|
Name |
Accession |
Description |
Interval |
E-value |
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1501-1804 |
2.79e-145 |
|
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: 454.35 E-value: 2.79e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1501 TELGRIASHFYVTHHSMATYNQHLKPMMGHIELFRVFALSDEFKYIPVREEEKMELSKLLERVPVPVKESIEEPTAKINV 1580
Cdd:pfam02889 2 TDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKGDIEDPHAKVNI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1581 LLQAYISQLRLDGFALVSDMVYVTQSAGRILRAIFEICLKRGWAQLTQKALDLCKMVEKRAWLSMSPLRQFKAMPADLVK 1660
Cdd:pfam02889 82 LLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPELIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1661 RLERKEFPWER--YFDLSTQELGELVGQTQAGRTLHRYVHQFPKLELQAHVQPVTRSLLKMELTITPDFQWDEKVHGVAE 1738
Cdd:pfam02889 162 KLEKKGVESVRdiLELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGKSE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1945600751 1739 AFWIMVEDVDGEHILHHEYFVLKQRYAEEEHLVSFTVPLYEPLPPNYFVTVVADRWLHSSTKLPVS 1804
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 ... |
979-1193 |
1.83e-144 |
|
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: 447.97 E-value: 1.83e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 979 IKDLPQWAQEAFPGAESLNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRDPQTGhIDLDSFKIVYIA 1058
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGT-INLDAFKIVYIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1059 PMKALVQEMVGNFSRRLRPYGISVAELTGDRQLTKQQIAETQIIVTTPEKWDVITRKATDRSYTALVRLIIIDEIHLLHD 1138
Cdd:cd18019 80 PMKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1945600751 1139 DRGPVLESIVSRTIRTMEQTQELVRLVGLSATLPNYADVAAFLRVNPKTGLFFFD 1193
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1844-2031 |
1.80e-120 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 378.14 E-value: 1.80e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1844 IDHFNPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALLRLWSSSEEARAVYVAPFQEIVDQRAADWKQKFK---GKE 1920
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGpllGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1921 IVTLTGETSADLKLLERGDVICCTPAQWDVVSRRWKQRKNVQNVNLFIADELHLIGGDIGPTYEVIVSRMRYIASQTNKS 2000
Cdd:cd18021 81 VVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 1945600751 2001 IRIVALSTSLANARDLGEWIGATSHSVFNFH 2031
Cdd:cd18021 161 IRIVGLSSSLANARDVGEWLGASKSTIFNFH 191
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1498-1806 |
6.03e-116 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 370.44 E-value: 6.03e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1498 FQVTELGRIASHFYVTHHSMATYNQHLKPMMGHIELFRVFALSDEFKYIPVREEEKMELSKLLERVPVPVK-ESIEEPTA 1576
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLEnPSLDDPHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1577 KINVLLQAYISQLRLDGFALVSDMVYVTQSAGRILRAIFEICLKRGWAQLTQKALDLCKMVEKRAWLSMSPLRQFKAMPA 1656
Cdd:smart00611 82 KANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1657 DLVKRLERKE-FPWERYFDLSTQELGELVGQTQA-GRTLHRYVHQFPKLELQAHVQPVTRSLLKMELTITPDFQWDEKVH 1734
Cdd:smart00611 162 EILKRLEKKKvLSLEDLLELEDEERGELLGLLDAeGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEIH 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1945600751 1735 GVAEAFWIMVEDVDGEHILHHEYFVLKQRYAEEEHLVSFTVPLYEPLpPNYFVTVVADRWLHSSTKLPVSFK 1806
Cdd:smart00611 242 GKQEGWWLVIGDSDGNELLHIERFSLNKKNVSEEVKLDFTAPATEGN-YQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
2328-2639 |
2.20e-110 |
|
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: 354.58 E-value: 2.20e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2328 PLNLGMIAAYYNINYTTVDMFSVSLKSTTKLKGLLEIVASATEFDGIPIRHQEDNVLKRIYDRLPVKLAtPKFNTPRIKT 2407
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVK-GDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2408 NVLLQAHFSRMQLP-PDLQSDQALVLGRVIPLLQACVDVISSNGWLSPALAAMELSQMSVQAMWDRDSPLKQVPYFNGDI 2486
Cdd:pfam02889 80 NILLQAYISRLKLPgFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2487 IKRCEEKEVESVFDIMELEDDVRNDVLRMDQRKLREVARFVNRYPSVEVGFDVadldSIASGGVVNVKVQLEreadedee 2566
Cdd:pfam02889 160 IKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEV----QPITRSVLRVEVTIT-------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2567 igeviaPFFPGKKD-----EGWWIVIGDPVTKTLLAIKRVTLQHKL---TVKLDFIAP--KAGHHNLKVFLMSDSFNGCD 2636
Cdd:pfam02889 228 ------PDFPWDKRvhgksEGFWLVVGDSDGNEILHIERFTLTKRTlagEHKLEFTVPpsDPGPPQLFVRLISDSWLGAD 301
|
...
gi 1945600751 2637 QEL 2639
Cdd:pfam02889 302 QEV 304
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
2325-2644 |
9.13e-107 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 344.24 E-value: 9.13e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2325 DVSPLNLGMIAAYYNINYTTVDMFSVSLKSTTKLKGLLEIVASATEFDGIPIRHQEDNVLKRIYDRLPVKLATPKFNTPR 2404
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2405 IKTNVLLQAHFSRMQLPP-DLQSDQALVLGRVIPLLQACVDVISSNGWLSPALAAMELSQMSVQAMWDRDSPLKQVPYFN 2483
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSfALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2484 GDIIKRCEEKEVESVFDIMELEDDVRNDVLRMDQRKLREVARFVNRYPSVEVGFDVADLDSIASGGVVNVKVQLEReade 2563
Cdd:smart00611 161 EEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTW---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2564 DEEIGEviapffpgkKDEGWWIVIGDPVTKTLLAIKRVTLQHK---LTVKLDFIAP-KAGHHNLKVFLMSDSFNGCDQEL 2639
Cdd:smart00611 237 DDEIHG---------KQEGWWLVIGDSDGNELLHIERFSLNKKnvsEEVKLDFTAPaTEGNYQYTLRLVSDSYLGCDQEY 307
|
....*
gi 1945600751 2640 DMELD 2644
Cdd:smart00611 308 PLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
979-1539 |
1.14e-103 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 344.19 E-value: 1.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 979 IKDLP-QWAQEAF--PGAESLNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldsfKIV 1055
Cdd:COG1204 3 VAELPlEKVIEFLkeRGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------KAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1056 YIAPMKALVQEMVGNFSRRLRPYGISVAELTGDRQLTKQQIAETQIIVTTPEKWDVITRKatdrSYTAL--VRLIIIDEI 1133
Cdd:COG1204 71 YIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRN----GPSWLrdVDLVVVDEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1134 HLLHD-DRGPVLESIVSRtIRTMEQTqelVRLVGLSATLPNYADVAAFLRVNPktglffFDGAFRPCPLKqqfIGVTEKK 1212
Cdd:COG1204 147 HLIDDeSRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPLN---EGVLYDG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1213 AIK---RFQVMNDVCYEKVMEQLDQREenQVLVFVHSRKETAKTAKTLRDMALEKDTIGHFLKQDSASREVLQTEAATVK 1289
Cdd:COG1204 214 VLRfddGSRRSKDPTLALALDLLEEGG--QVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1290 DPNLADLLPYGFAIHHAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPAHAVIIKgtqiySPEKGRWVELSPQDVL 1369
Cdd:COG1204 292 NEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-----DTKRGGMVPIPVLEFK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1370 QMLGRAGRPQFDTYGEGIIITAHTELQYYL---SLLNTQLPIESQFVKRMAD--NLNAEIVLGTIRNRDEAVQWLGYTYL 1444
Cdd:COG1204 367 QMAGRAGRPGYDPYGEAILVAKSSDEADELferYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFY 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1445 YVRMLRNPTLYNV--SIDDLDDDPYLEQkrvdlihsaatildkcnlikydkKSGRFQVTELGRIASHFYVTHHSMATYNQ 1522
Cdd:COG1204 447 AYQYDKGDLEEVVddALEFLLENGFIEE-----------------------DGDRLRATKLGKLVSRLYIDPLTAAELVD 503
|
570
....*....|....*..
gi 1945600751 1523 HLKPMMGHIELFRVFAL 1539
Cdd:COG1204 504 GLRKADEEFTDLGLLHL 520
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1197-1390 |
5.68e-67 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 223.58 E-value: 5.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1197 RPCPLKQQFIGVTEKKAIKRFQVMN----DVCYEKVMEQLdqREENQVLVFVHSRKETAKTAKTLRdmalekdtighflk 1272
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNkfdsDIIVLLKIETV--SEGKPVLVFCSSRKECEKTAKDLA-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1273 qdsasrevlqteaatvkdpnladllpyGFAIHHAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPAHAVIIKGTQI 1352
Cdd:cd18795 65 ---------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQR 117
|
170 180 190
....*....|....*....|....*....|....*...
gi 1945600751 1353 YSPEkgRWVELSPQDVLQMLGRAGRPQFDTYGEGIIIT 1390
Cdd:cd18795 118 YDGK--GYRELSPLEYLQMIGRAGRPGFDTRGEAIIMT 153
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1844-2366 |
3.73e-61 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 220.54 E-value: 3.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1844 IDHFNPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALLRLWSSSEeaRAVYVAPFQEIVDQRAADWKQKF--KGKEI 1921
Cdd:COG1204 20 IEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG--KALYIVPLRALASEKYREFKRDFeeLGIKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1922 VTLTGETSADLKLLERGDVICCTPAQWDVVSRrwKQRKNVQNVNLFIADELHLIG-GDIGPTYEVIVSRMRYIasqtNKS 2000
Cdd:COG1204 98 GVSTGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTLEVLLARLRRL----NPE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2001 IRIVALSTSLANARDLGEWIGATshsvfNFHPSVRPVPL--------EIHM-QSYNIPHFASLmmamakptYLAITTHSA 2071
Cdd:COG1204 172 AQIVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLnegvlydgVLRFdDGSRRSKDPTL--------ALALDLLEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2072 NKPVIVFVPSRKQCRLTAVDIITYCigDDTPDRFLHCKLEEIQPMLDRLQD-----KTLVETLQHGIGFYHEALSKQDKR 2146
Cdd:COG1204 239 GGQVLVFVSSRRDAESLAKKLADEL--KRRLTPEEREELEELAEELLEVSEethtnEKLADCLEKGVAFHHAGLPSELRR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2147 IVEQLYESGAIQVVVASrDTCWA---LPlnSHMVIVMGTqyfegkeHRYADYPIT--DVLQMMGRACRPREDDTGKCVLM 2221
Cdd:COG1204 317 LVEDAFREGLIKVLVAT-PTLAAgvnLP--ARRVIIRDT-------KRGGMVPIPvlEFKQMAGRAGRPGYDPYGEAILV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2222 CQANK--KEFYKKFLY-EALPVESHLDQL--LHDHFNAEIVTKTIENKQDAVDYLTWTFLYrrmahnpnyyglqgtsHRH 2296
Cdd:COG1204 387 AKSSDeaDELFERYILgEPEPIRSKLANEsaLRTHLLALIASGFANSREELLDFLENTFYA----------------YQY 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1945600751 2297 LSDHLSELVETTLNDLQETKCITIEDEMdVSPLNLGMIAAYYNINYTTVDMFSVSLKSTTK---LKGLLEIVA 2366
Cdd:COG1204 451 DKGDLEEVVDDALEFLLENGFIEEDGDR-LRATKLGKLVSRLYIDPLTAAELVDGLRKADEeftDLGLLHLIL 522
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
981-1394 |
2.24e-54 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 205.19 E-value: 2.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 981 DLPQWAQEAF--PGAESLNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldsfKIVYIA 1058
Cdd:PRK02362 7 PLPEGVIEFYeaEGIEELYPPQAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIARGG------------KALYIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1059 PMKALVQEMVGNFSRrLRPYGISVAELTGDRQLTKQQIAETQIIVTTPEKWDVITRKATdrSYTALVRLIIIDEIHLLHD 1138
Cdd:PRK02362 75 PLRALASEKFEEFER-FEELGVRVGISTGDYDSRDEWLGDNDIIVATSEKVDSLLRNGA--PWLDDITCVVVDEVHLIDS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1139 -DRGPVLESivsrTIRTMEQTQELVRLVGLSATLPNYADVAAFLR----------VNPKTGLFFfDGAFRpCPLKQQFIG 1207
Cdd:PRK02362 152 aNRGPTLEV----TLAKLRRLNPDLQVVALSATIGNADELADWLDaelvdsewrpIDLREGVFY-GGAIH-FDDSQREVE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1208 VTEKKaikrfQVMNDVcyekvmeqLDQREEN-QVLVFVHSRKETAKTAKTLRDmALEKdtigHFLKQDSAS--------R 1278
Cdd:PRK02362 226 VPSKD-----DTLNLV--------LDTLEEGgQCLVFVSSRRNAEGFAKRAAS-ALKK----TLTAAERAElaelaeeiR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1279 EVLQTEaaTVKDpnLADLLPYGFAIHHAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPAHAVIIKGTQIYSPEKG 1358
Cdd:PRK02362 288 EVSDTE--TSKD--LADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAG 363
|
410 420 430
....*....|....*....|....*....|....*....
gi 1945600751 1359 rwveLSPQDVL---QMLGRAGRPQFDTYGEGIIItAHTE 1394
Cdd:PRK02362 364 ----MQPIPVLeyhQMAGRAGRPGLDPYGEAVLL-AKSY 397
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
760-868 |
1.65e-50 |
|
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 is required for the assembly of a catalytically active spliceosome on a messenger RNA precursor. The domain is found in the N-terminal region and is non-canonically PWI-like. The PWI-like domain is thought to be involved in protein-protein interactions.
Pssm-ID: 436309 Cd Length: 111 Bit Score: 174.72 E-value: 1.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 760 KSDAISPHDLDAFWLQRQIATHYPDPHTAQEKTMKAFDILGAESSNMRDCENELMGLFDYDKFDLVRILTKNREIIYWCT 839
Cdd:pfam18149 1 DKDSLDPHDIDAFWLQRLLSKFYGDAIEAQKKAEEVLDILESAADDLRECENQLVELLDYDKFDLVKLLLKNRDKIVWCT 80
|
90 100 110
....*....|....*....|....*....|.
gi 1945600751 840 RLAR-VDGAEKSELEKEMQQK-GLGWILHDL 868
Cdd:pfam18149 81 KLARaQSEEEKQAIEEEMRSNpGLAWILDEL 111
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1008-1512 |
2.78e-50 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 191.63 E-value: 2.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1008 FGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldsfKIVYIAPMKALVQEMVGNFSRrLRPYGISVAELTG 1087
Cdd:PRK01172 34 LRKGENVIVSVPTAAGKTLIAYSAIYETFLAGL------------KSIYIVPLRSLAMEKYEELSR-LRSLGMRVKISIG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1088 DRQLTKQQIAETQIIVTTPEKWDVITRKatDRSYTALVRLIIIDEIHLLHD-DRGPVLESIVSrTIRTMEQTqelVRLVG 1166
Cdd:PRK01172 101 DYDDPPDFIKRYDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDeDRGPTLETVLS-SARYVNPD---ARILA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1167 LSATLPNYADVAAFLRVNpktglfFFDGAFRPCPLKqqfIGVTEKKAI-----KRFQV-MNDVCYEKVmeqldqREENQV 1240
Cdd:PRK01172 175 LSATVSNANELAQWLNAS------LIKSNFRPVPLK---LGILYRKRLildgyERSQVdINSLIKETV------NDGGQV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1241 LVFVHSRKETAKTAKTLrdmalekdtIGHFlkqDSASREVLQTEAATVKDPNLADLLPYGFAIHHAGMTRADRTLVEDLF 1320
Cdd:PRK01172 240 LVFVSSRKNAEDYAEML---------IQHF---PEFNDFKVSSENNNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1321 ADGHVKVLCSTATLAWGVNLPAHAVIIKGTQIYSPEKGRWveLSPQDVLQMLGRAGRPQFDTYGEGIIITA----HTELQ 1396
Cdd:PRK01172 308 RNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRY--LSNMEIKQMIGRAGRPGYDQYGIGYIYAAspasYDAAK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1397 YYLSllNTQLPIESQFVK--RMADNLNAEIVLGTIRNRDEAVQWLGYTYLYVRmlrnptlynvsiDDLDDDPYleqkrvd 1474
Cdd:PRK01172 386 KYLS--GEPEPVISYMGSqrKVRFNTLAAISMGLASSMEDLILFYNETLMAIQ------------NGVDEIDY------- 444
|
490 500 510
....*....|....*....|....*....|....*...
gi 1945600751 1475 LIHSAATILDKCNLIKYDKKsgrFQVTELGRIASHFYV 1512
Cdd:PRK01172 445 YIESSLKFLKENGFIKGDVT---LRATRLGKLTSDLYI 479
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
2035-2223 |
4.05e-42 |
|
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: 152.32 E-value: 4.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2035 RPVPLEIHMQSYNIPHFASLMMAMAK-----PTYLAITTHSANKPVIVFVPSRKQCRLTAVDIItycigddtpdrflhck 2109
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2110 leeiqpmldrlqdktlvetlqhGIGFYHEALSKQDKRIVEQLYESGAIQVVVASRDTCWALPLNSHMVIVMGTQYFEGKE 2189
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 1945600751 2190 HRYadYPITDVLQMMGRACRPREDDTGKCVLMCQ 2223
Cdd:cd18795 123 YRE--LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1844-2395 |
1.14e-37 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 153.82 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1844 IDHFNPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALL-RLWssSEEARAVYVAPFQEIVDQRAADWKQKFK-GKEI 1921
Cdd:PRK00254 21 IEELYPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVnKLL--REGGKAVYLVPLKALAEEKYREFKDWEKlGLRV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1922 VTLTGETSADLKLLERGDVICCTPAQWDVVSR---RWkqrknVQNVNLFIADELHLIGG-DIGPTYEVIVSRMRYIAsqt 1997
Cdd:PRK00254 99 AMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSyDRGATLEMILTHMLGRA--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1998 nksiRIVALSTSLANARDLGEWIGAtSHSVFNFhpsvRPVPLE--IHMQSYNIPHFASLMMAMAKPTYLAITTHSANKPV 2075
Cdd:PRK00254 171 ----QILGLSATVGNAEELAEWLNA-ELVVSDW----RPVKLRkgVFYQGFLFWEDGKIERFPNSWESLVYDAVKKGKGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2076 IVFVPSRKQCRLTAVDIitycigDDTPDRFLHCK-LEEIQPMLDRLQD----KTLVETLQHGIGFYHEALSKQDKRIVEQ 2150
Cdd:PRK00254 242 LVFVNTRRSAEKEALEL------AKKIKRFLTKPeLRALKELADSLEEnptnEKLKKALRGGVAFHHAGLGRTERVLIED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2151 LYESGAIQVVVASRDTCWALPLNSHMVIVMGTQyfegkehRYADY-----PITDVLQMMGRACRPREDDTGKCVLMCQAN 2225
Cdd:PRK00254 316 AFREGLIKVITATPTLSAGINLPAFRVIIRDTK-------RYSNFgwediPVLEIQQMMGRAGRPKYDEVGEAIIVATTE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2226 K-KEFYKKF-------LYEALPVESHL-DQLLhdhfnAEIVTKTIENKQDAVDYLTWTFlyrrmahnpnyYGLQGTSHRH 2296
Cdd:PRK00254 389 EpSKLMERYifgkpekLFSMLSNESAFrSQVL-----ALITNFGVSNFKELVNFLERTF-----------YAHQRKDLYS 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2297 LSDHLSELVETTL-NDLQEtkcITIEDEmdVSPLNLGMIAAYYNINYTTVDMFSVSLKSTTKLK---GLLEIVASATEFD 2372
Cdd:PRK00254 453 LEEKAKEIVYFLLeNEFID---IDLEDR--FIPLPLGIRTSQLYIDPLTAKKFKDAFPKIEKNPnplGIFQLIASTPDMT 527
|
570 580
....*....|....*....|...
