|
Name |
Accession |
Description |
Interval |
E-value |
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1007-1310 |
1.08e-143 |
|
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.
Pssm-ID: 460740 Cd Length: 307 Bit Score: 448.96 E-value: 1.08e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1007 TDLGRIASYYYISHGTIAAYNENLKPTMNDIELCRLFSLSEEFKYVTVRQDEKMELAKLLDRVPIPVKETLEDPSAKINV 1086
Cdd:pfam02889 2 TDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKGDIEDPHAKVNI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1087 LLQVYISKLKLEGLSLTSDMVYITQSAGRLLRAIFEIVLKRGWAQLSQKALNLSKMVGKRMWSVQTPLWQFPGIPKEILM 1166
Cdd:pfam02889 82 LLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPELIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1167 KLEKNDLVWER--YYDLSSQELGELICNPKMGRPLHKYIHQFPKLKLAAHVQPISRSVLQVELTVTPDFHWDDKANKYVE 1244
Cdd:pfam02889 162 KLEKKGVESVRdiLELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGKSE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227913 1245 PFWIIVEDNDGEKILHHEYFLFKKRVIDEDHTLNFTVPISEPIPPQYFIRVVSDKWLDSPTVLPVS 1310
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 ... |
489-702 |
1.58e-128 |
|
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: 402.13 E-value: 1.58e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 489 ISDLPEWAQPAFRGMQQLNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHQLGLNMNPGGTFNHGNYKIVYVAP 568
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGTINLDAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 569 MKALVAEVVDSLSQRLKDFGVTVKELSGDQSLTGQEIKETQIIVTTPEKWDIITRKSGDRTYTQLVRLLIIDEIHLLDDN 648
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15227913 649 RGPVLESIVARTLRQIESTKEHIRLVGLSATLPNCDDVASFLRVDLKNGLFIFD 702
Cdd:cd18019 161 RGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1003-1312 |
5.49e-113 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 361.96 E-value: 5.49e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1003 HFQVTDLGRIASYYYISHGTIAAYNENLKPTMNDIELCRLFSLSEEFKYVTVRQDEKMELAKLLDRVPIPVK-ETLEDPS 1081
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLEnPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1082 AKINVLLQVYISKLKLEGLSLTSDMVYITQSAGRLLRAIFEIVLKRGWAQLSQKALNLSKMVGKRMWSVQTPLWQFPGIP 1161
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1162 KEILMKLEKND-LVWERYYDLSSQELGELI-CNPKMGRPLHKYIHQFPKLKLAAHVQPISRSVLQVELTVTPDFHWDDKA 1239
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLgLLDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227913 1240 NKYVEPFWIIVEDNDGEKILHHEYFLFKKRVIDEDHTLNFTVPISEPIpPQYFIRVVSDKWLDSPTVLPVSFR 1312
Cdd:smart00611 241 HGKQEGWWLVIGDSDGNELLHIERFSLNKKNVSEEVKLDFTAPATEGN-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 ... |
1349-1540 |
5.17e-111 |
|
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: 350.79 E-value: 5.17e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGPDsaMRVVYIAPLEAIAKEQFRDWEKKFGKGLG 1428
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPK--GRAVYIAPMQELVDARYKDWRAKFGPLLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1429 LRVVELTGETLLDLKLLEKGQIIISTPEKWDALSRRWKQRKYIQQVSLFIVDELHLIGGQGGQVLEVIVSRMRYISSQVG 1508
Cdd:cd18021 79 KKVVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLE 158
|
170 180 190
....*....|....*....|....*....|..
gi 15227913 1509 NKIRIVALSTSLANAKDLGEWIGASSCGVFNF 1540
Cdd:cd18021 159 KPIRIVGLSSSLANARDVGEWLGASKSTIFNF 190
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1837-2160 |
2.39e-107 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 345.78 E-value: 2.39e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1837 DLSPLNLGMIASYYYINYTTIERFSSLLASKTKMKGLLEILTSASEYDLIPIRPGEEDAVRRLINHQRFSFQNPRCTDPR 1916
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1917 VKTSALLQAHFSRQK-ISGNLVMDQCEVLLSATRLLQAMVDVISSNGCLNLALLAMEVSQMVTQGMWDRDSMLLQLPHFT 1995
Cdd:smart00611 81 VKANLLLQAHLSRLKlPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1996 KDLAKRCHEnpgNNIETIFDLVEMEDDKRQELLQMSDAQLLDIARFCNRFPNIDLTYEIVGSNEVSPGKDITLQVLLERD 2075
Cdd:smart00611 161 EEILKRLEK---KKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 2076 MEgrtevgpvdapryPKTKEEGWWLVVGEAKTNQLMAIKRISLQRKA---QVKLEFAVPTETGEKSYTLYFMCDSYLGCD 2152
Cdd:smart00611 238 DE-------------IHGKQEGWWLVIGDSDGNELLHIERFSLNKKNvseEVKLDFTAPATEGNYQYTLRLVSDSYLGCD 304
|
....*...
gi 15227913 2153 QEYSFTVD 2160
Cdd:smart00611 305 QEYPLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
488-1019 |
3.44e-104 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 345.34 E-value: 3.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 488 KISDLPEWAQPAF---RGMQQLNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHQLglnmnpggtFNHGnyKIV 564
Cdd:COG1204 2 KVAELPLEKVIEFlkeRGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKAL---------LNGG--KAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 565 YVAPMKALVAEVVDSLSQRLKDFGVTVKELSGDQSLTGQEIKETQIIVTTPEKWDIITRKSGDrtYTQLVRLLIIDEIHL 644
Cdd:COG1204 71 YIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDVDLVVVDEAHL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 645 LDD-NRGPVLESIVARtLRQIESTkehIRLVGLSATLPNCDDVASFLRVDLknglfiFDRSYRPVPLgqqYIGINVKKPL 723
Cdd:COG1204 149 IDDeSRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGVL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 724 RrFQLMNDICYQKVVAVAGKH-----QVLIFVHSRKETAKTARAIRDTAMANDTLSRFLKEDSQSREILKCLAGLLKNND 798
Cdd:COG1204 216 R-FDDGSRRSKDPTLALALDLleeggQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTNEK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 799 LKELLPYGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPAHTVIIKgtqvyNPERGEWMELSPLDVMQMI 878
Cdd:COG1204 295 LADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-----DTKRGGMVPIPVLEFKQMA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 879 GRAGRPQYDQQGEGIIITGYSKLQYYLR---LMNEQLPIESQFISKLAD--QLNAEIVLGTIQNAREACHWLGYTYLYVR 953
Cdd:COG1204 370 GRAGRPGYDPYGEAILVAKSSDEADELFeryILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQ 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227913 954 MVRNptlygvSPDALAKDLLLEerradlihsaatiLDKNNLIkyDRKSGHFQVTDLGRIASYYYIS 1019
Cdd:COG1204 450 YDKG------DLEEVVDDALEF-------------LLENGFI--EEDGDRLRATKLGKLVSRLYID 494
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1840-2157 |
1.93e-103 |
|
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: 334.17 E-value: 1.93e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1840 PLNLGMIASYYYINYTTIERFSSLLASKTKMKGLLEILTSASEYDLIPIRPGEEDAVRRLINHQRFSFQnPRCTDPRVKT 1919
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVK-GDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1920 SALLQAHFSRQKISGN-LVMDQCEVLLSATRLLQAMVDVISSNGCLNLALLAMEVSQMVTQGMWDRDSMLLQLPHFTKDL 1998
Cdd:pfam02889 80 NILLQAYISRLKLPGFaLVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1999 AKRCHEnpgNNIETIFDLVEMEDDKRQELLQMSDAQLLDIARFCNRFPNIDLTYEIvgsnEVSPGKDITLQVLLERDMEg 2078
Cdd:pfam02889 160 IKKLEK---KGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEV----QPITRSVLRVEVTITPDFP- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 2079 rtevgpvdAPRYPKTKEEGWWLVVGEAKTNQLMAIKRISLQRKAQ---VKLEFAVP-TETGEKSYTLYFMCDSYLGCDQE 2154
Cdd:pfam02889 232 --------WDKRVHGKSEGFWLVVGDSDGNEILHIERFTLTKRTLageHKLEFTVPpSDPGPPQLFVRLISDSWLGADQE 303
|
...
gi 15227913 2155 YSF 2157
Cdd:pfam02889 304 VPI 306
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1349-1877 |
1.99e-76 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 264.83 E-value: 1.99e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGPdsamRVVYIAPLEAIAKEQFRDWEKKFGKgLG 1428
Cdd:COG1204 20 IEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----KALYIVPLRALASEKYREFKRDFEE-LG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1429 LRVVELTGETLLDLKLLEKGQIIISTPEKWDALSRrwKQRKYIQQVSLFIVDELHLIGGQG-GQVLEVIVSRMRYISSQv 1507
Cdd:COG1204 95 IKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDDESrGPTLEVLLARLRRLNPE- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1508 gnkIRIVALSTSLANAKDLGEWIGASscgvfNFPPNVRPVPLEIHIHGVDILSFEARMQAMTKPTYTAIVQHAKNKKPAI 1587
Cdd:COG1204 172 ---AQIVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNEGVLYDGVLRFDDGSRRSKDPTLALALDLLEEGGQVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1588 VFVPTRKHVRLTAVDLIaySHMDNMKSPDfLLGNLEELEPFLIQICEET-----LKETLRHGIGYLHEGLSNLDQEIVTQ 1662
Cdd:COG1204 244 VFVSSRRDAESLAKKLA--DELKRRLTPE-EREELEELAEELLEVSEEThtnekLADCLEKGVAFHHAGLPSELRRLVED 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1663 LFEAGRIQVCVMSSSLCWG--TPLKAhlvVVMGTHFYDGREnshsdyPISNL--LQMMGRGSRPLLDDAGKCVIFC--HA 1736
Cdd:COG1204 321 AFREGLIKVLVATPTLAAGvnLPARR---VIIRDTKRGGMV------PIPVLefKQMAGRAGRPGYDPYGEAILVAksSD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1737 PRKEYYKKFLY-EALPVESHL--QHFLHDNFNAEVVARVIENKQDAVDYLTWSFMYrrlpqnpnyynllgvsHRHLSDHL 1813
Cdd:COG1204 392 EADELFERYILgEPEPIRSKLanESALRTHLLALIASGFANSREELLDFLENTFYA----------------YQYDKGDL 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227913 1814 SELVENTLSDLEVSKCIEIDNELdLSPLNLGMIASYYYINYTTIERFSSLLASKTKMKGLLEIL 1877
Cdd:COG1204 456 EEVVDDALEFLLENGFIEEDGDR-LRATKLGKLVSRLYIDPLTAAELVDGLRKADEEFTDLGLL 518
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
706-896 |
3.80e-65 |
|
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: 217.81 E-value: 3.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 706 RPVPLGQQYIGINVKKPLRRFQLM-----NDICYQKVVAVAGKHQVLIFVHSRKETAKTARAIRdtamandtlsrflked 780
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMnkfdsDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 781 sqsreilkclagllknndlkellpyGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPAHTVIIKGTQVYN 860
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 15227913 861 PERgeWMELSPLDVMQMIGRAGRPQYDQQGEGIIIT 896
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMT 153
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
520-1018 |
2.90e-51 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 194.33 E-value: 2.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 520 KADNILLCAPTGAGKTNVAVLTILHqlglnmnpggTFNHgNYKIVYVAPMKALVAEVVDSLSqRLKDFGVTVKELSGDQS 599
Cdd:PRK01172 36 KGENVIVSVPTAAGKTLIAYSAIYE----------TFLA-GLKSIYIVPLRSLAMEKYEELS-RLRSLGMRVKISIGDYD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 600 LTGQEIKETQIIVTTPEKWDIITRKsgDRTYTQLVRLLIIDEIHLL-DDNRGPVLESiVARTLRQIEStkeHIRLVGLSA 678
Cdd:PRK01172 104 DPPDFIKRYDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIgDEDRGPTLET-VLSSARYVNP---DARILALSA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 679 TLPNCDDVASFLRVDLknglfiFDRSYRPVPLGqqyIGINVKKPL-----RRFQLMNDICYQKVVAVAGkhQVLIFVHSR 753
Cdd:PRK01172 178 TVSNANELAQWLNASL------IKSNFRPVPLK---LGILYRKRLildgyERSQVDINSLIKETVNDGG--QVLVFVSSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 754 KETAKTARairdtamandTLSRFLKEDSQsreilkcLAGLLKNND-----LKELLPYGFAIHHAGLTRTDREIVENQFRW 828
Cdd:PRK01172 247 KNAEDYAE----------MLIQHFPEFND-------FKVSSENNNvyddsLNEMLPHGVAFHHAGLSNEQRRFIEEMFRN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 829 GNLQVLISTATLAWGVNLPAHTVIIKGTQVYNpeRGEWMELSPLDVMQMIGRAGRPQYDQQGEGIII----TGYSKLQYY 904
Cdd:PRK01172 310 RYIKVIVATPTLAAGVNLPARLVIVRDITRYG--NGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYIYaaspASYDAAKKY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 905 LRlmNEQLPIESQFISKLADQLN--AEIVLGTIQNAREachwlgytylyVRMVRNPTLYGVSPDalaKDlLLEERradlI 982
Cdd:PRK01172 388 LS--GEPEPVISYMGSQRKVRFNtlAAISMGLASSMED-----------LILFYNETLMAIQNG---VD-EIDYY----I 446
|
490 500 510
....*....|....*....|....*....|....*.
gi 15227913 983 HSAATILDKNNLIKydrKSGHFQVTDLGRIASYYYI 1018
Cdd:PRK01172 447 ESSLKFLKENGFIK---GDVTLRATRLGKLTSDLYI 479
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1337-1889 |
1.30e-45 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 178.09 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1337 LRNPSYETLYqdfkhfnPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEgpdSAMRVVYIAPLEAIAKEQF 1416
Cdd:PRK00254 16 LKERGIEELY-------PPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR---EGGKAVYLVPLKALAEEKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1417 R---DWEKkfgkgLGLRVVELTGETLLDLKLLEKGQIIISTPEKWDALSRRwkQRKYIQQVSLFIVDELHLIGGQG-GQV 1492
Cdd:PRK00254 86 RefkDWEK-----LGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRH--GSSWIKDVKLVVADEIHLIGSYDrGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1493 LEVIVSRMRyissqvgNKIRIVALSTSLANAKDLGEWIGASScgvfnFPPNVRPVPLEIHIHGVDILSFE-ARMQAMTKP 1571
Cdd:PRK00254 159 LEMILTHML-------GRAQILGLSATVGNAEELAEWLNAEL-----VVSDWRPVKLRKGVFYQGFLFWEdGKIERFPNS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1572 TYTAIVQHAKNKKPAIVFVPTRKHVRLTAVDLiayshmdNMKSPDFL----LGNLEELEPFLIQI-CEETLKETLRHGIG 1646
Cdd:PRK00254 227 WESLVYDAVKKGKGALVFVNTRRSAEKEALEL-------AKKIKRFLtkpeLRALKELADSLEENpTNEKLKKALRGGVA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1647 YLHEGLSNLDQEIVTQLFEAGRIQVCVMSSSLCWGTPLKAHLVVVMGTHFYDgrENSHSDYPISNLLQMMGRGSRPLLDD 1726
Cdd:PRK00254 300 FHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1727 AGKCVIFCHA--PRK--EYYKK----FLYEALPVEShlqhflhdNFNAEVVARV----IENKQDAVDYLTWSFMYRrlpQ 1794
Cdd:PRK00254 378 VGEAIIVATTeePSKlmERYIFgkpeKLFSMLSNES--------AFRSQVLALItnfgVSNFKELVNFLERTFYAH---Q 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1795 NPNYYnllgvshrhlsdHLSELVENTLSDLEVSKCIEIDNELDLSPLNLGMIASYYYINYTTIERFSSLLASKTKMK--- 1871
Cdd:PRK00254 447 RKDLY------------SLEEKAKEIVYFLLENEFIDIDLEDRFIPLPLGIRTSQLYIDPLTAKKFKDAFPKIEKNPnpl 514
|
570
....*....|....*...
gi 15227913 1872 GLLEILTSASeyDLIPIR 1889
Cdd:PRK00254 515 GIFQLIASTP--DMTPLN 530
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
265-377 |
2.20e-40 |
|
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: 145.44 E-value: 2.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 265 EDTSLNVLDIDAYWLQRKISQEYEqkiDAQECQELAEELLKILAEGND--RDVEIKLLEHLQFEKFSLVKFLLQNRLKVV 342
Cdd:pfam18149 1 DKDSLDPHDIDAFWLQRLLSKFYG---DAIEAQKKAEEVLDILESAADdlRECENQLVELLDYDKFDLVKLLLKNRDKIV 77
|
90 100 110
....*....|....*....|....*....|....*
gi 15227913 343 WCTRLARGRDQEERNQIEEEMLGLgSELAAIVKEL 377
Cdd:pfam18149 78 WCTKLARAQSEEEKQAIEEEMRSN-PGLAWILDEL 111
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1353-1526 |
9.24e-36 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 134.29 E-value: 9.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1353 NPVQTQVFTVLYNtSDNVVVAAPTGSGKTICAEFAILrNHLEGPDSAMRVVYIAPLEAIAKEQFRDWeKKFGKGLGLRVV 1432
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPAL-EALDKLDNGPQALVLAPTRELAEQIYEEL-KKLGKGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1433 ELTG--ETLLDLKLLEKGQIIISTPEKWDALSRrwkQRKYIQQVSLFIVDELHLIGGQG-GQVLEVIVSRMRYissqvgn 1509
Cdd:pfam00270 78 SLLGgdSRKEQLEKLKGPDILVGTPGRLLDLLQ---ERKLLKNLKLLVLDEAHRLLDMGfGPDLEEILRRLPK------- 147
|
170
....*....|....*...
gi 15227913 1510 KIRIVALSTSLA-NAKDL 1526
Cdd:pfam00270 148 KRQILLLSATLPrNLEDL 165
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1545-1735 |
2.19e-35 |
|
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: 132.68 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1545 RPVPLEIHIHGVDILSFEARMQAMTKPTYTAIV----QHAKNKKPAIVFVPTRKHVRLTAVDLIayshmdnmkspdfllg 1620
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKFDSDIIVllkiETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1621 nleelepfliqiceetlketlrhGIGYLHEGLSNLDQEIVTQLFEAGRIQVCVMSSSLCWGTPLKAHLVVVMGTHFYDGR 1700
Cdd:cd18795 65 -----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGK 121
|
170 180 190
....*....|....*....|....*....|....*
gi 15227913 1701 EnsHSDYPISNLLQMMGRGSRPLLDDAGKCVIFCH 1735
Cdd:cd18795 122 G--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
507-686 |
1.34e-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: 128.13 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 507 NRVQSKVYGTALfKADNILLCAPTGAGKTNVAVLTILHQLGLNMNPggtfnhgnYKIVYVAPMKALVAEVVDSLSQRLKD 586
Cdd:pfam00270 1 TPIQAEAIPAIL-EGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG--------PQALVLAPTRELAEQIYEELKKLGKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 587 FGVTVKELSGDQSLTGQ--EIKETQIIVTTPEKWDIITRKsgdRTYTQLVRLLIIDEIH-LLDDNRGPVLESIVARtlrq 663
Cdd:pfam00270 72 LGLKVASLLGGDSRKEQleKLKGPDILVGTPGRLLDLLQE---RKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|....
