|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1327-1515 |
1.11e-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: 415.62 E-value: 1.11e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1327 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLGKKVI 1406
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1407 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKPVR 1486
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*....
gi 456367250 1487 IVGLSTALANARDLADWLNIKQMGLFNFR 1515
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
979-1287 |
8.76e-126 |
|
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: 398.11 E-value: 8.76e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 979 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDALLNNfCELSAPGGVENSYGKI 1058
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEK-VPIPVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1059 NILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSVLPPHI 1138
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1139 LTRLEEKNLTV--DKLKDMRKDEIGHILHHVNIGLKVKQCVHQIPSVTMEASIQPITRTVLRVSLNIYPDFSWNDQVHGT 1216
Cdd:pfam02889 160 IKKLEKKGVESvrDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456367250 1217 VgEPWWIWVEDPTNDHIYHSEYFLALKKQVINkeAQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIIN 1287
Cdd:pfam02889 240 S-EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
477-674 |
1.20e-124 |
|
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: 390.25 E-value: 1.20e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 477 RLNRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFHQ-GVLKKNEFKIVYVAPMKALAAEMTNYFSKRL 555
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 556 EPLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDVALSQIVKLLILDEVHLLHEDRGPVLESIVARTLRQ 635
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 456367250 636 VESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFYFD 674
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
976-1289 |
1.84e-112 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 360.42 E-value: 1.84e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 976 YFSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDALLNNFCELSAPGGVENSY 1055
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1056 GKINILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSVLP 1135
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1136 PHILTRLEEKN-LTVDKLKDMRKDEIGHILHHVN-IGLKVKQCVHQIPSVTMEASIQPITRTVLRVSLNIYPDFSWNDQV 1213
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLGLLDaEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456367250 1214 HGTVgEPWWIWVEDPTNDHIYHSEYFLALKKQVINKeaQLLVFTIPIFEPLPsQYYIRAVSDRWLGAEAVCIINFQ 1289
Cdd:smart00611 241 HGKQ-EGWWLVIGDSDGNELLHIERFSLNKKNVSEE--VKLDFTAPATEGNY-QYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1810-2176 |
2.28e-96 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 314.20 E-value: 2.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1810 SIEPLTCGRIASYYYLKHKTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHTNNELAKCLPIELNPHSFDSPH 1889
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1890 TKAHLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAASQGWLVTTLNITHLIQMVIQGRWLKDSSLLTIPNIE 1969
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1970 QHHLHLFRKWKppvkgphakcRTSIECLPELIHacEGKEHVFSSMVekelqpAKTKQAWNFLSHLPVINVGISVKGSwDD 2049
Cdd:smart00611 161 EEILKRLEKKK----------VLSLEDLLELED--EERGELLGLLD------AEGERVYKVLSRLPKLNIEISLEPI-TR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 2050 SVEGHNELSISTLTADKRdentwiklhadqqyvlqvslqrvhfefhkvKHEshavtprfpklKDEGWFLILGEVDKRELV 2129
Cdd:smart00611 222 TVLGVEVTLTVDLTWDDE------------------------------IHG-----------KQEGWWLVIGDSDGNELL 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 456367250 2130 AVKRVGF--VRTHHEASISFFTPEAPGRYIFTLYLMSDCYLGLDQQYDI 2176
Cdd:smart00611 261 HIERFSLnkKNVSEEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPL 309
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1328-1850 |
7.21e-96 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 321.07 E-value: 7.21e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1328 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKIRIEEkLGKKVIE 1407
Cdd:COG1204 23 LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEE-LGIKVGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1408 LTGDVTPDMKSIAKADLIVTTPEKWDGVSRswQNRSYVQQVNILIIDEIHLLG-EERGPVLEVIVSRtnfiSSHTEKPVR 1486