gi 1945600751 2373 GIPIRHQEDNVLKRIYDRLPVKL 2395
Cdd:PRK00254 528 PLNYSRKEMEDLLDEAYEMEDRL 550
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
997-1172 |
2.02e-34 |
|
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: 130.83 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 997 NRVQSRLYPTAFgSDENVLLCAPTGAGKTNVAMLTVLHEINKNrdpqtghidLDSFKIVYIAPMKALVQEMVGNFSRRLR 1076
Cdd:pfam00270 1 TPIQAEAIPAIL-EGRDVLVQAPTGSGKTLAFLLPALEALDKL---------DNGPQALVLAPTRELAEQIYEELKKLGK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1077 PYGISVAELTG--DRQLTKQQIAETQIIVTTPEKWDVITRKatdRSYTALVRLIIIDEIHLLHD-DRGPVLESIVSRtir 1153
Cdd:pfam00270 71 GLGLKVASLLGgdSRKEQLEKLKGPDILVGTPGRLLDLLQE---RKLLKNLKLLVLDEAHRLLDmGFGPDLEEILRR--- 144
|
170
....*....|....*....
gi 1945600751 1154 tmeqTQELVRLVGLSATLP 1172
Cdd:pfam00270 145 ----LPKKRQILLLSATLP 159
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
992-1205 |
1.16e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 109.89 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 992 GAESLNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRDPQTghidldsfkiVYIAPMKALVQEMVGNF 1071
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV----------LVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1072 SRRLRPYGISVAELTGD----RQLTKQQIAETQIIVTTPEKWdvITRKATDRSYTALVRLIIIDEIHLLHD-DRGPVLES 1146
Cdd:smart00487 75 KKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRL--LDLLENDKLSLSNVDLVILDEAHRLLDgGFGDQLEK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1945600751 1147 IVSRTIRTmeqtqelVRLVGLSATLPNYADVAAFLRVNpktGLFFFDGAFRPCPLKQQF 1205
Cdd:smart00487 153 LLKLLPKN-------VQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLEPIEQF 201
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1848-2016 |
1.97e-25 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 105.02 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1848 NPIQTQVFNTLYTtNDNVFIGAPTGSGKTVCAEFALL-RLWSSSEEARAVYVAPFQEIVDQRAADWKQKFKGKEI---VT 1923
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALeALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkvaSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1924 LTG-ETSADLKLLERGDVICCTPAQWDVVSRrwkQRKNVQNVNLFIADELHLIGG-DIGPTYEVIVSRMRyiasqtnKSI 2001
Cdd:pfam00270 80 LGGdSRKEQLEKLKGPDILVGTPGRLLDLLQ---ERKLLKNLKLLVLDEAHRLLDmGFGPDLEEILRRLP-------KKR 149
|
170
....*....|....*.
gi 1945600751 2002 RIVALSTSLA-NARDL 2016
Cdd:pfam00270 150 QILLLSATLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1839-2007 |
3.86e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1839 VYSGWIDHFNPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALLRLWSSSEEARAVYVAPFQEIVDQ---RAADWKQK 1915
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQwaeELKKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1916 FKGKEIVTLTGETS-ADLKLLERG--DVICCTPAQWDVVSRRWKqrKNVQNVNLFIADELH-LIGGDIGPTYEVIVSRMR 1991
Cdd:smart00487 81 LGLKVVGLYGGDSKrEQLRKLESGktDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP 158
|
170
....*....|....*.
gi 1945600751 1992 yiasqtnKSIRIVALS 2007
Cdd:smart00487 159 -------KNVQLLLLS 167
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
1007-1378 |
4.06e-17 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 88.38 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1007 AFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRDPQTGHIdldsfKIVYIAPMKALVQEMVGNFSRRLRPYG--ISVAE 1084
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSLIDLAGPEAPKEKGL-----HTLYITPLRALAVDIARNLQAPIEELGlpIRVET 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1085 LTGD---RQLTKQQIAETQIIVTTPEKWDV-ITRKATDRSYTALvRLIIIDEIH-LLHDDRGPVLESIVSRtirtMEQTQ 1159
Cdd:TIGR04121 99 RTGDtssSERARQRKKPPDILLTTPESLALlLSYPDAARLFKDL-RCVVVDEWHeLAGSKRGDQLELALAR----LRRLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1160 ELVRLVGLSATLPNYADVAAFLrVNPKTglfffdgafRPCPLkqqfIGVTEKKAIKRFQVMNDV-------------CYE 1226
Cdd:TIGR04121 174 PGLRRWGLSATIGNLEEARRVL-LGVGG---------APAVL----VRGKLPKAIEVISLLPESeerfpwaghlglrALP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1227 KVMEQLDQreENQVLVFVHSRKETAKTAKTLRDmalekdtighflkqdsasrevlqteaatvKDPNLADLLpygfAIHHA 1306
Cdd:TIGR04121 240 EVYAEIDQ--ARTTLVFTNTRSQAELWFQALWE-----------------------------ANPEFALPI----ALHHG 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1945600751 1307 GMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPAHAVIIkgtQIYSPeKG--RwvelspqdVLQMLGRAG-RP 1378
Cdd:TIGR04121 285 SLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSP-KGvaR--------LLQRAGRSNhRP 347
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
981-1399 |
5.76e-17 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 87.97 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 981 DLPQWAQEAFpgAESLNRVQ-SRLYP---TAFG---SDENVLLCAPTGAGKTNVAMLTVLHEINKNRDPqtghidldsfK 1053
Cdd:COG1205 36 PWPDWLPPEL--RAALKKRGiERLYShqaEAIEaarAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA----------T 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1054 IVYIAPMKALVQEMVGNFSRRLRPYG--ISVAELTGDrqlTKQQI-----AETQIIVTTP-----------EKWdvitrk 1115
Cdd:COG1205 104 ALYLYPTKALARDQLRRLRELAEALGlgVRVATYDGD---TPPEErrwirEHPDIVLTNPdmlhygllphhTRW------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1116 atDRSYTALvRLIIIDEIHLLhddRGpVLESIVSRTIRtmeqtqelvRL-------------VGLSATLPNYADVAAFLr 1182
Cdd:COG1205 175 --ARFFRNL-RYVVIDEAHTY---RG-VFGSHVANVLR---------RLrricrhygsdpqfILASATIGNPAEHAERL- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1183 vnpkTGLFF----FDGAFRP--------CPLKQQFI---GVTEKKAIKRFQVMNDVcyekvmeqldqreenQVLVFVHSR 1247
Cdd:COG1205 238 ----TGRPVtvvdEDGSPRGertfvlwnPPLVDDGIrrsALAEAARLLADLVREGL---------------RTLVFTRSR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1248 KETAKTAKTLRDMAlekdtighflkqdsasrevlqteaatvKDPNLADLLpygfAIHHAGMTRADRTLVEDLFADGHVKV 1327
Cdd:COG1205 299 RGAELLARYARRAL---------------------------REPDLADRV----AAYRAGYLPEERREIERGLRSGELLG 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1945600751 1328 LCSTATLAWGVNLPA-HAVIIKGtqiYSPekgrwvelSPQDVLQMLGRAGRPQfdtyGEGIIITAHTE--L-QYYL 1399
Cdd:COG1205 348 VVSTNALELGIDIGGlDAVVLAG---YPG--------TRASFWQQAGRAGRRG----QDSLVVLVAGDdpLdQYYV 408
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1293-1378 |
1.35e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 73.79 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1293 LADLL---PYGFAIHHAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLP-AHAVIIKGtqiyspekgrwVELSPQDV 1368
Cdd:smart00490 3 LAELLkelGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASY 71
|
90
....*....|
gi 1945600751 1369 LQMLGRAGRP 1378
Cdd:smart00490 72 IQRIGRAGRA 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1225-1377 |
2.36e-10 |
|
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: 59.92 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1225 YEKVMEQLDQREENQVLVFVHSRKetaktaktlrdmalekdtighflkqdsasrevlqteaaTVKDPNLADLLPYGFAIH 1304
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKK--------------------------------------TLEAELLLEKEGIKVARL 44
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1945600751 1305 HAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLP-AHAVIikgtqIYSPEKgrwvelSPQDVLQMLGRAGR 1377
Cdd:pfam00271 45 HGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVI-----NYDLPW------NPASYIQRIGRAGR 107
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1793-2018 |
8.23e-09 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 61.39 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1793 RWLHSSTKLPVSFKHL-ILPEKYAPHTELHD-LQPLPVSALRNPEYEQVYSgwidHfnpiQTQVFNtLYTTNDNVFIGAP 1870
Cdd:COG1205 9 ERLRASPRYGDQIVHVrTIPAREARYAPWPDwLPPELRAALKKRGIERLYS----H----QAEAIE-AARAGKNVVIATP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1871 TGSGKTVCaeFAL--LRLWSSSEEARAVYVAP-----------FQEIVDQRAADWKqkfkgkeIVTLTGETSADL--KLL 1935
Cdd:COG1205 80 TASGKSLA--YLLpvLEALLEDPGATALYLYPtkalardqlrrLRELAEALGLGVR-------VATYDGDTPPEErrWIR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1936 ERGDVICCTPaqwDVV-------SRRWkqRKNVQNVNLFIADELHliggdigpTYE--------VIVSRMRYIASQTNKS 2000
Cdd:COG1205 151 EHPDIVLTNP---DMLhygllphHTRW--ARFFRNLRYVVIDEAH--------TYRgvfgshvaNVLRRLRRICRHYGSD 217
|
250
....*....|....*...
gi 1945600751 2001 IRIVALSTSLANARDLGE 2018
Cdd:COG1205 218 PQFILASATIGNPAEHAE 235
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
1862-1973 |
1.27e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 54.11 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1862 NDNVFIGAPTGSGKTVcaeFALL----RLwsSSEEARAVYVAPFQEIVDQRAADWKQKFKGK--EIVTLTGETSAD--LK 1933
Cdd:PRK13766 29 KKNTLVVLPTGLGKTA---IALLviaeRL--HKKGGKVLILAPTKPLVEQHAEFFRKFLNIPeeKIVVFTGEVSPEkrAE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1945600751 1934 LLERGDVICCTP--AQWDVVSRRWkqrkNVQNVNLFIADELH 1973
Cdd:PRK13766 104 LWEKAKVIVATPqvIENDLIAGRI----SLEDVSLLIFDEAH 141
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1726-1947 |
3.13e-05 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 49.31 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1726 DFQWDEKVHGVAEAFWIMVEDVDGEHILHHEYFVLKQRYAEEEHLVSFTVPLYEPLPPNYFVT--VVADRWLHSSTKLPV 1803
Cdd:COG1203 4 LAKEALLGALALAALLLLLLALLLAALLLLLLAALLLALLLALLLLAALELALLLLLLLLLLLllLLLLLDLLLDDLAFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1804 SFKHLILPEKYAphTELHDLQPLPVSALRNPEYEQVY---SGWIDHFNPIQTQVFN---TLYTTNDNVFI-GAPTGSGKT 1876
Cdd:COG1203 84 FLLLLIDADWLD--SANFDMARQALDHLLAERLERLLpkkSKPRTPINPLQNEALElalEAAEEEPGLFIlTAPTGGGKT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1877 vcaEFAL---LRLWSSSEEARAVYVAPFQEIVDQ---RAADW----------KQKFKGKEIVTLTGETSADLKLLER--- 1937
Cdd:COG1203 162 ---EAALlfaLRLAAKHGGRRIIYALPFTSIINQtydRLRDLfgedvllhhsLADLDLLEEEEEYESEARWLKLLKElwd 238
|
250
....*....|
gi 1945600751 1938 GDVICCTPAQ 1947
Cdd:COG1203 239 APVVVTTIDQ 248
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1501-1804 |
2.79e-145 |
|
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: 454.35 E-value: 2.79e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1501 TELGRIASHFYVTHHSMATYNQHLKPMMGHIELFRVFALSDEFKYIPVREEEKMELSKLLERVPVPVKESIEEPTAKINV 1580
Cdd:pfam02889 2 TDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKGDIEDPHAKVNI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1581 LLQAYISQLRLDGFALVSDMVYVTQSAGRILRAIFEICLKRGWAQLTQKALDLCKMVEKRAWLSMSPLRQFKAMPADLVK 1660
Cdd:pfam02889 82 LLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPELIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1661 RLERKEFPWER--YFDLSTQELGELVGQTQAGRTLHRYVHQFPKLELQAHVQPVTRSLLKMELTITPDFQWDEKVHGVAE 1738
Cdd:pfam02889 162 KLEKKGVESVRdiLELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGKSE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1945600751 1739 AFWIMVEDVDGEHILHHEYFVLKQRYAEEEHLVSFTVPLYEPLPPNYFVTVVADRWLHSSTKLPVS 1804
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 ... |
979-1193 |
1.83e-144 |
|
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: 447.97 E-value: 1.83e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 979 IKDLPQWAQEAFPGAESLNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRDPQTGhIDLDSFKIVYIA 1058
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGT-INLDAFKIVYIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1059 PMKALVQEMVGNFSRRLRPYGISVAELTGDRQLTKQQIAETQIIVTTPEKWDVITRKATDRSYTALVRLIIIDEIHLLHD 1138
Cdd:cd18019 80 PMKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1945600751 1139 DRGPVLESIVSRTIRTMEQTQELVRLVGLSATLPNYADVAAFLRVNPKTGLFFFD 1193
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1844-2031 |
1.80e-120 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 378.14 E-value: 1.80e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1844 IDHFNPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALLRLWSSSEEARAVYVAPFQEIVDQRAADWKQKFK---GKE 1920
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGpllGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1921 IVTLTGETSADLKLLERGDVICCTPAQWDVVSRRWKQRKNVQNVNLFIADELHLIGGDIGPTYEVIVSRMRYIASQTNKS 2000
Cdd:cd18021 81 VVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 1945600751 2001 IRIVALSTSLANARDLGEWIGATSHSVFNFH 2031
Cdd:cd18021 161 IRIVGLSSSLANARDVGEWLGASKSTIFNFH 191
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1498-1806 |
6.03e-116 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 370.44 E-value: 6.03e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1498 FQVTELGRIASHFYVTHHSMATYNQHLKPMMGHIELFRVFALSDEFKYIPVREEEKMELSKLLERVPVPVK-ESIEEPTA 1576
Cdd:smart00611 2 IWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLEnPSLDDPHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1577 KINVLLQAYISQLRLDGFALVSDMVYVTQSAGRILRAIFEICLKRGWAQLTQKALDLCKMVEKRAWLSMSPLRQFKAMPA 1656
Cdd:smart00611 82 KANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1657 DLVKRLERKE-FPWERYFDLSTQELGELVGQTQA-GRTLHRYVHQFPKLELQAHVQPVTRSLLKMELTITPDFQWDEKVH 1734
Cdd:smart00611 162 EILKRLEKKKvLSLEDLLELEDEERGELLGLLDAeGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEIH 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1945600751 1735 GVAEAFWIMVEDVDGEHILHHEYFVLKQRYAEEEHLVSFTVPLYEPLpPNYFVTVVADRWLHSSTKLPVSFK 1806
Cdd:smart00611 242 GKQEGWWLVIGDSDGNELLHIERFSLNKKNVSEEVKLDFTAPATEGN-YQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
2328-2639 |
2.20e-110 |
|
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: 354.58 E-value: 2.20e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2328 PLNLGMIAAYYNINYTTVDMFSVSLKSTTKLKGLLEIVASATEFDGIPIRHQEDNVLKRIYDRLPVKLAtPKFNTPRIKT 2407
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVK-GDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2408 NVLLQAHFSRMQLP-PDLQSDQALVLGRVIPLLQACVDVISSNGWLSPALAAMELSQMSVQAMWDRDSPLKQVPYFNGDI 2486
Cdd:pfam02889 80 NILLQAYISRLKLPgFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2487 IKRCEEKEVESVFDIMELEDDVRNDVLRMDQRKLREVARFVNRYPSVEVGFDVadldSIASGGVVNVKVQLEreadedee 2566
Cdd:pfam02889 160 IKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEV----QPITRSVLRVEVTIT-------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2567 igeviaPFFPGKKD-----EGWWIVIGDPVTKTLLAIKRVTLQHKL---TVKLDFIAP--KAGHHNLKVFLMSDSFNGCD 2636
Cdd:pfam02889 228 ------PDFPWDKRvhgksEGFWLVVGDSDGNEILHIERFTLTKRTlagEHKLEFTVPpsDPGPPQLFVRLISDSWLGAD 301
|
...
