Cdd:PRK01172 324 GVNLPARLVIVRDIT-------RYGNGGIRylsnmEIKQMIGRAGRPGYDQYGIGYIyAASPASYDAAKKYLSgEPEPVI 396
|
410
....*....|..
gi 1317352187 1776 SHLDHFLHDHFN 1787
Cdd:PRK01172 397 SYMGSQRKVRFN 408
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
503-910 |
3.24e-28 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 123.85 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 503 HAENERLISIEELPpwVHGAFKgaRILNRIQSKIYPV---AFE----QDENLLVCAPTGSGKTNVA-MLCILNEMEKNRn 574
Cdd:COG1202 181 TTDEVDTVPVDDLD--LPPELK--DLLEGRGEELLPVqslAVEngllEGKDQLVVSATATGKTLIGeLAGIKNALEGKG- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 575 eetgiidtdafKIVYIAPMKALVQEMVGNFSSRlqqY--GIKVSELTGDRQLT---KQQISETQIIVTTPEKWDVITRka 649
Cdd:COG1202 256 -----------KMLFLVPLVALANQKYEDFKDR---YgdGLDVSIRVGASRIRddgTRFDPNADIIVGTYEGIDHALR-- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 650 TDRSYTNlVRLIIIDEVHLLHD-DRGPVIESIVSRtIRHM-EQTQemirLVGLSATLPNYGDVATFLRVDpkkgLFHFDS 727
Cdd:COG1202 320 TGRDLGD-IGTVVIDEVHMLEDpERGHRLDGLIAR-LKYYcPGAQ----WIYLSATVGNPEELAKKLGAK----LVEYEE 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 728 sfRPCPLKQEFIGVTEKKAIKRFQVMNEVTYQKVVEQAGKNQVLIFVHSRKETAKTAktikdmalekdtlrlflnpssas 807
Cdd:COG1202 390 --RPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFTNSRRRCHEIA----------------------- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 808 revlqdelpsikdpnlyELLPFGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPAHTVI-------IKgt 880
Cdd:COG1202 445 -----------------RALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIfdslamgIE-- 505
|
410 420 430
....*....|....*....|....*....|
gi 1317352187 881 qvyspekgrWveLSPQDVLQMLGRAGRPQY 910
Cdd:COG1202 506 ---------W--LSVQEFHQMLGRAGRPDY 524
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
542-731 |
3.54e-27 |
|
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: 111.15 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 542 EQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNeetgiidtdafKIVYIAPMKALVQEMVGNFSSRLQQYGIKVSELTGD 621
Cdd:cd18026 31 LEGRNLVYSLPTSGGKTLVAEILMLKRLLERRK-----------KALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 622 R-QLTKQQISETQIIVTTPEKWDVITRKATDRSYTNLVRLIIIDEVHLLHD-DRGPVIESIVSRtIRHMeqTQEMIRLVG 699
Cdd:cd18026 100 KgRSPPKRRKSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDgHRGALLELLLTK-LLYA--AQKNIQIVG 176
|
170 180 190
....*....|....*....|....*....|..
gi 1317352187 700 LSATLPNYGDVATFLRVDpkkglfHFDSSFRP 731
Cdd:cd18026 177 MSATLPNLEELASWLRAE------LYTTNFRP 202
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1394-1863 |
4.41e-27 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 120.06 E-value: 4.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1394 NVFVGAPTGSGKTVCAEFALLRlwSTPNHGRCVYIAPFQevvdlqvAQWRQKF----GKIQGGKNIVALTGETSADLRLL 1469
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAMLK--AIARGGKALYIVPLR-------ALASEKFeefeRFEELGVRVGISTGDYDSRDEWL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1470 ESGDVIFATPTQWDVMSR---RWkqrknVQTVALFIADELHLIGS-DVGPTYEIIVSRMRYIahqtkNP-IRIVCLSTSL 1544
Cdd:PRK02362 112 GDNDIIVATSEKVDSLLRngaPW-----LDDITCVVVDEVHLIDSaNRGPTLEVTLAKLRRL-----NPdLQVVALSATI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1545 ANAQDLGEWIGSTPhtifnFHPSVRPVPLEIHIQSYSIPHFASLMMAMAKPTYVAITNYSSDRPA-----IVFVPSRKQC 1619
Cdd:PRK02362 182 GNADELADWLDAEL-----VDSEWRPIDLREGVFYGGAIHFDDSQREVEVPSKDDTLNLVLDTLEeggqcLVFVSSRRNA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1620 RFTAVDlltfcAADGTTDRFLHAHASDIEDHLKQIND-------KALAETLQHGVGFYHEALSKQDKRIVEELFESGAIQ 1692
Cdd:PRK02362 257 EGFAKR-----AASALKKTLTAAERAELAELAEEIREvsdtetsKDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1693 VVVASRDTCWGINLSCHMVIVMGTQFFEGKEHrYADYPITDVLQMMGRACRPQHDDTGRCVLMC---QAIKKDFYKKFLY 1769
Cdd:PRK02362 332 VISSTPTLAAGLNLPARRVIIRDYRRYDGGAG-MQPIPVLEYHQMAGRAGRPGLDPYGEAVLLAksyDELDELFERYIWA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1770 EALPVESHL--DHFLHDHFNAEVVTKTIENKQDAVDYLTWTFlyrrmvenpnyYGMQGSDHRhlsdHLSELVETTVNDLS 1847
Cdd:PRK02362 411 DPEDVRSKLatEPALRTHVLSTIASGFARTRDGLLEFLEATF-----------YATQTDDTG----RLERVVDDVLDFLE 475
|
490
....*....|....*..
gi 1317352187 1848 ASKCIA-LEDELDVTPL 1863
Cdd:PRK02362 476 RNGMIEeDGETLEATEL 492
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
1378-1551 |
2.00e-26 |
|
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: 109.38 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1378 NPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLW-------STPNHG--RCVYIAPFQEVVDLQVAQwrqkFGK 1448
Cdd:cd18019 19 NRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIgkhrnpdGTINLDafKIVYIAPMKALVQEMVGN----FSK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1449 IQGGKNIVA--LTGETSADLRLLESGDVIFATPTQWDVMSRRWKQRKNVQTVALFIADELHLIGSDVGPTYEIIVSRMRY 1526
Cdd:cd18019 95 RLAPYGITVaeLTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDDRGPVLESIVARTIR 174
|
170 180
....*....|....*....|....*
gi 1317352187 1527 IAHQTKNPIRIVCLSTSLANAQDLG 1551
Cdd:cd18019 175 QIEQTQEYVRLVGLSATLPNYEDVA 199
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
544-714 |
3.03e-26 |
|
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: 106.90 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 544 DENLLVCAPTGSGKTNVAMLCILNEMEKNRNeetgiidtDAFKIVYIAPMKALVQEMVGNFSSRLQ--QYGIKVSELTGD 621
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPE--------KGVQVLYISPLKALINDQERRLEEPLDeiDLEIPVAVRHGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 622 ---RQLTKQQISETQIIVTTPEKWDVI-TRKATDRSYTNLvRLIIIDEVH-LLHDDRGPVIESIVSRtIRHMEQTQemIR 696
Cdd:cd17922 73 tsqSEKAKQLKNPPGILITTPESLELLlVNKKLRELFAGL-RYVVVDEIHaLLGSKRGVQLELLLER-LRKLTGRP--LR 148
|
170
....*....|....*...
gi 1317352187 697 LVGLSATLPNYGDVATFL 714
Cdd:cd17922 149 RIGLSATLGNLEEAAAFL 166
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
524-738 |
6.81e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 107.19 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 524 KGARILNRIQSKIYPVAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNeetgiidtdaFKIVYIAPMKALVQEMVGN 603
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKG----------GRVLVLVPTRELAEQWAEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 604 FSSRLQQYGIKVSELTGD----RQLTKQQISETQIIVTTPEKWdvITRKATDRSYTNLVRLIIIDEVHLLHD-DRGPVIE 678
Cdd:smart00487 74 LKKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRL--LDLLENDKLSLSNVDLVILDEAHRLLDgGFGDQLE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 679 SIVSRTIRhmeqtqeMIRLVGLSATLPNYGDVATFLRVdpkKGLFHFDSSFRPCPLKQEF 738
Cdd:smart00487 152 KLLKLLPK-------NVQLLLLSATPPEEIENLLELFL---NDPVFIDVGFTPLEPIEQF 201
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1378-1550 |
4.32e-25 |
|
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: 103.86 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1378 NPIQTQVFNALYNmNDNVFVGAPTGSGKTVCAEFALL-RLWSTPNHGRCVYIAPFQEVVDLQVAQWRqKFGKIQGGKNIV 1456
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALeALDKLDNGPQALVLAPTRELAEQIYEELK-KLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1457 ALTG-ETSADLRLLESGDVIFATPTQWDVMSRrwkQRKNVQTVALFIADELHLIGSDV-GPTYEIIVSRMRYiahqtknP 1534
Cdd:pfam00270 79 LLGGdSRKEQLEKLKGPDILVGTPGRLLDLLQ---ERKLLKNLKLLVLDEAHRLLDMGfGPDLEEILRRLPK-------K 148
|
170
....*....|....*..
gi 1317352187 1535 IRIVCLSTSLA-NAQDL 1550
Cdd:pfam00270 149 RQILLLSATLPrNLEDL 165
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
1376-1555 |
2.78e-22 |
|
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: 96.25 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1376 KFNPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLWStpNHGRCVYIAPFQEVVDlqvaQWRQKFGKIQGGKNI 1455
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLL--EGGKALYLVPLRALAS----EKYEEFKKLEEIGLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1456 VAL-TGETSADLRLLESGDVIFATPTQWDVMsrrWKQRKN-VQTVALFIADELHLIGS-DVGPTYEIIVSRMRYIAHQTk 1532
Cdd:cd18028 75 VGIsTGDYDEDDEWLGDYDIIVATYEKFDSL---LRHSPSwLRDVGVVVVDEIHLISDeERGPTLESIVARLRRLNPNT- 150
|
170 180
....*....|....*....|...