gi 15227913 664 iesTKEHIRLVGLSATLP-NCDDV 686
Cdd:pfam00270 145 ---LPKKRQILLLSATLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
501-714 |
4.95e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 101.80 E-value: 4.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 501 RGMQQLNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHQLglnmnpggtFNHGNYKIVYVAPMKALVAEVVDSL 580
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAL---------KRGKGGRVLVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 581 SQRLKDFGVTVKELSGDQSLTGQEIK----ETQIIVTTPEKWDIITRKsgDRTYTQLVRLLIIDEIH-LLDDNRGPVLES 655
Cdd:smart00487 75 KKLGPSLGLKVVGLYGGDSKREQLRKlesgKTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHrLLDGGFGDQLEK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15227913 656 IVARtlrqiesTKEHIRLVGLSATLPNCDDVASFLrvdLKNGLFIFDRSYRPVPLGQQY 714
Cdd:smart00487 153 LLKL-------LPKNVQLLLLSATPPEEIENLLEL---FLNDPVFIDVGFTPLEPIEQF 201
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
479-886 |
5.73e-24 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 110.37 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 479 KFDS------NEKLVKISDLPewAQPAFRGM-----QQLNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTilhqlG 547
Cdd:COG1202 174 KFDEisattdEVDTVPVDDLD--LPPELKDLlegrgEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELA-----G 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 548 LNmnpggTFNHGNYKIVYVAPMKALVAEVVDSLSQRLKD-FGVT-------VKELSGDQSLtgqeikETQIIVTTPEKWD 619
Cdd:COG1202 247 IK-----NALEGKGKMLFLVPLVALANQKYEDFKDRYGDgLDVSirvgasrIRDDGTRFDP------NADIIVGTYEGID 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 620 IITRKS---GDrtytqlVRLLIIDEIHLLDD-NRGPVLESIVARtLRQIestKEHIRLVGLSATLPNCDDVASFLRVDLk 695
Cdd:COG1202 316 HALRTGrdlGD------IGTVVIDEVHMLEDpERGHRLDGLIAR-LKYY---CPGAQWIYLSATVGNPEELAKKLGAKL- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 696 nglFIFDrsYRPVPLGQQYIGINVKKPLRrfqLMNDIC---YQKVVAVAGKHQVLIFVHSRKETAKTARAirdtamandt 772
Cdd:COG1202 385 ---VEYE--ERPVPLERHLTFADGREKIR---IINKLVkreFDTKSSKGYRGQTIIFTNSRRRCHEIARA---------- 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 773 lsrflkedsqsreilkclagllknndlkelLPYGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPAHTVI 852
Cdd:COG1202 447 ------------------------------LGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVI 496
|
410 420 430
....*....|....*....|....*....|....*...
gi 15227913 853 IK----GtqvynperGEWmeLSPLDVMQMIGRAGRPQY 886
Cdd:COG1202 497 FDslamG--------IEW--LSVQEFHQMLGRAGRPDY 524
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1349-1517 |
1.45e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 100.64 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGPDsaMRVVYIAPLEAIAKEQFRDWEKKFGKGLG 1428
Cdd:smart00487 6 FEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKG--GRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1429 LRVVELTGETLL-DLKLLEKG--QIIISTPEKWDALSRRWKqrKYIQQVSLFIVDELHLIGGQG-GQVLEVIVSRMRyis 1504
Cdd:smart00487 84 KVVGLYGGDSKReQLRKLESGktDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHRLLDGGfGDQLEKLLKLLP--- 158
|
170
....*....|...
gi 15227913 1505 sqvgNKIRIVALS 1517
Cdd:smart00487 159 ----KNVQLLLLS 167
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
525-884 |
4.23e-20 |
|
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: 97.62 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 525 LLCAPTGAGKTNVAVLTILHQLGLNMNPGGTFNHgnykIVYVAPMKALVAEVVDSLSQRLKDFG--VTVKELSGDqslTG 602
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKEKGLH----TLYITPLRALAVDIARNLQAPIEELGlpIRVETRTGD---TS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 603 QEIKETQ------IIVTTPEKWDI-ITRKSGDRTYTQLvRLLIIDEIH-LLDDNRGPVLESIVARtLRQIEStkeHIRLV 674
Cdd:TIGR04121 105 SSERARQrkkppdILLTTPESLALlLSYPDAARLFKDL-RCVVVDEWHeLAGSKRGDQLELALAR-LRRLAP---GLRRW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 675 GLSATLPNCDDVASFL-RVDLKNGLFIFDRSYRPVPLgQQYIGINVKKP-----LRRFQLmndicyQKVVAVAGKHQ-VL 747
Cdd:TIGR04121 180 GLSATIGNLEEARRVLlGVGGAPAVLVRGKLPKAIEV-ISLLPESEERFpwaghLGLRAL------PEVYAEIDQARtTL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 748 IFVHSRketaktarairdtamandtlsrflkedSQSREILKCLagLLKNNDLKELLpygfAIHHAGLTRTDREIVENQFR 827
Cdd:TIGR04121 253 VFTNTR---------------------------SQAELWFQAL--WEANPEFALPI----ALHHGSLDREQRRWVEAAMA 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15227913 828 WGNLQVLISTATLAWGVN-LPAHTVIikgtQVYNPeRGewmeLSPLdvMQMIGRAG-RP 884
Cdd:TIGR04121 300 AGRLRAVVCTSSLDLGVDfGPVDLVI----QIGSP-KG----VARL--LQRAGRSNhRP 347
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1368-1528 |
1.80e-16 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 86.04 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1368 DNVVVAAPTGSGKTICAEFAILRNHLEGPDSamRVVYIAPLEAIAKEQFRDWEKKFGK-GLGLRVVELTGETLLDL--KL 1444
Cdd:COG1205 72 KNVVIATPTASGKSLAYLLPVLEALLEDPGA--TALYLYPTKALARDQLRRLRELAEAlGLGVRVATYDGDTPPEErrWI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1445 LEKGQIIISTPEKWDA--LSRRWKQRKYIQQVSLFIVDELHL-IGGQGGQVLEVIvSRMRYISSQVGNKIRIVALSTSLA 1521
Cdd:COG1205 150 REHPDIVLTNPDMLHYglLPHHTRWARFFRNLRYVVIDEAHTyRGVFGSHVANVL-RRLRRICRHYGSDPQFILASATIG 228
|
....*..
gi 15227913 1522 NAKDLGE 1528
Cdd:COG1205 229 NPAEHAE 235
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
790-884 |
6.30e-16 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 74.56 E-value: 6.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 790 LAGLLKNNDlkellpYGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLP-AHTVIIKGtqvynpergewME 868
Cdd:smart00490 3 LAELLKELG------IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LP 65
|
90
....*....|....*.
gi 15227913 869 LSPLDVMQMIGRAGRP 884
Cdd:smart00490 66 WSPASYIQRIGRAGRA 81
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
519-895 |
9.40e-13 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 73.77 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 519 FKADNILLCAPTGAGKTNVAVLTILHQLgLNMNPGGTFNHGNYkIVYVAPMKAL-------VAEVVDSLSQRLKDFGVTV 591
Cdd:PRK13767 45 HEGKNVLISSPTGSGKTLAAFLAIIDEL-FRLGREGELEDKVY-CLYVSPLRALnndihrnLEEPLTEIREIAKERGEEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 592 KEL-----SGD--QSLTGQEIKET-QIIVTTPEKWDIITRKSGDRTYTQLVRLLIIDEIHLLDDN-RGPVLESIVARtLR 662
Cdd:PRK13767 123 PEIrvairTGDtsSYEKQKMLKKPpHILITTPESLAILLNSPKFREKLRTVKWVIVDEIHSLAENkRGVHLSLSLER-LE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 663 QIeSTKEHIRlVGLSATLPNCDDVASFL--RVDLKNG--LFIFDRSY-RPvplgqqyIGINVKKPLRRF-----QLMNDI 732
Cdd:PRK13767 202 EL-AGGEFVR-IGLSATIEPLEEVAKFLvgYEDDGEPrdCEIVDARFvKP-------FDIKVISPVDDLihtpaEEISEA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 733 CYQKVVAVAGKHQ-VLIFVHSRKETAKTARAIRdtamandtlSRFlkEDSQSREILKClagllknndlkellpygfaiHH 811
Cdd:PRK13767 273 LYETLHELIKEHRtTLIFTNTRSGAERVLYNLR---------KRF--PEEYDEDNIGA--------------------HH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 812 AGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPaHT--VIIKGtqvynpergewmelSPLDV---MQMIGRAGRpQY 886
Cdd:PRK13767 322 SSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG-YIdlVVLLG--------------SPKSVsrlLQRIGRAGH-RL 385
|
....*....
gi 15227913 887 DQQGEGIII 895
Cdd:PRK13767 386 GEVSKGRII 394
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
799-883 |
9.79e-11 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 60.69 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 799 LKELLPYGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLP-AHTVIIkgtqvYNPERgewmelSPLDVMQM 877
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YDLPW------NPASYIQR 101
|
....*.
gi 15227913 878 IGRAGR 883
Cdd:pfam00271 102 IGRAGR 107
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
1374-1531 |
2.12e-10 |
|
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: 66.04 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1374 APTGSGKTICAEFAILRNHLEG---PDSAMRVVYIAPLEAIAKEQFRDWEKK-FGKGLGLRVVELTGETLLDLKLLEKG- 1448
Cdd:TIGR04121 35 APTGSGKTLAGFLPSLIDLAGPeapKEKGLHTLYITPLRALAVDIARNLQAPiEELGLPIRVETRTGDTSSSERARQRKk 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1449 --QIIISTPEKWDALSRRWKQRKYIQQVSLFIVDELH-LIGGQGGQVLEVIVSRMRYISSQVgnkiRIVALSTSLANAKD 1525
Cdd:TIGR04121 115 ppDILLTTPESLALLLSYPDAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPGL----RRWGLSATIGNLEE 190
|
....*.
gi 15227913 1526 LGEWIG 1531
Cdd:TIGR04121 191 ARRVLL 196
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1631-1722 |
2.48e-07 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 50.29 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1631 QICEETLKEtLRHGIGYLHEGLSNLDQEIVTQLFEAGRIQVCVMSSSLCWGTPLK-AHLVVVMGthfydgrenshSDYPI 1709
Cdd:smart00490 1 EELAELLKE-LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSP 68
|
90
....*....|...
gi 15227913 1710 SNLLQMMGRGSRP 1722
Cdd:smart00490 69 ASYIQRIGRAGRA 81
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1372-1551 |
3.56e-07 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 55.70 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1372 VAAPTGSGKTICA-EFAILRNHLEG--------PDSAMRVVYIAPLEA---------------IAKEQFRDWEKKFGKGL 1427
Cdd:PRK09751 1 VIAPTGSGKTLAAfLYALDRLFREGgedtreahKRKTSRILYISPIKAlgtdvqrnlqiplkgIADERRRRGETEVNLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1428 GLRvvelTGETLLD--LKLLEK-GQIIISTPEKWdALSRRWKQRKYIQQVSLFIVDELHLIGG-QGGQVLEVIVSRMRYI 1503
Cdd:PRK09751 81 GIR----TGDTPAQerSKLTRNpPDILITTPESL-YLMLTSRARETLRGVETVIIDEVHAVAGsKRGAHLALSLERLDAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15227913 1504 SSQVGNKIrivALSTSLANAKDLGEWIGASSCGVFNFPPNVRPVPLEI 1551
Cdd:PRK09751 156 LHTSAQRI---GLSATVRSASDVAAFLGGDRPVTVVNPPAMRHPQIRI 200
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1007-1310 |
1.08e-143 |
|
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.
Pssm-ID: 460740 Cd Length: 307 Bit Score: 448.96 E-value: 1.08e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1007 TDLGRIASYYYISHGTIAAYNENLKPTMNDIELCRLFSLSEEFKYVTVRQDEKMELAKLLDRVPIPVKETLEDPSAKINV 1086
Cdd:pfam02889 2 TDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKGDIEDPHAKVNI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1087 LLQVYISKLKLEGLSLTSDMVYITQSAGRLLRAIFEIVLKRGWAQLSQKALNLSKMVGKRMWSVQTPLWQFPGIPKEILM 1166
Cdd:pfam02889 82 LLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPELIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1167 KLEKNDLVWER--YYDLSSQELGELICNPKMGRPLHKYIHQFPKLKLAAHVQPISRSVLQVELTVTPDFHWDDKANKYVE 1244
Cdd:pfam02889 162 KLEKKGVESVRdiLELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGKSE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227913 1245 PFWIIVEDNDGEKILHHEYFLFKKRVIDEDHTLNFTVPISEPIPPQYFIRVVSDKWLDSPTVLPVS 1310
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 ... |
489-702 |
1.58e-128 |
|
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: 402.13 E-value: 1.58e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 489 ISDLPEWAQPAFRGMQQLNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHQLGLNMNPGGTFNHGNYKIVYVAP 568
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGTINLDAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 569 MKALVAEVVDSLSQRLKDFGVTVKELSGDQSLTGQEIKETQIIVTTPEKWDIITRKSGDRTYTQLVRLLIIDEIHLLDDN 648
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15227913 649 RGPVLESIVARTLRQIESTKEHIRLVGLSATLPNCDDVASFLRVDLKNGLFIFD 702
Cdd:cd18019 161 RGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1003-1312 |
5.49e-113 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 361.96 E-value: 5.49e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1003 HFQVTDLGRIASYYYISHGTIAAYNENLKPTMNDIELCRLFSLSEEFKYVTVRQDEKMELAKLLDRVPIPVK-ETLEDPS 1081
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLEnPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1082 AKINVLLQVYISKLKLEGLSLTSDMVYITQSAGRLLRAIFEIVLKRGWAQLSQKALNLSKMVGKRMWSVQTPLWQFPGIP 1161
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1162 KEILMKLEKND-LVWERYYDLSSQELGELI-CNPKMGRPLHKYIHQFPKLKLAAHVQPISRSVLQVELTVTPDFHWDDKA 1239
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLgLLDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227913 1240 NKYVEPFWIIVEDNDGEKILHHEYFLFKKRVIDEDHTLNFTVPISEPIpPQYFIRVVSDKWLDSPTVLPVSFR 1312
Cdd:smart00611 241 HGKQEGWWLVIGDSDGNELLHIERFSLNKKNVSEEVKLDFTAPATEGN-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 ... |
1349-1540 |
5.17e-111 |
|
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: 350.79 E-value: 5.17e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGPDsaMRVVYIAPLEAIAKEQFRDWEKKFGKGLG 1428
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPK--GRAVYIAPMQELVDARYKDWRAKFGPLLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1429 LRVVELTGETLLDLKLLEKGQIIISTPEKWDALSRRWKQRKYIQQVSLFIVDELHLIGGQGGQVLEVIVSRMRYISSQVG 1508
Cdd:cd18021 79 KKVVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLE 158
|
170 180 190
....*....|....*....|....*....|..
gi 15227913 1509 NKIRIVALSTSLANAKDLGEWIGASSCGVFNF 1540
Cdd:cd18021 159 KPIRIVGLSSSLANARDVGEWLGASKSTIFNF 190
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1837-2160 |
2.39e-107 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 345.78 E-value: 2.39e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1837 DLSPLNLGMIASYYYINYTTIERFSSLLASKTKMKGLLEILTSASEYDLIPIRPGEEDAVRRLINHQRFSFQNPRCTDPR 1916
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1917 VKTSALLQAHFSRQK-ISGNLVMDQCEVLLSATRLLQAMVDVISSNGCLNLALLAMEVSQMVTQGMWDRDSMLLQLPHFT 1995
Cdd:smart00611 81 VKANLLLQAHLSRLKlPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1996 KDLAKRCHEnpgNNIETIFDLVEMEDDKRQELLQMSDAQLLDIARFCNRFPNIDLTYEIVGSNEVSPGKDITLQVLLERD 2075
Cdd:smart00611 161 EEILKRLEK---KKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 2076 MEgrtevgpvdapryPKTKEEGWWLVVGEAKTNQLMAIKRISLQRKA---QVKLEFAVPTETGEKSYTLYFMCDSYLGCD 2152
Cdd:smart00611 238 DE-------------IHGKQEGWWLVIGDSDGNELLHIERFSLNKKNvseEVKLDFTAPATEGNYQYTLRLVSDSYLGCD 304
|
....*...
gi 15227913 2153 QEYSFTVD 2160
Cdd:smart00611 305 QEYPLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
488-1019 |
3.44e-104 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 345.34 E-value: 3.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 488 KISDLPEWAQPAF---RGMQQLNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHQLglnmnpggtFNHGnyKIV 564
Cdd:COG1204 2 KVAELPLEKVIEFlkeRGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKAL---------LNGG--KAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 565 YVAPMKALVAEVVDSLSQRLKDFGVTVKELSGDQSLTGQEIKETQIIVTTPEKWDIITRKSGDrtYTQLVRLLIIDEIHL 644
Cdd:COG1204 71 YIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDVDLVVVDEAHL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 645 LDD-NRGPVLESIVARtLRQIESTkehIRLVGLSATLPNCDDVASFLRVDLknglfiFDRSYRPVPLgqqYIGINVKKPL 723
Cdd:COG1204 149 IDDeSRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGVL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 724 RrFQLMNDICYQKVVAVAGKH-----QVLIFVHSRKETAKTARAIRDTAMANDTLSRFLKEDSQSREILKCLAGLLKNND 798
Cdd:COG1204 216 R-FDDGSRRSKDPTLALALDLleeggQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTNEK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 799 LKELLPYGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPAHTVIIKgtqvyNPERGEWMELSPLDVMQMI 878
Cdd:COG1204 295 LADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-----DTKRGGMVPIPVLEFKQMA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 879 GRAGRPQYDQQGEGIIITGYSKLQYYLR---LMNEQLPIESQFISKLAD--QLNAEIVLGTIQNAREACHWLGYTYLYVR 953
Cdd:COG1204 370 GRAGRPGYDPYGEAILVAKSSDEADELFeryILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQ 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227913 954 MVRNptlygvSPDALAKDLLLEerradlihsaatiLDKNNLIkyDRKSGHFQVTDLGRIASYYYIS 1019
Cdd:COG1204 450 YDKG------DLEEVVDDALEF-------------LLENGFI--EEDGDRLRATKLGKLVSRLYID 494
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1840-2157 |
1.93e-103 |
|
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: 334.17 E-value: 1.93e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1840 PLNLGMIASYYYINYTTIERFSSLLASKTKMKGLLEILTSASEYDLIPIRPGEEDAVRRLINHQRFSFQnPRCTDPRVKT 1919
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVK-GDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1920 SALLQAHFSRQKISGN-LVMDQCEVLLSATRLLQAMVDVISSNGCLNLALLAMEVSQMVTQGMWDRDSMLLQLPHFTKDL 1998
Cdd:pfam02889 80 NILLQAYISRLKLPGFaLVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1999 AKRCHEnpgNNIETIFDLVEMEDDKRQELLQMSDAQLLDIARFCNRFPNIDLTYEIvgsnEVSPGKDITLQVLLERDMEg 2078
Cdd:pfam02889 160 IKKLEK---KGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEV----QPITRSVLRVEVTITPDFP- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 2079 rtevgpvdAPRYPKTKEEGWWLVVGEAKTNQLMAIKRISLQRKAQ---VKLEFAVP-TETGEKSYTLYFMCDSYLGCDQE 2154
Cdd:pfam02889 232 --------WDKRVHGKSEGFWLVVGDSDGNEILHIERFTLTKRTLageHKLEFTVPpSDPGPPQLFVRLISDSWLGADQE 303
|
...
gi 15227913 2155 YSF 2157
Cdd:pfam02889 304 VPI 306
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
1007-1311 |
7.56e-103 |
|
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: 332.79 E-value: 7.56e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1007 TDLGRIASYYYISHGTIAAYNENLKPTMNDIELCRLFSLSEEFKYVTVRQDEKMELAKLLDRVPIPVKET-LEDPSAKIN 1085
Cdd:smart00973 2 TELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGiIDSPHAKVN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1086 VLLQVYISKLKLEGLSLTSDMVYITQSAGRLLRAIFEIVLKRGWAQLSQKALNLSKMVGKRMWSV-QTPLWQFPGI-PKE 1163
Cdd:smart00973 82 LLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEDsDSPLKQLPHFlIED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1164 ILMKLEKNDLVW--ERYYDLSSQELGELICN-PKMGRPLHKYIHQFPKLKLAAHVQPISRSV-LQVELTVTPDFHWDDKA 1239
Cdd:smart00973 162 VYDKLELKDGSRsfELLLDMNAAELGEFLNRlPPNGRLIYELLRRFPKIEVEAEVLPITRDLtLRVELEITPVFAWDLPR 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227913 1240 NKYV-EPFWIIVEDNDGEKILHHEYFLFKKRVIDEDHTLNFTVPISEPIPPQYFIRVVSDKWLDSPTVLPVSF 1311
Cdd:smart00973 242 HKGKsESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKLDFTVPLSEPGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
506-702 |
4.33e-90 |
|
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: 291.26 E-value: 4.33e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 506 LNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHQLGLNMNPGGTFNHGNYKIVYVAPMKALVAEVVDSLSQRLK 585
Cdd:cd18020 2 LNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQGGVIKKDDFKIVYIAPMKALAAEMVEKFSKRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 586 DFGVTVKELSGDQSLTGQEIKETQIIVTTPEKWDIITRKS-GDRTYTQLVRLLIIDEIHLLDDNRGPVLESIVARTLRQI 664
Cdd:cd18020 82 PLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSsGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQV 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 15227913 665 ESTKEHIRLVGLSATLPNCDDVASFLRVDLKNGLFIFD 702
Cdd:cd18020 162 ESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1351-1541 |
4.43e-90 |
|
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: 290.81 E-value: 4.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1351 HFNPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGPDsaMRVVYIAPLEAIAKEQFRDWEKKFGKGLGLR 1430
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPG--SKVVYIAPLKALVRERVDDWKKRFEEKLGKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1431 VVELTGETLLDLKLLEKGQIIISTPEKWDALSRRWKQRKYIQQVSLFIVDELHLIGGQGGQVLEVIVSRMRYISSQVGNK 1510
Cdd:cd18022 79 VVELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKP 158
|
170 180 190
....*....|....*....|....*....|.
gi 15227913 1511 IRIVALSTSLANAKDLGEWIGASSCGVFNFP 1541
Cdd:cd18022 159 VRLVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
1840-2159 |
2.58e-88 |
|
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl domain) protein in which it was found. This protein is required for assembly of functional endoplasmic reticulum translocons. Other yeast proteins containing this domain include pre-mRNA splicing helicase BRR2, HFM1 protein and putative helicases.