gi 1945600751 2637 QEL 2639
Cdd:pfam02889 302 QEV 304
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
2325-2644 |
9.13e-107 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 344.24 E-value: 9.13e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2325 DVSPLNLGMIAAYYNINYTTVDMFSVSLKSTTKLKGLLEIVASATEFDGIPIRHQEDNVLKRIYDRLPVKLATPKFNTPR 2404
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2405 IKTNVLLQAHFSRMQLPP-DLQSDQALVLGRVIPLLQACVDVISSNGWLSPALAAMELSQMSVQAMWDRDSPLKQVPYFN 2483
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSfALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2484 GDIIKRCEEKEVESVFDIMELEDDVRNDVLRMDQRKLREVARFVNRYPSVEVGFDVADLDSIASGGVVNVKVQLEReade 2563
Cdd:smart00611 161 EEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTW---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2564 DEEIGEviapffpgkKDEGWWIVIGDPVTKTLLAIKRVTLQHK---LTVKLDFIAP-KAGHHNLKVFLMSDSFNGCDQEL 2639
Cdd:smart00611 237 DDEIHG---------KQEGWWLVIGDSDGNELLHIERFSLNKKnvsEEVKLDFTAPaTEGNYQYTLRLVSDSYLGCDQEY 307
|
....*
gi 1945600751 2640 DMELD 2644
Cdd:smart00611 308 PLSFD 312
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
1501-1805 |
9.67e-107 |
|
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: 344.34 E-value: 9.67e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1501 TELGRIASHFYVTHHSMATYNQHLKPMMGHIELFRVFALSDEFKYIPVREEEKMELSKLLERVPVPVKESIEE-PTAKIN 1579
Cdd:smart00973 2 TELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDsPHAKVN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1580 VLLQAYISQLRLDGFALVSDMVYVTQSAGRILRAIFEICLKRGWAQLTQKALDLCKMVEKRAWL-SMSPLRQFKAM-PAD 1657
Cdd:smart00973 82 LLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEdSDSPLKQLPHFlIED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1658 LVKRLERKEFPW--ERYFDLSTQELGELVGQTQ-AGRTLHRYVHQFPKLELQAHVQPVTRSL-LKMELTITPDFQWDEKV 1733
Cdd:smart00973 162 VYDKLELKDGSRsfELLLDMNAAELGEFLNRLPpNGRLIYELLRRFPKIEVEAEVLPITRDLtLRVELEITPVFAWDLPR 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1945600751 1734 -HGVAEAFWIMVEDVDGEHILHHEYFVLKQRYAEEEHLVSFTVPLYEPLPPNYFVTVVADRWLHSSTKLPVSF 1805
Cdd:smart00973 242 hKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNEVKLDFTVPLSEPGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
979-1539 |
1.14e-103 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 344.19 E-value: 1.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 979 IKDLP-QWAQEAF--PGAESLNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldsfKIV 1055
Cdd:COG1204 3 VAELPlEKVIEFLkeRGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------KAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1056 YIAPMKALVQEMVGNFSRRLRPYGISVAELTGDRQLTKQQIAETQIIVTTPEKWDVITRKatdrSYTAL--VRLIIIDEI 1133
Cdd:COG1204 71 YIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRN----GPSWLrdVDLVVVDEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1134 HLLHD-DRGPVLESIVSRtIRTMEQTqelVRLVGLSATLPNYADVAAFLRVNPktglffFDGAFRPCPLKqqfIGVTEKK 1212
Cdd:COG1204 147 HLIDDeSRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPLN---EGVLYDG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1213 AIK---RFQVMNDVCYEKVMEQLDQREenQVLVFVHSRKETAKTAKTLRDMALEKDTIGHFLKQDSASREVLQTEAATVK 1289
Cdd:COG1204 214 VLRfddGSRRSKDPTLALALDLLEEGG--QVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1290 DPNLADLLPYGFAIHHAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPAHAVIIKgtqiySPEKGRWVELSPQDVL 1369
Cdd:COG1204 292 NEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-----DTKRGGMVPIPVLEFK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1370 QMLGRAGRPQFDTYGEGIIITAHTELQYYL---SLLNTQLPIESQFVKRMAD--NLNAEIVLGTIRNRDEAVQWLGYTYL 1444
Cdd:COG1204 367 QMAGRAGRPGYDPYGEAILVAKSSDEADELferYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFY 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1445 YVRMLRNPTLYNV--SIDDLDDDPYLEQkrvdlihsaatildkcnlikydkKSGRFQVTELGRIASHFYVTHHSMATYNQ 1522
Cdd:COG1204 447 AYQYDKGDLEEVVddALEFLLENGFIEE-----------------------DGDRLRATKLGKLVSRLYIDPLTAAELVD 503
|
570
....*....|....*..
gi 1945600751 1523 HLKPMMGHIELFRVFAL 1539
Cdd:COG1204 504 GLRKADEEFTDLGLLHL 520
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
995-1193 |
5.63e-102 |
|
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: 325.54 E-value: 5.63e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 995 SLNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRDPQtGHIDLDSFKIVYIAPMKALVQEMVGNFSRR 1074
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQG-GVIKKDDFKIVYIAPMKALAAEMVEKFSKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1075 LRPYGISVAELTGDRQLTKQQIAETQIIVTTPEKWDVITRKAT-DRSYTALVRLIIIDEIHLLHDDRGPVLESIVSRTIR 1153
Cdd:cd18020 80 LAPLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSgDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1945600751 1154 TMEQTQELVRLVGLSATLPNYADVAAFLRVNPKTGLFFFD 1193
Cdd:cd18020 160 QVESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
2328-2643 |
2.42e-91 |
|
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: 300.04 E-value: 2.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2328 PLNLGMIAAYYNINYTTVDMFSVSLKSTTKLKGLLEIVASATEFDGIPIRHQEDNVLKRIYDRLPVKLATPKFNTPRIKT 2407
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2408 NVLLQAHFSRMQLPP-DLQSDQALVLGRVIPLLQACVDVISSNGWLSPALAAMELSQMSVQAMW-DRDSPLKQVPYFNgd 2485
Cdd:smart00973 81 NLLLQAHLSRLPLPDfDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWeDSDSPLKQLPHFL-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2486 iikrceekeVESVFDIMELEDDVRNDVLRMDQrKLREVARFVNR-YPSVEVGFDVADLDSIASGGVVNVKVQLEREADED 2564
Cdd:smart00973 159 ---------IEDVYDKLELKDGSRSFELLLDM-NAAELGEFLNRlPPNGRLIYELLRRFPKIEVEAEVLPITRDLTLRVE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2565 EEIGEVIAPFFP--GKKDEGWWIVIGDPVTKTLLAIKRVTLQHK---LTVKLDFIAP--KAGHHNLKVFLMSDSFNGCDQ 2637
Cdd:smart00973 229 LEITPVFAWDLPrhKGKSESWWLVVGDSDTNELLAIKRVTLRKKkksNEVKLDFTVPlsEPGPENYTVYLISDSYLGCDQ 308
|
....*.
gi 1945600751 2638 ELDMEL 2643
Cdd:smart00973 309 EVSFSL 314
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1846-2030 |
8.75e-82 |
|
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: 267.32 E-value: 8.75e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1846 HFNPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALLRLWSSSEEARAVYVAPFQEIVDQRAADWKQKFK---GKEIV 1922
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEeklGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1923 TLTGETSADLKLLERGDVICCTPAQWDVVSRRWKQRKNVQNVNLFIADELHLIGGDIGPTYEVIVSRMRYIASQTNKSIR 2002
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*...
gi 1945600751 2003 IVALSTSLANARDLGEWIGATSHSVFNF 2030
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNF 188
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1197-1390 |
5.68e-67 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 223.58 E-value: 5.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1197 RPCPLKQQFIGVTEKKAIKRFQVMN----DVCYEKVMEQLdqREENQVLVFVHSRKETAKTAKTLRdmalekdtighflk 1272
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNkfdsDIIVLLKIETV--SEGKPVLVFCSSRKECEKTAKDLA-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1273 qdsasrevlqteaatvkdpnladllpyGFAIHHAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPAHAVIIKGTQI 1352
Cdd:cd18795 65 ---------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQR 117
|
170 180 190
....*....|....*....|....*....|....*...
gi 1945600751 1353 YSPEkgRWVELSPQDVLQMLGRAGRPQFDTYGEGIIIT 1390
Cdd:cd18795 118 YDGK--GYRELSPLEYLQMIGRAGRPGFDTRGEAIIMT 153
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1844-2366 |
3.73e-61 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 220.54 E-value: 3.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1844 IDHFNPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALLRLWSSSEeaRAVYVAPFQEIVDQRAADWKQKF--KGKEI 1921
Cdd:COG1204 20 IEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG--KALYIVPLRALASEKYREFKRDFeeLGIKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1922 VTLTGETSADLKLLERGDVICCTPAQWDVVSRrwKQRKNVQNVNLFIADELHLIG-GDIGPTYEVIVSRMRYIasqtNKS 2000
Cdd:COG1204 98 GVSTGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTLEVLLARLRRL----NPE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2001 IRIVALSTSLANARDLGEWIGATshsvfNFHPSVRPVPL--------EIHM-QSYNIPHFASLmmamakptYLAITTHSA 2071
Cdd:COG1204 172 AQIVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLnegvlydgVLRFdDGSRRSKDPTL--------ALALDLLEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2072 NKPVIVFVPSRKQCRLTAVDIITYCigDDTPDRFLHCKLEEIQPMLDRLQD-----KTLVETLQHGIGFYHEALSKQDKR 2146
Cdd:COG1204 239 GGQVLVFVSSRRDAESLAKKLADEL--KRRLTPEEREELEELAEELLEVSEethtnEKLADCLEKGVAFHHAGLPSELRR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2147 IVEQLYESGAIQVVVASrDTCWA---LPlnSHMVIVMGTqyfegkeHRYADYPIT--DVLQMMGRACRPREDDTGKCVLM 2221
Cdd:COG1204 317 LVEDAFREGLIKVLVAT-PTLAAgvnLP--ARRVIIRDT-------KRGGMVPIPvlEFKQMAGRAGRPGYDPYGEAILV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2222 CQANK--KEFYKKFLY-EALPVESHLDQL--LHDHFNAEIVTKTIENKQDAVDYLTWTFLYrrmahnpnyyglqgtsHRH 2296
Cdd:COG1204 387 AKSSDeaDELFERYILgEPEPIRSKLANEsaLRTHLLALIASGFANSREELLDFLENTFYA----------------YQY 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1945600751 2297 LSDHLSELVETTLNDLQETKCITIEDEMdVSPLNLGMIAAYYNINYTTVDMFSVSLKSTTK---LKGLLEIVA 2366
Cdd:COG1204 451 DKGDLEEVVDDALEFLLENGFIEEDGDR-LRATKLGKLVSRLYIDPLTAAELVDGLRKADEeftDLGLLHLIL 522
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
997-1198 |
1.64e-60 |
|
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: 207.21 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 997 NRVQSRLYPTAFGSDENVLLCAPTGAGKTNV---AMLTVLHEINKNrdpqtghiDLDSFKIVYIAPMKALVQEMVGNFSR 1073
Cdd:cd18023 3 NRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLfelAILRLLKERNPL--------PWGNRKVVYIAPIKALCSEKYDDWKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1074 RLRPYGISVAELTGDRQLTK-QQIAETQIIVTTPEKWDVITRKATDR-SYTALVRLIIIDEIHLLHDDRGPVLESIVSRt 1151
Cdd:cd18023 75 KFGPLGLSCAELTGDTEMDDtFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIKENRGATLEVVVSR- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1945600751 1152 IRTMEQTQEL-------VRLVGLSATLPNYADVAAFLRVNPkTGLFFFDGAFRP 1198
Cdd:cd18023 154 MKTLSSSSELrgstvrpMRFVAVSATIPNIEDLAEWLGDNP-AGCFSFGESFRP 206
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
995-1193 |
1.45e-58 |
|
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: 200.57 E-value: 1.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 995 SLNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldsFKIVYIAPMKALVQEMVGNFSRR 1074
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSG-----------GKAVYIAPTRALVNQKEADLRER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1075 LRPYGISVAELTGDRQLTKQQIAETQIIVTTPEKWDVITRKATDRsYTALVRLIIIDEIHLLHD-DRGPVLESIVSRTIR 1153
Cdd:cd17921 70 FGPLGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDgERGVVLELLLSRLLR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1945600751 1154 TMEQtqelVRLVGLSATLPNYADVAAFLRVnpkTGLFFFD 1193
Cdd:cd17921 149 INKN----ARFVGLSATLPNAEDLAEWLGV---EDLIRFD 181
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
997-1193 |
7.17e-57 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350780 [Multi-domain] Cd Length: 189 Bit Score: 196.06 E-value: 7.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 997 NRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNrdPQtghidldsFKIVYIAPMKALVQEMVGNFSRRL- 1075
Cdd:cd18022 3 NPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKY--PG--------SKVVYIAPLKALVRERVDDWKKRFe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1076 RPYGISVAELTGDRQLTKQQIAETQIIVTTPEKWDVITRKATDRSYTALVRLIIIDEIHLLHDDRGPVLESIVSRTIRTM 1155
Cdd:cd18022 73 EKLGKKVVELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYIS 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1945600751 1156 EQTQELVRLVGLSATLPNYADVAAFLRVNpKTGLFFFD 1193
Cdd:cd18022 153 SQTEKPVRLVGLSTALANAGDLANWLGIK-KMGLFNFR 189
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
1846-2031 |
1.40e-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: 192.09 E-value: 1.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1846 HFNPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALLRLWSSSeEARAVYVAPFQEIVDQRAADWKQKFK--GKEIVT 1923
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-GGKAVYIAPTRALVNQKEADLRERFGplGKNVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1924 LTGETSADLKLLERGDVICCTPAQWDVVSRRWKQRkNVQNVNLFIADELHLIG-GDIGPTYEVIVSRMRYIasqtNKSIR 2002
Cdd:cd17921 80 LTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI----NKNAR 154
|
170 180
....*....|....*....|....*....
gi 1945600751 2003 IVALSTSLANARDLGEWIGATSHsvFNFH 2031
Cdd:cd17921 155 FVGLSATLPNAEDLAEWLGVEDL--IRFD 181
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
1847-2036 |
2.41e-55 |
|
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: 192.19 E-value: 2.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1847 FNPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALLRLWSSSEE-----ARAVYVAPFQEIVDQRAADWKQKFK--GK 1919
Cdd:cd18023 2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPlpwgnRKVVYIAPIKALCSEKYDDWKEKFGplGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1920 EIVTLTGETSA-DLKLLERGDVICCTPAQWDVVSRRWKQRKN-VQNVNLFIADELHLIGGDIGPTYEVIVSRMRYIASQT 1997
Cdd:cd18023 82 SCAELTGDTEMdDTFEIQDADIILTTPEKWDSMTRRWRDNGNlVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSSSS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1945600751 1998 NK------SIRIVALSTSLANARDLGEWIGATSHSVFNFHPSVRP 2036
Cdd:cd18023 162 ELrgstvrPMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
981-1394 |
2.24e-54 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 205.19 E-value: 2.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 981 DLPQWAQEAF--PGAESLNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldsfKIVYIA 1058
Cdd:PRK02362 7 PLPEGVIEFYeaEGIEELYPPQAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIARGG------------KALYIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1059 PMKALVQEMVGNFSRrLRPYGISVAELTGDRQLTKQQIAETQIIVTTPEKWDVITRKATdrSYTALVRLIIIDEIHLLHD 1138
Cdd:PRK02362 75 PLRALASEKFEEFER-FEELGVRVGISTGDYDSRDEWLGDNDIIVATSEKVDSLLRNGA--PWLDDITCVVVDEVHLIDS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1139 -DRGPVLESivsrTIRTMEQTQELVRLVGLSATLPNYADVAAFLR----------VNPKTGLFFfDGAFRpCPLKQQFIG 1207
Cdd:PRK02362 152 aNRGPTLEV----TLAKLRRLNPDLQVVALSATIGNADELADWLDaelvdsewrpIDLREGVFY-GGAIH-FDDSQREVE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1208 VTEKKaikrfQVMNDVcyekvmeqLDQREEN-QVLVFVHSRKETAKTAKTLRDmALEKdtigHFLKQDSAS--------R 1278
Cdd:PRK02362 226 VPSKD-----DTLNLV--------LDTLEEGgQCLVFVSSRRNAEGFAKRAAS-ALKK----TLTAAERAElaelaeeiR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1279 EVLQTEaaTVKDpnLADLLPYGFAIHHAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPAHAVIIKGTQIYSPEKG 1358
Cdd:PRK02362 288 EVSDTE--TSKD--LADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAG 363
|
410 420 430
....*....|....*....|....*....|....*....
gi 1945600751 1359 rwveLSPQDVL---QMLGRAGRPQFDTYGEGIIItAHTE 1394
Cdd:PRK02362 364 ----MQPIPVLeyhQMAGRAGRPGLDPYGEAVLL-AKSY 397
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
760-868 |
1.65e-50 |
|
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 is required for the assembly of a catalytically active spliceosome on a messenger RNA precursor. The domain is found in the N-terminal region and is non-canonically PWI-like. The PWI-like domain is thought to be involved in protein-protein interactions.