gi 1317352187 1533 npiRIVCLSTSLANAQDLGEWIG 1555
Cdd:cd18028 151 ---QIIGLSATIGNPDELAEWLN 170
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1376-1564 |
8.66e-22 |
|
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: 95.19 E-value: 8.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1376 KFNPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLR-LWSTPNHG--------RCVYIAPFQ----EVVDlqvaqw 1442
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHeIRQHVNQGgvikkddfKIVYIAPMKalaaEMVE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1443 rqKFGKIQGGKNIVA--LTGETSADLRLLESGDVIFATPTQWDVMSRRWKQRKN-VQTVALFIADELHLIGSDVGPTYEI 1519
Cdd:cd18020 75 --KFSKRLAPLGIKVkeLTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVAlSQLVRLLIIDEVHLLHDDRGPVIES 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1317352187 1520 IVSRMRYIAHQTKNPIRIVCLSTSLANAQDLGEWIGSTPHT-IFNF 1564
Cdd:cd18020 153 LVARTLRQVESTQSMIRIVGLSATLPNYLDVADFLRVNPYKgLFFF 198
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1376-1561 |
6.13e-20 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 90.24 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1376 KFNPIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEFALLRLWSTPNHGRCVYIAPFQEVVDlQVAQWRQKFGKIQGGKNI 1455
Cdd:smart00487 8 PLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAE-QWAEELKKLGPSLGLKVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1456 VALTGETS-ADLRLLESG--DVIFATPTQWDVMSRRWKqrKNVQTVALFIADELH-LIGSDVGPTYEIIVSRMRyiahqt 1531
Cdd:smart00487 87 GLYGGDSKrEQLRKLESGktDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP------ 158
|
170 180 190
....*....|....*....|....*....|.
gi 1317352187 1532 kNPIRIVCLS-TSLANAQDLGEWIGSTPHTI 1561
Cdd:smart00487 159 -KNVQLLLLSaTPPEEIENLLELFLNDPVFI 188
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
545-703 |
8.05e-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: 85.15 E-value: 8.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 545 ENLLVCAPTGSGKTNVAMLCILNEMEKNRneetgiidtdaFKIVYIAPMKALVQEMVGNFSSRLQQyGIKVSELTGDR-- 622
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKKG-----------KKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSsa 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 623 -QLTKQQISETQIIVTTPEKwdvITRK--ATDRSYTNLVRLIIIDEVHLLhDDRGPVIESIVSRTIRHMEQTqemIRLVG 699
Cdd:cd00046 70 eEREKNKLGDADIIIATPDM---LLNLllREDRLFLKDLKLIIVDEAHAL-LIDSRGALILDLAVRKAGLKN---AQVIL 142
|
....
gi 1317352187 700 LSAT 703
Cdd:cd00046 143 LSAT 146
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
540-908 |
2.88e-18 |
|
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: 91.84 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 540 AFEQDENLLVCAPTGSGKTNVAMLCILNEME-KNRNEETGIidtdafKIVYIAPMKALVQEMVGNFSSRLQQYG--IKVS 616
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSLIDLAgPEAPKEKGL------HTLYITPLRALAVDIARNLQAPIEELGlpIRVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 617 ELTGD---RQLTKQQISETQIIVTTPEKWDV-ITRKATDRSYTNLvRLIIIDEVH-LLHDDRGPVIESIVSRtirhMEQT 691
Cdd:TIGR04121 98 TRTGDtssSERARQRKKPPDILLTTPESLALlLSYPDAARLFKDL-RCVVVDEWHeLAGSKRGDQLELALAR----LRRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 692 QEMIRLVGLSATLpnyGDVATFLRVdpkkgLFHFDSSfrPCPLkqefIGVTEKKAIKRFQVMNEVT-------------Y 758
Cdd:TIGR04121 173 APGLRRWGLSATI---GNLEEARRV-----LLGVGGA--PAVL----VRGKLPKAIEVISLLPESEerfpwaghlglraL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 759 QKVVEQAGKNQ-VLIFVHSRketaktaktikdmalekdtlrlflnpSSASR--EVLQDELPSIKDPnlyellpfgFAIHH 835
Cdd:TIGR04121 239 PEVYAEIDQARtTLVFTNTR--------------------------SQAELwfQALWEANPEFALP---------IALHH 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317352187 836 AGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVN-LPAHTVIikgtQVYSPeKG--RwvelspqdVLQMLGRAG-RP 908
Cdd:TIGR04121 284 GSLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDfGPVDLVI----QIGSP-KGvaR--------LLQRAGRSNhRP 347
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
513-922 |
3.74e-18 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 91.70 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 513 EELPPWVHGAFKGA-RILNRIQSKIYPvAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNEETgiiDTDAFKIVYIA 591
Cdd:COG1201 8 SLLHPAVRAWFAARfGAPTPPQREAWP-AIAAGESTLLIAPTGSGKTLAAFLPALDELARRPRPGE---LPDGLRVLYIS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 592 PMKAL-----------VQEMVGNFSSRLQqyGIKVSELTGD-----RQltkQQISET-QIIVTTPEKWDV-ITRKATDRS 653
Cdd:COG1201 84 PLKALandiernlrapLEEIGEAAGLPLP--EIRVGVRTGDtpaseRQ---RQRRRPpHILITTPESLALlLTSPDAREL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 654 YTNlVRLIIIDEVHLLHDD-RGPVIESIVSRtIRHMeqTQEMIRLVGLSATLPNYGDVATFLrVDPkkglfhfdSSFRPC 732
Cdd:COG1201 159 LRG-VRTVIVDEIHALAGSkRGVHLALSLER-LRAL--APRPLQRIGLSATVGPLEEVARFL-VGY--------EDPRPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 733 -----PLKQEF---IGVTEKKAIKRFQ---VMNEVTYQKVVEQAGKNQ-VLIFVHSRKetaktaktikdMAlEKDTLRLf 800
Cdd:COG1201 226 tivdaGAGKKPdleVLVPVEDLIERFPwagHLWPHLYPRVLDLIEAHRtTLVFTNTRS-----------QA-ERLFQRL- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 801 lnpssasREVLQDELPSIkdpnlyellpfgfAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPA-HTVIikg 879
Cdd:COG1201 293 -------NELNPEDALPI-------------AAHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDvDLVI--- 349
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1317352187 880 tQVYSPeKGrwvelspqdV---LQMLGRAGRpQYDTFGEGIIITSH 922
Cdd:COG1201 350 -QVGSP-KS---------VarlLQRIGRAGH-RVGEVSKGRLVPTH 383
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
540-721 |
8.32e-18 |
|
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: 83.57 E-value: 8.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 540 AFEQDENLLVCAPTGSGKTNVAMLCilneMEKN-RNEETGIidtdafkIVYIAPMKALVQEMV----GNFSSRLQQYGIK 614
Cdd:cd18025 12 IVDRRESALIVAPTSSGKTFISYYC----MEKVlRESDDGV-------VVYVAPTKALVNQVVaevyARFSKKYPPSGKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 615 V-SELTGDRQLtkQQISETQIIVTTPEKWDVITRKATDRSYTNLVRLIIIDEVHLLhddrGPVIESIVsrtirhMEQTQE 693
Cdd:cd18025 81 LwGVFTRDYRH--NNPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSI----GQSEDGAV------WEQLLL 148
|
170 180 190
....*....|....*....|....*....|.
gi 1317352187 694 MIR--LVGLSATLPNYGDVATFL-RVDPKKG 721
Cdd:cd18025 149 LIPcpFLALSATIGNPQKFHEWLqSVQRARK 179
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
823-908 |
4.46e-17 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 77.64 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 823 LYELL---PFGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLP-AHTVIIKGtqvyspekgrwVELSPQDV 898
Cdd:smart00490 3 LAELLkelGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASY 71
|
90
....*....|
gi 1317352187 899 LQMLGRAGRP 908
Cdd:smart00490 72 IQRIGRAGRA 81
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
511-929 |
2.17e-16 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 85.66 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 511 SIEELPPWVHGAFKGAriLNR--IQsKIYPV---AFE---QDENLLVCAPTGSGKTNVAMLCILNEMEKNRNEetgiidt 582
Cdd:COG1205 33 RYAPWPDWLPPELRAA--LKKrgIE-RLYSHqaeAIEaarAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 583 dafKIVYIAPMKALVQEMVGNFSSRLQQYG--IKVSELTGDrqlTKQQI-----SETQIIVTTP-----------EKWdv 644
Cdd:COG1205 103 ---TALYLYPTKALARDQLRRLRELAEALGlgVRVATYDGD---TPPEErrwirEHPDIVLTNPdmlhygllphhTRW-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 645 itrkatDRSYTNLvRLIIIDEVHLLhddRGpVIESIVSRTIRhmeqtqemiRL-------------VGLSATLPNygdva 711
Cdd:COG1205 175 ------ARFFRNL-RYVVIDEAHTY---RG-VFGSHVANVLR---------RLrricrhygsdpqfILASATIGN----- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 712 tflrvdPKKglfHFdssfrpcplkQEFIG-----VTE---KKAIKRFQVMNEVTYQKVVE---------------QAGKn 768
Cdd:COG1205 230 ------PAE---HA----------ERLTGrpvtvVDEdgsPRGERTFVLWNPPLVDDGIRrsalaeaarlladlvREGL- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 769 QVLIFVHSRKETAKTAKTIKDMALEkdtlrlflnPSSASRevlqdelpsIkdpnlyellpfgfAIHHAGMSRTDRTTVED 848
Cdd:COG1205 290 RTLVFTRSRRGAELLARYARRALRE---------PDLADR---------V-------------AAYRAGYLPEERREIER 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 849 LFADGHIQVLVSTATLAWGVNLPA-HTVIIKGtqvYSPekgrwvelSPQDVLQMLGRAGRPQYDtfGEGIIITSHNEL-Q 926
Cdd:COG1205 339 GLRSGELLGVVSTNALELGIDIGGlDAVVLAG---YPG--------TRASFWQQAGRAGRRGQD--SLVVLVAGDDPLdQ 405
|
...
gi 1317352187 927 YYL 929
Cdd:COG1205 406 YYV 408
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
544-713 |
5.02e-15 |
|
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: 75.93 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 544 DENLLVCAPTGSGKTNVAMLCILNEMEKNRNEETGiidtdafKIVYIAPMKALVQEMVGNFSSRLQQYGIKVSELTGDRQ 623
Cdd:cd17927 17 GKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKG-------KVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 624 LT---KQQISETQIIVTTPEKWDVITRKATDRSYTNlVRLIIIDEVHllHDDRGPVIESIVSRTIRH-MEQTQEMIRLVG 699
Cdd:cd17927 90 ENvsvEQIVESSDVIIVTPQILVNDLKSGTIVSLSD-FSLLVFDECH--NTTKNHPYNEIMFRYLDQkLGSSGPLPQILG 166
|
170
....*....|....
