|
Name |
Accession |
Description |
Interval |
E-value |
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
982-1285 |
8.15e-152 |
|
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: 471.30 E-value: 8.15e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 982 TELGRIASHYYITNDTVQTYNQLLKPTLSEIELFRVFSLSSEFKNITVREEEKLELQKLLERVPIPVKESIEEPSAKINV 1061
Cdd:pfam02889 2 TDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKGDIEDPHAKVNI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1062 LLQAFISQLKLEGFALMADMVYVTQSAGRLMRAIFEIVLNRGWAQLTDKTLNLCKMIDKRMWQSMCPLRQFRKLPEEVVK 1141
Cdd:pfam02889 82 LLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPELIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1142 KIEKKNFP--FERLYDLNHNEIGELIRMPKMGKTIHKYVHLFPKLELSVHLQPITRSTLKVELTITPDFQWDEKVHGSSE 1219
Cdd:pfam02889 162 KLEKKGVEsvRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGKSE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40217847 1220 AFWILVEDVDSEVILHHEYFLLKAKYAQDEHLITFFVPVFEPLPPQYFIRVVSDRWLSCETQLPVS 1285
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 ... |
464-677 |
3.14e-149 |
|
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: 460.30 E-value: 3.14e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 464 VEKLPKYAQAGFEGFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREIGKHINMDGTINVDDFKIIYIAP 543
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGTINLDAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 544 MRSLVQEMVGSFGKRLATYGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGGERTYTQLVRLIILDEIHLLHDD 623
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 40217847 624 RGPVLEALVARAIRNIEMTQEDVRLIGLSATLPNYEDVATFLRVDPAKGLFYFD 677
Cdd:cd18019 161 RGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
979-1287 |
4.12e-129 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 407.80 E-value: 4.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 979 FQVTELGRIASHYYITNDTVQTYNQLLKPTLSEIELFRVFSLSSEFKNITVREEEKLELQKLLERVPIPVK-ESIEEPSA 1057
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLEnPSLDDPHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1058 KINVLLQAFISQLKLEGFALMADMVYVTQSAGRLMRAIFEIVLNRGWAQLTDKTLNLCKMIDKRMWQSMCPLRQFRKLPE 1137
Cdd:smart00611 82 KANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1138 EVVKKIEKKN-FPFERLYDLNHNEIGELIRMP-KMGKTIHKYVHLFPKLELSVHLQPITRSTLKVELTITPDFQWDEKVH 1215
Cdd:smart00611 162 EILKRLEKKKvLSLEDLLELEDEERGELLGLLdAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEIH 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40217847 1216 GSSEAFWILVEDVDSEVILHHEYFLLKAKYAQDEHLITFFVPVFEPLpPQYFIRVVSDRWLSCETQLPVSFR 1287
Cdd:smart00611 242 GKQEGWWLVIGDSDGNELLHIERFSLNKKNVSEEVKLDFTAPATEGN-YQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1325-1515 |
1.41e-125 |
|
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: 392.39 E-value: 1.41e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1325 FPFFNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEQVYMDWYEKFQDRLNKK 1404
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPLLGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1405 VVLLTGETSTDLKLLGKGNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVHLIGGENGPVLEVICSRMRYISSQIERP 1484
Cdd:cd18021 81 VVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 40217847 1485 IRIVALSSSLSNAKDVAHWLGCSATSTFNFH 1515
Cdd:cd18021 161 IRIVGLSSSLANARDVGEWLGASKSTIFNFH 191
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1809-2125 |
2.83e-124 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 393.93 E-value: 2.83e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1809 DVAPLNLGMIAAYYYINYTTIELFSMSLNAKTKVRGLIEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLNNPKFNDPH 1888
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1889 VKTNLLLQAHLSRMQL-SAELQSDTEEILSKAIRLIQACVDVLSSNGWLSPALAAMELAQMVTQAMWSKDSYLKQLPHFT 1967
Cdd:smart00611 81 VKANLLLQAHLSRLKLpSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1968 SEHIKRCTDKGVESVFDIMEMEDEERNALLQLTDSQIADVARFCNRYPNIELSYEVVDKDSIRSGGPVVVLVQLEREEEV 2047
Cdd:smart00611 161 EEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 2048 TGpviaplfpqkREEGWWVVIGDAKSNSLISIKRLTLQQKAK---VKLDFVAPAT-GAHNYTLYFMSDAYMGCDQEYKFS 2123
Cdd:smart00611 241 HG----------KQEGWWLVIGDSDGNELLHIERFSLNKKNVseeVKLDFTAPATeGNYQYTLRLVSDSYLGCDQEYPLS 310
|
..
gi 40217847 2124 VD 2125
Cdd:smart00611 311 FD 312
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1812-2123 |
2.71e-118 |
|
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: 376.93 E-value: 2.71e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1812 PLNLGMIAAYYYINYTTIELFSMSLNAKTKVRGLIEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLNnPKFNDPHVKT 1891
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVK-GDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1892 NLLLQAHLSRMQL-SAELQSDTEEILSKAIRLIQACVDVLSSNGWLSPALAAMELAQMVTQAMWSKDSYLKQLPHFTSEH 1970
Cdd:pfam02889 80 NILLQAYISRLKLpGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1971 IKRCTDKGVESVFDIMEMEDEERNALLQLTDSQIADVARFCNRYPNIELSYEVvdkdSIRSGGPVVVLVQLEreeevtgp 2050
Cdd:pfam02889 160 IKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEV----QPITRSVLRVEVTIT-------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 2051 viaPLFPQKRE-----EGWWVVIGDAKSNSLISIKRLTLQQKAK---VKLDFVAP--ATGAHNYTLYFMSDAYMGCDQEY 2120
Cdd:pfam02889 228 ---PDFPWDKRvhgksEGFWLVVGDSDGNEILHIERFTLTKRTLageHKLEFTVPpsDPGPPQLFVRLISDSWLGADQEV 304
|
...
gi 40217847 2121 KFS 2123
Cdd:pfam02889 305 PIS 307
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
462-1017 |
2.53e-99 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 331.09 E-value: 2.53e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 462 LPVEKLPKYAQAgfEGFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLreigKHINMDGtinvddfKIIYI 541
Cdd:COG1204 6 LPLEKVIEFLKE--RGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAIL----KALLNGG-------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 542 APMRSLVQEMVGSFGKRLATYGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGGErtYTQLVRLIILDEIHLLH 621
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDVDLVVVDEAHLID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 622 D-DRGPVLEALVARAIRniemTQEDVRLIGLSATLPNYEDVATFLRVDPakglfyFDNSFRPVPLeqtYVGITEKKAIkR 700
Cdd:COG1204 151 DeSRGPTLEVLLARLRR----LNPEAQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGVL-R 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 701 FQIMNEIVYEKI----MEHAGKN-QVLVFVHSRKETGKTARAIRDMCLEKDTLGLFLREGSASTEVLRTEAEQCKNLELK 775
Cdd:COG1204 217 FDDGSRRSKDPTlalaLDLLEEGgQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTNEKLA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 776 DLLPYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIKgtqvySPEKGRWTELGALDILQMLGR 855
Cdd:COG1204 297 DCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-----DTKRGGMVPIPVLEFKQMAGR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 856 AGRPQYDTKGEGILIT-SHGELQ--YYLSLLNQQLPIESQMVSK--LPDMLNAEIVLGNVQNAKDAVNWLGYAYLYIRML 930
Cdd:COG1204 372 AGRPGYDPYGEAILVAkSSDEADelFERYILGEPEPIRSKLANEsaLRTHLLALIASGFANSREELLDFLENTFYAYQYD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 931 RSPTLYGIshddlkgdplldQRRLDLvhtaalmLDKNNLVkyDKKTGNFQVTELGRIASHYYITNDTVQTYNQLLK---P 1007
Cdd:COG1204 452 KGDLEEVV------------DDALEF-------LLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadE 510
|
570
....*....|
gi 40217847 1008 TLSEIELFRV 1017
Cdd:COG1204 511 EFTDLGLLHL 520
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1309-1849 |
2.87e-79 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 272.92 E-value: 2.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1309 VSALRNSAFESLYqdkfpffnPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSseGRCVYITPMEALAEQ 1388
Cdd:COG1204 12 IEFLKERGIEELY--------PPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNG--GKALYIVPLRALASE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1389 VYMDWYEKFQDrLNKKVVLLTGETSTDLKLLGKGNIIISTPEKWDILSRrwKQRKNVQNINLFVVDEVHLIGGEN-GPVL 1467
Cdd:COG1204 82 KYREFKRDFEE-LGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDDESrGPTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1468 EVICSRMRyissQIERPIRIVALSSSLSNAKDVAHWLGCSA-TSTFnfhpnvRPVPL-ELHIQGFNISHTQTRLLSmAKP 1545
Cdd:COG1204 159 EVLLARLR----RLNPEAQIVALSATIGNAEEIAEWLDAELvKSDW------RPVPLnEGVLYDGVLRFDDGSRRS-KDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1546 VYHAITKHSPK-KPVIVFVPSRKQTRLTA---IDILTTCAADIQRQRFLHCTEKdLIPYLEKLS-DSTLKETLLNGVGYL 1620
Cdd:COG1204 228 TLALALDLLEEgGQVLVFVSSRRDAESLAkklADELKRRLTPEEREELEELAEE-LLEVSEETHtNEKLADCLEKGVAFH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1621 HEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAAHLVIIMDTQYYNGkihayVDYPIYDVLQMVGHANRPLQDDEG 1700
Cdd:COG1204 307 HAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1701 RCVIMCQGSK--KDFFKKFLY-EPLPVESHL--DHCMHDHFNAEIVTKTIENKQDAVDYLTWTFLYrrmtqnpnyynlqg 1775
Cdd:COG1204 382 EAILVAKSSDeaDELFERYILgEPEPIRSKLanESALRTHLLALIASGFANSREELLDFLENTFYA-------------- 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40217847 1776 isHRHLSDHLSELVEQTLSDLEQSKCISIEDEMdVAPLNLGMIAAYYYINYTTIELFSMSLNAKTK---VRGLIEII 1849
Cdd:COG1204 448 --YQYDKGDLEEVVDDALEFLLENGFIEEDGDR-LRATKLGKLVSRLYIDPLTAAELVDGLRKADEeftDLGLLHLI 521
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
681-871 |
1.21e-67 |
|
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: 225.12 E-value: 1.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 681 RPVPLEQTYVGITEKKAIKRFQIMNE-----IVYEKIMEHAGKNQVLVFVHSRKETGKTARAIRdmclekdtlglflreg 755
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 756 sastevlrteaeqcknlelkdllpyGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIKGTQVYS 835
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 40217847 836 PEkgRWTELGALDILQMLGRAGRPQYDTKGEGILIT 871
Cdd:cd18795 120 GK--GYRELSPLEYLQMIGRAGRPGFDTRGEAIIMT 153
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1310-1897 |
1.21e-55 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 208.52 E-value: 1.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1310 SALRNSAFESLYqdkfpffnPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSeGRCVYITPMEALAEQV 1389
Cdd:PRK00254 14 RVLKERGIEELY--------PPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREG-GKAVYLVPLKALAEEK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1390 YMDWyeKFQDRLNKKVVLLTGETSTDLKLLGKGNIIISTPEKWDILSR---RWkqrknVQNINLFVVDEVHLIGG-ENGP 1465
Cdd:PRK00254 85 YREF--KDWEKLGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSyDRGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1466 VLEVICSRMryissqIERPiRIVALSSSLSNAKDVAHWLGCSATSTfnfhpNVRPVPLELHI--QGFNI---SHTQTRLL 1540
Cdd:PRK00254 158 TLEMILTHM------LGRA-QILGLSATVGNAEELAEWLNAELVVS-----DWRPVKLRKGVfyQGFLFwedGKIERFPN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1541 SMAKPVYHAITKhspKKPVIVFVPSRKQTRLTAIDIlttcAADIQRqrflHCTEKDLIPyLEKLSDS--------TLKET 1612
Cdd:PRK00254 226 SWESLVYDAVKK---GKGALVFVNTRRSAEKEALEL----AKKIKR----FLTKPELRA-LKELADSleenptneKLKKA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1613 LLNGVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAAHLVIIMDTQYYNGkiHAYVDYPIYDVLQMVGHAN 1692
Cdd:PRK00254 294 LRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSN--FGWEDIPVLEIQQMMGRAG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1693 RPLQDDEGRCVIMCQGSK-KDFFKKFLY-EPLPVESHL--DHCMHDHFNAEIVTKTIENKQDAVDYLTWTFLYRrmtQNP 1768
Cdd:PRK00254 372 RPKYDEVGEAIIVATTEEpSKLMERYIFgKPEKLFSMLsnESAFRSQVLALITNFGVSNFKELVNFLERTFYAH---QRK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1769 NYYNLQGishrHLSDHLSELVEQTLSDleqskcISIEDEmdVAPLNLGMIAAYYYINYTTIELFSMSLNAKTK---VRGL 1845
Cdd:PRK00254 449 DLYSLEE----KAKEIVYFLLENEFID------IDLEDR--FIPLPLGIRTSQLYIDPLTAKKFKDAFPKIEKnpnPLGI 516
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40217847 1846 IEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLnnpKFNDPH------------VKTNLLLQA 1897
Cdd:PRK00254 517 FQLIASTPDMTPLNYSRKEMEDLLDEAYEMEDRL---YFNIPYwedykfqkflraFKTAKVLLD 577
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
477-1033 |
1.68e-50 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 192.72 E-value: 1.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 477 GFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCM----LREIGKhinmdgtinvddfkIIYIAPMRSLVQEMV 552
Cdd:PRK00254 20 GIEELYPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMvnklLREGGK--------------AVYLVPLKALAEEKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 553 GSFgKRLATYGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGGerTYTQLVRLIILDEIHLLHD-DRGPVLEAL 631
Cdd:PRK00254 86 REF-KDWEKLGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRHGS--SWIKDVKLVVADEIHLIGSyDRGATLEMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 632 VARAIrniemtqEDVRLIGLSATLPNYEDVATFLRVDPAKglfyfdNSFRPVPLEQT--YVG--ITEKKAIKRFQIM-NE 706
Cdd:PRK00254 163 LTHML-------GRAQILGLSATVGNAEELAEWLNAELVV------SDWRPVKLRKGvfYQGflFWEDGKIERFPNSwES 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 707 IVYEKIMEhagKNQVLVFVHSRKETGKTA----RAIRDMCLEKDTLGLflREGSASTEvlrteaEQCKNLELKDLLPYGF 782
Cdd:PRK00254 230 LVYDAVKK---GKGALVFVNTRRSAEKEAlelaKKIKRFLTKPELRAL--KELADSLE------ENPTNEKLKKALRGGV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 783 AIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIKGTQVYSpEKGrWTELGALDILQMLGRAGRPQYD 862
Cdd:PRK00254 299 AFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYS-NFG-WEDIPVLEIQQMMGRAGRPKYD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 863 TKGEGILITSHGE----LQYYL----SLLNQQLPIESQMVSKLPdmlnAEIVLGNVQNAKDAVNWLgyaylyirmlrSPT 934
Cdd:PRK00254 377 EVGEAIIVATTEEpsklMERYIfgkpEKLFSMLSNESAFRSQVL----ALITNFGVSNFKELVNFL-----------ERT 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 935 LYGISHDDLKgdpLLDQRRLDLVHtaalMLDKNNLVKYDKKTgNFQVTELGRIASHYYITNDTVQTYnqllKPTLSEIE- 1013
Cdd:PRK00254 442 FYAHQRKDLY---SLEEKAKEIVY----FLLENEFIDIDLED-RFIPLPLGIRTSQLYIDPLTAKKF----KDAFPKIEk 509
|
570 580
....*....|....*....|....*.
gi 40217847 1014 ------LFRVFSLSSEFKNITVREEE 1033
Cdd:PRK00254 510 npnplgIFQLIASTPDMTPLNYSRKE 535
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1519-1707 |
2.22e-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: 166.96 E-value: 2.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1519 RPVPLELHIQGFNISHTQTRLLSMAK-----PVYHAITKHSPKKPVIVFVPSRKQTRLTAIDILttcaadiqrqrflhct 1593
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1594 ekdlipyleklsdstlketllnGVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAAHLVIIMDTQYYNGKi 1673
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGK- 121
|
170 180 190
....*....|....*....|....*....|....
gi 40217847 1674 hAYVDYPIYDVLQMVGHANRPLQDDEGRCVIMCQ 1707
Cdd:cd18795 122 -GYRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
254-363 |
2.30e-46 |
|
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: 162.39 E-value: 2.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 254 KKKDLHPRDIDAFWLQRQLSRFYDDAIVSQKKADEVLEILKTASDD-RECENQLVLLLGFNTFDFIKVLRQHRMMILYCT 332
Cdd:pfam18149 1 DKDSLDPHDIDAFWLQRLLSKFYGDAIEAQKKAEEVLDILESAADDlRECENQLVELLDYDKFDLVKLLLKNRDKIVWCT 80
|
90 100 110
....*....|....*....|....*....|.
gi 40217847 333 LLASAQSEAEKERIMGKMEADPELSKFLYQL 363
Cdd:pfam18149 81 KLARAQSEEEKQAIEEEMRSNPGLAWILDEL 111
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1329-1500 |
3.55e-33 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 126.97 E-value: 3.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1329 NPIQTQVFNTVYnSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEG-RCVYITPMEALAEQVYMDWYEKFQDRLNKKVVL 1407
Cdd:pfam00270 1 TPIQAEAIPAIL-EGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGpQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1408 LTG-ETSTDLKLLGKGNIIISTPEKWDILSRrwkQRKNVQNINLFVVDEVHLIGGEN-GPVLEVICSRMRYissqierPI 1485
Cdd:pfam00270 80 LGGdSRKEQLEKLKGPDILVGTPGRLLDLLQ---ERKLLKNLKLLVLDEAHRLLDMGfGPDLEEILRRLPK-------KR 149
|
170
....*....|....*.
gi 40217847 1486 RIVALSSSLS-NAKDV 1500
Cdd:pfam00270 150 QILLLSATLPrNLEDL 165
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
482-661 |
6.86e-33 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 126.20 E-value: 6.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 482 NRIQSKLYRAALEtDENLLLCAPTGAGKTNVALMCMLREIGKhinmdgtiNVDDFKIIYIAPMRSLVQEMVGSFGKRLAT 561
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK--------LDNGPQALVLAPTRELAEQIYEELKKLGKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 562 YGITVAELTGDH--QLCKEEISATQIIVCTPEKWDIITRkggERTYTQLVRLIILDEIHLLHD-DRGPVLEALvarairn 638
Cdd:pfam00270 72 LGLKVASLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQ---ERKLLKNLKLLVLDEAHRLLDmGFGPDLEEI------- 141
|
170 180
....*....|....*....|....
gi 40217847 639 IEMTQEDVRLIGLSATLP-NYEDV 661
Cdd:pfam00270 142 LRRLPKKRQILLLSATLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1320-1508 |
1.33e-29 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 117.98 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1320 LYQDKFPFFNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEQVYMDWYEKFQD 1399
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1400 RLNKKVVLLTGETSTDLK---LLGKGNIIISTPEKWDILSRRWKqrKNVQNINLFVVDEVH-LIGGENGPVLEVICSRMR 1475
Cdd:smart00487 81 LGLKVVGLYGGDSKREQLrklESGKTDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP 158
|
170 180 190
....*....|....*....|....*....|...
