|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1229-1417 |
1.16e-133 |
|
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: 415.23 E-value: 1.16e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1229 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLGKKVI 1308
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1309 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKPVR 1388
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*....
gi 1720362714 1389 IVGLSTALANARDLADWLNIKQMGLFNFR 1417
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
379-576 |
1.62e-125 |
|
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: 392.56 E-value: 1.62e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 379 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQHFHQ-GVIKKNEFKIVYVAPMKALAAEMTNYFSKRL 457
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 458 EPLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDVALSQIVKLLILDEVHLLHEDRGPVLESIVARTLRQ 537
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720362714 538 VESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFYFD 576
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
881-1189 |
7.93e-125 |
|
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.
Pssm-ID: 460740 Cd Length: 307 Bit Score: 395.42 E-value: 7.93e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 881 STDLGRTASHFYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDALLNNfCELSAPGGVENSYGKI 960
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEK-VPIPVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 961 NILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSVLPPHI 1040
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1041 LTRLEEKNLTV--DKLKDMRKDEIGHILHHVNIGLKVKQCVHQIPSVTMEASIQPITRTVLRVSLNIHPDFSWNDQVHGT 1118
Cdd:pfam02889 160 IKKLEKKGVESvrDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720362714 1119 VgEPWWIWVEDPTNDHIYHSEYFLALKKQVINkeAQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIIN 1189
Cdd:pfam02889 240 S-EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
878-1191 |
2.16e-111 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 357.34 E-value: 2.16e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 878 YFSSTDLGRTASHFYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDALLNNFCELSAPGGVENSY 957
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 958 GKINILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSVLP 1037
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1038 PHILTRLEEKN-LTVDKLKDMRKDEIGHILHHVN-IGLKVKQCVHQIPSVTMEASIQPITRTVLRVSLNIHPDFSWNDQV 1115
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLGLLDaEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720362714 1116 HGTVgEPWWIWVEDPTNDHIYHSEYFLALKKQVINKeaQLLVFTIPIFEPLPsQYYIRAVSDRWLGAEAVCIINFQ 1191
Cdd:smart00611 241 HGKQ-EGWWLVIGDSDGNELLHIERFSLNKKNVSEE--VKLDFTAPATEGNY-QYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1712-2078 |
3.60e-96 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 313.43 E-value: 3.60e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1712 TIEPLTCGRIASYYYLKHKTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHTNNELAKCLPIELNPHSFDSPH 1791
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1792 TKAHLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAASQGWLVTVLNITHLIQMVIQGRWLKDSSLLTIPNIE 1871
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1872 QHHLHLFRKWKppvksshakcRTSIECLPELIHacEGKDHVFSSMVekelqpAKTKQAWNFLSRLPVINVGISVKGSwDD 1951
Cdd:smart00611 161 EEILKRLEKKK----------VLSLEDLLELED--EERGELLGLLD------AEGERVYKVLSRLPKLNIEISLEPI-TR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1952 LVEGHNELSISTLTADKRdenkwiklhadqeyvlqvslqrvhfglpkgKHEnhavtprfpklKDEGWFLILGEVDKRELM 2031
Cdd:smart00611 222 TVLGVEVTLTVDLTWDDE------------------------------IHG-----------KQEGWWLVIGDSDGNELL 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720362714 2032 AVKRVGFVRTHHD--ASISFFTPETPGRYIFTLYLMSDCYLGLDQQYDI 2078
Cdd:smart00611 261 HIERFSLNKKNVSeeVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPL 309
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1230-1752 |
1.23e-95 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 320.30 E-value: 1.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1230 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKIRIEEkLGKKVIE 1309
Cdd:COG1204 23 LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEE-LGIKVGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1310 LTGDVTPDMKSIAKADLIVTTPEKWDGVSRswQNRSYVQQVNILIIDEIHLLG-EERGPVLEVIVSRtnfiSSHTEKPVR 1388
Cdd:COG1204 100 STGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTLEVLLAR----LRRLNPEAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1389 IVGLSTALANARDLADWLNIKqmglfNFRPSVRPVPLE--VHIQG---FPGQHYCPRmasmnKPAFQAIRSHSPA-KPVL 1462
Cdd:COG1204 174 IVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSK-----DPTLALALDLLEEgGQVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1463 IFVSSRRQTRLTALELIAFLA---TEEDPKQWLNMDEQEMDniIGTVRDSNLKLT--LAFGIGMHHAGLHERDRKTVEEL 1537
Cdd:COG1204 244 VFVSSRRDAESLAKKLADELKrrlTPEEREELEELAEELLE--VSEETHTNEKLAdcLEKGVAFHHAGLPSELRRLVEDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1538 FVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGktrryVDFPITDVLQMMGRAGRPQFDDQGKAVILVHDIK---KD 1614
Cdd:COG1204 322 FREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDeadEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1615 FYKKFLYEPFPVESSLLGVLSD--HLNAEIAGGTITSKQDAMDYITWTYFFRRlimnPSYYSLGDVSQDSINKflshLIG 1692
Cdd:COG1204 397 FERYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQ----YDKGDLEEVVDDALEF----LLE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720362714 1693 QSLVElelshcievgEDNRTIEPLTCGRIASYYYLKHKTVKMFKDRLK---PECSTEELLSIL 1752
Cdd:COG1204 469 NGFIE----------EDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadEEFTDLGLLHLI 521
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
363-918 |
1.87e-95 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 319.92 E-value: 1.87e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 363 IKDLDEVG---QLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQHFhqgvikknefKIVYV 439
Cdd:COG1204 3 VAELPLEKvieFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 440 APMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGdvALSQIvKLLILDEVHLL 519
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDV-DLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 520 H-EDRGPVLESIVARtLRQVESTqsmIRILGLSATLPNYLDVATFLHVNPyiglfyFDGRFRPVPLgqtFLGIKSTNKmq 598
Cdd:COG1204 150 DdESRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGV-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 599 qlNNMDEVCYES-------VLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNSgqISCFLPTEGPEYGHALKQVQKSR- 670
Cdd:COG1204 215 --LRFDDGSRRSkdptlalALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRR--LTPEEREELEELAEELLEVSEETh 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 671 -NKQVRELFSDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTqiyaaKRGSFVDLGILDV 749
Cdd:COG1204 291 tNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-----KRGGMVPIPVLEF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 750 MQIFGRAGRPQFDKFGEGIIIT-THDKLSH--YLSLLTQQNPIESQFLE--SLADNLNAEIALGTVTNVEEAVRWMSYTY 824
Cdd:COG1204 366 KQMAGRAGRPGYDPYGEAILVAkSSDEADElfERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTF 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 825 LYVRMRANPLaygishkayqidptlrkhrEQLLIEVGQKLDKAKMIrfEERTGYFSSTDLGRTASHFYIKYNTIETFNEL 904
Cdd:COG1204 446 YAYQYDKGDL-------------------EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAELVDG 504
|
570
....*....|....
gi 1720362714 905 FDAHKTEGDIFAIV 918
Cdd:COG1204 505 LRKADEEFTDLGLL 518
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1715-2078 |
4.99e-72 |
|
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: 244.03 E-value: 4.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1715 PLTCGRIASYYYLKHKTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHTNNELAKCLPIELNPhSFDSPHTKA 1794
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKG-DIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1795 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAASQGWLVTVLNITHLIQMVIQGRWLKDSSLLTIPNIEqhh 1874
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIP--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1875 lhlfrkwkppvksshakcrtsieclPELIHACEGKDHVF-----SSMVEKELQ-----PAKTKQAWNFLSRLPVINVgis 1944
Cdd:pfam02889 157 -------------------------PELIKKLEKKGVESvrdilELDDAEELGelirnPKMGKDIAQFVNRFPKIEI--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1945 vkgswddlveghnELSISTLTADkrdenkwiklhadqeyVLQVSLQrvhfglpkgkhenhaVTPRFPKLKD-----EGWF 2019
Cdd:pfam02889 209 -------------EAEVQPITRS----------------VLRVEVT---------------ITPDFPWDKRvhgksEGFW 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720362714 2020 LILGEVDKRELMAVKRVGFVR--THHDASISFFTP-ETPGRYIFTLYLMSDCYLGLDQQYDI 2078
Cdd:pfam02889 245 LVVGDSDGNEILHIERFTLTKrtLAGEHKLEFTVPpSDPGPPQLFVRLISDSWLGADQEVPI 306
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1421-1609 |
1.50e-66 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 222.04 E-value: 1.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1421 RPVPLEVHIQGFPGQHYCPRMASMNK-----PAFQAIRSHSPAKPVLIFVSSRRQTRLTALELIaflateedpkqwlnmd 1495
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1496 eqemdniigtvrdsnlkltlafGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKT 1575
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 1720362714 1576 RRYvdFPITDVLQMMGRAGRPQFDDQGKAVILVH 1609
Cdd:cd18795 123 YRE--LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1247-1767 |
1.12e-59 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 220.46 E-value: 1.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFrvfNKYPTS--KAVYIAPLKALVRER---MDDWkirieEKLGKKVIELTGDVTPDMKSI 1321
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMV---NKLLREggKAVYLVPLKALAEEKyreFKDW-----EKLGLRVAMTTGDYDSTDEWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1322 AKADLIVTTPEKWDGVSRswQNRSYVQQVNILIIDEIHLLGE-ERGPVLEVIVSrtnfissHTEKPVRIVGLSTALANAR 1400
Cdd:PRK00254 113 GKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSyDRGATLEMILT-------HMLGRAQILGLSATVGNAE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1401 DLADWLNIKQMglfnfRPSVRPVPLE--VHIQGF------PGQHYcprMASMNKPAFQAIRShspAKPVLIFVSSRRQTR 1472
Cdd:PRK00254 184 ELAEWLNAELV-----VSDWRPVKLRkgVFYQGFlfwedgKIERF---PNSWESLVYDAVKK---GKGALVFVNTRRSAE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1473 LTALEL---IAFLATEEDPKQWLNMDEQEMDNiigtvrDSNLKLTLAF--GIGMHHAGLHERDRKTVEELFVNCKVQVLI 1547
Cdd:PRK00254 253 KEALELakkIKRFLTKPELRALKELADSLEEN------PTNEKLKKALrgGVAFHHAGLGRTERVLIEDAFREGLIKVIT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1548 ATSTLAWGVNFPAHLVIIKGTEYYDGKTrrYVDFPITDVLQMMGRAGRPQFDDQGKAVILVH-DIKKDFYKKF------- 1619
Cdd:PRK00254 327 ATPTLSAGINLPAFRVIIRDTKRYSNFG--WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERYifgkpek 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1620 LYEPFPVESSLLGvlsdHLNAEIAGGTITSKQDAMDYITWTYFFRRlimNPSYYSLgdvsQDSINKFLSHLIGQSLVELE 1699
Cdd:PRK00254 405 LFSMLSNESAFRS----QVLALITNFGVSNFKELVNFLERTFYAHQ---RKDLYSL----EEKAKEIVYFLLENEFIDID 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720362714 1700 LshcievgEDNrtIEPLTCGRIASYYYLKHKTVKMFKDRLkPECSTEE----LLSILSDAEEYTDLPVRHNE 1767
Cdd:PRK00254 474 L-------EDR--FIPLPLGIRTSQLYIDPLTAKKFKDAF-PKIEKNPnplgIFQLIASTPDMTPLNYSRKE 535
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
396-937 |
4.74e-57 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 212.75 E-value: 4.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 396 ENMLICAPTGAGKTNIAMLTILHEIRQhfhQGvikkneFKIVYVAPMKALAAEMTNYFsKRLEPLGIVVKELTGDMQlSK 475
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKLLR---EG------GKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYD-ST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 476 SEIL-RTQMLVTTPEKWDVVTRKSVgdvalSQI--VKLLILDEVHLL-HEDRGPVLESIVARTLRQVEstqsmirILGLS 551
Cdd:PRK00254 109 DEWLgKYDIIIATAEKFDSLLRHGS-----SWIkdVKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ-------ILGLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 552 ATLPNYLDVATFLHVNpyigLFYFDgrFRPVPL-------GQTFLGIKSTNKMQqlNNMDEVCYESVlkqvKAGHQVMVF 624
Cdd:PRK00254 177 ATVGNAEELAEWLNAE----LVVSD--WRPVKLrkgvfyqGFLFWEDGKIERFP--NSWESLVYDAV----KKGKGALVF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 625 VHARNATVRTAMSLieraknSGQISCFLPTegPEYgHALKQVQKS-----RNKQVRELFSDGFSIHHAGMLRQDRNLVEN 699
Cdd:PRK00254 245 VNTRRSAEKEALEL------AKKIKRFLTK--PEL-RALKELADSleenpTNEKLKKALRGGVAFHHAGLGRTERVLIED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 700 LFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTQIYAakRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDK---- 775
Cdd:PRK00254 316 AFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpskl 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 776 LSHYL--------SLLTQQNPIESQFLesladnlnAEIALGTVTNVEEAVRWMSYTYlYVRMRANPlaYGISHKAYQIDP 847
Cdd:PRK00254 394 MERYIfgkpeklfSMLSNESAFRSQVL--------ALITNFGVSNFKELVNFLERTF-YAHQRKDL--YSLEEKAKEIVY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 848 TLrkhREQLLIEvgqkldkakmIRFEERtgyFSSTDLGRTASHFYIKYNTIETFNELFDahKTEGD-----IFAIVSKAE 922
Cdd:PRK00254 463 FL---LENEFID----------IDLEDR---FIPLPLGIRTSQLYIDPLTAKKFKDAFP--KIEKNpnplgIFQLIASTP 524
|
570
....*....|....*
gi 1720362714 923 EFDQIKVREEEIEEL 937
Cdd:PRK00254 525 DMTPLNYSRKEMEDL 539
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
580-772 |
2.45e-52 |
|
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: 181.21 E-value: 2.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 580 RPVPLGQTFLGIKST----NKMQQLNNMDEVCYESVLKQVKAGHQVMVFVHARNATVRTAMSLIeraknsgqiscflpte 655
Cdd:cd18795 1 RPVPLEEYVLGFNGLgiklRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 656 gpeyghalkqvqksrnkqvrelfsdGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTQIYA 735
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720362714 736 AKRgsFVDLGILDVMQIFGRAGRPQFDKFGEGIIITT 772
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
381-559 |
1.23e-33 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 128.13 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 381 NRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTILHEIRQhfhqgviKKNEFKIVYVAPMKALAAEMTNYFSKRLEPL 460
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK-------LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 461 GIVVKELTGDMQLSK--SEILRTQMLVTTPEKWDVVTRKSvgdVALSQiVKLLILDEVHLLHE-DRGPVLESIVARtlrq 537
Cdd:pfam00270 73 GLKVASLLGGDSRKEqlEKLKGPDILVGTPGRLLDLLQER---KLLKN-LKLLVLDEAHRLLDmGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|..
gi 1720362714 538 vesTQSMIRILGLSATLPNYLD 559
Cdd:pfam00270 145 ---LPKKRQILLLSATLPRNLE 163
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1231-1402 |
2.93e-32 |
|
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: 124.28 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1231 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFN-KYPTSKAVYIAPLKALVRERMDDWKiRIEEKLGKKVIE 1309
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDkLDNGPQALVLAPTRELAEQIYEELK-KLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1310 LTGDVTP--DMKSIAKADLIVTTPEKWDGVsrsWQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNfisshteKP 1386
Cdd:pfam00270 79 LLGGDSRkeQLEKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRRLP-------KK 148
|
170
....*....|....*..