Cdd:COG1204 100 STGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTLEVLLAR----LRRLNPEAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1487 IVGLSTALANARDLADWLNIKqmglfNFRPSVRPVPLE--VHIQG---FPGQHYCPRmasmnKPAFQAIRSHSPA-KPVL 1560
Cdd:COG1204 174 IVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSK-----DPTLALALDLLEEgGQVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1561 IFVSSRRQTRLTALELIAFLA---TEEDPKQWLNMDEQEMEniIATVRDSNLKLT--LAFGIGMHHAGLHERDRKTVEEL 1635
Cdd:COG1204 244 VFVSSRRDAESLAKKLADELKrrlTPEEREELEELAEELLE--VSEETHTNEKLAdcLEKGVAFHHAGLPSELRRLVEDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1636 FVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGktrryVDFPITDVLQMMGRAGRPQFDDQGKAVILVHDIK---KD 1712
Cdd:COG1204 322 FREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDeadEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1713 FYKKFLYEPFPVESSLLGVLSD--HLNAEIAGGTITSKQDALDYITWTYFFRRlimnPSYYNLGDVSQDAINKflshLIG 1790
Cdd:COG1204 397 FERYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQ----YDKGDLEEVVDDALEF----LLE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456367250 1791 QSLVElelshcievgEDNRSIEPLTCGRIASYYYLKHKTVKMFKDRLK---PECSTEELLSIL 1850
Cdd:COG1204 469 NGFIE----------EDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadEEFTDLGLLHLI 521
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
461-1016 |
4.05e-94 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 316.07 E-value: 4.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 461 IQDLDEVG---QLAFKGMKRLNRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFhqgvlkknefKIVYV 537
Cdd:COG1204 3 VAELPLEKvieFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 538 APMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGdvALSQIvKLLILDEVHLL 617
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDV-DLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 618 H-EDRGPVLESIVARtLRQVESTqsmIRILGLSATLPNYLDVATFLHVNPyiglfyFDGRFRPVPLgqtFLGIKSANKmq 696
Cdd:COG1204 150 DdESRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGV-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 697 qlNNMDEVCYES-------VLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNSgqISCFLPTQGPEYGHALKQVQKSR- 768
Cdd:COG1204 215 --LRFDDGSRRSkdptlalALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRR--LTPEEREELEELAEELLEVSEETh 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 769 -NKQVRELFSDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTqiyaaKRGSFVDLGILDV 847
Cdd:COG1204 291 tNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-----KRGGMVPIPVLEF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 848 MQIFGRAGRPQFDKFGEGIIIT-THDKLSH--YLSLLTQQNPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWMSYTY 922
Cdd:COG1204 366 KQMAGRAGRPGYDPYGEAILVAkSSDEADElfERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTF 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 923 LYVRMRANPLaygishkayqmdptlrkhrEQLLIEVGQKLDKARMIrfEERTGYFSSTDLGRTASHYYIKYNTIETFNEL 1002
Cdd:COG1204 446 YAYQYDKGDL-------------------EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAELVDG 504
|
570
....*....|....
gi 456367250 1003 FDAHKTEGDIFAIV 1016
Cdd:COG1204 505 LRKADEEFTDLGLL 518
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1813-2176 |
1.16e-71 |
|
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: 242.88 E-value: 1.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1813 PLTCGRIASYYYLKHKTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHTNNELAKCLPIELNPhSFDSPHTKA 1892
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKG-DIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1893 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAASQGWLVTTLNITHLIQMVIQGRWLKDSSLLTIPNIEqhh 1972
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIP--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1973 lhlfrkwkppvkgphakcrtsieclPELIHACEGKEHVF-----SSMVEKELQ-----PAKTKQAWNFLSHLPVINVgis 2042
Cdd:pfam02889 157 -------------------------PELIKKLEKKGVESvrdilELDDAEELGelirnPKMGKDIAQFVNRFPKIEI--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 2043 vkgswddsveghnELSISTLTADkrdentwiklhadqqyVLQVSLQrvhfefhkvkheshaVTPRFPKLKD-----EGWF 2117
Cdd:pfam02889 209 -------------EAEVQPITRS----------------VLRVEVT---------------ITPDFPWDKRvhgksEGFW 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456367250 2118 LILGEVDKRELVAVKRVGFVR--THHEASISFFTP-EAPGRYIFTLYLMSDCYLGLDQQYDI 2176