gi 40217847 1476 yissqieRPIRIVALSSSLSNAKDVAHWLGCSA 1508
Cdd:smart00487 159 -------KNVQLLLLSATPPEEIENLLELFLND 184
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
477-684 |
8.82e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.81 E-value: 8.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 477 GFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREIGKHinmdgtinvDDFKIIYIAPMRSLVQEMVGSFG 556
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRG---------KGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 557 KRLA-TYGITVAELTGD---HQLCKEEISATQIIVCTPEKWDIITRKGgeRTYTQLVRLIILDEIHLLHD-DRGPVLEAL 631
Cdd:smart00487 76 KLGPsLGLKVVGLYGGDskrEQLRKLESGKTDILVTTPGRLLDLLEND--KLSLSNVDLVILDEAHRLLDgGFGDQLEKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 40217847 632 VARAIRNiemtqedVRLIGLSATLPNYEDVATFLRVdpaKGLFYFDNSFRPVP 684
Cdd:smart00487 154 LKLLPKN-------VQLLLLSATPPEEIENLLELFL---NDPVFIDVGFTPLE 196
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
458-865 |
3.39e-23 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 107.67 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 458 EEQLLPVEKL---PKYAQAGFEGFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCmlrEIGKHINMDGtinvd 534
Cdd:COG1202 184 EVDTVPVDDLdlpPELKDLLEGRGEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELA---GIKNALEGKG----- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 535 dfKIIYIAPMRSLVQEMVGSFGKRlatY--GITVAELTGDHQLC---KEEISATQIIVCTPEKWDIITRKGgeRTYTQlV 609
Cdd:COG1202 256 --KMLFLVPLVALANQKYEDFKDR---YgdGLDVSIRVGASRIRddgTRFDPNADIIVGTYEGIDHALRTG--RDLGD-I 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 610 RLIILDEIHLLHD-DRGPVLEALVARaIRNIemtQEDVRLIGLSATLPNYEDVATFLRvdpAKgLFYFDNsfRPVPLEQt 688
Cdd:COG1202 328 GTVVIDEVHMLEDpERGHRLDGLIAR-LKYY---CPGAQWIYLSATVGNPEELAKKLG---AK-LVEYEE--RPVPLER- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 689 YVGITEKKAIKRfqIMNEIV---YEKIMEHAGKNQVLVFVHSRKETGKTARAirdmclekdtlglflregsastevlrte 765
Cdd:COG1202 397 HLTFADGREKIR--IINKLVkreFDTKSSKGYRGQTIIFTNSRRRCHEIARA---------------------------- 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 766 aeqcknlelkdlLPYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVI-------IKgtqvyspek 838
Cdd:COG1202 447 ------------LGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIfdslamgIE--------- 505
|
410 420
....*....|....*....|....*..
gi 40217847 839 grWteLGALDILQMLGRAGRPQYDTKG 865
Cdd:COG1202 506 --W--LSVQEFHQMLGRAGRPDYHDRG 528
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
485-873 |
8.68e-17 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 86.84 E-value: 8.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 485 QSKLYRAALEtDENLLLCAPTGAGKTNVALMCMLREIGKhinmDGTINVDDFKIIYIAPMRSL-------VQEMVGSFGK 557
Cdd:TIGR04121 18 QLEMWAAALE-GRSGLLIAPTGSGKTLAGFLPSLIDLAG----PEAPKEKGLHTLYITPLRALavdiarnLQAPIEELGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 558 rlatyGITVAELTGD---HQLCKEEISATQIIVCTPEKWDI-ITRKGGERTYTQLvRLIILDEIH-LLHDDRGPVLEALV 632
Cdd:TIGR04121 93 -----PIRVETRTGDtssSERARQRKKPPDILLTTPESLALlLSYPDAARLFKDL-RCVVVDEWHeLAGSKRGDQLELAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 633 ARairnIEMTQEDVRLIGLSATLPNYEDVATFL-RVDPAKGLFYFDNSFRPVPLEqTYVGITEKK-------AIKRFqim 704
Cdd:TIGR04121 167 AR----LRRLAPGLRRWGLSATIGNLEEARRVLlGVGGAPAVLVRGKLPKAIEVI-SLLPESEERfpwaghlGLRAL--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 705 nEIVYEKIMEHagkNQVLVFVHSRKETGKTARAIRDmclekdtlglflregsastevlrteaeqcKNLELKDLLpygfAI 784
Cdd:TIGR04121 239 -PEVYAEIDQA---RTTLVFTNTRSQAELWFQALWE-----------------------------ANPEFALPI----AL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 785 HHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVN-LPAHTVIikgtQVYSPEkgrwtelGALDILQMLGRAG-RPqyD 862
Cdd:TIGR04121 282 HHGSLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDfGPVDLVI----QIGSPK-------GVARLLQRAGRSNhRP--G 348
|
410
....*....|.
gi 40217847 863 TKGEGILITSH 873
Cdd:TIGR04121 349 EPSRALLVPTN 359
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1292-1646 |
4.48e-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: 84.50 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1292 PEKYPPPTellDLQPLPVSALRNSAFESLYqdKFpffnpiQTQVFNTVYNsDDNVFVGAPTGSGKTICAEFAILRMLLQS 1371
Cdd:COG1205 32 ARYAPWPD---WLPPELRAALKKRGIERLY--SH------QAEAIEAARA-GKNVVIATPTASGKSLAYLLPVLEALLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1372 SEGRCVYITPMEALAEqvymDWYEKFQDRLNK-----KVVLLTGETSTDL--KLLGKGNIIISTPEKWD--ILSRRWKQR 1442
Cdd:COG1205 100 PGATALYLYPTKALAR----DQLRRLRELAEAlglgvRVATYDGDTPPEErrWIREHPDIVLTNPDMLHygLLPHHTRWA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1443 KNVQNINLFVVDEVHL---IGGENgpV------LEVIC----SRMRYISSQ-------------IERPIRIVALSSSLSN 1496
Cdd:COG1205 176 RFFRNLRYVVIDEAHTyrgVFGSH--VanvlrrLRRICrhygSDPQFILASatignpaehaerlTGRPVTVVDEDGSPRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1497 AKDVAHWlgcsatstfnfHPNVRPVPLELHiqgfniSHTQTRLLsMAKPVYHAItkhspkkPVIVFVPSRKQTRLTAIDI 1576
Cdd:COG1205 254 ERTFVLW-----------NPPLVDDGIRRS------ALAEAARL-LADLVREGL-------RTLVFTRSRRGAELLARYA 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40217847 1577 lttcaadiqRQRFLHCTEKDLI-PYleklsdstlketllngvgylHEGLSPMERRLVEQLFSSGAIQVVVA 1646
Cdd:COG1205 309 ---------RRALREPDLADRVaAY--------------------RAGYLPEERREIERGLRSGELLGVVS 350
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
773-859 |
1.18e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 68.01 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 773 ELKDLL---PYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLP-AHTVIIKGTqVYSPEkgrwtelgalD 848
Cdd:smart00490 2 ELAELLkelGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL-PWSPA----------S 70
|
90
....*....|.
gi 40217847 849 ILQMLGRAGRP 859
Cdd:smart00490 71 YIQRIGRAGRA 81
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
1350-1650 |
8.03e-11 |
|
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: 67.58 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1350 APTGSGKTICAEFAILRMLLQSSEGRC-----VYITPMEALAEQVY---------MDwyekfqdrLNKKVVLLTGETSTD 1415
Cdd:TIGR04121 35 APTGSGKTLAGFLPSLIDLAGPEAPKEkglhtLYITPLRALAVDIArnlqapieeLG--------LPIRVETRTGDTSSS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1416 LK---LLGKGNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVH-LIGGENGPVLEVICSRMRYISSQierpIRIVALS 1491
Cdd:TIGR04121 107 ERarqRKKPPDILLTTPESLALLLSYPDAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG----LRRWGLS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1492 SSLSNAKDVAHWLGcsatstfnfHPNVRPVPLelhIQGFN---------ISHTQTRL-------LSMAKPVYHAITKHsp 1555
Cdd:TIGR04121 183 ATIGNLEEARRVLL---------GVGGAPAVL---VRGKLpkaievislLPESEERFpwaghlgLRALPEVYAEIDQA-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1556 kKPVIVFVPSRKQTrltaidilttcaadiqrQRFLHCtekdlipYLEKLSDstlketlLNGVGYLHEG-LSPMERRLVEQ 1634
Cdd:TIGR04121 249 -RTTLVFTNTRSQA-----------------ELWFQA-------LWEANPE-------FALPIALHHGsLDREQRRWVEA 296
|
330
....*....|....*.
gi 40217847 1635 LFSSGAIQVVVASRSL 1650
Cdd:TIGR04121 297 AMAAGRLRAVVCTSSL 312
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1350-1662 |
1.08e-10 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 67.26 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1350 APTGSGKTICA-EFAILRMLLQSSE----------GRCVYITPMEALAEQV----------YMDWYEKFQD-RLNKKVVL 1407
Cdd:PRK09751 3 APTGSGKTLAAfLYALDRLFREGGEdtreahkrktSRILYISPIKALGTDVqrnlqiplkgIADERRRRGEtEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1408 LTGETSTD--LKLLGK-GNIIISTPEK-WDILSRRwkQRKNVQNINLFVVDEVHLIGG-ENGPVLEVICSRMryiSSQIE 1482
Cdd:PRK09751 83 RTGDTPAQerSKLTRNpPDILITTPESlYLMLTSR--ARETLRGVETVIIDEVHAVAGsKRGAHLALSLERL---DALLH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1483 RPIRIVALSSSLSNAKDVAHWLGCSATSTFNFHPNVRPVPLELHIQGFNISHT------------QTRLLSMAKPVYHAI 1550
Cdd:PRK09751 158 TSAQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRHPQIRIVVPVANMDDVssvasgtgedshAGREGSIWPYIETGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1551 TKHS-PKKPVIVFVPSRKQT-RLTAiDILTTCAADIQRqrflhcTEKDLIP--YLEKLSDSTLK-----ETLLngvGYLH 1621
Cdd:PRK09751 238 LDEVlRHRSTIVFTNSRGLAeKLTA-RLNELYAARLQR------SPSIAVDaaHFESTSGATSNrvqssDVFI---ARSH 307
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 40217847 1622 EG-LSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAA-HLVI 1662
Cdd:PRK09751 308 HGsVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAvDLVI 350
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1616-1694 |
7.64e-10 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 57.22 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1616 GVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNV-AAHLVIIMDtqyyngkihayVDYPIYDVLQMVGHANRP 1694
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLpGVDLVIIYD-----------LPWSPASYIQRIGRAGRA 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
774-858 |
1.83e-08 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 54.14 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 774 LKDLLPYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLP-AHTVIIkgtqvYSPEKGRwtelgaLDILQM 852
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YDLPWNP------ASYIQR 101
|
....*.
gi 40217847 853 LGRAGR 858
Cdd:pfam00271 102 IGRAGR 107
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
485-618 |
2.26e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 52.95 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 485 QSKLYRAALETdeNLLLCAPTGAGKTNVALMCMLREIGKHinmDGtinvddfKIIYIAPMRSLVQEMVGSFGKRLATYGI 564
Cdd:PRK13766 20 QQLLAATALKK--NTLVVLPTGLGKTAIALLVIAERLHKK---GG-------KVLILAPTKPLVEQHAEFFRKFLNIPEE 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 40217847 565 TVAELTGDHQLCK--EEISATQIIVCTPE--KWDIITrkggERTYTQLVRLIILDEIH 618
Cdd:PRK13766 88 KIVVFTGEVSPEKraELWEKAKVIVATPQviENDLIA----GRISLEDVSLLIFDEAH 141
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1617-1665 |
7.83e-03 |
|
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: 37.96 E-value: 7.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 40217847 1617 VGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNV-AAHLVIIMD 1665
Cdd:pfam00271 41 VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLpDVDLVINYD 90
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
982-1285 |
8.15e-152 |
|
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: 471.30 E-value: 8.15e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 982 TELGRIASHYYITNDTVQTYNQLLKPTLSEIELFRVFSLSSEFKNITVREEEKLELQKLLERVPIPVKESIEEPSAKINV 1061
Cdd:pfam02889 2 TDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKGDIEDPHAKVNI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1062 LLQAFISQLKLEGFALMADMVYVTQSAGRLMRAIFEIVLNRGWAQLTDKTLNLCKMIDKRMWQSMCPLRQFRKLPEEVVK 1141
Cdd:pfam02889 82 LLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPELIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1142 KIEKKNFP--FERLYDLNHNEIGELIRMPKMGKTIHKYVHLFPKLELSVHLQPITRSTLKVELTITPDFQWDEKVHGSSE 1219
Cdd:pfam02889 162 KLEKKGVEsvRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGKSE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40217847 1220 AFWILVEDVDSEVILHHEYFLLKAKYAQDEHLITFFVPVFEPLPPQYFIRVVSDRWLSCETQLPVS 1285
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 ... |
464-677 |
3.14e-149 |
|
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: 460.30 E-value: 3.14e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 464 VEKLPKYAQAGFEGFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREIGKHINMDGTINVDDFKIIYIAP 543
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGTINLDAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 544 MRSLVQEMVGSFGKRLATYGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGGERTYTQLVRLIILDEIHLLHDD 623
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 40217847 624 RGPVLEALVARAIRNIEMTQEDVRLIGLSATLPNYEDVATFLRVDPAKGLFYFD 677
Cdd:cd18019 161 RGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
979-1287 |
4.12e-129 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 407.80 E-value: 4.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 979 FQVTELGRIASHYYITNDTVQTYNQLLKPTLSEIELFRVFSLSSEFKNITVREEEKLELQKLLERVPIPVK-ESIEEPSA 1057
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLEnPSLDDPHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1058 KINVLLQAFISQLKLEGFALMADMVYVTQSAGRLMRAIFEIVLNRGWAQLTDKTLNLCKMIDKRMWQSMCPLRQFRKLPE 1137
Cdd:smart00611 82 KANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1138 EVVKKIEKKN-FPFERLYDLNHNEIGELIRMP-KMGKTIHKYVHLFPKLELSVHLQPITRSTLKVELTITPDFQWDEKVH 1215
Cdd:smart00611 162 EILKRLEKKKvLSLEDLLELEDEERGELLGLLdAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEIH 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40217847 1216 GSSEAFWILVEDVDSEVILHHEYFLLKAKYAQDEHLITFFVPVFEPLpPQYFIRVVSDRWLSCETQLPVSFR 1287
Cdd:smart00611 242 GKQEGWWLVIGDSDGNELLHIERFSLNKKNVSEEVKLDFTAPATEGN-YQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1325-1515 |
1.41e-125 |
|
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: 392.39 E-value: 1.41e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1325 FPFFNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEQVYMDWYEKFQDRLNKK 1404
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPLLGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1405 VVLLTGETSTDLKLLGKGNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVHLIGGENGPVLEVICSRMRYISSQIERP 1484
Cdd:cd18021 81 VVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 40217847 1485 IRIVALSSSLSNAKDVAHWLGCSATSTFNFH 1515
Cdd:cd18021 161 IRIVGLSSSLANARDVGEWLGASKSTIFNFH 191
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1809-2125 |
2.83e-124 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 393.93 E-value: 2.83e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1809 DVAPLNLGMIAAYYYINYTTIELFSMSLNAKTKVRGLIEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLNNPKFNDPH 1888
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1889 VKTNLLLQAHLSRMQL-SAELQSDTEEILSKAIRLIQACVDVLSSNGWLSPALAAMELAQMVTQAMWSKDSYLKQLPHFT 1967
Cdd:smart00611 81 VKANLLLQAHLSRLKLpSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1968 SEHIKRCTDKGVESVFDIMEMEDEERNALLQLTDSQIADVARFCNRYPNIELSYEVVDKDSIRSGGPVVVLVQLEREEEV 2047
Cdd:smart00611 161 EEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 2048 TGpviaplfpqkREEGWWVVIGDAKSNSLISIKRLTLQQKAK---VKLDFVAPAT-GAHNYTLYFMSDAYMGCDQEYKFS 2123
Cdd:smart00611 241 HG----------KQEGWWLVIGDSDGNELLHIERFSLNKKNVseeVKLDFTAPATeGNYQYTLRLVSDSYLGCDQEYPLS 310
|
..
gi 40217847 2124 VD 2125
Cdd:smart00611 311 FD 312
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1812-2123 |
2.71e-118 |
|
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: 376.93 E-value: 2.71e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1812 PLNLGMIAAYYYINYTTIELFSMSLNAKTKVRGLIEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLNnPKFNDPHVKT 1891
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVK-GDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1892 NLLLQAHLSRMQL-SAELQSDTEEILSKAIRLIQACVDVLSSNGWLSPALAAMELAQMVTQAMWSKDSYLKQLPHFTSEH 1970
Cdd:pfam02889 80 NILLQAYISRLKLpGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1971 IKRCTDKGVESVFDIMEMEDEERNALLQLTDSQIADVARFCNRYPNIELSYEVvdkdSIRSGGPVVVLVQLEreeevtgp 2050
Cdd:pfam02889 160 IKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEV----QPITRSVLRVEVTIT-------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 2051 viaPLFPQKRE-----EGWWVVIGDAKSNSLISIKRLTLQQKAK---VKLDFVAP--ATGAHNYTLYFMSDAYMGCDQEY 2120
Cdd:pfam02889 228 ---PDFPWDKRvhgksEGFWLVVGDSDGNEILHIERFTLTKRTLageHKLEFTVPpsDPGPPQLFVRLISDSWLGADQEV 304
|
...
gi 40217847 2121 KFS 2123
Cdd:pfam02889 305 PIS 307
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
982-1286 |
1.56e-109 |
|
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: 352.05 E-value: 1.56e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 982 TELGRIASHYYITNDTVQTYNQLLKPTLSEIELFRVFSLSSEFKNITVREEEKLELQKLLERVPIPVKESIEE-PSAKIN 1060
Cdd:smart00973 2 TELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDsPHAKVN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1061 VLLQAFISQLKLEGFALMADMVYVTQSAGRLMRAIFEIVLNRGWAQLTDKTLNLCKMIDKRMW-QSMCPLRQF-RKLPEE 1138
Cdd:smart00973 82 LLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWeDSDSPLKQLpHFLIED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1139 VVKKIEKKNFP--FERLYDLNHNEIGELI-RMPKMGKTIHKYVHLFPKLELSVHLQPITRS-TLKVELTITPDFQWDEKV 1214
Cdd:smart00973 162 VYDKLELKDGSrsFELLLDMNAAELGEFLnRLPPNGRLIYELLRRFPKIEVEAEVLPITRDlTLRVELEITPVFAWDLPR 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40217847 1215 -HGSSEAFWILVEDVDSEVILHHEYFLLKAKYAQDEHLITFFVPVFEPLPPQYFIRVVSDRWLSCETQLPVSF 1286
Cdd:smart00973 242 hKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKLDFTVPLSEPGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
1812-2124 |
3.54e-104 |
|
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: 336.64 E-value: 3.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1812 PLNLGMIAAYYYINYTTIELFSMSLNAKTKVRGLIEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLNNPKFNDPHVKT 1891
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1892 NLLLQAHLSRMQL-SAELQSDTEEILSKAIRLIQACVDVLSSNGWLSPALAAMELAQMVTQAMWS-KDSYLKQLPHFTse 1969
Cdd:smart00973 81 NLLLQAHLSRLPLpDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEdSDSPLKQLPHFL-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1970 hikrctdkgVESVFDIMEMEDEERNaLLQLTDSQIADVARFCNR-YPNIELSYEVVDKDSIRSGGPVVVLVQLE---REE 2045
Cdd:smart00973 159 ---------IEDVYDKLELKDGSRS-FELLLDMNAAELGEFLNRlPPNGRLIYELLRRFPKIEVEAEVLPITRDltlRVE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 2046 EVTGPVIAPLFPQ--KREEGWWVVIGDAKSNSLISIKRLTLQQKAK---VKLDFVAPAT--GAHNYTLYFMSDAYMGCDQ 2118
Cdd:smart00973 229 LEITPVFAWDLPRhkGKSESWWLVVGDSDTNELLAIKRVTLRKKKKsneVKLDFTVPLSepGPENYTVYLISDSYLGCDQ 308
|
....*.