gi 1317352187 700 LSATlPNYGDVATF 713
Cdd:cd17927 167 LTAS-PGVGGAKNT 179
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
545-906 |
2.26e-14 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 79.16 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 545 ENLLVCAPTGSGKTNVAMLCILNEM-EKNRNEETgiidTDAFKIVYIAPMKALVQEMVGNFSSRLQQ-------YGIKVS 616
Cdd:PRK13767 48 KNVLISSPTGSGKTLAAFLAIIDELfRLGREGEL----EDKVYCLYVSPLRALNNDIHRNLEEPLTEireiakeRGEELP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 617 EL-----TGD-----RQltkQQISET-QIIVTTPEKWDVITRKATDRSYTNLVRLIIIDEVHLLHDD-RGpvieSIVSRT 684
Cdd:PRK13767 124 EIrvairTGDtssyeKQ---KMLKKPpHILITTPESLAILLNSPKFREKLRTVKWVIVDEIHSLAENkRG----VHLSLS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 685 IRHME--QTQEMIRlVGLSATLPNYGDVATFLrvdpkkGLFHFDSSFRPCplkqEFIGVTEKKAIKrFQVMNEVtyqkvv 762
Cdd:PRK13767 197 LERLEelAGGEFVR-IGLSATIEPLEEVAKFL------VGYEDDGEPRDC----EIVDARFVKPFD-IKVISPV------ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 763 eqagKNqvliFVHSRKE--TAKTAKTIKDMALEKDTLRLFLNPSSASREVLQdelpsikdpNLYELLPFGFAI-----HH 835
Cdd:PRK13767 259 ----DD----LIHTPAEeiSEALYETLHELIKEHRTTLIFTNTRSGAERVLY---------NLRKRFPEEYDEdnigaHH 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317352187 836 AGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPAHTVIIkgtQVYSPEkgrwvelSPQDVLQMLGRAG 906
Cdd:PRK13767 322 SSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVV---LLGSPK-------SVSRLLQRIGRAG 382
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
542-706 |
1.65e-13 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 71.08 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 542 EQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNEetgiidtdafKIVYIAPMKALVQEMVGNFSSRLQQY--GIKVSELT 619
Cdd:cd17923 13 RAGRSVVVTTGTASGKSLCYQLPILEALLRDPGS----------RALYLYPTKALAQDQLRSLRELLEQLglGIRVATYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 620 GD---RQLTKQQISETQIIVTTPEK--WDVITRKATDRSYTNLVRLIIIDEVHLLhddRGpVIESIVSRTIRHMEQTQEM 694
Cdd:cd17923 83 GDtprEERRAIIRNPPRILLTNPDMlhYALLPHHDRWARFLRNLRYVVLDEAHTY---RG-VFGSHVALLLRRLRRLCRR 158
|
170
....*....|....*.
gi 1317352187 695 ----IRLVGLSATLPN 706
Cdd:cd17923 159 ygadPQFILTSATIGN 174
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
1378-1754 |
2.01e-12 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 72.36 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1378 NPIQTQVFNALYNM-----NDNVFVgAPTGSGKTVCAEFALLRLwstPNHGRCVYIAPFQEVVDlqvaQWRQKFGKIQGG 1452
Cdd:COG1061 82 RPYQQEALEALLAAlerggGRGLVV-APTGTGKTVLALALAAEL---LRGKRVLVLVPRRELLE----QWAEELRRFLGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1453 KNIVALTGETSAdlrllesgDVIFATptqWDVMSRRWKQRKNVQTVALFIADELHLIGSdvgPTYEIIVSRM--RYI--- 1527
Cdd:COG1061 154 PLAGGGKKDSDA--------PITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHAGA---PSYRRILEAFpaAYRlgl 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1528 ----AHQTKNPIRI-----VCLSTSLANAQDLGeWIgsTPHTIFnfhpsVRPVPLEIHIQSYSIP--HFASLMMAMAKPT 1596
Cdd:COG1061 220 tatpFRSDGREILLflfdgIVYEYSLKEAIEDG-YL--APPEYY-----GIRVDLTDERAEYDALseRLREALAADAERK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1597 YVAITN----YSSDRPAIVFVPSRKQCRFtavdlltfcaadgttdrflhahasdIEDHLKQINDKALAetlqhgvgFYHE 1672
Cdd:COG1061 292 DKILREllreHPDDRKTLVFCSSVDHAEA-------------------------LAELLNEAGIRAAV--------VTGD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1673 ALSKQDKRIVEElFESGAIQVVVASR--DTcwGINLS--CHMVIVMGTQFfegkehryadypITDVLQMMGRACRPqHDD 1748
Cdd:COG1061 339 TPKKEREEILEA-FRDGELRILVTVDvlNE--GVDVPrlDVAILLRPTGS------------PREFIQRLGRGLRP-APG 402
|
....*.
gi 1317352187 1749 TGRCVL 1754
Cdd:COG1061 403 KEDALV 408
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
545-705 |
6.10e-12 |
|
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: 67.12 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 545 ENLLVCAPTGSGKTNVAMLCILNEMEKNRNE-ETGiidtdafKIVYIAPMKALVQEMVGNFSSRLQQyGIKVSELTGDRQ 623
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAgEKG-------RVVVLVNKVPLVEQQLEKFFKYFRK-GYKVTGLSGDSS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 624 L---TKQQISETQIIVTTPEKWDVITRKAT--DRSYTNLVRLIIIDEVHllHDDRGPVIESIVSRTIRHMEQTQ-EMIRL 697
Cdd:cd18036 90 HkvsFGQIVKASDVIICTPQILINNLLSGReeERVYLSDFSLLIFDECH--HTQKEHPYNKIMRMYLDKKLSSQgPLPQI 167
|
....*...
gi 1317352187 698 VGLSATLP 705
Cdd:cd18036 168 LGLTASPG 175
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
549-906 |
6.50e-12 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 71.49 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 549 VCAPTGSGKTNVAMLCILNEMEKNRNEETGIIDTDAF-KIVYIAPMKALVQEMVGNFSSRLQQYG------------IKV 615
Cdd:PRK09751 1 VIAPTGSGKTLAAFLYALDRLFREGGEDTREAHKRKTsRILYISPIKALGTDVQRNLQIPLKGIAderrrrgetevnLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 616 SELTGD---RQLTKQQISETQIIVTTPEK-WDVITRKAtdRSYTNLVRLIIIDEVHLLH-DDRGPVIESIVSRTIRHMEQ 690
Cdd:PRK09751 81 GIRTGDtpaQERSKLTRNPPDILITTPESlYLMLTSRA--RETLRGVETVIIDEVHAVAgSKRGAHLALSLERLDALLHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 691 TQEMIrlvGLSATLPNYGDVATFLRVDpkkglfhfdssfRPcplkqefIGVTEKKAIKRFQV--------MNEVTyqKVV 762
Cdd:PRK09751 159 SAQRI---GLSATVRSASDVAAFLGGD------------RP-------VTVVNPPAMRHPQIrivvpvanMDDVS--SVA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 763 EQAGKNQ---------------VLIFVHSRKETAKTAKTiKDMAlEKDTLRlfLNPSSASRevLQDELPSIKDPNLYELL 827
Cdd:PRK09751 215 SGTGEDShagregsiwpyietgILDEVLRHRSTIVFTNS-RGLA-EKLTAR--LNELYAAR--LQRSPSIAVDAAHFEST 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 828 ------------PFGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPAHTVIIkgtQVYSPekgrwveLSP 895
Cdd:PRK09751 289 sgatsnrvqssdVFIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVI---QVATP-------LSV 358
|
410
....*....|.
gi 1317352187 896 QDVLQMLGRAG 906
Cdd:PRK09751 359 ASGLQRIGRAG 369
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
546-908 |
8.09e-12 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 70.44 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 546 NLLVCAPTGSGKTNVAMLCILNEMEKNRneetgiidtdafkIVYIAPMKALV-QemvgnFSSRLQQYGIKVSELTGDRQl 624
Cdd:COG1061 102 RGLVVAPTGTGKTVLALALAAELLRGKR-------------VLVLVPRRELLeQ-----WAEELRRFLGDPLAGGGKKD- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 625 tkqqiSETQIIVTTpekWDVITRKATDRSYTNLVRLIIIDEVHLLhddRGPVIEsivsRTIRHMEQTqemiRLVGLSATl 704
Cdd:COG1061 163 -----SDAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHA---GAPSYR----RILEAFPAA----YRLGLTAT- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 705 PNYGD-----VATFL----RVDPKKGL-------FHF---DSSFRPCPLKQEFIGVTEKKAIKRFQVMNEVTYQKVVEQA 765
Cdd:COG1061 223 PFRSDgreilLFLFDgivyEYSLKEAIedgylapPEYygiRVDLTDERAEYDALSERLREALAADAERKDKILRELLREH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 766 GKN-QVLIFVHSRketaKTAKTIKDMalekdtlrlflnpssasrevlqdelpsikdpnlyeLLPFGFAIH--HAGMSRTD 842
Cdd:COG1061 303 PDDrKTLVFCSSV----DHAEALAEL-----------------------------------LNEAGIRAAvvTGDTPKKE 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317352187 843 RTTVEDLFADGHIQVLVSTATLAWGVNLPAHTVIIkgtqVYSPEKgrwvelSPQDVLQMLGRAGRP 908
Cdd:COG1061 344 REEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI----LLRPTG------SPREFIQRLGRGLRP 399
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
823-907 |
1.99e-11 |
|
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: 62.61 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 823 LYELLPFGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLP-AHTVIIkgtqvYSPEKgrwvelSPQDVLQM 901
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YDLPW------NPASYIQR 101
|
....*.
gi 1317352187 902 LGRAGR 907
Cdd:pfam00271 102 IGRAGR 107
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1352-1755 |
2.45e-11 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 69.15 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1352 DMQPLPVSALR-NREYEAVYNGWVDKFNPIQT-QVFNALYNmNDNVFVGAPTGSGKTVCAEFA----LLRlwstpNHGRC 1425
Cdd:COG1202 184 EVDTVPVDDLDlPPELKDLLEGRGEELLPVQSlAVENGLLE-GKDQLVVSATATGKTLIGELAgiknALE-----GKGKM 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1426 VYIAPFqevvdlqVA-------QWRQKFGK-----IQGGKNIVALTGETSaDLRllesGDVIFATPTQWDVMSRRWKQRK 1493
Cdd:COG1202 258 LFLVPL-------VAlanqkyeDFKDRYGDgldvsIRVGASRIRDDGTRF-DPN----ADIIVGTYEGIDHALRTGRDLG 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1494 NVQTValfIADELHLIG-SDVGPTYEIIVSRMRYIAHQTKnpirIVCLSTSLANAQDLGEWIGSTPhTIFNfhpsVRPVP 1572
Cdd:COG1202 326 DIGTV---VIDEVHMLEdPERGHRLDGLIARLKYYCPGAQ----WIYLSATVGNPEELAKKLGAKL-VEYE----ERPVP 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1573 LEIHIQsysiphFAS------LMMAMAKPTYVAITNYSSDRPAIVFVPSRKQCrftavdlltfcaadgttdrflhahasd 1646
Cdd:COG1202 394 LERHLT------FADgrekirIINKLVKREFDTKSSKGYRGQTIIFTNSRRRC--------------------------- 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1647 iedHLkqindkaLAETLQHGVGFYHEALSKQDKRIVEELFESGAIQVVVASRDTCWGINLSCHMVI----VMGTQFFEGK 1722
Cdd:COG1202 441 ---HE-------IARALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIfdslAMGIEWLSVQ 510
|
410 420 430
....*....|....*....|....*....|...