gi 1720362714 1387 VRIVGLS-TALANARDL 1402
Cdd:pfam00270 149 RQILLLSaTLPRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
372-583 |
1.58e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 109.12 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 372 LAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQHFHQgvikknefKIVYVAPMKALAAEMTN 451
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGG--------RVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 452 YFSKRLEPLGIVVKELTGD----MQLSKSEILRTQMLVTTPEKWDVVTRKsvGDVALSQiVKLLILDEVH-LLHEDRGPV 526
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRLLDLLEN--DKLSLSN-VDLVILDEAHrLLDGGFGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362714 527 LESIVARTLRqvestqsMIRILGLSATLPNYLDVATFLHVNpyiGLFYFDGRFRPVP 583
Cdd:smart00487 150 LEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1232-1608 |
9.70e-26 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 115.76 E-value: 9.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1232 PVQT-QIFHTLYHTDcNVLLGAPTGSGKTVAAELA-IFRVFNKypTSKAVYIAPLKALVRERMDDWKIRIEEKLgkKVIE 1309
Cdd:COG1202 212 PVQSlAVENGLLEGK-DQLVVSATATGKTLIGELAgIKNALEG--KGKMLFLVPLVALANQKYEDFKDRYGDGL--DVSI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1310 LTGDV---TPDMKSIAKADLIVTTPEKWDGVSRSwqnRSYVQQVNILIIDEIHLLGE-ERGPVLEVIVSRTNFISSHTEk 1385
Cdd:COG1202 287 RVGASrirDDGTRFDPNADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEVHMLEDpERGHRLDGLIARLKYYCPGAQ- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1386 pvrIVGLSTALANARDLADWLNIKQMgLFNfrpsVRPVPLEVHIQGFPGQHYCPRMASMNKPAFQAIRSHSPAKPVLIFV 1465
Cdd:COG1202 363 ---WIYLSATVGNPEELAKKLGAKLV-EYE----ERPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1466 SSRRQTRltaleliaflateedpkqwlnmdeqemdniigtvrdsnlKLTLAFGIGM--HHAGLHERDRKTVEELFVNCKV 1543
Cdd:COG1202 435 NSRRRCH---------------------------------------EIARALGYKAapYHAGLDYGERKKVERRFADQEL 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720362714 1544 QVLIATSTLAWGVNFPAHLVIIK----GTEYydgktrryvdFPITDVLQMMGRAGRPQFDDQGKAVILV 1608
Cdd:COG1202 476 AAVVTTAALAAGVDFPASQVIFDslamGIEW----------LSVQEFHQMLGRAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1225-1424 |
5.23e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 104.50 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1225 YNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLG 1304
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1305 KKVIELTGDVT-PDMKSIAK--ADLIVTTPEKWDGVSRswQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNfis 1380
Cdd:smart00487 84 KVVGLYGGDSKrEQLRKLESgkTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720362714 1381 shteKPVRIVGLS-TALANARDLADWLNIkqmGLFNFRPSVRPVP 1424
Cdd:smart00487 159 ----KNVQLLLLSaTPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
1249-1564 |
2.40e-16 |
|
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: 85.68 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1249 LLGAPTGSGKTVAAELAIFRVFNKYPTSK-----AVYIAPLKALVR----------ERMdDWKIRIEEKlgkkvielTGD 1313
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKekglhTLYITPLRALAVdiarnlqapiEEL-GLPIRVETR--------TGD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1314 VTPDMKSIAKA---DLIVTTPEkwdgvsrSWQ-------NRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNFISSH 1382
Cdd:TIGR04121 103 TSSSERARQRKkppDILLTTPE-------SLAlllsypdAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1383 tekpVRIVGLSTALANARDLADWLnikqMGLFNFRPSV------RPVPLEV----HIQGFP-GQHYCPRMASmnkPAFQA 1451
Cdd:TIGR04121 176 ----LRRWGLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISllpeSEERFPwAGHLGLRALP---EVYAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1452 IRSHspaKPVLIFVSSRRQTRLTALELIAFLAteedpkqwlnmdeqemdniigtvrDSNLKltlafgIGMHHAGLHERDR 1531
Cdd:TIGR04121 245 IDQA---RTTLVFTNTRSQAELWFQALWEANP------------------------EFALP------IALHHGSLDREQR 291
|
330 340 350
....*....|....*....|....*....|....
gi 1720362714 1532 KTVEELFVNCKVQVLIATSTLAWGVNF-PAHLVI 1564
Cdd:TIGR04121 292 RWVEAAMAAGRLRAVVCTSSLDLGVDFgPVDLVI 325
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
391-759 |
3.22e-15 |
|
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: 81.83 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 391 AYNTNENMLICAPTGAGKTNIAMLTILHEIrqhFHQGVIKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLG--IVVKELT 468
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSLIDL---AGPEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGlpIRVETRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 469 GDMQLSKSEILRTQM---LVTTPEKWDVVTrkSVGDVA-LSQIVKLLILDEVH-LLHEDRGPVLESIVARtLRQvesTQS 543
Cdd:TIGR04121 101 GDTSSSERARQRKKPpdiLLTTPESLALLL--SYPDAArLFKDLRCVVVDEWHeLAGSKRGDQLELALAR-LRR---LAP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 544 MIRILGLSATLPNyLDVA--TFLHVNPYIGLFYFDGRFRPVPL-------GQTF-----LGIKStnkmqqlnnmdevcYE 609
Cdd:TIGR04121 175 GLRRWGLSATIGN-LEEArrVLLGVGGAPAVLVRGKLPKAIEVisllpesEERFpwaghLGLRA--------------LP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 610 SVLKQVKAGHQVMVFVHARNATVRTAMSLIEraknsgqiscflptegpeyghalkqvqksrnkqVRELFSDGFSIHHAGM 689
Cdd:TIGR04121 240 EVYAEIDQARTTLVFTNTRSQAELWFQALWE---------------------------------ANPEFALPIALHHGSL 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720362714 690 LRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtQIYAAKrgsfvdlGILDVMQIFGRAG-RP 759
Cdd:TIGR04121 287 DREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSPK-------GVARLLQRAGRSNhRP 347
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1517-1596 |
8.45e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 71.09 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1517 FGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryVDFPITDVLQMMGRAGR 1595
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVII-----YD------LPWSPASYIQRIGRAGR 80
|
.
gi 1720362714 1596 P 1596
Cdd:smart00490 81 A 81
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
681-759 |
1.62e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.93 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 681 GFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVVIKGtqiyaakrgsfVDLGILDVMQIFGRAGRP 759
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASYIQRIGRAGRA 81
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
395-582 |
3.44e-10 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 65.29 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNIAMLTILHEIrqhFHQGVIKKNEFKI--VYVAPMKALAAEMtnyfsKR--LEPL-GI--VVKEL 467
Cdd:PRK13767 47 GKNVLISSPTGSGKTLAAFLAIIDEL---FRLGREGELEDKVycLYVSPLRALNNDI-----HRnlEEPLtEIreIAKER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 468 ------------TGDM-QLSKSEILRT--QMLVTTPEKWDVVT-----RKSVGDvalsqiVKLLILDEVHLLHED-RGPV 526
Cdd:PRK13767 119 geelpeirvairTGDTsSYEKQKMLKKppHILITTPESLAILLnspkfREKLRT------VKWVIVDEIHSLAENkRGVH 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720362714 527 LesivARTLRQVES--TQSMIRIlGLSATLPNYLDVATFLhvnpyiGLFYFDGRFRPV 582
Cdd:PRK13767 193 L----SLSLERLEElaGGEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDC 239
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1511-1595 |
7.64e-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: 57.99 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1511 LKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryVDFPITDVLQM 1589
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YD------LPWNPASYIQR 101
|
....*.
gi 1720362714 1590 MGRAGR 1595
Cdd:pfam00271 102 IGRAGR 107
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1227-1393 |
1.43e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 63.37 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1227 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAI----FRVFNK-------YptskAVYIAPLKAL---VRERM 1292
Cdd:PRK13767 30 FGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREgeledkvY----CLYVSPLRALnndIHRNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1293 DDWKIRIEEKLGKKVIEL--------TGDVTPDMKS--------IakadLIvTTPEKWDGVSRSWQNRSYVQQVNILIID 1356
Cdd:PRK13767 105 EEPLTEIREIAKERGEELpeirvairTGDTSSYEKQkmlkkpphI----LI-TTPESLAILLNSPKFREKLRTVKWVIVD 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720362714 1357 EIHLLGE-ERGPVLEVIVSRTNFISSHteKPVRIvGLS 1393
Cdd:PRK13767 180 EIHSLAEnKRGVHLSLSLERLEELAGG--EFVRI-GLS 214
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
395-517 |
3.79e-08 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 58.59 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNIAMLTILHeirqhfhqgVIKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLS 474
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE---------RLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1720362714 475 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivkLLILDEVH 517
Cdd:COG1111 88 KRKELweKARIIVATPQviENDLIAgRIDLDDVS------LLIFDEAH 129
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
677-758 |
9.32e-07 |
|
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: 49.13 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 677 LFSDGFSI--HHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtqIYAAkrgsfvDLGILDVMQIFG 754
Cdd:pfam00271 34 LEKEGIKVarLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVI----NYDL------PWNPASYIQRIG 103
|
....
gi 1720362714 755 RAGR 758
Cdd:pfam00271 104 RAGR 107
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1229-1417 |
1.16e-133 |
|
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: 415.23 E-value: 1.16e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1229 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLGKKVI 1308
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1309 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKPVR 1388
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*....
gi 1720362714 1389 IVGLSTALANARDLADWLNIKQMGLFNFR 1417
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
379-576 |
1.62e-125 |
|
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: 392.56 E-value: 1.62e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 379 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQHFHQ-GVIKKNEFKIVYVAPMKALAAEMTNYFSKRL 457
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 458 EPLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDVALSQIVKLLILDEVHLLHEDRGPVLESIVARTLRQ 537
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720362714 538 VESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFYFD 576
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
881-1189 |
7.93e-125 |
|
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.
Pssm-ID: 460740 Cd Length: 307 Bit Score: 395.42 E-value: 7.93e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 881 STDLGRTASHFYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDALLNNfCELSAPGGVENSYGKI 960
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEK-VPIPVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 961 NILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSVLPPHI 1040
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1041 LTRLEEKNLTV--DKLKDMRKDEIGHILHHVNIGLKVKQCVHQIPSVTMEASIQPITRTVLRVSLNIHPDFSWNDQVHGT 1118
Cdd:pfam02889 160 IKKLEKKGVESvrDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720362714 1119 VgEPWWIWVEDPTNDHIYHSEYFLALKKQVINkeAQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIIN 1189
Cdd:pfam02889 240 S-EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
363-576 |
4.60e-113 |
|
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: 357.84 E-value: 4.60e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 363 IKDLDEVGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQHFHQ-GVIKKNEFKIVYVAP 441
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPdGTINLDAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 442 MKALAAEMTNYFSKRLEPLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSvGDVALSQIVKLLILDEVHLLHE 521
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKS-GDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720362714 522 DRGPVLESIVARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFYFD 576
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
878-1191 |
2.16e-111 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 357.34 E-value: 2.16e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 878 YFSSTDLGRTASHFYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDALLNNFCELSAPGGVENSY 957
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 958 GKINILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSVLP 1037
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1038 PHILTRLEEKN-LTVDKLKDMRKDEIGHILHHVN-IGLKVKQCVHQIPSVTMEASIQPITRTVLRVSLNIHPDFSWNDQV 1115
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLGLLDaEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720362714 1116 HGTVgEPWWIWVEDPTNDHIYHSEYFLALKKQVINKeaQLLVFTIPIFEPLPsQYYIRAVSDRWLGAEAVCIINFQ 1191
Cdd:smart00611 241 HGKQ-EGWWLVIGDSDGNELLHIERFSLNKKNVSEE--VKLDFTAPATEGNY-QYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1712-2078 |
3.60e-96 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 313.43 E-value: 3.60e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1712 TIEPLTCGRIASYYYLKHKTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHTNNELAKCLPIELNPHSFDSPH 1791
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1792 TKAHLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAASQGWLVTVLNITHLIQMVIQGRWLKDSSLLTIPNIE 1871
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1872 QHHLHLFRKWKppvksshakcRTSIECLPELIHacEGKDHVFSSMVekelqpAKTKQAWNFLSRLPVINVGISVKGSwDD 1951
Cdd:smart00611 161 EEILKRLEKKK----------VLSLEDLLELED--EERGELLGLLD------AEGERVYKVLSRLPKLNIEISLEPI-TR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1952 LVEGHNELSISTLTADKRdenkwiklhadqeyvlqvslqrvhfglpkgKHEnhavtprfpklKDEGWFLILGEVDKRELM 2031
Cdd:smart00611 222 TVLGVEVTLTVDLTWDDE------------------------------IHG-----------KQEGWWLVIGDSDGNELL 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720362714 2032 AVKRVGFVRTHHD--ASISFFTPETPGRYIFTLYLMSDCYLGLDQQYDI 2078
Cdd:smart00611 261 HIERFSLNKKNVSeeVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPL 309
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1230-1752 |
1.23e-95 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 320.30 E-value: 1.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1230 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKIRIEEkLGKKVIE 1309
Cdd:COG1204 23 LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEE-LGIKVGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1310 LTGDVTPDMKSIAKADLIVTTPEKWDGVSRswQNRSYVQQVNILIIDEIHLLG-EERGPVLEVIVSRtnfiSSHTEKPVR 1388
Cdd:COG1204 100 STGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTLEVLLAR----LRRLNPEAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1389 IVGLSTALANARDLADWLNIKqmglfNFRPSVRPVPLE--VHIQG---FPGQHYCPRmasmnKPAFQAIRSHSPA-KPVL 1462
Cdd:COG1204 174 IVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSK-----DPTLALALDLLEEgGQVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1463 IFVSSRRQTRLTALELIAFLA---TEEDPKQWLNMDEQEMDniIGTVRDSNLKLT--LAFGIGMHHAGLHERDRKTVEEL 1537
Cdd:COG1204 244 VFVSSRRDAESLAKKLADELKrrlTPEEREELEELAEELLE--VSEETHTNEKLAdcLEKGVAFHHAGLPSELRRLVEDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1538 FVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGktrryVDFPITDVLQMMGRAGRPQFDDQGKAVILVHDIK---KD 1614
Cdd:COG1204 322 FREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDeadEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1615 FYKKFLYEPFPVESSLLGVLSD--HLNAEIAGGTITSKQDAMDYITWTYFFRRlimnPSYYSLGDVSQDSINKflshLIG 1692
Cdd:COG1204 397 FERYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQ----YDKGDLEEVVDDALEF----LLE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720362714 1693 QSLVElelshcievgEDNRTIEPLTCGRIASYYYLKHKTVKMFKDRLK---PECSTEELLSIL 1752
Cdd:COG1204 469 NGFIE----------EDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadEEFTDLGLLHLI 521
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
363-918 |
1.87e-95 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 319.92 E-value: 1.87e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 363 IKDLDEVG---QLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQHFhqgvikknefKIVYV 439
Cdd:COG1204 3 VAELPLEKvieFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 440 APMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGdvALSQIvKLLILDEVHLL 519
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDV-DLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 520 H-EDRGPVLESIVARtLRQVESTqsmIRILGLSATLPNYLDVATFLHVNPyiglfyFDGRFRPVPLgqtFLGIKSTNKmq 598
Cdd:COG1204 150 DdESRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGV-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 599 qlNNMDEVCYES-------VLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNSgqISCFLPTEGPEYGHALKQVQKSR- 670
Cdd:COG1204 215 --LRFDDGSRRSkdptlalALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRR--LTPEEREELEELAEELLEVSEETh 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 671 -NKQVRELFSDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTqiyaaKRGSFVDLGILDV 749
Cdd:COG1204 291 tNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-----KRGGMVPIPVLEF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 750 MQIFGRAGRPQFDKFGEGIIIT-THDKLSH--YLSLLTQQNPIESQFLE--SLADNLNAEIALGTVTNVEEAVRWMSYTY 824
Cdd:COG1204 366 KQMAGRAGRPGYDPYGEAILVAkSSDEADElfERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTF 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 825 LYVRMRANPLaygishkayqidptlrkhrEQLLIEVGQKLDKAKMIrfEERTGYFSSTDLGRTASHFYIKYNTIETFNEL 904
Cdd:COG1204 446 YAYQYDKGDL-------------------EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAELVDG 504
|
570
....*....|....