gi 40217847 2119 EYKFSV 2124
Cdd:smart00973 309 EVSFSL 314
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
462-1017 |
2.53e-99 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 331.09 E-value: 2.53e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 462 LPVEKLPKYAQAgfEGFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLreigKHINMDGtinvddfKIIYI 541
Cdd:COG1204 6 LPLEKVIEFLKE--RGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAIL----KALLNGG-------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 542 APMRSLVQEMVGSFGKRLATYGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGGErtYTQLVRLIILDEIHLLH 621
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDVDLVVVDEAHLID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 622 D-DRGPVLEALVARAIRniemTQEDVRLIGLSATLPNYEDVATFLRVDPakglfyFDNSFRPVPLeqtYVGITEKKAIkR 700
Cdd:COG1204 151 DeSRGPTLEVLLARLRR----LNPEAQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGVL-R 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 701 FQIMNEIVYEKI----MEHAGKN-QVLVFVHSRKETGKTARAIRDMCLEKDTLGLFLREGSASTEVLRTEAEQCKNLELK 775
Cdd:COG1204 217 FDDGSRRSKDPTlalaLDLLEEGgQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTNEKLA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 776 DLLPYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIKgtqvySPEKGRWTELGALDILQMLGR 855
Cdd:COG1204 297 DCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-----DTKRGGMVPIPVLEFKQMAGR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 856 AGRPQYDTKGEGILIT-SHGELQ--YYLSLLNQQLPIESQMVSK--LPDMLNAEIVLGNVQNAKDAVNWLGYAYLYIRML 930
Cdd:COG1204 372 AGRPGYDPYGEAILVAkSSDEADelFERYILGEPEPIRSKLANEsaLRTHLLALIASGFANSREELLDFLENTFYAYQYD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 931 RSPTLYGIshddlkgdplldQRRLDLvhtaalmLDKNNLVkyDKKTGNFQVTELGRIASHYYITNDTVQTYNQLLK---P 1007
Cdd:COG1204 452 KGDLEEVV------------DDALEF-------LLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadE 510
|
570
....*....|
gi 40217847 1008 TLSEIELFRV 1017
Cdd:COG1204 511 EFTDLGLLHL 520
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
480-677 |
6.64e-93 |
|
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: 299.35 E-value: 6.64e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 480 TLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREIGKHINMDGTINVDDFKIIYIAPMRSLVQEMVGSFGKRL 559
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQGGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 560 ATYGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKG-GERTYTQLVRLIILDEIHLLHDDRGPVLEALVARAIRN 638
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSsGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 40217847 639 IEMTQEDVRLIGLSATLPNYEDVATFLRVDPAKGLFYFD 677
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1327-1514 |
4.90e-83 |
|
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: 270.78 E-value: 4.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1327 FFNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEQVYMDWYEKFQDRLNKKVV 1406
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1407 LLTGETSTDLKLLGKGNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVHLIGGENGPVLEVICSRMRYISSQIERPIR 1486
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*...
gi 40217847 1487 IVALSSSLSNAKDVAHWLGCSATSTFNF 1514
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNF 188
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1309-1849 |
2.87e-79 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 272.92 E-value: 2.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1309 VSALRNSAFESLYqdkfpffnPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSseGRCVYITPMEALAEQ 1388
Cdd:COG1204 12 IEFLKERGIEELY--------PPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNG--GKALYIVPLRALASE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1389 VYMDWYEKFQDrLNKKVVLLTGETSTDLKLLGKGNIIISTPEKWDILSRrwKQRKNVQNINLFVVDEVHLIGGEN-GPVL 1467
Cdd:COG1204 82 KYREFKRDFEE-LGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDDESrGPTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1468 EVICSRMRyissQIERPIRIVALSSSLSNAKDVAHWLGCSA-TSTFnfhpnvRPVPL-ELHIQGFNISHTQTRLLSmAKP 1545
Cdd:COG1204 159 EVLLARLR----RLNPEAQIVALSATIGNAEEIAEWLDAELvKSDW------RPVPLnEGVLYDGVLRFDDGSRRS-KDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1546 VYHAITKHSPK-KPVIVFVPSRKQTRLTA---IDILTTCAADIQRQRFLHCTEKdLIPYLEKLS-DSTLKETLLNGVGYL 1620
Cdd:COG1204 228 TLALALDLLEEgGQVLVFVSSRRDAESLAkklADELKRRLTPEEREELEELAEE-LLEVSEETHtNEKLADCLEKGVAFH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1621 HEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAAHLVIIMDTQYYNGkihayVDYPIYDVLQMVGHANRPLQDDEG 1700
Cdd:COG1204 307 HAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1701 RCVIMCQGSK--KDFFKKFLY-EPLPVESHL--DHCMHDHFNAEIVTKTIENKQDAVDYLTWTFLYrrmtqnpnyynlqg 1775
Cdd:COG1204 382 EAILVAKSSDeaDELFERYILgEPEPIRSKLanESALRTHLLALIASGFANSREELLDFLENTFYA-------------- 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40217847 1776 isHRHLSDHLSELVEQTLSDLEQSKCISIEDEMdVAPLNLGMIAAYYYINYTTIELFSMSLNAKTK---VRGLIEII 1849
Cdd:COG1204 448 --YQYDKGDLEEVVDDALEFLLENGFIEEDGDR-LRATKLGKLVSRLYIDPLTAAELVDGLRKADEeftDLGLLHLI 521
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
681-871 |
1.21e-67 |
|
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: 225.12 E-value: 1.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 681 RPVPLEQTYVGITEKKAIKRFQIMNE-----IVYEKIMEHAGKNQVLVFVHSRKETGKTARAIRdmclekdtlglflreg 755
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 756 sastevlrteaeqcknlelkdllpyGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIKGTQVYS 835
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 40217847 836 PEkgRWTELGALDILQMLGRAGRPQYDTKGEGILIT 871
Cdd:cd18795 120 GK--GYRELSPLEYLQMIGRAGRPGFDTRGEAIIMT 153
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
1327-1515 |
1.26e-67 |
|
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: 225.99 E-value: 1.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1327 FFNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQsSEGRCVYITPMEALAEQVYMDWYEKFQdRLNKKVV 1406
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALAT-SGGKAVYIAPTRALVNQKEADLRERFG-PLGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1407 LLTGETSTDLKLLGKGNIIISTPEKWDILSRRWKQRkNVQNINLFVVDEVHLIG-GENGPVLEVICSRMRYissqIERPI 1485
Cdd:cd17921 79 LLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLR----INKNA 153
|
170 180 190
....*....|....*....|....*....|
gi 40217847 1486 RIVALSSSLSNAKDVAHWLGCsaTSTFNFH 1515
Cdd:cd17921 154 RFVGLSATLPNAEDLAEWLGV--EDLIRFD 181
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
1328-1520 |
5.99e-63 |
|
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: 213.76 E-value: 5.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1328 FNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEG-----RCVYITPMEALAEQVYMDWYEKFqDRLN 1402
Cdd:cd18023 2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLpwgnrKVVYIAPIKALCSEKYDDWKEKF-GPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1403 KKVVLLTGETST-DLKLLGKGNIIISTPEKWDILSRRWKQRKN-VQNINLFVVDEVHLIGGENGPVLEVICSRMRYISSQ 1480
Cdd:cd18023 81 LSCAELTGDTEMdDTFEIQDADIILTTPEKWDSMTRRWRDNGNlVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSSS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 40217847 1481 IE------RPIRIVALSSSLSNAKDVAHWLGCSATSTFNFHPNVRP 1520
Cdd:cd18023 161 SElrgstvRPMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
480-677 |
1.35e-62 |
|
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: 211.74 E-value: 1.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 480 TLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREIGKHINmdgtinvddfKIIYIAPMRSLVQEMVGSFGKRL 559
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGG----------KAVYIAPTRALVNQKEADLRERF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 560 ATYGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGGERtYTQLVRLIILDEIHLLHD-DRGPVLEALVARAIRN 638
Cdd:cd17921 71 GPLGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDgERGVVLELLLSRLLRI 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 40217847 639 iemtQEDVRLIGLSATLPNYEDVATFLRVdpaKGLFYFD 677
Cdd:cd17921 150 ----NKNARFVGLSATLPNAEDLAEWLGV---EDLIRFD 181
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
482-682 |
5.02e-56 |
|
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: 194.11 E-value: 5.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 482 NRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREIgKHINMDGTINVddfKIIYIAPMRSLVQEMVGSFGKRLAT 561
Cdd:cd18023 3 NRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLL-KERNPLPWGNR---KVVYIAPIKALCSEKYDDWKEKFGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 562 YGITVAELTGDHQLCK-EEISATQIIVCTPEKWDIITRKGGER-TYTQLVRLIILDEIHLLHDDRGPVLEALVARaIRNI 639
Cdd:cd18023 79 LGLSCAELTGDTEMDDtFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIKENRGATLEVVVSR-MKTL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 40217847 640 EMTQE-------DVRLIGLSATLPNYEDVATFLRVDPAkGLFYFDNSFRP 682
Cdd:cd18023 158 SSSSElrgstvrPMRFVAVSATIPNIEDLAEWLGDNPA-GCFSFGESFRP 206
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1310-1897 |
1.21e-55 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 208.52 E-value: 1.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1310 SALRNSAFESLYqdkfpffnPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSeGRCVYITPMEALAEQV 1389
Cdd:PRK00254 14 RVLKERGIEELY--------PPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREG-GKAVYLVPLKALAEEK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1390 YMDWyeKFQDRLNKKVVLLTGETSTDLKLLGKGNIIISTPEKWDILSR---RWkqrknVQNINLFVVDEVHLIGG-ENGP 1465
Cdd:PRK00254 85 YREF--KDWEKLGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSyDRGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1466 VLEVICSRMryissqIERPiRIVALSSSLSNAKDVAHWLGCSATSTfnfhpNVRPVPLELHI--QGFNI---SHTQTRLL 1540
Cdd:PRK00254 158 TLEMILTHM------LGRA-QILGLSATVGNAEELAEWLNAELVVS-----DWRPVKLRKGVfyQGFLFwedGKIERFPN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1541 SMAKPVYHAITKhspKKPVIVFVPSRKQTRLTAIDIlttcAADIQRqrflHCTEKDLIPyLEKLSDS--------TLKET 1612
Cdd:PRK00254 226 SWESLVYDAVKK---GKGALVFVNTRRSAEKEALEL----AKKIKR----FLTKPELRA-LKELADSleenptneKLKKA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1613 LLNGVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAAHLVIIMDTQYYNGkiHAYVDYPIYDVLQMVGHAN 1692
Cdd:PRK00254 294 LRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSN--FGWEDIPVLEIQQMMGRAG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1693 RPLQDDEGRCVIMCQGSK-KDFFKKFLY-EPLPVESHL--DHCMHDHFNAEIVTKTIENKQDAVDYLTWTFLYRrmtQNP 1768
Cdd:PRK00254 372 RPKYDEVGEAIIVATTEEpSKLMERYIFgKPEKLFSMLsnESAFRSQVLALITNFGVSNFKELVNFLERTFYAH---QRK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1769 NYYNLQGishrHLSDHLSELVEQTLSDleqskcISIEDEmdVAPLNLGMIAAYYYINYTTIELFSMSLNAKTK---VRGL 1845
Cdd:PRK00254 449 DLYSLEE----KAKEIVYFLLENEFID------IDLEDR--FIPLPLGIRTSQLYIDPLTAKKFKDAFPKIEKnpnPLGI 516
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40217847 1846 IEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLnnpKFNDPH------------VKTNLLLQA 1897
Cdd:PRK00254 517 FQLIASTPDMTPLNYSRKEMEDLLDEAYEMEDRL---YFNIPYwedykfqkflraFKTAKVLLD 577
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
477-1033 |
1.68e-50 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 192.72 E-value: 1.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 477 GFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCM----LREIGKhinmdgtinvddfkIIYIAPMRSLVQEMV 552
Cdd:PRK00254 20 GIEELYPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMvnklLREGGK--------------AVYLVPLKALAEEKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 553 GSFgKRLATYGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGGerTYTQLVRLIILDEIHLLHD-DRGPVLEAL 631
Cdd:PRK00254 86 REF-KDWEKLGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRHGS--SWIKDVKLVVADEIHLIGSyDRGATLEMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 632 VARAIrniemtqEDVRLIGLSATLPNYEDVATFLRVDPAKglfyfdNSFRPVPLEQT--YVG--ITEKKAIKRFQIM-NE 706
Cdd:PRK00254 163 LTHML-------GRAQILGLSATVGNAEELAEWLNAELVV------SDWRPVKLRKGvfYQGflFWEDGKIERFPNSwES 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 707 IVYEKIMEhagKNQVLVFVHSRKETGKTA----RAIRDMCLEKDTLGLflREGSASTEvlrteaEQCKNLELKDLLPYGF 782
Cdd:PRK00254 230 LVYDAVKK---GKGALVFVNTRRSAEKEAlelaKKIKRFLTKPELRAL--KELADSLE------ENPTNEKLKKALRGGV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 783 AIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIKGTQVYSpEKGrWTELGALDILQMLGRAGRPQYD 862
Cdd:PRK00254 299 AFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYS-NFG-WEDIPVLEIQQMMGRAGRPKYD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 863 TKGEGILITSHGE----LQYYL----SLLNQQLPIESQMVSKLPdmlnAEIVLGNVQNAKDAVNWLgyaylyirmlrSPT 934
Cdd:PRK00254 377 EVGEAIIVATTEEpsklMERYIfgkpEKLFSMLSNESAFRSQVL----ALITNFGVSNFKELVNFL-----------ERT 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 935 LYGISHDDLKgdpLLDQRRLDLVHtaalMLDKNNLVKYDKKTgNFQVTELGRIASHYYITNDTVQTYnqllKPTLSEIE- 1013
Cdd:PRK00254 442 FYAHQRKDLY---SLEEKAKEIVY----FLLENEFIDIDLED-RFIPLPLGIRTSQLYIDPLTAKKF----KDAFPKIEk 509
|
570 580
....*....|....*....|....*.
gi 40217847 1014 ------LFRVFSLSSEFKNITVREEE 1033
Cdd:PRK00254 510 npnplgIFQLIASTPDMTPLNYSRKE 535
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
482-677 |
4.07e-49 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350780 [Multi-domain] Cd Length: 189 Bit Score: 173.33 E-value: 4.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 482 NRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREIGKHINMdgtinvddfKIIYIAPMRSLVQEMVGSFGKRLAT 561
Cdd:cd18022 3 NPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGS---------KVVYIAPLKALVRERVDDWKKRFEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 562 -YGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGGERTYTQLVRLIILDEIHLLHDDRGPVLEALVARAIRNIE 640
Cdd:cd18022 74 kLGKKVVELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISS 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 40217847 641 MTQEDVRLIGLSATLPNYEDVATFLRVdPAKGLFYFD 677
Cdd:cd18022 154 QTEKPVRLVGLSTALANAGDLANWLGI-KKMGLFNFR 189
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
493-1069 |
5.07e-49 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 187.40 E-value: 5.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 493 LETDENLLLCAPTGAGKTNVALMCMLREIGKHInmdgtinvddfKIIYIAPMRSLVQEMVGSFgKRLATYGITVAELTGD 572
Cdd:PRK01172 34 LRKGENVIVSVPTAAGKTLIAYSAIYETFLAGL-----------KSIYIVPLRSLAMEKYEEL-SRLRSLGMRVKISIGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 573 HQLCKEEISATQIIVCTPEKWDIITRKggERTYTQLVRLIILDEIHLLHD-DRGPVLEAlVARAIRNIemtQEDVRLIGL 651
Cdd:PRK01172 102 YDDPPDFIKRYDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDeDRGPTLET-VLSSARYV---NPDARILAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 652 SATLPNYEDVATFLRVDPAKglfyfdNSFRPVPLEqtyVGITEKKAI-----KRFQIMNEIVYEKIMEHAGknQVLVFVH 726
Cdd:PRK01172 176 SATVSNANELAQWLNASLIK------SNFRPVPLK---LGILYRKRLildgyERSQVDINSLIKETVNDGG--QVLVFVS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 727 SRKETGKTARAIRDMCLEKDTLGLFLREGSASTEVLrteaeqcknlelKDLLPYGFAIHHAGMTRVDRTLVEDLFADKHI 806
Cdd:PRK01172 245 SRKNAEDYAEMLIQHFPEFNDFKVSSENNNVYDDSL------------NEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 807 QVLVSTATLAWGVNLPAHTVIIKGTQVYSpeKGRWTELGALDILQMLGRAGRPQYDTKGEGILI----TSHGELQYYLSl 882
Cdd:PRK01172 313 KVIVATPTLAAGVNLPARLVIVRDITRYG--NGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYIYaaspASYDAAKKYLS- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 883 lNQQLPIESQMVSKLPDMLN--AEIVLGNVQNAKDavnwlgyaylyIRMLRSPTLYGIShddlKGDPLLDQRrldlVHTA 960
Cdd:PRK01172 390 -GEPEPVISYMGSQRKVRFNtlAAISMGLASSMED-----------LILFYNETLMAIQ----NGVDEIDYY----IESS 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 961 ALMLDKNNLVKYDKktgNFQVTELGRIASHYYITNDTVQTYNQLLKPTLSEIELFRVFSLSSEFKNITVREEEKLElqKL 1040
Cdd:PRK01172 450 LKFLKENGFIKGDV---TLRATRLGKLTSDLYIDPESALILKSAFDHDYDEDLALYYISLCREIIPANTRDDYYAM--EF 524
|
570 580
....*....|....*....|....*....
gi 40217847 1041 LERVPIpVKESIEepSAKINVLLQAFISQ 1069
Cdd:PRK01172 525 LEDIGV-IDGDIS--AAKTAMVLRGWISE 550
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
497-877 |
1.51e-48 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 187.09 E-value: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 497 ENLLLCAPTGAGKTNVALMCMLREIGKhinmDGtinvddfKIIYIAPMRSLVQEMVGSFgKRLATYGITVAELTGDHQLC 576
Cdd:PRK02362 40 KNLLAAIPTASGKTLIAELAMLKAIAR----GG-------KALYIVPLRALASEKFEEF-ERFEELGVRVGISTGDYDSR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 577 KEEISATQIIVCTPEKWDIITRKGGerTYTQLVRLIILDEIHLLHD-DRGPVLEALVARAIRniemTQEDVRLIGLSATL 655
Cdd:PRK02362 108 DEWLGDNDIIVATSEKVDSLLRNGA--PWLDDITCVVVDEVHLIDSaNRGPTLEVTLAKLRR----LNPDLQVVALSATI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 656 PNYEDVATFLR----------VDPAKGLFY-----FDNSFRPVPLEQTYvgitekkaikrfQIMNeIVYEKIMEHAgknQ 720
Cdd:PRK02362 182 GNADELADWLDaelvdsewrpIDLREGVFYggaihFDDSQREVEVPSKD------------DTLN-LVLDTLEEGG---Q 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 721 VLVFVHSRKET----GKTARAIrdmcleKDTLGLFLREGSA--STEVLRT-EAEQCKNLelKDLLPYGFAIHHAGMTRVD 793
Cdd:PRK02362 246 CLVFVSSRRNAegfaKRAASAL------KKTLTAAERAELAelAEEIREVsDTETSKDL--ADCVAKGAAFHHAGLSREH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 794 RTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIKGTQVYSPEKGRwTELGALDILQMLGRAGRPQYDTKGEGILIT-S 872
Cdd:PRK02362 318 RELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAGM-QPIPVLEYHQMAGRAGRPGLDPYGEAVLLAkS 396
|
....*
gi 40217847 873 HGELQ 877
Cdd:PRK02362 397 YDELD 401
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1519-1707 |
2.22e-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: 166.96 E-value: 2.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1519 RPVPLELHIQGFNISHTQTRLLSMAK-----PVYHAITKHSPKKPVIVFVPSRKQTRLTAIDILttcaadiqrqrflhct 1593
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1594 ekdlipyleklsdstlketllnGVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAAHLVIIMDTQYYNGKi 1673
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGK- 121
|
170 180 190
....*....|....*....|....*....|....
gi 40217847 1674 hAYVDYPIYDVLQMVGHANRPLQDDEGRCVIMCQ 1707
Cdd:cd18795 122 -GYRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
254-363 |
2.30e-46 |
|
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: 162.39 E-value: 2.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 254 KKKDLHPRDIDAFWLQRQLSRFYDDAIVSQKKADEVLEILKTASDD-RECENQLVLLLGFNTFDFIKVLRQHRMMILYCT 332
Cdd:pfam18149 1 DKDSLDPHDIDAFWLQRLLSKFYGDAIEAQKKAEEVLDILESAADDlRECENQLVELLDYDKFDLVKLLLKNRDKIVWCT 80
|
90 100 110
....*....|....*....|....*....|.