gi 1317352187 1723 EhryadypitdVLQMMGRACRPQHDDTGRCVLM 1755
Cdd:COG1202 511 E----------FHQMLGRAGRPDYHDRGKVYLL 533
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
542-703 |
5.14e-11 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 63.07 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 542 EQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNEetgiidtdafKIVYIAPMKALVQEMVGNFSSRLQQYGIKVSELTGD 621
Cdd:pfam04851 21 NGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK----------KVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 622 RQLTKQQisETQIIVTTPEKWDVITRKATDRSYTNLVRLIIIDEVHLLHDDrgpviesivsrtirHMEQTQEMI---RLV 698
Cdd:pfam04851 91 KKDESVD--DNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAHRSGAS--------------SYRNILEYFkpaFLL 154
|
....*
gi 1317352187 699 GLSAT 703
Cdd:pfam04851 155 GLTAT 159
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
532-705 |
5.53e-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: 64.00 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 532 IQSKIYPVAFEqDENLLVCAPTGSGKTnVA----MLCILNEMEKNRNEETGIIdtdafkIvyIAPMKALVQEMVGNFSSR 607
Cdd:cd00268 16 IQAQAIPLILS-GRDVIGQAQTGSGKT-LAfllpILEKLLPEPKKKGRGPQAL------V--LAPTRELAMQIAEVARKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 608 LQQYGIKVSELTGDRQLTKQQISE---TQIIVTTPEK-WDVITRKATDrsyTNLVRLIIIDEV-HLLHDDRGPVIESIVS 682
Cdd:cd00268 86 GKGTGLKVAAIYGGAPIKKQIEALkkgPDIVVGTPGRlLDLIERGKLD---LSNVKYLVLDEAdRMLDMGFEEDVEKILS 162
|
170 180
....*....|....*....|...
gi 1317352187 683 RtIRHMEQTqemirlVGLSATLP 705
Cdd:cd00268 163 A-LPKDRQT------LLFSATLP 178
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
529-907 |
1.15e-10 |
|
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: 66.64 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 529 LNRIQSKIY---PVAFEQDENLLV-CAPTGSGKTNVAMLCILNEMEKNRNEetgiidtdafKIVYIAPMKALVQEMvgnf 604
Cdd:COG1203 128 INPLQNEALelaLEAAEEEPGLFIlTAPTGGGKTEAALLFALRLAAKHGGR----------RIIYALPFTSIINQT---- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 605 SSRLQQ-YGIKVSELTGDRQLTKQQISE-----------------TQIIVTTPekwD-----VITRKATD-RSYTNLVR- 659
Cdd:COG1203 194 YDRLRDlFGEDVLLHHSLADLDLLEEEEeyesearwlkllkelwdAPVVVTTI---DqlfesLFSNRKGQeRRLHNLANs 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 660 LIIIDEVHLLHDDRGPVIEsivsRTIRHMEQTQemIRLVGLSATLPnygdvaTFLRvdpkkgLFHFDSSFRPCPLKQEFI 739
Cdd:COG1203 271 VIILDEVQAYPPYMLALLL----RLLEWLKNLG--GSVILMTATLP------PLLR------EELLEAYELIPDEPEELP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 740 GVTEKKAIKRFQV-MNEVTYQKVVEQA-----GKNQVLIFVHSRKETAKTAKTIKDmalekdtlrlflnpssasrevlqd 813
Cdd:COG1203 333 EYFRAFVRKRVELkEGPLSDEELAELIlealhKGKSVLVIVNTVKDAQELYEALKE------------------------ 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 814 elpSIKDPNLYeLLpfgfaihHAGMSRTDRTTVE----DLFADGHIQVLVST----AtlawGVNLPAHTVIIkgtqvysp 885
Cdd:COG1203 389 ---KLPDEEVY-LL-------HSRFCPADRSEIEkeikERLERGKPCILVSTqvveA----GVDIDFDVVIR-------- 445
|
410 420
....*....|....*....|...
gi 1317352187 886 ekgrwvELSPQD-VLQmlgRAGR 907
Cdd:COG1203 446 ------DLAPLDsLIQ---RAGR 459
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
1394-1542 |
3.36e-10 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 60.49 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1394 NVFVGAPTGSGKTVCAEFALLRLwSTPNHGRCVYIAPFQEVVdLQVAQWRQKFGKIqgGKNIVALTGETSADLRLLESG- 1472
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLL-LLKKGKKVLVLVPTKALA-LQTAERLRELFGP--GIRVAVLVGGSSAEEREKNKLg 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317352187 1473 --DVIFATPTQWDVMSRRWKQRKnVQTVALFIADELHLIGSDVGPTYEIivsRMRYIAHQTKNPIRIVCLST 1542
Cdd:cd00046 79 daDIIIATPDMLLNLLLREDRLF-LKDLKLIIVDEAHALLIDSRGALIL---DLAVRKAGLKNAQVILLSAT 146
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
540-702 |
9.03e-09 |
|
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: 57.66 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 540 AFEQ--DENLLVCAPTGSGKTNVAMLCILNEMEKNRNEETGIidtdafKI-VYIAPMKALVQEMVgnfsSRLQQY-GIKV 615
Cdd:cd18034 10 LFEAalKRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNPK------KRaVFLVPTVPLVAQQA----EAIRSHtDLKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 616 SELTGD-------RQLTKQQISETQIIVTTPEkwdvITRKATDRSYTNL--VRLIIIDEVHL---LHDDRGpviesiVSR 683
Cdd:cd18034 80 GEYSGEmgvdkwtKERWKEELEKYDVLVMTAQ----ILLDALRHGFLSLsdINLLIFDECHHatgDHPYAR------IMK 149
|
170
....*....|....*....
gi 1317352187 684 TIRHMEQTQEMIRLVGLSA 702
Cdd:cd18034 150 EFYHLEGRTSRPRILGLTA 168
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
544-707 |
1.84e-08 |
|
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: 56.53 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 544 DENLLVCAPTGSGKTNVAMLCILNEMEKNRneetgiidtdAFKIVYIAPMKALVQEMVGNFSSRLQQYGI--KVSELTGD 621
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWALKLAARGG----------KRRIIYALPTRATINQMYERIREILGRLDDedKVLLLHSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 622 RQLTKQQISETQ---------------------IIVTTpekWD-----VITRKATDRSYTNLVR-LIIIDEVHLLHDDRG 674
Cdd:cd17930 71 AALELLESDEEPdddpveavdwalllkrswlapIVVTT---IDqllesLLKYKHFERRLHGLANsVVVLDEVQAYDPEYM 147
|
170 180 190
....*....|....*....|....*....|...
gi 1317352187 675 PVIESIVSRTIRHMEqtqemIRLVGLSATLPNY 707
Cdd:cd17930 148 ALLLKALLELLGELG-----GPVVLMTATLPAL 175
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
824-907 |
3.20e-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: 54.58 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 824 YELLPFGFAIHHAGMSRTDRTTVEDLFADGHIQVLVSTATLAWGVNLPA-HTVIikgtQVYSPekgrwveLSPQDVLQML 902
Cdd:cd18796 64 DRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDvDLVI----QIGSP-------KSVARLLQRL 132
|
....*
gi 1317352187 903 GRAGR 907
Cdd:cd18796 133 GRSGH 137
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
543-665 |
5.21e-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: 55.29 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 543 QDENLLVCAPTGSGKTnVAMLC-ILNEMEKNRNEETgiidtdaFKIVYIAPMKALVQEMVGNFSSRLQQYGIKVSELT-G 620
Cdd:cd17957 26 HGRDLLACAPTGSGKT-LAFLIpILQKLGKPRKKKG-------LRALILAPTRELASQIYRELLKLSKGTGLRIVLLSkS 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1317352187 621 DRQLTKQQISETQ---IIVTTPEKW-DVITRKATDRSytnLVRLIIIDE 665
Cdd:cd17957 98 LEAKAKDGPKSITkydILVSTPLRLvFLLKQGPIDLS---SVEYLVLDE 143
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
1399-1554 |
7.05e-08 |
|
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: 54.91 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1399 APTGSGKTVCAEFALLR-LWstpNHGR-CVYIAPFQEVVDLQVaQWRQKFGkIQGGKNIVALTGETS-ADLRLLESGDVI 1475
Cdd:cd18026 40 LPTSGGKTLVAEILMLKrLL---ERRKkALFVLPYVSIVQEKV-DALSPLF-EELGFRVEGYAGNKGrSPPKRRKSLSVA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1476 FATPTQWDVMSRRWKQRKNVQTVALFIADELHLIG-SDVGPTYEIIVSRMRYIAHQTknpIRIVCLSTSLANAQDLGEWI 1554
Cdd:cd18026 115 VCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGdGHRGALLELLLTKLLYAAQKN---IQIVGMSATLPNLEELASWL 191
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
1394-1552 |
1.06e-07 |
|
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: 54.13 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1394 NVFVGAPTGSGKTVCAEFALL-RLWSTPnHGRCVYIAPFQEVVDLQVAQWRQKFGKIQGGKNIVALTGETSADLR---LL 1469
Cdd:cd17923 17 SVVVTTGTASGKSLCYQLPILeALLRDP-GSRALYLYPTKALAQDQLRSLRELLEQLGLGIRVATYDGDTPREERraiIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1470 ESGDVIFATPTQWDVM----SRRWkqRKNVQTVALFIADELH----LIGSDVGptyeIIVSRMRYIAHQTKNPIRIVCLS 1541
Cdd:cd17923 96 NPPRILLTNPDMLHYAllphHDRW--ARFLRNLRYVVLDEAHtyrgVFGSHVA----LLLRRLRRLCRRYGADPQFILTS 169
|
170
....*....|.