Cdd:pfam02889 245 LVVGDSDGNEILHIERFTLTKrtLAGEHKLEFTVPpSDPGPPQLFVRLISDSWLGADQEVPI 306
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1519-1707 |
1.58e-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: 1.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1519 RPVPLEVHIQGFPGQHYCPRMASMNK-----PAFQAIRSHSPAKPVLIFVSSRRQTRLTALELIaflateedpkqwlnmd 1593
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1594 eqemeniiatvrdsnlkltlafGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKT 1673
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 456367250 1674 RRYvdFPITDVLQMMGRAGRPQFDDQGKAVILVH 1707
Cdd:cd18795 123 YRE--LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1345-1865 |
9.67e-60 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 220.84 E-value: 9.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFrvfNKYPTS--KAVYIAPLKALVRER---MDDWkirieEKLGKKVIELTGDVTPDMKSI 1419
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMV---NKLLREggKAVYLVPLKALAEEKyreFKDW-----EKLGLRVAMTTGDYDSTDEWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1420 AKADLIVTTPEKWDGVSRswQNRSYVQQVNILIIDEIHLLGE-ERGPVLEVIVSrtnfissHTEKPVRIVGLSTALANAR 1498
Cdd:PRK00254 113 GKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSyDRGATLEMILT-------HMLGRAQILGLSATVGNAE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1499 DLADWLNIKQMglfnfRPSVRPVPLE--VHIQGF------PGQHYcprMASMNKPAFQAIRShspAKPVLIFVSSRRQTR 1570
Cdd:PRK00254 184 ELAEWLNAELV-----VSDWRPVKLRkgVFYQGFlfwedgKIERF---PNSWESLVYDAVKK---GKGALVFVNTRRSAE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1571 LTALELIAFLateedpKQWLNMDEQEMENIIATVRDSN-----LKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLI 1645
Cdd:PRK00254 253 KEALELAKKI------KRFLTKPELRALKELADSLEENptnekLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVIT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1646 ATSTLAWGVNFPAHLVIIKGTEYYDGKTrrYVDFPITDVLQMMGRAGRPQFDDQGKAVILVH-DIKKDFYKKF------- 1717
Cdd:PRK00254 327 ATPTLSAGINLPAFRVIIRDTKRYSNFG--WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERYifgkpek 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1718 LYEPFPVESSLLGvlsdHLNAEIAGGTITSKQDALDYITWTYFfrrlimnpsYYNLGDVS--QDAINKFLSHLIGQSLVE 1795
Cdd:PRK00254 405 LFSMLSNESAFRS----QVLALITNFGVSNFKELVNFLERTFY---------AHQRKDLYslEEKAKEIVYFLLENEFID 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 456367250 1796 LELshcievgEDNrsIEPLTCGRIASYYYLKHKTVKMFKDRLkPECSTEE----LLSILSDAEEYTDLPVRHNE 1865
Cdd:PRK00254 472 IDL-------EDR--FIPLPLGIRTSQLYIDPLTAKKFKDAF-PKIEKNPnplgIFQLIASTPDMTPLNYSRKE 535
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
494-1035 |
2.05e-56 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 210.83 E-value: 2.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 494 ENMLICAPTGAGKTNIAMLTVLHEIRQhfhQGvlkkneFKIVYVAPMKALAAEMTNYFsKRLEPLGIVVKELTGDMQlSK 573
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKLLR---EG------GKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYD-ST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 574 SEIL-RTQMLVTTPEKWDVVTRKSVgdvalSQI--VKLLILDEVHLL-HEDRGPVLESIVARTLRQVEstqsmirILGLS 649
Cdd:PRK00254 109 DEWLgKYDIIIATAEKFDSLLRHGS-----SWIkdVKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ-------ILGLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 650 ATLPNYLDVATFLHVNpyigLFYFDgrFRPVPL-----GQTFLGIKSANKMQQLNNMDEVCYESVlkqvKAGHQVMVFVH 724
Cdd:PRK00254 177 ATVGNAEELAEWLNAE----LVVSD--WRPVKLrkgvfYQGFLFWEDGKIERFPNSWESLVYDAV----KKGKGALVFVN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 725 ARNATVRTAMSLieraknSGQISCFLPTqgPEYgHALKQVQKS-----RNKQVRELFSDGFSIHHAGMLRQDRNLVENLF 799
Cdd:PRK00254 247 TRRSAEKEALEL------AKKIKRFLTK--PEL-RALKELADSleenpTNEKLKKALRGGVAFHHAGLGRTERVLIEDAF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 800 SNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYAakRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDK----LS 875
Cdd:PRK00254 318 REGLIKVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklME 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 876 HYL--------SLLTQQNPIESQFLesladnlnAEIALGTVTNVEEAVKWMSYTYlYVRMRANPlaYGISHKAYQMDPTL 947
Cdd:PRK00254 396 RYIfgkpeklfSMLSNESAFRSQVL--------ALITNFGVSNFKELVNFLERTF-YAHQRKDL--YSLEEKAKEIVYFL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 948 rkhREQLLIEvgqkldkarmIRFEERtgyFSSTDLGRTASHYYIKYNTIETFNELFDahKTEGD-----IFAIVSKAEEF 1022
Cdd:PRK00254 465 ---LENEFID----------IDLEDR---FIPLPLGIRTSQLYIDPLTAKKFKDAFP--KIEKNpnplgIFQLIASTPDM 526
|
570
....*....|...