gi 40217847 333 LLASAQSEAEKERIMGKMEADPELSKFLYQL 363
Cdd:pfam18149 81 KLARAQSEEEKQAIEEEMRSNPGLAWILDEL 111
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
491-893 |
7.53e-45 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 175.90 E-value: 7.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 491 AALETDENLLLCAPTGAGKTNVA---LMCMLREiGKhinmdgtinvddfKIIYIAPMRSLV----QEMVGSFGkrlatyG 563
Cdd:COG4581 35 LALEAGRSVLVAAPTGSGKTLVAefaIFLALAR-GR-------------RSFYTAPIKALSnqkfFDLVERFG------A 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 564 ITVAELTGDhqlckEEISAT-QIIVCTPEkwdiITRKGGERTYTQLVRL--IILDEIHLLHD-DRGPVLEAlvarAIrnI 639
Cdd:COG4581 95 ENVGLLTGD-----ASVNPDaPIVVMTTE----ILRNMLYREGADLEDVgvVVMDEFHYLADpDRGWVWEE----PI--I 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 640 EMTqEDVRLIGLSATLPNYEDVATFLR--------VDpakglfyfdNSFRPVPLEQTYV-------GITEKKAIKRFQIM 704
Cdd:COG4581 160 HLP-ARVQLVLLSATVGNAEEFAEWLTrvrgetavVV---------SEERPVPLEFHYLvtprlfpLFRVNPELLRPPSR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 705 NEIVyeKIMEHAGKNQVLVFVHSRKETGKTARAIRDMCL----EKDTLGLFLREGSASTEVLRTEaeqcknlELKDLLPY 780
Cdd:COG4581 230 HEVI--EELDRGGLLPAIVFIFSRRGCDEAAQQLLSARLttkeERAEIREAIDEFAEDFSVLFGK-------TLSRLLRR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 781 GFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIKGTQVYSPEKGRwtELGALDILQMLGRAGRPQ 860
Cdd:COG4581 301 GIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHR--PLTAREFHQIAGRAGRRG 378
|
410 420 430
....*....|....*....|....*....|....*
gi 40217847 861 YDTKGE-GILITSHGELQYYLSLLNQQL-PIESQM 893
Cdd:COG4581 379 IDTEGHvVVLAPEHDDPKKFARLASARPePLRSSF 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 ... |
478-677 |
5.31e-39 |
|
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: 144.71 E-value: 5.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 478 FKTLNRIQSKLYRAALETDENLLLCAPTGAGKT---NVALMCMLREIGKHinmdgtinvddfKIIYIAPMRSLVQEMV-- 552
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTvcaELALLRHWRQNPKG------------RAVYIAPMQELVDARYkd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 553 --GSFGKRLatyGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGGERTYTQLVRLIILDEIHLLHDDRGPVLEA 630
Cdd:cd18021 69 wrAKFGPLL---GKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 40217847 631 LVARaIRNIE-MTQEDVRLIGLSATLPNYEDVATFLRVDPAkGLFYFD 677
Cdd:cd18021 146 VVSR-MRYISsQLEKPIRIVGLSSSLANARDVGEWLGASKS-TIFNFH 191
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1302-1895 |
2.08e-38 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 155.89 E-value: 2.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1302 LDLQPLPVSALRNSAFESLYqdkfpffnPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSseGRCVYITP 1381
Cdd:PRK02362 6 LPLPEGVIEFYEAEGIEELY--------PPQAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIARG--GKALYIVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1382 MEALAEqvymdwyEKFQDRLNK-----KVVLLTGETSTDLKLLGKGNIIISTPEKWDILSR---RWkqrknVQNINLFVV 1453
Cdd:PRK02362 76 LRALAS-------EKFEEFERFeelgvRVGISTGDYDSRDEWLGDNDIIVATSEKVDSLLRngaPW-----LDDITCVVV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1454 DEVHLIGGEN-GPVLEVICSRMRYISSQIErpirIVALSSSLSNAKDVAHWLGCS-ATSTFnfhpnvRPVplELHI---- 1527
Cdd:PRK02362 144 DEVHLIDSANrGPTLEVTLAKLRRLNPDLQ----VVALSATIGNADELADWLDAElVDSEW------RPI--DLREgvfy 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1528 -QGFNISHTQTRLlsmakpvyhaitKHSPKKPV--------------IVFVPSRK-------------QTRLTAID--IL 1577
Cdd:PRK02362 212 gGAIHFDDSQREV------------EVPSKDDTlnlvldtleeggqcLVFVSSRRnaegfakraasalKKTLTAAEraEL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1578 TTCAADIQRQRflhctekdlipylEKLSDSTLKETLLNGVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVA 1657
Cdd:PRK02362 280 AELAEEIREVS-------------DTETSKDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1658 AHLVIIMDTQYYNGkihayvDY-----PIYDVLQMVGHANRPLQDDEGRCVIMC--QGSKKDFFKKFLY-EPLPVESHL- 1728
Cdd:PRK02362 347 ARRVIIRDYRRYDG------GAgmqpiPVLEYHQMAGRAGRPGLDPYGEAVLLAksYDELDELFERYIWaDPEDVRSKLa 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1729 -DHCMHDHFNAEIVTKTIENKQDAVDYLTWTFlYRRMTQNPNYynlqgishrhlsdhLSELVEQTLSDLEQSKCIsIEDE 1807
Cdd:PRK02362 421 tEPALRTHVLSTIASGFARTRDGLLEFLEATF-YATQTDDTGR--------------LERVVDDVLDFLERNGMI-EEDG 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1808 MDVAPLNLGMIAAYYYINYTTIELFSMSLNAKTKV--RGLIEIISN----------AAEYENIP--IRHHEDNLLrqlaQ 1873
Cdd:PRK02362 485 ETLEATELGHLVSRLYIDPLSAAEIIDGLEAAKKPtdLGLLHLVCStpdmyelylrSGDYEWLNeyLYEHEDELL----G 560
|
650 660
....*....|....*....|....
gi 40217847 1874 KVPHKLNNPKFND--PHVKTNLLL 1895
Cdd:PRK02362 561 DVPSEFEDDEFEDflSAVKTALLL 584
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1345-1761 |
4.60e-38 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 153.89 E-value: 4.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1345 NVFVGAPTGSGKTICAEFAILRMLLQSSegRCVYITPMEALAeqvyMDWYEKFQD--RLNKKVVLLTGETSTDLKLLGKG 1422
Cdd:PRK01172 39 NVIVSVPTAAGKTLIAYSAIYETFLAGL--KSIYIVPLRSLA----MEKYEELSRlrSLGMRVKISIGDYDDPPDFIKRY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1423 NIIISTPEKWDILSRRwkQRKNVQNINLFVVDEVHLIGGEN-GPVLEVICSRMRYISSQIerpiRIVALSSSLSNAKDVA 1501
Cdd:PRK01172 113 DVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDEDrGPTLETVLSSARYVNPDA----RILALSATVSNANELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1502 HWLGCSATSTfnfhpNVRPVPLELHIQGFN------ISHTQTRLLSMAKPVYhaitkhSPKKPVIVFVPSRKQTRLTAID 1575
Cdd:PRK01172 187 QWLNASLIKS-----NFRPVPLKLGILYRKrlildgYERSQVDINSLIKETV------NDGGQVLVFVSSRKNAEDYAEM 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1576 ILttcaadiqrQRFLHCTEKDLIPYLEKLSDSTLKETLLNGVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMN 1655
Cdd:PRK01172 256 LI---------QHFPEFNDFKVSSENNNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1656 VAAHLVIIMD-TQYYNGKIHAYVDypiYDVLQMVGHANRPLQDDEGRCVI-MCQGSKKDFFKKFLY-EPLPVESHLDHCM 1732
Cdd:PRK01172 327 LPARLVIVRDiTRYGNGGIRYLSN---MEIKQMIGRAGRPGYDQYGIGYIyAASPASYDAAKKYLSgEPEPVISYMGSQR 403
|
410 420 430
....*....|....*....|....*....|.
gi 40217847 1733 HDHFN--AEIVTKTIENKQDAVDYLTWTFLY 1761
Cdd:PRK01172 404 KVRFNtlAAISMGLASSMEDLILFYNETLMA 434
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1341-1727 |
7.79e-37 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 151.25 E-value: 7.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1341 NSDDNVFVGAPTGSGKTICAEFAILRMLLQSseGRCVYITPMEALAEQVYMDwyekFQDRLNK-KVVLLTGETStdlkLL 1419
Cdd:COG4581 38 EAGRSVLVAAPTGSGKTLVAEFAIFLALARG--RRSFYTAPIKALSNQKFFD----LVERFGAeNVGLLTGDAS----VN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1420 GKGNIIISTPEkwdILSrrwkqrknvqNINL----------FVV-DEVHLIG-GENGPVLEVIcsrmryIssqIERP--I 1485
Cdd:COG4581 108 PDAPIVVMTTE---ILR----------NMLYregadledvgVVVmDEFHYLAdPDRGWVWEEP------I---IHLParV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1486 RIVALSSSLSNAKDVAHWL----GCSA--TSTFnfhpnvRPVPLELH-------IQGFNISHTQTRLLSMAKPVYHAITK 1552
Cdd:COG4581 166 QLVLLSATVGNAEEFAEWLtrvrGETAvvVSEE------RPVPLEFHylvtprlFPLFRVNPELLRPPSRHEVIEELDRG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1553 HspKKPVIVFVPSRKQ-----TRLTAIDILTTCAADIQRQRFLhctekDLIPYLEKLSDSTLKETLLNGVGYLHEGLSPM 1627
Cdd:COG4581 240 G--LLPAIVFIFSRRGcdeaaQQLLSARLTTKEERAEIREAID-----EFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1628 ERRLVEQLFSSGAIQVVVASRSLCWGMNVAAHLVIIMDTQYYNGKIHAYVDyPIyDVLQMVGHANRPLQDDEGRCVImcQ 1707
Cdd:COG4581 313 YRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLT-AR-EFHQIAGRAGRRGIDTEGHVVV--L 388
|
410 420
....*....|....*....|....
gi 40217847 1708 GSKKDFFKKFLY----EPLPVESH 1727
Cdd:COG4581 389 APEHDDPKKFARlasaRPEPLRSS 412
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
1322-1504 |
5.41e-36 |
|
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: 136.73 E-value: 5.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1322 QDKFPFF---NPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRML---------LQSSEGRCVYITPMEAL-AEQ 1388
Cdd:cd18019 9 QPAFEGFkslNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIgkhrnpdgtINLDAFKIVYIAPMKALvQEM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1389 VymdwyEKFQDRL---NKKVVLLTGETSTDLKLLGKGNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVHLIGGENGP 1465
Cdd:cd18019 89 V-----GNFSKRLapyGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDDRGP 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 40217847 1466 VLEVICSRMRYISSQIERPIRIVALSSSLSNAKDVAHWL 1504
Cdd:cd18019 164 VLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFL 202
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1329-1514 |
9.81e-35 |
|
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: 132.55 E-value: 9.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1329 NPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRML---------LQSSEGRCVYITPMEALAEQVymdwYEKFQD 1399
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIrqhvnqggvIKKDDFKIVYIAPMKALAAEM----VEKFSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1400 RL---NKKVVLLTGETSTDLKLLGKGNIIISTPEKWDILSRRWKQRKN-VQNINLFVVDEVHLIGGENGPVLEVICSRMR 1475
Cdd:cd18020 79 RLaplGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVAlSQLVRLLIIDEVHLLHDDRGPVIESLVARTL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 40217847 1476 YISSQIERPIRIVALSSSLSNAKDVAHWLGCS-ATSTFNF 1514
Cdd:cd18020 159 RQVESTQSMIRIVGLSATLPNYLDVADFLRVNpYKGLFFF 198
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
1328-1505 |
1.17e-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: 131.69 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1328 FNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSseGRCVYITPMEALAEQVymdwYEKFQD--RLNKKV 1405
Cdd:cd18028 2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEG--GKALYLVPLRALASEK----YEEFKKleEIGLKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1406 VLLTGETSTDLKLLGKGNIIISTPEKWDILsrrWKQRKN-VQNINLFVVDEVHLIGGEN-GPVLEVICSRMRYISSQier 1483
Cdd:cd18028 76 GISTGDYDEDDEWLGDYDIIVATYEKFDSL---LRHSPSwLRDVGVVVVDEIHLISDEErGPTLESIVARLRRLNPN--- 149
|
170 180
....*....|....*....|..
gi 40217847 1484 pIRIVALSSSLSNAKDVAHWLG 1505
Cdd:cd18028 150 -TQIIGLSATIGNPDELAEWLN 170
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
480-665 |
4.84e-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: 129.76 E-value: 4.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 480 TLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREIgkhinMDGTinvddfKIIYIAPMRSLVQEMVGSFgKRL 559
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTL-----LEGG------KALYLVPLRALASEKYEEF-KKL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 560 ATYGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGgeRTYTQLVRLIILDEIHLLHD-DRGPVLEALVARairn 638
Cdd:cd18028 69 EEIGLKVGISTGDYDEDDEWLGDYDIIVATYEKFDSLLRHS--PSWLRDVGVVVVDEIHLISDeERGPTLESIVAR---- 142
|
170 180
....*....|....*....|....*..
gi 40217847 639 IEMTQEDVRLIGLSATLPNYEDVATFL 665
Cdd:cd18028 143 LRRLNPNTQIIGLSATIGNPDELAEWL 169
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1329-1500 |
3.55e-33 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 126.97 E-value: 3.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1329 NPIQTQVFNTVYnSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEG-RCVYITPMEALAEQVYMDWYEKFQDRLNKKVVL 1407
Cdd:pfam00270 1 TPIQAEAIPAIL-EGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGpQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1408 LTG-ETSTDLKLLGKGNIIISTPEKWDILSRrwkQRKNVQNINLFVVDEVHLIGGEN-GPVLEVICSRMRYissqierPI 1485
Cdd:pfam00270 80 LGGdSRKEQLEKLKGPDILVGTPGRLLDLLQ---ERKLLKNLKLLVLDEAHRLLDMGfGPDLEEILRRLPK-------KR 149
|
170
....*....|....*.
gi 40217847 1486 RIVALSSSLS-NAKDV 1500
Cdd:pfam00270 150 QILLLSATLPrNLEDL 165
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
482-661 |
6.86e-33 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 126.20 E-value: 6.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 482 NRIQSKLYRAALEtDENLLLCAPTGAGKTNVALMCMLREIGKhinmdgtiNVDDFKIIYIAPMRSLVQEMVGSFGKRLAT 561
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK--------LDNGPQALVLAPTRELAEQIYEELKKLGKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 562 YGITVAELTGDH--QLCKEEISATQIIVCTPEKWDIITRkggERTYTQLVRLIILDEIHLLHD-DRGPVLEALvarairn 638
Cdd:pfam00270 72 LGLKVASLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQ---ERKLLKNLKLLVLDEAHRLLDmGFGPDLEEI------- 141
|
170 180
....*....|....*....|....
gi 40217847 639 IEMTQEDVRLIGLSATLP-NYEDV 661
Cdd:pfam00270 142 LRRLPKKRQILLLSATLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1320-1508 |
1.33e-29 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 117.98 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1320 LYQDKFPFFNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEQVYMDWYEKFQD 1399
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1400 RLNKKVVLLTGETSTDLK---LLGKGNIIISTPEKWDILSRRWKqrKNVQNINLFVVDEVH-LIGGENGPVLEVICSRMR 1475
Cdd:smart00487 81 LGLKVVGLYGGDSKREQLrklESGKTDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP 158
|
170 180 190
....*....|....*....|....*....|...
gi 40217847 1476 yissqieRPIRIVALSSSLSNAKDVAHWLGCSA 1508
Cdd:smart00487 159 -------KNVQLLLLSATPPEEIENLLELFLND 184
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
462-682 |
4.59e-28 |
|
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: 113.46 E-value: 4.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 462 LPVEKLPKYAQAGFegfktlnriqSKLY--------RAALETDENLLLCAPTGAGKTNVALMCMLREI---GKhinmdgt 530
Cdd:cd18026 1 LPDAVREAYAKKGI----------KKLYdwqkeclsLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRLlerRK------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 531 invddfKIIYIAPMRSLVQEMVGSFGKRLATYGITVAELTGdhqlCKEEI-----SATQIIVCTPEKWDIITRKGGERTY 605
Cdd:cd18026 64 ------KALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAG----NKGRSppkrrKSLSVAVCTIEKANSLVNSLIEEGR 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40217847 606 TQLVRLIILDEIHLLHD-DRGPVLEALVARAIRnieMTQEDVRLIGLSATLPNYEDVATFLRVDpakglfYFDNSFRP 682
Cdd:cd18026 134 LDELGLVVVDELHMLGDgHRGALLELLLTKLLY---AAQKNIQIVGMSATLPNLEELASWLRAE------LYTTNFRP 202
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
477-684 |
8.82e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.81 E-value: 8.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 477 GFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREIGKHinmdgtinvDDFKIIYIAPMRSLVQEMVGSFG 556
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRG---------KGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 557 KRLA-TYGITVAELTGD---HQLCKEEISATQIIVCTPEKWDIITRKGgeRTYTQLVRLIILDEIHLLHD-DRGPVLEAL 631
Cdd:smart00487 76 KLGPsLGLKVVGLYGGDskrEQLRKLESGKTDILVTTPGRLLDLLEND--KLSLSNVDLVILDEAHRLLDgGFGDQLEKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 40217847 632 VARAIRNiemtqedVRLIGLSATLPNYEDVATFLRVdpaKGLFYFDNSFRPVP 684
Cdd:smart00487 154 LKLLPKN-------VQLLLLSATPPEEIENLLELFL---NDPVFIDVGFTPLE 196
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
496-665 |
2.97e-23 |
|
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: 98.42 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 496 DENLLLCAPTGAGKTNVALMCMLREIGKHinmdgtiNVDDFKIIYIAPMRSLVQEMVgsfgKRLATY------GITVAEL 569
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADE-------PEKGVQVLYISPLKALINDQE----RRLEEPldeidlEIPVAVR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 570 TGDhqlckeeISATQ----------IIVCTPEKWDII-TRKGGERTYTQLvRLIILDEIH-LLHDDRGPVLEALVARaIR 637
Cdd:cd17922 70 HGD-------TSQSEkakqlknppgILITTPESLELLlVNKKLRELFAGL-RYVVVDEIHaLLGSKRGVQLELLLER-LR 140
|
170 180
....*....|....*....|....*...
gi 40217847 638 niEMTQEDVRLIGLSATLPNYEDVATFL 665
Cdd:cd17922 141 --KLTGRPLRRIGLSATLGNLEEAAAFL 166
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
458-865 |
3.39e-23 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 107.67 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 458 EEQLLPVEKL---PKYAQAGFEGFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCmlrEIGKHINMDGtinvd 534
Cdd:COG1202 184 EVDTVPVDDLdlpPELKDLLEGRGEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELA---GIKNALEGKG----- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 535 dfKIIYIAPMRSLVQEMVGSFGKRlatY--GITVAELTGDHQLC---KEEISATQIIVCTPEKWDIITRKGgeRTYTQlV 609
Cdd:COG1202 256 --KMLFLVPLVALANQKYEDFKDR---YgdGLDVSIRVGASRIRddgTRFDPNADIIVGTYEGIDHALRTG--RDLGD-I 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 610 RLIILDEIHLLHD-DRGPVLEALVARaIRNIemtQEDVRLIGLSATLPNYEDVATFLRvdpAKgLFYFDNsfRPVPLEQt 688
Cdd:COG1202 328 GTVVIDEVHMLEDpERGHRLDGLIAR-LKYY---CPGAQWIYLSATVGNPEELAKKLG---AK-LVEYEE--RPVPLER- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 689 YVGITEKKAIKRfqIMNEIV---YEKIMEHAGKNQVLVFVHSRKETGKTARAirdmclekdtlglflregsastevlrte 765
Cdd:COG1202 397 HLTFADGREKIR--IINKLVkreFDTKSSKGYRGQTIIFTNSRRRCHEIARA---------------------------- 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 766 aeqcknlelkdlLPYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVI-------IKgtqvyspek 838
Cdd:COG1202 447 ------------LGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIfdslamgIE--------- 505
|
410 420
....*....|....*....|....*..