Pssm-ID: 214946 Cd Length: 314 Bit Score: 291.18 E-value: 2.58e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1840 PLNLGMIASYYYINYTTIERFSSLLASKTKMKGLLEILTSASEYDLIPIRPGEEDAVRRLINHQRFSFQNPRCTDPRVKT 1919
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1920 SALLQAHFSRQKISG-NLVMDQCEVLLSATRLLQAMVDVISSNGCLNLALLAMEVSQMVTQGMW-DRDSMLLQLPHFTkd 1997
Cdd:smart00973 81 NLLLQAHLSRLPLPDfDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWeDSDSPLKQLPHFL-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1998 lakrchenpgnnIETIFDLVEMEDDKRqELLQMSDAQLLDIARFCNR-FPNIDLTYEIVgsnEVSPGKDITLQVLL---E 2073
Cdd:smart00973 159 ------------IEDVYDKLELKDGSR-SFELLLDMNAAELGEFLNRlPPNGRLIYELL---RRFPKIEVEAEVLPitrD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 2074 RDMEGRTEVGPVDAPRYP--KTKEEGWWLVVGEAKTNQLMAIKRISLQRK---AQVKLEFAVP-TETGEKSYTLYFMCDS 2147
Cdd:smart00973 223 LTLRVELEITPVFAWDLPrhKGKSESWWLVVGDSDTNELLAIKRVTLRKKkksNEVKLDFTVPlSEPGPENYTVYLISDS 302
|
330
....*....|..
gi 15227913 2148 YLGCDQEYSFTV 2159
Cdd:smart00973 303 YLGCDQEVSFSL 314
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1349-1877 |
1.99e-76 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 264.83 E-value: 1.99e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGPdsamRVVYIAPLEAIAKEQFRDWEKKFGKgLG 1428
Cdd:COG1204 20 IEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----KALYIVPLRALASEKYREFKRDFEE-LG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1429 LRVVELTGETLLDLKLLEKGQIIISTPEKWDALSRrwKQRKYIQQVSLFIVDELHLIGGQG-GQVLEVIVSRMRYISSQv 1507
Cdd:COG1204 95 IKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDDESrGPTLEVLLARLRRLNPE- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1508 gnkIRIVALSTSLANAKDLGEWIGASscgvfNFPPNVRPVPLEIHIHGVDILSFEARMQAMTKPTYTAIVQHAKNKKPAI 1587
Cdd:COG1204 172 ---AQIVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNEGVLYDGVLRFDDGSRRSKDPTLALALDLLEEGGQVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1588 VFVPTRKHVRLTAVDLIaySHMDNMKSPDfLLGNLEELEPFLIQICEET-----LKETLRHGIGYLHEGLSNLDQEIVTQ 1662
Cdd:COG1204 244 VFVSSRRDAESLAKKLA--DELKRRLTPE-EREELEELAEELLEVSEEThtnekLADCLEKGVAFHHAGLPSELRRLVED 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1663 LFEAGRIQVCVMSSSLCWG--TPLKAhlvVVMGTHFYDGREnshsdyPISNL--LQMMGRGSRPLLDDAGKCVIFC--HA 1736
Cdd:COG1204 321 AFREGLIKVLVATPTLAAGvnLPARR---VIIRDTKRGGMV------PIPVLefKQMAGRAGRPGYDPYGEAILVAksSD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1737 PRKEYYKKFLY-EALPVESHL--QHFLHDNFNAEVVARVIENKQDAVDYLTWSFMYrrlpqnpnyynllgvsHRHLSDHL 1813
Cdd:COG1204 392 EADELFERYILgEPEPIRSKLanESALRTHLLALIASGFANSREELLDFLENTFYA----------------YQYDKGDL 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227913 1814 SELVENTLSDLEVSKCIEIDNELdLSPLNLGMIASYYYINYTTIERFSSLLASKTKMKGLLEIL 1877
Cdd:COG1204 456 EEVVDDALEFLLENGFIEEDGDR-LRATKLGKLVSRLYIDPLTAAELVDGLRKADEEFTDLGLL 518
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
706-896 |
3.80e-65 |
|
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: 217.81 E-value: 3.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 706 RPVPLGQQYIGINVKKPLRRFQLM-----NDICYQKVVAVAGKHQVLIFVHSRKETAKTARAIRdtamandtlsrflked 780
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMnkfdsDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 781 sqsreilkclagllknndlkellpyGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPAHTVIIKGTQVYN 860
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 15227913 861 PERgeWMELSPLDVMQMIGRAGRPQYDQQGEGIIIT 896
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMT 153
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
1352-1546 |
1.19e-62 |
|
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: 212.99 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1352 FNPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGPDSA---MRVVYIAPLEAIAKEQFRDWEKKFGKgLG 1428
Cdd:cd18023 2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPwgnRKVVYIAPIKALCSEKYDDWKEKFGP-LG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1429 LRVVELTGET-LLDLKLLEKGQIIISTPEKWDALSRRWKQRK-YIQQVSLFIVDELHLIGGQGGQVLEVIVSRMRYISSQ 1506
Cdd:cd18023 81 LSCAELTGDTeMDDTFEIQDADIILTTPEKWDSMTRRWRDNGnLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSSS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15227913 1507 VGNK------IRIVALSTSLANAKDLGEWIGASSCGVFNFPPNVRP 1546
Cdd:cd18023 161 SELRgstvrpMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
1351-1541 |
1.05e-59 |
|
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: 203.65 E-value: 1.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1351 HFNPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGPDsamRVVYIAPLEAIAKEQFRDWEKKFGKgLGLR 1430
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGG---KAVYIAPTRALVNQKEADLRERFGP-LGKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1431 VVELTGETLLDLKLLEKGQIIISTPEKWDALSRRWKQRkYIQQVSLFIVDELHLIG-GQGGQVLEVIVSRMRYISSqvgn 1509
Cdd:cd17921 77 VGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRINK---- 151
|
170 180 190
....*....|....*....|....*....|..
gi 15227913 1510 KIRIVALSTSLANAKDLGEWIGasSCGVFNFP 1541
Cdd:cd17921 152 NARFVGLSATLPNAEDLAEWLG--VEDLIRFD 181
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
505-707 |
1.20e-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: 195.65 E-value: 1.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 505 QLNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHQL-GLNMNPggtfnHGNYKIVYVAPMKALVAEVVDSLSQR 583
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLkERNPLP-----WGNRKVVYIAPIKALCSEKYDDWKEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 584 LKDFGVTVKELSGDQSLTG-QEIKETQIIVTTPEKWDIITRKSGDR-TYTQLVRLLIIDEIHLLDDNRGPVLESIVAR-- 659
Cdd:cd18023 76 FGPLGLSCAELTGDTEMDDtFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIKENRGATLEVVVSRmk 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15227913 660 ---TLRQIE-STKEHIRLVGLSATLPNCDDVASFLRVDlKNGLFIFDRSYRP 707
Cdd:cd18023 156 tlsSSSELRgSTVRPMRFVAVSATIPNIEDLAEWLGDN-PAGCFSFGESFRP 206
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
506-692 |
2.05e-55 |
|
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: 191.32 E-value: 2.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 506 LNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHqlglnmnpggTFNHGNYKIVYVAPMKALVAEVVDSLSQRLK 585
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILR----------ALATSGGKAVYIAPTRALVNQKEADLRERFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 586 DFGVTVKELSGDQSLTGQEIKETQIIVTTPEKWDIITRKSGDRtYTQLVRLLIIDEIHLLDD-NRGPVLESIVARTLRQi 664
Cdd:cd17921 72 PLGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDgERGVVLELLLSRLLRI- 149
|
170 180
....*....|....*....|....*...
gi 15227913 665 estKEHIRLVGLSATLPNCDDVASFLRV 692
Cdd:cd17921 150 ---NKNARFVGLSATLPNAEDLAEWLGV 174
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
507-702 |
1.61e-51 |
|
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: 180.26 E-value: 1.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 507 NRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHqlGLNMNPGgtfnhgnYKIVYVAPMKALVAEVVDSLSQRLKD 586
Cdd:cd18022 3 NPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFR--AFNKYPG-------SKVVYIAPLKALVRERVDDWKKRFEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 587 -FGVTVKELSGDQSLTGQEIKETQIIVTTPEKWDIITRKSGDRTYTQLVRLLIIDEIHLLDDNRGPVLESIVARTlRQIE 665
Cdd:cd18022 74 kLGKKVVELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRM-NYIS 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 15227913 666 S-TKEHIRLVGLSATLPNCDDVASFLRVDlKNGLFIFD 702
Cdd:cd18022 153 SqTEKPVRLVGLSTALANAGDLANWLGIK-KMGLFNFR 189
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
520-1018 |
2.90e-51 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 194.33 E-value: 2.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 520 KADNILLCAPTGAGKTNVAVLTILHqlglnmnpggTFNHgNYKIVYVAPMKALVAEVVDSLSqRLKDFGVTVKELSGDQS 599
Cdd:PRK01172 36 KGENVIVSVPTAAGKTLIAYSAIYE----------TFLA-GLKSIYIVPLRSLAMEKYEELS-RLRSLGMRVKISIGDYD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 600 LTGQEIKETQIIVTTPEKWDIITRKsgDRTYTQLVRLLIIDEIHLL-DDNRGPVLESiVARTLRQIEStkeHIRLVGLSA 678
Cdd:PRK01172 104 DPPDFIKRYDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIgDEDRGPTLET-VLSSARYVNP---DARILALSA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 679 TLPNCDDVASFLRVDLknglfiFDRSYRPVPLGqqyIGINVKKPL-----RRFQLMNDICYQKVVAVAGkhQVLIFVHSR 753
Cdd:PRK01172 178 TVSNANELAQWLNASL------IKSNFRPVPLK---LGILYRKRLildgyERSQVDINSLIKETVNDGG--QVLVFVSSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 754 KETAKTARairdtamandTLSRFLKEDSQsreilkcLAGLLKNND-----LKELLPYGFAIHHAGLTRTDREIVENQFRW 828
Cdd:PRK01172 247 KNAEDYAE----------MLIQHFPEFND-------FKVSSENNNvyddsLNEMLPHGVAFHHAGLSNEQRRFIEEMFRN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 829 GNLQVLISTATLAWGVNLPAHTVIIKGTQVYNpeRGEWMELSPLDVMQMIGRAGRPQYDQQGEGIII----TGYSKLQYY 904
Cdd:PRK01172 310 RYIKVIVATPTLAAGVNLPARLVIVRDITRYG--NGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYIYaaspASYDAAKKY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 905 LRlmNEQLPIESQFISKLADQLN--AEIVLGTIQNAREachwlgytylyVRMVRNPTLYGVSPDalaKDlLLEERradlI 982
Cdd:PRK01172 388 LS--GEPEPVISYMGSQRKVRFNtlAAISMGLASSMED-----------LILFYNETLMAIQNG---VD-EIDYY----I 446
|
490 500 510
....*....|....*....|....*....|....*.
gi 15227913 983 HSAATILDKNNLIKydrKSGHFQVTDLGRIASYYYI 1018
Cdd:PRK01172 447 ESSLKFLKENGFIK---GDVTLRATRLGKLTSDLYI 479
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
501-1067 |
6.17e-51 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 194.27 E-value: 6.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 501 RGMQQLNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHQLglnMNPGGtfnhgnyKIVYVAPMKALVAEVVdsl 580
Cdd:PRK00254 19 RGIEELYPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVNKL---LREGG-------KAVYLVPLKALAEEKY--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 581 sQRLKDF---GVTVKELSGDQSLTGQEIKETQIIVTTPEKWDIITRKSGdrTYTQLVRLLIIDEIHLLDD-NRGPVLESI 656
Cdd:PRK00254 86 -REFKDWeklGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRHGS--SWIKDVKLVVADEIHLIGSyDRGATLEMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 657 VARTLRQIEstkehirLVGLSATLPNCDDVASFLRVDLknglfiFDRSYRPVPL--GQQYIGINV-------KKPLRRFQ 727
Cdd:PRK00254 163 LTHMLGRAQ-------ILGLSATVGNAEELAEWLNAEL------VVSDWRPVKLrkGVFYQGFLFwedgkieRFPNSWES 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 728 LMNDicyqkvvAVAGKHQVLIFVHSRKETAKTARAIrdtamaNDTLSRFL--KEDSQSREILKCLAGLLKNNDLKELLPY 805
Cdd:PRK00254 230 LVYD-------AVKKGKGALVFVNTRRSAEKEALEL------AKKIKRFLtkPELRALKELADSLEENPTNEKLKKALRG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 806 GFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPAHTVIIKGTQVYNpERGeWMELSPLDVMQMIGRAGRPQ 885
Cdd:PRK00254 297 GVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYS-NFG-WEDIPVLEIQQMMGRAGRPK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 886 YDQQGEGIIITGYSK----LQYYLRLMNE----QLPIESQFISkladQLNAEIVLGTIQNAREACHWLGYT-YLYVRmvr 956
Cdd:PRK00254 375 YDEVGEAIIVATTEEpsklMERYIFGKPEklfsMLSNESAFRS----QVLALITNFGVSNFKELVNFLERTfYAHQR--- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 957 nptlygvspdalaKDL-LLEERRADLIHsaatILDKNNLIKYDRKSgHFQVTDLGRIASYYYISHGTIAAYN---ENLKP 1032
Cdd:PRK00254 448 -------------KDLySLEEKAKEIVY----FLLENEFIDIDLED-RFIPLPLGIRTSQLYIDPLTAKKFKdafPKIEK 509
|
570 580 590
....*....|....*....|....*....|....*
gi 15227913 1033 TMNDIELCRLFSLSEEFKYVTVRqdeKMELAKLLD 1067
Cdd:PRK00254 510 NPNPLGIFQLIASTPDMTPLNYS---RKEMEDLLD 541
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
491-1018 |
2.71e-48 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 186.32 E-value: 2.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 491 DLPEWAQPAFR--GMQQLNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHQLGLnmnpGGtfnhgnyKIVYVAP 568
Cdd:PRK02362 7 PLPEGVIEFYEaeGIEELYPPQAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIAR----GG-------KALYIVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 569 MKALVAEVVDSLSqRLKDFGVTVKELSGDQSLTGQEIKETQIIVTTPEKWDIITRKSGDrtYTQLVRLLIIDEIHLLDD- 647
Cdd:PRK02362 76 LRALASEKFEEFE-RFEELGVRVGISTGDYDSRDEWLGDNDIIVATSEKVDSLLRNGAP--WLDDITCVVVDEVHLIDSa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 648 NRGPVLESIVARTLRQIEStkehIRLVGLSATLPNCDDVASFLR----------VDLKNGLFI-----FDRSYRPVPLGQ 712
Cdd:PRK02362 153 NRGPTLEVTLAKLRRLNPD----LQVVALSATIGNADELADWLDaelvdsewrpIDLREGVFYggaihFDDSQREVEVPS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 713 QYIGINvkkplrrfqLMNDicyqkvvAVAGKHQVLIFVHSRKETAKTARAirdtamANDTLSRFLkeDSQSREILKCLAG 792
Cdd:PRK02362 229 KDDTLN---------LVLD-------TLEEGGQCLVFVSSRRNAEGFAKR------AASALKKTL--TAAERAELAELAE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 793 -LLKN------NDLKELLPYGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPAHTVIIKGTQVYNPERGe 865
Cdd:PRK02362 285 eIREVsdtetsKDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAG- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 866 wmeLSPLDVM---QMIGRAGRPQYDQQGEGIIITG-YSKLQyylRLMNEQLPIESQFI-SKLADQ--LNAEiVLGTIQN- 937
Cdd:PRK02362 364 ---MQPIPVLeyhQMAGRAGRPGLDPYGEAVLLAKsYDELD---ELFERYIWADPEDVrSKLATEpaLRTH-VLSTIASg 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 938 -AREACHWLGYtylyvrMVRnpTLYGVSPDAlakdlllEERRADLIHSAATILDKNNLIkyDRKSGHFQVTDLGRIASYY 1016
Cdd:PRK02362 437 fARTRDGLLEF------LEA--TFYATQTDD-------TGRLERVVDDVLDFLERNGMI--EEDGETLEATELGHLVSRL 499
|
..
gi 15227913 1017 YI 1018
Cdd:PRK02362 500 YI 501
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1337-1889 |
1.30e-45 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 178.09 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1337 LRNPSYETLYqdfkhfnPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEgpdSAMRVVYIAPLEAIAKEQF 1416
Cdd:PRK00254 16 LKERGIEELY-------PPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR---EGGKAVYLVPLKALAEEKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1417 R---DWEKkfgkgLGLRVVELTGETLLDLKLLEKGQIIISTPEKWDALSRRwkQRKYIQQVSLFIVDELHLIGGQG-GQV 1492
Cdd:PRK00254 86 RefkDWEK-----LGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRH--GSSWIKDVKLVVADEIHLIGSYDrGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1493 LEVIVSRMRyissqvgNKIRIVALSTSLANAKDLGEWIGASScgvfnFPPNVRPVPLEIHIHGVDILSFE-ARMQAMTKP 1571
Cdd:PRK00254 159 LEMILTHML-------GRAQILGLSATVGNAEELAEWLNAEL-----VVSDWRPVKLRKGVFYQGFLFWEdGKIERFPNS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1572 TYTAIVQHAKNKKPAIVFVPTRKHVRLTAVDLiayshmdNMKSPDFL----LGNLEELEPFLIQI-CEETLKETLRHGIG 1646
Cdd:PRK00254 227 WESLVYDAVKKGKGALVFVNTRRSAEKEALEL-------AKKIKRFLtkpeLRALKELADSLEENpTNEKLKKALRGGVA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1647 YLHEGLSNLDQEIVTQLFEAGRIQVCVMSSSLCWGTPLKAHLVVVMGTHFYDgrENSHSDYPISNLLQMMGRGSRPLLDD 1726
Cdd:PRK00254 300 FHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1727 AGKCVIFCHA--PRK--EYYKK----FLYEALPVEShlqhflhdNFNAEVVARV----IENKQDAVDYLTWSFMYRrlpQ 1794
Cdd:PRK00254 378 VGEAIIVATTeePSKlmERYIFgkpeKLFSMLSNES--------AFRSQVLALItnfgVSNFKELVNFLERTFYAH---Q 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1795 NPNYYnllgvshrhlsdHLSELVENTLSDLEVSKCIEIDNELDLSPLNLGMIASYYYINYTTIERFSSLLASKTKMK--- 1871
Cdd:PRK00254 447 RKDLY------------SLEEKAKEIVYFLLENEFIDIDLEDRFIPLPLGIRTSQLYIDPLTAKKFKDAFPKIEKNPnpl 514
|
570
....*....|....*...