gi 1720362714 905 FDAHKTEGDIFAIV 918
Cdd:COG1204 505 LRKADEEFTDLGLL 518
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
881-1190 |
1.79e-94 |
|
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: 308.90 E-value: 1.79e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 881 STDLGRTASHFYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELdALLNNFCELSAPGGVENS-YGK 959
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKEL-NELNKRVPIPVKEGIIDSpHAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 960 INILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLW-GWASPLRQF-SVLP 1037
Cdd:smart00973 80 VNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWeDSDSPLKQLpHFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1038 PHILTRLEEKNL--TVDKLKDMRKDEIGHILH-HVNIGLKVKQCVHQIPSVTMEASIQPITRTV-LRVSLNIHPDFSWND 1113
Cdd:smart00973 160 EDVYDKLELKDGsrSFELLLDMNAAELGEFLNrLPPNGRLIYELLRRFPKIEVEAEVLPITRDLtLRVELEITPVFAWDL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362714 1114 QVHGTVGEPWWIWVEDPTNDHIYHSEYFLALKKQVINKeaQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIINF 1190
Cdd:smart00973 240 PRHKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNE--VKLDFTVPLSEPGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1227-1417 |
2.59e-90 |
|
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: 291.47 E-value: 2.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1227 FSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLGKK 1306
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPLLGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1307 VIELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKP 1386
Cdd:cd18021 81 VVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 1720362714 1387 VRIVGLSTALANARDLADWLNIKQMGLFNFR 1417
Cdd:cd18021 161 IRIVGLSSSLANARDVGEWLGASKSTIFNFH 191
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
1715-2080 |
1.83e-81 |
|
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: 271.15 E-value: 1.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1715 PLTCGRIASYYYLKHKTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHTNNELAKCLPIELNPHSFDSPHTKA 1794
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1795 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAASQGWLVTVLNITHLIQMVIQGRWL-KDSSLLTIPNIeqh 1873
Cdd:smart00973 81 NLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEdSDSPLKQLPHF--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1874 hlhlfrkwkppvksshakcrtsieCLPELIHACEGKDHVFSSMVEKELQPAKTKQAWNFLSRLPVINVGISVKGSWDDLv 1953
Cdd:smart00973 158 ------------------------LIEDVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEV- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1954 eghnELSISTLTADkrdenKWIKLHADQEYVLQVSLQRvhfglpkgkhenhavtprfPKLKDEGWFLILGEVDKRELMAV 2033
Cdd:smart00973 213 ----EAEVLPITRD-----LTLRVELEITPVFAWDLPR-------------------HKGKSESWWLVVGDSDTNELLAI 264
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1720362714 2034 KRVGFVR--THHDASISFFTPET-PGRYIFTLYLMSDCYLGLDQQYDIYL 2080
Cdd:smart00973 265 KRVTLRKkkKSNEVKLDFTVPLSePGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1715-2078 |
4.99e-72 |
|
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: 244.03 E-value: 4.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1715 PLTCGRIASYYYLKHKTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHTNNELAKCLPIELNPhSFDSPHTKA 1794
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKG-DIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1795 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAASQGWLVTVLNITHLIQMVIQGRWLKDSSLLTIPNIEqhh 1874
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIP--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1875 lhlfrkwkppvksshakcrtsieclPELIHACEGKDHVF-----SSMVEKELQ-----PAKTKQAWNFLSRLPVINVgis 1944
Cdd:pfam02889 157 -------------------------PELIKKLEKKGVESvrdilELDDAEELGelirnPKMGKDIAQFVNRFPKIEI--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1945 vkgswddlveghnELSISTLTADkrdenkwiklhadqeyVLQVSLQrvhfglpkgkhenhaVTPRFPKLKD-----EGWF 2019
Cdd:pfam02889 209 -------------EAEVQPITRS----------------VLRVEVT---------------ITPDFPWDKRvhgksEGFW 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720362714 2020 LILGEVDKRELMAVKRVGFVR--THHDASISFFTP-ETPGRYIFTLYLMSDCYLGLDQQYDI 2078
Cdd:pfam02889 245 LVVGDSDGNEILHIERFTLTKrtLAGEHKLEFTVPpSDPGPPQLFVRLISDSWLGADQEVPI 306
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
1229-1417 |
1.09e-66 |
|
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: 223.29 E-value: 1.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1229 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDDWKIRIEEkLGKKVI 1308
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSG-GKAVYIAPTRALVNQKEADLRERFGP-LGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1309 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRsYVQQVNILIIDEIHLLG-EERGPVLEVIVSRTNFIsshtEKPV 1387
Cdd:cd17921 79 LLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI----NKNA 153
|
170 180 190
....*....|....*....|....*....|
gi 1720362714 1388 RIVGLSTALANARDLADWLNIKqmGLFNFR 1417
Cdd:cd17921 154 RFVGLSATLPNAEDLAEWLGVE--DLIRFD 181
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1421-1609 |
1.50e-66 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 222.04 E-value: 1.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1421 RPVPLEVHIQGFPGQHYCPRMASMNK-----PAFQAIRSHSPAKPVLIFVSSRRQTRLTALELIaflateedpkqwlnmd 1495
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1496 eqemdniigtvrdsnlkltlafGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKT 1575
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 1720362714 1576 RRYvdFPITDVLQMMGRAGRPQFDDQGKAVILVH 1609
Cdd:cd18795 123 YRE--LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
1230-1422 |
1.23e-65 |
|
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: 221.46 E-value: 1.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1230 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTS-----KAVYIAPLKALVRERMDDWKIRIeEKLG 1304
Cdd:cd18023 2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLpwgnrKVVYIAPIKALCSEKYDDWKEKF-GPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1305 KKVIELTGD-VTPDMKSIAKADLIVTTPEKWDGVSRSW-QNRSYVQQVNILIIDEIHLLGEERGPVLEVIVSRTNFISSH 1382
Cdd:cd18023 81 LSCAELTGDtEMDDTFEIQDADIILTTPEKWDSMTRRWrDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSSS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720362714 1383 TEK------PVRIVGLSTALANARDLADWLNIKQMGLFNFRPSVRP 1422
Cdd:cd18023 161 SELrgstvrPMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1247-1767 |
1.12e-59 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 220.46 E-value: 1.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFrvfNKYPTS--KAVYIAPLKALVRER---MDDWkirieEKLGKKVIELTGDVTPDMKSI 1321
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMV---NKLLREggKAVYLVPLKALAEEKyreFKDW-----EKLGLRVAMTTGDYDSTDEWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1322 AKADLIVTTPEKWDGVSRswQNRSYVQQVNILIIDEIHLLGE-ERGPVLEVIVSrtnfissHTEKPVRIVGLSTALANAR 1400
Cdd:PRK00254 113 GKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSyDRGATLEMILT-------HMLGRAQILGLSATVGNAE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1401 DLADWLNIKQMglfnfRPSVRPVPLE--VHIQGF------PGQHYcprMASMNKPAFQAIRShspAKPVLIFVSSRRQTR 1472
Cdd:PRK00254 184 ELAEWLNAELV-----VSDWRPVKLRkgVFYQGFlfwedgKIERF---PNSWESLVYDAVKK---GKGALVFVNTRRSAE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1473 LTALEL---IAFLATEEDPKQWLNMDEQEMDNiigtvrDSNLKLTLAF--GIGMHHAGLHERDRKTVEELFVNCKVQVLI 1547
Cdd:PRK00254 253 KEALELakkIKRFLTKPELRALKELADSLEEN------PTNEKLKKALrgGVAFHHAGLGRTERVLIEDAFREGLIKVIT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1548 ATSTLAWGVNFPAHLVIIKGTEYYDGKTrrYVDFPITDVLQMMGRAGRPQFDDQGKAVILVH-DIKKDFYKKF------- 1619
Cdd:PRK00254 327 ATPTLSAGINLPAFRVIIRDTKRYSNFG--WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERYifgkpek 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1620 LYEPFPVESSLLGvlsdHLNAEIAGGTITSKQDAMDYITWTYFFRRlimNPSYYSLgdvsQDSINKFLSHLIGQSLVELE 1699
Cdd:PRK00254 405 LFSMLSNESAFRS----QVLALITNFGVSNFKELVNFLERTFYAHQ---RKDLYSL----EEKAKEIVYFLLENEFIDID 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720362714 1700 LshcievgEDNrtIEPLTCGRIASYYYLKHKTVKMFKDRLkPECSTEE----LLSILSDAEEYTDLPVRHNE 1767
Cdd:PRK00254 474 L-------EDR--FIPLPLGIRTSQLYIDPLTAKKFKDAF-PKIEKNPnplgIFQLIASTPDMTPLNYSRKE 535
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
380-576 |
1.47e-57 |
|
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: 197.48 E-value: 1.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 380 LNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQHfhqgvikknEFKIVYVAPMKALAAEMTNYFSKRLEP 459
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS---------GGKAVYIAPTRALVNQKEADLRERFGP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 460 LGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDvaLSQIVKLLILDEVHLLH-EDRGPVLESIVARTLRQv 538
Cdd:cd17921 73 LGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER--LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI- 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720362714 539 estQSMIRILGLSATLPNYLDVATFLHVnpyIGLFYFD 576
Cdd:cd17921 150 ---NKNARFVGLSATLPNAEDLAEWLGV---EDLIRFD 181
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
396-937 |
4.74e-57 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 212.75 E-value: 4.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 396 ENMLICAPTGAGKTNIAMLTILHEIRQhfhQGvikkneFKIVYVAPMKALAAEMTNYFsKRLEPLGIVVKELTGDMQlSK 475
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKLLR---EG------GKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYD-ST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 476 SEIL-RTQMLVTTPEKWDVVTRKSVgdvalSQI--VKLLILDEVHLL-HEDRGPVLESIVARTLRQVEstqsmirILGLS 551
Cdd:PRK00254 109 DEWLgKYDIIIATAEKFDSLLRHGS-----SWIkdVKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ-------ILGLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 552 ATLPNYLDVATFLHVNpyigLFYFDgrFRPVPL-------GQTFLGIKSTNKMQqlNNMDEVCYESVlkqvKAGHQVMVF 624
Cdd:PRK00254 177 ATVGNAEELAEWLNAE----LVVSD--WRPVKLrkgvfyqGFLFWEDGKIERFP--NSWESLVYDAV----KKGKGALVF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 625 VHARNATVRTAMSLieraknSGQISCFLPTegPEYgHALKQVQKS-----RNKQVRELFSDGFSIHHAGMLRQDRNLVEN 699
Cdd:PRK00254 245 VNTRRSAEKEALEL------AKKIKRFLTK--PEL-RALKELADSleenpTNEKLKKALRGGVAFHHAGLGRTERVLIED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 700 LFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTQIYAakRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDK---- 775
Cdd:PRK00254 316 AFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpskl 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 776 LSHYL--------SLLTQQNPIESQFLesladnlnAEIALGTVTNVEEAVRWMSYTYlYVRMRANPlaYGISHKAYQIDP 847
Cdd:PRK00254 394 MERYIfgkpeklfSMLSNESAFRSQVL--------ALITNFGVSNFKELVNFLERTF-YAHQRKDL--YSLEEKAKEIVY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 848 TLrkhREQLLIEvgqkldkakmIRFEERtgyFSSTDLGRTASHFYIKYNTIETFNELFDahKTEGD-----IFAIVSKAE 922
Cdd:PRK00254 463 FL---LENEFID----------IDLEDR---FIPLPLGIRTSQLYIDPLTAKKFKDAFP--KIEKNpnplgIFQLIASTP 524
|
570
....*....|....*
gi 1720362714 923 EFDQIKVREEEIEEL 937
Cdd:PRK00254 525 DMTPLNYSRKEMEDL 539
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
381-581 |
5.38e-56 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 193.73 E-value: 5.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 381 NRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQhfhQGVIKKNEFKIVYVAPMKALAAEMTNYFSKRLEPL 460
Cdd:cd18023 3 NRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKE---RNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 461 GIVVKELTGDMQLSKS-EILRTQMLVTTPEKWDVVTRKSVGDVALSQIVKLLILDEVHLLHEDRGPVLESIVARTLRQVE 539
Cdd:cd18023 80 GLSCAELTGDTEMDDTfEIQDADIILTTPEKWDSMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720362714 540 STQSM------IRILGLSATLPNYLDVATFLHVNPyIGLFYFDGRFRP 581
Cdd:cd18023 160 SSELRgstvrpMRFVAVSATIPNIEDLAEWLGDNP-AGCFSFGESFRP 206
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
1213-1416 |
4.68e-53 |
|
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: 185.65 E-value: 4.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1213 ITALGCKAYEALYNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKY--PTS-------KAVYIAP 1283
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHrnPDGtinldafKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1284 LKALVRERMDDWKIRIEEkLGKKVIELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIHLLGE 1363
Cdd:cd18019 81 MKALVQEMVGNFSKRLAP-YGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720362714 1364 ERGPVLEVIVSRTNFISSHTEKPVRIVGLSTALANARDLADWLNIK-QMGLFNF 1416
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDpKKGLFYF 213
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
580-772 |
2.45e-52 |
|
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: 181.21 E-value: 2.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 580 RPVPLGQTFLGIKST----NKMQQLNNMDEVCYESVLKQVKAGHQVMVFVHARNATVRTAMSLIeraknsgqiscflpte 655
Cdd:cd18795 1 RPVPLEEYVLGFNGLgiklRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 656 gpeyghalkqvqksrnkqvrelfsdGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTQIYA 735
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720362714 736 AKRgsFVDLGILDVMQIFGRAGRPQFDKFGEGIIITT 772
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1247-1663 |
5.60e-52 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 196.26 E-value: 5.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWkIRIEEkLGKKVIELTGDV--TPDMksIAKA 1324
Cdd:PRK01172 39 NVIVSVPTAAGKTLIAYSAIYETFLA--GLKSIYIVPLRSLAMEKYEEL-SRLRS-LGMRVKISIGDYddPPDF--IKRY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1325 DLIVTTPEKWDgvSRSWQNRSYVQQVNILIIDEIHLLGEE-RGPVLEVIVSRTNFISSHTekpvRIVGLSTALANARDLA 1403
Cdd:PRK01172 113 DVVILTSEKAD--SLIHHDPYIINDVGLIVADEIHIIGDEdRGPTLETVLSSARYVNPDA----RILALSATVSNANELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1404 DWLNIKQMglfnfRPSVRPVPLEVHIQgFPGQHYCPRMASMNKPAFQAIRSH-SPAKPVLIFVSSRRQTRLTALELIAFL 1482
Cdd:PRK01172 187 QWLNASLI-----KSNFRPVPLKLGIL-YRKRLILDGYERSQVDINSLIKETvNDGGQVLVFVSSRKNAEDYAEMLIQHF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1483 ATEEDpkqwLNMDEQEMDniigtVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHL 1562
Cdd:PRK01172 261 PEFND----FKVSSENNN-----VYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1563 VIIKG-TEYYDGKTRryvdfPIT--DVLQMMGRAGRPQFDDQGKAVILV-----HDIKKDFYKKflyEPFPVESSLLGVL 1634
Cdd:PRK01172 332 VIVRDiTRYGNGGIR-----YLSnmEIKQMIGRAGRPGYDQYGIGYIYAaspasYDAAKKYLSG---EPEPVISYMGSQR 403
|
410 420 430
....*....|....*....|....*....|.