Pssm-ID: 436309 Cd Length: 111 Bit Score: 174.72 E-value: 1.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 760 KSDAISPHDLDAFWLQRQIATHYPDPHTAQEKTMKAFDILGAESSNMRDCENELMGLFDYDKFDLVRILTKNREIIYWCT 839
Cdd:pfam18149 1 DKDSLDPHDIDAFWLQRLLSKFYGDAIEAQKKAEEVLDILESAADDLRECENQLVELLDYDKFDLVKLLLKNRDKIVWCT 80
|
90 100 110
....*....|....*....|....*....|.
gi 1945600751 840 RLAR-VDGAEKSELEKEMQQK-GLGWILHDL 868
Cdd:pfam18149 81 KLARaQSEEEKQAIEEEMRSNpGLAWILDEL 111
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1008-1512 |
2.78e-50 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 191.63 E-value: 2.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1008 FGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldsfKIVYIAPMKALVQEMVGNFSRrLRPYGISVAELTG 1087
Cdd:PRK01172 34 LRKGENVIVSVPTAAGKTLIAYSAIYETFLAGL------------KSIYIVPLRSLAMEKYEELSR-LRSLGMRVKISIG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1088 DRQLTKQQIAETQIIVTTPEKWDVITRKatDRSYTALVRLIIIDEIHLLHD-DRGPVLESIVSrTIRTMEQTqelVRLVG 1166
Cdd:PRK01172 101 DYDDPPDFIKRYDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDeDRGPTLETVLS-SARYVNPD---ARILA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1167 LSATLPNYADVAAFLRVNpktglfFFDGAFRPCPLKqqfIGVTEKKAI-----KRFQV-MNDVCYEKVmeqldqREENQV 1240
Cdd:PRK01172 175 LSATVSNANELAQWLNAS------LIKSNFRPVPLK---LGILYRKRLildgyERSQVdINSLIKETV------NDGGQV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1241 LVFVHSRKETAKTAKTLrdmalekdtIGHFlkqDSASREVLQTEAATVKDPNLADLLPYGFAIHHAGMTRADRTLVEDLF 1320
Cdd:PRK01172 240 LVFVSSRKNAEDYAEML---------IQHF---PEFNDFKVSSENNNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1321 ADGHVKVLCSTATLAWGVNLPAHAVIIKGTQIYSPEKGRWveLSPQDVLQMLGRAGRPQFDTYGEGIIITA----HTELQ 1396
Cdd:PRK01172 308 RNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRY--LSNMEIKQMIGRAGRPGYDQYGIGYIYAAspasYDAAK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1397 YYLSllNTQLPIESQFVK--RMADNLNAEIVLGTIRNRDEAVQWLGYTYLYVRmlrnptlynvsiDDLDDDPYleqkrvd 1474
Cdd:PRK01172 386 KYLS--GEPEPVISYMGSqrKVRFNTLAAISMGLASSMEDLILFYNETLMAIQ------------NGVDEIDY------- 444
|
490 500 510
....*....|....*....|....*....|....*...
gi 1945600751 1475 LIHSAATILDKCNLIKYDKKsgrFQVTELGRIASHFYV 1512
Cdd:PRK01172 445 YIESSLKFLKENGFIKGDVT---LRATRLGKLTSDLYI 479
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
980-1420 |
2.95e-50 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 192.85 E-value: 2.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 980 KDLPQWAQEAFPGAESLNRVQS-RLYP------TAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldsf 1052
Cdd:COG4581 2 TLSPARADARLEALADFAEERGfELDPfqeeaiLALEAGRSVLVAAPTGSGKTLVAEFAIFLALARGR------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1053 KIVYIAPMKALVQEMVGNFSRRlrpYG-ISVAELTGDRQLtkqqIAETQIIVTTPEkwdvITRKATDRSYTALVRL--II 1129
Cdd:COG4581 70 RSFYTAPIKALSNQKFFDLVER---FGaENVGLLTGDASV----NPDAPIVVMTTE----ILRNMLYREGADLEDVgvVV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1130 IDEIHLLHD-DRGPVLE-SIVsrtirtmeqtqEL---VRLVGLSATLPNYADVAAFL-RVNPKTGLFffDGAFRPCPLKQ 1203
Cdd:COG4581 139 MDEFHYLADpDRGWVWEePII-----------HLparVQLVLLSATVGNAEEFAEWLtRVRGETAVV--VSEERPVPLEF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1204 QFigVTEKKAIKRFQVMNDVCYE----KVMEQLDQREENQVLVFVHSRKETAKTAKTLRDMAL----EKDTIGHFLKQDS 1275
Cdd:COG4581 206 HY--LVTPRLFPLFRVNPELLRPpsrhEVIEELDRGGLLPAIVFIFSRRGCDEAAQQLLSARLttkeERAEIREAIDEFA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1276 ASREVLQTEAatvkdpnLADLLPYGFAIHHAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPAHAVIIKGTQIYSP 1355
Cdd:COG4581 284 EDFSVLFGKT-------LSRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDG 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1945600751 1356 EKGRwvELSPQDVLQMLGRAGRPQFDTYGEGIII-TAHTELQYYLSLLNTQL-PIESQFV--KRMADNL 1420
Cdd:COG4581 357 ERHR--PLTAREFHQIAGRAGRRGIDTEGHVVVLaPEHDDPKKFARLASARPePLRSSFRpsYNMVLNL 423
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
992-1394 |
1.41e-48 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 187.33 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 992 GAESLNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKnrdpQTGhidldsfKIVYIAPMKALVQEMVGNF 1071
Cdd:PRK00254 20 GIEELYPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR----EGG-------KAVYLVPLKALAEEKYREF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1072 sRRLRPYGISVAELTGDRQLTKQQIAETQIIVTTPEKWDVITRKATdrSYTALVRLIIIDEIHLLHD-DRGPVLESIVSr 1150
Cdd:PRK00254 89 -KDWEKLGLRVAMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRHGS--SWIKDVKLVVADEIHLIGSyDRGATLEMILT- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1151 tirtmeQTQELVRLVGLSATLPNYADVAAFLRVNpktgLFFFDgaFRPCPLK-----QQFIgVTEKKAIKRFQvmnDVCY 1225
Cdd:PRK00254 165 ------HMLGRAQILGLSATVGNAEELAEWLNAE----LVVSD--WRPVKLRkgvfyQGFL-FWEDGKIERFP---NSWE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1226 EKVMEQLdqREENQVLVFVHSRKETAKTAktlrdMALEKdTIGHFL--KQDSASREVLQTEAATVKDPNLADLLPYGFAI 1303
Cdd:PRK00254 229 SLVYDAV--KKGKGALVFVNTRRSAEKEA-----LELAK-KIKRFLtkPELRALKELADSLEENPTNEKLKKALRGGVAF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1304 HHAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPAHAVIIKGTQIYSpEKGrWVELSPQDVLQMLGRAGRPQFDTY 1383
Cdd:PRK00254 301 HHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYS-NFG-WEDIPVLEIQQMMGRAGRPKYDEV 378
|
410
....*....|.
gi 1945600751 1384 GEGIIItAHTE 1394
Cdd:PRK00254 379 GEAIIV-ATTE 388
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
2035-2223 |
4.05e-42 |
|
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: 152.32 E-value: 4.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2035 RPVPLEIHMQSYNIPHFASLMMAMAK-----PTYLAITTHSANKPVIVFVPSRKQCRLTAVDIItycigddtpdrflhck 2109
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2110 leeiqpmldrlqdktlvetlqhGIGFYHEALSKQDKRIVEQLYESGAIQVVVASRDTCWALPLNSHMVIVMGTQYFEGKE 2189
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 1945600751 2190 HRYadYPITDVLQMMGRACRPREDDTGKCVLMCQ 2223
Cdd:cd18795 123 YRE--LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
996-1193 |
2.72e-41 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 151.26 E-value: 2.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 996 LNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNrdpqtghidlDSFKIVYIAPMKALVQEMVGNFSRRL 1075
Cdd:cd18021 4 FNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQN----------PKGRAVYIAPMQELVDARYKDWRAKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1076 RPY-GISVAELTGDRQLTKQQIAETQIIVTTPEKWDVITRKATDRSYTALVRLIIIDEIHLLHDDRGPVLESIVSRTIRT 1154
Cdd:cd18021 74 GPLlGKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYI 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1945600751 1155 MEQTQELVRLVGLSATLPNYADVAAFLRVNPKTgLFFFD 1193
Cdd:cd18021 154 SSQLEKPIRIVGLSSSLANARDVGEWLGASKST-IFNFH 191
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1844-2395 |
1.14e-37 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 153.82 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1844 IDHFNPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALL-RLWssSEEARAVYVAPFQEIVDQRAADWKQKFK-GKEI 1921
Cdd:PRK00254 21 IEELYPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVnKLL--REGGKAVYLVPLKALAEEKYREFKDWEKlGLRV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1922 VTLTGETSADLKLLERGDVICCTPAQWDVVSR---RWkqrknVQNVNLFIADELHLIGG-DIGPTYEVIVSRMRYIAsqt 1997
Cdd:PRK00254 99 AMTTGDYDSTDEWLGKYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSyDRGATLEMILTHMLGRA--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1998 nksiRIVALSTSLANARDLGEWIGAtSHSVFNFhpsvRPVPLE--IHMQSYNIPHFASLMMAMAKPTYLAITTHSANKPV 2075
Cdd:PRK00254 171 ----QILGLSATVGNAEELAEWLNA-ELVVSDW----RPVKLRkgVFYQGFLFWEDGKIERFPNSWESLVYDAVKKGKGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2076 IVFVPSRKQCRLTAVDIitycigDDTPDRFLHCK-LEEIQPMLDRLQD----KTLVETLQHGIGFYHEALSKQDKRIVEQ 2150
Cdd:PRK00254 242 LVFVNTRRSAEKEALEL------AKKIKRFLTKPeLRALKELADSLEEnptnEKLKKALRGGVAFHHAGLGRTERVLIED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2151 LYESGAIQVVVASRDTCWALPLNSHMVIVMGTQyfegkehRYADY-----PITDVLQMMGRACRPREDDTGKCVLMCQAN 2225
Cdd:PRK00254 316 AFREGLIKVITATPTLSAGINLPAFRVIIRDTK-------RYSNFgwediPVLEIQQMMGRAGRPKYDEVGEAIIVATTE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2226 K-KEFYKKF-------LYEALPVESHL-DQLLhdhfnAEIVTKTIENKQDAVDYLTWTFlyrrmahnpnyYGLQGTSHRH 2296
Cdd:PRK00254 389 EpSKLMERYifgkpekLFSMLSNESAFrSQVL-----ALITNFGVSNFKELVNFLERTF-----------YAHQRKDLYS 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2297 LSDHLSELVETTL-NDLQEtkcITIEDEmdVSPLNLGMIAAYYNINYTTVDMFSVSLKSTTKLK---GLLEIVASATEFD 2372
Cdd:PRK00254 453 LEEKAKEIVYFLLeNEFID---IDLEDR--FIPLPLGIRTSQLYIDPLTAKKFKDAFPKIEKNPnplGIFQLIASTPDMT 527
|
570 580
....*....|....*....|...
gi 1945600751 2373 GIPIRHQEDNVLKRIYDRLPVKL 2395
Cdd:PRK00254 528 PLNYSRKEMEDLLDEAYEMEDRL 550
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
997-1172 |
2.02e-34 |
|
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: 130.83 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 997 NRVQSRLYPTAFgSDENVLLCAPTGAGKTNVAMLTVLHEINKNrdpqtghidLDSFKIVYIAPMKALVQEMVGNFSRRLR 1076
Cdd:pfam00270 1 TPIQAEAIPAIL-EGRDVLVQAPTGSGKTLAFLLPALEALDKL---------DNGPQALVLAPTRELAEQIYEELKKLGK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1077 PYGISVAELTG--DRQLTKQQIAETQIIVTTPEKWDVITRKatdRSYTALVRLIIIDEIHLLHD-DRGPVLESIVSRtir 1153
Cdd:pfam00270 71 GLGLKVASLLGgdSRKEQLEKLKGPDILVGTPGRLLDLLQE---RKLLKNLKLLVLDEAHRLLDmGFGPDLEEILRR--- 144
|
170
....*....|....*....
gi 1945600751 1154 tmeqTQELVRLVGLSATLP 1172
Cdd:pfam00270 145 ----LPKKRQILLLSATLP 159
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
995-1181 |
5.37e-33 |
|
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: 127.07 E-value: 5.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 995 SLNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldsfKIVYIAPMKALVQEMVGNFSrR 1074
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG------------KALYLVPLRALASEKYEEFK-K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1075 LRPYGISVAELTGDRQLTKQQIAETQIIVTTPEKWDVITRKATdrSYTALVRLIIIDEIHLLHD-DRGPVLESIVSRtIR 1153
Cdd:cd18028 68 LEEIGLKVGISTGDYDEDDEWLGDYDIIVATYEKFDSLLRHSP--SWLRDVGVVVVDEIHLISDeERGPTLESIVAR-LR 144
|
170 180
....*....|....*....|....*...
gi 1945600751 1154 TMEQTqelVRLVGLSATLPNYADVAAFL 1181
Cdd:cd18028 145 RLNPN---TQIIGLSATIGNPDELAEWL 169
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1862-2277 |
1.17e-30 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 131.54 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1862 NDNVFIGAPTGSGKTVCAEFALLRLWSSSEeaRAVYVAPFQEIVDQRAADWKQ-KFKGKEIVTLTGETSADLKLLERGDV 1940
Cdd:PRK01172 37 GENVIVSVPTAAGKTLIAYSAIYETFLAGL--KSIYIVPLRSLAMEKYEELSRlRSLGMRVKISIGDYDDPPDFIKRYDV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1941 ICCTPAQWDvvSRRWKQRKNVQNVNLFIADELHLIGG-DIGPTYEVIVSRMRYIasqtNKSIRIVALSTSLANARDLGEW 2019
Cdd:PRK01172 115 VILTSEKAD--SLIHHDPYIINDVGLIVADEIHIIGDeDRGPTLETVLSSARYV----NPDARILALSATVSNANELAQW 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2020 IGAtSHSVFNFhpsvRPVPLEIHMQSYNIPHFASLMMAMAKPTYLAITTHSANKPVIVFVPSRKQCRLTAVDIITYCigd 2099
Cdd:PRK01172 189 LNA-SLIKSNF----RPVPLKLGILYRKRLILDGYERSQVDINSLIKETVNDGGQVLVFVSSRKNAEDYAEMLIQHF--- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2100 dTPDRFLHCKLEEIQPMldrlqDKTLVETLQHGIGFYHEALSKQDKRIVEQLYESGAIQVVVASRDTCWALPLNSHMVIV 2179
Cdd:PRK01172 261 -PEFNDFKVSSENNNVY-----DDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2180 MGTQyfegkehRYADYPIT-----DVLQMMGRACRPREDDTG-KCVLMCQANKKEFYKKFLY-EALPVESHLDQLLHDHF 2252
Cdd:PRK01172 335 RDIT-------RYGNGGIRylsnmEIKQMIGRAGRPGYDQYGiGYIYAASPASYDAAKKYLSgEPEPVISYMGSQRKVRF 407
|
410 420
....*....|....*....|....*..
gi 1945600751 2253 N--AEIVTKTIENKQDAVDYLTWTFLY 2277
Cdd:PRK01172 408 NtlAAISMGLASSMEDLILFYNETLMA 434
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
1011-1181 |
1.44e-28 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 113.83 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1011 DENVLLCAPTGAGKTNVAMLTVLHEINKNrdpqtghiDLDSFKIVYIAPMKALVQEMvgnfSRRLRPY------GISVAE 1084
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADE--------PEKGVQVLYISPLKALINDQ----ERRLEEPldeidlEIPVAV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1085 LTGD--RQLTKQQIAET-QIIVTTPEKWDVI-TRKATDRSYTALvRLIIIDEIH-LLHDDRGPVLESIVSRtIRTMEQTq 1159
Cdd:cd17922 69 RHGDtsQSEKAKQLKNPpGILITTPESLELLlVNKKLRELFAGL-RYVVVDEIHaLLGSKRGVQLELLLER-LRKLTGR- 145
|
170 180
....*....|....*....|..
gi 1945600751 1160 ELVRlVGLSATLPNYADVAAFL 1181
Cdd:cd17922 146 PLRR-IGLSATLGNLEEAAAFL 166
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1864-2332 |
2.89e-28 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 124.30 E-value: 2.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1864 NVFIGAPTGSGKTVCAEFALLRlwSSSEEARAVYVAPFQEIvdqrAADWKQKFKGKEIVTL-----TGETSADLKLLERG 1938
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAMLK--AIARGGKALYIVPLRAL----ASEKFEEFERFEELGVrvgisTGDYDSRDEWLGDN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1939 DVICCTPAQWDVVSR---RWkqrknVQNVNLFIADELHLIG-GDIGPTYEVIVSRMRYIasqtNKSIRIVALSTSLANAR 2014
Cdd:PRK02362 115 DIIVATSEKVDSLLRngaPW-----LDDITCVVVDEVHLIDsANRGPTLEVTLAKLRRL----NPDLQVVALSATIGNAD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2015 DLGEWIGA---TS--------HSVF-----NFHPSVRPVPLEIHMQSYNiphfaslmmamakptyLAITTHSANKPVIVF 2078
Cdd:PRK02362 186 ELADWLDAelvDSewrpidlrEGVFyggaiHFDDSQREVEVPSKDDTLN----------------LVLDTLEEGGQCLVF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2079 VPSRKQC-----RLTAVdiITYCIGDDTPDRFLHCKlEEIQPMLDRLQDKTLVETLQHGIGFYHEALSKQDKRIVEQLYE 2153
Cdd:PRK02362 250 VSSRRNAegfakRAASA--LKKTLTAAERAELAELA-EEIREVSDTETSKDLADCVAKGAAFHHAGLSREHRELVEDAFR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2154 SGAIQVVvASRDTCWA-LPLNSHMVIVMGTQYFEGKEHrYADYPITDVLQMMGRACRPREDDTGKCVLMCQaNKKEFYKK 2232
Cdd:PRK02362 327 DRLIKVI-SSTPTLAAgLNLPARRVIIRDYRRYDGGAG-MQPIPVLEYHQMAGRAGRPGLDPYGEAVLLAK-SYDELDEL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2233 FLY----EALPVESHL--DQLLHDHFNAEIVTKTIENKQDAVDYLTWTFlyrrmahnpnyYGLQGTSHRhlsdHLSELVE 2306
Cdd:PRK02362 404 FERyiwaDPEDVRSKLatEPALRTHVLSTIASGFARTRDGLLEFLEATF-----------YATQTDDTG----RLERVVD 468
|
490 500
....*....|....*....|....*.
gi 1945600751 2307 TTLNDLQETKCITiEDEMDVSPLNLG 2332
Cdd:PRK02362 469 DVLDFLERNGMIE-EDGETLEATELG 493
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
1848-2017 |
4.92e-28 |
|
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: 114.00 E-value: 4.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1848 NPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALLRLWSSS---------EEARAVYVAPFQEIVDQRAADWKQKFK- 1917
Cdd:cd18019 19 NRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHrnpdgtinlDAFKIVYIAPMKALVQEMVGNFSKRLAp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1918 -GKEIVTLTGETSADLKLLERGDVICCTPAQWDVVSRRWKQRKNVQNVNLFIADELHLIGGDIGPTYEVIVSRMRYIASQ 1996
Cdd:cd18019 99 yGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDDRGPVLESIVARTIRQIEQ 178
|
170 180
....*....|....*....|.