gi 40217847 839 grWteLGALDILQMLGRAGRPQYDTKG 865
Cdd:COG1202 506 --W--LSVQEFHQMLGRAGRPDYHDRG 528
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
1343-1504 |
7.21e-19 |
|
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: 85.71 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1343 DDNVFVGAPTGSGKTICAEFAILRMLLQSSE--GRCVYITPMEALAEQVYM---DWYEKFQdrLNKKVVLLTGETSTDLK 1417
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEkgVQVLYISPLKALINDQERrleEPLDEID--LEIPVAVRHGDTSQSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1418 --LLGK-GNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVH-LIGGENGPVLEVICSRMRYIssqIERPIRIVALSSS 1493
Cdd:cd17922 79 akQLKNpPGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHaLLGSKRGVQLELLLERLRKL---TGRPLRRIGLSAT 155
|
170
....*....|.
gi 40217847 1494 LSNAKDVAHWL 1504
Cdd:cd17922 156 LGNLEEAAAFL 166
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1344-1705 |
7.95e-19 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 93.42 E-value: 7.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1344 DNVFVGAPTGSGKTICAEFAILRMLLQSsEGRCVYITPMEALAEQVYmdwyEKFQDRLNK--KVVLLTG-------ETST 1414
Cdd:COG1202 226 KDQLVVSATATGKTLIGELAGIKNALEG-KGKMLFLVPLVALANQKY----EDFKDRYGDglDVSIRVGasrirddGTRF 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1415 DLKllgkGNIIISTPEKWDILSRRwkqRKNVQNINLFVVDEVHLIG-GENGPVLEVICSRMRYISSQIErpirIVALSSS 1493
Cdd:COG1202 301 DPN----ADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEVHMLEdPERGHRLDGLIARLKYYCPGAQ----WIYLSAT 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1494 LSNAKDVAHWLGCSATSTfnfhpNVRPVPLELHIQgFNISHTQTRLLS-MAKPVYHAITKHSPKKPVIVFVPSRKQTRLT 1572
Cdd:COG1202 370 VGNPEELAKKLGAKLVEY-----EERPVPLERHLT-FADGREKIRIINkLVKREFDTKSSKGYRGQTIIFTNSRRRCHEI 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1573 AidilttcaadiqrqRFLhctEKDLIPYleklsdstlketllngvgylHEGLSPMERRLVEQLFSSGAIQVVVASRSLCW 1652
Cdd:COG1202 444 A--------------RAL---GYKAAPY--------------------HAGLDYGERKKVERRFADQELAAVVTTAALAA 486
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1653 GmnvaahlviimdtqyyngkihayVDYP----IYDVL-------------QMVGHANRPLQDDEGRCVIM 1705
Cdd:COG1202 487 G-----------------------VDFPasqvIFDSLamgiewlsvqefhQMLGRAGRPDYHDRGKVYLL 533
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
1350-1516 |
4.21e-18 |
|
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: 84.57 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1350 APTGSGKTICAEFAILRMLLQssEGR-CVYITPMEALAEQvYMDWYEKFQDRLNKKVVLLTGETST-DLKLLGKGNIIIS 1427
Cdd:cd18026 40 LPTSGGKTLVAEILMLKRLLE--RRKkALFVLPYVSIVQE-KVDALSPLFEELGFRVEGYAGNKGRsPPKRRKSLSVAVC 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1428 TPEKWDILSRRWKQRKNVQNINLFVVDEVHLIG-GENGPVLEVICSRMRYISsqiERPIRIVALSSSLSNAKDVAHWLGC 1506
Cdd:cd18026 117 TIEKANSLVNSLIEEGRLDELGLVVVDELHMLGdGHRGALLELLLTKLLYAA---QKNIQIVGMSATLPNLEELASWLRA 193
|
170
....*....|
gi 40217847 1507 SATSTfNFHP 1516
Cdd:cd18026 194 ELYTT-NFRP 202
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
492-672 |
3.71e-17 |
|
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: 81.65 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 492 ALETDENLLLCAPTGAGKTNVALMCM---LREigkhinmdgtinVDDFKIIYIAPMRSLVQEMVGS----FGKRLATYGI 564
Cdd:cd18025 12 IVDRRESALIVAPTSSGKTFISYYCMekvLRE------------SDDGVVVYVAPTKALVNQVVAEvyarFSKKYPPSGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 565 TV-AELTGDHQLckEEISATQIIVCTPEKWDIITRKGGERTYTQLVRLIILDEIHLL-HDDRGPVLEALVARAirniemt 642
Cdd:cd18025 80 SLwGVFTRDYRH--NNPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIgQSEDGAVWEQLLLLI------- 150
|
170 180 190
....*....|....*....|....*....|.
gi 40217847 643 qeDVRLIGLSATLPNYEDVATFL-RVDPAKG 672
Cdd:cd18025 151 --PCPFLALSATIGNPQKFHEWLqSVQRARK 179
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
485-873 |
8.68e-17 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 86.84 E-value: 8.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 485 QSKLYRAALEtDENLLLCAPTGAGKTNVALMCMLREIGKhinmDGTINVDDFKIIYIAPMRSL-------VQEMVGSFGK 557
Cdd:TIGR04121 18 QLEMWAAALE-GRSGLLIAPTGSGKTLAGFLPSLIDLAG----PEAPKEKGLHTLYITPLRALavdiarnLQAPIEELGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 558 rlatyGITVAELTGD---HQLCKEEISATQIIVCTPEKWDI-ITRKGGERTYTQLvRLIILDEIH-LLHDDRGPVLEALV 632
Cdd:TIGR04121 93 -----PIRVETRTGDtssSERARQRKKPPDILLTTPESLALlLSYPDAARLFKDL-RCVVVDEWHeLAGSKRGDQLELAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 633 ARairnIEMTQEDVRLIGLSATLPNYEDVATFL-RVDPAKGLFYFDNSFRPVPLEqTYVGITEKK-------AIKRFqim 704
Cdd:TIGR04121 167 AR----LRRLAPGLRRWGLSATIGNLEEARRVLlGVGGAPAVLVRGKLPKAIEVI-SLLPESEERfpwaghlGLRAL--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 705 nEIVYEKIMEHagkNQVLVFVHSRKETGKTARAIRDmclekdtlglflregsastevlrteaeqcKNLELKDLLpygfAI 784
Cdd:TIGR04121 239 -PEVYAEIDQA---RTTLVFTNTRSQAELWFQALWE-----------------------------ANPEFALPI----AL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 785 HHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVN-LPAHTVIikgtQVYSPEkgrwtelGALDILQMLGRAG-RPqyD 862
Cdd:TIGR04121 282 HHGSLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDfGPVDLVI----QIGSPK-------GVARLLQRAGRSNhRP--G 348
|
410
....*....|.
gi 40217847 863 TKGEGILITSH 873
Cdd:TIGR04121 349 EPSRALLVPTN 359
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1292-1646 |
4.48e-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: 84.50 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1292 PEKYPPPTellDLQPLPVSALRNSAFESLYqdKFpffnpiQTQVFNTVYNsDDNVFVGAPTGSGKTICAEFAILRMLLQS 1371
Cdd:COG1205 32 ARYAPWPD---WLPPELRAALKKRGIERLY--SH------QAEAIEAARA-GKNVVIATPTASGKSLAYLLPVLEALLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1372 SEGRCVYITPMEALAEqvymDWYEKFQDRLNK-----KVVLLTGETSTDL--KLLGKGNIIISTPEKWD--ILSRRWKQR 1442
Cdd:COG1205 100 PGATALYLYPTKALAR----DQLRRLRELAEAlglgvRVATYDGDTPPEErrWIREHPDIVLTNPDMLHygLLPHHTRWA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1443 KNVQNINLFVVDEVHL---IGGENgpV------LEVIC----SRMRYISSQ-------------IERPIRIVALSSSLSN 1496
Cdd:COG1205 176 RFFRNLRYVVIDEAHTyrgVFGSH--VanvlrrLRRICrhygSDPQFILASatignpaehaerlTGRPVTVVDEDGSPRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1497 AKDVAHWlgcsatstfnfHPNVRPVPLELHiqgfniSHTQTRLLsMAKPVYHAItkhspkkPVIVFVPSRKQTRLTAIDI 1576
Cdd:COG1205 254 ERTFVLW-----------NPPLVDDGIRRS------ALAEAARL-LADLVREGL-------RTLVFTRSRRGAELLARYA 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40217847 1577 lttcaadiqRQRFLHCTEKDLI-PYleklsdstlketllngvgylHEGLSPMERRLVEQLFSSGAIQVVVA 1646
Cdd:COG1205 309 ---------RRALREPDLADRVaAY--------------------RAGYLPEERREIERGLRSGELLGVVS 350
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
463-876 |
8.13e-16 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 84.00 E-value: 8.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 463 PVEKLPKYAQAGFEG-FKTLNRIQSKLYRAALEtDENLLLCAPTGAGKT----NVALMCMLREIGKHINMDGTinvddfK 537
Cdd:COG1201 6 VLSLLHPAVRAWFAArFGAPTPPQREAWPAIAA-GESTLLIAPTGSGKTlaafLPALDELARRPRPGELPDGL------R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 538 IIYIAPMRSL-----------VQEMVGSFGKRLAtyGITVAELTGDhqlckeeISATQ----------IIVCTPEKWDI- 595
Cdd:COG1201 79 VLYISPLKALandiernlrapLEEIGEAAGLPLP--EIRVGVRTGD-------TPASErqrqrrrpphILITTPESLALl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 596 ITRKGGERTYTQlVRLIILDEIHLLHDD-RGPVLEALVARaIRNIemTQEDVRLIGLSATLPNYEDVATFL--------- 665
Cdd:COG1201 150 LTSPDARELLRG-VRTVIVDEIHALAGSkRGVHLALSLER-LRAL--APRPLQRIGLSATVGPLEEVARFLvgyedprpv 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 666 -RVDPAKGlfyfdnsfRPVPLEqtyVGITEKKAIKRFQIMNEI---VYEKIMEHAGKNQ-VLVFVHSRKETGKTARAIRD 740
Cdd:COG1201 226 tIVDAGAG--------KKPDLE---VLVPVEDLIERFPWAGHLwphLYPRVLDLIEAHRtTLVFTNTRSQAERLFQRLNE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 741 MclekdtlglflregsastevlrteaeqckNLELKDLLpygfAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVN 820
Cdd:COG1201 295 L-----------------------------NPEDALPI----AAHHGSLSREQRLEVEEALKAGELRAVVATSSLELGID 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 40217847 821 LPA-HTVIikgtQVYSPeKGrwteLGALdiLQMLGRAGRpQYDTKGEGILITSH-GEL 876
Cdd:COG1201 342 IGDvDLVI----QVGSP-KS----VARL--LQRIGRAGH-RVGEVSKGRLVPTHrDEL 387
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
481-858 |
3.16e-15 |
|
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: 81.28 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 481 LNRIQSKLYRAALETDEN----LLLCAPTGAGKTNVALMCMLREIGKHINmdgtinvddFKIIYIAPMRSLVQEMVGSFG 556
Cdd:COG1203 128 INPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKHGG---------RRIIYALPFTSIINQTYDRLR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 557 KrlaTYGITVAELTGD---HQLCKEEISATQ--------------IIVCTPekwD------IITRKGGERTYTQLVR-LI 612
Cdd:COG1203 199 D---LFGEDVLLHHSLadlDLLEEEEEYESEarwlkllkelwdapVVVTTI---DqlfeslFSNRKGQERRLHNLANsVI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 613 ILDEIHLL-HDDRGPVLEALvaRAIRNIemtqeDVRLIGLSATLPnyedvaTFLRvdpaKGLFyfdNSFRPVP-LEQTYV 690
Cdd:COG1203 273 ILDEVQAYpPYMLALLLRLL--EWLKNL-----GGSVILMTATLP------PLLR----EELL---EAYELIPdEPEELP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 691 GITEKKAIKRFQ-----IMNEIVYEKIMEHA-GKNQVLVFVHSRKEtgktARAIRDmclekdtlglflregsastevlrt 764
Cdd:COG1203 333 EYFRAFVRKRVElkegpLSDEELAELILEALhKGKSVLVIVNTVKD----AQELYE------------------------ 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 765 eaeqcknlELKDLLPYGFAIH-HAGMTRVDRTLVE----DLFADKHIQVLVST----AtlawGVNLPAHTVIikgtqvys 835
Cdd:COG1203 385 --------ALKEKLPDEEVYLlHSRFCPADRSEIEkeikERLERGKPCILVSTqvveA----GVDIDFDVVI-------- 444
|
410 420
....*....|....*....|....
gi 40217847 836 pekgrwTELGALD-ILQmlgRAGR 858
Cdd:COG1203 445 ------RDLAPLDsLIQ---RAGR 459
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
497-654 |
1.27e-14 |
|
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: 72.82 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 497 ENLLLCAPTGAGKTNVALMCMLREIGKHInmdgtinvddFKIIYIAPMRSLVQEMVGSFgKRLATYGITVAELTGDHQLC 576
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKKG----------KKVLVLVPTKALALQTAERL-RELFGPGIRVAVLVGGSSAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 577 KEEISATQ---IIVCTPEK-WDIITRKGGERTYTQlvRLIILDEIH-LLHDDRGPVLEALvarAIRNIEMTqeDVRLIGL 651
Cdd:cd00046 71 EREKNKLGdadIIIATPDMlLNLLLREDRLFLKDL--KLIIVDEAHaLLIDSRGALILDL---AVRKAGLK--NAQVILL 143
|
...
gi 40217847 652 SAT 654
Cdd:cd00046 144 SAT 146
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1324-1505 |
2.39e-14 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 73.45 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1324 KFPF-FNPIQTQVFNTVyNSDDNVFVGAPTGSGKTICAEFAIlrMLLQSSEGRCVYITPMEALAEQVYMDWYEKFQDrln 1402
Cdd:cd18027 4 KWPFeLDVFQKQAILHL-EAGDSVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1403 kkVVLLTGetstDLKLLGKGNIIISTPEkwdIL-SRRWKQRKNVQNINLFVVDEVHLIG-GENGPVLEVICsrmryissq 1480
Cdd:cd18027 78 --VGLITG----DVQLNPEASCLIMTTE---ILrSMLYNGSDVIRDLEWVIFDEVHYINdAERGVVWEEVL--------- 139
|
170 180
....*....|....*....|....*..
gi 40217847 1481 IERP--IRIVALSSSLSNAKDVAHWLG 1505
Cdd:cd18027 140 IMLPdhVSIILLSATVPNTVEFADWIG 166
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1308-1650 |
7.78e-14 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 77.45 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1308 PVSALRNSAFESLYQDKFPFFNPIQTQVFnTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEG-------RCVYIT 1380
Cdd:COG1201 5 DVLSLLHPAVRAWFAARFGAPTPPQREAW-PAIAAGESTLLIAPTGSGKTLAAFLPALDELARRPRPgelpdglRVLYIS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1381 PMEALA-------EQVYMDWYEKFQDRLNK-KVVLLTGETSTDLK---LLGKGNIIISTPEKWDIL--SRRWKQR-KNVQ 1446
Cdd:COG1201 84 PLKALAndiernlRAPLEEIGEAAGLPLPEiRVGVRTGDTPASERqrqRRRPPHILITTPESLALLltSPDARELlRGVR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1447 NInlfVVDEVH-LIGGENGPVLEVICSRMRYISsqiERPIRIVALSSSLSNAKDVAHWLGCsatstfnfHPNVRPV---- 1521
Cdd:COG1201 164 TV---IVDEIHaLAGSKRGVHLALSLERLRALA---PRPLQRIGLSATVGPLEEVARFLVG--------YEDPRPVtivd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1522 -------------PLELHIQGFNISHTQTRllSMAKPVYHAITKHspkKPVIVFVPSRKQT-RLTaidilttcaadiQRQ 1587
Cdd:COG1201 230 agagkkpdlevlvPVEDLIERFPWAGHLWP--HLYPRVLDLIEAH---RTTLVFTNTRSQAeRLF------------QRL 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40217847 1588 RFLHCTEKDLIpyleklsdstlketllngvgYLHEG-LSPMERRLVEQLFSSGAIQVVVASRSL 1650
Cdd:COG1201 293 NELNPEDALPI--------------------AAHHGsLSREQRLEVEEALKAGELRAVVATSSL 336
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
773-859 |
1.18e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 68.01 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 773 ELKDLL---PYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLP-AHTVIIKGTqVYSPEkgrwtelgalD 848
Cdd:smart00490 2 ELAELLkelGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL-PWSPA----------S 70
|
90
....*....|.
gi 40217847 849 ILQMLGRAGRP 859
Cdd:smart00490 71 YIQRIGRAGRA 81
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
1345-1461 |
1.47e-13 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 70.12 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1345 NVFVGAPTGSGKTICAE-FAILRMLLQssEGRCVYITPMEALAEQvymdWYEKFQDRL--NKKVVLLTGETSTDLKLLGK 1421
Cdd:cd00046 3 NVLITAPTGSGKTLAALlAALLLLLKK--GKKVLVLVPTKALALQ----TAERLRELFgpGIRVAVLVGGSSAEEREKNK 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 40217847 1422 GN---IIISTPEKWDILSRRWKQRKnVQNINLFVVDEVHLIGG 1461
Cdd:cd00046 77 LGdadIIIATPDMLLNLLLREDRLF-LKDLKLIIVDEAHALLI 118
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
1325-1504 |
2.17e-12 |
|
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: 68.24 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1325 FPF-FNPIQTQVFNTVYNSDdNVFVGAPTGSGKTICAEFAILRMLlqSSEGRCVYITPMEALAEQVYMDWYEKFQDrlnk 1403
Cdd:cd18024 29 YPFtLDPFQKTAIACIERNE-SVLVSAHTSAGKTVVAEYAIAQSL--RDKQRVIYTSPIKALSNQKYRELQEEFGD---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1404 kVVLLTGetstDLKLLGKGNIIISTPEkwdIL-SRRWKQRKNVQNINLFVVDEVHLI-GGENGPVLEvicsrmryiSSQI 1481
Cdd:cd18024 102 -VGLMTG----DVTINPNASCLVMTTE---ILrSMLYRGSEIMREVAWVIFDEIHYMrDKERGVVWE---------ETII 164
|
170 180
....*....|....*....|....*
gi 40217847 1482 ERP--IRIVALSSSLSNAKDVAHWL 1504
Cdd:cd18024 165 LLPdkVRYVFLSATIPNARQFAEWI 189
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
1345-1501 |
3.27e-12 |
|
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: 67.22 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1345 NVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEqvymDWYEKFQDRLNK-----KVVLLTGETSTDLK-- 1417
Cdd:cd17923 17 SVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQ----DQLRSLRELLEQlglgiRVATYDGDTPREERra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1418 -LLGKGNIIISTPEK--WDILSRRWKQRKNVQNINLFVVDEVHLIGGENGPVLEVICSRMRYISSQIERPIRIVALSSSL 1494
Cdd:cd17923 93 iIRNPPRILLTNPDMlhYALLPHHDRWARFLRNLRYVVLDEAHTYRGVFGSHVALLLRRLRRLCRRYGADPQFILTSATI 172
|
....*..
gi 40217847 1495 SNAKDVA 1501
Cdd:cd17923 173 GNPAEHA 179
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1343-1504 |
7.85e-12 |
|
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: 66.24 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1343 DDNVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEQVYMDWYEKFQDRL---NKKVV-LLTGETSTDLKL 1418
Cdd:cd18025 16 RESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYppsGKSLWgVFTRDYRHNNPM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1419 lgKGNIIISTPEKWDI--LSR---RWKQRknvqnINLFVVDEVHLIGG-ENGPVLEVICSRMryissqierPIRIVALSS 1492
Cdd:cd18025 96 --NCQVLITVPECLEIllLSPhnaSWVPR-----IKYVIFDEIHSIGQsEDGAVWEQLLLLI---------PCPFLALSA 159
|
170
....*....|..