gi 1720362714 1635 SDHLN--AEIAGGTITSKQDAMDYITWTYFF 1663
Cdd:PRK01172 404 KVRFNtlAAISMGLASSMEDLILFYNETLMA 434
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1247-1765 |
1.22e-50 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 193.64 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKIRieEKLGKKVIELTGDVTPDMKSIAKADL 1326
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAMLKAIAR--GGKALYIVPLRALASEKFEEFERF--EELGVRVGISTGDYDSRDEWLGDNDI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1327 IVTTPEKWDGVSRswqNR-SYVQQVNILIIDEIHLLG-EERGPVLEVIVS---RTNfisshtekP-VRIVGLSTALANAR 1400
Cdd:PRK02362 117 IVATSEKVDSLLR---NGaPWLDDITCVVVDEVHLIDsANRGPTLEVTLAklrRLN--------PdLQVVALSATIGNAD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1401 DLADWLNIK-----------QMGLF-----NFRPSVRPVP-----------LEVHIQGfpGQhyCprmasmnkpafqair 1453
Cdd:PRK02362 186 ELADWLDAElvdsewrpidlREGVFyggaiHFDDSQREVEvpskddtlnlvLDTLEEG--GQ--C--------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1454 shspakpvLIFVSSRRQTRLTALELIAFLateedpKQWLNMDEQ-EMDNIIGTVRDS-------NLKLTLAFGIGMHHAG 1525
Cdd:PRK02362 247 --------LVFVSSRRNAEGFAKRAASAL------KKTLTAAERaELAELAEEIREVsdtetskDLADCVAKGAAFHHAG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1526 LHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGkTRRYVDFPITDVLQMMGRAGRPQFDDQGKAV 1605
Cdd:PRK02362 313 LSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDG-GAGMQPIPVLEYHQMAGRAGRPGLDPYGEAV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1606 ILV--HDIKKDFYKKFLY-EPFPVESSLL--GVLSDHLNAEIAGGTITSKQDAMDYITWTYFFrrlimnpsyyslgdvSQ 1680
Cdd:PRK02362 392 LLAksYDELDELFERYIWaDPEDVRSKLAtePALRTHVLSTIASGFARTRDGLLEFLEATFYA---------------TQ 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1681 DSINKFLSHLIGQSLVELELSHCIEvgEDNRTIEPLTCGRIASYYYlkhktvkmfkdrLKPeCSTEELLSILSDAEEYTD 1760
Cdd:PRK02362 457 TDDTGRLERVVDDVLDFLERNGMIE--EDGETLEATELGHLVSRLY------------IDP-LSAAEIIDGLEAAKKPTD 521
|
....*
gi 1720362714 1761 LPVRH 1765
Cdd:PRK02362 522 LGLLH 526
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
381-576 |
1.69e-49 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350780 [Multi-domain] Cd Length: 189 Bit Score: 174.48 E-value: 1.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 381 NRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQHFHqgvikkneFKIVYVAPMKALAAEMTNYFSKRL-EP 459
Cdd:cd18022 3 NPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPG--------SKVVYIAPLKALVRERVDDWKKRFeEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 460 LGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVV-----TRKSVgdvalsQIVKLLILDEVHLLHEDRGPVLESIVART 534
Cdd:cd18022 75 LGKKVVELTGDVTPDMKALADADIIITTPEKWDGIsrswqTREYV------QQVSLIIIDEIHLLGSDRGPVLEVIVSRM 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720362714 535 LRQVESTQSMIRILGLSATLPNYLDVATFLHVNPyIGLFYFD 576
Cdd:cd18022 149 NYISSQTEKPVRLVGLSTALANAGDLANWLGIKK-MGLFNFR 189
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
395-893 |
7.01e-48 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 185.16 E-value: 7.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNIAMLTILHEIrqhfhqgvikKNEFKIVYVAPMKALAAEMTNYFSkRLEPLGIVVKELTGDMQlS 474
Cdd:PRK02362 39 GKNLLAAIPTASGKTLIAELAMLKAI----------ARGGKALYIVPLRALASEKFEEFE-RFEELGVRVGISTGDYD-S 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 475 KSEIL-RTQMLVTTPEKWDVVTRKsvGDVALSQIvKLLILDEVHLL-HEDRGPVLESIVARTLRQVESTQsmirILGLSA 552
Cdd:PRK02362 107 RDEWLgDNDIIVATSEKVDSLLRN--GAPWLDDI-TCVVVDEVHLIdSANRGPTLEVTLAKLRRLNPDLQ----VVALSA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 553 TLPNYLDVATFLH----------VNPYIGLFY-----FDGRFRPVPLGqtflgikstNKMQQLNnmdevcyeSVLKQVKA 617
Cdd:PRK02362 180 TIGNADELADWLDaelvdsewrpIDLREGVFYggaihFDDSQREVEVP---------SKDDTLN--------LVLDTLEE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 618 GHQVMVFVHARnatvRTAMSLIERAKNSGQiSCFLPTEGPEYGHALKQVQKSRNKQVRELFSD----GFSIHHAGMLRQD 693
Cdd:PRK02362 243 GGQCLVFVSSR----RNAEGFAKRAASALK-KTLTAAERAELAELAEEIREVSDTETSKDLADcvakGAAFHHAGLSREH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 694 RNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTQIYAAKRGSfVDLGILDVMQIFGRAGRPQFDKFGEGIIIT-T 772
Cdd:PRK02362 318 RELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAGM-QPIPVLEYHQMAGRAGRPGLDPYGEAVLLAkS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 773 HDKLS----HYLSLLTQqnPIESQFLE--SLADNLNAEIALGTVTNVEEAVRWMSYTyLYvrmranplaygishkAYQID 846
Cdd:PRK02362 397 YDELDelfeRYIWADPE--DVRSKLATepALRTHVLSTIASGFARTRDGLLEFLEAT-FY---------------ATQTD 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1720362714 847 PTLRKHReqLLIEVGQKLDKAKMIrfEERTGYFSSTDLGRTASHFYI 893
Cdd:PRK02362 459 DTGRLER--VVDDVLDFLERNGMI--EEDGETLEATELGHLVSRLYI 501
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1247-1629 |
9.26e-47 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 181.68 E-value: 9.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKirieEKLGK-KVIELTGDVT--PDmksiak 1323
Cdd:COG4581 42 SVLVAAPTGSGKTLVAEFAIFLALAR--GRRSFYTAPIKALSNQKFFDLV----ERFGAeNVGLLTGDASvnPD------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1324 ADLIVTTPEkwdgVSRswqNRSY--------VQQVnilIIDEIHLLGE-ERGPVLEVIVsrtnfIssHTEKPVRIVGLST 1394
Cdd:COG4581 110 APIVVMTTE----ILR---NMLYregadledVGVV---VMDEFHYLADpDRGWVWEEPI-----I--HLPARVQLVLLSA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1395 ALANARDLADWLNikqmglfnfrpSV-----------RPVPLEvhiqgfpgQHYC--PRMASMNKPAFQAIRSHSPAK-- 1459
Cdd:COG4581 173 TVGNAEEFAEWLT-----------RVrgetavvvseeRPVPLE--------FHYLvtPRLFPLFRVNPELLRPPSRHEvi 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1460 ---------PVLIFVSSRRQTRLTALELIAFLATEEDPKQWLNMDEQEMDNIIGTVRDSNLKLTLAFGIGMHHAGLHERD 1530
Cdd:COG4581 234 eeldrggllPAIVFIFSRRGCDEAAQQLLSARLTTKEERAEIREAIDEFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPKY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1531 RKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKTRRyvdfPIT--DVLQMMGRAGRPQFDDQGKAVILV 1608
Cdd:COG4581 314 RRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHR----PLTarEFHQIAGRAGRRGIDTEGHVVVLA 389
|
410 420
....*....|....*....|....*
gi 1720362714 1609 HDiKKDFyKKFLY----EPFPVESS 1629
Cdd:COG4581 390 PE-HDDP-KKFARlasaRPEPLRSS 412
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
395-933 |
1.29e-45 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 177.00 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNIAMltilHEIRQHFHQGVikknefKIVYVAPMKALAAEMTNYFSkRLEPLGIVVKELTGDMQLS 474
Cdd:PRK01172 37 GENVIVSVPTAAGKTLIAY----SAIYETFLAGL------KSIYIVPLRSLAMEKYEELS-RLRSLGMRVKISIGDYDDP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 475 KSEILRTQMLVTTPEKWDVVTRKsvgDVALSQIVKLLILDEVHLLH-EDRGPVLESiVARTLRQVESTqsmIRILGLSAT 553
Cdd:PRK01172 106 PDFIKRYDVVILTSEKADSLIHH---DPYIINDVGLIVADEIHIIGdEDRGPTLET-VLSSARYVNPD---ARILALSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 554 LPNYLDVATFLHVNPYIGlfyfdgRFRPVPLGqtfLGIKSTNKM----QQLNNMDEVcyeSVLKQ-VKAGHQVMVFVHAR 628
Cdd:PRK01172 179 VSNANELAQWLNASLIKS------NFRPVPLK---LGILYRKRLildgYERSQVDIN---SLIKEtVNDGGQVLVFVSSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 629 NATVRTAMSLIERAknsGQISCFLPTEGPEYGHalkqvqksrNKQVRELFSDGFSIHHAGMLRQDRNLVENLFSNGHIKV 708
Cdd:PRK01172 247 KNAEDYAEMLIQHF---PEFNDFKVSSENNNVY---------DDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 709 LVCTATLAWGVNLPAHAVVIKGTQIYAAKRGSFvdLGILDVMQIFGRAGRPQFDKFGEGIII----TTHDKLSHYLSllT 784
Cdd:PRK01172 315 IVATPTLAAGVNLPARLVIVRDITRYGNGGIRY--LSNMEIKQMIGRAGRPGYDQYGIGYIYaaspASYDAAKKYLS--G 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 785 QQNPIESQF--LESLADNLNAEIALGTVTNVEEAVRWMSYTYLYVRMRANPLAYGISHKAYqidptlrkhreqLLIEVGq 862
Cdd:PRK01172 391 EPEPVISYMgsQRKVRFNTLAAISMGLASSMEDLILFYNETLMAIQNGVDEIDYYIESSLK------------FLKENG- 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720362714 863 kldkakmirFEERTGYFSSTDLGRTASHFYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEE 933
Cdd:PRK01172 458 ---------FIKGDVTLRATRLGKLTSDLYIDPESALILKSAFDHDYDEDLALYYISLCREIIPANTRDDY 519
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1231-1416 |
1.97e-45 |
|
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: 163.37 E-value: 1.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1231 NPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTS---------KAVYIAPLKALVRERMDDWKIRIEe 1301
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQggvikkddfKIVYIAPMKALAAEMVEKFSKRLA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1302 KLGKKVIELTGDVTPDMKSIAKADLIVTTPEKWDGVSR-SWQNRSYVQQVNILIIDEIHLLGEERGPVLEVIVSRTNFIS 1380
Cdd:cd18020 82 PLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRkSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQV 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720362714 1381 SHTEKPVRIVGLSTALANARDLADWLNIKQM-GLFNF 1416
Cdd:cd18020 162 ESTQSMIRIVGLSATLPNYLDVADFLRVNPYkGLFFF 198
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
378-568 |
4.59e-42 |
|
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: 153.18 E-value: 4.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 378 KRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHeirqHFHQGvikkNEFKIVYVAPMKALAAEMTNYFSKRL 457
Cdd:cd18021 2 KFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLR----HWRQN----PKGRAVYIAPMQELVDARYKDWRAKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 458 EP-LGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVV-----TRKSVgdvalsQIVKLLILDEVHLLHEDRGPVLESIV 531
Cdd:cd18021 74 GPlLGKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLsrrwkQRKNV------QSVELFIADELHLIGGENGPVYEVVV 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720362714 532 ARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNP 568
Cdd:cd18021 148 SRMRYISSQLEKPIRIVGLSSSLANARDVGEWLGASK 184
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
1230-1409 |
3.58e-38 |
|
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: 141.70 E-value: 3.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1230 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIfrVFNKYPTSKAVYIAPLKALVRERMDDWKIRieEKLGKKVIE 1309
Cdd:cd18028 2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAM--VNTLLEGGKALYLVPLRALASEKYEEFKKL--EEIGLKVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1310 LTGDVTPDMKSIAKADLIVTTPEKWDGVsrsWQNR-SYVQQVNILIIDEIHLLG-EERGPVLEVIVSRTNfissHTEKPV 1387
Cdd:cd18028 78 STGDYDEDDEWLGDYDIIVATYEKFDSL---LRHSpSWLRDVGVVVVDEIHLISdEERGPTLESIVARLR----RLNPNT 150
|
170 180
....*....|....*....|..
gi 1720362714 1388 RIVGLSTALANARDLADWLNIK 1409
Cdd:cd18028 151 QIIGLSATIGNPDELAEWLNAE 172
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
391-866 |
1.96e-36 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 149.70 E-value: 1.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 391 AYNTNENMLICAPTGAGKTNIAMltilHEIRQHFHQGVikknefKIVYVAPMKALAAEmtNYF--SKRL--EPLGIvvke 466
Cdd:COG4581 36 ALEAGRSVLVAAPTGSGKTLVAE----FAIFLALARGR------RSFYTAPIKALSNQ--KFFdlVERFgaENVGL---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 467 LTGDMQL--------SKSEILRTQMLVTTPEKWDVvtrksvgDVAlsqivkllILDEVHLLHE-DRGPVLE-SIVARTLR 536
Cdd:COG4581 100 LTGDASVnpdapivvMTTEILRNMLYREGADLEDV-------GVV--------VMDEFHYLADpDRGWVWEePIIHLPAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 537 qvestqsmIRILGLSATLPNYLDVATFLH--------VnpyiglfyfDGRFRPVPLGQTFLGIKSTNKMQQLNNMDEVCY 608
Cdd:COG4581 165 --------VQLVLLSATVGNAEEFAEWLTrvrgetavV---------VSEERPVPLEFHYLVTPRLFPLFRVNPELLRPP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 609 E--SVLKQVKAGHQ--VMVFVHARNATVRTAMSLIERAKNSgqiscflPTEGPEYGHALKQVQKSRN----KQVRELFSD 680
Cdd:COG4581 228 SrhEVIEELDRGGLlpAIVFIFSRRGCDEAAQQLLSARLTT-------KEERAEIREAIDEFAEDFSvlfgKTLSRLLRR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 681 GFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGtqiyAAKR--GSFVDLGILDVMQIFGRAGR 758
Cdd:COG4581 301 GIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTK----LSKFdgERHRPLTAREFHQIAGRAGR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 759 PQFDKFGEGIIITT-HDKLSHYLSLLTQQ-NPIESQFlesladnlnaEIALGTVTNVeeaVRWMSYTylyvRMRAnplAY 836
Cdd:COG4581 377 RGIDTEGHVVVLAPeHDDPKKFARLASARpEPLRSSF----------RPSYNMVLNL---LARPGLE----RARE---LL 436
|
490 500 510
....*....|....*....|....*....|
gi 1720362714 837 GISHKAYQIDPTLRKHREQlLIEVGQKLDK 866
Cdd:COG4581 437 EDSFAQFQADRSVVGLARR-ARELERALAG 465
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
381-559 |
1.23e-33 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 128.13 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 381 NRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTILHEIRQhfhqgviKKNEFKIVYVAPMKALAAEMTNYFSKRLEPL 460
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK-------LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 461 GIVVKELTGDMQLSK--SEILRTQMLVTTPEKWDVVTRKSvgdVALSQiVKLLILDEVHLLHE-DRGPVLESIVARtlrq 537
Cdd:pfam00270 73 GLKVASLLGGDSRKEqlEKLKGPDILVGTPGRLLDLLQER---KLLKN-LKLLVLDEAHRLLDmGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|..
gi 1720362714 538 vesTQSMIRILGLSATLPNYLD 559
Cdd:pfam00270 145 ---LPKKRQILLLSATLPRNLE 163
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1231-1402 |
2.93e-32 |
|
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: 124.28 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1231 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFN-KYPTSKAVYIAPLKALVRERMDDWKiRIEEKLGKKVIE 1309
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDkLDNGPQALVLAPTRELAEQIYEELK-KLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1310 LTGDVTP--DMKSIAKADLIVTTPEKWDGVsrsWQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNfisshteKP 1386
Cdd:pfam00270 79 LLGGDSRkeQLEKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRRLP-------KK 148
|
170
....*....|....*..
gi 1720362714 1387 VRIVGLS-TALANARDL 1402
Cdd:pfam00270 149 RQILLLSaTLPRNLEDL 165
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
379-564 |
1.56e-29 |
|
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: 116.66 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 379 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQHfhqgvikkneFKIVYVAPMKALAAEMTNYFSKrLE 458
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEG----------GKALYLVPLRALASEKYEEFKK-LE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 459 PLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSvgdVALSQIVKLLILDEVHLLH-EDRGPVLESIVARTLRQ 537
Cdd:cd18028 70 EIGLKVGISTGDYDEDDEWLGDYDIIVATYEKFDSLLRHS---PSWLRDVGVVVVDEIHLISdEERGPTLESIVARLRRL 146
|
170 180
....*....|....*....|....*..