gi 1317352187 1542 TSLANAQDLGE 1552
Cdd:cd17923 170 ATIGNPAEHAR 180
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
1392-1554 |
1.22e-07 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 53.36 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1392 NDNVFVGAPTGSGKTVCAEFALLRLW--STPNHGRCVYIAPF-----------QEVVDLQVAQWRqkfgkiqggkniVAL 1458
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLadEPEKGVQVLYISPLkalindqerrlEEPLDEIDLEIP------------VAV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1459 -TGETSADLR--LLES-GDVIFATPTQWDVM---SRRWKQRKNVQTValfIADELH-LIGSDVGPTYEIIVSRMRyiaHQ 1530
Cdd:cd17922 69 rHGDTSQSEKakQLKNpPGILITTPESLELLlvnKKLRELFAGLRYV---VVDEIHaLLGSKRGVQLELLLERLR---KL 142
|
170 180
....*....|....*....|....
gi 1317352187 1531 TKNPIRIVCLSTSLANAQDLGEWI 1554
Cdd:cd17922 143 TGRPLRRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
542-706 |
1.40e-07 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350782 [Multi-domain] Cd Length: 205 Bit Score: 53.99 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 542 EQDENLLVCAPTGSGKTNVAMLCILNEMEKNRneetgiidtdafKIVYIAPMKALVQEMVGNFSSRLQQYGIkvseLTGD 621
Cdd:cd18024 45 ERNESVLVSAHTSAGKTVVAEYAIAQSLRDKQ------------RVIYTSPIKALSNQKYRELQEEFGDVGL----MTGD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 622 RQLTkqqiSETQIIVTTPEkwdvITRKATDR--SYTNLVRLIIIDEVHLLHD-DRGPVIEsivsRTIRHMEQTqemIRLV 698
Cdd:cd18024 109 VTIN----PNASCLVMTTE----ILRSMLYRgsEIMREVAWVIFDEIHYMRDkERGVVWE----ETIILLPDK---VRYV 173
|
....*...
gi 1317352187 699 GLSATLPN 706
Cdd:cd18024 174 FLSATIPN 181
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1373-1557 |
2.19e-07 |
|
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: 53.04 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1373 WVDKFNPIQTQVFNALyNMNDNVFVGAPTGSGKTVCAEFALlrLWSTPNHGRCVYIAPFQEVVDLQVAQWRQKFGkiqgg 1452
Cdd:cd18027 5 WPFELDVFQKQAILHL-EAGDSVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFG----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1453 kNIVALTGetsaDLRLLESGDVIFATPTQwdVMSRRWKQRKNVQTVALFIADELHLIG-SDVGPTYEIIVSRMryiahqt 1531
Cdd:cd18027 77 -DVGLITG----DVQLNPEASCLIMTTEI--LRSMLYNGSDVIRDLEWVIFDEVHYINdAERGVVWEEVLIML------- 142
|
170 180
....*....|....*....|....*.
gi 1317352187 1532 KNPIRIVCLSTSLANAQDLGEWIGST 1557
Cdd:cd18027 143 PDHVSIILLSATVPNTVEFADWIGRI 168
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1659-1744 |
2.21e-07 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 50.29 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1659 LAETLQ---HGVGFYHEALSKQDKRIVEELFESGAIQVVVASRDTCWGINLSC-HMVIVMGtqffegkehryADYPITDV 1734
Cdd:smart00490 3 LAELLKelgIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGvDLVIIYD-----------LPWSPASY 71
|
90
....*....|
gi 1317352187 1735 LQMMGRACRP 1744
Cdd:smart00490 72 IQRIGRAGRA 81
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
539-704 |
2.72e-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: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 539 VAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKnrneetgiidtdafKIVYIAPMKALVQEMVGNFssrlQQYGIKVS-- 616
Cdd:cd17926 13 LAHKNNRRGILVLPTGSGKTLTALALIAYLKEL--------------RTLIVVPTDALLDQWKERF----EDFLGDSSig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 617 ELTGDRqltKQQISETQIIVTTPEKwdVITRKATDRSYTNLVRLIIIDEVHLLHddrGPVIESIVSRTIRHmeqtqemiR 696
Cdd:cd17926 75 LIGGGK---KKDFDDANVVVATYQS--LSNLAEEEKDLFDQFGLLIVDEAHHLP---AKTFSEILKELNAK--------Y 138
|
....*...
gi 1317352187 697 LVGLSATL 704
Cdd:cd17926 139 RLGLTATP 146
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
1384-1523 |
2.91e-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: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1384 VFNALYNMNDN--VFVgAPTGSGKTVCAEFALLRLWStpnhGRCVYIAPFQEVVDlqvaQWRQKFGKIQGGKNIVALTGE 1461
Cdd:cd17926 9 LEAWLAHKNNRrgILV-LPTGSGKTLTALALIAYLKE----LRTLIVVPTDALLD----QWKERFEDFLGDSSIGLIGGG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317352187 1462 TSADlrlLESGDVIFATPTQWDVMSRRWKQRKNVQtvALFIADELHLIGSDvgpTYEIIVSR 1523
Cdd:cd17926 80 KKKD---FDDANVVVATYQSLSNLAEEEKDLFDQF--GLLIVDEAHHLPAK---TFSEILKE 133
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1399-1706 |
4.57e-07 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 55.70 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1399 APTGSGKTVCA-EFALLRLWS-------TPNHG---RCVYIAPFQEV-VDLQ---------VAQWRQKFGKIQGGKNIVA 1457
Cdd:PRK09751 3 APTGSGKTLAAfLYALDRLFReggedtrEAHKRktsRILYISPIKALgTDVQrnlqiplkgIADERRRRGETEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1458 LTGETSADLR---LLESGDVIFATPTQWDVM--SRRWKQRKNVQTValfIADELHLI-GSDVGPTYEIIVSRMRYIAHqt 1531
Cdd:PRK09751 83 RTGDTPAQERsklTRNPPDILITTPESLYLMltSRARETLRGVETV---IIDEVHAVaGSKRGAHLALSLERLDALLH-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1532 kNPIRIVCLSTSLANAQDLGEWI-GSTPHTIFNfHPSVRPVPLEIHIQSYSIPHFASLMMAMAKPTYVA----------- 1599
Cdd:PRK09751 158 -TSAQRIGLSATVRSASDVAAFLgGDRPVTVVN-PPAMRHPQIRIVVPVANMDDVSSVASGTGEDSHAGregsiwpyiet 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1600 --ITNYSSDRPAIVFVPSRKqcrftavdlltfcAADGTTDRFLHAHASDIEDHLKQINDKALAETLQHGVG--------- 1668
Cdd:PRK09751 236 giLDEVLRHRSTIVFTNSRG-------------LAEKLTARLNELYAARLQRSPSIAVDAAHFESTSGATSnrvqssdvf 302
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1317352187 1669 ---FYHEALSKQDKRIVEELFESGAIQVVVASRDTCWGINL 1706
Cdd:PRK09751 303 iarSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDM 343
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
1391-1507 |
5.60e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.12 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1391 MNDNVFVGAPTGSGKTVCAEFALLRLWSTPNhGRCVYIAPFQEVVDlQVAQWRQKFGKIQGGKnIVALTGETSADLR--L 1468
Cdd:COG1111 16 LRKNTLVVLPTGLGKTAVALLVIAERLHKKG-GKVLFLAPTKPLVE-QHAEFFKEALNIPEDE-IVVFTGEVSPEKRkeL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1317352187 1469 LESGDVIFATP--TQWDVMSRRWkqrkNVQTVALFIADELH 1507
Cdd:COG1111 93 WEKARIIVATPqvIENDLIAGRI----DLDDVSLLIFDEAH 129
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
532-861 |
6.60e-07 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 54.00 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 532 IQSKIYPVAFEqDENLLVCAPTGSGKTnVA-MLCILNEMEKNRNEET-GIIdtdafkivyIAPMKAL---VQEMVGNFSS 606
Cdd:COG0513 28 IQAQAIPLILA-GRDVLGQAQTGTGKT-AAfLLPLLQRLDPSRPRAPqALI---------LAPTRELalqVAEELRKLAK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 607 RLqqyGIKVSELTG----DRQLtkQQISE-TQIIVTTPEK-WDVITRKATDrsyTNLVRLIIIDEV-HLLhdDRG--PVI 677
Cdd:COG0513 97 YL---GLRVATVYGgvsiGRQI--RALKRgVDIVVATPGRlLDLIERGALD---LSGVETLVLDEAdRML--DMGfiEDI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 678 ESIVSRTirhMEQTQEMIrlvgLSATLPNygDVATFLR---VDPKKglFHFDSSFRPCP-LKQEFIGVTEKkaiKRFQVM 753
Cdd:COG0513 167 ERILKLL---PKERQTLL----FSATMPP--EIRKLAKrylKNPVR--IEVAPENATAEtIEQRYYLVDKR---DKLELL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 754 NevtyqKVVEQAGKNQVLIFVHSRKETAKTAKtikdmALEKDtlrlflnpssasrevlqdelpsikdpnlyellpfGF-- 831
Cdd:COG0513 233 R-----RLLRDEDPERAIVFCNTKRGADRLAE-----KLQKR----------------------------------GIsa 268
|
330 340 350
....*....|....*....|....*....|.
gi 1317352187 832 -AIhHAGMSRTDRTTVEDLFADGHIQVLVST 861
Cdd:COG0513 269 aAL-HGDLSQGQRERALDAFRNGKIRVLVAT 298
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
544-667 |
6.75e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 54.74 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 544 DENLLVCAPTGSGKTNVAMLCILNEMEKNRNeetgiidtdafKIVYIAPMKALVQEMVGNFSSRLQQYGIKVSELTGDRQ 623
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAERLHKKGG-----------KVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVS 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1317352187 624 LTKQQI--SETQIIVTTPE--KWDVITRkatdRSYTNLVRLIIIDEVH 667
Cdd:COG1111 86 PEKRKElwEKARIIVATPQviENDLIAG----RIDLDDVSLLIFDEAH 129
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
1394-1546 |
8.73e-07 |
|
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: 51.66 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1394 NVFVGAPTGSGKT-----VCAEfaLLRLWSTPNHGRCVYIAPFQEVVDLQVAQWRQKFGKIqgGKNIVALTGETSADLR- 1467
Cdd:cd17927 19 NTIICLPTGSGKTfvavlICEH--HLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERP--GYKVTGLSGDTSENVSv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1468 --LLESGDVIFATPT--QWDVMSRRWKQRKNvqtVALFIADELHL-IGSDVgptYEIIVSR--MRYIAHQTKNPiRIVCL 1540
Cdd:cd17927 95 eqIVESSDVIIVTPQilVNDLKSGTIVSLSD---FSLLVFDECHNtTKNHP---YNEIMFRylDQKLGSSGPLP-QILGL 167
|
....*.