gi 1945600751 1997 TNKSIRIVALSTSLANARDLG 2017
Cdd:cd18019 179 TQEYVRLVGLSATLPNYEDVA 199
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
992-1205 |
1.16e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 109.89 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 992 GAESLNRVQSRLYPTAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRDPQTghidldsfkiVYIAPMKALVQEMVGNF 1071
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV----------LVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1072 SRRLRPYGISVAELTGD----RQLTKQQIAETQIIVTTPEKWdvITRKATDRSYTALVRLIIIDEIHLLHD-DRGPVLES 1146
Cdd:smart00487 75 KKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRL--LDLLENDKLSLSNVDLVILDEAHRLLDgGFGDQLEK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1945600751 1147 IVSRTIRTmeqtqelVRLVGLSATLPNYADVAAFLRVNpktGLFFFDGAFRPCPLKQQF 1205
Cdd:smart00487 153 LLKLLPKN-------VQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLEPIEQF 201
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1848-2016 |
1.97e-25 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 105.02 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1848 NPIQTQVFNTLYTtNDNVFIGAPTGSGKTVCAEFALL-RLWSSSEEARAVYVAPFQEIVDQRAADWKQKFKGKEI---VT 1923
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALeALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkvaSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1924 LTG-ETSADLKLLERGDVICCTPAQWDVVSRrwkQRKNVQNVNLFIADELHLIGG-DIGPTYEVIVSRMRyiasqtnKSI 2001
Cdd:pfam00270 80 LGGdSRKEQLEKLKGPDILVGTPGRLLDLLQ---ERKLLKNLKLLVLDEAHRLLDmGFGPDLEEILRRLP-------KKR 149
|
170
....*....|....*.
gi 1945600751 2002 RIVALSTSLA-NARDL 2016
Cdd:pfam00270 150 QILLLSATLPrNLEDL 165
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
1847-2022 |
7.80e-25 |
|
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: 103.57 E-value: 7.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1847 FNPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALLRLWssSEEARAVYVAPFQEIVDQRAADWKQKFK-GKEIVTLT 1925
Cdd:cd18028 2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTL--LEGGKALYLVPLRALASEKYEEFKKLEEiGLKVGIST 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1926 GETSADLKLLERGDVICCTPAQWDVVsrrWKQRKN-VQNVNLFIADELHLIGG-DIGPTYEVIVSRMRYIasqtNKSIRI 2003
Cdd:cd18028 80 GDYDEDDEWLGDYDIIVATYEKFDSL---LRHSPSwLRDVGVVVVDEIHLISDeERGPTLESIVARLRRL----NPNTQI 152
|
170
....*....|....*....
gi 1945600751 2004 VALSTSLANARDLGEWIGA 2022
Cdd:cd18028 153 IGLSATIGNPDELAEWLNA 171
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1863-2243 |
3.79e-24 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 111.18 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1863 DNVFIGAPTGSGKTVCAEFAL-LRLwssSEEARAVYVAPFQEIVDQRAADWKQKFkGKEIVTL-TGETSadlkllERGD- 1939
Cdd:COG4581 41 RSVLVAAPTGSGKTLVAEFAIfLAL---ARGRRSFYTAPIKALSNQKFFDLVERF-GAENVGLlTGDAS------VNPDa 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1940 -VICCTpAQwdvVSRRWKQRK--NVQNVNLFIADELHLIG-GDIGPTYEVIVSRMRyiasqtnKSIRIVALSTSLANARD 2015
Cdd:COG4581 111 pIVVMT-TE---ILRNMLYREgaDLEDVGVVVMDEFHYLAdPDRGWVWEEPIIHLP-------ARVQLVLLSATVGNAEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2016 LGEWI----GATsHSVFNFHpsvRPVPLEIHM--QSYNIPHFASLMMAMAKPTYLAI-----TTHSAnkPVIVFVPSRKQ 2084
Cdd:COG4581 180 FAEWLtrvrGET-AVVVSEE---RPVPLEFHYlvTPRLFPLFRVNPELLRPPSRHEVieeldRGGLL--PAIVFIFSRRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2085 CrLTAVDIIT-YCIGDDTPDRFLHCKLEEIQPMLDRLQDKTLVETLQHGIGFYHEALSKQDKRIVEQLYESGAIQVVVAS 2163
Cdd:COG4581 254 C-DEAAQQLLsARLTTKEERAEIREAIDEFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFAT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2164 rDTCwALPLN--SHMVIVMGTQYFEGKEHRyadyPIT--DVLQMMGRACRPREDDTGKCVlmCQANKKEFYKKFLY---- 2235
Cdd:COG4581 333 -DTL-AVGINmpARTVVFTKLSKFDGERHR----PLTarEFHQIAGRAGRRGIDTEGHVV--VLAPEHDDPKKFARlasa 404
|
....*...
gi 1945600751 2236 EALPVESH 2243
Cdd:COG4581 405 RPEPLRSS 412
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1848-2022 |
6.15e-24 |
|
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: 101.74 E-value: 6.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1848 NPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALLRLWSSS---------EEARAVYVAPFQEIVDQRAADWKQKFKG 1918
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHvnqggvikkDDFKIVYIAPMKALAAEMVEKFSKRLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1919 KEIVT--LTGETSADLKLLERGDVICCTPAQWDVVSRRWKQRKN-VQNVNLFIADELHLIGGDIGPTYEVIVSRMRYIAS 1995
Cdd:cd18020 83 LGIKVkeLTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVAlSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQVE 162
|
170 180
....*....|....*....|....*..
gi 1945600751 1996 QTNKSIRIVALSTSLANARDLGEWIGA 2022
Cdd:cd18020 163 STQSMIRIVGLSATLPNYLDVADFLRV 189
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
940-1380 |
5.37e-23 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 107.28 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 940 NKKVKLPDGSFKRSKKGYEEIHVPAPKAHTfeageklVPIKDL--PQWAQEAFPG-AESLNRVQSRLYPTAFGSDENVLL 1016
Cdd:COG1202 158 DRVLNLLSGRLDPDLTKFDEISATTDEVDT-------VPVDDLdlPPELKDLLEGrGEELLPVQSLAVENGLLEGKDQLV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1017 CAPTGAGKTNVAMLTVLHEINKNRDpqtghidldsfKIVYIAPMKALVQEMVGNFSRRLRPyGISVAELTGDRQLT---K 1093
Cdd:COG1202 231 VSATATGKTLIGELAGIKNALEGKG-----------KMLFLVPLVALANQKYEDFKDRYGD-GLDVSIRVGASRIRddgT 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1094 QQIAETQIIVTTPEKWDVITR--KATDRSYTalvrlIIIDEIHLLHD-DRGPVLESIVSRTIRTMEQTQelvrLVGLSAT 1170
Cdd:COG1202 299 RFDPNADIIVGTYEGIDHALRtgRDLGDIGT-----VVIDEVHMLEDpERGHRLDGLIARLKYYCPGAQ----WIYLSAT 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1171 LPNYADVAAFLRVNpktgLFFFDGafRPCPLKQQFIGVTEKKAIKrfqvmndvcyekVMEQLDQREEN---------QVL 1241
Cdd:COG1202 370 VGNPEELAKKLGAK----LVEYEE--RPVPLERHLTFADGREKIR------------IINKLVKREFDtksskgyrgQTI 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1242 VFVHSRKETaktaktlrdmalekdtigHflkqdsasrevlqteaatvkdpNLADLLPYGFAIHHAGMTRADRTLVEDLFA 1321
Cdd:COG1202 432 IFTNSRRRC------------------H----------------------EIARALGYKAAPYHAGLDYGERKKVERRFA 471
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1945600751 1322 DGHVKVLCSTATLAWGVNLPAHAVI-------IKgtqiyspekgrWveLSPQDVLQMLGRAGRPQF 1380
Cdd:COG1202 472 DQELAAVVTTAALAAGVDFPASQVIfdslamgIE-----------W--LSVQEFHQMLGRAGRPDY 524
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
979-1198 |
1.59e-22 |
|
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: 97.67 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 979 IKDLPQWAQEAFpgaeSLNRVQSRlyptafgsdENVLLCAPTGAGKTNVAMLTVLHEINKNRDpqtghidldsfKIVYIA 1058
Cdd:cd18026 14 IKKLYDWQKECL----SLPGLLEG---------RNLVYSLPTSGGKTLVAEILMLKRLLERRK-----------KALFVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1059 PMKALVQEMVGNFSRRLRPYGISVAELTGDR-QLTKQQIAETQIIVTTPEKWDVITRKATDRSYTALVRLIIIDEIHLLH 1137
Cdd:cd18026 70 PYVSIVQEKVDALSPLFEELGFRVEGYAGNKgRSPPKRRKSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1945600751 1138 D-DRGPVLESIVSRTirtMEQTQELVRLVGLSATLPNYADVAAFLRVnpktglFFFDGAFRP 1198
Cdd:cd18026 150 DgHRGALLELLLTKL---LYAAQKNIQIVGMSATLPNLEELASWLRA------ELYTTNFRP 202
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
1012-1170 |
1.95e-19 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 87.07 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1012 ENVLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldsFKIVYIAPMKALVQEMVGNFSRRLRPyGISVAELTGDR-- 1089
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKKG-----------KKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSsa 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1090 -QLTKQQIAETQIIVTTPEKwdvITRK--ATDRSYTALVRLIIIDEIHLLhDDRGPVLESIVSRTIRTMeqtQELVRLVG 1166
Cdd:cd00046 70 eEREKNKLGDADIIIATPDM---LLNLllREDRLFLKDLKLIIVDEAHAL-LIDSRGALILDLAVRKAG---LKNAQVIL 142
|
....
gi 1945600751 1167 LSAT 1170
Cdd:cd00046 143 LSAT 146
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1007-1392 |
1.74e-18 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 92.86 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1007 AFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRDPQTGHidlDSFKIVYIAPMKAL-----------VQEMVGNFSRRL 1075
Cdd:COG1201 35 AIAAGESTLLIAPTGSGKTLAAFLPALDELARRPRPGELP---DGLRVLYISPLKALandiernlrapLEEIGEAAGLPL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1076 RPygISVAELTGD-----RQltkQQIAET-QIIVTTPE---------KWdvitrkatdRSYTALVRLIIIDEIHLLHDD- 1139
Cdd:COG1201 112 PE--IRVGVRTGDtpaseRQ---RQRRRPpHILITTPEslallltspDA---------RELLRGVRTVIVDEIHALAGSk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1140 RGPVLESIVSRtIRTMeQTQELVRlVGLSATLPNYADVAAFLrvnpkTGlfffDGAFRPC-----PLKQQF---IGVTEK 1211
Cdd:COG1201 178 RGVHLALSLER-LRAL-APRPLQR-IGLSATVGPLEEVARFL-----VG----YEDPRPVtivdaGAGKKPdleVLVPVE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1212 KAIKRFQ---VMNDVCYEKVMEQLDQReeNQVLVFVHSRKETAKTAKTLRDMAlekdtighflkqdsasrevlqteaatv 1288
Cdd:COG1201 246 DLIERFPwagHLWPHLYPRVLDLIEAH--RTTLVFTNTRSQAERLFQRLNELN--------------------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1289 kdPNLADLLpygfAIHHAGMTRADRTLVEDLFADGHVKVLCSTATLA----WG-VNLpahaVIikgtQIYSPeKGrwvel 1363
Cdd:COG1201 297 --PEDALPI----AAHHGSLSREQRLEVEEALKAGELRAVVATSSLElgidIGdVDL----VI----QVGSP-KS----- 356
|
410 420 430
....*....|....*....|....*....|....*.
gi 1945600751 1364 spqdV---LQMLGRAG-RPqfdtyGE---GIIITAH 1392
Cdd:COG1201 357 ----VarlLQRIGRAGhRV-----GEvskGRLVPTH 383
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1839-2007 |
3.86e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1839 VYSGWIDHFNPIQTQVFNTLYTTNDNVFIGAPTGSGKTVCAEFALLRLWSSSEEARAVYVAPFQEIVDQ---RAADWKQK 1915
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQwaeELKKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1916 FKGKEIVTLTGETS-ADLKLLERG--DVICCTPAQWDVVSRRWKqrKNVQNVNLFIADELH-LIGGDIGPTYEVIVSRMR 1991
Cdd:smart00487 81 LGLKVVGLYGGDSKrEQLRKLESGktDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP 158
|
170
....*....|....*.
gi 1945600751 1992 yiasqtnKSIRIVALS 2007
Cdd:smart00487 159 -------KNVQLLLLS 167
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
1007-1378 |
4.06e-17 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 88.38 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1007 AFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRDPQTGHIdldsfKIVYIAPMKALVQEMVGNFSRRLRPYG--ISVAE 1084
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSLIDLAGPEAPKEKGL-----HTLYITPLRALAVDIARNLQAPIEELGlpIRVET 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1085 LTGD---RQLTKQQIAETQIIVTTPEKWDV-ITRKATDRSYTALvRLIIIDEIH-LLHDDRGPVLESIVSRtirtMEQTQ 1159
Cdd:TIGR04121 99 RTGDtssSERARQRKKPPDILLTTPESLALlLSYPDAARLFKDL-RCVVVDEWHeLAGSKRGDQLELALAR----LRRLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1160 ELVRLVGLSATLPNYADVAAFLrVNPKTglfffdgafRPCPLkqqfIGVTEKKAIKRFQVMNDV-------------CYE 1226
Cdd:TIGR04121 174 PGLRRWGLSATIGNLEEARRVL-LGVGG---------APAVL----VRGKLPKAIEVISLLPESeerfpwaghlglrALP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1227 KVMEQLDQreENQVLVFVHSRKETAKTAKTLRDmalekdtighflkqdsasrevlqteaatvKDPNLADLLpygfAIHHA 1306
Cdd:TIGR04121 240 EVYAEIDQ--ARTTLVFTNTRSQAELWFQALWE-----------------------------ANPEFALPI----ALHHG 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1945600751 1307 GMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPAHAVIIkgtQIYSPeKG--RwvelspqdVLQMLGRAG-RP 1378
Cdd:TIGR04121 285 SLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSP-KGvaR--------LLQRAGRSNhRP 347
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
981-1399 |
5.76e-17 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 87.97 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 981 DLPQWAQEAFpgAESLNRVQ-SRLYP---TAFG---SDENVLLCAPTGAGKTNVAMLTVLHEINKNRDPqtghidldsfK 1053
Cdd:COG1205 36 PWPDWLPPEL--RAALKKRGiERLYShqaEAIEaarAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA----------T 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1054 IVYIAPMKALVQEMVGNFSRRLRPYG--ISVAELTGDrqlTKQQI-----AETQIIVTTP-----------EKWdvitrk 1115
Cdd:COG1205 104 ALYLYPTKALARDQLRRLRELAEALGlgVRVATYDGD---TPPEErrwirEHPDIVLTNPdmlhygllphhTRW------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1116 atDRSYTALvRLIIIDEIHLLhddRGpVLESIVSRTIRtmeqtqelvRL-------------VGLSATLPNYADVAAFLr 1182
Cdd:COG1205 175 --ARFFRNL-RYVVIDEAHTY---RG-VFGSHVANVLR---------RLrricrhygsdpqfILASATIGNPAEHAERL- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1183 vnpkTGLFF----FDGAFRP--------CPLKQQFI---GVTEKKAIKRFQVMNDVcyekvmeqldqreenQVLVFVHSR 1247
Cdd:COG1205 238 ----TGRPVtvvdEDGSPRGertfvlwnPPLVDDGIrrsALAEAARLLADLVREGL---------------RTLVFTRSR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1248 KETAKTAKTLRDMAlekdtighflkqdsasrevlqteaatvKDPNLADLLpygfAIHHAGMTRADRTLVEDLFADGHVKV 1327
Cdd:COG1205 299 RGAELLARYARRAL---------------------------REPDLADRV----AAYRAGYLPEERREIERGLRSGELLG 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1945600751 1328 LCSTATLAWGVNLPA-HAVIIKGtqiYSPekgrwvelSPQDVLQMLGRAGRPQfdtyGEGIIITAHTE--L-QYYL 1399
Cdd:COG1205 348 VVSTNALELGIDIGGlDAVVLAG---YPG--------TRASFWQQAGRAGRRG----QDSLVVLVAGDdpLdQYYV 408
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1293-1378 |
1.35e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 73.79 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1293 LADLL---PYGFAIHHAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLP-AHAVIIKGtqiyspekgrwVELSPQDV 1368
Cdd:smart00490 3 LAELLkelGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASY 71
|
90
....*....|
gi 1945600751 1369 LQMLGRAGRP 1378
Cdd:smart00490 72 IQRIGRAGRA 81
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
1011-1170 |
4.57e-15 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 76.32 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1011 DENVLLCAPTGAGKTNVAMLTVLHEINKNRDPQTGhidldsfKIVYIAPMKALVQEMVGNFSRRLRPYGISVAELTGDRQ 1090
Cdd:cd17927 17 GKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKG-------KVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1091 LT--KQQIAET-QIIVTTPEKWDVITRKATDRSYTaLVRLIIIDEIHllHDDRGPVLESIVSRTIR-TMEQTQELVRLVG 1166
Cdd:cd17927 90 ENvsVEQIVESsDVIIVTPQILVNDLKSGTIVSLS-DFSLLVFDECH--NTTKNHPYNEIMFRYLDqKLGSSGPLPQILG 166
|
....
gi 1945600751 1167 LSAT 1170
Cdd:cd17927 167 LTAS 170
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1011-1173 |
5.67e-15 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350783 [Multi-domain] Cd Length: 192 Bit Score: 75.87 E-value: 5.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1011 DENVLLCAPTGAGKTNV---AMLTVLHEINKNrdpqtghidldsfKIVYIAPMKALVQEMV----GNFSRRLRPYGISV- 1082
Cdd:cd18025 16 RESALIVAPTSSGKTFIsyyCMEKVLRESDDG-------------VVVYVAPTKALVNQVVaevyARFSKKYPPSGKSLw 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1083 AELTGDRQLtkQQIAETQIIVTTPEKWDVITRKATDRSYTALVRLIIIDEIHLLhddrGPVLESIVsrtirtMEQTQELV 1162
Cdd:cd18025 83 GVFTRDYRH--NNPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSI----GQSEDGAV------WEQLLLLI 150
|
170
....*....|...