gi 40217847 1493 SLSNAKDVAHWL 1504
Cdd:cd18025 160 TIGNPQKFHEWL 171
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
1350-1462 |
4.03e-11 |
|
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: 63.09 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1350 APTGSGKTICAeFAILRMLlqsSEGRCVYITPMEALAEQvymdWYEKFQDRLNKKVVLLTGetSTDLKLLGKGNIIISTP 1429
Cdd:cd17926 25 LPTGSGKTLTA-LALIAYL---KELRTLIVVPTDALLDQ----WKERFEDFLGDSSIGLIG--GGKKKDFDDANVVVATY 94
|
90 100 110
....*....|....*....|....*....|...
gi 40217847 1430 EKWDILSRRWKQRKNVQniNLFVVDEVHLIGGE 1462
Cdd:cd17926 95 QSLSNLAEEEKDLFDQF--GLLIVDEAHHLPAK 125
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1350-1457 |
5.23e-11 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 63.07 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1350 APTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEQvymdWYEKFQDRLNKKvVLLTGETSTDLKL--LGKGNIIIS 1427
Cdd:pfam04851 30 MATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQ----ALEEFKKFLPNY-VEIGEIISGDKKDesVDDNKIVVT 104
|
90 100 110
....*....|....*....|....*....|
gi 40217847 1428 TPEKWDILSRRWKQRKNVQNINLFVVDEVH 1457
Cdd:pfam04851 105 TIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
485-619 |
6.16e-11 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 63.99 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 485 QSKLYRAALEtDENLLLCAPTGAGKTNVALMCMLREIGKHINMDGTinvddfKIIYIAPMRSLVQEMVGSFGKRLATYGI 564
Cdd:cd17927 7 QLELAQPALK-GKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKG------KVVFLANKVPLVEQQKEVFRKHFERPGY 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 565 TVAELTGDHQL---CKEEISATQIIVCTPEkwdIITR--KGGERTYTQLVRLIILDEIHL 619
Cdd:cd17927 80 KVTGLSGDTSEnvsVEQIVESSDVIIVTPQ---ILVNdlKSGTIVSLSDFSLLVFDECHN 136
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
1341-1650 |
7.06e-11 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 67.36 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1341 NSDDNVFVgAPTGSGKTICAEFAILRMLLQsseGRCVYITPMEALAEQvymdWYEKFQDRLNKKvvlLTGETSTDLkllg 1420
Cdd:COG1061 99 GGGRGLVV-APTGTGKTVLALALAAELLRG---KRVLVLVPRRELLEQ----WAEELRRFLGDP---LAGGGKKDS---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1421 KGNIIISTpekWDILSRRWKQRKNVQNINLFVVDEVHLIGgenGPVLEVIcsrMRYISSQI------------ERPIRI- 1487
Cdd:COG1061 164 DAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHAG---APSYRRI---LEAFPAAYrlgltatpfrsdGREILLf 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1488 ----VALSSSLSNAKDvAHWLgcsatSTFNFHPnvRPVPLELHIQGFNISHTQ--TRLLSMAKPVYHAIT----KHSPKK 1557
Cdd:COG1061 235 lfdgIVYEYSLKEAIE-DGYL-----APPEYYG--IRVDLTDERAEYDALSERlrEALAADAERKDKILRellrEHPDDR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1558 PVIVFVPSRKQtrltaidilttcaadiqrqrflhctekdlipyLEKLSDstlketLLNGVGY----LHEGLSPMERRLVE 1633
Cdd:COG1061 307 KTLVFCSSVDH--------------------------------AEALAE------LLNEAGIraavVTGDTPKKEREEIL 348
|
330
....*....|....*..
gi 40217847 1634 QLFSSGAIQVVVASRSL 1650
Cdd:COG1061 349 EAFRDGELRILVTVDVL 365
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
1350-1650 |
8.03e-11 |
|
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: 67.58 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1350 APTGSGKTICAEFAILRMLLQSSEGRC-----VYITPMEALAEQVY---------MDwyekfqdrLNKKVVLLTGETSTD 1415
Cdd:TIGR04121 35 APTGSGKTLAGFLPSLIDLAGPEAPKEkglhtLYITPLRALAVDIArnlqapieeLG--------LPIRVETRTGDTSSS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1416 LK---LLGKGNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVH-LIGGENGPVLEVICSRMRYISSQierpIRIVALS 1491
Cdd:TIGR04121 107 ERarqRKKPPDILLTTPESLALLLSYPDAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG----LRRWGLS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1492 SSLSNAKDVAHWLGcsatstfnfHPNVRPVPLelhIQGFN---------ISHTQTRL-------LSMAKPVYHAITKHsp 1555
Cdd:TIGR04121 183 ATIGNLEEARRVLL---------GVGGAPAVL---VRGKLpkaievislLPESEERFpwaghlgLRALPEVYAEIDQA-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1556 kKPVIVFVPSRKQTrltaidilttcaadiqrQRFLHCtekdlipYLEKLSDstlketlLNGVGYLHEG-LSPMERRLVEQ 1634
Cdd:TIGR04121 249 -RTTLVFTNTRSQA-----------------ELWFQA-------LWEANPE-------FALPIALHHGsLDREQRRWVEA 296
|
330
....*....|....*.
gi 40217847 1635 LFSSGAIQVVVASRSL 1650
Cdd:TIGR04121 297 AMAAGRLRAVVCTSSL 312
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
1309-1456 |
8.96e-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: 63.23 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1309 VSALRNSAFESLyqdkfpffNPIQTQVFNTVYnSDDNVFVGAPTGSGKTICaeFA--ILRMLLQSSEG-----RCVYITP 1381
Cdd:cd00268 2 LKALKKLGFEKP--------TPIQAQAIPLIL-SGRDVIGQAQTGSGKTLA--FLlpILEKLLPEPKKkgrgpQALVLAP 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40217847 1382 MEALAEQVYMDwYEKFQDRLNKKVVLLTGETS--TDLKLLGKG-NIIISTPEK-WDILSRRwkqRKNVQNINLFVVDEV 1456
Cdd:cd00268 71 TRELAMQIAEV-ARKLGKGTGLKVAAIYGGAPikKQIEALKKGpDIVVGTPGRlLDLIERG---KLDLSNVKYLVLDEA 145
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1350-1662 |
1.08e-10 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 67.26 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1350 APTGSGKTICA-EFAILRMLLQSSE----------GRCVYITPMEALAEQV----------YMDWYEKFQD-RLNKKVVL 1407
Cdd:PRK09751 3 APTGSGKTLAAfLYALDRLFREGGEdtreahkrktSRILYISPIKALGTDVqrnlqiplkgIADERRRRGEtEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1408 LTGETSTD--LKLLGK-GNIIISTPEK-WDILSRRwkQRKNVQNINLFVVDEVHLIGG-ENGPVLEVICSRMryiSSQIE 1482
Cdd:PRK09751 83 RTGDTPAQerSKLTRNpPDILITTPESlYLMLTSR--ARETLRGVETVIIDEVHAVAGsKRGAHLALSLERL---DALLH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1483 RPIRIVALSSSLSNAKDVAHWLGCSATSTFNFHPNVRPVPLELHIQGFNISHT------------QTRLLSMAKPVYHAI 1550
Cdd:PRK09751 158 TSAQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRHPQIRIVVPVANMDDVssvasgtgedshAGREGSIWPYIETGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1551 TKHS-PKKPVIVFVPSRKQT-RLTAiDILTTCAADIQRqrflhcTEKDLIP--YLEKLSDSTLK-----ETLLngvGYLH 1621
Cdd:PRK09751 238 LDEVlRHRSTIVFTNSRGLAeKLTA-RLNELYAARLQR------SPSIAVDaaHFESTSGATSNrvqssDVFI---ARSH 307
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 40217847 1622 EG-LSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAA-HLVI 1662
Cdd:PRK09751 308 HGsVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAvDLVI 350
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
487-859 |
1.75e-10 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 66.20 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 487 KLYRAALETDENLLLCAPTGAGKTNVALMCMLREIGKHinmdgtinvddfKIIYIAPMRSLVQEMVGSFGKRLatygiTV 566
Cdd:COG1061 91 ALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK------------RVLVLVPRRELLEQWAEELRRFL-----GD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 567 AELTGDHQlckeEISAtQIIVCTpekWDIITRKGGERTYTQLVRLIILDEIHLLhddRGPVLEALVARAirniemtqEDV 646
Cdd:COG1061 154 PLAGGGKK----DSDA-PITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHA---GAPSYRRILEAF--------PAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 647 RLIGLSATlPNYEDVATFLrvdpakgLFYFDN-------------------SFRPVPLEQT-----YVGITEK--KAIKR 700
Cdd:COG1061 215 YRLGLTAT-PFRSDGREIL-------LFLFDGivyeyslkeaiedgylappEYYGIRVDLTderaeYDALSERlrEALAA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 701 FQIMNEIVYEKIM-EHAGKNQVLVFVhsrkETGKTARAIRDmclekdtlgLFLREGSASTEVlrteaeqcknlelkdllp 779
Cdd:COG1061 287 DAERKDKILRELLrEHPDDRKTLVFC----SSVDHAEALAE---------LLNEAGIRAAVV------------------ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 780 ygfaihHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIKGTQVYSPekgrwtelgaLDILQMLGRAGRP 859
Cdd:COG1061 336 ------TGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSP----------REFIQRLGRGLRP 399
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1616-1694 |
7.64e-10 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 57.22 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1616 GVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNV-AAHLVIIMDtqyyngkihayVDYPIYDVLQMVGHANRP 1694
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLpGVDLVIIYD-----------LPWSPASYIQRIGRAGRA 81
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
496-658 |
1.02e-09 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 60.00 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 496 DENLLLCAPTGAGKTNVALMCMLREIGKHInmdgtinvdDFKIIYIAPMRSLVQEMVG----SFGKRLATYGITVA---- 567
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWALKLAARGG---------KRRIIYALPTRATINQMYErireILGRLDDEDKVLLLhska 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 568 ---ELTGDHQLCKEEISATQ------------IIVCTpekWD-----IITRKGGERTYTQLVR-LIILDEIHLLhDDR-- 624
Cdd:cd17930 72 aleLLESDEEPDDDPVEAVDwalllkrswlapIVVTT---IDqllesLLKYKHFERRLHGLANsVVVLDEVQAY-DPEym 147
|
170 180 190
....*....|....*....|....*....|....
gi 40217847 625 GPVLEALVARAirniemTQEDVRLIGLSATLPNY 658
Cdd:cd17930 148 ALLLKALLELL------GELGGPVVLMTATLPAL 175
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
1324-1455 |
4.67e-09 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 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: 350718 [Multi-domain] Cd Length: 202 Bit Score: 58.36 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1324 KFPFFNPIQTQVfNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEG------RCVYITPMEALAEQVYmDWYEKF 1397
Cdd:cd17960 9 GFTSMTPVQAAT-IPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANlkkgqvGALIISPTRELATQIY-EVLQSF 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40217847 1398 QDRLNKKV--VLLTG--ETSTDLKLL--GKGNIIISTPEK-WDILSRRWKQRKnVQNINLFVVDE 1455
Cdd:cd17960 87 LEHHLPKLkcQLLIGgtNVEEDVKKFkrNGPNILVGTPGRlEELLSRKADKVK-VKSLEVLVLDE 150
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
1343-1457 |
6.94e-09 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 61.28 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1343 DDNVFVGAPTGSGKTICAEFAILRMlLQSSEGRCVYITPMEALAEQvYMDWYEKFQDRLNKKVVLLTGETSTD--LKLLG 1420
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAER-LHKKGGKVLFLAPTKPLVEQ-HAEFFKEALNIPEDEIVVFTGEVSPEkrKELWE 94
|
90 100 110
....*....|....*....|....*....|....*....
gi 40217847 1421 KGNIIISTPE--KWDILSRRWkqrkNVQNINLFVVDEVH 1457
Cdd:COG1111 95 KARIIVATPQviENDLIAGRI----DLDDVSLLIFDEAH 129
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
485-880 |
7.89e-09 |
|
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: 61.00 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 485 QSKLYRAALEtDENLLLCAPTGAGKTNVALMCMLREIGKHinmdgtinvDDFKIIYIAPMRSLVQEMVGSFgKRLATY-- 562
Cdd:COG1205 61 QAEAIEAARA-GKNVVIATPTASGKSLAYLLPVLEALLED---------PGATALYLYPTKALARDQLRRL-RELAEAlg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 563 -GITVAELTGD---HQlcKEEI-SATQIIVCTP-----------EKWDiitrkggeRTYTQLvRLIILDEIHLLhddRGp 626
Cdd:COG1205 130 lGVRVATYDGDtppEE--RRWIrEHPDIVLTNPdmlhygllphhTRWA--------RFFRNL-RYVVIDEAHTY---RG- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 627 VLE---ALVARAIRNI-EMTQEDVRLIGLSATLPNYEDVATFLrvdpakglfyfdnsfrpvpLEQTYVGITE---KKAIK 699
Cdd:COG1205 195 VFGshvANVLRRLRRIcRHYGSDPQFILASATIGNPAEHAERL-------------------TGRPVTVVDEdgsPRGER 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 700 RFQIMNEIVYEK------------IMEHAGKN--QVLVFVHSRKETGKTARAIRDMclekdtlglfLREGSASTEVlrte 765
Cdd:COG1205 256 TFVLWNPPLVDDgirrsalaeaarLLADLVREglRTLVFTRSRRGAELLARYARRA----------LREPDLADRV---- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 766 aeqcknlelkdllpygfAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPA-HTVIIKGtqvYsPekGRWTEL 844
Cdd:COG1205 322 -----------------AAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVVLAG---Y-P--GTRASF 378
|
410 420 430
....*....|....*....|....*....|....*..
gi 40217847 845 galdiLQMLGRAGRPQYDtkGEGILITSHGEL-QYYL 880
Cdd:COG1205 379 -----WQQAGRAGRRGQD--SLVVLVAGDDPLdQYYV 408
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
1345-1457 |
7.95e-09 |
|
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: 57.14 E-value: 7.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1345 NVFVGAPTGSGKTIcaeFAILRML--LQSSEGRCVYITPMEALAEQvymdWYEKFQDRLN--KKVVLLTGETSTD--LKL 1418
Cdd:cd18035 18 NTLIVLPTGLGKTI---IAILVAAdrLTKKGGKVLILAPSRPLVEQ----HAENLKRVLNipDKITSLTGEVKPEerAER 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 40217847 1419 LGKGNIIISTPE--KWDILSRRWkqrkNVQNINLFVVDEVH 1457
Cdd:cd18035 91 WDASKIIVATPQviENDLLAGRI----TLDDVSLLIFDEAH 127
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
479-653 |
1.11e-08 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 57.28 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 479 KTLNRIQSKLYRAALetDENLLLCAPTGAGKTNVALMCMLREIgkHINMDGTINvdDFKIIYIAPMRSLVQEMVgsfgKR 558
Cdd:cd18034 1 FTPRSYQLELFEAAL--KRNTIVVLPTGSGKTLIAVMLIKEMG--ELNRKEKNP--KKRAVFLVPTVPLVAQQA----EA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 559 LATY-GITVAELTGD-------HQLCKEEISATQIIVCTPEKW-DIITRKggertYTQL--VRLIILDEIHL---LHddr 624
Cdd:cd18034 71 IRSHtDLKVGEYSGEmgvdkwtKERWKEELEKYDVLVMTAQILlDALRHG-----FLSLsdINLLIFDECHHatgDH--- 142
|
170 180
....*....|....*....|....*....
gi 40217847 625 gPVleALVARAIRNIEMTQEDVRLIGLSA 653
Cdd:cd18034 143 -PY--ARIMKEFYHLEGRTSRPRILGLTA 168
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
1343-1498 |
1.59e-08 |
|
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: 56.67 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1343 DDNVFVGAPTGSGKT-----ICAEFaiLRMLLQSSEGRCVYITPMEALAEQvYMDWYEKFQDRLNKKVVLLTGETSTDL- 1416
Cdd:cd17927 17 GKNTIICLPTGSGKTfvavlICEHH--LKKFPAGRKGKVVFLANKVPLVEQ-QKEVFRKHFERPGYKVTGLSGDTSENVs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1417 --KLLGKGNIIISTPEkwdILSRRWKQRKNVQ--NINLFVVDEVHLIGGeNGPVLEVIcsrMRYISSQIERPI---RIVA 1489
Cdd:cd17927 94 veQIVESSDVIIVTPQ---ILVNDLKSGTIVSlsDFSLLVFDECHNTTK-NHPYNEIM---FRYLDQKLGSSGplpQILG 166
|
....*....
gi 40217847 1490 LSSSLSNAK 1498
Cdd:cd17927 167 LTASPGVGG 175
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
774-858 |
1.83e-08 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 54.14 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 774 LKDLLPYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLP-AHTVIIkgtqvYSPEKGRwtelgaLDILQM 852
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YDLPWNP------ASYIQR 101
|
....*.
gi 40217847 853 LGRAGR 858
Cdd:pfam00271 102 IGRAGR 107
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
1343-1498 |
1.88e-08 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 56.51 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1343 DDNVFVGAPTGSGKTICAEFAILRML-----LQSSEGRCVYITPMEALAEQvymdWYEKFQDRLNKKVVLLTGETSTDLK 1417
Cdd:cd18034 16 KRNTIVVLPTGSGKTLIAVMLIKEMGelnrkEKNPKKRAVFLVPTVPLVAQ----QAEAIRSHTDLKVGEYSGEMGVDKW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1418 -------LLGKGNIIISTPEKW-DILSRRWKQrknVQNINLFVVDEVHLIGGENgPVLEVicsrMR--YISSQIERPIRI 1487
Cdd:cd18034 92 tkerwkeELEKYDVLVMTAQILlDALRHGFLS---LSDINLLIFDECHHATGDH-PYARI----MKefYHLEGRTSRPRI 163
|
170
....*....|.
gi 40217847 1488 VALSSSLSNAK 1498
Cdd:cd18034 164 LGLTASPVNGK 174
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
485-660 |
2.26e-08 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 59.36 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 485 QSKLYRAALetDENLLLCAPTGAGKTNVALM---CMLREIGKhinmdgtinvddfKIIYIAPMRSLVQEMVGSFGKRLAT 561
Cdd:COG1111 8 QLNLAASAL--RKNTLVVLPTGLGKTAVALLviaERLHKKGG-------------KVLFLAPTKPLVEQHAEFFKEALNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 562 YGITVAELTGDHQLCK--EEISATQIIVCTPE--KWDIItrkgGERTYTQLVRLIILDEIHllhddRGPVLEALVARAIR 637
Cdd:COG1111 73 PEDEIVVFTGEVSPEKrkELWEKARIIVATPQviENDLI----AGRIDLDDVSLLIFDEAH-----RAVGNYAYVYIAER 143
|
170 180
....*....|....*....|...
gi 40217847 638 NIEmTQEDVRLIGLSATLPNYED 660
Cdd:COG1111 144 YHE-DAKDPLILGMTASPGSDEE 165
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
477-656 |
3.79e-08 |
|
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: 55.53 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 477 GFKTLNRIQSKLYRAALEtDENLLLCAPTGAGKTNVALMCMLReigkHINMDGTINVDDFKIIYIAPMRSL---VQEMVG 553
Cdd:cd00268 9 GFEKPTPIQAQAIPLILS-GRDVIGQAQTGSGKTLAFLLPILE----KLLPEPKKKGRGPQALVLAPTRELamqIAEVAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 554 SFGKRLatyGITVAELTG----DHQLcKEEISATQIIVCTPEK-WDIITRKggeRTYTQLVRLIILDEI-HLLHDDRGPV 627
Cdd:cd00268 84 KLGKGT---GLKVAAIYGgapiKKQI-EALKKGPDIVVGTPGRlLDLIERG---KLDLSNVKYLVLDEAdRMLDMGFEED 156
|
170 180
....*....|....*....|....*....