gi 1317352187 1541 STSLAN 1546
Cdd:cd17927 168 TASPGV 173
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
545-710 |
8.96e-07 |
|
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: 52.37 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 545 ENLLVCAPTGSGKTNVAMLCILNE-MEKNRNEETGIidtDAFKIVYIAPMKALVQEmVGNFSSRLQQY-GIKVSELTGDR 622
Cdd:cd17948 28 RNTLCAAETGSGKTLTYLLPIIQRlLRYKLLAEGPF---NAPRGLVITPSRELAEQ-IGSVAQSLTEGlGLKVKVITGGR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 623 qlTKQQI-----SETQIIVTTPekwDVITRKATDRSY-TNLVRLIIIDEVH-LLHDDRGPVIESIVSRT---IRHMEQTQ 692
Cdd:cd17948 104 --TKRQIrnphfEEVDILVATP---GALSKLLTSRIYsLEQLRHLVLDEADtLLDDSFNEKLSHFLRRFplaSRRSENTD 178
|
170 180
....*....|....*....|..
gi 1317352187 693 EMIR---LVGLSATLP-NYGDV 710
Cdd:cd17948 179 GLDPgtqLVLVSATMPsGVGEV 200
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1381-1743 |
9.85e-07 |
|
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: 54.07 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1381 QTQVFNALYNmNDNVFVGAPTGSGKTVCaeF---ALLRLWSTPNhGRCVYIAPFQEVVDLQVAQWRQKFGKIQGGKNIVA 1457
Cdd:COG1205 61 QAEAIEAARA-GKNVVIATPTASGKSLA--YllpVLEALLEDPG-ATALYLYPTKALARDQLRRLRELAEALGLGVRVAT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1458 LTGETSADLR--LLESGDVIFATPtqwDVM-------SRRWkqRKNVQTVALFIADELH----LIGSDVGptyeIIVSRM 1524
Cdd:COG1205 137 YDGDTPPEERrwIREHPDIVLTNP---DMLhygllphHTRW--ARFFRNLRYVVIDEAHtyrgVFGSHVA----NVLRRL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1525 RYIAHQTKNPIRIVCLSTSLANAQDLGE-WIGSTPHTI-----------FNFhpsVRPVPLEIHIQSYSIPHFASLMMAM 1592
Cdd:COG1205 208 RRICRHYGSDPQFILASATIGNPAEHAErLTGRPVTVVdedgsprgertFVL---WNPPLVDDGIRRSALAEAARLLADL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1593 AKptyvaitnysSDRPAIVFVPSRKQcrftaVDLLtfcaadgttdrflhahASDIEDHLKQindkalaETLQHGVGFYHE 1672
Cdd:COG1205 285 VR----------EGLRTLVFTRSRRG-----AELL----------------ARYARRALRE-------PDLADRVAAYRA 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317352187 1673 ALSKQDKRIVEELFESGAIQVVVAsrdTC---WGINLSC-HMVIVMGtqffegkehryadYP--ITDVLQMMGRACR 1743
Cdd:COG1205 327 GYLPEERREIERGLRSGELLGVVS---TNaleLGIDIGGlDAVVLAG-------------YPgtRASFWQQAGRAGR 387
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1376-1507 |
1.28e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 50.36 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1376 KFNPIQTQVFNALYNM----NDNVFVGAPTGSGKTVCAEFALLRLWSTPNHGRCVYIAPFQEVVDlqvaQWRQKFGKIQG 1451
Cdd:pfam04851 3 ELRPYQIEAIENLLESikngQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLE----QALEEFKKFLP 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1317352187 1452 GKniVALTGETSADLRLLESGD--VIFATPTQWDVMSRRWKQRKNVQTVALFIADELH 1507
Cdd:pfam04851 79 NY--VEIGEIISGDKKDESVDDnkIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
1358-1505 |
2.31e-06 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 50.52 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1358 VSALRNREYEavyngwvdKFNPIQTQVFNALYNmNDNVFVGAPTGSGKTVCaeFAL-------LRLWSTPNHGRCVYIAP 1430
Cdd:cd00268 2 LKALKKLGFE--------KPTPIQAQAIPLILS-GRDVIGQAQTGSGKTLA--FLLpilekllPEPKKKGRGPQALVLAP 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317352187 1431 FQEVVdLQVAQWRQKFGKIQGGKnIVALTGETS--ADLRLLESG-DVIFATPTQ-WDVMSRRWKQRKNVQTVALfiaDE 1505
Cdd:cd00268 71 TRELA-MQIAEVARKLGKGTGLK-VAAIYGGAPikKQIEALKKGpDIVVGTPGRlLDLIERGKLDLSNVKYLVL---DE 144
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
541-723 |
3.12e-06 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 49.57 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 541 FEQDENLLVCAPTGSGKTNVAMLCIlnemeknrneetGIIDTDAFKIVYIAPMKALVQEMVGNFSSRLQQYGIkvseLTG 620
Cdd:cd18027 20 LEAGDSVFVAAHTSAGKTVVAEYAI------------ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGL----ITG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 621 DRQLTkqqiSETQIIVTTPEkwdvITRKATDRSyTNLVR---LIIIDEVHLLHD-DRGPVIESIVSRTIRHmeqtqemIR 696
Cdd:cd18027 84 DVQLN----PEASCLIMTTE----ILRSMLYNG-SDVIRdleWVIFDEVHYINDaERGVVWEEVLIMLPDH-------VS 147
|
170 180
....*....|....*....|....*..
gi 1317352187 697 LVGLSATLPNYGDVATFLRVDPKKGLF 723
Cdd:cd18027 148 IILLSATVPNTVEFADWIGRIKKKNIY 174
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
1379-1507 |
8.43e-06 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 48.28 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1379 PIQTQVFNALYNMNDNVFVGAPTGSGKTVCAEF-ALLRLwsTPNHGRCVYIAPFQEVVDLQVAQWRQKFgkiQGGKNIVA 1457
Cdd:cd18035 3 RRLYQVLIAAVALNGNTLIVLPTGLGKTIIAILvAADRL--TKKGGKVLILAPSRPLVEQHAENLKRVL---NIPDKITS 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1317352187 1458 LTGETSADLR--LLESGDVIFATP--TQWDVMSRRWkqrkNVQTVALFIADELH 1507
Cdd:cd18035 78 LTGEVKPEERaeRWDASKIIVATPqvIENDLLAGRI----TLDDVSLLIFDEAH 127
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
544-667 |
1.08e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 50.64 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 544 DENLLVCAPTGSGKTNVAMLCILnemeknrneetGIIDTDAFKIVYIAPMKALVQEMVGNFSSRLQQYGIKVSELTGDRQ 623
Cdd:PRK13766 29 KKNTLVVLPTGLGKTAIALLVIA-----------ERLHKKGGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVS 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1317352187 624 LTKQQI--SETQIIVTTPE--KWDVITRkatdRSYTNLVRLIIIDEVH 667
Cdd:PRK13766 98 PEKRAElwEKAKVIVATPQviENDLIAG----RISLEDVSLLIFDEAH 141
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
543-667 |
1.42e-05 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350831 [Multi-domain] Cd Length: 202 Bit Score: 48.28 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 543 QDENLLVCAPTGSGKTNVAMLCILNEMEKNRNEETGiidtdafKIVYIAPMKALVQEMVGNFSSRLQQYGIKVSELTGDR 622
Cdd:cd18073 16 KGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKG-------KVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGAT 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1317352187 623 Q---LTKQQISETQIIVTTPEKWDVITRKATDRSYTnLVRLIIIDEVH 667
Cdd:cd18073 89 AenvPVEQIIENNDIIILTPQILVNNLKKGTIPSLS-IFTLMIFDECH 135
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
1375-1517 |
1.45e-05 |
|
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: 47.91 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1375 DKFNPIQTQVFNALYNmNDNVFVGAPTGSGKTVCAEF-ALLRlwstpnHGRCVYIAPFQEVVDLQVAQWRQKfgkiqgGK 1453
Cdd:cd17920 11 DEFRPGQLEAINAVLA-GRDVLVVMPTGGGKSLCYQLpALLL------DGVTLVVSPLISLMQDQVDRLQQL------GI 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317352187 1454 NIVALTGETSAD-----LRLLESG--DVIFATP--TQWDVMSRRWKQRKNVQTVALFIADELHLI---GSDVGPTY 1517
Cdd:cd17920 78 RAAALNSTLSPEekrevLLRIKNGqyKLLYVTPerLLSPDFLELLQRLPERKRLALIVVDEAHCVsqwGHDFRPDY 153
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
545-703 |
1.93e-05 |
|
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: 47.32 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 545 ENLLVCAPTGSGKTNVAMLCILNEMeknRNEETGiidtdafKIVYIAPMKALVQEMVGNFSSRLqqyGIKVS---ELTG- 620
Cdd:cd18033 17 QNTLVALPTGLGKTFIAAVVMLNYY---RWFPKG-------KIVFMAPTKPLVSQQIEACYKIT---GIPSSqtaELTGs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 621 DRQLTKQQISET-QIIVTTPEKWDV-ITRKATDRSYtnlVRLIIIDEVHllhddRGP-------VIESIVSRTIRhmeqt 691
Cdd:cd18033 84 VPPTKRAELWASkRVFFLTPQTLENdLKEGDCDPKS---IVCLVIDEAH-----RATgnyaycqVVRELMRYNSH----- 150
|
170
....*....|..