gi 15227913 1872 GLLEILTSASeyDLIPIR 1889
Cdd:PRK00254 515 GIFQLIASTP--DMTPLN 530
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
265-377 |
2.20e-40 |
|
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: 145.44 E-value: 2.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 265 EDTSLNVLDIDAYWLQRKISQEYEqkiDAQECQELAEELLKILAEGND--RDVEIKLLEHLQFEKFSLVKFLLQNRLKVV 342
Cdd:pfam18149 1 DKDSLDPHDIDAFWLQRLLSKFYG---DAIEAQKKAEEVLDILESAADdlRECENQLVELLDYDKFDLVKLLLKNRDKIV 77
|
90 100 110
....*....|....*....|....*....|....*
gi 15227913 343 WCTRLARGRDQEERNQIEEEMLGLgSELAAIVKEL 377
Cdd:pfam18149 78 WCTKLARAQSEEEKQAIEEEMRSN-PGLAWILDEL 111
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
517-918 |
3.02e-40 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 161.65 E-value: 3.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 517 ALFKADNILLCAPTGAGKTNVAVLTILHQLglnmnpggtfnHGNYKIVYVAPMKALVAEVVDSLSQRlkdFG-VTVKELS 595
Cdd:COG4581 36 ALEAGRSVLVAAPTGSGKTLVAEFAIFLAL-----------ARGRRSFYTAPIKALSNQKFFDLVER---FGaENVGLLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 596 GDQSLTGqeikETQIIVTTPEkwdiITRKSGDRTYTQLVRL--LIIDEIHLLDDN-RGPVLE-SIvartlrqIESTkEHI 671
Cdd:COG4581 102 GDASVNP----DAPIVVMTTE----ILRNMLYREGADLEDVgvVVMDEFHYLADPdRGWVWEePI-------IHLP-ARV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 672 RLVGLSATLPNCDDVASFLR-----VDLKNGLFifdrsyRPVPLGQQYIGINVKKPLRRF--QLMNDICYQKVVAV---A 741
Cdd:COG4581 166 QLVLLSATVGNAEEFAEWLTrvrgeTAVVVSEE------RPVPLEFHYLVTPRLFPLFRVnpELLRPPSRHEVIEEldrG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 742 GKHQVLIFVHSRKETAKTARAIRDTAMANDtlsrflKEDSQSREILKCLA---GLLKNNDLKELLPYGFAIHHAGLTRTD 818
Cdd:COG4581 240 GLLPAIVFIFSRRGCDEAAQQLLSARLTTK------EERAEIREAIDEFAedfSVLFGKTLSRLLRRGIAVHHAGMLPKY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 819 REIVENQFRWGNLQVLISTATLAWGVNLPAHTVIIKGTQVYNPERGEwmELSPLDVMQMIGRAGRPQYDQQGEGIIITG- 897
Cdd:COG4581 314 RRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHR--PLTAREFHQIAGRAGRRGIDTEGHVVVLAPe 391
|
410 420
....*....|....*....|..
gi 15227913 898 YSKLQYYLRLMNEQL-PIESQF 918
Cdd:COG4581 392 HDDPKKFARLASARPePLRSSF 413
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
1346-1527 |
1.51e-39 |
|
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: 147.13 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1346 YQDFKHFNPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILR---NHLEgPD-----SAMRVVYIAPLEAIAKEQFR 1417
Cdd:cd18019 12 FEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILReigKHRN-PDgtinlDAFKIVYIAPMKALVQEMVG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1418 DWEKKFgKGLGLRVVELTGETLLDLKLLEKGQIIISTPEKWDALSRRWKQRKYIQQVSLFIVDELHLIGGQGGQVLEVIV 1497
Cdd:cd18019 91 NFSKRL-APYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDDRGPVLESIV 169
|
170 180 190
....*....|....*....|....*....|
gi 15227913 1498 SRMRYISSQVGNKIRIVALSTSLANAKDLG 1527
Cdd:cd18019 170 ARTIRQIEQTQEYVRLVGLSATLPNYEDVA 199
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1369-1853 |
3.63e-38 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 154.27 E-value: 3.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1369 NVVVAAPTGSGKTICAEFAILRNHLEGPDSamrvVYIAPLEAIAKEQFRDWEKKfgKGLGLRVVELTGETLLDLKLLEKG 1448
Cdd:PRK01172 39 NVIVSVPTAAGKTLIAYSAIYETFLAGLKS----IYIVPLRSLAMEKYEELSRL--RSLGMRVKISIGDYDDPPDFIKRY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1449 QIIISTPEKWDALSRRwkQRKYIQQVSLFIVDELHLIGGQG-GQVLEVIVSRMRYISSQVgnkiRIVALSTSLANAKDLG 1527
Cdd:PRK01172 113 DVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDEDrGPTLETVLSSARYVNPDA----RILALSATVSNANELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1528 EWIGASScgvfnFPPNVRPVPLEIHIHGVD--ILSFEARMQAMTKPTYTAIVQhakNKKPAIVFVPTRKHVRLTAVDLIA 1605
Cdd:PRK01172 187 QWLNASL-----IKSNFRPVPLKLGILYRKrlILDGYERSQVDINSLIKETVN---DGGQVLVFVSSRKNAEDYAEMLIQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1606 YSHMDNmkspDFLLGNLEElepfliQICEETLKETLRHGIGYLHEGLSNLDQEIVTQLFEAGRIQVCVMSSSLCWGTPLK 1685
Cdd:PRK01172 259 HFPEFN----DFKVSSENN------NVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1686 AHLVVVMGTHFYDgrenshSDY--PISNL--LQMMGRGSRPLLDDAGKCVIFCHAPRK-EYYKKFLY-EALPVESHLQHF 1759
Cdd:PRK01172 329 ARLVIVRDITRYG------NGGirYLSNMeiKQMIGRAGRPGYDQYGIGYIYAASPASyDAAKKYLSgEPEPVISYMGSQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1760 LHDNFN--AEVVARVIENKQDAVDYLTWSFMYrrlPQNpnyynllGVshrhlsDHLSELVENTLSDLEVSKCieIDNELD 1837
Cdd:PRK01172 403 RKVRFNtlAAISMGLASSMEDLILFYNETLMA---IQN-------GV------DEIDYYIESSLKFLKENGF--IKGDVT 464
|
490
....*....|....*.
gi 15227913 1838 LSPLNLGMIASYYYIN 1853
Cdd:PRK01172 465 LRATRLGKLTSDLYID 480
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
504-702 |
1.65e-37 |
|
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: 140.09 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 504 QQLNRVQSKVYgTALFKAD-NILLCAPTGAGKTNVAVLTILHQLglNMNPGGtfnhgnyKIVYVAPMKALVAEVVDSLSQ 582
Cdd:cd18021 2 KFFNPIQTQVF-NSLYNTDdNVFVGAPTGSGKTVCAELALLRHW--RQNPKG-------RAVYIAPMQELVDARYKDWRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 583 RLKD-FGVTVKELSGDQSLTGQEIKETQIIVTTPEKWDIITRKSGDRTYTQLVRLLIIDEIHLLDDNRGPVLESIVARTl 661
Cdd:cd18021 72 KFGPlLGKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRM- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15227913 662 RQIES-TKEHIRLVGLSATLPNCDDVASFLRVDlKNGLFIFD 702
Cdd:cd18021 151 RYISSqLEKPIRIVGLSSSLANARDVGEWLGAS-KSTIFNFH 191
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1353-1526 |
9.24e-36 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 134.29 E-value: 9.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1353 NPVQTQVFTVLYNtSDNVVVAAPTGSGKTICAEFAILrNHLEGPDSAMRVVYIAPLEAIAKEQFRDWeKKFGKGLGLRVV 1432
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPAL-EALDKLDNGPQALVLAPTRELAEQIYEEL-KKLGKGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1433 ELTG--ETLLDLKLLEKGQIIISTPEKWDALSRrwkQRKYIQQVSLFIVDELHLIGGQG-GQVLEVIVSRMRYissqvgn 1509
Cdd:pfam00270 78 SLLGgdSRKEQLEKLKGPDILVGTPGRLLDLLQ---ERKLLKNLKLLVLDEAHRLLDMGfGPDLEEILRRLPK------- 147
|
170
....*....|....*...
gi 15227913 1510 KIRIVALSTSLA-NAKDL 1526
Cdd:pfam00270 148 KRQILLLSATLPrNLEDL 165
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
1352-1532 |
1.66e-35 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 134.00 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1352 FNPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGPdsamRVVYIAPLEAIAKEQFRDWEKKfgKGLGLRV 1431
Cdd:cd18028 2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG----KALYLVPLRALASEKYEEFKKL--EEIGLKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1432 VELTGETLLDLKLLEKGQIIISTPEKWDALsrrWKQRK-YIQQVSLFIVDELHLIGGQG-GQVLEVIVSRMRyissQVGN 1509
Cdd:cd18028 76 GISTGDYDEDDEWLGDYDIIVATYEKFDSL---LRHSPsWLRDVGVVVVDEIHLISDEErGPTLESIVARLR----RLNP 148
|
170 180
....*....|....*....|...
gi 15227913 1510 KIRIVALSTSLANAKDLGEWIGA 1532
Cdd:cd18028 149 NTQIIGLSATIGNPDELAEWLNA 171
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1545-1735 |
2.19e-35 |
|
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: 132.68 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1545 RPVPLEIHIHGVDILSFEARMQAMTKPTYTAIV----QHAKNKKPAIVFVPTRKHVRLTAVDLIayshmdnmkspdfllg 1620
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKFDSDIIVllkiETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1621 nleelepfliqiceetlketlrhGIGYLHEGLSNLDQEIVTQLFEAGRIQVCVMSSSLCWGTPLKAHLVVVMGTHFYDGR 1700
Cdd:cd18795 65 -----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGK 121
|
170 180 190
....*....|....*....|....*....|....*
gi 15227913 1701 EnsHSDYPISNLLQMMGRGSRPLLDDAGKCVIFCH 1735
Cdd:cd18795 122 G--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1353-1540 |
4.93e-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: 133.32 E-value: 4.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1353 NPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAIL---RNHLEGPDSAMR----VVYIAPLEAIAKEQFRDWEKKFgK 1425
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILheiRQHVNQGGVIKKddfkIVYIAPMKALAAEMVEKFSKRL-A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1426 GLGLRVVELTGETLLDLKLLEKGQIIISTPEKWDALSRRWKQ-RKYIQQVSLFIVDELHLIGGQGGQVLEVIVSR-MRYI 1503
Cdd:cd18020 82 PLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGdVALSQLVRLLIIDEVHLLHDDRGPVIESLVARtLRQV 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 15227913 1504 -SSQVGnkIRIVALSTSLANAKDLGEWIGASS-CGVFNF 1540
Cdd:cd18020 162 eSTQSM--IRIVGLSATLPNYLDVADFLRVNPyKGLFFF 198
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
507-686 |
1.34e-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: 128.13 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 507 NRVQSKVYGTALfKADNILLCAPTGAGKTNVAVLTILHQLGLNMNPggtfnhgnYKIVYVAPMKALVAEVVDSLSQRLKD 586
Cdd:pfam00270 1 TPIQAEAIPAIL-EGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG--------PQALVLAPTRELAEQIYEELKKLGKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 587 FGVTVKELSGDQSLTGQ--EIKETQIIVTTPEKWDIITRKsgdRTYTQLVRLLIIDEIH-LLDDNRGPVLESIVARtlrq 663
Cdd:pfam00270 72 LGLKVASLLGGDSRKEQleKLKGPDILVGTPGRLLDLLQE---RKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|....
gi 15227913 664 iesTKEHIRLVGLSATLP-NCDDV 686
Cdd:pfam00270 145 ---LPKKRQILLLSATLPrNLEDL 165
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1369-1957 |
4.75e-33 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 138.94 E-value: 4.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1369 NVVVAAPTGSGKTICAEFAILRNHLEGPdsamRVVYIAPLEAIAKEQFRDWEKKfgKGLGLRVVELTGETLLDLKLLEKG 1448
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAMLKAIARGG----KALYIVPLRALASEKFEEFERF--EELGVRVGISTGDYDSRDEWLGDN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1449 QIIISTPEKWDALSR---RWkqrkyIQQVSLFIVDELHLIGGQG-GQVLEVIVSRMRYISSQVgnkiRIVALSTSLANAK 1524
Cdd:PRK02362 115 DIIVATSEKVDSLLRngaPW-----LDDITCVVVDEVHLIDSANrGPTLEVTLAKLRRLNPDL----QVVALSATIGNAD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1525 DLGEWIGA----SSCgvfnfppnvRPVPLEIHIHGVDILSFEARMQAMTKPtytaivqhakNKKPA-------------- 1586
Cdd:PRK02362 186 ELADWLDAelvdSEW---------RPIDLREGVFYGGAIHFDDSQREVEVP----------SKDDTlnlvldtleeggqc 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1587 IVFVPTRKHV-----RLTAVdliAYSHMDNMKSPDfllgnLEELEPFLIQICE----ETLKETLRHGIGYLHEGLSNLDQ 1657
Cdd:PRK02362 247 LVFVSSRRNAegfakRAASA---LKKTLTAAERAE-----LAELAEEIREVSDtetsKDLADCVAKGAAFHHAGLSREHR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1658 EIVTQLFEAGRIQVCVMSSSLCWGTPLKAHLVVVMGTHFYDGRENSHsdyPISNL--LQMMGRGSRPLLDDAGKCVIFC- 1734
Cdd:PRK02362 319 ELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAGMQ---PIPVLeyHQMAGRAGRPGLDPYGEAVLLAk 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1735 -HAPRKEYYKKFLY-EALPVESHLQ-------HFLhdnfnAEVVARVIENKQDAVDYLTWSFmYRRLPQNPNYynllgvs 1805
Cdd:PRK02362 396 sYDELDELFERYIWaDPEDVRSKLAtepalrtHVL-----STIASGFARTRDGLLEFLEATF-YATQTDDTGR------- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1806 hrhlsdhLSELVENTLSDLEVSKCIEIDNElDLSPLNLGMIASYYYINYTTIERFS-SLLASK--TKMkGLLEILTSASE 1882
Cdd:PRK02362 463 -------LERVVDDVLDFLERNGMIEEDGE-TLEATELGHLVSRLYIDPLSAAEIIdGLEAAKkpTDL-GLLHLVCSTPD 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1883 YDLIPIRPGEEDAVRRLI-NHQR-FSFQNPRCTDPR--------VKTSALLQ--AH-FSRQKIS-------GNL--VMDQ 1940
Cdd:PRK02362 534 MYELYLRSGDYEWLNEYLyEHEDeLLGDVPSEFEDDefedflsaVKTALLLEdwIDeVDEERITerygvgpGDIrgKVET 613
|
650
....*....|....*..
gi 15227913 1941 CEVLLSATRLLQAMVDV 1957
Cdd:PRK02362 614 AEWLLHAAERLASELDL 630
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
505-694 |
7.48e-31 |
|
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: 120.52 E-value: 7.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 505 QLNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHQLglnmnpggtFNHGnyKIVYVAPMKALVAEVVDSLSqRL 584
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTL---------LEGG--KALYLVPLRALASEKYEEFK-KL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 585 KDFGVTVKELSGDQSLTGQEIKETQIIVTTPEKWDIITRKSgdRTYTQLVRLLIIDEIHLLDD-NRGPVLESIVARTLRQ 663
Cdd:cd18028 69 EEIGLKVGISTGDYDEDDEWLGDYDIIVATYEKFDSLLRHS--PSWLRDVGVVVVDEIHLISDeERGPTLESIVARLRRL 146
|
170 180 190
....*....|....*....|....*....|.
gi 15227913 664 IESTkehiRLVGLSATLPNCDDVASFLRVDL 694
Cdd:cd18028 147 NPNT----QIIGLSATIGNPDELAEWLNAEL 173
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1368-1757 |
1.57e-26 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 118.50 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1368 DNVVVAAPTGSGKTICAEFAILRNHLEGPdsamRVVYIAPLEAIAKEQFRDWEKKFGK---GLglrvveLTGETlldlKL 1444
Cdd:COG4581 41 RSVLVAAPTGSGKTLVAEFAIFLALARGR----RSFYTAPIKALSNQKFFDLVERFGAenvGL------LTGDA----SV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1445 LEKGQIIISTPE--------KWDALSRrwkqrkyIQQVslfIVDELHLIG-GQGGQVLEVIVSrmrYISSQVgnkiRIVA 1515
Cdd:COG4581 107 NPDAPIVVMTTEilrnmlyrEGADLED-------VGVV---VMDEFHYLAdPDRGWVWEEPII---HLPARV----QLVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1516 LSTSLANAKDLGEWIgASSCG----VFNFppnVRPVPLEIHIHGVDILS--FEARMQAMTKPTYTAIVQH--AKNKKPAI 1587
Cdd:COG4581 170 LSATVGNAEEFAEWL-TRVRGetavVVSE---ERPVPLEFHYLVTPRLFplFRVNPELLRPPSRHEVIEEldRGGLLPAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1588 VFVPTRKHVrLTAVDLIAYSHMDNMKSPDFLLGNLEELEPFLIQICEETLKETLRHGIGYLHEGLSNLDQEIVTQLFEAG 1667
Cdd:COG4581 246 VFIFSRRGC-DEAAQQLLSARLTTKEERAEIREAIDEFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPKYRRLVEELFQAG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1668 RIQVCVMSSSLCWGTPLKAHLVVVMGTHFYDGRENSH---SDYpisnlLQMMGRGSRPLLDDAGKCVIFchAPRKEYYKK 1744
Cdd:COG4581 325 LLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPltaREF-----HQIAGRAGRRGIDTEGHVVVL--APEHDDPKK 397
|
410
....*....|....*..
gi 15227913 1745 FLY----EALPVESHLQ 1757
Cdd:COG4581 398 FARlasaRPEPLRSSFR 414
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
522-690 |
2.60e-24 |
|
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: 101.51 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 522 DNILLCAPTGAGKTNVAVLTILHQLgLNMNPGGTfnhgnyKIVYVAPMKALVAEVVDSLSQRLK--DFGVTVKELSGDqs 599
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALSSL-ADEPEKGV------QVLYISPLKALINDQERRLEEPLDeiDLEIPVAVRHGD-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 600 lTGQEIKETQ------IIVTTPEKWDII-TRKSGDRTYTQLvRLLIIDEIH-LLDDNRGPVLESIVARtLRQIesTKEHI 671
Cdd:cd17922 73 -TSQSEKAKQlknppgILITTPESLELLlVNKKLRELFAGL-RYVVVDEIHaLLGSKRGVQLELLLER-LRKL--TGRPL 147
|
170
....*....|....*....
gi 15227913 672 RLVGLSATLPNCDDVASFL 690
Cdd:cd17922 148 RRIGLSATLGNLEEAAAFL 166
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
501-714 |
4.95e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 101.80 E-value: 4.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 501 RGMQQLNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTILHQLglnmnpggtFNHGNYKIVYVAPMKALVAEVVDSL 580
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAL---------KRGKGGRVLVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 581 SQRLKDFGVTVKELSGDQSLTGQEIK----ETQIIVTTPEKWDIITRKsgDRTYTQLVRLLIIDEIH-LLDDNRGPVLES 655
Cdd:smart00487 75 KKLGPSLGLKVVGLYGGDSKREQLRKlesgKTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHrLLDGGFGDQLEK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15227913 656 IVARtlrqiesTKEHIRLVGLSATLPNCDDVASFLrvdLKNGLFIFDRSYRPVPLGQQY 714
Cdd:smart00487 153 LLKL-------LPKNVQLLLLSATPPEEIENLLEL---FLNDPVFIDVGFTPLEPIEQF 201
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
479-886 |
5.73e-24 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 110.37 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 479 KFDS------NEKLVKISDLPewAQPAFRGM-----QQLNRVQSKVYGTALFKADNILLCAPTGAGKTNVAVLTilhqlG 547
Cdd:COG1202 174 KFDEisattdEVDTVPVDDLD--LPPELKDLlegrgEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELA-----G 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 548 LNmnpggTFNHGNYKIVYVAPMKALVAEVVDSLSQRLKD-FGVT-------VKELSGDQSLtgqeikETQIIVTTPEKWD 619
Cdd:COG1202 247 IK-----NALEGKGKMLFLVPLVALANQKYEDFKDRYGDgLDVSirvgasrIRDDGTRFDP------NADIIVGTYEGID 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 620 IITRKS---GDrtytqlVRLLIIDEIHLLDD-NRGPVLESIVARtLRQIestKEHIRLVGLSATLPNCDDVASFLRVDLk 695
Cdd:COG1202 316 HALRTGrdlGD------IGTVVIDEVHMLEDpERGHRLDGLIAR-LKYY---CPGAQWIYLSATVGNPEELAKKLGAKL- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 696 nglFIFDrsYRPVPLGQQYIGINVKKPLRrfqLMNDIC---YQKVVAVAGKHQVLIFVHSRKETAKTARAirdtamandt 772
Cdd:COG1202 385 ---VEYE--ERPVPLERHLTFADGREKIR---IINKLVkreFDTKSSKGYRGQTIIFTNSRRRCHEIARA---------- 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 773 lsrflkedsqsreilkclagllknndlkelLPYGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPAHTVI 852
Cdd:COG1202 447 ------------------------------LGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVI 496
|
410 420 430
....*....|....*....|....*....|....*...