gi 456367250 1023 DQIKVREEEIEEL 1035
Cdd:PRK00254 527 TPLNYSRKEMEDL 539
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
678-870 |
3.24e-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: 180.83 E-value: 3.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 678 RPVPLGQTFLGIKS----ANKMQQLNNMDEVCYESVLKQVKAGHQVMVFVHARNATVRTAMSLIeraknsgqiscflptq 753
Cdd:cd18795 1 RPVPLEEYVLGFNGlgikLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 754 gpeyghalkqvqksrnkqvrelfsdGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYA 833
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 456367250 834 AKRgsFVDLGILDVMQIFGRAGRPQFDKFGEGIIITT 870
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
479-657 |
4.49e-33 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 126.59 E-value: 4.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 479 NRIQSIVFDTAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQhfhqgvlKKNEFKIVYVAPMKALAAEMTNYFSKRLEPL 558
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK-------LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 559 GIVVKELTGDMQLSK--SEILRTQMLVTTPEKWDVVTRKSvgdVALSQiVKLLILDEVHLLHE-DRGPVLESIVARtlrq 635
Cdd:pfam00270 73 GLKVASLLGGDSRKEqlEKLKGPDILVGTPGRLLDLLQER---KLLKN-LKLLVLDEAHRLLDmGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|..
gi 456367250 636 vesTQSMIRILGLSATLPNYLD 657
Cdd:pfam00270 145 ---LPKKRQILLLSATLPRNLE 163
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1329-1500 |
3.17e-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: 3.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1329 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFN-KYPTSKAVYIAPLKALVRERMDDWKiRIEEKLGKKVIE 1407
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDkLDNGPQALVLAPTRELAEQIYEELK-KLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1408 LTGDVTP--DMKSIAKADLIVTTPEKWDGVsrsWQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNfisshteKP 1484
Cdd:pfam00270 79 LLGGDSRkeQLEKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRRLP-------KK 148
|
170
....*....|....*..
gi 456367250 1485 VRIVGLS-TALANARDL 1500
Cdd:pfam00270 149 RQILLLSaTLPRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
470-681 |
6.76e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 107.19 E-value: 6.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 470 LAFKGMKRLNRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFHQGVLkknefkivYVAPMKALAAEMTN 549
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVL--------VLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 550 YFSKRLEPLGIVVKELTGD----MQLSKSEILRTQMLVTTPEKWDVVTRKsvGDVALSQiVKLLILDEVH-LLHEDRGPV 624
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRLLDLLEN--DKLSLSN-VDLVILDEAHrLLDGGFGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 456367250 625 LESIVARTLRqvestqsMIRILGLSATLPNYLDVATFLHVNpyiGLFYFDGRFRPVP 681
Cdd:smart00487 150 LEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1330-1706 |
1.06e-25 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 115.76 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1330 PVQT-QIFHTLYHTDcNVLLGAPTGSGKTVAAELA-IFRVFNKypTSKAVYIAPLKALVRERMDDWKIRIEEKLgkKVIE 1407
Cdd:COG1202 212 PVQSlAVENGLLEGK-DQLVVSATATGKTLIGELAgIKNALEG--KGKMLFLVPLVALANQKYEDFKDRYGDGL--DVSI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1408 LTGDV---TPDMKSIAKADLIVTTPEKWDGVSRSwqnRSYVQQVNILIIDEIHLLGE-ERGPVLEVIVSRTNFISSHTEk 1483
Cdd:COG1202 287 RVGASrirDDGTRFDPNADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEVHMLEDpERGHRLDGLIARLKYYCPGAQ- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1484 pvrIVGLSTALANARDLADWLNIKQMgLFNfrpsVRPVPLEVHIQGFPGQHYCPRMASMNKPAFQAIRSHSPAKPVLIFV 1563
Cdd:COG1202 363 ---WIYLSATVGNPEELAKKLGAKLV-EYE----ERPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1564 SSRRQTRltaleliaflateedpkqwlnmdeqemeniiatvrdsnlKLTLAFGIGM--HHAGLHERDRKTVEELFVNCKV 1641
Cdd:COG1202 435 NSRRRCH---------------------------------------EIARALGYKAapYHAGLDYGERKKVERRFADQEL 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456367250 1642 QVLIATSTLAWGVNFPAHLVIIK----GTEYydgktrryvdFPITDVLQMMGRAGRPQFDDQGKAVILV 1706
Cdd:COG1202 476 AAVVTTAALAAGVDFPASQVIFDslamGIEW----------LSVQEFHQMLGRAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1323-1522 |
4.86e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 104.88 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1323 YNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLG 1402
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1403 KKVIELTGDVT-PDMKSIAK--ADLIVTTPEKWDGVSRswQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNfis 1478
Cdd:smart00487 84 KVVGLYGGDSKrEQLRKLESgkTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 456367250 1479 shteKPVRIVGLS-TALANARDLADWLNIkqmGLFNFRPSVRPVP 1522
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 ... |
1347-1662 |
3.20e-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: 85.30 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1347 LLGAPTGSGKTVAAELAIFRVFNKYPTSK-----AVYIAPLKALVR----------ERMdDWKIRIEEKlgkkvielTGD 1411
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKekglhTLYITPLRALAVdiarnlqapiEEL-GLPIRVETR--------TGD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1412 VTPDMKSIAKA---DLIVTTPEkwdgvsrSWQ-------NRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNFISSH 1480
Cdd:TIGR04121 103 TSSSERARQRKkppDILLTTPE-------SLAlllsypdAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1481 tekpVRIVGLSTALANARDLADWLnikqMGLFNFRPSV------RPVPLEV----HIQGFP-GQHYCPRMASmnkPAFQA 1549
Cdd:TIGR04121 176 ----LRRWGLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISllpeSEERFPwAGHLGLRALP---EVYAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1550 IRSHspaKPVLIFVSSRRQTRLTALELIAFLAteedpkqwlnmdeqemeniiatvrDSNLKltlafgIGMHHAGLHERDR 1629
Cdd:TIGR04121 245 IDQA---RTTLVFTNTRSQAELWFQALWEANP------------------------EFALP------IALHHGSLDREQR 291
|
330 340 350
....*....|....*....|....*....|....