gi 1945600751 1163 R--LVGLSATLPN 1173
Cdd:cd18025 151 PcpFLALSATIGN 163
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1012-1376 |
6.85e-15 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 81.09 E-value: 6.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1012 ENVLLCAPTGAGKTNVAMLTVLHEInkNRDPQTGHIDlDSFKIVYIAPMKALVQEMVGNF------------SRRLRPYG 1079
Cdd:PRK13767 48 KNVLISSPTGSGKTLAAFLAIIDEL--FRLGREGELE-DKVYCLYVSPLRALNNDIHRNLeeplteireiakERGEELPE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1080 ISVAELTGD-RQLTKQQIAET--QIIVTTPEKWDVITRKATDRSYTALVRLIIIDEIHLLHDD-RG-------PVLESIV 1148
Cdd:PRK13767 125 IRVAIRTGDtSSYEKQKMLKKppHILITTPESLAILLNSPKFREKLRTVKWVIVDEIHSLAENkRGvhlslslERLEELA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1149 SRtirtmeqtqELVRlVGLSATLPNYADVAAFLrvnpktGLFFFDGAFRPC---------PLKQQFIGVTEKKAIKRFQV 1219
Cdd:PRK13767 205 GG---------EFVR-IGLSATIEPLEEVAKFL------VGYEDDGEPRDCeivdarfvkPFDIKVISPVDDLIHTPAEE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1220 MNDVCYEKVMEqLDQREENqVLVFVHSRKETAKTAKTLRDMALEKDTIGhflkqdsasrevlQTEAatvkdpnladllpy 1299
Cdd:PRK13767 269 ISEALYETLHE-LIKEHRT-TLIFTNTRSGAERVLYNLRKRFPEEYDED-------------NIGA-------------- 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1945600751 1300 gfaiHHAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPAHAVIIkgtQIYSPEkgrwvelSPQDVLQMLGRAG 1376
Cdd:PRK13767 320 ----HHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVV---LLGSPK-------SVSRLLQRIGRAG 382
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
993-1179 |
2.65e-13 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 70.69 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 993 AESLNRVQSRlyptafgsdENVLLCAPTGAGKTNVAMLTVLHEInkNRDPQTghidldsfKIVYIAPMKALVQEMVGNFS 1072
Cdd:cd17923 6 AEAIEAARAG---------RSVVVTTGTASGKSLCYQLPILEAL--LRDPGS--------RALYLYPTKALAQDQLRSLR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1073 RRLRPY--GISVAELTGD---RQLTKQQIAETQIIVTTPEK--WDVITRKATDRSYTALVRLIIIDEIHLLhddRGpVLE 1145
Cdd:cd17923 67 ELLEQLglGIRVATYDGDtprEERRAIIRNPPRILLTNPDMlhYALLPHHDRWARFLRNLRYVVLDEAHTY---RG-VFG 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 1945600751 1146 SIVSRTIRTMEQTQEL----VRLVGLSATLPNYADVAA 1179
Cdd:cd17923 143 SHVALLLRRLRRLCRRygadPQFILTSATIGNPAEHAR 180
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
1013-1378 |
1.87e-12 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 72.75 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1013 NVLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldsfkIVYIAPMKALVQEMVGNFSRRLRpygisVAELTGDRqlt 1092
Cdd:COG1061 102 RGLVVAPTGTGKTVLALALAAELLRGKR-------------VLVLVPRRELLEQWAEELRRFLG-----DPLAGGGK--- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1093 kqQIAETQIIVTTpekWDVITRKATDRSYTALVRLIIIDEIHLLhddRGPVLESIVSRTIRTmeqtqelvRLVGLSATlP 1172
Cdd:COG1061 161 --KDSDAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHA---GAPSYRRILEAFPAA--------YRLGLTAT-P 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1173 NYADVAAFLrvnpktgLFFFDG-AFRpCPLKQQFigvtEKKAIKRFQVMN------------DVCYEKVMEQLDQREENQ 1239
Cdd:COG1061 224 FRSDGREIL-------LFLFDGiVYE-YSLKEAI----EDGYLAPPEYYGirvdltderaeyDALSERLREALAADAERK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1240 VLVFVHSRKETAKTAKTL-----RDMAlekDTIGHFLKQDSAsrevlqtEAATVkdpnladllpygfaihHAGMTRADRT 1314
Cdd:COG1061 292 DKILRELLREHPDDRKTLvfcssVDHA---EALAELLNEAGI-------RAAVV----------------TGDTPKKERE 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1945600751 1315 LVEDLFADGHVKVLCSTATLAWGVNLPA--HAVIIKGTQiyspekgrwvelSPQDVLQMLGRAGRP 1378
Cdd:COG1061 346 EILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPTG------------SPREFIQRLGRGLRP 399
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
1864-2032 |
1.06e-11 |
|
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: 66.47 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1864 NVFIGAPTGSGKTVCAEFALLR-LWSssEEARAVYVAPFQEIVdQRAADWKQKF---KGKEIVTLTGETS-ADLKLLERG 1938
Cdd:cd18026 35 NLVYSLPTSGGKTLVAEILMLKrLLE--RRKKALFVLPYVSIV-QEKVDALSPLfeeLGFRVEGYAGNKGrSPPKRRKSL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1939 DVICCTPAQWDVVSRRWKQRKNVQNVNLFIADELHLIG-GDIGPTYEVIVSRMRYIASqtnKSIRIVALSTSLANARDLG 2017
Cdd:cd18026 112 SVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGdGHRGALLELLLTKLLYAAQ---KNIQIVGMSATLPNLEELA 188
|
170
....*....|....*
gi 1945600751 2018 EWIGAtSHSVFNFHP 2032
Cdd:cd18026 189 SWLRA-ELYTTNFRP 202
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
1012-1172 |
3.25e-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: 65.19 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1012 ENVLLCAPTGAGKTNVAMLTVLHEINKNRDP-QTGhidldsfKIVYIAPMKALVQEMVGNFSRRLRPyGISVAELTGDRQ 1090
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAgEKG-------RVVVLVNKVPLVEQQLEKFFKYFRK-GYKVTGLSGDSS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1091 L---TKQQIAETQIIVTTPEKWDVITRKAT--DRSYTALVRLIIIDEIHllHDDRGPVLESIVSRTIR-TMEQTQELVRL 1164
Cdd:cd18036 90 HkvsFGQIVKASDVIICTPQILINNLLSGReeERVYLSDFSLLIFDECH--HTQKEHPYNKIMRMYLDkKLSSQGPLPQI 167
|
....*...
gi 1945600751 1165 VGLSATLP 1172
Cdd:cd18036 168 LGLTASPG 175
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1225-1377 |
2.36e-10 |
|
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: 59.92 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1225 YEKVMEQLDQREENQVLVFVHSRKetaktaktlrdmalekdtighflkqdsasrevlqteaaTVKDPNLADLLPYGFAIH 1304
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKK--------------------------------------TLEAELLLEKEGIKVARL 44
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1945600751 1305 HAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLP-AHAVIikgtqIYSPEKgrwvelSPQDVLQMLGRAGR 1377
Cdd:pfam00271 45 HGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVI-----NYDLPW------NPASYIQRIGRAGR 107
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1014-1331 |
5.87e-10 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 64.72 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1014 VLLCAPTGAGKTNVAMLTVLHEINKNrdpqtghidlDSFKIVYIAPMKALVQEMvgnFSRRLRPYGISVAELTGDRQLTK 1093
Cdd:COG1203 150 FILTAPTGGGKTEAALLFALRLAAKH----------GGRRIIYALPFTSIINQT---YDRLRDLFGEDVLLHHSLADLDL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1094 QQIAE-----------------TQIIVTTPekwD-----VITRKatdRSYTA-LVRL----IIIDEIHLLHDDRGPVLEs 1146
Cdd:COG1203 217 LEEEEeyesearwlkllkelwdAPVVVTTI---DqlfesLFSNR---KGQERrLHNLansvIILDEVQAYPPYMLALLL- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1147 ivsRTIRTMEQTQelVRLVGLSATLPnyadvaAFLRvnpktgLFFFDGAFRPCPLKQQFIGVTEKKAIKRFQV-MNDVCY 1225
Cdd:COG1203 290 ---RLLEWLKNLG--GSVILMTATLP------PLLR------EELLEAYELIPDEPEELPEYFRAFVRKRVELkEGPLSD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1226 EKVMEQLDQ--REENQVLVFVHSRKETAKTAKTLRDMALEKDTIgHFlkqdsasrevlqteaatvkdpnladllpygfai 1303
Cdd:COG1203 353 EELAELILEalHKGKSVLVIVNTVKDAQELYEALKEKLPDEEVY-LL--------------------------------- 398
|
330 340 350
....*....|....*....|....*....|..
gi 1945600751 1304 hHAGMTRADRTLVE----DLFADGHVKVLCST 1331
Cdd:COG1203 399 -HSRFCPADRSEIEkeikERLERGKPCILVST 429
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
1869-2215 |
6.12e-10 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 64.66 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1869 APTGSGKTVCAEFALLRLwssSEEARAVYVAPFQEIVDQraadWKQKFKGKEIVTLTGETSADlkllERGDVICCTPAQw 1948
Cdd:COG1061 107 APTGTGKTVLALALAAEL---LRGKRVLVLVPRRELLEQ----WAEELRRFLGDPLAGGGKKD----SDAPITVATYQS- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1949 dvVSRRWKQRKNVQNVNLFIADELHLIGgdiGPTYEVIVSRMryiasqtnKSIRIVALStslanA---RDLGEWIGATSH 2025
Cdd:COG1061 175 --LARRAHLDELGDRFGLVIIDEAHHAG---APSYRRILEAF--------PAAYRLGLT-----AtpfRSDGREILLFLF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2026 S--VFNFHPS--------------VRPVPLEIHMQSYNIP--HFASLMMAMAKPTYLAITT----HSANKPVIVFVPSRK 2083
Cdd:COG1061 237 DgiVYEYSLKeaiedgylappeyyGIRVDLTDERAEYDALseRLREALAADAERKDKILREllreHPDDRKTLVFCSSVD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 2084 QCrltavdiitycigddtpdrflhcklEEIQPMLDRLQDKTLVetlqhgigFYHEALSKQDKRIVEQLyESGAIQVVVAS 2163
Cdd:COG1061 317 HA-------------------------EALAELLNEAGIRAAV--------VTGDTPKKEREEILEAF-RDGELRILVTV 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1945600751 2164 R--DTCWALP-LNsHMVIVMGTQYfegkehryadypITDVLQMMGRACRPREDDT 2215
Cdd:COG1061 363 DvlNEGVDVPrLD-VAILLRPTGS------------PREFIQRLGRGLRPAPGKE 404
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1018-1376 |
1.82e-09 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 63.79 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1018 APTGAGKTNVAMLTVLHEINKNRDPQTGHI-DLDSFKIVYIAPMKALVQEMVGNFSRRLRPYG------------ISVAE 1084
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFREGGEDTREAhKRKTSRILYISPIKALGTDVQRNLQIPLKGIAderrrrgetevnLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1085 LTGDRqlTKQQIAE-----TQIIVTTPEK-WDVITRKAtdRSYTALVRLIIIDEIHLLH-DDRGPVLESIVSRTIRTMEQ 1157
Cdd:PRK09751 83 RTGDT--PAQERSKltrnpPDILITTPESlYLMLTSRA--RETLRGVETVIIDEVHAVAgSKRGAHLALSLERLDALLHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1158 TQElvrLVGLSATLPNYADVAAFLrvnpktglfffdGAFRPcplkqqfIGVTEKKAIKRFQV--------MNDVCYEKVM 1229
Cdd:PRK09751 159 SAQ---RIGLSATVRSASDVAAFL------------GGDRP-------VTVVNPPAMRHPQIrivvpvanMDDVSSVASG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1230 EQLDQREE--------------NQVL------VFVHSRKETAKTAKTLRDMALEKDTIGHFLKQDSASREvlQTEAATVK 1289
Cdd:PRK09751 217 TGEDSHAGregsiwpyietgilDEVLrhrstiVFTNSRGLAEKLTARLNELYAARLQRSPSIAVDAAHFE--STSGATSN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1290 DPNLADllPYGFAIHHAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPAHAVIIkgtQIYSPekgrwveLSPQDVL 1369
Cdd:PRK09751 295 RVQSSD--VFIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVI---QVATP-------LSVASGL 362
|
....*..
gi 1945600751 1370 QMLGRAG 1376
Cdd:PRK09751 363 QRIGRAG 369
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
1225-1377 |
2.80e-09 |
|
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: 58.04 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1225 YEKVMEQLDQreENQVLVFVHSRKETAKTAKTLRDmALEKDTIGHFlkqdsasrevlqteaatvkdpnladllpygFAIH 1304
Cdd:cd18796 28 YAEVIFLLER--HKSTLVFTNTRSQAERLAQRLRE-LCPDRVPPDF------------------------------IALH 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1945600751 1305 HAGMTRADRTLVEDLFADGHVKVLCSTATLAWGVNLPA-HAVIikgtQIYSPekgrwveLSPQDVLQMLGRAGR 1377
Cdd:cd18796 75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDvDLVI----QIGSP-------KSVARLLQRLGRSGH 137
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1793-2018 |
8.23e-09 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 61.39 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1793 RWLHSSTKLPVSFKHL-ILPEKYAPHTELHD-LQPLPVSALRNPEYEQVYSgwidHfnpiQTQVFNtLYTTNDNVFIGAP 1870
Cdd:COG1205 9 ERLRASPRYGDQIVHVrTIPAREARYAPWPDwLPPELRAALKKRGIERLYS----H----QAEAIE-AARAGKNVVIATP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1871 TGSGKTVCaeFAL--LRLWSSSEEARAVYVAP-----------FQEIVDQRAADWKqkfkgkeIVTLTGETSADL--KLL 1935
Cdd:COG1205 80 TASGKSLA--YLLpvLEALLEDPGATALYLYPtkalardqlrrLRELAEALGLGVR-------VATYDGDTPPEErrWIR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1936 ERGDVICCTPaqwDVV-------SRRWkqRKNVQNVNLFIADELHliggdigpTYE--------VIVSRMRYIASQTNKS 2000
Cdd:COG1205 151 EHPDIVLTNP---DMLhygllphHTRW--ARFFRNLRYVVIDEAH--------TYRgvfgshvaNVLRRLRRICRHYGSD 217
|
250
....*....|....*...
gi 1945600751 2001 IRIVALSTSLANARDLGE 2018
Cdd:COG1205 218 PQFILASATIGNPAEHAE 235
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
1869-1989 |
9.03e-09 |
|
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: 56.55 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1869 APTGSGKTVCAEFALLRLWssseEARAVYVAPFQEIVDQRAADWKQKFKGKEIVTLTGEtsaDLKLLERGDVICCTpaqW 1948
Cdd:cd17926 25 LPTGSGKTLTALALIAYLK----ELRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGG---KKKDFDDANVVVAT---Y 94
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1945600751 1949 DVVSRRWKQRKNVQNVN-LFIADELHLIGGDigpTYEVIVSR 1989
Cdd:cd17926 95 QSLSNLAEEEKDLFDQFgLLIVDEAHHLPAK---TFSEILKE 133
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
1864-1978 |
9.56e-09 |
|
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: 56.26 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1864 NVFIGAPTGSGKTVCAEFALLRLwSSSEEARAVYVAPFQEIVDQRAADWKQKFKGKE-IVTLTGETSADLKLLERG---D 1939
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLL-LLKKGKKVLVLVPTKALALQTAERLRELFGPGIrVAVLVGGSSAEEREKNKLgdaD 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 1945600751 1940 VICCTPAQWDVVSRRWKQRKnVQNVNLFIADELHLIGGD 1978
Cdd:cd00046 82 IIIATPDMLLNLLLREDRLF-LKDLKLIIVDEAHALLID 119
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1862-1973 |
1.49e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 56.14 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1862 NDNVFIGAPTGSGKTVCAEFALLRLWSSSEEARAVYVAPFQEIVDQraadWKQKFK--GKEIVTLTGETSADLKLLERGD 1939
Cdd:pfam04851 23 QKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQ----ALEEFKkfLPNYVEIGEIISGDKKDESVDD 98
|
90 100 110
....*....|....*....|....*....|....*.
gi 1945600751 1940 --VICCTPAQWDVVSRRWKQRKNVQNVNLFIADELH 1973
Cdd:pfam04851 99 nkIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1011-1134 |
1.61e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 56.14 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1011 DENVLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldSFKIVYIAPMKALVQEMVGNFSRRLRPYGISVAELTGDRQ 1090
Cdd:pfam04851 23 QKRGLIVMATGSGKTLTAAKLIARLFKKGP----------IKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKK 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1945600751 1091 LTKQQiaETQIIVTTPEKWDVITRKATDRSYTALVRLIIIDEIH 1134
Cdd:pfam04851 93 DESVD--DNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1843-2023 |
1.69e-08 |
|
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: 56.50 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1843 WIDHFNPIQTQVFNTLyTTNDNVFIGAPTGSGKTVCAEFALlrLWSSSEEARAVYVAPFQEIVDQRAADWKQKFkgKEIV 1922
Cdd:cd18027 5 WPFELDVFQKQAILHL-EAGDSVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFKNTF--GDVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1923 TLTGetsaDLKLLERGDVICCTPAQwdVVSRRWKQRKNVQNVNLFIADELHLIG-GDIGPTYEVIVSRMryiasqtNKSI 2001
Cdd:cd18027 80 LITG----DVQLNPEASCLIMTTEI--LRSMLYNGSDVIRDLEWVIFDEVHYINdAERGVVWEEVLIML-------PDHV 146
|
170 180
....*....|....*....|..
gi 1945600751 2002 RIVALSTSLANARDLGEWIGAT 2023
Cdd:cd18027 147 SIILLSATVPNTVEFADWIGRI 168
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
999-1172 |
2.92e-08 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 56.30 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 999 VQSRLYPTAFgSDENVLLCAPTGAGKTNVAMLTVLHEINKNRDPQTGHIdldsfKIVYIAPMKALVQEMVGNFSRRLRPY 1078
Cdd:cd00268 16 IQAQAIPLIL-SGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGP-----QALVLAPTRELAMQIAEVARKLGKGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1079 GISVAELTGDRQLTKQQIAE---TQIIVTTPEK-WDVITRKATDrsyTALVRLIIIDEI-HLLHDDRGPVLESIVSrtiR 1153
Cdd:cd00268 90 GLKVAAIYGGAPIKKQIEALkkgPDIVVGTPGRlLDLIERGKLD---LSNVKYLVLDEAdRMLDMGFEEDVEKILS---A 163
|
170
....*....|....*....