gi 15227913 853 IK----GtqvynperGEWmeLSPLDVMQMIGRAGRPQY 886
Cdd:COG1202 497 FDslamG--------IEW--LSVQEFHQMLGRAGRPDY 524
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1349-1517 |
1.45e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 100.64 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGPDsaMRVVYIAPLEAIAKEQFRDWEKKFGKGLG 1428
Cdd:smart00487 6 FEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKG--GRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1429 LRVVELTGETLL-DLKLLEKG--QIIISTPEKWDALSRRWKqrKYIQQVSLFIVDELHLIGGQG-GQVLEVIVSRMRyis 1504
Cdd:smart00487 84 KVVGLYGGDSKReQLRKLESGktDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHRLLDGGfGDQLEKLLKLLP--- 158
|
170
....*....|...
gi 15227913 1505 sqvgNKIRIVALS 1517
Cdd:smart00487 159 ----KNVQLLLLS 167
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
488-906 |
4.78e-23 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 107.23 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 488 KISDLPEWAQPAF------RGMQQLNRVQSKVYgTALFKADNILLCAPTGAGKT---NVAVLTILHQlglnmNPGGTfnh 558
Cdd:COG1205 33 RYAPWPDWLPPELraalkkRGIERLYSHQAEAI-EAARAGKNVVIATPTASGKSlayLLPVLEALLE-----DPGAT--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 559 gnykIVYVAPMKALVAEVVDSLSQRLKDFG--VTVKELSGDqslTGQEIKET-----QIIVTTP-----------EKWdi 620
Cdd:COG1205 104 ----ALYLYPTKALARDQLRRLRELAEALGlgVRVATYDGD---TPPEERRWirehpDIVLTNPdmlhygllphhTRW-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 621 itrksgDRTYTQLvRLLIIDEIHLLddnRGpVLESIVA---RTLRQI-ESTKEHIRLVGLSATLPNCDDVASFLrvdlkn 696
Cdd:COG1205 175 ------ARFFRNL-RYVVIDEAHTY---RG-VFGSHVAnvlRRLRRIcRHYGSDPQFILASATIGNPAEHAERL------ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 697 glfiFDRSYRPV-----PLGQQYIGI----NVKKPLRR--FQLMNDICyqkVVAVAGKHQVLIFVHSRKETAKTARAIRd 765
Cdd:COG1205 238 ----TGRPVTVVdedgsPRGERTFVLwnppLVDDGIRRsaLAEAARLL---ADLVREGLRTLVFTRSRRGAELLARYAR- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 766 tamandtlsRFLKEDSQSREIlkclagllknndlkellpygfAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVN 845
Cdd:COG1205 310 ---------RALREPDLADRV---------------------AAYRAGYLPEERREIERGLRSGELLGVVSTNALELGID 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227913 846 LPA-HTVIIKGtqvyNPerGEWMELspldvMQMIGRAGRPQydQQGEGIIITGYSKL-QYYLR 906
Cdd:COG1205 360 IGGlDAVVLAG----YP--GTRASF-----WQQAGRAGRRG--QDSLVVLVAGDDPLdQYYVR 409
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
523-707 |
6.36e-23 |
|
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: 98.83 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 523 NILLCAPTGAGKTNVAVLTILHQLgLNMNPggtfnhgnyKIVYVAPMKALVAEVVDSLSQRLKDFGVTVKELSGDQS-LT 601
Cdd:cd18026 35 NLVYSLPTSGGKTLVAEILMLKRL-LERRK---------KALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGNKGrSP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 602 GQEIKETQIIVTTPEKWDIITRKSGDRTYTQLVRLLIIDEIHLL-DDNRGPVLESIVARTLRqieSTKEHIRLVGLSATL 680
Cdd:cd18026 105 PKRRKSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLgDGHRGALLELLLTKLLY---AAQKNIQIVGMSATL 181
|
170 180
....*....|....*....|....*..
gi 15227913 681 PNCDDVASFLRVDLknglfiFDRSYRP 707
Cdd:cd18026 182 PNLEELASWLRAEL------YTTNFRP 202
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
1369-1533 |
1.24e-20 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 92.28 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1369 NVVVAAPTGSGKTICAEFAILRNHLEGPDSAMrvvYIAPLEAIAKEQFrDWEKKFGKGLGLRVVELTGET-LLDLKLLEK 1447
Cdd:cd18026 35 NLVYSLPTSGGKTLVAEILMLKRLLERRKKAL---FVLPYVSIVQEKV-DALSPLFEELGFRVEGYAGNKgRSPPKRRKS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1448 GQIIISTPEKWDALSRRWKQRKYIQQVSLFIVDELHLIG-GQGGQVLEVIVSRMRYISsqvGNKIRIVALSTSLANAKDL 1526
Cdd:cd18026 111 LSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGdGHRGALLELLLTKLLYAA---QKNIQIVGMSATLPNLEEL 187
|
....*..
gi 15227913 1527 GEWIGAS 1533
Cdd:cd18026 188 ASWLRAE 194
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
1368-1530 |
1.30e-20 |
|
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: 90.72 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1368 DNVVVAAPTGSGKTICAEFAILRNHLEGPDSAMRVVYIAPLEAIAKEQFRDWEKKF-GKGLGLRVVELTGET--LLDLKL 1444
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLdEIDLEIPVAVRHGDTsqSEKAKQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1445 LEK-GQIIISTPEKWDALSRRWKQRKYIQQVSLFIVDELH-LIGGQGGQVLEVIVSRMRYISsqvGNKIRIVALSTSLAN 1522
Cdd:cd17922 82 LKNpPGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHaLLGSKRGVQLELLLERLRKLT---GRPLRRIGLSATLGN 158
|
....*...
gi 15227913 1523 AKDLGEWI 1530
Cdd:cd17922 159 LEEAAAFL 166
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
525-884 |
4.23e-20 |
|
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: 97.62 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 525 LLCAPTGAGKTNVAVLTILHQLGLNMNPGGTFNHgnykIVYVAPMKALVAEVVDSLSQRLKDFG--VTVKELSGDqslTG 602
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKEKGLH----TLYITPLRALAVDIARNLQAPIEELGlpIRVETRTGD---TS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 603 QEIKETQ------IIVTTPEKWDI-ITRKSGDRTYTQLvRLLIIDEIH-LLDDNRGPVLESIVARtLRQIEStkeHIRLV 674
Cdd:TIGR04121 105 SSERARQrkkppdILLTTPESLALlLSYPDAARLFKDL-RCVVVDEWHeLAGSKRGDQLELALAR-LRRLAP---GLRRW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 675 GLSATLPNCDDVASFL-RVDLKNGLFIFDRSYRPVPLgQQYIGINVKKP-----LRRFQLmndicyQKVVAVAGKHQ-VL 747
Cdd:TIGR04121 180 GLSATIGNLEEARRVLlGVGGAPAVLVRGKLPKAIEV-ISLLPESEERFpwaghLGLRAL------PEVYAEIDQARtTL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 748 IFVHSRketaktarairdtamandtlsrflkedSQSREILKCLagLLKNNDLKELLpygfAIHHAGLTRTDREIVENQFR 827
Cdd:TIGR04121 253 VFTNTR---------------------------SQAELWFQAL--WEANPEFALPI----ALHHGSLDREQRRWVEAAMA 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15227913 828 WGNLQVLISTATLAWGVN-LPAHTVIikgtQVYNPeRGewmeLSPLdvMQMIGRAG-RP 884
Cdd:TIGR04121 300 AGRLRAVVCTSSLDLGVDfGPVDLVI----QIGSP-KG----VARL--LQRAGRSNhRP 347
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
522-895 |
4.76e-18 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 91.32 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 522 DNILLCAPTGAGKTNVAVLTILHQLgLNMNPGGTFNHGNYkIVYVAPMKALVAEVVDSLSQRLKDFGVTVKEL------- 594
Cdd:COG1201 40 ESTLLIAPTGSGKTLAAFLPALDEL-ARRPRPGELPDGLR-VLYISPLKALANDIERNLRAPLEEIGEAAGLPlpeirvg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 595 --SGDqslTGQEIKETQ------IIVTTPEKWDI-ITRKSGDRTYTQlVRLLIIDEIH-LLDDNRGPVLESIVARtLRQI 664
Cdd:COG1201 118 vrTGD---TPASERQRQrrrpphILITTPESLALlLTSPDARELLRG-VRTVIVDEIHaLAGSKRGVHLALSLER-LRAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 665 esTKEHIRLVGLSATLPNCDDVASFLrvdlknglfIFDRSYRPV-----PLGQQY---IGINVKKPLRRFQLMNDI---C 733
Cdd:COG1201 193 --APRPLQRIGLSATVGPLEEVARFL---------VGYEDPRPVtivdaGAGKKPdleVLVPVEDLIERFPWAGHLwphL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 734 YQKVVAVAGKHQ-VLIFVHSRKETAKTARAIrdtamandtlsrflkedsqsREILKCLAGLLknndlkellpygfAIHHA 812
Cdd:COG1201 262 YPRVLDLIEAHRtTLVFTNTRSQAERLFQRL--------------------NELNPEDALPI-------------AAHHG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 813 GLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPA-HTVIikgtQVynperGewmelSPLDV---MQMIGRAGRpQYDQ 888
Cdd:COG1201 309 SLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDvDLVI----QV-----G-----SPKSVarlLQRIGRAGH-RVGE 373
|
....*..
gi 15227913 889 QGEGIII 895
Cdd:COG1201 374 VSKGRLV 380
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1368-1528 |
1.80e-16 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 86.04 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1368 DNVVVAAPTGSGKTICAEFAILRNHLEGPDSamRVVYIAPLEAIAKEQFRDWEKKFGK-GLGLRVVELTGETLLDL--KL 1444
Cdd:COG1205 72 KNVVIATPTASGKSLAYLLPVLEALLEDPGA--TALYLYPTKALARDQLRRLRELAEAlGLGVRVATYDGDTPPEErrWI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1445 LEKGQIIISTPEKWDA--LSRRWKQRKYIQQVSLFIVDELHL-IGGQGGQVLEVIvSRMRYISSQVGNKIRIVALSTSLA 1521
Cdd:COG1205 150 REHPDIVLTNPDMLHYglLPHHTRWARFFRNLRYVVIDEAHTyRGVFGSHVANVL-RRLRRICRHYGSDPQFILASATIG 228
|
....*..
gi 15227913 1522 NAKDLGE 1528
Cdd:COG1205 229 NPAEHAE 235
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
790-884 |
6.30e-16 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 74.56 E-value: 6.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 790 LAGLLKNNDlkellpYGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLP-AHTVIIKGtqvynpergewME 868
Cdd:smart00490 3 LAELLKELG------IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LP 65
|
90
....*....|....*.
gi 15227913 869 LSPLDVMQMIGRAGRP 884
Cdd:smart00490 66 WSPASYIQRIGRAGRA 81
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
1369-1528 |
3.64e-15 |
|
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: 75.70 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1369 NVVVAAPTGSGKTICAEFAILrNHLEGpDSAMRVVYIAPLEAIAKEQ---FRDWEKKFGKGLGLRVveLTGETLLDLK-- 1443
Cdd:cd17923 17 SVVVTTGTASGKSLCYQLPIL-EALLR-DPGSRALYLYPTKALAQDQlrsLRELLEQLGLGIRVAT--YDGDTPREERra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1444 -LLEKGQIIISTP-----------EKWDALSRRWkqrKYIqqvslfIVDELH-LIGGQGGQVLEVIvSRMRYISSQVGNK 1510
Cdd:cd17923 93 iIRNPPRILLTNPdmlhyallphhDRWARFLRNL---RYV------VLDEAHtYRGVFGSHVALLL-RRLRRLCRRYGAD 162
|
170
....*....|....*...
gi 15227913 1511 IRIVALSTSLANAKDLGE 1528
Cdd:cd17923 163 PQFILTSATIGNPAEHAR 180
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
510-679 |
1.02e-14 |
|
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: 74.78 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 510 QSKVYGTALfKADNILLCAPTGAGKTNVAVLTILHQL-GLNMNPGGtfnhgnyKIVYVAPMKALVAEVVDSLSQRLKDFG 588
Cdd:cd17927 7 QLELAQPAL-KGKNTIICLPTGSGKTFVAVLICEHHLkKFPAGRKG-------KVVFLANKVPLVEQQKEVFRKHFERPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 589 VTVKELSGDQSLT---GQEIKETQIIVTTPEkwdIITR--KSGDRTYTQLVRLLIIDEIHLLDDNRgpVLESIVARTLRQ 663
Cdd:cd17927 79 YKVTGLSGDTSENvsvEQIVESSDVIIVTPQ---ILVNdlKSGTIVSLSDFSLLVFDECHNTTKNH--PYNEIMFRYLDQ 153
|
170
....*....|....*..
gi 15227913 664 -IESTKEHIRLVGLSAT 679
Cdd:cd17927 154 kLGSSGPLPQILGLTAS 170
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1349-1531 |
1.28e-13 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 71.14 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKH---FNPVQTQVFTVLyNTSDNVVVAAPTGSGKTICAEFAILRNHlegpDSAMRVVYIAPLEAIAKEQFRDWEKKFGK 1425
Cdd:cd18027 3 FKWpfeLDVFQKQAILHL-EAGDSVFVAAHTSAGKTVVAEYAIALAQ----KHMTRTIYTSPIKALSNQKFRDFKNTFGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1426 gLGLrvveLTGetllDLKLLEKGQIIISTPEKWDalSRRWKQRKYIQQVSLFIVDELHLIGGQGGQVL--EVIVsrmryi 1503
Cdd:cd18027 78 -VGL----ITG----DVQLNPEASCLIMTTEILR--SMLYNGSDVIRDLEWVIFDEVHYINDAERGVVweEVLI------ 140
|
170 180
....*....|....*....|....*...
gi 15227913 1504 ssQVGNKIRIVALSTSLANAKDLGEWIG 1531
Cdd:cd18027 141 --MLPDHVSIILLSATVPNTVEFADWIG 166
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
492-883 |
3.10e-13 |
|
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: 74.73 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 492 LPEWAQPAFRgmqqLNRVQSKVYGTALFKADN----ILLCAPTGAGKTNVAVLTILHQLGlnmnpggtfNHGNYKIVYVA 567
Cdd:COG1203 118 LPKKSKPRTP----INPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAA---------KHGGRRIIYAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 568 PMKALvaevVDSLSQRLKD-FGVTVKELSGDQSLTGQEIKE-----------------TQIIVTTPekwD------IITR 623
Cdd:COG1203 185 PFTSI----INQTYDRLRDlFGEDVLLHHSLADLDLLEEEEeyesearwlkllkelwdAPVVVTTI---DqlfeslFSNR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 624 KSGDRTYTQLVR-LLIIDEIHLLDDNRGPVLEsivaRTLRQIESTkeHIRLVGLSATLPncddvaSFLRVDLKNGL-FIF 701
Cdd:COG1203 258 KGQERRLHNLANsVIILDEVQAYPPYMLALLL----RLLEWLKNL--GGSVILMTATLP------PLLREELLEAYeLIP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 702 DRSYRPVPLGQQYIGINVKkpLRRFQLMNDICYQKVV-AVAGKHQVLIFVHSRKetaktaRAIRdtamandtLSRFLKED 780
Cdd:COG1203 326 DEPEELPEYFRAFVRKRVE--LKEGPLSDEELAELILeALHKGKSVLVIVNTVK------DAQE--------LYEALKEK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 781 SQSREILkclagLLknndlkellpygfaihHAGLTRTDREIVENQ----FRWGNLQVLIST----AtlawGVNLPAHTVI 852
Cdd:COG1203 390 LPDEEVY-----LL----------------HSRFCPADRSEIEKEikerLERGKPCILVSTqvveA----GVDIDFDVVI 444
|
410 420 430
....*....|....*....|....*....|..
gi 15227913 853 IkgtqvynpergewmELSPLD-VMQmigRAGR 883
Cdd:COG1203 445 R--------------DLAPLDsLIQ---RAGR 459
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
519-895 |
9.40e-13 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 73.77 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 519 FKADNILLCAPTGAGKTNVAVLTILHQLgLNMNPGGTFNHGNYkIVYVAPMKAL-------VAEVVDSLSQRLKDFGVTV 591
Cdd:PRK13767 45 HEGKNVLISSPTGSGKTLAAFLAIIDEL-FRLGREGELEDKVY-CLYVSPLRALnndihrnLEEPLTEIREIAKERGEEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 592 KEL-----SGD--QSLTGQEIKET-QIIVTTPEKWDIITRKSGDRTYTQLVRLLIIDEIHLLDDN-RGPVLESIVARtLR 662
Cdd:PRK13767 123 PEIrvairTGDtsSYEKQKMLKKPpHILITTPESLAILLNSPKFREKLRTVKWVIVDEIHSLAENkRGVHLSLSLER-LE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 663 QIeSTKEHIRlVGLSATLPNCDDVASFL--RVDLKNG--LFIFDRSY-RPvplgqqyIGINVKKPLRRF-----QLMNDI 732
Cdd:PRK13767 202 EL-AGGEFVR-IGLSATIEPLEEVAKFLvgYEDDGEPrdCEIVDARFvKP-------FDIKVISPVDDLihtpaEEISEA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 733 CYQKVVAVAGKHQ-VLIFVHSRKETAKTARAIRdtamandtlSRFlkEDSQSREILKClagllknndlkellpygfaiHH 811
Cdd:PRK13767 273 LYETLHELIKEHRtTLIFTNTRSGAERVLYNLR---------KRF--PEEYDEDNIGA--------------------HH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 812 AGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPaHT--VIIKGtqvynpergewmelSPLDV---MQMIGRAGRpQY 886
Cdd:PRK13767 322 SSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG-YIdlVVLLG--------------SPKSVsrlLQRIGRAGH-RL 385
|
....*....
gi 15227913 887 DQQGEGIII 895
Cdd:PRK13767 386 GEVSKGRII 394
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
1369-1495 |
1.05e-12 |
|
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: 67.43 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1369 NVVVAAPTGSGKTICAEFAILRNHLEGPDsamRVVYIAPLEAIAKEQ---FRDWEKKfgkglGLRVVELTGET----LLD 1441
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKGK---KVLVLVPTKALALQTaerLRELFGP-----GIRVAVLVGGSsaeeREK 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15227913 1442 LKLLEKgQIIISTPEKWDALSRRWKQRkYIQQVSLFIVDELHLIGGQGGQVLEV 1495
Cdd:cd00046 75 NKLGDA-DIIIATPDMLLNLLLREDRL-FLKDLKLIIVDEAHALLIDSRGALIL 126
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
523-679 |
1.13e-11 |
|
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: 64.73 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 523 NILLCAPTGAGKTnvavLTILHQLGLNMNPGGTfnhgnyKIVYVAPMKALVAEVVDSLSQRLkDFGVTVKELSGDQS--- 599
Cdd:cd00046 3 NVLITAPTGSGKT----LAALLAALLLLLKKGK------KVLVLVPTKALALQTAERLRELF-GPGIRVAVLVGGSSaee 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 600 LTGQEIKETQIIVTTPEKwdiITRK--SGDRTYTQLVRLLIIDEIHLLDDN-RGPVLESIVARTLRQIEStkehiRLVGL 676
Cdd:cd00046 72 REKNKLGDADIIIATPDM---LLNLllREDRLFLKDLKLIIVDEAHALLIDsRGALILDLAVRKAGLKNA-----QVILL 143
|
...
gi 15227913 677 SAT 679
Cdd:cd00046 144 SAT 146
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
494-681 |
1.22e-11 |
|
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: 65.96 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 494 EWAQPAFRGmqqlnrvqskvygtalfkaDNILLCAPTGAGKTNVAVLTILHQLGLNMNPGGTfnhgnYKIVYVAPMKALV 573
Cdd:cd18036 9 ELVLPALRG-------------------KNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEK-----GRVVVLVNKVPLV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 574 AEVVDSLSQRLKDfGVTVKELSGDQSL---TGQEIKETQIIVTTPEKWDIITRKS--GDRTYTQLVRLLIIDEIHLLDDN 648
Cdd:cd18036 65 EQQLEKFFKYFRK-GYKVTGLSGDSSHkvsFGQIVKASDVIICTPQILINNLLSGreEERVYLSDFSLLIFDECHHTQKE 143
|
170 180 190
....*....|....*....|....*....|....