gi 456367250 1630 KTVEELFVNCKVQVLIATSTLAWGVNF-PAHLVI 1662
Cdd:TIGR04121 292 RWVEAAMAAGRLRAVVCTSSLDLGVDFgPVDLVI 325
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1615-1694 |
7.73e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 71.47 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1615 FGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryVDFPITDVLQMMGRAGR 1693
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVII-----YD------LPWSPASYIQRIGRAGR 80
|
.
gi 456367250 1694 P 1694
Cdd:smart00490 81 A 81
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
489-857 |
9.45e-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: 80.29 E-value: 9.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 489 AYNTNENMLICAPTGAGKTNIAMLTVLHEIrqhFHQGVLKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLG--IVVKELT 566
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSLIDL---AGPEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGlpIRVETRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 567 GDMQLSKSEILRTQM---LVTTPEKWDVVTrkSVGDVA-LSQIVKLLILDEVH-LLHEDRGPVLESIVARtLRQvesTQS 641
Cdd:TIGR04121 101 GDTSSSERARQRKKPpdiLLTTPESLALLL--SYPDAArLFKDLRCVVVDEWHeLAGSKRGDQLELALAR-LRR---LAP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 642 MIRILGLSATLPNyLDVA--TFLHVNPYIGLFYFDGRFRPVPL-------GQTF-----LGIKSAnkmqqlnnmdevcyE 707
Cdd:TIGR04121 175 GLRRWGLSATIGN-LEEArrVLLGVGGAPAVLVRGKLPKAIEVisllpesEERFpwaghLGLRAL--------------P 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 708 SVLKQVKAGHQVMVFVHARNATVRTAMSLIEraknsgqiscflptqgpeyghalkqvqksrnkqVRELFSDGFSIHHAGM 787
Cdd:TIGR04121 240 EVYAEIDQARTTLVFTNTRSQAELWFQALWE---------------------------------ANPEFALPIALHHGSL 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456367250 788 LRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIkgtQIYAAKrgsfvdlGILDVMQIFGRAG-RP 857
Cdd:TIGR04121 287 DREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSPK-------GVARLLQRAGRSNhRP 347
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
779-857 |
6.47e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 66.08 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 779 GFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIKGtqiyaakrgsfVDLGILDVMQIFGRAGRP 857
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASYIQRIGRAGRA 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1599-1693 |
3.44e-10 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 59.15 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1599 NIIATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryV 1677
Cdd:pfam00271 23 QTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YD------L 91
|
90
....*....|....*.