gi 1720362714 538 VESTQsmirILGLSATLPNYLDVATFL 564
Cdd:cd18028 147 NPNTQ----IIGLSATIGNPDELAEWL 169
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
372-583 |
1.58e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 109.12 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 372 LAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQHFHQgvikknefKIVYVAPMKALAAEMTN 451
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGG--------RVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 452 YFSKRLEPLGIVVKELTGD----MQLSKSEILRTQMLVTTPEKWDVVTRKsvGDVALSQiVKLLILDEVH-LLHEDRGPV 526
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRLLDLLEN--DKLSLSN-VDLVILDEAHrLLDGGFGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362714 527 LESIVARTLRqvestqsMIRILGLSATLPNYLDVATFLHVNpyiGLFYFDGRFRPVP 583
Cdd:smart00487 150 LEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1232-1608 |
9.70e-26 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 115.76 E-value: 9.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1232 PVQT-QIFHTLYHTDcNVLLGAPTGSGKTVAAELA-IFRVFNKypTSKAVYIAPLKALVRERMDDWKIRIEEKLgkKVIE 1309
Cdd:COG1202 212 PVQSlAVENGLLEGK-DQLVVSATATGKTLIGELAgIKNALEG--KGKMLFLVPLVALANQKYEDFKDRYGDGL--DVSI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1310 LTGDV---TPDMKSIAKADLIVTTPEKWDGVSRSwqnRSYVQQVNILIIDEIHLLGE-ERGPVLEVIVSRTNFISSHTEk 1385
Cdd:COG1202 287 RVGASrirDDGTRFDPNADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEVHMLEDpERGHRLDGLIARLKYYCPGAQ- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1386 pvrIVGLSTALANARDLADWLNIKQMgLFNfrpsVRPVPLEVHIQGFPGQHYCPRMASMNKPAFQAIRSHSPAKPVLIFV 1465
Cdd:COG1202 363 ---WIYLSATVGNPEELAKKLGAKLV-EYE----ERPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1466 SSRRQTRltaleliaflateedpkqwlnmdeqemdniigtvrdsnlKLTLAFGIGM--HHAGLHERDRKTVEELFVNCKV 1543
Cdd:COG1202 435 NSRRRCH---------------------------------------EIARALGYKAapYHAGLDYGERKKVERRFADQEL 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720362714 1544 QVLIATSTLAWGVNFPAHLVIIK----GTEYydgktrryvdFPITDVLQMMGRAGRPQFDDQGKAVILV 1608
Cdd:COG1202 476 AAVVTTAALAAGVDFPASQVIFDslamGIEW----------LSVQEFHQMLGRAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1225-1424 |
5.23e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 104.50 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1225 YNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLG 1304
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1305 KKVIELTGDVT-PDMKSIAK--ADLIVTTPEKWDGVSRswQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNfis 1380
Cdd:smart00487 84 KVVGLYGGDSKrEQLRKLESgkTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720362714 1381 shteKPVRIVGLS-TALANARDLADWLNIkqmGLFNFRPSVRPVP 1424
Cdd:smart00487 159 ----KNVQLLLLSaTPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
1245-1418 |
1.31e-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: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1245 DCNVLLGAPTGSGKTVAAELAIFRVF--NKyptSKAVYIAPLKALVRERMDdWKIRIEEKLGKKVIELTGDVTPDM-KSI 1321
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLleRR---KKALFVLPYVSIVQEKVD-ALSPLFEELGFRVEGYAGNKGRSPpKRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1322 AKADLIVTTPEKWDG-VSRSWQNRSyVQQVNILIIDEIHLLGEE-RGPVLEVIVSRtnfISSHTEKPVRIVGLSTALANA 1399
Cdd:cd18026 109 KSLSVAVCTIEKANSlVNSLIEEGR-LDELGLVVVDELHMLGDGhRGALLELLLTK---LLYAAQKNIQIVGMSATLPNL 184
|
170 180
....*....|....*....|.
gi 1720362714 1400 RDLADWLNIKqmgLF--NFRP 1418
Cdd:cd18026 185 EELASWLRAE---LYttNFRP 202
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
1247-1406 |
1.56e-21 |
|
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: 93.42 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKYPTS--KAVYIAPLKALVRermdDWKIRIEE-----KLGKKVIELTGDVTPDMK 1319
Cdd:cd17922 3 NVLIAAPTGSGKTEAAFLPALSSLADEPEKgvQVLYISPLKALIN----DQERRLEEpldeiDLEIPVAVRHGDTSQSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1320 SIAKA---DLIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRtnfISSHTEKPVRIVGLSTA 1395
Cdd:cd17922 79 AKQLKnppGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHaLLGSKRGVQLELLLER---LRKLTGRPLRRIGLSAT 155
|
170
....*....|.
gi 1720362714 1396 LANARDLADWL 1406
Cdd:cd17922 156 LGNLEEAAAFL 166
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
395-581 |
8.21e-21 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 92.66 E-value: 8.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNIAMLTILHEIRQhfhqgvikkNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDmqLS 474
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLLE---------RRKKALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGN--KG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 475 KSEILR---TQMLVTTPEKWDVVTRKSVGDVALSQIvKLLILDEVHLLHE-DRGPVLESIVARTLRqveSTQSMIRILGL 550
Cdd:cd18026 102 RSPPKRrksLSVAVCTIEKANSLVNSLIEEGRLDEL-GLVVVDELHMLGDgHRGALLELLLTKLLY---AAQKNIQIVGM 177
|
170 180 190
....*....|....*....|....*....|.
gi 1720362714 551 SATLPNYLDVATFLHVnpyiglFYFDGRFRP 581
Cdd:cd18026 178 SATLPNLEELASWLRA------ELYTTNFRP 202
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
395-564 |
1.02e-20 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 91.11 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNIAMLTILHEIRQHFHQGVikknefKIVYVAPMKALAAEMTnyfsKRLE------PLGIVVKELT 468
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV------QVLYISPLKALINDQE----RRLEepldeiDLEIPVAVRH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 469 GDM-QLSKSEILRT--QMLVTTPEKWDVVTRKSVGDVALSQiVKLLILDEVH-LLHEDRGPVLESIVARtLRQVESTQsm 544
Cdd:cd17922 71 GDTsQSEKAKQLKNppGILITTPESLELLLVNKKLRELFAG-LRYVVVDEIHaLLGSKRGVQLELLLER-LRKLTGRP-- 146
|
170 180
....*....|....*....|
gi 1720362714 545 IRILGLSATLPNYLDVATFL 564
Cdd:cd17922 147 LRRIGLSATLGNLEEAAAFL 166
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1227-1564 |
6.73e-19 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 94.01 E-value: 6.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1227 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAIF-RVFNKYPTSKA------VYIAPLKAL---VRERMDDWK 1296
Cdd:COG1201 22 FGAPTPPQREAW-PAIAAGESTLLIAPTGSGKTLAAFLPALdELARRPRPGELpdglrvLYISPLKALandIERNLRAPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1297 IRIEEKLGKKVIEL-----TGDVTPDMKSIAKA---DLIVTTPE---------KWdgvsrswqnRSYVQQVNILIIDEIH 1359
Cdd:COG1201 101 EEIGEAAGLPLPEIrvgvrTGDTPASERQRQRRrppHILITTPEslallltspDA---------RELLRGVRTVIVDEIH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1360 -LLGEERGPVLEVIVSRtnfISSHTEKPVRIVGLSTALANARDLADWLnikqMGLFNFRPS--VRP-----------VPL 1425
Cdd:COG1201 172 aLAGSKRGVHLALSLER---LRALAPRPLQRIGLSATVGPLEEVARFL----VGYEDPRPVtiVDAgagkkpdlevlVPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1426 EVHIQGFP-----GQHYCPRMAsmnkpafQAIRSHspaKPVLIFVSSRRQTRLTALELIAFLATEEDPkqwlnmdeqemd 1500
Cdd:COG1201 245 EDLIERFPwaghlWPHLYPRVL-------DLIEAH---RTTLVFTNTRSQAERLFQRLNELNPEDALP------------ 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720362714 1501 niigtvrdsnlkltlafgIGMHHAGL-HERdRKTVEELFVNCKVQVLIATSTLAWGVNFPA-HLVI 1564
Cdd:COG1201 303 ------------------IAAHHGSLsREQ-RLEVEEALKAGELRAVVATSSLELGIDIGDvDLVI 349
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
372-780 |
2.13e-16 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 85.66 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 372 LAFKGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTILHEIRQHfhqgvikkNEFKIVYVAPMKALAA---- 447
Cdd:COG1205 49 LKKRGIERLYSHQAEAIEAARA-GKNVVIATPTASGKSLAYLLPVLEALLED--------PGATALYLYPTKALARdqlr 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 448 EMTNYFSKRlePLGIVVKELTGDMQLS-KSEILRT-QMLVTTP-----------EKWDVVTRKsvgdvalsqiVKLLILD 514
Cdd:COG1205 120 RLRELAEAL--GLGVRVATYDGDTPPEeRRWIREHpDIVLTNPdmlhygllphhTRWARFFRN----------LRYVVID 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 515 EVHLLhedRGpVLESIVA----RTLRQVESTQSMIRILGLSATLPNYLDVA---------------------TFLHVNPY 569
Cdd:COG1205 188 EAHTY---RG-VFGSHVAnvlrRLRRICRHYGSDPQFILASATIGNPAEHAerltgrpvtvvdedgsprgerTFVLWNPP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 570 IglfYFDGRFRPVPLgqtflgikstnkmqqlnnmdEVCYesVLKQ-VKAGHQVMVFVHARNATVRTAMSLIERAKNsgqi 648
Cdd:COG1205 264 L---VDDGIRRSALA--------------------EAAR--LLADlVREGLRTLVFTRSRRGAELLARYARRALRE---- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 649 scflptegPEYGHALkqvqksrnkqvrelfsdgfSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPA-HAVV 727
Cdd:COG1205 315 --------PDLADRV-------------------AAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVV 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1720362714 728 IKGtqiYAAKRGSFVdlgildvmQIFGRAGRPQFDkfGEGIIITTHDKLSHYL 780
Cdd:COG1205 368 LAG---YPGTRASFW--------QQAGRAGRRGQD--SLVVLVAGDDPLDQYY 407
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
1249-1564 |
2.40e-16 |
|
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: 85.68 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1249 LLGAPTGSGKTVAAELAIFRVFNKYPTSK-----AVYIAPLKALVR----------ERMdDWKIRIEEKlgkkvielTGD 1313
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKekglhTLYITPLRALAVdiarnlqapiEEL-GLPIRVETR--------TGD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1314 VTPDMKSIAKA---DLIVTTPEkwdgvsrSWQ-------NRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNFISSH 1382
Cdd:TIGR04121 103 TSSSERARQRKkppDILLTTPE-------SLAlllsypdAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1383 tekpVRIVGLSTALANARDLADWLnikqMGLFNFRPSV------RPVPLEV----HIQGFP-GQHYCPRMASmnkPAFQA 1451
Cdd:TIGR04121 176 ----LRRWGLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISllpeSEERFPwAGHLGLRALP---EVYAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1452 IRSHspaKPVLIFVSSRRQTRLTALELIAFLAteedpkqwlnmdeqemdniigtvrDSNLKltlafgIGMHHAGLHERDR 1531
Cdd:TIGR04121 245 IDQA---RTTLVFTNTRSQAELWFQALWEANP------------------------EFALP------IALHHGSLDREQR 291
|
330 340 350
....*....|....*....|....*....|....
gi 1720362714 1532 KTVEELFVNCKVQVLIATSTLAWGVNF-PAHLVI 1564
Cdd:TIGR04121 292 RWVEAAMAAGRLRAVVCTSSLDLGVDFgPVDLVI 325
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
1247-1393 |
6.25e-16 |
|
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: 76.67 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDdwKIRIEEKLGKKVIELTGDVTP---DMKSIAK 1323
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKG-KKVLVLVPTKALALQTAE--RLRELFGPGIRVAVLVGGSSAeerEKNKLGD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720362714 1324 ADLIVTTPEKWDGVSRSwQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTnfissHTEKPVRIVGLS 1393
Cdd:cd00046 80 ADIIIATPDMLLNLLLR-EDRLFLKDLKLIIVDEAHaLLIDSRGALILDLAVRK-----AGLKNAQVILLS 144
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
396-773 |
2.87e-15 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 82.07 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 396 ENMLICAPTGAGKTNIAMLTILHEIRQHFHQGViKKNEFKIVYVAPMKALA-----------AEMTNYFSKRLEPLGIVV 464
Cdd:COG1201 40 ESTLLIAPTGSGKTLAAFLPALDELARRPRPGE-LPDGLRVLYISPLKALAndiernlraplEEIGEAAGLPLPEIRVGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 465 KelTGDMqlSKSEilRTQM-------LVTTPE---------KWdvvtRKSVGDvalsqiVKLLILDEVHLLHED-RGPVL 527
Cdd:COG1201 119 R--TGDT--PASE--RQRQrrrpphiLITTPEslallltspDA----RELLRG------VRTVIVDEIHALAGSkRGVHL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 528 ESIVARtLRQVeSTQSMIRIlGLSATLPNYLDVATFLhvnpyIGlfyfDGRFRPV--------------------PLGQT 587
Cdd:COG1201 183 ALSLER-LRAL-APRPLQRI-GLSATVGPLEEVARFL-----VG----YEDPRPVtivdagagkkpdlevlvpveDLIER 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 588 FLGIKSTNKMQqlnnmdevcYESVLKQVKAGHQVMVFVHARNATVRTAMSLIERAKnsgqiscflptEGPEyghalkqvq 667
Cdd:COG1201 251 FPWAGHLWPHL---------YPRVLDLIEAHRTTLVFTNTRSQAERLFQRLNELNP-----------EDAL--------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 668 ksrnkQVRelfsdgfsIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtQIYAAK---RGsfvdl 744
Cdd:COG1201 302 -----PIA--------AHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVI---QVGSPKsvaRL----- 360
|
410 420
....*....|....*....|....*....
gi 1720362714 745 gildvMQIFGRAGRpQFDKFGEGIIITTH 773
Cdd:COG1201 361 -----LQRIGRAGH-RVGEVSKGRLVPTH 383
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
391-759 |
3.22e-15 |
|
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: 81.83 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 391 AYNTNENMLICAPTGAGKTNIAMLTILHEIrqhFHQGVIKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLG--IVVKELT 468
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSLIDL---AGPEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGlpIRVETRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 469 GDMQLSKSEILRTQM---LVTTPEKWDVVTrkSVGDVA-LSQIVKLLILDEVH-LLHEDRGPVLESIVARtLRQvesTQS 543
Cdd:TIGR04121 101 GDTSSSERARQRKKPpdiLLTTPESLALLL--SYPDAArLFKDLRCVVVDEWHeLAGSKRGDQLELALAR-LRR---LAP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 544 MIRILGLSATLPNyLDVA--TFLHVNPYIGLFYFDGRFRPVPL-------GQTF-----LGIKStnkmqqlnnmdevcYE 609
Cdd:TIGR04121 175 GLRRWGLSATIGN-LEEArrVLLGVGGAPAVLVRGKLPKAIEVisllpesEERFpwaghLGLRA--------------LP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 610 SVLKQVKAGHQVMVFVHARNATVRTAMSLIEraknsgqiscflptegpeyghalkqvqksrnkqVRELFSDGFSIHHAGM 689
Cdd:TIGR04121 240 EVYAEIDQARTTLVFTNTRSQAELWFQALWE---------------------------------ANPEFALPIALHHGSL 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720362714 690 LRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtQIYAAKrgsfvdlGILDVMQIFGRAG-RP 759
Cdd:TIGR04121 287 DREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSPK-------GVARLLQRAGRSNhRP 347
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
357-761 |
3.68e-15 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 81.48 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 357 EEKPVYIKDLDEVGQlaFKGM-----KRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIrqhfhqgviKK 431
Cdd:COG1202 184 EVDTVPVDDLDLPPE--LKDLlegrgEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAGIKNA---------LE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 432 NEFKIVYVAPMKALAAEMTNYFSKRLEPlGIVVKELTGDMQLSKSE---ILRTQMLVTTPEKWDVVTR--KSVGDVALsq 506
Cdd:COG1202 253 GKGKMLFLVPLVALANQKYEDFKDRYGD-GLDVSIRVGASRIRDDGtrfDPNADIIVGTYEGIDHALRtgRDLGDIGT-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 507 ivklLILDEVHLLHE-DRGPVLESIVARtLRQV-ESTQsmirILGLSATLPNYLDVATFLHVNpyigLFYFDGRfrPVPL 584
Cdd:COG1202 330 ----VVIDEVHMLEDpERGHRLDGLIAR-LKYYcPGAQ----WIYLSATVGNPEELAKKLGAK----LVEYEER--PVPL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 585 GQTFLGIKSTNKMQQLNNMDEVCYESVLKQvkaGH--QVMVFVHARnatvrtamslieraKNSGQISCFLPTEGPEYgha 662
Cdd:COG1202 395 ERHLTFADGREKIRIINKLVKREFDTKSSK---GYrgQTIIFTNSR--------------RRCHEIARALGYKAAPY--- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 663 lkqvqksrnkqvrelfsdgfsihHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVikgtqiyaakrgsFV 742
Cdd:COG1202 455 -----------------------HAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVI-------------FD 498
|
410 420
....*....|....*....|....*.