gi 15227913 649 RgpVLESIVARTLRQ-IESTKEHIRLVGLSATLP 681
Cdd:cd18036 144 H--PYNKIMRMYLDKkLSSQGPLPQILGLTASPG 175
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
528-882 |
1.36e-11 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 70.34 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 528 APTGAGKTNVAVLTILHQLGLNMNPGGTFNH--GNYKIVYVAPMKALVAEVVDSLSQRLKDFG------------VTVKE 593
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFREGGEDTREAHkrKTSRILYISPIKALGTDVQRNLQIPLKGIAderrrrgetevnLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 594 LSGD---QSLTGQEIKETQIIVTTPEK-WDIITRKSgdRTYTQLVRLLIIDEIHLL-DDNRGPVLESIVARTLRQIESTK 668
Cdd:PRK09751 83 RTGDtpaQERSKLTRNPPDILITTPESlYLMLTSRA--RETLRGVETVIIDEVHAVaGSKRGAHLALSLERLDALLHTSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 669 EHIrlvGLSATLPNCDDVASFLRVDlknglfifdrsyRPV----PLGQQYIGINVKKPLRRfqlMNDICyqkvvAVAGKH 744
Cdd:PRK09751 161 QRI---GLSATVRSASDVAAFLGGD------------RPVtvvnPPAMRHPQIRIVVPVAN---MDDVS-----SVASGT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 745 ----------------------QVL------IFVHSR----KETAK-----TARAIRDTAMANDT-----LSRFLKEDSQ 782
Cdd:PRK09751 218 gedshagregsiwpyietgildEVLrhrstiVFTNSRglaeKLTARlnelyAARLQRSPSIAVDAahfesTSGATSNRVQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 783 SREILKCLAgllknndlkellpygfaiHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPAHTVIIkgtQVYNPe 862
Cdd:PRK09751 298 SSDVFIARS------------------HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVI---QVATP- 355
|
410 420
....*....|....*....|
gi 15227913 863 rgewmeLSPLDVMQMIGRAG 882
Cdd:PRK09751 356 ------LSVASGLQRIGRAG 369
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
1340-1530 |
2.58e-11 |
|
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: 65.16 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1340 PSYETLYQDFKHF--NPVQTQVFTV---------LYNTSDNVVVAAPTGSGKTICAEFAI---LRNHlegpdsaMRVVYI 1405
Cdd:cd18024 9 PDYDYTPISAHKPpgNPARTYPFTLdpfqktaiaCIERNESVLVSAHTSAGKTVVAEYAIaqsLRDK-------QRVIYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1406 APLEAIAKEQFRDWEKKFGKgLGLrvveLTGetllDLKLLEKGQIIISTPEKWDALSRRWKQrkYIQQVSLFIVDELHLI 1485
Cdd:cd18024 82 SPIKALSNQKYRELQEEFGD-VGL----MTG----DVTINPNASCLVMTTEILRSMLYRGSE--IMREVAWVIFDEIHYM 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15227913 1486 GGQGGQVL--EVIVsrmryissQVGNKIRIVALSTSLANAKDLGEWI 1530
Cdd:cd18024 151 RDKERGVVweETII--------LLPDKVRYVFLSATIPNARQFAEWI 189
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
459-884 |
4.72e-11 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 67.74 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 459 RSFRIRGKEFDEVHVPWVSKKFDSNEK-LVKISDLPEWAQPAFRGMQQ--LNRVQSKVYGtalfKADNILLCAPTGAGKT 535
Cdd:COG1061 39 RLAIKEGTREDGRRLPEEDTERELAEAeALEAGDEASGTSFELRPYQQeaLEALLAALER----GGGRGLVVAPTGTGKT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 536 NVAvLTILHQLglnmnpggtfnHGNYKIVYVAPMKALVAEVVDSLSQRLKDFGVTvkelsgdqslTGQEIKETQIIVTTp 615
Cdd:COG1061 115 VLA-LALAAEL-----------LRGKRVLVLVPRRELLEQWAEELRRFLGDPLAG----------GGKKDSDAPITVAT- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 616 ekWDIITRKSGDRTYTQLVRLLIIDEIHLLddnrgpvlesiVARTLRQIESTKEHIRLVGLSATLpncddvasfLRVDLK 695
Cdd:COG1061 172 --YQSLARRAHLDELGDRFGLVIIDEAHHA-----------GAPSYRRILEAFPAAYRLGLTATP---------FRSDGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 696 NGLFIFdrsyrpvplgqqYIGINVKKPLRrfQLMND--ICYQKVVAVAGKHQVLIFVHSRKETAKTARAIRDTAMANDTL 773
Cdd:COG1061 230 EILLFL------------FDGIVYEYSLK--EAIEDgyLAPPEYYGIRVDLTDERAEYDALSERLREALAADAERKDKIL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 774 SRFLKEDSQSREIL---------KCLAGLLKNNDLKellpygfAIH-HAGLTRTDREIVENQFRWGNLQVLISTATLAWG 843
Cdd:COG1061 296 RELLREHPDDRKTLvfcssvdhaEALAELLNEAGIR-------AAVvTGDTPKKEREEILEAFRDGELRILVTVDVLNEG 368
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15227913 844 VNLPAHTVII--KGTQvynpergewmelSPLDVMQMIGRAGRP 884
Cdd:COG1061 369 VDVPRLDVAIllRPTG------------SPREFIQRLGRGLRP 399
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1343-1553 |
6.52e-11 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 67.99 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1343 ETLYQDFKHFNPVQT-QVFTVLYNTSDNVVVAApTGSGKTICAEFAILRNHLEGPDsamRVVYIAPLEAIAKEQFRDWEK 1421
Cdd:COG1202 201 DLLEGRGEELLPVQSlAVENGLLEGKDQLVVSA-TATGKTLIGELAGIKNALEGKG---KMLFLVPLVALANQKYEDFKD 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1422 KFGKGL--GLRVveltGETLLDLKLLEKG---QIIISTPEKWDALSRRwkqRKYIQQVSLFIVDELHLIGGQG-GQVLEV 1495
Cdd:COG1202 277 RYGDGLdvSIRV----GASRIRDDGTRFDpnaDIIVGTYEGIDHALRT---GRDLGDIGTVVIDEVHMLEDPErGHRLDG 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15227913 1496 IVSRMRYISSqvgnKIRIVALSTSLANAKDLGEWIGASscgVFNFppNVRPVPLEIHI 1553
Cdd:COG1202 350 LIARLKYYCP----GAQWIYLSATVGNPEELAKKLGAK---LVEY--EERPVPLERHL 398
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
799-883 |
9.79e-11 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 60.69 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 799 LKELLPYGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLP-AHTVIIkgtqvYNPERgewmelSPLDVMQM 877
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YDLPW------NPASYIQR 101
|
....*.
gi 15227913 878 IGRAGR 883
Cdd:pfam00271 102 IGRAGR 107
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
525-690 |
1.33e-10 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350783 [Multi-domain] Cd Length: 192 Bit Score: 62.77 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 525 LLCAPTGAGKTNVAVLTILHQLGLNmnpggtfNHGnyKIVYVAPMKALVAEVVDSLSQRLKDfgvtvKELSGDQSLTG-- 602
Cdd:cd18025 20 LIVAPTSSGKTFISYYCMEKVLRES-------DDG--VVVYVAPTKALVNQVVAEVYARFSK-----KYPPSGKSLWGvf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 603 ------QEIKETQIIVTTPEKWDIITRKSGDRTYTQLVRLLIIDEIHLLDDNRGPVLEsivartlrqiestkEHIRL--- 673
Cdd:cd18025 86 trdyrhNNPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVW--------------EQLLLlip 151
|
170 180
....*....|....*....|
gi 15227913 674 ---VGLSATLPNCDDVASFL 690
Cdd:cd18025 152 cpfLALSATIGNPQKFHEWL 171
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
1374-1531 |
2.12e-10 |
|
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: 66.04 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1374 APTGSGKTICAEFAILRNHLEG---PDSAMRVVYIAPLEAIAKEQFRDWEKK-FGKGLGLRVVELTGETLLDLKLLEKG- 1448
Cdd:TIGR04121 35 APTGSGKTLAGFLPSLIDLAGPeapKEKGLHTLYITPLRALAVDIARNLQAPiEELGLPIRVETRTGDTSSSERARQRKk 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1449 --QIIISTPEKWDALSRRWKQRKYIQQVSLFIVDELH-LIGGQGGQVLEVIVSRMRYISSQVgnkiRIVALSTSLANAKD 1525
Cdd:TIGR04121 115 ppDILLTTPESLALLLSYPDAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPGL----RRWGLSATIGNLEE 190
|
....*.
gi 15227913 1526 LGEWIG 1531
Cdd:TIGR04121 191 ARRVLL 196
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
1349-1481 |
4.12e-10 |
|
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: 61.30 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTVLYNTSDnVVVAAPTGSGKTICaeFAI-----LRNHLEGPDSAMRVVYIAP---L-EAIAkEQFRdw 1419
Cdd:cd00268 10 FEKPTPIQAQAIPLILSGRD-VIGQAQTGSGKTLA--FLLpilekLLPEPKKKGRGPQALVLAPtreLaMQIA-EVAR-- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15227913 1420 ekKFGKGLGLRVVELTGETLLD--LKLLEKG-QIIISTPEK-WDALsrrwkQRKYIQ--QVSLFIVDE 1481
Cdd:cd00268 84 --KLGKGTGLKVAAIYGGAPIKkqIEALKKGpDIVVGTPGRlLDLI-----ERGKLDlsNVKYLVLDE 144
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
1369-1524 |
5.64e-10 |
|
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: 61.29 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1369 NVVVAAPTGSGKTICAEFaILRNHLEGPDSAM--RVVYIAPLEAIAKEQFRDWEKKFGKgLGLRVVELTGETLLDL---K 1443
Cdd:cd17927 19 NTIICLPTGSGKTFVAVL-ICEHHLKKFPAGRkgKVVFLANKVPLVEQQKEVFRKHFER-PGYKVTGLSGDTSENVsveQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1444 LLEKGQIIISTPEKW--DALSRRWKQRkyiQQVSLFIVDELHLigGQGGQVLEVIVsrMRYISSQVGNKI---RIVALST 1518
Cdd:cd17927 97 IVESSDVIIVTPQILvnDLKSGTIVSL---SDFSLLVFDECHN--TTKNHPYNEIM--FRYLDQKLGSSGplpQILGLTA 169
|
....*.
gi 15227913 1519 SLANAK 1524
Cdd:cd17927 170 SPGVGG 175
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
1347-1481 |
6.81e-10 |
|
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: 60.68 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1347 QDFKHFNPVQTQVFTVLYNTSDnVVVAAPTGSGKTICaeFAI-LRNHLEGPDSA--MRVVYIAPLEAIAKEQFRDWeKKF 1423
Cdd:cd17957 8 SGYREPTPIQMQAIPILLHGRD-LLACAPTGSGKTLA--FLIpILQKLGKPRKKkgLRALILAPTRELASQIYREL-LKL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227913 1424 GKGLGLRVVELTGETLL----DLKLLEKGQIIISTPEKwdaLSRRWKQRK-YIQQVSLFIVDE 1481
Cdd:cd17957 84 SKGTGLRIVLLSKSLEAkakdGPKSITKYDILVSTPLR---LVFLLKQGPiDLSSVEYLVLDE 143
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
520-678 |
5.51e-09 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 58.05 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 520 KADNILLCAPTGAGKTNVAVLTI--LHQLGLNMNPGGTFnhgnykIVYVAPMKALV---AEVVDSLSqrlkdfGVTVKEL 594
Cdd:cd18034 15 LKRNTIVVLPTGSGKTLIAVMLIkeMGELNRKEKNPKKR------AVFLVPTVPLVaqqAEAIRSHT------DLKVGEY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 595 SGDQSLTGQ-------EIKETQIIVTTPEkwdiITRKSGDRTYTQL--VRLLIIDEIHLLddnrgpVLESIVARTLRQI- 664
Cdd:cd18034 83 SGEMGVDKWtkerwkeELEKYDVLVMTAQ----ILLDALRHGFLSLsdINLLIFDECHHA------TGDHPYARIMKEFy 152
|
170
....*....|....*.
gi 15227913 665 --ESTKEHIRLVGLSA 678
Cdd:cd18034 153 hlEGRTSRPRILGLTA 168
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
501-700 |
8.76e-09 |
|
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: 57.45 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 501 RGMQQLNRVQSKVYGTALFKADnILLCAPTGAGKTNVAVLTILHQLGLNMNPGGTFNhgnyKIVYVAPMKALVAEVVDSL 580
Cdd:cd00268 8 LGFEKPTPIQAQAIPLILSGRD-VIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGP----QALVLAPTRELAMQIAEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 581 SQRLKDFGVTVKELSGDQSLTGQEIKE---TQIIVTTPEK-WDIITRKSGDrtyTQLVRLLIIDEI-HLLDDNRGPVLES 655
Cdd:cd00268 83 RKLGKGTGLKVAAIYGGAPIKKQIEALkkgPDIVVGTPGRlLDLIERGKLD---LSNVKYLVLDEAdRMLDMGFEEDVEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15227913 656 IVARTL--RQIestkehirlVGLSATLPncDDVASFLRVDLKNGLFI 700
Cdd:cd00268 160 ILSALPkdRQT---------LLFSATLP--EEVKELAKKFLKNPVRI 195
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
1369-1524 |
8.92e-09 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 57.66 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1369 NVVVAAPTGSGKTICAEFAILRNH---LEGPDSAMRVVYIAPLEAIAKEQFrdweKKFGKGLGLRVVELTGETLLDLK-- 1443
Cdd:cd18034 18 NTIVVLPTGSGKTLIAVMLIKEMGelnRKEKNPKKRAVFLVPTVPLVAQQA----EAIRSHTDLKVGEYSGEMGVDKWtk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1444 -----LLEKGQIIISTPEKW-DALSRRWKQrkyIQQVSLFIVDELHLIGGQ--GGQVLEVIvsrmrYISSQVGNKIRIVA 1515
Cdd:cd18034 94 erwkeELEKYDVLVMTAQILlDALRHGFLS---LSDINLLIFDECHHATGDhpYARIMKEF-----YHLEGRTSRPRILG 165
|
....*....
gi 15227913 1516 LSTSLANAK 1524
Cdd:cd18034 166 LTASPVNGK 174
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
1358-1877 |
8.96e-09 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 60.42 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1358 QVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGpdsamRVVYIAPLEAIAkEQfrdWEKKFGKGLGLRVVELTGE 1437
Cdd:COG1061 91 ALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK-----RVLVLVPRRELL-EQ---WAEELRRFLGDPLAGGGKK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1438 TlldlkllEKGQIIISTpekWDALSRRWKQRKYIQQVSLFIVDELHLIGGQGGQVLevivsrMRYISSQvgnkiRIVALS 1517
Cdd:COG1061 162 D-------SDAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHAGAPSYRRI------LEAFPAA-----YRLGLT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1518 tslanA----KDLGEWIGASSCG-VFNFPPN-------VRPVplEIHIHGVDILSFEARMQAMTKPTYTAIVQHAKNK-- 1583
Cdd:COG1061 221 -----AtpfrSDGREILLFLFDGiVYEYSLKeaiedgyLAPP--EYYGIRVDLTDERAEYDALSERLREALAADAERKdk 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1584 ------------KPAIVFVPTRKHVRltavdliayshmdnmkspdfllgnleelepfliQICEETLKETLRhgIGYLHEG 1651
Cdd:COG1061 294 ilrellrehpddRKTLVFCSSVDHAE---------------------------------ALAELLNEAGIR--AAVVTGD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1652 LSNLDQEIVTQLFEAGRIQVCVMSSSLCWGTPLKA--HLVVVMGThfydgreNSHSDYpisnlLQMMGRGSRPlldDAGK 1729
Cdd:COG1061 339 TPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPT-------GSPREF-----IQRLGRGLRP---APGK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1730 --CVIFCHAPRKEYYKKFLYEALPVESHLQHFLHDNFNAEVVARVIENKQDAVDYltWSFMYRRLPQNPNYYNLLGVSHR 1807
Cdd:COG1061 404 edALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVK--GELEEELLEELELLEDALLLVLA 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1808 HLSDHLSELVENTLSDLEVSKCIEIDNELDLSPLNLGMIASYYYINYTTIERFSSLLASKTKMKGLLEIL 1877
Cdd:COG1061 482 ELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEEL 551
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1369-1483 |
9.33e-09 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 56.53 E-value: 9.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1369 NVVVAAPTGSGKTICAEFAILRNHLEGPdsAMRVVYIAPLEAIAKEQFRDWeKKFGKGLGLRVVELTGETllDLKLLEKG 1448
Cdd:pfam04851 25 RGLIVMATGSGKTLTAAKLIARLFKKGP--IKKVLFLVPRKDLLEQALEEF-KKFLPNYVEIGEIISGDK--KDESVDDN 99
|
90 100 110
....*....|....*....|....*....|....*
gi 15227913 1449 QIIISTPEKWDALSRRWKQRKYIQQVSLFIVDELH 1483
Cdd:pfam04851 100 KIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
523-682 |
1.87e-08 |
|
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: 56.05 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 523 NILLCAPTGAGKTNVAVLTILHQLgLNmNPGGTFnhgnykiVYVAPMKALVAEVVDSLSQRLKD--FGVTVKELSGDqsl 600
Cdd:cd17923 17 SVVVTTGTASGKSLCYQLPILEAL-LR-DPGSRA-------LYLYPTKALAQDQLRSLRELLEQlgLGIRVATYDGD--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 601 TGQEIKET------QIIVTTPEKWDIITRKSGDRTYTQL--VRLLIIDEIHLLddnRGpVLESIVA----RTLRQIESTK 668
Cdd:cd17923 85 TPREERRAiirnppRILLTNPDMLHYALLPHHDRWARFLrnLRYVVLDEAHTY---RG-VFGSHVAlllrRLRRLCRRYG 160
|
170
....*....|....
gi 15227913 669 EHIRLVGLSATLPN 682
Cdd:cd17923 161 ADPQFILTSATIGN 174
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
521-685 |
3.55e-08 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 55.38 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 521 ADNILLCAPTGAGKTNVAVLTILHQLglnmnpggtFNHGNYKIVYVAPMKALV----AEVVDSLSQRLKDFGVT------ 590
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWALKLA---------ARGGKRRIIYALPTRATInqmyERIREILGRLDDEDKVLllhska 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 591 -VKELSGDQSLTGQEIKETQ------------IIVTTpekWD-----IITRKSGDRTYTQLVR-LLIIDEIHLLDDNRGP 651
Cdd:cd17930 72 aLELLESDEEPDDDPVEAVDwalllkrswlapIVVTT---IDqllesLLKYKHFERRLHGLANsVVVLDEVQAYDPEYMA 148
|
170 180 190
....*....|....*....|....*....|....
gi 15227913 652 VLEsivaRTLRQIESTKeHIRLVGLSATLPNCDD 685
Cdd:cd17930 149 LLL----KALLELLGEL-GGPVVLMTATLPALLR 177
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
518-681 |
3.84e-08 |
|
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: 56.22 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 518 LFKADNILLCAPTGAGKTNVAVLTILHQ-LGLNMNPGGTFNHGnyKIVYVAPMKAL---VAEVVDSLSQRLkdfGVTVKE 593
Cdd:cd17948 24 ILRGRNTLCAAETGSGKTLTYLLPIIQRlLRYKLLAEGPFNAP--RGLVITPSRELaeqIGSVAQSLTEGL---GLKVKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 594 LSGD---QSLTGQEIKETQIIVTTPekwDIITRKSGDRTY-TQLVRLLIIDEIH-LLDDNRGPVLESIVART---LRQIE 665
Cdd:cd17948 99 ITGGrtkRQIRNPHFEEVDILVATP---GALSKLLTSRIYsLEQLRHLVLDEADtLLDDSFNEKLSHFLRRFplaSRRSE 175
|
170
....*....|....*....
gi 15227913 666 STKEHIR---LVGLSATLP 681
Cdd:cd17948 176 NTDGLDPgtqLVLVSATMP 194
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
502-700 |
4.49e-08 |
|
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: 55.67 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 502 GMQQLNRVQSKVYGTALFKADNILLCAPTGAGKTnVAVLTILHQLGLNMNPGGtfNHGNYKIVYVAPMKAL---VAEVVD 578
Cdd:cd17964 13 GFETMTPVQQKTLKPILSTGDDVLARAKTGTGKT-LAFLLPAIQSLLNTKPAG--RRSGVSALIISPTRELalqIAAEAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 579 SLSQRLKDFGVtvkelsgdQSLTG-----QEIKETQ-----IIVTTPEKWDIITRKSGDRTYTQLVRLLIIDEI-HLLDD 647
Cdd:cd17964 90 KLLQGLRKLRV--------QSAVGgtsrrAELNRLRrgrpdILVATPGRLIDHLENPGVAKAFTDLDYLVLDEAdRLLDM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15227913 648 NRGPVLESIVaRTLRQIESTkeHIRLVGLSATLPncDDVASFLRVDLKNG-LFI 700
Cdd:cd17964 162 GFRPDLEQIL-RHLPEKNAD--PRQTLLFSATVP--DEVQQIARLTLKKDyKFI 210
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1370-1533 |
6.72e-08 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350783 [Multi-domain] Cd Length: 192 Bit Score: 54.68 E-value: 6.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1370 VVVAAPTGSGKTICAEFA---ILRNHLEGPdsamrVVYIAPLEAIAKEQFRDWEKKFGKGL---GLRVVE-LTGETLLDl 1442
Cdd:cd18025 19 ALIVAPTSSGKTFISYYCmekVLRESDDGV-----VVYVAPTKALVNQVVAEVYARFSKKYppsGKSLWGvFTRDYRHN- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1443 kLLEKGQIIISTPEKWDA--LSR---RWKQR-KYIqqvslfIVDELHLIGGQ-GGQVLEVIVsrmryissqVGNKIRIVA 1515
Cdd:cd18025 93 -NPMNCQVLITVPECLEIllLSPhnaSWVPRiKYV------IFDEIHSIGQSeDGAVWEQLL---------LLIPCPFLA 156
|
170
....*....|....*...