gi 456367250 1678 DFPITDVLQMMGRAGR 1693
Cdd:pfam00271 92 PWNPASYIQRIGRAGR 107
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
493-820 |
5.14e-10 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 64.91 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNIAMLTVLHEIRQHFHQGVLkKNEFKIVYVAPMKALAAEMtnyfsKR--LEPL-GI--VVKEL-- 565
Cdd:PRK13767 47 GKNVLISSPTGSGKTLAAFLAIIDELFRLGREGEL-EDKVYCLYVSPLRALNNDI-----HRnlEEPLtEIreIAKERge 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 566 ----------TGDM-QLSKSEILRT--QMLVTTPEKWDVVT-----RKSVGDvalsqiVKLLILDEVHLLHED-RGPVLe 626
Cdd:PRK13767 121 elpeirvairTGDTsSYEKQKMLKKppHILITTPESLAILLnspkfREKLRT------VKWVIVDEIHSLAENkRGVHL- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 627 sivARTLRQVES--TQSMIRIlGLSATLPNYLDVATFLhvnpyiGLFYFDGRFRPVPLGQT-F---LGIK---------- 690
Cdd:PRK13767 194 ---SLSLERLEElaGGEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDCEIVDArFvkpFDIKvispvddlih 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 691 -SANKMQqlnnmdEVCYESVLKQVKAGHQVMVFVHARNATVRTAMSLieraknsgqiscflptqgpeyghalkqvqksrn 769
Cdd:PRK13767 264 tPAEEIS------EALYETLHELIKEHRTTLIFTNTRSGAERVLYNL--------------------------------- 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 456367250 770 kqvRELFSDGFSI-----HHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP 820
Cdd:PRK13767 305 ---RKRFPEEYDEdnigaHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG 357
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1325-1491 |
1.37e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 63.75 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1325 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAI----FRVFNK-------YptskAVYIAPLKAL---VRERM 1390
Cdd:PRK13767 30 FGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREgeledkvY----CLYVSPLRALnndIHRNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1391 DDWKIRIEEKLGKKVIEL--------TGDVTPDMKS--------IakadLIvTTPEKWDGVSRSWQNRSYVQQVNILIID 1454
Cdd:PRK13767 105 EEPLTEIREIAKERGEELpeirvairTGDTSSYEKQkmlkkpphI----LI-TTPESLAILLNSPKFREKLRTVKWVIVD 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 456367250 1455 EIHLLGE-ERGPVLEVIVSRTNFISSHteKPVRIvGLS 1491
Cdd:PRK13767 180 EIHSLAEnKRGVHLSLSLERLEELAGG--EFVRI-GLS 214
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
493-615 |
5.80e-08 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 58.20 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNIAMLTVLHeirqhfhqgVLKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLS 572
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE---------RLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 456367250 573 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivkLLILDEVH 615
Cdd:COG1111 88 KRKELweKARIIVATPQviENDLIAgRIDLDDVS------LLIFDEAH 129
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
775-856 |
9.22e-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: 49.52 E-value: 9.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 775 LFSDGFSI--HHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIkgtqiyaakrgSFVDLGILDVMQIF 851
Cdd:pfam00271 34 LEKEGIKVarLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----------YDLPWNPASYIQRI 102
|
....*
gi 456367250 852 GRAGR 856
Cdd:pfam00271 103 GRAGR 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; ... |
1327-1515 |
1.11e-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: 415.62 E-value: 1.11e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1327 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLGKKVI 1406
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1407 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKPVR 1486
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*....
gi 456367250 1487 IVGLSTALANARDLADWLNIKQMGLFNFR 1515
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
979-1287 |
8.76e-126 |
|
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: 398.11 E-value: 8.76e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 979 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDALLNNfCELSAPGGVENSYGKI 1058
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEK-VPIPVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1059 NILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSVLPPHI 1138
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1139 LTRLEEKNLTV--DKLKDMRKDEIGHILHHVNIGLKVKQCVHQIPSVTMEASIQPITRTVLRVSLNIYPDFSWNDQVHGT 1216
Cdd:pfam02889 160 IKKLEKKGVESvrDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456367250 1217 VgEPWWIWVEDPTNDHIYHSEYFLALKKQVINkeAQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIIN 1287
Cdd:pfam02889 240 S-EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
477-674 |
1.20e-124 |
|
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: 390.25 E-value: 1.20e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 477 RLNRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFHQ-GVLKKNEFKIVYVAPMKALAAEMTNYFSKRL 555
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 556 EPLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDVALSQIVKLLILDEVHLLHEDRGPVLESIVARTLRQ 635
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 456367250 636 VESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFYFD 674
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
461-674 |
1.81e-112 |
|
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: 355.91 E-value: 1.81e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 461 IQDLDEVGQLAFKGMKRLNRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFHQ-GVLKKNEFKIVYVAP 539
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPdGTINLDAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 540 MKALAAEMTNYFSKRLEPLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSvGDVALSQIVKLLILDEVHLLHE 619
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKS-GDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 456367250 620 DRGPVLESIVARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFYFD 674
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
976-1289 |
1.84e-112 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 360.42 E-value: 1.84e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 976 YFSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDALLNNFCELSAPGGVENSY 1055
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1056 GKINILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSVLP 1135