gi 1720362714 743 DL--GI--LDV---MQIFGRAGRPQF 761
Cdd:COG1202 499 SLamGIewLSVqefHQMLGRAGRPDY 524
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1517-1596 |
8.45e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 71.09 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1517 FGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryVDFPITDVLQMMGRAGR 1595
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVII-----YD------LPWSPASYIQRIGRAGR 80
|
.
gi 1720362714 1596 P 1596
Cdd:smart00490 81 A 81
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1192-1638 |
2.27e-14 |
|
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: 79.11 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1192 HLILPERHPPHTELLD-LQPLPITALGCKAYEALYnfSHfnpvQTQIFHtLYHTDCNVLLGAPTGSGKTVAAELAIFRVF 1270
Cdd:COG1205 24 VRTIPAREARYAPWPDwLPPELRAALKKRGIERLY--SH----QAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1271 NKYPTSKAVYIAPLKALVRERMDDWKiRIEEKLGK--KVIELTGDVTPDMKS--IAKADLIVTTP-----------EKWd 1335
Cdd:COG1205 97 LEDPGATALYLYPTKALARDQLRRLR-ELAEALGLgvRVATYDGDTPPEERRwiREHPDIVLTNPdmlhygllphhTRW- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1336 gvSRSWQNRSYVqqvnilIIDEIHLLgeeRGpvleV-------IVSRTNFISSHTEKPVRIVGLSTALANARDLAdwlni 1408
Cdd:COG1205 175 --ARFFRNLRYV------VIDEAHTY---RG----VfgshvanVLRRLRRICRHYGSDPQFILASATIGNPAEHA----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1409 kqMGLFNfrpsvRPVpleVHIQG----FPGQHycprMASMNKPAFQAIRSHSPAK--------------PVLIFVSSRRQ 1470
Cdd:COG1205 235 --ERLTG-----RPV---TVVDEdgspRGERT----FVLWNPPLVDDGIRRSALAeaarlladlvreglRTLVFTRSRRG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1471 TRLTALELIAFLATEEDPKQwlnmdeqemdniigtvrdsnlkltlafgIGMHHAGLHERDRKTVEELFVNCKVQVLIATS 1550
Cdd:COG1205 301 AELLARYARRALREPDLADR----------------------------VAAYRAGYLPEERREIERGLRSGELLGVVSTN 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1551 TLAWGVNFPA-HLVIIKGteyydgktrryvdFP--ITDVLQMMGRAGRpqfDDQGKAVILV--HDIKKDFYKK---FLYE 1622
Cdd:COG1205 353 ALELGIDIGGlDAVVLAG-------------YPgtRASFWQQAGRAGR---RGQDSLVVLVagDDPLDQYYVRhpeELFE 416
|
490 500
....*....|....*....|.
gi 1720362714 1623 PfPVESSLLG-----VLSDHL 1638
Cdd:COG1205 417 R-PPEAAVIDpdnpyVLAPHL 436
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
395-556 |
3.02e-14 |
|
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: 73.17 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNI---AMLTILHEirqhfhqgvikKNEFKIVYVAPMKAL----AAEMTNYFSKRLEPLGIVV-KE 466
Cdd:cd18025 16 RESALIVAPTSSGKTFIsyyCMEKVLRE-----------SDDGVVVYVAPTKALvnqvVAEVYARFSKKYPPSGKSLwGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 467 LTGDMQLskSEILRTQMLVTTPEKWDVVTRkSVGDVALSQIVKLLILDEVHLL-HEDRGPVLESIVArtlrqvestqsMI 545
Cdd:cd18025 85 FTRDYRH--NNPMNCQVLITVPECLEILLL-SPHNASWVPRIKYVIFDEIHSIgQSEDGAVWEQLLL-----------LI 150
|
170
....*....|...
gi 1720362714 546 R--ILGLSATLPN 556
Cdd:cd18025 151 PcpFLALSATIGN 163
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
395-553 |
8.80e-14 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 70.51 E-value: 8.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNIAMLTILHEIRqhfhqgvikKNEFKIVYVAPMKALAAEMTNYFsKRLEPLGIVVKELTGDM--- 471
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLL---------KKGKKVLVLVPTKALALQTAERL-RELFGPGIRVAVLVGGSsae 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 472 QLSKSEILRTQMLVTTPEKwdvVTRKSVGDVALSQI-VKLLILDEVH-LLHEDRGPVLESIVARTLRQVEStqsmiRILG 549
Cdd:cd00046 71 EREKNKLGDADIIIATPDM---LLNLLLREDRLFLKdLKLIIVDEAHaLLIDSRGALILDLAVRKAGLKNA-----QVIL 142
|
....
gi 1720362714 550 LSAT 553
Cdd:cd00046 143 LSAT 146
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
396-553 |
7.75e-13 |
|
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: 69.38 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 396 ENMLICAPTGAGKTNIAMLtilheIRQHFHQGVIKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLSK 475
Cdd:cd17927 18 KNTIICLPTGSGKTFVAVL-----ICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 476 S---EILRTQMLVTTPEKWdVVTRKSVGDVALSqIVKLLILDEVHllHEDRGPVLESIVARTLRQ-VESTQSMIRILGLS 551
Cdd:cd17927 93 SveqIVESSDVIIVTPQIL-VNDLKSGTIVSLS-DFSLLVFDECH--NTTKNHPYNEIMFRYLDQkLGSSGPLPQILGLT 168
|
..
gi 1720362714 552 AT 553
Cdd:cd17927 169 AS 170
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
681-759 |
1.62e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.93 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 681 GFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVVIKGtqiyaakrgsfVDLGILDVMQIFGRAGRP 759
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASYIQRIGRAGRA 81
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1252-1594 |
3.74e-11 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 68.80 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1252 APTGSGKTVAAEL-AIFRVF----------NKYPTSKAVYIAPLKALVRERMDDWKIRIE------EKLGKKVIELT-GD 1313
Cdd:PRK09751 3 APTGSGKTLAAFLyALDRLFreggedtreaHKRKTSRILYISPIKALGTDVQRNLQIPLKgiaderRRRGETEVNLRvGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1314 VTPDMKSIAKA-------DLIVTTPEKWDGVSRSwQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNFIsSHTek 1385
Cdd:PRK09751 83 RTGDTPAQERSkltrnppDILITTPESLYLMLTS-RARETLRGVETVIIDEVHaVAGSKRGAHLALSLERLDAL-LHT-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1386 PVRIVGLSTALANARDLADWLNIKQMGLFNFRPSVR--------PVPLEVHIQGFPGQH----YCPRMASMnKPAFQA-- 1451
Cdd:PRK09751 159 SAQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRhpqirivvPVANMDDVSSVASGTgedsHAGREGSI-WPYIETgi 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1452 IRSHSPAKPVLIFVSSRRQT-RLTAL--ELIA--FLATEEDPKqwlnmDEQEMDNIIGTV--RDSNLKLTLAFGigmHHA 1524
Cdd:PRK09751 238 LDEVLRHRSTIVFTNSRGLAeKLTARlnELYAarLQRSPSIAV-----DAAHFESTSGATsnRVQSSDVFIARS---HHG 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720362714 1525 GLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKgteyydgktrryVDFP--ITDVLQMMGRAG 1594
Cdd:PRK09751 310 SVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQ------------VATPlsVASGLQRIGRAG 369
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
1248-1406 |
6.85e-11 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350782 [Multi-domain] Cd Length: 205 Bit Score: 64.00 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1248 VLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDwkirIEEKLGKkVIELTGDVT--PDmksiakAD 1325
Cdd:cd18024 50 VLVSAHTSAGKTVVAEYAIAQSLRD--KQRVIYTSPIKALSNQKYRE----LQEEFGD-VGLMTGDVTinPN------AS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1326 LIVTTPEkwdgVSRS--WQNRSYVQQVNILIIDEIHLLGE-ERGPVLEvivsRTNFISSHTekpVRIVGLSTALANARDL 1402
Cdd:cd18024 117 CLVMTTE----ILRSmlYRGSEIMREVAWVIFDEIHYMRDkERGVVWE----ETIILLPDK---VRYVFLSATIPNARQF 185
|
....
gi 1720362714 1403 ADWL 1406
Cdd:cd18024 186 AEWI 189
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
1236-1611 |
3.03e-10 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 65.43 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1236 QIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTskaVYIAPLKALVRermdDWKIRIEEKLGKkvIELTGDVT 1315
Cdd:COG1061 91 ALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV---LVLVPRRELLE----QWAEELRRFLGD--PLAGGGKK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1316 PDmksiaKADLIVTTpekWDGVSRSWQNRSYVQQVNILIIDEIHLLGeerGPVLEVIVSRTNfisshtekPVRIVGLS-T 1394
Cdd:COG1061 162 DS-----DAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHAG---APSYRRILEAFP--------AAYRLGLTaT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1395 AlanardladwlnikqmglfnFRPSVRPVPLEVhiqgFPGQHYcprmasmNKPAFQAIRSHSPAKPVLIfvssRRQTRLT 1474
Cdd:COG1061 223 P--------------------FRSDGREILLFL----FDGIVY-------EYSLKEAIEDGYLAPPEYY----GIRVDLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1475 AlELIAFLATEEDPKQWLNMDEQEMDNIIGTVRDSNLKL--TLAFGIGMHHA-------------------GLHERDRKT 1533
Cdd:COG1061 268 D-ERAEYDALSERLREALAADAERKDKILRELLREHPDDrkTLVFCSSVDHAealaellneagiraavvtgDTPKKEREE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1534 VEELFVNCKVQVLIATSTLAWGVNFPA--HLVIIKGTeyydgKTRRYvdfpitdVLQMMGRAGRPqfdDQGKAVILVHDI 1611
Cdd:COG1061 347 ILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPT-----GSPRE-------FIQRLGRGLRP---APGKEDALVYDF 411
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
395-582 |
3.44e-10 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 65.29 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNIAMLTILHEIrqhFHQGVIKKNEFKI--VYVAPMKALAAEMtnyfsKR--LEPL-GI--VVKEL 467
Cdd:PRK13767 47 GKNVLISSPTGSGKTLAAFLAIIDEL---FRLGREGELEDKVycLYVSPLRALNNDI-----HRnlEEPLtEIreIAKER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 468 ------------TGDM-QLSKSEILRT--QMLVTTPEKWDVVT-----RKSVGDvalsqiVKLLILDEVHLLHED-RGPV 526
Cdd:PRK13767 119 geelpeirvairTGDTsSYEKQKMLKKppHILITTPESLAILLnspkfREKLRT------VKWVIVDEIHSLAENkRGVH 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720362714 527 LesivARTLRQVES--TQSMIRIlGLSATLPNYLDVATFLhvnpyiGLFYFDGRFRPV 582
Cdd:PRK13767 193 L----SLSLERLEElaGGEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDC 239
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1248-1407 |
3.87e-10 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350783 [Multi-domain] Cd Length: 192 Bit Score: 61.23 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1248 VLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLGKKVIELTGDVTPD--MKSIAKAD 1325
Cdd:cd18025 19 ALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYPPSGKSLWGVFTRDyrHNNPMNCQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1326 LIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIHLLG-EERGPVLEVIVsrtnfisshTEKPVRIVGLSTALANARDLAD 1404
Cdd:cd18025 99 VLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGqSEDGAVWEQLL---------LLIPCPFLALSATIGNPQKFHE 169
|
...
gi 1720362714 1405 WLN 1407
Cdd:cd18025 170 WLQ 172
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1231-1414 |
4.01e-10 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 61.13 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1231 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIfrVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEklgkkVIEL 1310
Cdd:cd18027 10 DVFQKQAILHLEAGD-SVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGD-----VGLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1311 TGDVT--PDMKSiakadLIVTTPekwdgVSRS--WQNRSYVQQVNILIIDEIHLLGE-ERGPVLEVIVSrtnFISSHtek 1385
Cdd:cd18027 82 TGDVQlnPEASC-----LIMTTE-----ILRSmlYNGSDVIRDLEWVIFDEVHYINDaERGVVWEEVLI---MLPDH--- 145
|
170 180 190
....*....|....*....|....*....|
gi 1720362714 1386 pVRIVGLSTALANARDLADWLN-IKQMGLF 1414
Cdd:cd18027 146 -VSIILLSATVPNTVEFADWIGrIKKKNIY 174
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1511-1595 |
7.64e-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: 57.99 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1511 LKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryVDFPITDVLQM 1589
Cdd:pfam00271 33 LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YD------LPWNPASYIQR 101
|
....*.
gi 1720362714 1590 MGRAGR 1595
Cdd:pfam00271 102 IGRAGR 107
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
396-561 |
9.36e-10 |
|
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: 59.91 E-value: 9.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 396 ENMLICAPTGAGKTNIAMLTILHEIrqhfhqgvIKKNEFKIVYVAPMKALAAEMTNYFSKRLEPL--GIVVKELTGDMQL 473
Cdd:cd17923 16 RSVVVTTGTASGKSLCYQLPILEAL--------LRDPGSRALYLYPTKALAQDQLRSLRELLEQLglGIRVATYDGDTPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 474 SKSEILRTQ---MLVTTPEKWDV-VTRKSVGDVALSQIVKLLILDEVHLLhedRGpVLESIVA----RTLRQVESTQSMI 545
Cdd:cd17923 88 EERRAIIRNpprILLTNPDMLHYaLLPHHDRWARFLRNLRYVVLDEAHTY---RG-VFGSHVAlllrRLRRLCRRYGADP 163
|
170
....*....|....*.
gi 1720362714 546 RILGLSATLPNYLDVA 561
Cdd:cd17923 164 QFILTSATIGNPAEHA 179
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1227-1393 |
1.43e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 63.37 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1227 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAI----FRVFNK-------YptskAVYIAPLKAL---VRERM 1292
Cdd:PRK13767 30 FGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREgeledkvY----CLYVSPLRALnndIHRNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1293 DDWKIRIEEKLGKKVIEL--------TGDVTPDMKS--------IakadLIvTTPEKWDGVSRSWQNRSYVQQVNILIID 1356
Cdd:PRK13767 105 EEPLTEIREIAKERGEELpeirvairTGDTSSYEKQkmlkkpphI----LI-TTPESLAILLNSPKFREKLRTVKWVIVD 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720362714 1357 EIHLLGE-ERGPVLEVIVSRTNFISSHteKPVRIvGLS 1393
Cdd:PRK13767 180 EIHSLAEnKRGVHLSLSLERLEELAGG--EFVRI-GLS 214
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
1247-1403 |
2.06e-09 |
|
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: 59.14 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVR---ERMDDWKIRIEEKLgkKVIELTGDvTP--DMKSI 1321
Cdd:cd17923 17 SVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQdqlRSLRELLEQLGLGI--RVATYDGD-TPreERRAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1322 AK--ADLIVTTP-----------EKWDGVSRSWQnrsYVqqvnilIIDEIH----LLGEERGPVLEVIVSRTNFISSHte 1384
Cdd:cd17923 94 IRnpPRILLTNPdmlhyallphhDRWARFLRNLR---YV------VLDEAHtyrgVFGSHVALLLRRLRRLCRRYGAD-- 162
|
170
....*....|....*....