gi 15227913 1516 LSTSLANAKDLGEWIGAS 1533
Cdd:cd18025 157 LSATIGNPQKFHEWLQSV 174
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
1371-1499 |
6.94e-08 |
|
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: 53.46 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1371 VVAAPTGSGKTICAEFAILRNHlegpdsAMRVVYIAPLEAIAkEQfrdWEKKFGKGLGLRVVELTGEtlLDLKLLEKGQI 1450
Cdd:cd17926 22 ILVLPTGSGKTLTALALIAYLK------ELRTLIVVPTDALL-DQ---WKERFEDFLGDSSIGLIGG--GKKKDFDDANV 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15227913 1451 IISTpekWDALSRRWKQRKYI-QQVSLFIVDELHLIGGQGgqvLEVIVSR 1499
Cdd:cd17926 90 VVAT---YQSLSNLAEEEKDLfDQFGLLIVDEAHHLPAKT---FSEILKE 133
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
799-883 |
8.65e-08 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 53.42 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 799 LKELLPYG-----FAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPA-HTVIikgtQVynpergewmeLSPL 872
Cdd:cd18796 58 LRELCPDRvppdfIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDvDLVI----QI----------GSPK 123
|
90
....*....|....
gi 15227913 873 DV---MQMIGRAGR 883
Cdd:cd18796 124 SVarlLQRLGRSGH 137
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
1369-1520 |
9.59e-08 |
|
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: 54.79 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1369 NVVVAAPTGSGKTICAEFaILRNHLEGPDSAM---RVVYIAPLEAIAKEQFRDWEKKFGKglGLRVVELTGETLLDL--- 1442
Cdd:cd18036 19 NTIICAPTGSGKTRVAVY-ICRHHLEKRRSAGekgRVVVLVNKVPLVEQQLEKFFKYFRK--GYKVTGLSGDSSHKVsfg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1443 KLLEKGQIIISTPEKW--DALSRRWKQRKYIQQVSLFIVDELHLIGGQGgqVLEVIVSR-MRYISSQVGNKIRIVALSTS 1519
Cdd:cd18036 96 QIVKASDVIICTPQILinNLLSGREEERVYLSDFSLLIFDECHHTQKEH--PYNKIMRMyLDKKLSSQGPLPQILGLTAS 173
|
.
gi 15227913 1520 L 1520
Cdd:cd18036 174 P 174
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1631-1722 |
2.48e-07 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 50.29 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1631 QICEETLKEtLRHGIGYLHEGLSNLDQEIVTQLFEAGRIQVCVMSSSLCWGTPLK-AHLVVVMGthfydgrenshSDYPI 1709
Cdd:smart00490 1 EELAELLKE-LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSP 68
|
90
....*....|...
gi 15227913 1710 SNLLQMMGRGSRP 1722
Cdd:smart00490 69 ASYIQRIGRAGRA 81
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
524-883 |
2.55e-07 |
|
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: 55.13 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 524 ILLCAPTGAGKTNVAVLTILHQLglnmnPGGTFNhgnyKIVYVAPMKALVAEVVDSLSQRLKDFGVTVK----------- 592
Cdd:cd09639 2 LVIEAPTGYGKTEAALLWALHSL-----KSQKAD----RVIIALPTRATINAMYRRAKEAFGETGLYHSsilssrikemg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 593 ---ELSGDQSLTGQEIKE---TQIIVTTPEKWDI-ITRKSGDRTYTQL---VRLLIIDEIHLLDDNrgpvlesivarTLR 662
Cdd:cd09639 73 dseEFEHLFPLYIHSNDTlflDPITVCTIDQVLKsVFGEFGHYEFTLAsiaNSLLIFDEVHFYDEY-----------TLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 663 QIESTKEHIRLVG-----LSATLPNcddvaSFLRVDLKNGLFIFDRSYRPVPLGQQYIGINVKKPLRRFQLMNDIcyqkV 737
Cdd:cd09639 142 LILAVLEVLKDNDvpillMSATLPK-----FLKEYAEKIGYVEENEPLDLKPNERAPFIKIESDKVGEISSLERL----L 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 738 VAVAGKHQVLIFVHsrkeTAKTARAIRDTamandtlsrfLKEDSQSREILkclagllknndlkellpygfaIHHAGLTRT 817
Cdd:cd09639 213 EFIKKGGSVAIIVN----TVDRAQEFYQQ----------LKEKGPEEEIM---------------------LIHSRFTEK 257
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 818 DREIVENQF--RWGNLQ--VLISTATLAWGVNLPAHTVIikgtqvynpergewMELSPLDvmQMIGRAGR 883
Cdd:cd09639 258 DRAKKEAELllEFKKSEkfVIVATQVIEASLDISVDVMI--------------TELAPID--SLIQRLGR 311
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1372-1551 |
3.56e-07 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 55.70 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1372 VAAPTGSGKTICA-EFAILRNHLEG--------PDSAMRVVYIAPLEA---------------IAKEQFRDWEKKFGKGL 1427
Cdd:PRK09751 1 VIAPTGSGKTLAAfLYALDRLFREGgedtreahKRKTSRILYISPIKAlgtdvqrnlqiplkgIADERRRRGETEVNLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1428 GLRvvelTGETLLD--LKLLEK-GQIIISTPEKWdALSRRWKQRKYIQQVSLFIVDELHLIGG-QGGQVLEVIVSRMRYI 1503
Cdd:PRK09751 81 GIR----TGDTPAQerSKLTRNpPDILITTPESL-YLMLTSRARETLRGVETVIIDEVHAVAGsKRGAHLALSLERLDAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15227913 1504 SSQVGNKIrivALSTSLANAKDLGEWIGASSCGVFNFPPNVRPVPLEI 1551
Cdd:PRK09751 156 LHTSAQRI---GLSATVRSASDVAAFLGGDRPVTVVNPPAMRHPQIRI 200
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
1367-1483 |
3.97e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.51 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1367 SDNVVVAAPTGSGKTICAEFAILRnHLEGPDSamRVVYIAPLEAIAkEQFRDWEKKFGKGLGLRVVELTGETLLD--LKL 1444
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE-RLHKKGG--KVLFLAPTKPLV-EQHAEFFKEALNIPEDEIVVFTGEVSPEkrKEL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15227913 1445 LEKGQIIISTPE--KWDALSRRWKqrkyIQQVSLFIVDELH 1483
Cdd:COG1111 93 WEKARIIVATPQviENDLIAGRID----LDDVSLLIFDEAH 129
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
1349-1485 |
5.78e-07 |
|
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: 52.15 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTVLYNTSDnVVVAAPTGSGKTICAEFAILrnHLEGPdsamrVVYIAPLEAIAKEQFRDWEKkfgkgLG 1428
Cdd:cd17920 10 YDEFRPGQLEAINAVLAGRD-VLVVMPTGGGKSLCYQLPAL--LLDGV-----TLVVSPLISLMQDQVDRLQQ-----LG 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227913 1429 LRVVELTGETLLD-----LKLLEKGQ--IIISTPEK--WDALSRRWKQRKYIQQVSLFIVDELHLI 1485
Cdd:cd17920 77 IRAAALNSTLSPEekrevLLRIKNGQykLLYVTPERllSPDFLELLQRLPERKRLALIVVDEAHCV 142
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
1354-1481 |
7.49e-07 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 52.37 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1354 PVQTQVFTVLYNTSdNVVVAAPTGSGKTICAEFAILRNHL------EGPDSAMRVVYIAPLEAIAkEQFRDWEKKFGKGL 1427
Cdd:cd17948 15 TVQKQGIPSILRGR-NTLCAAETGSGKTLTYLLPIIQRLLrykllaEGPFNAPRGLVITPSRELA-EQIGSVAQSLTEGL 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15227913 1428 GLRVVELT-GETLLDLKLLEKGQ--IIISTPekwDALSRRWKQRKY-IQQVSLFIVDE 1481
Cdd:cd17948 93 GLKVKVITgGRTKRQIRNPHFEEvdILVATP---GALSKLLTSRIYsLEQLRHLVLDE 147
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
1349-1481 |
1.20e-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: 51.43 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTVLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGPD----SAMRVVYIAPLEAIAKEQFRDWEKKFG 1424
Cdd:cd17964 14 FETMTPVQQKTLKPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPagrrSGVSALIISPTRELALQIAAEAKKLLQ 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15227913 1425 KGLGLRVVELTGET--LLDLKLLEKG--QIIISTPEKWDALSRRWKQRKYIQQVSLFIVDE 1481
Cdd:cd17964 94 GLRKLRVQSAVGGTsrRAELNRLRRGrpDILVATPGRLIDHLENPGVAKAFTDLDYLVLDE 154
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
523-641 |
1.21e-06 |
|
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: 51.05 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 523 NILLCAPTGAGKTNVAVLTILHQLGLNMNPGGtfnhgnYKIVYVAPMKALVAEVVDSLSQRLKDFGVTVKELSGDQSLTG 602
Cdd:cd17957 29 DLLACAPTGSGKTLAFLIPILQKLGKPRKKKG------LRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEAKA 102
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15227913 603 QEIKET----QIIVTTPEKwdIITRKSGDRTYTQLVRLLIIDE 641
Cdd:cd17957 103 KDGPKSitkyDILVSTPLR--LVFLLKQGPIDLSSVEYLVLDE 143
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
505-679 |
1.75e-06 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 50.40 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 505 QLNRVQSkvygtALFKadNILLCAPTGAGKTNVAVLTILhqlglnmnpggtfnhgNY-------KIVYVAPMKALVAEVV 577
Cdd:cd18033 7 QFTIVQK-----ALFQ--NTLVALPTGLGKTFIAAVVML----------------NYyrwfpkgKIVFMAPTKPLVSQQI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 578 DSLSQrlkdfgVTVKELSGDQSLTGQ--------EIKETQIIVTTPEKW--DIitrKSGDRTYTQLVrLLIIDEIHlldD 647
Cdd:cd18033 64 EACYK------ITGIPSSQTAELTGSvpptkraeLWASKRVFFLTPQTLenDL---KEGDCDPKSIV-CLVIDEAH---R 130
|
170 180 190
....*....|....*....|....*....|..
gi 15227913 648 NRGPVLESIVARTLRQIEStkeHIRLVGLSAT 679
Cdd:cd18033 131 ATGNYAYCQVVRELMRYNS---HFRILALTAT 159
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
1349-1455 |
1.90e-06 |
|
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: 51.09 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQV---------FTVLYNTSDnVVVAAPTGSGKTICAEFAILRNHLEGPDSAMRVVYIAPLEAIAKeQFRDW 1419
Cdd:cd17956 10 ITSAFPVQAAVipwllpsskSTPPYRPGD-LCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKELVQ-QVYKV 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15227913 1420 EKKFGKGLGLRVVELTG------ETLLDLK-----LLEKGQIIISTP 1455
Cdd:cd17956 88 FESLCKGTGLKVVSLSGqksfkkEQKLLLVdtsgrYLSRVDILVATP 134
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
498-696 |
2.46e-06 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 49.96 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 498 PAFRGMQQLNRVQSKVYgTALFKADNILLCAPTGAGKTNVAVLTILHQLGlNMNpggtfnhgnyKIVYVAPMKALVaevv 577
Cdd:cd18027 1 PAFKWPFELDVFQKQAI-LHLEAGDSVFVAAHTSAGKTVVAEYAIALAQK-HMT----------RTIYTSPIKALS---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 578 dslSQRLKDFGVT---VKELSGDQSLTgqeiKETQIIVTTPEKWDIITRKSGDrtYTQLVRLLIIDEIHLLDD-NRGPVL 653
Cdd:cd18027 65 ---NQKFRDFKNTfgdVGLITGDVQLN----PEASCLIMTTEILRSMLYNGSD--VIRDLEWVIFDEVHYINDaERGVVW 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15227913 654 ESIVARTlrqiestKEHIRLVGLSATLPNCDDVASFL-RVDLKN 696
Cdd:cd18027 136 EEVLIML-------PDHVSIILLSATVPNTVEFADWIgRIKKKN 172
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1349-1593 |
2.46e-06 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 52.80 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTvLYNTSDNVVVAAPTGSGKTICAEFAILRNHLEGPDSAM-----RVVYIAPLEAIAkeqfRDWEK-- 1421
Cdd:COG1201 22 FGAPTPPQREAWP-AIAAGESTLLIAPTGSGKTLAAFLPALDELARRPRPGElpdglRVLYISPLKALA----NDIERnl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1422 -----KFGKGLGLRVVEL-----TGETLLD--LKLLEK-GQIIISTPEkwdAL-----SRRWkqRKYIQQVSLFIVDELH 1483
Cdd:COG1201 97 rapleEIGEAAGLPLPEIrvgvrTGDTPASerQRQRRRpPHILITTPE---SLallltSPDA--RELLRGVRTVIVDEIH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1484 -LIGGQGGQVLEVIVSRMRYIssqVGNKIRIVALSTSLANAKDLGEWIGAsscgvfnfPPNVRPVPL-------EIHIhg 1555
Cdd:COG1201 172 aLAGSKRGVHLALSLERLRAL---APRPLQRIGLSATVGPLEEVARFLVG--------YEDPRPVTIvdagagkKPDL-- 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15227913 1556 vDILSFEARMQAMTKPT-------YTAIVQHAKNKKPAIVFVPTR 1593
Cdd:COG1201 239 -EVLVPVEDLIERFPWAghlwphlYPRVLDLIEAHRTTLVFTNTR 282
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
510-643 |
2.55e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 52.95 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 510 QSKVYGTALfkADNILLCAPTGAGKTNVAVLTILHQLglnMNPGGtfnhgnyKIVYVAPMKALVAEVVDSLSQ--RLKDF 587
Cdd:PRK13766 20 QQLLAATAL--KKNTLVVLPTGLGKTAIALLVIAERL---HKKGG-------KVLILAPTKPLVEQHAEFFRKflNIPEE 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227913 588 GVTVkelsgdqsLTG-------QEI-KETQIIVTTPE--KWDIITRksgdRTYTQLVRLLIIDEIH 643
Cdd:PRK13766 88 KIVV--------FTGevspekrAELwEKAKVIVATPQviENDLIAG----RISLEDVSLLIFDEAH 141
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
525-680 |
3.17e-06 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 48.84 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 525 LLCAPTGAGKTNVAVLTILHQlglnmnpggtfnhGNYKIVYVAPMKALVAEVVDslsqRLKDFG--VTVKELSGDQSltg 602
Cdd:cd17926 22 ILVLPTGSGKTLTALALIAYL-------------KELRTLIVVPTDALLDQWKE----RFEDFLgdSSIGLIGGGKK--- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15227913 603 QEIKETQIIVTTpekWDIITRKSGD-RTYTQLVRLLIIDEIHLLDdnrgpvlesivARTLRQIESTKEHIRLVGLSATL 680
Cdd:cd17926 82 KDFDDANVVVAT---YQSLSNLAEEeKDLFDQFGLLIVDEAHHLP-----------AKTFSEILKELNAKYRLGLTATP 146
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1349-1455 |
3.40e-06 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 51.69 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTVLYNTSDnVVVAAPTGSGKTicAEFA--ILRNHLEGPDSAMRVVYIAP---L-EAIAkEQFRdwekK 1422
Cdd:COG0513 22 YTTPTPIQAQAIPLILAGRD-VLGQAQTGTGKT--AAFLlpLLQRLDPSRPRAPQALILAPtreLaLQVA-EELR----K 93
|
90 100 110
....*....|....*....|....*....|....*.
gi 15227913 1423 FGKGLGLRVVELTGETLLD--LKLLEKG-QIIISTP 1455
Cdd:COG0513 94 LAKYLGLRVATVYGGVSIGrqIRALKRGvDIVVATP 129
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
1368-1511 |
3.43e-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: 49.60 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1368 DNVVVAAPTGSGKTICAEFAILRNHLEGPDSamRVVYIAPLEAIAKEQFRDWEKKFGKGLG-LRVVELTGETLLDL--KL 1444
Cdd:cd17930 2 GLVILEAPTGSGKTEAALLWALKLAARGGKR--RIIYALPTRATINQMYERIREILGRLDDeDKVLLLHSKAALELleSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1445 LEKGQIIISTPEKWDALSRRW-----------------KQRKY------IQQvSLFIVDELHLIggqGGQVLEVIVSRMR 1501
Cdd:cd17930 80 EEPDDDPVEAVDWALLLKRSWlapivvttidqllesllKYKHFerrlhgLAN-SVVVLDEVQAY---DPEYMALLLKALL 155
|
170
....*....|
gi 15227913 1502 YISSQVGNKI 1511
Cdd:cd17930 156 ELLGELGGPV 165
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
524-883 |
4.04e-06 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 51.30 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 524 ILLCAPTGAGKTNVAVLTILHQLGlnmnpggtfNHGNYKIVYVAPMKA----------------LVAEVVDSLSQRLKDF 587
Cdd:TIGR01587 2 LVIEAPTGYGKTEAALLWALHSIK---------SQKADRVIIALPTRAtinamyrrakelfgseLVGLHHSSSFSRIKEM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 588 GVTvKELSGDQSLTGQEIKE---TQIIVTTPEKWDI-ITRKSGDRTYTQL---VRLLIIDEIHLLDDNrgpvlesivarT 660
Cdd:TIGR01587 73 GDS-EEFEHLFPLYIHSNDKlflDPITVCTIDQVLKsVFGEFGHYEFTLAsiaNSLLIFDEVHFYDEY-----------T 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 661 LRQIESTKEHIRLVG-----LSATLPNcddvaSFLRVDLKNGLFIFDRSYRPVPLGQ---QYIGINVKKPLRRFQLMNDI 732
Cdd:TIGR01587 141 LALILAVLEVLKDNDvpillMSATLPK-----FLKEYAEKIGYVEFNEPLDLKEERRfenHRFILIESDKVGEISSLERL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 733 cyqkVVAVAGKHQVLIFVHsrkeTAKTARAIRDTamandtlsrfLKEDSQSREILkclagllknndlkellpygfaIHHA 812
Cdd:TIGR01587 216 ----LEFIKKGGSIAIIVN----TVDRAQEFYQQ----------LKEKAPEEEII---------------------LYHS 256
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227913 813 GLTRTDREIVENQF--RWGNLQ---VLISTATLAWGVNLPAHTVIikgtqvynpergewMELSPLDvmQMIGRAGR 883
Cdd:TIGR01587 257 RFTEKDRAKKEAELlrEMKKSNekfVIVATQVIEASLDISADVMI--------------TELAPID--SLIQRLGR 316
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
518-679 |
4.16e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 48.82 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 518 LFKADNILLCAPTGAGKTNVAVLTILHQLGlnmnpggtfNHGNYKIVYVAPMKALVAEVVDSLSQRLKDFGVTVKELSGD 597
Cdd:pfam04851 20 KNGQKRGLIVMATGSGKTLTAAKLIARLFK---------KGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 598 QSLtgQEIKETQIIVTTPEKWDIITRKSGDRTYTQLVRLLIIDEIHllddnRGPvlesivARTLRQIESTKEHIRLVGLS 677
Cdd:pfam04851 91 KKD--ESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH-----RSG------ASSYRNILEYFKPAFLLGLT 157
|
..