gi 1945600751 1154 TMEQTQELVrlvgLSATLP 1172
Cdd:cd00268 164 LPKDRQTLL----FSATLP 178
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
1862-1978 |
8.97e-08 |
|
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: 54.44 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1862 NDNVFIGAPTGSGKTVCAEF-ALLRLwsSSEEARAVYVAPFQEIVDQRAADWKQKFKGKE-IVTLTGETSAD--LKLLER 1937
Cdd:cd18035 16 NGNTLIVLPTGLGKTIIAILvAADRL--TKKGGKVLILAPSRPLVEQHAENLKRVLNIPDkITSLTGEVKPEerAERWDA 93
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1945600751 1938 GDVICCTPA--QWDVVSRRWkqrkNVQNVNLFIADELHLIGGD 1978
Cdd:cd18035 94 SKIIVATPQviENDLLAGRI----TLDDVSLLIFDEAHHAVGN 132
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
1011-1174 |
9.93e-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: 54.60 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1011 DENVLLCAPTGAGKTNVAMLTVLHEINKNRDPqtghidldsfKIVYIAPMKALVQEMVGNFSRRLRPYGI--SVAELTGD 1088
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWALKLAARGGKR----------RIIYALPTRATINQMYERIREILGRLDDedKVLLLHSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1089 RQLTKQQIAETQ---------------------IIVTTpekWD-----VITRKATDRSYTALVR-LIIIDEIHLLhDDRg 1141
Cdd:cd17930 71 AALELLESDEEPdddpveavdwalllkrswlapIVVTT---IDqllesLLKYKHFERRLHGLANsVVVLDEVQAY-DPE- 145
|
170 180 190
....*....|....*....|....*....|....*
gi 1945600751 1142 pvlesIVSRTIRTMEQTQE--LVRLVGLSATLPNY 1174
Cdd:cd17930 146 -----YMALLLKALLELLGelGGPVVLMTATLPAL 175
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
1862-2009 |
1.38e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 57.05 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1862 NDNVFIGAPTGSGKTVCAEF-ALLRLwsSSEEARAVYVAPFQEIVDQRAADWKQKFKGKE--IVTLTGETSAD--LKLLE 1936
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLvIAERL--HKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEdeIVVFTGEVSPEkrKELWE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1945600751 1937 RGDVICCTP--AQWDVVSRRWkqrkNVQNVNLFIADELHLIGGDIGPTYevIVSRMRyiasQTNKSIRIVALSTS 2009
Cdd:COG1111 95 KARIIVATPqvIENDLIAGRI----DLDDVSLLIFDEAHRAVGNYAYVY--IAERYH----EDAKDPLILGMTAS 159
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
1864-2012 |
1.64e-07 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 53.98 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1864 NVFIGAPTGSGKT-----VCAEfaLLRLWSSSEEARAVYVAPFQEIVDQRAADWKQKF--KGKEIVTLTGETSADL---K 1933
Cdd:cd17927 19 NTIICLPTGSGKTfvavlICEH--HLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFerPGYKVTGLSGDTSENVsveQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1934 LLERGDVICCTPaqwDVVSRRWKQRKNVQ--NVNLFIADELHLIGGDiGPTYEVIVSRMRYIASQTNKSIRIVALSTSLA 2011
Cdd:cd17927 97 IVESSDVIIVTP---QILVNDLKSGTIVSlsDFSLLVFDECHNTTKN-HPYNEIMFRYLDQKLGSSGPLPQILGLTASPG 172
|
.
gi 1945600751 2012 N 2012
Cdd:cd17927 173 V 173
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
1012-1173 |
1.70e-07 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350782 [Multi-domain] Cd Length: 205 Bit Score: 54.37 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1012 ENVLLCAPTGAGKTNVAMLTVLHEInknRDPQtghidldsfKIVYIAPMKALVQEMVGNFSRRLRPYGIsvaeLTGDRQL 1091
Cdd:cd18024 48 ESVLVSAHTSAGKTVVAEYAIAQSL---RDKQ---------RVIYTSPIKALSNQKYRELQEEFGDVGL----MTGDVTI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1092 TkqqiAETQIIVTTPEkwdvITRKATDRSYTAL--VRLIIIDEIHLLHD-DRGPVLEsivsRTIRTMEQTqelVRLVGLS 1168
Cdd:cd18024 112 N----PNASCLVMTTE----ILRSMLYRGSEIMreVAWVIFDEIHYMRDkERGVVWE----ETIILLPDK---VRYVFLS 176
|
....*
gi 1945600751 1169 ATLPN 1173
Cdd:cd18024 177 ATIPN 181
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
999-1172 |
7.66e-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: 52.75 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 999 VQSRLYPTAFGSdENVLLCAPTGAGKTNVAMLTVLHEInkNRDPQTGHIDLDSFKIVYIAPMKALVQEmVGNFSRRL-RP 1077
Cdd:cd17948 16 VQKQGIPSILRG-RNTLCAAETGSGKTLTYLLPIIQRL--LRYKLLAEGPFNAPRGLVITPSRELAEQ-IGSVAQSLtEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1078 YGISVAELTGDRqlTKQQI-----AETQIIVTTPekwDVITRKATDRSY-TALVRLIIIDEIH-LLHDDRGPVLESIVSR 1150
Cdd:cd17948 92 LGLKVKVITGGR--TKRQIrnphfEEVDILVATP---GALSKLLTSRIYsLEQLRHLVLDEADtLLDDSFNEKLSHFLRR 166
|
170 180
....*....|....*....|....*...
gi 1945600751 1151 T---IRTMEQTQEL---VRLVGLSATLP 1172
Cdd:cd17948 167 FplaSRRSENTDGLdpgTQLVLVSATMP 194
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
1012-1132 |
8.07e-07 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 52.21 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1012 ENVLLCAPTGAGKTNVAMLTVLHEINKNRDPqtghidlDSFKIVYIAPMKALVQEMVGNFSRRLRPYGISVAELT-GDRQ 1090
Cdd:cd17957 28 RDLLACAPTGSGKTLAFLIPILQKLGKPRKK-------KGLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSkSLEA 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1945600751 1091 LTKQQIAETQ---IIVTTPEKW-DVITRKATDRSytaLVRLIIIDE 1132
Cdd:cd17957 101 KAKDGPKSITkydILVSTPLRLvFLLKQGPIDLS---SVEYLVLDE 143
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
1864-2018 |
8.77e-07 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 51.43 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1864 NVFIGAPTGSGKTVCAEFALLRLWSSSEEARAVYVAPFQEIV-DQ--RAADWKQKFKGKEIV-TLTGETSADLK---LLE 1936
Cdd:cd17923 17 SVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAqDQlrSLRELLEQLGLGIRVaTYDGDTPREERraiIRN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1937 RGDVICCTPAQ--WDVVSRRWKQRKNVQNVNLFIADELHLIGGDIGPTYEVIVSRMRYIASQTNKSIRIVALSTSLANAR 2014
Cdd:cd17923 97 PPRILLTNPDMlhYALLPHHDRWARFLRNLRYVVLDEAHTYRGVFGSHVALLLRRLRRLCRRYGADPQFILTSATIGNPA 176
|
....
gi 1945600751 2015 DLGE 2018
Cdd:cd17923 177 EHAR 180
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
1862-1973 |
1.27e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 54.11 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1862 NDNVFIGAPTGSGKTVcaeFALL----RLwsSSEEARAVYVAPFQEIVDQRAADWKQKFKGK--EIVTLTGETSAD--LK 1933
Cdd:PRK13766 29 KKNTLVVLPTGLGKTA---IALLviaeRL--HKKGGKVLILAPTKPLVEQHAEFFRKFLNIPeeKIVVFTGEVSPEkrAE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1945600751 1934 LLERGDVICCTP--AQWDVVSRRWkqrkNVQNVNLFIADELH 1973
Cdd:PRK13766 104 LWEKAKVIVATPqvIENDLIAGRI----SLEDVSLLIFDEAH 141
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
1011-1169 |
1.41e-06 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 51.50 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1011 DENVLLCAPTGAGKTNVAMLTVLHEINKNRDPQTGHidldsfKI-VYIAPMKALVQ---EMVGNFSrrlrpyGISVAELT 1086
Cdd:cd18034 16 KRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNPK------KRaVFLVPTVPLVAqqaEAIRSHT------DLKVGEYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1087 GD-------RQLTKQQIAETQIIVTTPEkwdvITRKATDRSYTAL--VRLIIIDEIHL---LHDDRGpvlesiVSRTIRT 1154
Cdd:cd18034 84 GEmgvdkwtKERWKEELEKYDVLVMTAQ----ILLDALRHGFLSLsdINLLIFDECHHatgDHPYAR------IMKEFYH 153
|
170
....*....|....*
gi 1945600751 1155 MEQTQELVRLVGLSA 1169
Cdd:cd18034 154 LEGRTSRPRILGLTA 168
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
999-1134 |
2.19e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 53.20 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 999 VQSRLYPT---AFGSDENVLLCAPTGAGKTNVAMLT---VLHEINKnrdpqtghidldsfKIVYIAPMKALVQEMVGNFS 1072
Cdd:COG1111 2 IERRLYQLnlaASALRKNTLVVLPTGLGKTAVALLViaeRLHKKGG--------------KVLFLAPTKPLVEQHAEFFK 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1945600751 1073 RRLRPYGISVAELTGDRQLTKQQI--AETQIIVTTPE--KWDVITRkatdRSYTALVRLIIIDEIH 1134
Cdd:COG1111 68 EALNIPEDEIVVFTGEVSPEKRKElwEKARIIVATPQviENDLIAG----RIDLDDVSLLIFDEAH 129
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
1844-1971 |
2.72e-06 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 50.52 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1844 IDHFNPIQTQVFNTLYTTNDnVFIGAPTGSGKTVCaeFAL-------LRLWSSSEEARAVYVAPFQEIVDQRAADWKQ-- 1914
Cdd:cd00268 10 FEKPTPIQAQAIPLILSGRD-VIGQAQTGSGKTLA--FLLpilekllPEPKKKGRGPQALVLAPTRELAMQIAEVARKlg 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1945600751 1915 KFKGKEIVTLTGETS--ADLKLLERG-DVICCTPAQ-WDVVSRRwkqRKNVQNVNLFIADE 1971
Cdd:cd00268 87 KGTGLKVAAIYGGAPikKQIEALKKGpDIVVGTPGRlLDLIERG---KLDLSNVKYLVLDE 144
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
1012-1134 |
5.16e-06 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350831 [Multi-domain] Cd Length: 202 Bit Score: 49.82 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1012 ENVLLCAPTGAGKTNVAMLTVLHEINKNRDPQTGhidldsfKIVYIAPMKALVQEMVGNFSRRLRPYGISVAELTGD--R 1089
Cdd:cd18073 18 KNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKG-------KVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGAtaE 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1945600751 1090 QLTKQQIAE-TQIIVTTPEKWDVITRKATDRSYTALVrLIIIDEIH 1134
Cdd:cd18073 91 NVPVEQIIEnNDIIILTPQILVNNLKKGTIPSLSIFT-LMIFDECH 135
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
997-1134 |
5.92e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 51.80 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 997 NRVQSRLYP---TAFGSDENVLLCAPTGAGKTNVAMLTV---LHEINKnrdpqtghidldsfKIVYIAPMKALVQEMVGN 1070
Cdd:PRK13766 12 NTIEARLYQqllAATALKKNTLVVLPTGLGKTAIALLVIaerLHKKGG--------------KVLILAPTKPLVEQHAEF 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1945600751 1071 FSRRLRPYGISVAELTGDRQLTKQQIA--ETQIIVTTPE--KWDVITRkatdRSYTALVRLIIIDEIH 1134
Cdd:PRK13766 78 FRKFLNIPEEKIVVFTGEVSPEKRAELweKAKVIVATPQviENDLIAG----RISLEDVSLLIFDEAH 141
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
1862-2020 |
8.59e-06 |
|
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: 48.35 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1862 NDNVFIGAPTGSGKTVCAEFALLRLWSSSEEA--RAVYVAPFQE-IVDQ-----RAADWKQkfKGKEIVTLTGETSADLK 1933
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKgvQVLYISPLKAlINDQerrleEPLDEID--LEIPVAVRHGDTSQSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1934 --LLER-GDVICCTPAQWDV--VSRR-WKQRKNVQNVnlfIADELH-LIGGDIGPTYEVIVSRMRYIasqTNKSIRIVAL 2006
Cdd:cd17922 79 akQLKNpPGILITTPESLELllVNKKlRELFAGLRYV---VVDEIHaLLGSKRGVQLELLLERLRKL---TGRPLRRIGL 152
|
170
....*....|....
gi 1945600751 2007 STSLANARDLGEWI 2020
Cdd:cd17922 153 SATLGNLEEAAAFL 166
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
1014-1279 |
1.17e-05 |
|
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: 50.12 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1014 VLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldSFKIVYIAPMKAL-------VQEMVGN--------FSRRLRPY 1078
Cdd:cd09639 2 LVIEAPTGYGKTEAALLWALHSLKSQK----------ADRVIIALPTRATinamyrrAKEAFGEtglyhssiLSSRIKEM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1079 GiSVAELTGDRQLTKQQIAE---TQIIVTTPEKWDVITRKATDRSYTALVRL----IIIDEIHLLhddrgpvLESIVSRT 1151
Cdd:cd09639 72 G-DSEEFEHLFPLYIHSNDTlflDPITVCTIDQVLKSVFGEFGHYEFTLASIanslLIFDEVHFY-------DEYTLALI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1152 IRTMEQTQEL-VRLVGLSATLPNYadvaaFLRVNPKTGLFFFDGAFRPCPLKQQFIGVTEKKAIKRFQVMNDvcyekVME 1230
Cdd:cd09639 144 LAVLEVLKDNdVPILLMSATLPKF-----LKEYAEKIGYVEENEPLDLKPNERAPFIKIESDKVGEISSLER-----LLE 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1945600751 1231 QLDqrEENQVLVFVHSRKETAKTAKTLRDMALEKDTI---GHFLKQDSASRE 1279
Cdd:cd09639 214 FIK--KGGSVAIIVNTVDRAQEFYQQLKEKGPEEEIMlihSRFTEKDRAKKE 263
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
999-1170 |
1.57e-05 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 48.09 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 999 VQSRLYptafgsdENVLLCAPTGAGKT---NVAMLtvlheiNKNRDPQTGhidldsfKIVYIAPMKALV-QEM-----VG 1069
Cdd:cd18033 11 VQKALF-------QNTLVALPTGLGKTfiaAVVML------NYYRWFPKG-------KIVFMAPTKPLVsQQIeacykIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1070 NFSRRlrpygiSVAELTGDRQLTK--QQIAETQIIVTTPEKWDV-ITRKATDRSYtalVRLIIIDEIHllhddRGP---- 1142
Cdd:cd18033 71 GIPSS------QTAELTGSVPPTKraELWASKRVFFLTPQTLENdLKEGDCDPKS---IVCLVIDEAH-----RATgnya 136
|
170 180 190
....*....|....*....|....*....|.
gi 1945600751 1143 ---VLESIVSRTIRTmeqtqelvRLVGLSAT 1170
Cdd:cd18033 137 ycqVVRELMRYNSHF--------RILALTAT 159
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1726-1947 |
3.13e-05 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 49.31 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1726 DFQWDEKVHGVAEAFWIMVEDVDGEHILHHEYFVLKQRYAEEEHLVSFTVPLYEPLPPNYFVT--VVADRWLHSSTKLPV 1803
Cdd:COG1203 4 LAKEALLGALALAALLLLLLALLLAALLLLLLAALLLALLLALLLLAALELALLLLLLLLLLLllLLLLLDLLLDDLAFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1804 SFKHLILPEKYAphTELHDLQPLPVSALRNPEYEQVY---SGWIDHFNPIQTQVFN---TLYTTNDNVFI-GAPTGSGKT 1876
Cdd:COG1203 84 FLLLLIDADWLD--SANFDMARQALDHLLAERLERLLpkkSKPRTPINPLQNEALElalEAAEEEPGLFIlTAPTGGGKT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1877 vcaEFAL---LRLWSSSEEARAVYVAPFQEIVDQ---RAADW----------KQKFKGKEIVTLTGETSADLKLLER--- 1937
Cdd:COG1203 162 ---EAALlfaLRLAAKHGGRRIIYALPFTSIINQtydRLRDLfgedvllhhsLADLDLLEEEEEYESEARWLKLLKElwd 238
|
250
....*....|
gi 1945600751 1938 GDVICCTPAQ 1947
Cdd:COG1203 239 APVVVTTIDQ 248
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
1012-1140 |
3.15e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 47.14 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1012 ENVLLCAPTGAGKTNVAMLTVLHeinknRDPQTghidldsfkIVyIAPMKALVQEMVgnfsRRLRPYGISVAELTG---- 1087
Cdd:cd17920 28 RDVLVVMPTGGGKSLCYQLPALL-----LDGVT---------LV-VSPLISLMQDQV----DRLQQLGIRAAALNStlsp 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1945600751 1088 -DRQLTKQQIA--ETQIIVTTPEKW---DVITRKATDRSyTALVRLIIIDEIHLL----HDDR 1140
Cdd:cd17920 89 eEKREVLLRIKngQYKLLYVTPERLlspDFLELLQRLPE-RKRLALIVVDEAHCVsqwgHDFR 150
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
1864-2010 |
3.91e-05 |
|
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: 47.09 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1864 NVFIGAPTGSGKTVCAEFALLR----LWSSSEEARAVYVAPFQEIVDQRAADWKQKF-KGKEIVTLTGETSADL---KLL 1935
Cdd:cd18036 19 NTIICAPTGSGKTRVAVYICRHhlekRRSAGEKGRVVVLVNKVPLVEQQLEKFFKYFrKGYKVTGLSGDSSHKVsfgQIV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1945600751 1936 ERGDVICCTPA--QWDVVSRRWKQRKNVQNVNLFIADELHLIGGDiGPtYEVIVSR-MRYIASQTNKSIRIVALSTSL 2010
Cdd:cd18036 99 KASDVIICTPQilINNLLSGREEERVYLSDFSLLIFDECHHTQKE-HP-YNKIMRMyLDKKLSSQGPLPQILGLTASP 174
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1862-2022 |
1.05e-04 |
|
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: 45.82 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1862 NDNVFIGAPTGSGKTVCAEFALLRLWSSSEEARAVYVAPFQEIVDQRAADWKQKFK------GKEIV-TLTGETSADlkL 1934
Cdd:cd18025 16 RESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSkkyppsGKSLWgVFTRDYRHN--N 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1935 LERGDVICCTPA--QWDVVSR---RWKQRknvqnVNLFIADELHLIGGDI-GPTYEVIVSRMRyiasqtnksIRIVALST 2008
Cdd:cd18025 94 PMNCQVLITVPEclEILLLSPhnaSWVPR-----IKYVIFDEIHSIGQSEdGAVWEQLLLLIP---------CPFLALSA 159
|
170
....*....|....