gi 1720362714 1385 kpVRIVGLSTALANARDLA 1403
Cdd:cd17923 163 --PQFILTSATIGNPAEHA 179
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
400-757 |
2.46e-09 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 63.02 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 400 ICAPTGAGKTniaMLTILHEIRQHFHQGVI------KKNEFKIVYVAPMKALAAEMTNYFSKRLEPLG------------ 461
Cdd:PRK09751 1 VIAPTGSGKT---LAAFLYALDRLFREGGEdtreahKRKTSRILYISPIKALGTDVQRNLQIPLKGIAderrrrgetevn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 462 IVVKELTGDMQLS-KSEILRT--QMLVTTPEKWDVV----TRKSVGDvalsqiVKLLILDEVHLLH-EDRGPVLesivAR 533
Cdd:PRK09751 78 LRVGIRTGDTPAQeRSKLTRNppDILITTPESLYLMltsrARETLRG------VETVIIDEVHAVAgSKRGAHL----AL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 534 TLRQVEST--QSMIRIlGLSATLPNYLDVATFLhvnpyiglfyfdGRFRPV----PLGQTFLGIKSTNKMQQLNNMDEVC 607
Cdd:PRK09751 148 SLERLDALlhTSAQRI-GLSATVRSASDVAAFL------------GGDRPVtvvnPPAMRHPQIRIVVPVANMDDVSSVA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 608 YE-------------------SVLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNSGQISCFLPTEGPEY----GHALK 664
Cdd:PRK09751 215 SGtgedshagregsiwpyietGILDEVLRHRSTIVFTNSRGLAEKLTARLNELYAARLQRSPSIAVDAAHFestsGATSN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 665 QVQKSRNKQVRElfsdgfsiHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtQIYAAkrgsfvdL 744
Cdd:PRK09751 295 RVQSSDVFIARS--------HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVI---QVATP-------L 356
|
410
....*....|...
gi 1720362714 745 GILDVMQIFGRAG 757
Cdd:PRK09751 357 SVASGLQRIGRAG 369
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
384-552 |
4.04e-09 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 58.43 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 384 QSIVFETAynTNENMLICAPTGAGKTNIAMLTILHEIRQhfhQGVIKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLgiv 463
Cdd:cd18034 7 QLELFEAA--LKRNTIVVLPTGSGKTLIAVMLIKEMGEL---NRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHTDLK--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 464 VKELTGDMQLS-------KSEILRTQMLVTTPEKW-DVVTRksvGDVALSQIvKLLILDEVHL---LHEDRGpvlesiVA 532
Cdd:cd18034 79 VGEYSGEMGVDkwtkerwKEELEKYDVLVMTAQILlDALRH---GFLSLSDI-NLLIFDECHHatgDHPYAR------IM 148
|
170 180
....*....|....*....|
gi 1720362714 533 RTLRQVESTQSMIRILGLSA 552
Cdd:cd18034 149 KEFYHLEGRTSRPRILGLTA 168
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1247-1359 |
1.41e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 56.14 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLgKKVIELTGDvtPDMKSIAKADL 1326
Cdd:pfam04851 25 RGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYV-EIGEIISGD--KKDESVDDNKI 101
|
90 100 110
....*....|....*....|....*....|...
gi 1720362714 1327 IVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIH 1359
Cdd:pfam04851 102 VVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
395-561 |
1.54e-08 |
|
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: 57.07 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNIAMLTILHEIRqhfhqgvikkNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVvkelTGDMQLS 474
Cdd:cd18024 47 NESVLVSAHTSAGKTVVAEYAIAQSLR----------DKQRVIYTSPIKALSNQKYRELQEEFGDVGLM----TGDVTIN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 475 KS--------EILRTqMLVTTPEkwdvVTRKsvgdvalsqiVKLLILDEVHLLHE-DRGPVLE-SIVArtlrqvesTQSM 544
Cdd:cd18024 113 PNasclvmttEILRS-MLYRGSE----IMRE----------VAWVIFDEIHYMRDkERGVVWEeTIIL--------LPDK 169
|
170
....*....|....*..
gi 1720362714 545 IRILGLSATLPNYLDVA 561
Cdd:cd18024 170 VRYVFLSATIPNARQFA 186
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
395-515 |
1.76e-08 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 56.44 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNIAMLTILHEIRQHFHQGvikknEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLS 474
Cdd:cd17957 27 GRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK-----GLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEAK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1720362714 475 KSE----ILRTQMLVTTPEKwdVVTRKSVGDVALSQiVKLLILDE 515
Cdd:cd17957 102 AKDgpksITKYDILVSTPLR--LVFLLKQGPIDLSS-VEYLVLDE 143
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
395-517 |
3.79e-08 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 58.59 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNIAMLTILHeirqhfhqgVIKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLS 474
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE---------RLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1720362714 475 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivkLLILDEVH 517
Cdd:COG1111 88 KRKELweKARIIVATPQviENDLIAgRIDLDDVS------LLIFDEAH 129
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
1247-1360 |
5.17e-08 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 55.13 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKYP---TSKAVYIAPLKALVRERMDDWKiRIEEKLGKKVIELTGDVTPDM---KS 1320
Cdd:cd17927 19 NTIICLPTGSGKTFVAVLICEHHLKKFPagrKGKVVFLANKVPLVEQQKEVFR-KHFERPGYKVTGLSGDTSENVsveQI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1720362714 1321 IAKADLIVTTP-------EKWDGVSRSwqnrsyvqQVNILIIDEIHL 1360
Cdd:cd17927 98 VESSDVIIVTPqilvndlKSGTIVSLS--------DFSLLVFDECHN 136
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
1252-1378 |
5.22e-08 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 53.85 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1252 APTGSGKTVAAELAIFRVFNKyptsKAVYIAPLKALVrermDDWKIRIEEKLGKKVI-ELTGDVTpdmKSIAKADLIVTT 1330
Cdd:cd17926 25 LPTGSGKTLTALALIAYLKEL----RTLIVVPTDALL----DQWKERFEDFLGDSSIgLIGGGKK---KDFDDANVVVAT 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720362714 1331 PEkwdgvSRSWQN---RSYVQQVNILIIDEIHLLGeerGPVLEVIVSRTNF 1378
Cdd:cd17926 94 YQ-----SLSNLAeeeKDLFDQFGLLIVDEAHHLP---AKTFSEILKELNA 136
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
339-763 |
6.96e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 57.73 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 339 KLYEEVRIPYGEPMPVGFEEKPVYIKDLDEVGQLAFKGMKRLNRIQSIVFETAYNT----NENMLICAPTGAGKTNIAML 414
Cdd:COG1061 40 LAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQQEALEALLAAlergGGRGLVVAPTGTGKTVLALA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 415 TILHEIRQHfhqgvikknefKIVYVAPMKAL----AAEMTNYFSKRLEPLGivVKELTGDmqlskseilrtqMLVTTpek 490
Cdd:COG1061 120 LAAELLRGK-----------RVLVLVPRRELleqwAEELRRFLGDPLAGGG--KKDSDAP------------ITVAT--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 491 WDVVTRKSVGDvALSQIVKLLILDEVHLLhedrgpvlesiVARTLRQVESTQSMIRILGLSATlPNYLDVATflhvnpyI 570
Cdd:COG1061 172 YQSLARRAHLD-ELGDRFGLVIIDEAHHA-----------GAPSYRRILEAFPAAYRLGLTAT-PFRSDGRE-------I 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 571 GLFYFDG-------------------RFRPVPLGQTFLGIKSTNKMQQLNN--------MDEVCyESVLKQVKAGHQVMV 623
Cdd:COG1061 232 LLFLFDGivyeyslkeaiedgylappEYYGIRVDLTDERAEYDALSERLREalaadaerKDKIL-RELLREHPDDRKTLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 624 FVharnATVRTAmslieraknsgqiscflptegpeyghalkqvqksrnKQVRELFSD-GFSIH--HAGMLRQDRNLVENL 700
Cdd:COG1061 311 FC----SSVDHA------------------------------------EALAELLNEaGIRAAvvTGDTPKKEREEILEA 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720362714 701 FSNGHIKVLVCTATLAWGVNLPAHAVVikgtqIYAAKRGSfvdLGILdvMQIFGRAGRPQFDK 763
Cdd:COG1061 351 FRDGELRILVTVDVLNEGVDVPRLDVA-----ILLRPTGS---PREF--IQRLGRGLRPAPGK 403
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
397-517 |
8.99e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.58 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 397 NMLICAPTGAGKTNIAMLTILheirqhfhqGVIKKNEFKIVYVAPMKALAAEMTNYFSK--RLEPLGIVVkeLTGDMQLS 474
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIA---------ERLHKKGGKVLILAPTKPLVEQHAEFFRKflNIPEEKIVV--FTGEVSPE 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1720362714 475 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivkLLILDEVH 517
Cdd:PRK13766 100 KRAELweKAKVIVATPQviENDLIAgRISLEDVS------LLIFDEAH 141
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
394-554 |
9.33e-08 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350831 [Multi-domain] Cd Length: 202 Bit Score: 54.44 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 394 TNENMLICAPTGAGKTNIAMLTILHEIRQhFHQGviKKNefKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDMQL 473
Cdd:cd18073 16 KGKNTIICAPTGCGKTFVSLLICEHHLKK-FPQG--QKG--KVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGATAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 474 SKSE---ILRTQMLVTTPEKwdVVTRKSVGDVALSQIVKLLILDEVHllHEDRGPVLESIVARTLRQ--VESTQSMIRIL 548
Cdd:cd18073 91 NVPVeqiIENNDIIILTPQI--LVNNLKKGTIPSLSIFTLMIFDECH--NTSGNHPYNMIMFRYLDQklGGSSGPLPQII 166
|
....*.
gi 1720362714 549 GLSATL 554
Cdd:cd18073 167 GLTASV 172
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
375-566 |
1.59e-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: 54.29 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 375 KGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTILHEIRQHFHQGVIKKNEFKIVYVAPMKALAAEMTNYFS 454
Cdd:cd17948 8 QGITKPTTVQKQGIPSILR-GRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNAPRGLVITPSRELAEQIGSVAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 455 KRLEPLGIVVKELTGDMqlSKSEILRTQM-----LVTTPEK-WDVVTRksvGDVALSQiVKLLILDEVH-LLHEDRGPVL 527
Cdd:cd17948 87 SLTEGLGLKVKVITGGR--TKRQIRNPHFeevdiLVATPGAlSKLLTS---RIYSLEQ-LRHLVLDEADtLLDDSFNEKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720362714 528 ESIVART---LRQVESTQSMIR---ILGLSATLPNYL--------DVATFLHV 566
Cdd:cd17948 161 SHFLRRFplaSRRSENTDGLDPgtqLVLVSATMPSGVgevlskviDVDSIETV 213
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
378-712 |
1.91e-07 |
|
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: 56.24 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 378 KRLNRIQSIVFETAYNTNEN----MLICAPTGAGKTNIAMLTILHEIRQHFHQGVIkknefkivYVAPMKAL----AAEM 449
Cdd:COG1203 126 TPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKHGGRRII--------YALPFTSIinqtYDRL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 450 TNYF--------SKRLEPLGIVVKELTGDMQLSK--SEILRTQMLVTTPekwD-----VVTRKSvgdvalSQIVKL---- 510
Cdd:COG1203 198 RDLFgedvllhhSLADLDLLEEEEEYESEARWLKllKELWDAPVVVTTI---DqlfesLFSNRK------GQERRLhnla 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 511 ---LILDEVHLL-HEDRGPVLesivaRTLRQVESTQSmiRILGLSATLPNYLDVATF----LHVNPYIGLFYFDGRFRpv 582
Cdd:COG1203 269 nsvIILDEVQAYpPYMLALLL-----RLLEWLKNLGG--SVILMTATLPPLLREELLeayeLIPDEPEELPEYFRAFV-- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 583 plgqtflgiKSTNKMQQLNNMDEVCYESVLKQVKAGHQVMVFVharnATVRTAMSLieraknsgqiscflptegpeYgha 662
Cdd:COG1203 340 ---------RKRVELKEGPLSDEELAELILEALHKGKSVLVIV----NTVKDAQEL--------------------Y--- 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720362714 663 lkqvqksrnKQVRELFSDGFSIH-HAGMLRQDRNLVEN----LFSNGHIKVLVCT 712
Cdd:COG1203 384 ---------EALKEKLPDEEVYLlHSRFCPADRSEIEKeikeRLERGKPCILVST 429
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1203-1421 |
2.11e-07 |
|
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: 55.86 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1203 TELLDLQPLPITALGCKAYEALYNF-----SHFNPVQTQIFHTLYHTDCN----VLLGAPTGSGKTVAAELAIFRVFNKY 1273
Cdd:COG1203 96 SANFDMARQALDHLLAERLERLLPKkskprTPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKH 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1274 PTSKAVYIAPLKALVrERMDDwkiRIEEKLGKKVIELTGDVTPDMKSIAK-----------------ADLIVTTPEK-WD 1335
Cdd:COG1203 176 GGRRIIYALPFTSII-NQTYD---RLRDLFGEDVLLHHSLADLDLLEEEEeyesearwlkllkelwdAPVVVTTIDQlFE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1336 GV--SRSWQNRSYVQQVN-ILIIDEIHLLGEERGPVLEvivsrtNFISSHTEKPVRIVgLSTA---------LANARDLA 1403
Cdd:COG1203 252 SLfsNRKGQERRLHNLANsVIILDEVQAYPPYMLALLL------RLLEWLKNLGGSVI-LMTAtlppllreeLLEAYELI 324
|
250
....*....|....*...
gi 1720362714 1404 DWLNIKQMGLFNFRPSVR 1421
Cdd:COG1203 325 PDEPEELPEYFRAFVRKR 342
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
384-553 |
2.78e-07 |
|
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: 52.71 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 384 QSIVFETAYNtneNMLICAPTGAGKTNIAMLTILHEIRQhFHQGvikknefKIVYVAPMKALAAEMTNYFSKRLE-PLGI 462
Cdd:cd18033 8 FTIVQKALFQ---NTLVALPTGLGKTFIAAVVMLNYYRW-FPKG-------KIVFMAPTKPLVSQQIEACYKITGiPSSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 463 VVkELTGDMQLSK-SEILRT-QMLVTTPEkwdVVTRKSVGDVALSQIVKLLILDEVhllHEDRGPVLESIVARTLRQVES 540
Cdd:cd18033 77 TA-ELTGSVPPTKrAELWASkRVFFLTPQ---TLENDLKEGDCDPKSIVCLVIDEA---HRATGNYAYCQVVRELMRYNS 149
|
170
....*....|...
gi 1720362714 541 TqsmIRILGLSAT 553
Cdd:cd18033 150 H---FRILALTAT 159
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
1247-1399 |
3.07e-07 |
|
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: 53.04 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRV-----FNKYPTSKAVYIAPLKALVRERMddwkIRIEEKLGKKVIELTGDVTPDMKS- 1320
Cdd:cd18034 18 NTIVVLPTGSGKTLIAVMLIKEMgelnrKEKNPKKRAVFLVPTVPLVAQQA----EAIRSHTDLKVGEYSGEMGVDKWTk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1321 ------IAKADLIVTTPEkwdgVSRSWQNRSYVQ--QVNILIIDEIHLLGEERgpVLEVIVSRTNFISSHTEKPvRIVGL 1392
Cdd:cd18034 94 erwkeeLEKYDVLVMTAQ----ILLDALRHGFLSlsDINLLIFDECHHATGDH--PYARIMKEFYHLEGRTSRP-RILGL 166
|
....*..
gi 1720362714 1393 STALANA 1399
Cdd:cd18034 167 TASPVNG 173
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
1247-1373 |
4.01e-07 |
|
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: 52.29 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDdwkiRIEEKLGK-----KVIELTGDVTPDM--K 1319
Cdd:cd17930 3 LVILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINQMYE----RIREILGRlddedKVLLLHSKAALELleS 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362714 1320 SIAKADLIVTTPEKWDGVSRSWQNR----SYVQ------QVN------------ILIIDEIHLLGEER-GPVLEVIV 1373
Cdd:cd17930 79 DEEPDDDPVEAVDWALLLKRSWLAPivvtTIDQllesllKYKhferrlhglansVVVLDEVQAYDPEYmALLLKALL 155
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
396-564 |
4.54e-07 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 52.27 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 396 ENMLICAPTGAGKTNIAMLTIlheirqhfhqGVIKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIvvkeLTGDMQLS- 474
Cdd:cd18027 24 DSVFVAAHTSAGKTVVAEYAI----------ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGL----ITGDVQLNp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 475 -------KSEILRTqMLVTTPEkwdvVTRKsvgdvalsqiVKLLILDEVHLLHE-DRGPVLESIVARTLRQVestqsmiR 546
Cdd:cd18027 90 easclimTTEILRS-MLYNGSD----VIRD----------LEWVIFDEVHYINDaERGVVWEEVLIMLPDHV-------S 147
|
170
....*....|....*...