gi 15227913 678 AT 679
Cdd:pfam04851 158 AT 159
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1349-1513 |
5.29e-06 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 51.81 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFtVLYNTSDNVVVAAPTGSGKTICAEFAIL--------RNHLEgpDSaMRVVYIAPLEAIAKEQFRDWE 1420
Cdd:PRK13767 30 FGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIIdelfrlgrEGELE--DK-VYCLYVSPLRALNNDIHRNLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1421 ----------KKFGKGL-GLRVVELTGETLLD--LKLLEKG-QIIISTPEKWDALSRRWKQRKYIQQVSLFIVDELH-LI 1485
Cdd:PRK13767 106 eplteireiaKERGEELpEIRVAIRTGDTSSYekQKMLKKPpHILITTPESLAILLNSPKFREKLRTVKWVIVDEIHsLA 185
|
170 180
....*....|....*....|....*...
gi 15227913 1486 GGQGGQVLEVIVSRMRYISSqvGNKIRI 1513
Cdd:PRK13767 186 ENKRGVHLSLSLERLEELAG--GEFVRI 211
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
510-643 |
5.85e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 51.65 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 510 QSKVYGTALFKadNILLCAPTGAGKTNVAVLTILHQLglnMNPGGtfnhgnyKIVYVAPMKALVAEVVDSLSQRLKDFGV 589
Cdd:COG1111 8 QLNLAASALRK--NTLVVLPTGLGKTAVALLVIAERL---HKKGG-------KVLFLAPTKPLVEQHAEFFKEALNIPED 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15227913 590 TVKELSGDqslTGQEI-----KETQIIVTTPE--KWDIITRksgdRTYTQLVRLLIIDEIH 643
Cdd:COG1111 76 EIVVFTGE---VSPEKrkelwEKARIIVATPQviENDLIAG----RIDLDDVSLLIFDEAH 129
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
1335-1455 |
6.69e-06 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 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: 350717 [Multi-domain] Cd Length: 205 Bit Score: 49.23 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1335 MALRNPSYETLY-QDFKHFNPVQTQVFTVLYNTSDnVVVAAPTGSGKTicAEFAI-----LRNHLegPDSAMRVVYIAPL 1408
Cdd:cd17959 6 MGLSPPLLRAIKkKGYKVPTPIQRKTIPLILDGRD-VVAMARTGSGKT--AAFLIpmiekLKAHS--PTVGARALILSPT 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15227913 1409 EAIAKEQFRdWEKKFGKGLGLRVVELTGETLLDLK---LLEKGQIIISTP 1455
Cdd:cd17959 81 RELALQTLK-VTKELGKFTDLRTALLVGGDSLEEQfeaLASNPDIIIATP 129
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
524-682 |
8.03e-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: 48.98 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 524 ILLCAPTGAGKTNVAVLTILHQLglnmnpggtfnHGNYKIVYVAPMKALVAEVVDSLSQRLKDFGVtvkeLSGDQSLTgq 603
Cdd:cd18024 50 VLVSAHTSAGKTVVAEYAIAQSL-----------RDKQRVIYTSPIKALSNQKYRELQEEFGDVGL----MTGDVTIN-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 604 eiKETQIIVTTPEkwdiITRKSGDR--TYTQLVRLLIIDEIHLL-DDNRGPVLE-SIVArtlrqiesTKEHIRLVGLSAT 679
Cdd:cd18024 113 --PNASCLVMTTE----ILRSMLYRgsEIMREVAWVIFDEIHYMrDKERGVVWEeTIIL--------LPDKVRYVFLSAT 178
|
...
gi 15227913 680 LPN 682
Cdd:cd18024 179 IPN 181
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
501-837 |
8.51e-06 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 50.53 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 501 RGMQQLNRVQSKVYGTALfKADNILLCAPTGAGKTnVA-VLTILHQLGLNmNPGGTfnhgnyKIVYVAPMKALVAEVVDS 579
Cdd:COG0513 20 LGYTTPTPIQAQAIPLIL-AGRDVLGQAQTGTGKT-AAfLLPLLQRLDPS-RPRAP------QALILAPTRELALQVAEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 580 LSQRLKDFGVTVKELSGDQSLTGQ--EIKE-TQIIVTTPEK-WDIITRKSGDrtyTQLVRLLIIDEI-HLLDDnrG--PV 652
Cdd:COG0513 91 LRKLAKYLGLRVATVYGGVSIGRQirALKRgVDIVVATPGRlLDLIERGALD---LSGVETLVLDEAdRMLDM--GfiED 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 653 LESIVARTLRQiestkehiRLVGL-SATLPncDDVASFLRVDLKNGLFI-FDRSYRPVPLGQQYIgINVKKPlRRFQLMN 730
Cdd:COG0513 166 IERILKLLPKE--------RQTLLfSATMP--PEIRKLAKRYLKNPVRIeVAPENATAETIEQRY-YLVDKR-DKLELLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 731 DIcyqkvVAVAGKHQVLIFVhSRKETAktarairdtamanDTLSRFLKEDsqsreilkclagllknndlkellpyGF--- 807
Cdd:COG0513 234 RL-----LRDEDPERAIVFC-NTKRGA-------------DRLAEKLQKR-------------------------GIsaa 269
|
330 340 350
....*....|....*....|....*....|
gi 15227913 808 AIhHAGLTRTDREIVENQFRWGNLQVLIST 837
Cdd:COG0513 270 AL-HGDLSQGQRERALDAFRNGKIRVLVAT 298
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
1367-1483 |
1.06e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 50.64 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1367 SDNVVVAAPTGSGKTICAEFAILrNHLEGPDSamRVVYIAPLEAIAkEQFRDWEKKFGKGLGLRVVELTGETLLD--LKL 1444
Cdd:PRK13766 29 KKNTLVVLPTGLGKTAIALLVIA-ERLHKKGG--KVLILAPTKPLV-EQHAEFFRKFLNIPEEKIVVFTGEVSPEkrAEL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15227913 1445 LEKGQIIISTPE--KWDALSRRWKqrkyIQQVSLFIVDELH 1483
Cdd:PRK13766 105 WEKAKVIVATPQviENDLIAGRIS----LEDVSLLIFDEAH 141
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
519-643 |
1.38e-05 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350831 [Multi-domain] Cd Length: 202 Bit Score: 48.28 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 519 FKADNILLCAPTGAGKTNVAVLTILHQLGlNMnPGGTfnhgNYKIVYVAPMKALVAEVVDSLSQRLKDFGVTVKELSGD- 597
Cdd:cd18073 15 MKGKNTIICAPTGCGKTFVSLLICEHHLK-KF-PQGQ----KGKVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGAt 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15227913 598 --QSLTGQEIKETQIIVTTPEkwdIITR--KSGDRTYTQLVRLLIIDEIH 643
Cdd:cd18073 89 aeNVPVEQIIENNDIIILTPQ---ILVNnlKKGTIPSLSIFTLMIFDECH 135
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
1349-1481 |
2.44e-05 |
|
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: 47.57 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTVLYNTSDnVVVAAPTGSGKTI-----CAEfAILRNHLEGPDSAMRVVYIAPLEAIAKeQFRDWEKKF 1423
Cdd:cd17960 10 FTSMTPVQAATIPLFLSNKD-VVVEAVTGSGKTLaflipVLE-ILLKRKANLKKGQVGALIISPTRELAT-QIYEVLQSF 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227913 1424 GKGLG--LRVVELTG--ETLLDLKLL--EKGQIIISTPEK-WDALSRRWKQRKyIQQVSLFIVDE 1481
Cdd:cd17960 87 LEHHLpkLKCQLLIGgtNVEEDVKKFkrNGPNILVGTPGRlEELLSRKADKVK-VKSLEVLVLDE 150
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
524-641 |
2.68e-05 |
|
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: 47.63 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 524 ILLCAPTGAGKTNVAVLTILHQLGlnmnpggTFNHGNYKIVYVAPMKALVAEVVDSLSQRLKDFGVTVKELSGDQSLTgQ 603
Cdd:cd17956 39 LCVSAPTGSGKTLAYVLPIVQALS-------KRVVPRLRALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFK-K 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15227913 604 EIKETQ------------IIVTTPEKW-DIITRKSGdrtYT-QLVRLLIIDE 641
Cdd:cd17956 111 EQKLLLvdtsgrylsrvdILVATPGRLvDHLNSTPG---FTlKHLRFLVIDE 159
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
1369-1483 |
6.65e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 45.97 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1369 NVVVAAPTGSGKTICAeFAILRNHLEGPDSamRVVYIAPLEAIAKEQFRDWEKKFgkGLGLRVVELTGETLLD--LKLLE 1446
Cdd:cd18035 18 NTLIVLPTGLGKTIIA-ILVAADRLTKKGG--KVLILAPSRPLVEQHAENLKRVL--NIPDKITSLTGEVKPEerAERWD 92
|
90 100 110
....*....|....*....|....*....|....*....
gi 15227913 1447 KGQIIISTPE--KWDALSRRWKqrkyIQQVSLFIVDELH 1483
Cdd:cd18035 93 ASKIIVATPQviENDLLAGRIT----LDDVSLLIFDEAH 127
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
1354-1455 |
1.53e-04 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 45.45 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1354 PVQTQVFTVLYNTSDnVVVAAPTGSGKTICAEFAILRNHLE----GPDSAMRVVYIAPLEAIAKEQFRDWeKKFGKGLGL 1429
Cdd:cd17953 37 PIQAQALPAIMSGRD-VIGIAKTGSGKTLAFLLPMFRHIKDqrpvKPGEGPIGLIMAPTRELALQIYVEC-KKFSKALGL 114
|
90 100 110
....*....|....*....|....*....|..
gi 15227913 1430 RVVELTG-----ETLLDLKlleKG-QIIISTP 1455
Cdd:cd17953 115 RVVCVYGgsgisEQIAELK---RGaEIVVCTP 143
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
1369-1530 |
2.37e-04 |
|
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: 44.43 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1369 NVVVAAPTGSGKTICAeFAILRNHLEG-PDSAM-RVVYIAPLEAIAKEQFRDWEKKFgKGLGLRVVELTGETLLDL---K 1443
Cdd:cd18073 19 NTIICAPTGCGKTFVS-LLICEHHLKKfPQGQKgKVVFFATKVPVYEQQKSVFSKYF-ERHGYRVTGISGATAENVpveQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1444 LLEKGQIIISTPEKW-DALsrrwkQRKYIQQVSLF---IVDELHLIGGQggQVLEVIVSrmRYISSQVGNKI----RIVA 1515
Cdd:cd18073 97 IIENNDIIILTPQILvNNL-----KKGTIPSLSIFtlmIFDECHNTSGN--HPYNMIMF--RYLDQKLGGSSgplpQIIG 167
|
170
....*....|....*..
gi 15227913 1516 LSTSL--ANAKDLGEWI 1530
Cdd:cd18073 168 LTASVgvGDAKNTDEAL 184
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
1370-1750 |
6.80e-04 |
|
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: 44.34 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1370 VVVAAPTGSGKTICAefAILRNHLEGPDSAMRVVYIAPLEAIAKEQFRDWEKKFGKGLGLRVVEL---------TGETLL 1440
Cdd:cd09639 2 LVIEAPTGYGKTEAA--LLWALHSLKSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILssrikemgdSEEFEH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1441 DLKLLEKGQ-------IIISTPEK-WDALSRRWKQRKYIQ---QVSLFIVDELHLIGGQGGQVLEVIVSRMRYissqvgN 1509
Cdd:cd09639 80 LFPLYIHSNdtlfldpITVCTIDQvLKSVFGEFGHYEFTLasiANSLLIFDEVHFYDEYTLALILAVLEVLKD------N 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1510 KIRIVALSTSLAN-AKDLGEWIGASscgVFNFPPNVRPVPLEIHIHGVDILSFEARMQamtkptyTAIVQHAKNKKPAIV 1588
Cdd:cd09639 154 DVPILLMSATLPKfLKEYAEKIGYV---EENEPLDLKPNERAPFIKIESDKVGEISSL-------ERLLEFIKKGGSVAI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1589 FVPT-----------RKHVRLTAVDLI--AYSHMDNMKSPDFLLGNLEELEPFLIqiceetlketlrhgigylheglsnl 1655
Cdd:cd09639 224 IVNTvdraqefyqqlKEKGPEEEIMLIhsRFTEKDRAKKEAELLLEFKKSEKFVI------------------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1656 dqeIVTQLFEAG-RIQVCVMSSSLCwgtplkahlvvvmgthfydgrenshsdyPISNLLQMMGRGSRPLLDDAGKCVIFC 1734
Cdd:cd09639 279 ---VATQVIEASlDISVDVMITELA----------------------------PIDSLIQRLGRLHRYGEKNGEEVYIIT 327
|
410
....*....|....*.
gi 15227913 1735 HAPRKEYYKKFLYEAL 1750
Cdd:cd09639 328 DAPDGKGQKPYPYDLV 343
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
1349-1481 |
7.26e-04 |
|
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: 43.08 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1349 FKHFNPVQTQVFTVLYNTSDNVVVAaPTGSGKTicAEFAI-------------LRNHLEGPdsamRVVYIAPLEAIAKeQ 1415
Cdd:cd17945 10 YKEPTPIQRQAIPIGLQNRDIIGIA-ETGSGKT--AAFLIpllvyisrlppldEETKDDGP----YALILAPTRELAQ-Q 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227913 1416 FRDWEKKFGKGLGLRVVELTGETLLD---LKLLEKGQIIISTPEKW-DALSRRwkqrkYI--QQVSLFIVDE 1481
Cdd:cd17945 82 IEEETQKFAKPLGIRVVSIVGGHSIEeqaFSLRNGCEILIATPGRLlDCLERR-----LLvlNQCTYVVLDE 148
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
1370-1485 |
7.94e-04 |
|
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: 43.98 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1370 VVVAAPTGSGKTICAefAILRNHLEGPDSAMRVVYIAPLEAIAKEQFRDWEKKFGKGLGLR-----------------VV 1432
Cdd:TIGR01587 2 LVIEAPTGYGKTEAA--LLWALHSIKSQKADRVIIALPTRATINAMYRRAKELFGSELVGLhhsssfsrikemgdseeFE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15227913 1433 ELTGETLLDLKLLEKGQIIISTPEK-WDALSRRWKQRKYIQ---QVSLFIVDELHLI 1485
Cdd:TIGR01587 80 HLFPLYIHSNDKLFLDPITVCTIDQvLKSVFGEFGHYEFTLasiANSLLIFDEVHFY 136
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
799-883 |
7.95e-04 |
|
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: 42.25 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 799 LKELLP-YGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPAHTVIIkgtqVYNPERgewMELSPLdvMQM 877
Cdd:cd18792 54 LKELVPeARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMI----IEDADR---FGLSQL--HQL 124
|
....*.
gi 15227913 878 IGRAGR 883
Cdd:cd18792 125 RGRVGR 130
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
525-643 |
8.83e-04 |
|
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350749 [Multi-domain] Cd Length: 193 Bit Score: 42.56 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 525 LLCAPTGAGKTNVAVLTILHQLGlnmnpggtfnhGNYKIVYVAPMKALVAEVVDSLSQRLKDFGVTVKELSG-----DQS 599
Cdd:cd17991 40 LICGDVGFGKTEVAMRAAFKAVL-----------SGKQVAVLVPTTLLAQQHYETFKERFANFPVNVELLSRfttaaEQR 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15227913 600 LTGQEIKETQIivttpekwDII--TRK--SGDRTYTQLvRLLIIDEIH 643
Cdd:cd17991 109 EILEGLKEGKV--------DIVigTHRllSKDVEFKNL-GLLIIDEEQ 147
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
502-691 |
9.58e-04 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 44.13 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 502 GMQQLNRVQSKVYGTALFKADNILLcAPTGAGKTNVAVLTILHQLgLNMNPGGTFNHGNYKIVYVAPMKALVAEVVDSLS 581
Cdd:PRK01297 106 GFPYCTPIQAQVLGYTLAGHDAIGR-AQTGTGKTAAFLISIINQL-LQTPPPKERYMGEPRALIIAPTRELVVQIAKDAA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 582 QRLKDFGVTVKELSG----DQSLTGQEIKETQIIVTTPEKW-DIITRKSgdrTYTQLVRLLIIDEI-HLLDDNRGPVLES 655
Cdd:PRK01297 184 ALTKYTGLNVMTFVGgmdfDKQLKQLEARFCDILVATPGRLlDFNQRGE---VHLDMVEVMVLDEAdRMLDMGFIPQVRQ 260
|
170 180 190
....*....|....*....|....*....|....*.
gi 15227913 656 IVARTLRqiestKEHIRLVGLSATLpnCDDVASFLR 691
Cdd:PRK01297 261 IIRQTPR-----KEERQTLLFSATF--TDDVMNLAK 289
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
523-658 |
2.33e-03 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) 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: 350713 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 523 NILLCAPTGAGKTNVAVLTILHQLGlnMNPGGTFNhgnykiVYVAPMKAL---VAEVVDSLSQRLkdfGVTVKELSGDQS 599
Cdd:cd17955 38 DVIGGAKTGSGKTAAFALPILQRLS--EDPYGIFA------LVLTPTRELayqIAEQFRALGAPL---GLRCCVIVGGMD 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227913 600 LTGQEIKETQ---IIVTTPEKW-DIITRKSGDRTYTQLVRLLIIDEI-HLLDDNRGPVLESIVA 658
Cdd:cd17955 107 MVKQALELSKrphIVVATPGRLaDHLRSSDDTTKVLSRVKFLVLDEAdRLLTGSFEDDLATILS 170
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
782-883 |
2.75e-03 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 40.32 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 782 QSREILKCLAGLLKNNDLKE-LLPYGFAIHHAGLTRTDREIVENQFRWGNLQVLISTATLAWGVN---LPAhtVIIKGtq 857
Cdd:cd18797 43 RSRKLAELLLRYLKARLVEEgPLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDiggLDA--VVLAG-- 118
|
90 100
....*....|....*....|....*.
gi 15227913 858 vyNPErgewmelSPLDVMQMIGRAGR 883
Cdd:cd18797 119 --YPG-------SLASLWQQAGRAGR 135
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
1369-1481 |
4.39e-03 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) 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: 350713 [Multi-domain] Cd Length: 204 Bit Score: 40.67 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1369 NVVVAAPTGSGKTICAEFAILRNHLEGPDSAMRVVYIAPLE---AIAkEQFRdwekKFGKGLGLRVVELTGEtlLD---- 1441
Cdd:cd17955 38 DVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRElayQIA-EQFR----ALGAPLGLRCCVIVGG--MDmvkq 110
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15227913 1442 -LKLLEKGQIIISTPEKW-DALSRRWKQRKYIQQVSLFIVDE 1481
Cdd:cd17955 111 aLELSKRPHIVVATPGRLaDHLRSSDDTTKVLSRVKFLVLDE 152
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1324-1485 |
5.04e-03 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 41.99 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1324 TELLDLQPLPVMALRNPSYETLYQDFK----HFNPVQTQVFTVLYNTSDN----VVVAAPTGSGKTIcAEFAILRNHLEG 1395
Cdd:COG1203 96 SANFDMARQALDHLLAERLERLLPKKSkprtPINPLQNEALELALEAAEEepglFILTAPTGGGKTE-AALLFALRLAAK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 1396 PDsAMRVVYIAPLEAIAkEQ-FRDWEKKFGKGLGL----------RVVELTGETLLDLKLLEK---GQIIISTPEK-WDA 1460
Cdd:COG1203 175 HG-GRRIIYALPFTSII-NQtYDRLRDLFGEDVLLhhsladldllEEEEEYESEARWLKLLKElwdAPVVVTTIDQlFES 252
|
170 180
....*....|....*....|....*...
gi 15227913 1461 L-SRRWKQ-RKYIQQV-SLFIVDELHLI 1485
Cdd:COG1203 253 LfSNRKGQeRRLHNLAnSVIILDEVQAY 280
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
811-883 |
9.36e-03 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 40.97 E-value: 9.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227913 811 HAGLTRTDREIVENQFRWGNLQVLISTATLAWGVNLPAHTVIIKgtqvYNpergewMELSPLDVMQMIGRAGR 883
Cdd:PTZ00424 298 HGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVIN----YD------LPASPENYIHRIGRSGR 360
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
517-643 |
9.45e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 39.44 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 517 ALFKADNILLCAPTGAGKtnvavlTILHQLGLNMNPGGTfnhgnykIVyVAPMKALVAEVVDSLSQRlkdfGVTVKELSG 596
Cdd:cd17920 23 AVLAGRDVLVVMPTGGGK------SLCYQLPALLLDGVT-------LV-VSPLISLMQDQVDRLQQL----GIRAAALNS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227913 597 DQSLTGQE-----IK--ETQIIVTTPEK------WDIITRKsgdrTYTQLVRLLIIDEIH 643
Cdd:cd17920 85 TLSPEEKRevllrIKngQYKLLYVTPERllspdfLELLQRL----PERKRLALIVVDEAH 140
|
|
| |