gi 40217847 628 LEALvarairnIEMTQEDVRLIGLSATLP 656
Cdd:cd00268 157 VEKI-------LSALPKDRQTLLFSATLP 178
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
1322-1459 |
4.13e-08 |
|
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: 55.62 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1322 QDKFPF--FNPIQTQVFNTVYNSDDnVFVGAPTGSGKTICAEF-AILRmllqssEGRCVYITPMEAL-AEQVymdwyEKF 1397
Cdd:cd17920 5 KEVFGYdeFRPGQLEAINAVLAGRD-VLVVMPTGGGKSLCYQLpALLL------DGVTLVVSPLISLmQDQV-----DRL 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40217847 1398 QdRLNKKVVLLTGETSTDLK-------LLGKGNIIISTPEKwdILSRRWKQR----KNVQNINLFVVDEVHLI 1459
Cdd:cd17920 73 Q-QLGIRAAALNSTLSPEEKrevllriKNGQYKLLYVTPER--LLSPDFLELlqrlPERKRLALIVVDEAHCV 142
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
1343-1457 |
7.11e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.96 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1343 DDNVFVGAPTGSGKTICAEFAILRmLLQSSEGRCVYITPMEALAEQVYmDWYEKFQDRLNKKVVLLTGETSTD--LKLLG 1420
Cdd:PRK13766 29 KKNTLVVLPTGLGKTAIALLVIAE-RLHKKGGKVLILAPTKPLVEQHA-EFFRKFLNIPEEKIVVFTGEVSPEkrAELWE 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 40217847 1421 KGNIIISTPE--KWDILSRRWkqrkNVQNINLFVVDEVH 1457
Cdd:PRK13766 107 KAKVIVATPQviENDLIAGRI----SLEDVSLLIFDEAH 141
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
1330-1455 |
1.27e-07 |
|
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: 54.13 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1330 PIQTQVFNTVYNSDDnVFVGAPTGSGKTICAEFAILRMLLQSSEG---RCVYITPMEALAEQVYMDwYEKFQDRLNKKVV 1406
Cdd:cd17957 15 PIQMQAIPILLHGRD-LLACAPTGSGKTLAFLIPILQKLGKPRKKkglRALILAPTRELASQIYRE-LLKLSKGTGLRIV 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 40217847 1407 LLTGETST----DLKLLGKGNIIISTPEKW-DILSRRWKQRKNVQNinlFVVDE 1455
Cdd:cd17957 93 LLSKSLEAkakdGPKSITKYDILVSTPLRLvFLLKQGPIDLSSVEY---LVLDE 143
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1323-1505 |
1.41e-07 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 56.82 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1323 DKFPFFNPIQTQVFNTVYNSDdNVFVGAPTGSGKTICAEFAILRMLLQ-SSEGR------CVYITPMEALA-------EQ 1388
Cdd:PRK13767 28 EKFGTFTPPQRYAIPLIHEGK-NVLISSPTGSGKTLAAFLAIIDELFRlGREGEledkvyCLYVSPLRALNndihrnlEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1389 VYMDWYEKFQDRLNK----KVVLLTGETSTD--LKLLGKG-NIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVH-LIG 1460
Cdd:PRK13767 107 PLTEIREIAKERGEElpeiRVAIRTGDTSSYekQKMLKKPpHILITTPESLAILLNSPKFREKLRTVKWVIVDEIHsLAE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 40217847 1461 GENGPVLEVICSRMRYIssqIERPIRIVALSSSLSNAKDVAHWLG 1505
Cdd:PRK13767 187 NKRGVHLSLSLERLEEL---AGGEFVRIGLSATIEPLEEVAKFLV 228
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
480-656 |
2.27e-07 |
|
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: 53.63 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 480 TLNRIQSKLYRAALEtDENLLLCAPTGAGKTNVALMCMLREIGKHinmdgTINVDDFKIIYIAPMRSLVQEMVGSFGKRL 559
Cdd:cd18036 2 ELRNYQLELVLPALR-GKNTIICAPTGSGKTRVAVYICRHHLEKR-----RSAGEKGRVVVLVNKVPLVEQQLEKFFKYF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 560 ATyGITVAELTGDHQL---CKEEISATQIIVCTPEKWDIITRKG--GERTYTQLVRLIILDEIHllHDDRGPVLEALVAR 634
Cdd:cd18036 76 RK-GYKVTGLSGDSSHkvsFGQIVKASDVIICTPQILINNLLSGreEERVYLSDFSLLIFDECH--HTQKEHPYNKIMRM 152
|
170 180
....*....|....*....|...
gi 40217847 635 AIR-NIEMTQEDVRLIGLSATLP 656
Cdd:cd18036 153 YLDkKLSSQGPLPQILGLTASPG 175
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
469-657 |
3.82e-07 |
|
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: 53.15 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 469 KYAQAGFEGfKTLNRIQSKLYRA----------ALETDENLLLCAPTGAGKTNVALMCMLReigkHINMDGTINVDDFKI 538
Cdd:cd17953 13 KWSQCGLSE-KVLDLIKKLGYEKptpiqaqalpAIMSGRDVIGIAKTGSGKTLAFLLPMFR----HIKDQRPVKPGEGPI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 539 -IYIAPMRSLVQEMVGSFGKRLATYGITVAELTGDHQLcKEEIS----ATQIIVCTPEKW-DIITRKGGERTYTQLVRLI 612
Cdd:cd17953 88 gLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGI-SEQIAelkrGAEIVVCTPGRMiDILTANNGRVTNLRRVTYV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 40217847 613 ILDEIHLLHdDRGpvLEALVARAIRNIemtQEDVRLIGLSATLPN 657
Cdd:cd17953 167 VLDEADRMF-DMG--FEPQIMKIVNNI---RPDRQTVLFSATFPR 205
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
1309-1429 |
4.23e-07 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 53.02 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1309 VSALRNSAFESLYqdkfpffnPIQTQVF--------NTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQ--SSEGRCVY 1378
Cdd:cd17956 2 LKNLQNNGITSAF--------PVQAAVIpwllpsskSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKrvVPRLRALI 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40217847 1379 ITPMEALAEQVYmDWYEKFQDRLNKKVVLLTGETST--DLKLLGKG---------NIIISTP 1429
Cdd:cd17956 74 VVPTKELVQQVY-KVFESLCKGTGLKVVSLSGQKSFkkEQKLLLVDtsgrylsrvDILVATP 134
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
1343-1439 |
1.12e-06 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 51.14 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1343 DDNVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEQ---VYMDWYEKFQDrlNKKVVLLTGETSTDLKLL 1419
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINQmyeRIREILGRLDD--EDKVLLLHSKAALELLES 78
|
90 100
....*....|....*....|..
gi 40217847 1420 G--KGNIIISTPEKWDILSRRW 1439
Cdd:cd17930 79 DeePDDDPVEAVDWALLLKRSW 100
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
1345-1483 |
1.33e-06 |
|
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: 51.17 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1345 NVFVGAPTGSGKTicAEFAIlrMLLQSSegRCVYITPMEALAEQVY--MDWYEKFQDRLNKKVVLLTGETSTD--LKLLG 1420
Cdd:cd17938 38 DVLMAAETGSGKT--GAFCL--PVLQIV--VALILEPSRELAEQTYncIENFKKYLDNPKLRVALLIGGVKAReqLKRLE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40217847 1421 KG-NIIISTPEK-WDILSrrwKQRKNVQNINLFVVDEV-HLIGGENGPVLEVICSRMRYISSQIER 1483
Cdd:cd17938 112 SGvDIVVGTPGRlEDLIK---TGKLDLSSVRFFVLDEAdRLLSQGNLETINRIYNRIPKITSDGKR 174
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
485-657 |
1.50e-06 |
|
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: 50.66 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 485 QSKLYRAALEtDENLLLCAPTGAGKTNVALMCMLREIGKHINMdgtinvddfKIIYIAPMRSLVQEMVGSFGKRLATY-- 562
Cdd:cd17923 5 QAEAIEAARA-GRSVVVTTGTASGKSLCYQLPILEALLRDPGS---------RALYLYPTKALAQDQLRSLRELLEQLgl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 563 GITVAELTGDHQLCKEE---ISATQIIVCTPEK--WDIITRKGGERTYTQLVRLIILDEIHLLhddRGP----VleALVA 633
Cdd:cd17923 75 GIRVATYDGDTPREERRaiiRNPPRILLTNPDMlhYALLPHHDRWARFLRNLRYVVLDEAHTY---RGVfgshV--ALLL 149
|
170 180
....*....|....*....|....*
gi 40217847 634 RAIRNI-EMTQEDVRLIGLSATLPN 657
Cdd:cd17923 150 RRLRRLcRRYGADPQFILTSATIGN 174
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
715-858 |
1.99e-06 |
|
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: 49.57 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 715 HAGKNqVLVFVHSRKETGKTARAIRDMClEKDTLGLFlregsastevlrteaeqcknlelkdllpygFAIHHAGMTRVDR 794
Cdd:cd18796 36 ERHKS-TLVFTNTRSQAERLAQRLRELC-PDRVPPDF------------------------------IALHHGSLSRELR 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40217847 795 TLVEDLFADKHIQVLVSTATLAWGVNLPA-HTVIikgtQVYSPekgrwteLGALDILQMLGRAGR 858
Cdd:cd18796 84 EEVEAALKRGDLKVVVATSSLELGIDIGDvDLVI----QIGSP-------KSVARLLQRLGRSGH 137
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
485-618 |
2.26e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 52.95 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 485 QSKLYRAALETdeNLLLCAPTGAGKTNVALMCMLREIGKHinmDGtinvddfKIIYIAPMRSLVQEMVGSFGKRLATYGI 564
Cdd:PRK13766 20 QQLLAATALKK--NTLVVLPTGLGKTAIALLVIAERLHKK---GG-------KVLILAPTKPLVEQHAEFFRKFLNIPEE 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 40217847 565 TVAELTGDHQLCK--EEISATQIIVCTPE--KWDIITrkggERTYTQLVRLIILDEIH 618
Cdd:PRK13766 88 KIVVFTGEVSPEKraELWEKAKVIVATPQviENDLIA----GRISLEDVSLLIFDEAH 141
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
491-657 |
2.86e-06 |
|
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: 50.13 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 491 AALETDENLLLCAPTGAGKTNVA----LMCmLReigkhinmdgtinvDDFKIIYIAPMRSL----VQEMVGSFGKrlaty 562
Cdd:cd18024 42 ACIERNESVLVSAHTSAGKTVVAeyaiAQS-LR--------------DKQRVIYTSPIKALsnqkYRELQEEFGD----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 563 gitVAELTGDHQLckeEISATqIIVCTPEkwdiITR----KGGErtYTQLVRLIILDEIHLLHD-DRGPVLEalvaraiR 637
Cdd:cd18024 102 ---VGLMTGDVTI---NPNAS-CLVMTTE----ILRsmlyRGSE--IMREVAWVIFDEIHYMRDkERGVVWE-------E 161
|
170 180
....*....|....*....|
gi 40217847 638 NIEMTQEDVRLIGLSATLPN 657
Cdd:cd18024 162 TIILLPDKVRYVFLSATIPN 181
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
485-618 |
3.50e-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: 49.44 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 485 QSKLYRAALETdeNLLLCAPTGAGKTNVALMCMLREIGKHinmdgtinvdDFKIIYIAPMRSLVQEMVGSFgKRLATYGI 564
Cdd:cd18035 7 QVLIAAVALNG--NTLIVLPTGLGKTIIAILVAADRLTKK----------GGKVLILAPSRPLVEQHAENL-KRVLNIPD 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 40217847 565 TVAELTGDHQLCK--EEISATQIIVCTPE--KWDIITrkggERTYTQLVRLIILDEIH 618
Cdd:cd18035 74 KITSLTGEVKPEEraERWDASKIIVATPQviENDLLA----GRITLDDVSLLIFDEAH 127
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
499-745 |
3.84e-06 |
|
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: 51.28 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 499 LLLCAPTGAGKTNVALMCMLREIGKHINMdgtinvddfKIIYIAPMRSLVQEM----VGSFG-----------KRLATYG 563
Cdd:cd09639 2 LVIEAPTGYGKTEAALLWALHSLKSQKAD---------RVIIALPTRATINAMyrraKEAFGetglyhssilsSRIKEMG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 564 --ITVAELTGDHQLCKEEISATQIIVCTPEKWDI-ITRKGGERTYTQL---VRLIILDEIHLLHDDRGPVLEALVARAIR 637
Cdd:cd09639 73 dsEEFEHLFPLYIHSNDTLFLDPITVCTIDQVLKsVFGEFGHYEFTLAsiaNSLLIFDEVHFYDEYTLALILAVLEVLKD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 638 NiemtqeDVRLIGLSATLPNyedvatFLRVDPAKGLFYFDNSFRPV-PLEQTYVGITEKKAIKRFQIMNEIvyekIMEHA 716
Cdd:cd09639 153 N------DVPILLMSATLPK------FLKEYAEKIGYVEENEPLDLkPNERAPFIKIESDKVGEISSLERL----LEFIK 216
|
250 260
....*....|....*....|....*....
gi 40217847 717 GKNQVLVFVHsrkeTGKTARAIRDMCLEK 745
Cdd:cd09639 217 KGGSVAIIVN----TVDRAQEFYQQLKEK 241
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
493-665 |
4.63e-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: 49.19 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 493 LETDENLLLCAPTGAGKTNVALMCMLREIgKHINmdgtinvddfKIIYIAPMRSLVQEMVGSFGKRLATYGItvaeLTGD 572
Cdd:cd18027 20 LEAGDSVFVAAHTSAGKTVVAEYAIALAQ-KHMT----------RTIYTSPIKALSNQKFRDFKNTFGDVGL----ITGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 573 HQLCKEeisaTQIIVCTPEKWDIITRKGGErtYTQLVRLIILDEIHLLHD-DRGPVLEALVArairnieMTQEDVRLIGL 651
Cdd:cd18027 85 VQLNPE----ASCLIMTTEILRSMLYNGSD--VIRDLEWVIFDEVHYINDaERGVVWEEVLI-------MLPDHVSIILL 151
|
170
....*....|....
gi 40217847 652 SATLPNYEDVATFL 665
Cdd:cd18027 152 SATVPNTVEFADWI 165
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
1317-1455 |
5.63e-06 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 49.50 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1317 FESLYQDKFPFFNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICaeF---AILRML-----LQSSEGRCVYITPMEALAEQ 1388
Cdd:cd17964 6 LKALTRMGFETMTPVQQKTLKPILSTGDDVLARAKTGTGKTLA--FllpAIQSLLntkpaGRRSGVSALIISPTRELALQ 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40217847 1389 VYMDwYEKFQDRLNK-KVVLLTGETS--TDLKLLGKG--NIIISTPEKW-DILSR-RWkqRKNVQNINLFVVDE 1455
Cdd:cd17964 84 IAAE-AKKLLQGLRKlRVQSAVGGTSrrAELNRLRRGrpDILVATPGRLiDHLENpGV--AKAFTDLDYLVLDE 154
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
493-654 |
6.83e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 48.44 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 493 LETDENLLLCAPTGAGKTNVALMCMLREIGKHINmdgtinvddFKIIYIAPMRSLVQEMVGSFGKRLATYGITVAELTGD 572
Cdd:pfam04851 20 KNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPI---------KKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 573 HQlcKEEISATQIIVCTPEKWDIITRKGGERTYTQLVRLIILDEIHLLHDDrgpvlealvarAIRNIEMTQEDVRLIGLS 652
Cdd:pfam04851 91 KK--DESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAHRSGAS-----------SYRNILEYFKPAFLLGLT 157
|
..
gi 40217847 653 AT 654
Cdd:pfam04851 158 AT 159
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
499-745 |
7.38e-06 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 50.53 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 499 LLLCAPTGAGKTNVALMCMLREIGKHINMdgtinvddfKIIYIAPMRSLVQEM----VGSFGKRLATY-------GITVA 567
Cdd:TIGR01587 2 LVIEAPTGYGKTEAALLWALHSIKSQKAD---------RVIIALPTRATINAMyrraKELFGSELVGLhhsssfsRIKEM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 568 ELTGDHQLCKEEIS-------ATQIIVCTPEKWDI-ITRKGGERTYTQL---VRLIILDEIHLLHDDRGPVLEALVARAI 636
Cdd:TIGR01587 73 GDSEEFEHLFPLYIhsndklfLDPITVCTIDQVLKsVFGEFGHYEFTLAsiaNSLLIFDEVHFYDEYTLALILAVLEVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 637 RNiemtqeDVRLIGLSATLPNyedvatFLRVDPAKGLFYFDNSFRPV----PLEQTYVGITEKKAIKRFQIMNEIvyekI 712
Cdd:TIGR01587 153 DN------DVPILLMSATLPK------FLKEYAEKIGYVEFNEPLDLkeerRFENHRFILIESDKVGEISSLERL----L 216
|
250 260 270
....*....|....*....|....*....|...
gi 40217847 713 MEHAGKNQVLVFVHsrkeTGKTARAIRDMCLEK 745
Cdd:TIGR01587 217 EFIKKGGSIAIIVN----TVDRAQEFYQQLKEK 245
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
477-667 |
8.47e-06 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 48.73 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 477 GFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTnvaLMCMLREIGKHINMDGTINVDDFKIIYIAPMRSLVQEmVGSFG 556
Cdd:cd17964 13 GFETMTPVQQKTLKPILSTGDDVLARAKTGTGKT---LAFLLPAIQSLLNTKPAGRRSGVSALIISPTRELALQ-IAAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 557 KRLATY--GITVAELTG----DHQLCKEEISATQIIVCTPEKW-DIITRKGGERTYTQLvRLIILDEI-HLLhdDRG--P 626
Cdd:cd17964 89 KKLLQGlrKLRVQSAVGgtsrRAELNRLRRGRPDILVATPGRLiDHLENPGVAKAFTDL-DYLVLDEAdRLL--DMGfrP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 40217847 627 VLEALvaraIRNIEMTQEDVRLIGL-SATLPnyEDVATFLRV 667
Cdd:cd17964 166 DLEQI----LRHLPEKNADPRQTLLfSATVP--DEVQQIARL 201
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
1345-1495 |
9.70e-06 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 48.63 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1345 NVFVGAPTGSGKTICAEFAILRML----LQSSEGRCVYITPMEALAEQvymdWYEKFQDRLNK--KVVLLTGETSTDL-- 1416
Cdd:cd18036 19 NTIICAPTGSGKTRVAVYICRHHLekrrSAGEKGRVVVLVNKVPLVEQ----QLEKFFKYFRKgyKVTGLSGDSSHKVsf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1417 -KLLGKGNIIISTPEKW--DILSRRWKQRKNVQNINLFVVDEVHLIGGeNGPVLEVICSRMRY-ISSQIERPiRIVALSS 1492
Cdd:cd18036 95 gQIVKASDVIICTPQILinNLLSGREEERVYLSDFSLLIFDECHHTQK-EHPYNKIMRMYLDKkLSSQGPLP-QILGLTA 172
|
...