gi 1720362714 547 ILGLSATLPNYLDVATFL 564
Cdd:cd18027 148 IILLSATVPNTVEFADWI 165
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
372-568 |
4.55e-07 |
|
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: 52.44 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 372 LAFKGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTnIA-MLTILHEIRQhfhQGVIKKNEFKIVYVAPMKALA---A 447
Cdd:cd00268 5 LKKLGFEKPTPIQAQAIPLILS-GRDVIGQAQTGSGKT-LAfLLPILEKLLP---EPKKKGRGPQALVLAPTRELAmqiA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 448 EMTNYFSKrlePLGIVVKELTGDMQLSKSEIL---RTQMLVTTPEK-WDVVTRksvGDVALSQiVKLLILDEV-HLLHED 522
Cdd:cd00268 80 EVARKLGK---GTGLKVAAIYGGAPIKKQIEAlkkGPDIVVGTPGRlLDLIER---GKLDLSN-VKYLVLDEAdRMLDMG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720362714 523 RGPVLESIVARTLRQvesTQSMIrilgLSATLPNYLD--VATFLHvNP 568
Cdd:cd00268 153 FEEDVEKILSALPKD---RQTLL----FSATLPEEVKelAKKFLK-NP 192
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
396-559 |
5.17e-07 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 51.91 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 396 ENMLICAPTGAGKTNIAMLTILHEIRQHFHQGVIkknefkivYVAPMKALA----AEMTNYFSKRLEPLGIV-------V 464
Cdd:cd17930 2 GLVILEAPTGSGKTEAALLWALKLAARGGKRRII--------YALPTRATInqmyERIREILGRLDDEDKVLllhskaaL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 465 KELTGDMQLSKSEILRTQMLVTTPEKWD---VVT----------------RKSVGdvaLSQivKLLILDEVHLLhedrGP 525
Cdd:cd17930 74 ELLESDEEPDDDPVEAVDWALLLKRSWLapiVVTtidqllesllkykhfeRRLHG---LAN--SVVVLDEVQAY----DP 144
|
170 180 190
....*....|....*....|....*....|....
gi 1720362714 526 VLESIVARTLRQVESTQSmIRILGLSATLPNYLD 559
Cdd:cd17930 145 EYMALLLKALLELLGELG-GPVVLMTATLPALLR 177
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
396-555 |
9.17e-07 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 51.71 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 396 ENMLICAPTGAGKTNIAMLTILHEIRQHFHQGvikkNEFKIVYVAPMKALAAEMTNYFSKRLEPlGIVVKELTGDMQLSK 475
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAG----EKGRVVVLVNKVPLVEQQLEKFFKYFRK-GYKVTGLSGDSSHKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 476 S---EILRTQMLVTTPEKWDVVTRKSVGDVALS-QIVKLLILDEVHllHEDRGPVLESIVARTLRQ-VESTQSMIRILGL 550
Cdd:cd18036 93 SfgqIVKASDVIICTPQILINNLLSGREEERVYlSDFSLLIFDECH--HTQKEHPYNKIMRMYLDKkLSSQGPLPQILGL 170
|
....*
gi 1720362714 551 SATLP 555
Cdd:cd18036 171 TASPG 175
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
677-758 |
9.32e-07 |
|
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: 49.13 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 677 LFSDGFSI--HHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtqIYAAkrgsfvDLGILDVMQIFG 754
Cdd:pfam00271 34 LEKEGIKVarLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVI----NYDL------PWNPASYIQRIG 103
|
....
gi 1720362714 755 RAGR 758
Cdd:pfam00271 104 RAGR 107
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
608-758 |
1.20e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 49.96 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 608 YESVLKQVKAGHQVMVFVHARNATVRTAMSLIERAknsgqiscflptegPEYGHALKqvqksrnkqvrelfsdgFSIHHA 687
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELC--------------PDRVPPDF-----------------IALHHG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720362714 688 GMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIkgtQIYAAKrgsfvdlGILDVMQIFGRAGR 758
Cdd:cd18796 77 SLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVI---QIGSPK-------SVARLLQRLGRSGH 137
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
1230-1359 |
1.65e-06 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 50.40 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1230 FNPVQTQIFHtlyhtdcNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKiRIEEKLGKKVIE 1309
Cdd:cd18033 8 FTIVQKALFQ-------NTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACY-KITGIPSSQTAE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1720362714 1310 LTGDVTPDMKSI--AKADLIVTTPEKWDGVSRSwqNRSYVQQVNILIIDEIH 1359
Cdd:cd18033 80 LTGSVPPTKRAElwASKRVFFLTPQTLENDLKE--GDCDPKSIVCLVIDEAH 129
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
1247-1359 |
2.47e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 52.81 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKyPTSKAVYIAPLKALVRERMDDWK--IRIEEklgKKVIELTGDVTPD--MKSIA 1322
Cdd:COG1111 19 NTLVVLPTGLGKTAVALLVIAERLHK-KGGKVLFLAPTKPLVEQHAEFFKeaLNIPE---DEIVVFTGEVSPEkrKELWE 94
|
90 100 110
....*....|....*....|....*....|....*....
gi 1720362714 1323 KADLIVTTPE--KWDGVSrswqNRSYVQQVNILIIDEIH 1359
Cdd:COG1111 95 KARIIVATPQviENDLIA----GRIDLDDVSLLIFDEAH 129
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
393-553 |
9.44e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 47.67 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 393 NTNENMLICAPTGAGKTniamLTILHEIRQHFHQGVIKknefKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDmq 472
Cdd:pfam04851 21 NGQKRGLIVMATGSGKT----LTAAKLIARLFKKGPIK----KVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 473 lSKSEILRT-QMLVTTPEKWDVVTRKSVGDVALSQIVkLLILDEVHllhedRGPvlesivARTLRQVESTQSMIRILGLS 551
Cdd:pfam04851 91 -KKDESVDDnKIVVTTIQSLYKALELASLELLPDFFD-VIIIDEAH-----RSG------ASSYRNILEYFKPAFLLGLT 157
|
..
gi 1720362714 552 AT 553
Cdd:pfam04851 158 AT 159
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
395-517 |
1.11e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 47.89 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 395 NENMLICAPTGAGKTNIAMLTILheirqhfhqGVIKKNEFKIVYVAPMKALAAEMTNYFsKRLEPLGIVVKELTGDMQLS 474
Cdd:cd18035 16 NGNTLIVLPTGLGKTIIAILVAA---------DRLTKKGGKVLILAPSRPLVEQHAENL-KRVLNIPDKITSLTGEVKPE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1720362714 475 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivkLLILDEVH 517
Cdd:cd18035 86 ERAERwdASKIIVATPQviENDLLAgRITLDDVS------LLIFDEAH 127
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
399-646 |
2.45e-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: 48.97 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 399 LICAPTGAGKTNIAMLTILHEIRQhfhqgvikKNEFKIVYVAPMKALAAEMTNYFSKRL-EPLGIVVKELTGD--MQLSK 475
Cdd:cd09639 3 VIEAPTGYGKTEAALLWALHSLKS--------QKADRVIIALPTRATINAMYRRAKEAFgETGLYHSSILSSRikEMGDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 476 SEILR--------------TQMLVTTPEKWDVVTRKSVGDVALSQ---IVKLLILDEVHLLHEDrgpVLESIVA--RTLR 536
Cdd:cd09639 75 EEFEHlfplyihsndtlflDPITVCTIDQVLKSVFGEFGHYEFTLasiANSLLIFDEVHFYDEY---TLALILAvlEVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 537 QVEstqsmIRILGLSATLPNYLDvATFLHVNPYIGLFYFDgrFRPVPLGQTFLGIKSTN-KMQQLNNMDEVCyesvlkqv 615
Cdd:cd09639 152 DND-----VPILLMSATLPKFLK-EYAEKIGYVEENEPLD--LKPNERAPFIKIESDKVgEISSLERLLEFI-------- 215
|
250 260 270
....*....|....*....|....*....|.
gi 1720362714 616 KAGHQVMVFVHarnaTVRTAMSLIERAKNSG 646
Cdd:cd09639 216 KKGGSVAIIVN----TVDRAQEFYQQLKEKG 242
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
1247-1359 |
4.41e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 46.35 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKYpTSKAVYIAPLKALVRERMDDWK--IRIEEklgkKVIELTGDVTPDMKS--IA 1322
Cdd:cd18035 18 NTLIVLPTGLGKTIIAILVAADRLTKK-GGKVLILAPSRPLVEQHAENLKrvLNIPD----KITSLTGEVKPEERAerWD 92
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720362714 1323 KADLIVTTPEKWDgvSRSWQNRSYVQQVNILIIDEIH 1359
Cdd:cd18035 93 ASKIIVATPQVIE--NDLLAGRITLDDVSLLIFDEAH 127
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
391-554 |
2.66e-04 |
|
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: 43.06 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 391 AYNTNENMLICAPTGAGKTNIAMLTILheirqhfhqgviKKNEFKIVYVAPMKAL----AAEMTNYFSKRleplgiVVKE 466
Cdd:cd17926 14 AHKNNRRGILVLPTGSGKTLTALALIA------------YLKELRTLIVVPTDALldqwKERFEDFLGDS------SIGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 467 LTGDmqlSKSEILRTQMLVTTPEK--WDVVTRKSVGDVALsqivkLLILDEVHllhedRGPvlesivARTLRQVESTQSM 544
Cdd:cd17926 76 IGGG---KKKDFDDANVVVATYQSlsNLAEEEKDLFDQFG-----LLIVDEAH-----HLP------AKTFSEILKELNA 136
|
170
....*....|
gi 1720362714 545 IRILGLSATL 554
Cdd:cd17926 137 KYRLGLTATP 146
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
1247-1359 |
4.08e-04 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 45.63 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDDWK--IRIEEklgKKVIELTGDVTPD--MKSIA 1322
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIAERLHKKG-GKVLILAPTKPLVEQHAEFFRkfLNIPE---EKIVVFTGEVSPEkrAELWE 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 1720362714 1323 KADLIVTTPE--KWDGVSrswqNRSYVQQVNILIIDEIH 1359
Cdd:PRK13766 107 KAKVIVATPQviENDLIA----GRISLEDVSLLIFDEAH 141
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
376-555 |
1.09e-03 |
|
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: 42.57 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 376 GMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTnIAML--TILHEIRQHFHQgviKKNEFKIVYVAPMKALAAEMTNYF 453
Cdd:cd17964 13 GFETMTPVQQKTLKPILSTGDDVLARAKTGTGKT-LAFLlpAIQSLLNTKPAG---RRSGVSALIISPTRELALQIAAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 454 SKRLEPL-GIVVKELTGDMQLSKSEI----LRTQMLVTTPEKW-DVVTRKSVGDVALSqiVKLLILDEV-HLLheDRG-- 524
Cdd:cd17964 89 KKLLQGLrKLRVQSAVGGTSRRAELNrlrrGRPDILVATPGRLiDHLENPGVAKAFTD--LDYLVLDEAdRLL--DMGfr 164
|
170 180 190
....*....|....*....|....*....|.
gi 1720362714 525 PVLESIVaRTLRQVESTQsmIRILGLSATLP 555
Cdd:cd17964 165 PDLEQIL-RHLPEKNADP--RQTLLFSATVP 192
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
1225-1384 |
1.24e-03 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 42.74 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1225 YNFSHFNPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAV-YIAPLkALV----RERMDdwKIR- 1298
Cdd:cd17948 8 QGITKPTTVQKQGIPSILRGR-NTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpFNAPR-GLVitpsRELAE--QIGs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1299 ----IEEKLGKKVIELTGDVTpdMKSI-----AKADLIVTTPekwDGVSRSWQNRSY-VQQVNILIIDEIH-LLGEERGP 1367
Cdd:cd17948 84 vaqsLTEGLGLKVKVITGGRT--KRQIrnphfEEVDILVATP---GALSKLLTSRIYsLEQLRHLVLDEADtLLDDSFNE 158
|
170
....*....|....*..
gi 1720362714 1368 VLEVIVSRTNFISSHTE 1384
Cdd:cd17948 159 KLSHFLRRFPLASRRSE 175
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
1523-1595 |
1.82e-03 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 40.65 E-value: 1.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720362714 1523 HAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-----AHLVIIKGTE-YYdgktrryvdfpitdvlQMMGRAGR 1595
Cdd:cd18794 61 HAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPdvrfvIHYSLPKSMEsYY----------------QESGRAGR 123
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
1227-1359 |
1.95e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 41.75 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1227 FSHFNPVQTQ-IFHTLYHTDCNVLLgaPTGSGKTVAAELAIFrVFNKyPTskaVYIAPLKALvrerMDDWKIRIEEkLGK 1305
Cdd:cd17920 10 YDEFRPGQLEaINAVLAGRDVLVVM--PTGGGKSLCYQLPAL-LLDG-VT---LVVSPLISL----MQDQVDRLQQ-LGI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720362714 1306 KVIELTGDVTPDMKSIA-------KADLIVTTPEK--WDGVSRSWQNRSYVQQVNILIIDEIH 1359
Cdd:cd17920 78 RAAALNSTLSPEEKREVllrikngQYKLLYVTPERllSPDFLELLQRLPERKRLALIVVDEAH 140
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
1232-1331 |
3.04e-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: 41.04 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1232 PVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIF---RVFNKYPTSKAVYIAPLKAL----VRErmddwKIRIEEKLG 1304
Cdd:cd17957 15 PIQMQAIPILLHGR-DLLACAPTGSGKTLAFLIPILqklGKPRKKKGLRALILAPTRELasqiYRE-----LLKLSKGTG 88
|
90 100 110
....*....|....*....|....*....|.
gi 1720362714 1305 KKVIELTGDVTP----DMKSIAKADLIVTTP 1331
Cdd:cd17957 89 LRIVLLSKSLEAkakdGPKSITKYDILVSTP 119
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
1247-1359 |
3.76e-03 |
|
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: 40.92 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1247 NVLLGAPTGSGKTVAAELAIFRVFNKYP----TSKAVYIAPLKALVrERMDDWKIRIEEKlGKKVIELTGD--VTPDMKS 1320
Cdd:cd18036 19 NTIICAPTGSGKTRVAVYICRHHLEKRRsageKGRVVVLVNKVPLV-EQQLEKFFKYFRK-GYKVTGLSGDssHKVSFGQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1720362714 1321 IAKA-DLIVTTPEKWDGVSRS--WQNRSYVQQVNILIIDEIH 1359
Cdd:cd18036 97 IVKAsDVIICTPQILINNLLSgrEEERVYLSDFSLLIFDECH 138
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
1545-1595 |
6.34e-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: 39.08 E-value: 6.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720362714 1545 VLIATSTLAWGVNFPAHLVIIKGTEYYDGKTRRyvDFPITDVLQMMGRAGR 1595
Cdd:cd18805 73 VLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMR--PLSPSEVKQIAGRAGR 121
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
1226-1331 |
8.37e-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: 39.92 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1226 NFSHFNPVQTQIFHTLYHTD--------CNVLLGAPTGSGKTVAAELAIFRVFNKYPTSK--AVYIAPLKAL---VRERM 1292
Cdd:cd17956 9 GITSAFPVQAAVIPWLLPSSkstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRlrALIVVPTKELvqqVYKVF 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1720362714 1293 DdwkiRIEEKLGKKVIELTG--DVTPDMKSIA---------KADLIVTTP 1331
Cdd:cd17956 89 E----SLCKGTGLKVVSLSGqkSFKKEQKLLLvdtsgrylsRVDILVATP 134
|
|
| |