gi 1945600751 2009 SLANARDLGEWIGA 2022
Cdd:cd18025 160 TIGNPQKFHEWLQS 173
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
999-1134 |
1.44e-04 |
|
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: 45.20 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 999 VQSRLYP---TAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNRDpqtghidldsfKIVYIAPMKALVQEMVGNFsRRL 1075
Cdd:cd18035 1 EERRLYQvliAAVALNGNTLIVLPTGLGKTIIAILVAADRLTKKGG-----------KVLILAPSRPLVEQHAENL-KRV 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1945600751 1076 RPYGISVAELTGDRQLTKQQ--IAETQIIVTTPE--KWDVITRKATDRSytalVRLIIIDEIH 1134
Cdd:cd18035 69 LNIPDKITSLTGEVKPEERAerWDASKIIVATPQviENDLLAGRITLDD----VSLLIFDEAH 127
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
994-1193 |
2.14e-04 |
|
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: 44.88 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 994 ESLNRVQSRLYPTAFGSDENVLLCAPTGAGKTnVAML--TVLHEINKNRDPQTGHIdldsfKIVYIAPMKALVQEM---V 1068
Cdd:cd17964 15 ETMTPVQQKTLKPILSTGDDVLARAKTGTGKT-LAFLlpAIQSLLNTKPAGRRSGV-----SALIISPTRELALQIaaeA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1069 GNFSRRLRPYGISVAelTG----DRQLTKQQIAETQIIVTTPEKWDVITRKATDRSYTALVRLIIIDEI-HLLhdDRG-- 1141
Cdd:cd17964 89 KKLLQGLRKLRVQSA--VGgtsrRAELNRLRRGRPDILVATPGRLIDHLENPGVAKAFTDLDYLVLDEAdRLL--DMGfr 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1945600751 1142 PVLESIVSR-TIRTMEQTQELVrlvgLSATLPnyADVAAFLRVNPKTGLFFFD 1193
Cdd:cd17964 165 PDLEQILRHlPEKNADPRQTLL----FSATVP--DEVQQIARLTLKKDYKFID 211
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
999-1185 |
2.99e-04 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 999 VQSRLYPTAFGSDEnVLLCAPTGAGKTNVAMLTVLheinknrdpqtghidldsfKIV---YIAPMKALVQ---EMVGNFS 1072
Cdd:cd17938 25 IQAEAIPLILGGGD-VLMAAETGSGKTGAFCLPVL-------------------QIVvalILEPSRELAEqtyNCIENFK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1073 RRLRPYGISVAELTGD---RQLTKQQIAETQIIVTTPEK-WDVITRKATDRSYtalVRLIIIDEI-HLLHDDRGPVLESI 1147
Cdd:cd17938 85 KYLDNPKLRVALLIGGvkaREQLKRLESGVDIVVGTPGRlEDLIKTGKLDLSS---VRFFVLDEAdRLLSQGNLETINRI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1945600751 1148 VSRTIRTMEQTQELVRLVgLSATL--PNYADVAAFLRVNP 1185
Cdd:cd17938 162 YNRIPKITSDGKRLQVIV-CSATLhsFEVKKLADKIMHFP 200
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1012-1181 |
3.00e-04 |
|
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: 44.18 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1012 ENVLLCAPTGAGKTNVAMLTV-LHEINKNRdpqtghidldsfkIVYIAPMKALVQEMVGNFSRRLRPYGIsvaeLTGDRQ 1090
Cdd:cd18027 24 DSVFVAAHTSAGKTVVAEYAIaLAQKHMTR-------------TIYTSPIKALSNQKFRDFKNTFGDVGL----ITGDVQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1091 LTkqqiAETQIIVTTPEkwdvITRKATDRSYTAL--VRLIIIDEIHLLHD-DRGPVLESIVSrtirtmeQTQELVRLVGL 1167
Cdd:cd18027 87 LN----PEASCLIMTTE----ILRSMLYNGSDVIrdLEWVIFDEVHYINDaERGVVWEEVLI-------MLPDHVSIILL 151
|
170
....*....|....
gi 1945600751 1168 SATLPNYADVAAFL 1181
Cdd:cd18027 152 SATVPNTVEFADWI 165
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
1014-1279 |
3.08e-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: 45.52 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1014 VLLCAPTGAGKTNVAMLTVLHEINKNRdpqtghidldSFKIVYIAPMKALVQEM----VGNFSRRLRPYG---------- 1079
Cdd:TIGR01587 2 LVIEAPTGYGKTEAALLWALHSIKSQK----------ADRVIIALPTRATINAMyrraKELFGSELVGLHhsssfsrike 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1080 -ISVAELTGDRQLTKQQIAE---TQIIVTTPEKWDVITRKATDRSYTALVRL----IIIDEIHLLhddrgpvLESIVSRT 1151
Cdd:TIGR01587 72 mGDSEEFEHLFPLYIHSNDKlflDPITVCTIDQVLKSVFGEFGHYEFTLASIanslLIFDEVHFY-------DEYTLALI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1152 IRTMEQTQEL-VRLVGLSATLPNYadvaaFLRVNPKTGLFFFDGAFRPCPLKQ---QFIGVTEKKAIKRFQVMNDvcyek 1227
Cdd:TIGR01587 145 LAVLEVLKDNdVPILLMSATLPKF-----LKEYAEKIGYVEFNEPLDLKEERRfenHRFILIESDKVGEISSLER----- 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1945600751 1228 VMEQLDqrEENQVLVFVHSRKETAKTAKTLRDMALEKDTI---GHFLKQDSASRE 1279
Cdd:TIGR01587 215 LLEFIK--KGGSIAIIVNTVDRAQEFYQQLKEKAPEEEIIlyhSRFTEKDRAKKE 267
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
1864-2013 |
4.83e-04 |
|
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: 43.79 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1864 NVFIGAPTGSGKTVCA-----EFALLRLWSSSEEARAVYVAPFQEIVDQRAADWKQ--KFKGKEIVTLTG---ETSADLK 1933
Cdd:cd18034 18 NTIVVLPTGSGKTLIAvmlikEMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRShtDLKVGEYSGEMGvdkWTKERWK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1934 -LLERGDVICCTPAqwdvVSRRWKQRKNVQ--NVNLFIADELHLIGGDiGPtYEVIVSRMRYIASQTNKSiRIVALSTSL 2010
Cdd:cd18034 98 eELEKYDVLVMTAQ----ILLDALRHGFLSlsDINLLIFDECHHATGD-HP-YARIMKEFYHLEGRTSRP-RILGLTASP 170
|
...
gi 1945600751 2011 ANA 2013
Cdd:cd18034 171 VNG 173
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
1863-1924 |
5.14e-04 |
|
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: 43.43 E-value: 5.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1945600751 1863 DNVFIGAPTGSGKTvcaEFAL---LRLWSSSEEARAVYVAPFQEIVDQ---RAADWKQKFKGKEIVTL 1924
Cdd:cd17930 2 GLVILEAPTGSGKT---EAALlwaLKLAARGGKRRIIYALPTRATINQmyeRIREILGRLDDEDKVLL 66
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
980-1173 |
5.95e-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: 43.91 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 980 KDLPQ----WAQEAFP----------GAESLNRVQSRLYPtAFGSDENVLLCAPTGAGKTNVAMLTVLHEINKNR--DPQ 1043
Cdd:cd17953 5 KDCPKpiqkWSQCGLSekvldlikklGYEKPTPIQAQALP-AIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRpvKPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1044 TGHIDLdsfkivYIAPMKALVQEMVGNFSRRLRPYGISVAELTGDRQLtKQQIAE----TQIIVTTPEKW-DVITrkATD 1118
Cdd:cd17953 84 EGPIGL------IMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGI-SEQIAElkrgAEIVVCTPGRMiDILT--ANN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1945600751 1119 RSYTALVRL--IIIDEIHLLHD-DRGPVLESIVSrTIRTMEQTqelvrlVGLSATLPN 1173
Cdd:cd17953 155 GRVTNLRRVtyVVLDEADRMFDmGFEPQIMKIVN-NIRPDRQT------VLFSATFPR 205
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
1869-1973 |
9.43e-04 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 42.16 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1869 APTGSGKTVCAEFALLRLWSSSEEARAVYVAPFQEIVDQRAADWKQKFKGKEIVTLTGETSADLKllerGDVICCTpaqW 1948
Cdd:cd18032 27 MATGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLEQAERSFKEVLPDGSFGNLKGGKKKPDD----ARVVFAT---V 99
|
90 100
....*....|....*....|....*.
gi 1945600751 1949 DVVSRRWKQRK-NVQNVNLFIADELH 1973
Cdd:cd18032 100 QTLNKRKRLEKfPPDYFDLIIIDEAH 125
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1012-1183 |
1.15e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.98 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1012 ENVLLCAPTGAGKTnvamlTVLHEInknrdpqTGHIDLDSFKIVYIAPMKALVQEMvgnFSRRLRPYGISVAELTGDRQL 1091
Cdd:smart00382 3 EVILIVGPPGSGKT-----TLARAL-------ARELGPPGGGVIYIDGEDILEEVL---DQLLLIIVGGKKASGSGELRL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1092 tkqqiaetqiivttpekwdvitRKATDRSYTALVRLIIIDEIHLLHDDRGPVLE-SIVSRTIRTMEQTQELVRLVGLSAT 1170
Cdd:smart00382 68 ----------------------RLALALARKLKPDVLILDEITSLLDAEQEALLlLLEELRLLLLLKSEKNLTVILTTND 125
|
170
....*....|...
gi 1945600751 1171 LPNYADVAAFLRV 1183
Cdd:smart00382 126 EKDLGPALLRRRF 138
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
1015-1171 |
1.27e-03 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 41.52 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1015 LLCAPTGAGKTNVAMLTVLheinknrdpqtghiDLDSFKIVYIAPMKALVQEMVGNFsRRLRPyGISVAELTGDRqltKQ 1094
Cdd:cd17926 22 ILVLPTGSGKTLTALALIA--------------YLKELRTLIVVPTDALLDQWKERF-EDFLG-DSSIGLIGGGK---KK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1945600751 1095 QIAETQIIVTTPEKwdVITRKATDRSYTALVRLIIIDEIHLLHddrGPVLESIVSRTIRTmeqtqelvRLVGLSATL 1171
Cdd:cd17926 83 DFDDANVVVATYQS--LSNLAEEEKDLFDQFGLLIVDEAHHLP---AKTFSEILKELNAK--------YRLGLTATP 146
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
1851-2007 |
2.31e-03 |
|
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: 41.54 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1851 QTQVFNTLYTtndNVFIGAPTGSGKTVCAEFALLRLWSSSEEARAVYVAPFQEIVDQRaADWKQKFKG---KEIVTLTGE 1927
Cdd:cd18033 8 FTIVQKALFQ---NTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQ-IEACYKITGipsSQTAELTGS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1928 TSAD--LKLLERGDVICCTPAQwdVVSRRWKQRKNVQNVNLFIADELHLIGGDIgpTYEVIVSR-MRYiasqtNKSIRIV 2004
Cdd:cd18033 84 VPPTkrAELWASKRVFFLTPQT--LENDLKEGDCDPKSIVCLVIDEAHRATGNY--AYCQVVRElMRY-----NSHFRIL 154
|
...
gi 1945600751 2005 ALS 2007
Cdd:cd18033 155 ALT 157
|
|
| DEXHc_RLR-2 |
cd18074 |
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma ... |
1012-1153 |
3.21e-03 |
|
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma differentiation-associated protein 5 or Mda5 and IFIH1) is a viral double-stranded RNA (dsRNA) receptor that shares sequence similarity and signaling pathways with RIG-I, yet plays essential functions in antiviral immunity through distinct specificity for viral RNA. RLR-2 recognizes the internal duplex structure, whereas RIG-I recognizes the terminus of dsRNA. RLR-2 uses direct protein-protein contacts to stack along dsRNA in a head-to-tail arrangement. The signaling domain (tandem CARD), which decorates the outside of the core RLR-2 filament, also has an intrinsic propensity to oligomerize into an elongated structure that activates the signaling adaptor, MAVS. RLR-2 uses long dsRNA as a signaling platform to cooperatively assemble the core filament, which in turn promotes stochastic assembly of the tandem CARD oligomers for signaling. LGP2 appears to positively and negatively regulate RLR-2 and RIG-I signaling, respectively. RLR-2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350832 [Multi-domain] Cd Length: 216 Bit Score: 41.38 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1012 ENVLLCAPTGAGKTNVAM-LTVLHEINKNRDPQTGHIdldsfkIVYIAPMKALVQEMVGNFSRRLRPYgISVAELTGDRQ 1090
Cdd:cd18074 18 KNIIICLPTGSGKTRVAVyITKDHLDKKRKASEPGKV------IVLVNKVPLVEQHYRKEFNPFLKHW-YQVIGLSGDSQ 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1091 LT---KQQIAETQIIVTTPEKWDVITRKATDRSYTAL----VRLIIIDEIHllHDDRGPVLESIVSRTIR 1153
Cdd:cd18074 91 LKisfPEVVKRYDVIICTAQILENSLLNATEEEDEGVqlsdFSLIIIDECH--HTQKEAVYNNIMRRYLK 158
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
1319-1391 |
3.77e-03 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350192 [Multi-domain] Cd Length: 135 Bit Score: 39.85 E-value: 3.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1945600751 1319 LFADGH--VKVLCSTATLAWGVNLPAHAVIIkgTQIYSPEKGRWVELSPQDVLQMLGRAGRpqFDTYGEGIIITA 1391
Cdd:cd18805 63 LFNDPEsgYDVLVASDAIGMGLNLNIRRVIF--SSLSKFDGNEMRPLSPSEVKQIAGRAGR--FGSHFPEGEVTT 133
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
1864-1995 |
6.16e-03 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1864 NVFIGAPTGSGKTvcAEFALLRLwsssEEARAVYVAPFQEIVDQ---RAADWKQKFKGKEIVTLT---GE-TSADLKLLE 1936
Cdd:cd17938 38 DVLMAAETGSGKT--GAFCLPVL----QIVVALILEPSRELAEQtynCIENFKKYLDNPKLRVALligGVkAREQLKRLE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1945600751 1937 RG-DVICCTPAQ-WDVVSrrwKQRKNVQNVNLFIADEL-HLIGGDIGPTYEVIVSRMRYIAS 1995
Cdd:cd17938 112 SGvDIVVGTPGRlEDLIK---TGKLDLSSVRFFVLDEAdRLLSQGNLETINRIYNRIPKITS 170
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
988-1151 |
6.31e-03 |
|
orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274354 [Multi-domain] Cd Length: 365 Bit Score: 41.46 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 988 EAFPGAES-LNRVQSRLYPTAFGSD-ENVLLCAPTGAGKTNVAMLTV--LHEINKNRDpqtghidlDSFKIVYI--APMK 1061
Cdd:TIGR02928 15 DRIVHRDEqIEELAKALRPILRGSRpSNVFIYGKTGTGKTAVTKYVMkeLEEAAEDRD--------VRVVTVYVncQILD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1062 ALVQEMVgNFSRRLRPYGISVAElTGdrqltkqqiaetqiiVTTPEKWDVITrKATDRSYTALVrlIIIDEIHLLHDDRG 1141
Cdd:TIGR02928 87 TLYQVLV-ELANQLRGSGEEVPT-TG---------------LSTSEVFRRLY-KELNERGDSLI--IVLDEIDYLVGDDD 146
|
170
....*....|
gi 1945600751 1142 PVLESIvSRT 1151
Cdd:TIGR02928 147 DLLYQL-SRA 155
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
1015-1134 |
6.39e-03 |
|
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: 40.25 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1015 LLCAPTGAGKTNVAMLTVLHEInknrdpqtghidLDSFKIVYIAPMKALVQEMVGNFSRRLRPYGISVAELTG-----DR 1089
Cdd:cd17991 40 LICGDVGFGKTEVAMRAAFKAV------------LSGKQVAVLVPTTLLAQQHYETFKERFANFPVNVELLSRfttaaEQ 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1945600751 1090 QLTKQQIAE--TQIIVTTpekwdviTRKATDRSYTALVRLIIIDEIH 1134
Cdd:cd17991 108 REILEGLKEgkVDIVIGT-------HRLLSKDVEFKNLGLLIIDEEQ 147
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
1006-1171 |
6.46e-03 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438711 [Multi-domain] Cd Length: 174 Bit Score: 40.01 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1006 TAFGSDENVLLCAPTGAGKTNVAMLTVLHeinknrdpqtgHIDLDSFKIVYIAP-----------MKALVQEMVGNF-SR 1073
Cdd:cd17990 12 AALDAGGQVVLEAPPGAGKTTRVPLALLA-----------ELWIAGGKIIVLEPrrvaaraaarrLATLLGEAPGETvGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1074 RLRpygisvaeltGDRQLTKqqiaETQIIVTTPekwDVITRKATDRSYTALVRLIIIDEIH--LLHDDRGPVLESIVSRT 1151
Cdd:cd17990 81 RVR----------GESRVGR----RTRVEVVTE---GVLLRRLQRDPELSGVGAVILDEFHerSLDADLALALLLEVQQL 143
|
170 180
....*....|....*....|
gi 1945600751 1152 IRtmeqtQELvRLVGLSATL 1171
Cdd:cd17990 144 LR-----DDL-RLLAMSATL 157
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
1000-1106 |
9.13e-03 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 40.31 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1000 QSRLYPTAFGSDenVLLCAPTGAGKTNVAMLTVLHEINKNRDPQTghidldsfKIVYIAPMKALVQEMVGNFSRRLRPYG 1079
Cdd:cd17956 27 SSKSTPPYRPGD--LCVSAPTGSGKTLAYVLPIVQALSKRVVPRL--------RALIVVPTKELVQQVYKVFESLCKGTG 96
|
90 100 110
....*....|....*....|....*....|....*...
gi 1945600751 1080 ISVAELTGDRQLTKQQIA-----------ETQIIVTTP 1106
Cdd:cd17956 97 LKVVSLSGQKSFKKEQKLllvdtsgrylsRVDILVATP 134
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
1849-1945 |
9.79e-03 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 39.88 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945600751 1849 PIQTQVFNTLYTTNDnvFIG-APTGSGKTvcAEFAL-----LRLWSSSEEARAVYVAPFQEIVDQRAADWKQ--KFKGKE 1920
Cdd:cd17957 15 PIQMQAIPILLHGRD--LLAcAPTGSGKT--LAFLIpilqkLGKPRKKKGLRALILAPTRELASQIYRELLKlsKGTGLR 90
|
90 100
....*....|....*....|....*....
gi 1945600751 1921 IVTLTGETSA----DLKLLERGDVICCTP 1945
Cdd:cd17957 91 IVLLSKSLEAkakdGPKSITKYDILVSTP 119
|
|
| |