gi 1317352187 692 qemIRLVGLSAT 703
Cdd:cd18033 151 ---FRILALTAT 159
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
533-667 |
2.76e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 47.12 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 533 QSKIYPVAFEQdeNLLVCAPTGSGKTNVAMLCILNEMEKNRNeetgiidtdafKIVYIAPMKALVQEMVGNFsSRLQQYG 612
Cdd:cd18035 7 QVLIAAVALNG--NTLIVLPTGLGKTIIAILVAADRLTKKGG-----------KVLILAPSRPLVEQHAENL-KRVLNIP 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1317352187 613 IKVSELTGDRQLTKQQ--ISETQIIVTTPE--KWDVITRKATDRSytnlVRLIIIDEVH 667
Cdd:cd18035 73 DKITSLTGEVKPEERAerWDASKIIVATPQviENDLLAGRITLDD----VSLLIFDEAH 127
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
545-673 |
3.92e-05 |
|
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: 46.76 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 545 ENLLVCAPTGSGKTnvamLC-----ILNEMeknrneeTGIIdtdafkivyIAPMKALVQEMVgnfsSRLQQYGIKVSELT 619
Cdd:cd17920 28 RDVLVVMPTGGGKS----LCyqlpaLLLDG-------VTLV---------VSPLISLMQDQV----DRLQQLGIRAAALN 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317352187 620 G-----DRQLTKQQIS--ETQIIVTTPEKW---DVITRKATDRSyTNLVRLIIIDEVHLL----HDDR 673
Cdd:cd17920 84 StlspeEKREVLLRIKngQYKLLYVTPERLlspDFLELLQRLPE-RKRLALIVVDEAHCVsqwgHDFR 150
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1392-1556 |
4.43e-05 |
|
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: 46.59 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1392 NDNVFVGAPTGSGKTVCAEFALLRLWSTPNHGRCVYIAPFQEVVDLQVAQWRQKFGK--IQGGKNIVA-LTGETSADlrL 1468
Cdd:cd18025 16 RESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKkyPPSGKSLWGvFTRDYRHN--N 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1469 LESGDVIFATPTQWDVM-----SRRWKQRknVQTValfIADELHLIGSDV-GPTYEIIVsrmryiahqTKNPIRIVCLST 1542
Cdd:cd18025 94 PMNCQVLITVPECLEILllsphNASWVPR--IKYV---IFDEIHSIGQSEdGAVWEQLL---------LLIPCPFLALSA 159
|
170
....*....|....
gi 1317352187 1543 SLANAQDLGEWIGS 1556
Cdd:cd18025 160 TIGNPQKFHEWLQS 173
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
1386-1507 |
5.29e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 48.33 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1386 NALynmNDNVFVGAPTGSGKTVCAEFALLRLWSTPNhGRCVYIAPFQEVVDlQVAQWRQKFGKIQGGKnIVALTGETSAD 1465
Cdd:PRK13766 26 TAL---KKNTLVVLPTGLGKTAIALLVIAERLHKKG-GKVLILAPTKPLVE-QHAEFFRKFLNIPEEK-IVVFTGEVSPE 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1317352187 1466 LR--LLESGDVIFATP--TQWDVMSRRWkqrkNVQTVALFIADELH 1507
Cdd:PRK13766 100 KRaeLWEKAKVIVATPqvIENDLIAGRI----SLEDVSLLIFDEAH 141
|
|
| DEXHc_RLR-2 |
cd18074 |
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma ... |
545-686 |
6.18e-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: 46.39 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 545 ENLLVCAPTGSGKTNVAMLCILNEMEKNRNE-ETGIIdtdafkIVYIAPMKALVQEMVGNFSSRLQQYgIKVSELTGDRQ 623
Cdd:cd18074 18 KNIIICLPTGSGKTRVAVYITKDHLDKKRKAsEPGKV------IVLVNKVPLVEQHYRKEFNPFLKHW-YQVIGLSGDSQ 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317352187 624 LtkqQISETQIIvttpEKWDVI--TRKATDRSYTNLVR------------LIIIDEVHllHDDRGPVIESIVSRTIR 686
Cdd:cd18074 91 L---KISFPEVV----KRYDVIicTAQILENSLLNATEeedegvqlsdfsLIIIDECH--HTQKEAVYNNIMRRYLK 158
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
1381-1507 |
2.23e-04 |
|
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: 44.24 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1381 QTQVFNALYNmndNVFVGAPTGSGKTVCAEFALLRL--WsTPNhGRCVYIAPFQEVvdlqVAQWRQKFGKIQGGKN--IV 1456
Cdd:cd18033 8 FTIVQKALFQ---NTLVALPTGLGKTFIAAVVMLNYyrW-FPK-GKIVFMAPTKPL----VSQQIEACYKITGIPSsqTA 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1317352187 1457 ALTGETSADLR--LLESGDVIFATPTQwdVMSRRWKQRKNVQTVALFIADELH 1507
Cdd:cd18033 79 ELTGSVPPTKRaeLWASKRVFFLTPQT--LENDLKEGDCDPKSIVCLVIDEAH 129
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
532-669 |
2.87e-04 |
|
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: 44.11 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 532 IQSKIYPVAFEQdENLLVCAPTGSGKTNVAMLCILNEMEKNRNEEtgiIDTDAFKIVYIAPMKALVQEmVGNFSSRLQQY 611
Cdd:cd17961 20 IQSKAIPLALEG-KDILARARTGSGKTAAYALPIIQKILKAKAES---GEEQGTRALILVPTRELAQQ-VSKVLEQLTAY 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317352187 612 G---IKVSELTG--DRQLTKQQISET-QIIVTTPEK-WDVITRKATDRSYTnlVRLIIIDEVHLL 669
Cdd:cd17961 95 CrkdVRVVNLSAssSDSVQRALLAEKpDIVVSTPARlLSHLESGSLLLLST--LKYLVIDEADLV 157
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
532-704 |
2.95e-04 |
|
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: 44.54 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 532 IQSKIYPVAFEQDENLLVCAPTGSGKT---NVAMLC-ILNEMEKNRNEE-----TGIIdtdafkivyIAPMKALVQEMVG 602
Cdd:cd17946 16 IQALALPAAIRDGKDVIGAAETGSGKTlafGIPILErLLSQKSSNGVGGkqkplRALI---------LTPTRELAVQVKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 603 NFSSRLQQYGIKVSELTGDRQLTKQQ--ISET-QIIVTTPEK-WDVITRkatDRSYTNLVRLI---IIDEV-HLLHDDRG 674
Cdd:cd17946 87 HLKAIAKYTNIKIASIVGGLAVQKQErlLKKRpEIVVATPGRlWELIQE---GNEHLANLKSLrflVLDEAdRMLEKGHF 163
|
170 180 190
....*....|....*....|....*....|
gi 1317352187 675 PVIESIVSRTIRHMEQTQEMIRLVGLSATL 704
Cdd:cd17946 164 AELEKILELLNKDRAGKKRKRQTFVFSATL 193
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
532-706 |
2.99e-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: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 532 IQSKIYPvAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNR--NEETGIIDtdafkiVYIAPMKALVQEM---VGNFSS 606
Cdd:cd17953 38 IQAQALP-AIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRpvKPGEGPIG------LIMAPTRELALQIyveCKKFSK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 607 RLqqyGIKVSELTGDRQLtKQQISE----TQIIVTTPEKW-DVITrkATDRSYTNLVRL--IIIDEVHLLHD-DRGPVIE 678
Cdd:cd17953 111 AL---GLRVVCVYGGSGI-SEQIAElkrgAEIVVCTPGRMiDILT--ANNGRVTNLRRVtyVVLDEADRMFDmGFEPQIM 184
|
170 180
....*....|....*....|....*...
gi 1317352187 679 SIVSrTIRHMEQTqemirlVGLSATLPN 706
Cdd:cd17953 185 KIVN-NIRPDRQT------VLFSATFPR 205
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1358-1531 |
3.19e-04 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 45.99 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1358 VSALRNREYEavyngwvdKFNPIQTQVFNALYNMNDnVFVGAPTGSGKTVCAEFALLR-LWSTPNHGRCVYIAPFQEVVd 1436
Cdd:PRK11634 18 LEALNDLGYE--------KPSPIQAECIPHLLNGRD-VLGMAQTGSGKTAAFSLPLLHnLDPELKAPQILVLAPTRELA- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1437 LQVAQWRQKFGKIQGGKNIVALTGETSAD--LRLLESG-DVIFATPTQ-WDVMSRRWKQRKNVQTVALFIADELHLIG-- 1510
Cdd:PRK11634 88 VQVAEAMTDFSKHMRGVNVVALYGGQRYDvqLRALRQGpQIVVGTPGRlLDHLKRGTLDLSKLSGLVLDEADEMLRMGfi 167
|
170 180
....*....|....*....|.
gi 1317352187 1511 SDVgptyEIIVSRMRyIAHQT 1531
Cdd:PRK11634 168 EDV----ETIMAQIP-EGHQT 183
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
525-681 |
3.28e-04 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 44.23 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 525 GARILNRIQSKIYPVAFeQDENLLVCAPTGSGKTNVAMLCILNEMeknrneetgIIDTDAFKIVYIAPMKALVQEMVGNF 604
Cdd:cd17954 19 GWKKPTKIQEEAIPVAL-QGRDIIGLAETGSGKTAAFALPILQAL---------LENPQRFFALVLAPTRELAQQISEQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 605 SSRLQQYGIKVSELTGDRQLTKQQISETQ---IIVTTPEK-WDVITRkaTDRSYTNLVRLIIIDEV-HLLHDDRGPVIES 679
Cdd:cd17954 89 EALGSSIGLKSAVLVGGMDMMAQAIALAKkphVIVATPGRlVDHLEN--TKGFSLKSLKFLVMDEAdRLLNMDFEPEIDK 166
|
..
gi 1317352187 680 IV 681
Cdd:cd17954 167 IL 168
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
1399-1507 |
3.99e-04 |
|
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: 43.32 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1399 APTGSGKTVCAEFALLRLWSTPNHGRCVYIAPFQEVVDlqvaQWRQKFGKIQGGKNIVALTGETSADlrllESGDVIFAT 1478
Cdd:cd18032 27 MATGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLE----QAERSFKEVLPDGSFGNLKGGKKKP----DDARVVFAT 98
|
90 100 110
....*....|....*....|....*....|
gi 1317352187 1479 ptqWDVMSRRWKQRK-NVQTVALFIADELH 1507
Cdd:cd18032 99 ---VQTLNKRKRLEKfPPDYFDLIIIDEAH 125
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
1376-1559 |
6.49e-04 |
|
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: 43.20 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1376 KFNPIQTQVFNALYNmNDNVFVGAPTGSGKTVCAEFALLRlwSTPNHGRCVYIAPFQevvdlqvAQWRQKFGKIQggkni 1455
Cdd:cd18024 32 TLDPFQKTAIACIER-NESVLVSAHTSAGKTVVAEYAIAQ--SLRDKQRVIYTSPIK-------ALSNQKYRELQ----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1456 valtgETSADLRLLeSGDVIFATPTQWDVM------SRRWKQRKNVQTVALFIADELHLI-GSDVGPTYE---IIVSRMr 1525
Cdd:cd18024 97 -----EEFGDVGLM-TGDVTINPNASCLVMtteilrSMLYRGSEIMREVAWVIFDEIHYMrDKERGVVWEetiILLPDK- 169
|
170 180 190
....*....|....*....|....*....|....