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1136 PHILTRLEEKN-LTVDKLKDMRKDEIGHILHHVN-IGLKVKQCVHQIPSVTMEASIQPITRTVLRVSLNIYPDFSWNDQV 1213
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLGLLDaEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456367250 1214 HGTVgEPWWIWVEDPTNDHIYHSEYFLALKKQVINKeaQLLVFTIPIFEPLPsQYYIRAVSDRWLGAEAVCIINFQ 1289
Cdd:smart00611 241 HGKQ-EGWWLVIGDSDGNELLHIERFSLNKKNVSEE--VKLDFTAPATEGNY-QYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1810-2176 |
2.28e-96 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 314.20 E-value: 2.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1810 SIEPLTCGRIASYYYLKHKTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHTNNELAKCLPIELNPHSFDSPH 1889
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1890 TKAHLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAASQGWLVTTLNITHLIQMVIQGRWLKDSSLLTIPNIE 1969
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1970 QHHLHLFRKWKppvkgphakcRTSIECLPELIHacEGKEHVFSSMVekelqpAKTKQAWNFLSHLPVINVGISVKGSwDD 2049
Cdd:smart00611 161 EEILKRLEKKK----------VLSLEDLLELED--EERGELLGLLD------AEGERVYKVLSRLPKLNIEISLEPI-TR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 2050 SVEGHNELSISTLTADKRdentwiklhadqqyvlqvslqrvhfefhkvKHEshavtprfpklKDEGWFLILGEVDKRELV 2129
Cdd:smart00611 222 TVLGVEVTLTVDLTWDDE------------------------------IHG-----------KQEGWWLVIGDSDGNELL 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 456367250 2130 AVKRVGF--VRTHHEASISFFTPEAPGRYIFTLYLMSDCYLGLDQQYDI 2176
Cdd:smart00611 261 HIERFSLnkKNVSEEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPL 309
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1328-1850 |
7.21e-96 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 321.07 E-value: 7.21e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1328 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKIRIEEkLGKKVIE 1407
Cdd:COG1204 23 LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEE-LGIKVGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1408 LTGDVTPDMKSIAKADLIVTTPEKWDGVSRswQNRSYVQQVNILIIDEIHLLG-EERGPVLEVIVSRtnfiSSHTEKPVR 1486
Cdd:COG1204 100 STGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTLEVLLAR----LRRLNPEAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1487 IVGLSTALANARDLADWLNIKqmglfNFRPSVRPVPLE--VHIQG---FPGQHYCPRmasmnKPAFQAIRSHSPA-KPVL 1560
Cdd:COG1204 174 IVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSK-----DPTLALALDLLEEgGQVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1561 IFVSSRRQTRLTALELIAFLA---TEEDPKQWLNMDEQEMEniIATVRDSNLKLT--LAFGIGMHHAGLHERDRKTVEEL 1635
Cdd:COG1204 244 VFVSSRRDAESLAKKLADELKrrlTPEEREELEELAEELLE--VSEETHTNEKLAdcLEKGVAFHHAGLPSELRRLVEDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1636 FVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGktrryVDFPITDVLQMMGRAGRPQFDDQGKAVILVHDIK---KD 1712
Cdd:COG1204 322 FREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDeadEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1713 FYKKFLYEPFPVESSLLGVLSD--HLNAEIAGGTITSKQDALDYITWTYFFRRlimnPSYYNLGDVSQDAINKflshLIG 1790
Cdd:COG1204 397 FERYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQ----YDKGDLEEVVDDALEF----LLE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456367250 1791 QSLVElelshcievgEDNRSIEPLTCGRIASYYYLKHKTVKMFKDRLK---PECSTEELLSIL 1850
Cdd:COG1204 469 NGFIE----------EDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadEEFTDLGLLHLI 521
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
979-1288 |
9.39e-96 |
|
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: 312.37 E-value: 9.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 979 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELdALLNNFCELSAPGGVENS-YGK 1057
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKEL-NELNKRVPIPVKEGIIDSpHAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1058 INILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLW-GWASPLRQF-SVLP 1135
Cdd:smart00973 80 VNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWeDSDSPLKQLpHFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1136 PHILTRLEEKNL--TVDKLKDMRKDEIGHILH-HVNIGLKVKQCVHQIPSVTMEASIQPITRTV-LRVSLNIYPDFSWND 1211
Cdd:smart00973 160 EDVYDKLELKDGsrSFELLLDMNAAELGEFLNrLPPNGRLIYELLRRFPKIEVEAEVLPITRDLtLRVELEITPVFAWDL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456367250 1212 QVHGTVGEPWWIWVEDPTNDHIYHSEYFLALKKQVINKeaQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIINF 1288
Cdd:smart00973 240 PRHKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNE--VKLDFTVPLSEPGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
461-1016 |
4.05e-94 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 316.07 E-value: 4.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 461 IQDLDEVG---QLAFKGMKRLNRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFhqgvlkknefKIVYV 537
Cdd:COG1204 3 VAELPLEKvieFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 538 APMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGdvALSQIvKLLILDEVHLL 617
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDV-DLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 618 H-EDRGPVLESIVARtLRQVESTqsmIRILGLSATLPNYLDVATFLHVNPyiglfyFDGRFRPVPLgqtFLGIKSANKmq 696
Cdd:COG1204 150 DdESRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGV-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 697 qlNNMDEVCYES-------VLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNSgqISCFLPTQGPEYGHALKQVQKSR- 768
Cdd:COG1204 215 --LRFDDGSRRSkdptlalALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRR--LTPEEREELEELAEELLEVSEETh 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 769 -NKQVRELFSDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTqiyaaKRGSFVDLGILDV 847
Cdd:COG1204 291 tNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-----KRGGMVPIPVLEF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 848 MQIFGRAGRPQFDKFGEGIIIT-THDKLSH--YLSLLTQQNPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWMSYTY 922
Cdd:COG1204 366 KQMAGRAGRPGYDPYGEAILVAkSSDEADElfERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTF 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 923 LYVRMRANPLaygishkayqmdptlrkhrEQLLIEVGQKLDKARMIrfEERTGYFSSTDLGRTASHYYIKYNTIETFNEL 1002
Cdd:COG1204 446 YAYQYDKGDL-------------------EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAELVDG 504
|
570
....*....|....