gi 40217847 1493 SLS 1495
Cdd:cd18036 173 SPG 175
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1299-1417 |
1.03e-05 |
|
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: 50.47 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1299 TELLDLQPLPVSALRNSAFESLYQDKFPF---FNPIQTQVFNTVYNS---DDNVFV-GAPTGSGKTICAEFAILRMLLQS 1371
Cdd:COG1203 96 SANFDMARQALDHLLAERLERLLPKKSKPrtpINPLQNEALELALEAaeeEPGLFIlTAPTGGGKTEAALLFALRLAAKH 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 40217847 1372 SEGRCVYITPMEALAEQvyMdwYEKFQDRLNKKVVLLTGETSTDLK 1417
Cdd:COG1203 176 GGRRIIYALPFTSIINQ--T--YDRLRDLFGEDVLLHHSLADLDLL 217
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
1330-1455 |
1.21e-05 |
|
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: 48.53 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1330 PIQTQVFNTVYNSDDNVFVgAPTGSGKTICAEFAILRML-----LQSSEGRCVYI-TPMEALAEQVYMDwYEKFQDRLNK 1403
Cdd:cd17953 37 PIQAQALPAIMSGRDVIGI-AKTGSGKTLAFLLPMFRHIkdqrpVKPGEGPIGLImAPTRELALQIYVE-CKKFSKALGL 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 40217847 1404 KVVLLTGETS-----TDLKllgKG-NIIISTPEKW-DILSRRWKQRKNVQNINLFVVDE 1455
Cdd:cd17953 115 RVVCVYGGSGiseqiAELK---RGaEIVVCTPGRMiDILTANNGRVTNLRRVTYVVLDE 170
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
497-654 |
2.15e-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: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 497 ENLLLCAPTGAGKTNVALMCMLreigkhinmdgtinvdDF-------KIIYIAPMRSLV-QEMVgsfgkrlATYGIT--- 565
Cdd:cd18033 17 QNTLVALPTGLGKTFIAAVVML----------------NYyrwfpkgKIVFMAPTKPLVsQQIE-------ACYKITgip 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 566 ---VAELTGdhQLCK----EEISATQIIVCTPEKWDIITRKGgeRTYTQLVRLIILDEIHllhddRGP-------VLEAL 631
Cdd:cd18033 74 ssqTAELTG--SVPPtkraELWASKRVFFLTPQTLENDLKEG--DCDPKSIVCLVIDEAH-----RATgnyaycqVVREL 144
|
170 180
....*....|....*....|...
gi 40217847 632 VARAIRniemtqedVRLIGLSAT 654
Cdd:cd18033 145 MRYNSH--------FRILALTAT 159
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
1328-1457 |
2.55e-05 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 47.36 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1328 FNPIQTQVFNTVYnSDDNVFVGAPTGSGKTICAEFAILrmllqSSEGRCVYITPMEALAE-QVymdWYEKfqdRLNKKVV 1406
Cdd:cd18015 19 FRPLQLETINATM-AGRDVFLVMPTGGGKSLCYQLPAL-----CSDGFTLVVSPLISLMEdQL---MALK---KLGISAT 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40217847 1407 LLTGETSTD-----LKLLGKGN----IIISTPEKWdILSRRWKQR----KNVQNINLFVVDEVH 1457
Cdd:cd18015 87 MLNASSSKEhvkwvHAALTDKNselkLLYVTPEKI-AKSKRFMSKlekaYNAGRLARIAIDEVH 149
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1302-1455 |
6.04e-05 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 47.83 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1302 LDLQPLPVSALRNSAFESLyqdkfpffNPIQTQVFNTVYNSDDnVFVGAPTGSGKTicAEFA--ILRMLLQSSEG--RCV 1377
Cdd:COG0513 7 LGLSPPLLKALAELGYTTP--------TPIQAQAIPLILAGRD-VLGQAQTGTGKT--AAFLlpLLQRLDPSRPRapQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1378 YITPMEALAEQVY--MDWYEKFqdrLNKKVVLLTGETS--TDLKLLGKG-NIIISTPekwdilsRR----WKQRK-NVQN 1447
Cdd:COG0513 76 ILAPTRELALQVAeeLRKLAKY---LGLRVATVYGGVSigRQIRALKRGvDIVVATP-------GRlldlIERGAlDLSG 145
|
....*...
gi 40217847 1448 INLFVVDE 1455
Cdd:COG0513 146 VETLVLDE 153
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
497-616 |
1.18e-04 |
|
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: 45.27 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 497 ENLLLCAPTGAGKTNVALMCMLREIGKHINMDGtinvddFKIIYIAPMRSLVQEMVGSFGKRLATYGITVAELT-GDHQL 575
Cdd:cd17957 28 RDLLACAPTGSGKTLAFLIPILQKLGKPRKKKG------LRALILAPTRELASQIYRELLKLSKGTGLRIVLLSkSLEAK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 40217847 576 CKEEISATQ---IIVCTPEKwdIITRKGGERTYTQLVRLIILDE 616
Cdd:cd17957 102 AKDGPKSITkydILVSTPLR--LVFLLKQGPIDLSSVEYLVLDE 143
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
490-655 |
2.08e-04 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438711 [Multi-domain] Cd Length: 174 Bit Score: 44.24 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 490 RAALETDENLLLCAPTGAGKTNVALMCMLREIGkhiNMDGtinvddfKIIYIAP----MRSLVQEMVGSFGKRL-ATYGI 564
Cdd:cd17990 11 RAALDAGGQVVLEAPPGAGKTTRVPLALLAELW---IAGG-------KIIVLEPrrvaARAAARRLATLLGEAPgETVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 565 TVaelTGDHQLCKeeisATQIIVCTPekwDIITRKGGERTYTQLVRLIILDEIH--LLHDDRGPVLEALVARAIRniemt 642
Cdd:cd17990 81 RV---RGESRVGR----RTRVEVVTE---GVLLRRLQRDPELSGVGAVILDEFHerSLDADLALALLLEVQQLLR----- 145
|
170
....*....|...
gi 40217847 643 qEDVRLIGLSATL 655
Cdd:cd17990 146 -DDLRLLAMSATL 157
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
1330-1455 |
3.62e-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: 44.15 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1330 PIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVY----------ITPMEALAEQVyMDWYEKFQD 1399
Cdd:cd17946 15 PIQALALPAAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGgkqkplraliLTPTRELAVQV-KDHLKAIAK 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1400 RLNKKVVLLTGETST--DLKLLGKG-NIIISTPEK-WDILSRRWKQRKNVQNINLFVVDE 1455
Cdd:cd17946 94 YTNIKIASIVGGLAVqkQERLLKKRpEIVVATPGRlWELIQEGNEHLANLKSLRFLVLDE 153
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
1353-1428 |
3.80e-04 |
|
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: 44.06 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1353 GSGKTICAEFAILRMLLQSseGRCVYITPMEALAEQVYmDWYEKFQDRLNKKVVLLTGETSTD-----LKLL--GKGNII 1425
Cdd:cd17992 76 GSGKTVVAALAMLAAVENG--YQVALMAPTEILAEQHY-DSLKKLLEPLGIRVALLTGSTKAKekreiLEKIasGEIDIV 152
|
...
gi 40217847 1426 IST 1428
Cdd:cd17992 153 IGT 155
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
1321-1493 |
8.45e-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: 42.31 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1321 YQdkfpfFNPIQTQVFNtvynsddNVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEQvYMDWYEKFQDR 1400
Cdd:cd18033 6 YQ-----FTIVQKALFQ-------NTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQ-QIEACYKITGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1401 LNKKVVLLTGETSTD--LKLLGKGNIIISTPEKW--DILsrrwKQRKNVQNINLFVVDEVHLIGGeNGPVLEVICSRMRY 1476
Cdd:cd18033 73 PSSQTAELTGSVPPTkrAELWASKRVFFLTPQTLenDLK----EGDCDPKSIVCLVIDEAHRATG-NYAYCQVVRELMRY 147
|
170
....*....|....*..
gi 40217847 1477 ISSqierpIRIVALSSS 1493
Cdd:cd18033 148 NSH-----FRILALTAT 159
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
492-655 |
1.19e-03 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 41.52 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 492 ALETDENLLLCAPTGAGKTNV--ALMCMLREigkhinmdgtinvddFKIIYIAPMRSLVQEMVgsfgKRLATYGITVA-- 567
Cdd:cd17926 14 AHKNNRRGILVLPTGSGKTLTalALIAYLKE---------------LRTLIVVPTDALLDQWK----ERFEDFLGDSSig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 568 ELTGDHQLCKEEISatqIIVCTpekWDIITRKGGE-RTYTQLVRLIILDEIHLLHddrGPVLEALVARAIRNiemtqedv 646
Cdd:cd17926 75 LIGGGKKKDFDDAN---VVVAT---YQSLSNLAEEeKDLFDQFGLLIVDEAHHLP---AKTFSEILKELNAK-------- 137
|
....*....
gi 40217847 647 RLIGLSATL 655
Cdd:cd17926 138 YRLGLTATP 146
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
479-618 |
1.29e-03 |
|
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: 42.12 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 479 KTLNRIQSKLYRAALeTDENLLLCAPTGAGKTNVALMcmlreIGKHiNMDGTINVDDFKIIYIAPMRSLVQEMVGSFGKR 558
Cdd:cd18073 1 FKPRNYQLELALPAM-KGKNTIICAPTGCGKTFVSLL-----ICEH-HLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKY 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40217847 559 LATYGITVAELTGD---HQLCKEEISATQIIVCTPEkwdIITR--KGGERTYTQLVRLIILDEIH 618
Cdd:cd18073 74 FERHGYRVTGISGAtaeNVPVEQIIENNDIIILTPQ---ILVNnlKKGTIPSLSIFTLMIFDECH 135
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
503-616 |
1.39e-03 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 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: 350703 [Multi-domain] Cd Length: 220 Bit Score: 42.31 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 503 APTGAGKTNVALMCMLREIGKHINMDGTINVDDFKIIYIAPMRSLVQEMVGSFGKRLATYGITVAELTGDHQLckEEISA 582
Cdd:cd17945 34 AETGSGKTAAFLIPLLVYISRLPPLDEETKDDGPYALILAPTRELAQQIEEETQKFAKPLGIRVVSIVGGHSI--EEQAF 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 40217847 583 T-----QIIVCTPEKW-DIItrkggERTYTQLVRL--IILDE 616
Cdd:cd17945 112 SlrngcEILIATPGRLlDCL-----ERRLLVLNQCtyVVLDE 148
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
476-616 |
1.64e-03 |
|
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 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: 350710 [Multi-domain] Cd Length: 197 Bit Score: 42.02 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 476 EGFKTLNRIQSKLYRAALeTDENLLLCAPTGAGKTNVALMCML------REIGKHinmDGTINVddfkiiYIAPMRSLVQ 549
Cdd:cd17952 8 QEYEQPTPIQAQALPVAL-SGRDMIGIAKTGSGKTAAFIWPMLvhimdqRELEKG---EGPIAV------IVAPTRELAQ 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40217847 550 EM---VGSFGKRlatYGITVAELTG---DHQLCKEEISATQIIVCTPEKW-DIITRKGgerTYTQLVRLIILDE 616
Cdd:cd17952 78 QIyleAKKFGKA---YNLRVVAVYGggsKWEQAKALQEGAEIVVATPGRLiDMVKKKA---TNLQRVTYLVLDE 145
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
1345-1459 |
1.72e-03 |
|
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: 41.80 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1345 NVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVY-------ITPMEALAEQVYmdwyeKFQDRLNK------KVVLLTGE 1411
Cdd:cd17961 33 DILARARTGSGKTAAYALPIIQKILKAKAESGEEqgtraliLVPTRELAQQVS-----KVLEQLTAycrkdvRVVNLSAS 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 40217847 1412 TSTDLK---LLGKGNIIISTPEK-WDILSRrwKQRKNVQNINLFVVDEVHLI 1459
Cdd:cd17961 108 SSDSVQralLAEKPDIVVSTPARlLSHLES--GSLLLLSTLKYLVIDEADLV 157
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
758-858 |
1.99e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 41.10 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 758 STEVLRTEAEQCKNLELKDLLP-YGFAIHHAGMT--RVDRTLVEdlFADKHIQVLVSTATLAWGVNLPAHTVIIkgtqVY 834
Cdd:cd18792 38 ESEKLDLKSIEALAEELKELVPeARVALLHGKMTedEKEAVMLE--FREGEYDILVSTTVIEVGIDVPNANTMI----IE 111
|
90 100
....*....|....*....|....
gi 40217847 835 SPEKgrwteLGALDILQMLGRAGR 858
Cdd:cd18792 112 DADR-----FGLSQLHQLRGRVGR 130
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
1309-1455 |
2.53e-03 |
|
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 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: 350710 [Multi-domain] Cd Length: 197 Bit Score: 41.25 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1309 VSALRNSAFESlyqdkfPffNPIQTQVFNTVYNSDDNVFVgAPTGSGKTicAEFaILRML--------LQSSEGR-CVYI 1379
Cdd:cd17952 2 LNAIRKQEYEQ------P--TPIQAQALPVALSGRDMIGI-AKTGSGKT--AAF-IWPMLvhimdqreLEKGEGPiAVIV 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40217847 1380 TPMEALAEQVYMDwYEKFQDRLNKKVVLLTGETST--DLKLLGKG-NIIISTPEKwdILSRRWKQRKNVQNINLFVVDE 1455
Cdd:cd17952 70 APTRELAQQIYLE-AKKFGKAYNLRVVAVYGGGSKweQAKALQEGaEIVVATPGR--LIDMVKKKATNLQRVTYLVLDE 145
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
1350-1456 |
3.50e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain] Cd Length: 189 Bit Score: 40.77 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1350 APTGSGKTIcaeF-AILRMLLQSSEGRCVYITPMEALAEQVYmDWYEKFQDRLNKKVVLL-------TGETSTDLKLLGK 1421
Cdd:cd17924 39 APTGVGKTT---FgLATSLYLASKGKRSYLIFPTKSLVKQAY-ERLSKYAEKAGVEVKILvyhsrlkKKEKEELLEKIEK 114
|
90 100 110
....*....|....*....|....*....|....*..
gi 40217847 1422 G--NIIISTPEkwdILSRRWKQRKNvQNINLFVVDEV 1456
Cdd:cd17924 115 GdfDILVTTNQ---FLSKNFDLLSN-KKFDFVFVDDV 147
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
1330-1429 |
3.61e-03 |
|
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: 41.20 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1330 PIQTQVFNTVYNSDdNVFVGAPTGSGKTICAEFAILRMLLQSSEG--------RCVYITPMEALAEQVYMDwYEKFQDRL 1401
Cdd:cd17948 15 TVQKQGIPSILRGR-NTLCAAETGSGKTLTYLLPIIQRLLRYKLLaegpfnapRGLVITPSRELAEQIGSV-AQSLTEGL 92
|
90 100 110
....*....|....*....|....*....|.
gi 40217847 1402 NKKV-VLLTGETSTDLKL--LGKGNIIISTP 1429
Cdd:cd17948 93 GLKVkVITGGRTKRQIRNphFEEVDILVATP 123
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
477-590 |
5.31e-03 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 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: 350699 [Multi-domain] Cd Length: 198 Bit Score: 40.35 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 477 GFKTLNRIQSKLYRAALEtDENLLLCAPTGAGKTnvalMCMLREIGKHINMDGTINVDDFKIIYIAPMRSLVQEMVGSFg 556
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQ-GRDILGAAKTGSGKT----LAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQIFEVL- 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 40217847 557 KRLATYGITVAEL-TG--DHQLCKEEISATQIIVCTP 590
Cdd:cd17941 83 RKVGKYHSFSAGLiIGgkDVKEEKERINRMNILVCTP 119
|
|
| DEXQc_Suv3 |
cd17913 |
DEXQ-box helicase domain of Suv3; Suppressor of var1 3-like protein (Suv3) is a DNA/RNA ... |
1351-1460 |
5.80e-03 |
|
DEXQ-box helicase domain of Suv3; Suppressor of var1 3-like protein (Suv3) is a DNA/RNA unwinding enzyme belonging to the class of DexH-box helicases. It localizes predominantly in the mitochondria, where it forms an RNA-degrading complex called mitochondrial degradosome (mtEXO) with exonuclease PNP (polynucleotide phosphorylase), that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Suv3 plays a role in the RNA surveillance system in mitochondria; it regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. It also confers salinity and drought stress tolerance by maintaining both photosynthesis and antioxidant machinery, probably via an increase in plant hormone levels such as gibberellic acid (GA3), the cytokinin zeatin (Z), and indole-3-acetic acid (IAA). Suv3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350671 [Multi-domain] Cd Length: 142 Bit Score: 39.08 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1351 PTGSGKTicaeFAILRMLLQSSEGrcVYITPMEALAEQVYmdwyekfqDRLNKKVV---LLTGEtstDLKLLGKGNIIIS 1427
Cdd:cd17913 9 PTNSGKT----YHALQRLKSAKSG--VYCGPLRLLAWEVY--------ERLNAEGVpcdLVTGQ---ERREVEGATHVSC 71
|
90 100 110
....*....|....*....|....*....|...
gi 40217847 1428 TPEKWDIlSRRWkqrknvqniNLFVVDEVHLIG 1460
Cdd:cd17913 72 TVEMASI-SEPY---------DVAVIDEIQMIG 94
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
758-858 |
6.28e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It 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: 350198 [Multi-domain] Cd Length: 159 Bit Score: 39.63 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 758 STEVLRTEAEQCKNLELKDLLP--YGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIkgtqVYS 835
Cdd:cd18811 38 ESEKLDLKAAVAMYEYLKERFRpeLNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMV----IED 113
|
90 100
....*....|....*....|...
gi 40217847 836 PEKgrwteLGALDILQMLGRAGR 858
Cdd:cd18811 114 AER-----FGLSQLHQLRGRVGR 131
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1350-1456 |
6.62e-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: 40.72 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 1350 APTGSGKTicAEF--AILRMLL-------QSSEGR---CVYITPMEALAEQVYMDwYEKFQDRLNKKVVLLTGETST--D 1415
Cdd:cd18052 87 AQTGSGKT--AAFllPVLTGMMkegltasSFSEVQepqALIVAPTRELANQIFLE-ARKFSYGTCIRPVVVYGGVSVghQ 163
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 40217847 1416 LKLLGKG-NIIISTPEKW-DILSRRwkqRKNVQNINLFVVDEV 1456
Cdd:cd18052 164 IRQIEKGcHILVATPGRLlDFIGRG---KISLSKLKYLILDEA 203
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1617-1665 |
7.83e-03 |
|
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: 37.96 E-value: 7.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 40217847 1617 VGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNV-AAHLVIIMD 1665
Cdd:pfam00271 41 VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLpDVDLVINYD 90
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
477-664 |
7.91e-03 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350721 [Multi-domain] Cd Length: 196 Bit Score: 39.87 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 477 GFKTLNRIQSklyrAAL-----ETDENLLLCAPTGAGKTNVALMCMLREIgkhinmDGTINVDdfKIIYIAPMRSLVQ-- 549
Cdd:cd17963 13 GFNKPSKIQE----TALplilsDPPENLIAQSQSGTGKTAAFVLAMLSRV------DPTLKSP--QALCLAPTRELARqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 550 -EMVGSFGKRLatyGITVA-ELTGDHQLCKEEISAtQIIVCTPEK-WDIITRKggeRTYTQLVRLIILDEIHLLHDDRGp 626
Cdd:cd17963 81 gEVVEKMGKFT---GVKVAlAVPGNDVPRGKKITA-QIVIGTPGTvLDWLKKR---QLDLKKIKILVLDEADVMLDTQG- 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 40217847 627 vleaLVARAIRNIEMTQEDVRLIGLSATLPnyEDVATF 664
Cdd:cd17963 153 ----HGDQSIRIKRMLPRNCQILLFSATFP--DSVRKF 184
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
485-652 |
9.72e-03 |
|
orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274354 [Multi-domain] Cd Length: 365 Bit Score: 40.69 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 485 QSKLYRAAL------ETDENLLLCAPTGAGKTNVA--LMCMLREIGKHINMD---GTINVDDFKIIYIApMRSLVQEmVG 553
Cdd:TIGR02928 23 QIEELAKALrpilrgSRPSNVFIYGKTGTGKTAVTkyVMKELEEAAEDRDVRvvtVYVNCQILDTLYQV-LVELANQ-LR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40217847 554 SFGKRLATYGITVAELTGdhqlckeeisatqiivctpEKWDIItrkggERTYTQLVrlIILDEIHLLHDDRGPVLEALVa 633
Cdd:TIGR02928 101 GSGEEVPTTGLSTSEVFR-------------------RLYKEL-----NERGDSLI--IVLDEIDYLVGDDDDLLYQLS- 153
|
170
....*....|....*....
gi 40217847 634 RAIRNIEMTQEDVRLIGLS 652
Cdd:TIGR02928 154 RARSNGDLDNAKVGVIGIS 172
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