gi 1317352187 1526 yiahqtknpIRIVCLSTSLANAQDLGEWIGSTPH 1559
Cdd:cd18024 170 ---------VRYVFLSATIPNARQFAEWICKIHK 194
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
548-704 |
6.74e-04 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 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: 350696 [Multi-domain] Cd Length: 204 Bit Score: 43.08 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 548 LVCAPTGSGKTNVAMLCILnemeknrneetgiidtdafKIV---YIAPMKALVQ---EMVGNFSSRLQQYGIKVSELTGD 621
Cdd:cd17938 40 LMAAETGSGKTGAFCLPVL-------------------QIVvalILEPSRELAEqtyNCIENFKKYLDNPKLRVALLIGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 622 ---RQLTKQQISETQIIVTTPEK-WDVITRKATDRSYtnlVRLIIIDEV-HLLHDDRGPVIESIVSRTIRHMEQTQEMIR 696
Cdd:cd17938 101 vkaREQLKRLESGVDIVVGTPGRlEDLIKTGKLDLSS---VRFFVLDEAdRLLSQGNLETINRIYNRIPKITSDGKRLQV 177
|
....*...
gi 1317352187 697 LVgLSATL 704
Cdd:cd17938 178 IV-CSATL 184
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
546-667 |
8.26e-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: 42.40 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 546 NLLVCAPTGSGKTNVAMLCILNEMEKNRNeetgiidtdafkIVYIAPMKALVQEMVGNFSSRLQQygIKVSELTGDrqlT 625
Cdd:cd17918 38 DRLLSGDVGSGKTLVALGAALLAYKNGKQ------------VAILVPTEILAHQHYEEARKFLPF--INVELVTGG---T 100
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1317352187 626 KQQI-SETQIIVTTPEkwdVITRkatDRSYTNLVrLIIIDEVH 667
Cdd:cd17918 101 KAQIlSGISLLVGTHA---LLHL---DVKFKNLD-LVIVDEQH 136
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1332-1479 |
9.41e-04 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 43.98 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1332 PMSFRHLILPKkypphtELLDmqplpvsALRNREYEavyngwvdKFNPIQTQVFNALYNMNDnVFVGAPTGSGKTvcAEF 1411
Cdd:COG0513 1 MMSFADLGLSP------PLLK-------ALAELGYT--------TPTPIQAQAIPLILAGRD-VLGQAQTGTGKT--AAF 56
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317352187 1412 AL---LRL-WSTPNHGRCVYIAPFQEVVdLQVAQWRQKFGKIQGGKnIVALTGETSAD--LRLLESG-DVIFATP 1479
Cdd:COG0513 57 LLpllQRLdPSRPRAPQALILAPTRELA-LQVAEELRKLAKYLGLR-VATVYGGVSIGrqIRALKRGvDIVVATP 129
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
849-922 |
1.33e-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: 41.01 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 849 LFADGHI--QVLVSTATLAWGVNLPAHTVIIkgTQVYSPEKGRWVELSPQDVLQMLGRAGRpqydtFG----EGIIITSH 922
Cdd:cd18805 63 LFNDPESgyDVLVASDAIGMGLNLNIRRVIF--SSLSKFDGNEMRPLSPSEVKQIAGRAGR-----FGshfpEGEVTTLR 135
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
540-703 |
1.82e-03 |
|
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: 41.01 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 540 AFEQDEN-LLVCAPTGSGKTNVAMLCILNEMEKNRNEetgiidtdafKIVYIAPMKALVQEMVGNFssRLQQYGIKVSEL 618
Cdd:cd18032 15 AREKGQRrALLVMATGTGKTYTAAFLIKRLLEANRKK----------RILFLAHREELLEQAERSF--KEVLPDGSFGNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 619 TGDrqltKQQISETQIIVTTpekWDVITRKATDRSYT-NLVRLIIIDEVHllhddRGpvIESIVSRTIRHMEQTqemiRL 697
Cdd:cd18032 83 KGG----KKKPDDARVVFAT---VQTLNKRKRLEKFPpDYFDLIIIDEAH-----HA--IASSYRKILEYFEPA----FL 144
|
....*.
gi 1317352187 698 VGLSAT 703
Cdd:cd18032 145 LGLTAT 150
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
547-717 |
2.90e-03 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are 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: 350810 [Multi-domain] Cd Length: 264 Bit Score: 41.88 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 547 LLVCAPTGSGKTNVAMLCILNEMEKNRNEETGIIDTDAFKIVYIAPMKALVQEM---VGNFSsrlqqYG--IKVSELTGD 621
Cdd:cd18052 83 LMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIfleARKFS-----YGtcIRPVVVYGG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 622 RQlTKQQISETQ----IIVTTPEKW-DVITRKatdrsYTNL--VRLIIIDEVhllhdDR------GPVIESIVSRTirHM 688
Cdd:cd18052 158 VS-VGHQIRQIEkgchILVATPGRLlDFIGRG-----KISLskLKYLILDEA-----DRmldmgfGPEIRKLVSEP--GM 224
|
170 180 190
....*....|....*....|....*....|...
gi 1317352187 689 EQTQEMIRLVgLSATLPNygDV----ATFLRVD 717
Cdd:cd18052 225 PSKEDRQTLM-FSATFPE--EIqrlaAEFLKED 254
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
1381-1548 |
3.79e-03 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 40.71 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1381 QTQVFNALynMNDNVFVGAPTGSGKTVCA-----EFALLRLWSTPNHGRCVYIAPFQEVVDLQVAQWRQ----KFGKIQG 1451
Cdd:cd18034 7 QLELFEAA--LKRNTIVVLPTGSGKTLIAvmlikEMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRShtdlKVGEYSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1452 GKNIVALTGETSadLRLLESGDVIFATP-TQWDVMSRRWKQRKNVQtvaLFIADELHLIGSDvGPtYEIIVSRMRYIAHQ 1530
Cdd:cd18034 85 EMGVDKWTKERW--KEELEKYDVLVMTAqILLDALRHGFLSLSDIN---LLIFDECHHATGD-HP-YARIMKEFYHLEGR 157
|
170
....*....|....*...
gi 1317352187 1531 TKNPiRIVCLSTSLANAQ 1548
Cdd:cd18034 158 TSRP-RILGLTASPVNGK 174
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1348-1432 |
5.51e-03 |
|
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: 41.61 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 1348 TELLDMQPLPVSALRNREYEAVYNGWVD---KFNPIQTQVFNALYNMNDN----VFVGAPTGSGKTvcaEFAL---LRLW 1417
Cdd:COG1203 96 SANFDMARQALDHLLAERLERLLPKKSKprtPINPLQNEALELALEAAEEepglFILTAPTGGGKT---EAALlfaLRLA 172
|
90
....*....|....*
gi 1317352187 1418 STPNHGRCVYIAPFQ 1432
Cdd:COG1203 173 AKHGGRRIIYALPFT 187
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
547-795 |
5.54e-03 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 41.26 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 547 LLVCAPTGSGKTNVAMLCILNEMEKnrneetGIIDtdafKIVYIAPMKALVQEM------------VGNFSSRLQQYGIK 614
Cdd:cd09639 2 LVIEAPTGYGKTEAALLWALHSLKS------QKAD----RVIIALPTRATINAMyrrakeafgetgLYHSSILSSRIKEM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 615 VSELTGDRQLTKQQISE-----TQIIVTTPEKWDVITRKATDRSYTNLVRL----IIIDEVHLLHDDRGPVIESIVsRTI 685
Cdd:cd09639 72 GDSEEFEHLFPLYIHSNdtlflDPITVCTIDQVLKSVFGEFGHYEFTLASIanslLIFDEVHFYDEYTLALILAVL-EVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 686 RHMEQtqemiRLVGLSATLPNYgdvatFLRVDPKKGLFHFDSSFRPCPLKQEFIGVTEKKAIKRFQVMNE---------- 755
Cdd:cd09639 151 KDNDV-----PILLMSATLPKF-----LKEYAEKIGYVEENEPLDLKPNERAPFIKIESDKVGEISSLERllefikkggs 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1317352187 756 ------------VTYQKVVEQAGKNQVLIFvHSR-KETAKTAKTIKDMALEKD 795
Cdd:cd09639 221 vaiivntvdraqEFYQQLKEKGPEEEIMLI-HSRfTEKDRAKKEAELLLEFKK 272
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
548-709 |
5.67e-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: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 548 LVCAPTGSGKTNVAMLCILNEM--------EKNRNEETGIIDTDAFKIVYIAPMKALVQEmVGNFSSRLQQY-GIKVSEL 618
Cdd:cd17965 65 LLAAETGSGKTLAYLAPLLDYLkrqeqepfEEAEEEYESAKDTGRPRSVILVPTHELVEQ-VYSVLKKLSHTvKLGIKTF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 619 TGDRQLTKQQISE-----TQIIVTTPEKwdvITRKATDRSYT-NLVRLIIIDEVHLLHDDrgpvieSIVSRTIRHMEQTQ 692
Cdd:cd17965 144 SSGFGPSYQRLQLafkgrIDILVTTPGK---LASLAKSRPKIlSRVTHLVVDEADTLFDR------SFLQDTTSIIKRAP 214
|
170
....*....|....*..
gi 1317352187 693 EMIRLVGLSATLPNYGD 709
Cdd:cd17965 215 KLKHLILCSATIPKEFD 231
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
554-667 |
6.22e-03 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member 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: 350750 [Multi-domain] Cd Length: 225 Bit Score: 40.59 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 554 GSGKTNVAMLCILNEMEknrneetgiidtDAFKIVYIAPMKALVQEMVGNFSSRLQQYGIKVSELTG-----DRQLTKQQ 628
Cdd:cd17992 76 GSGKTVVAALAMLAAVE------------NGYQVALMAPTEILAEQHYDSLKKLLEPLGIRVALLTGstkakEKREILEK 143
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1317352187 629 ISETQIIVttpekwdVITRKA---TDRSYTNLvRLIIIDEVH 667
Cdd:cd17992 144 IASGEIDI-------VIGTHAliqEDVEFHNL-GLVIIDEQH 177
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
527-667 |
9.39e-03 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350687 [Multi-domain] Cd Length: 178 Bit Score: 39.50 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317352187 527 RILNRIQSkiypvAFEQDENLLVCAPTGSGKTNVAMLCILNEMEKNRNeetgiidtdafkIVYIAPMKALVQEMVGNFSS 606
Cdd:cd17929 3 KAYEAIVS-----SLGGFKTFLLHGVTGSGKTEVYIELIEKVLAKGKQ------------VLVLVPEISLTPQLIKRFKK 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317352187 607 RlqqYGIKV----SELT-GDRQLTKQQISETQIIVttpekwdVI-TRKATDRSYTNLvRLIIIDEVH 667
Cdd:cd17929 66 R---FGDKVavlhSKLSdKERADEWRKIKRGEAKV-------VIgARSALFAPFKNL-GLIIVDEEH 121
|
|
| |