gi 456367250 1003 FDAHKTEGDIFAIV 1016
Cdd:COG1204 505 LRKADEEFTDLGLL 518
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1325-1515 |
3.34e-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: 3.34e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1325 FSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLGKK 1404
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPLLGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1405 VIELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKP 1484
Cdd:cd18021 81 VVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 456367250 1485 VRIVGLSTALANARDLADWLNIKQMGLFNFR 1515
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 ... |
1813-2176 |
7.18e-80 |
|
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: 266.92 E-value: 7.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1813 PLTCGRIASYYYLKHKTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHTNNELAKCLPIELNPHSFDSPHTKA 1892
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1893 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAASQGWLVTTLNITHLIQMVIQGRWL-KDSSLLTIPNIeqh 1971
Cdd:smart00973 81 NLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEdSDSPLKQLPHF--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1972 hlhlfrkwkppvkgphakcrtsieCLPELIHACEGKEHVFSSMVEKELQPAKTKQAWNFLSHLPVINVGISVKGSWDDsv 2051
Cdd:smart00973 158 ------------------------LIEDVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIE-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 2052 eghNELSISTLTADkrdenTWIKLHADQQYVLQVSLQRvhfefhkvkheshavtprfPKLKDEGWFLILGEVDKRELVAV 2131
Cdd:smart00973 212 ---VEAEVLPITRD-----LTLRVELEITPVFAWDLPR-------------------HKGKSESWWLVVGDSDTNELLAI 264
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 456367250 2132 KRVGFVR--THHEASISFFTPE-APGRYIFTLYLMSDCYLGLDQQYDI 2176
Cdd:smart00973 265 KRVTLRKkkKSNEVKLDFTVPLsEPGPENYTVYLISDSYLGCDQEVSF 312
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1813-2176 |
1.16e-71 |
|
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: 242.88 E-value: 1.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1813 PLTCGRIASYYYLKHKTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHTNNELAKCLPIELNPhSFDSPHTKA 1892
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKG-DIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1893 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAASQGWLVTTLNITHLIQMVIQGRWLKDSSLLTIPNIEqhh 1972
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIP--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1973 lhlfrkwkppvkgphakcrtsieclPELIHACEGKEHVF-----SSMVEKELQ-----PAKTKQAWNFLSHLPVINVgis 2042
Cdd:pfam02889 157 -------------------------PELIKKLEKKGVESvrdilELDDAEELGelirnPKMGKDIAQFVNRFPKIEI--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 2043 vkgswddsveghnELSISTLTADkrdentwiklhadqqyVLQVSLQrvhfefhkvkheshaVTPRFPKLKD-----EGWF 2117
Cdd:pfam02889 209 -------------EAEVQPITRS----------------VLRVEVT---------------ITPDFPWDKRvhgksEGFW 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456367250 2118 LILGEVDKRELVAVKRVGFVR--THHEASISFFTP-EAPGRYIFTLYLMSDCYLGLDQQYDI 2176
Cdd:pfam02889 245 LVVGDSDGNEILHIERFTLTKrtLAGEHKLEFTVPpSDPGPPQLFVRLISDSWLGADQEVPI 306
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
1327-1515 |
1.27e-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: 1.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1327 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDDWKIRIEEkLGKKVI 1406
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSG-GKAVYIAPTRALVNQKEADLRERFGP-LGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1407 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRsYVQQVNILIIDEIHLLG-EERGPVLEVIVSRTNFIsshtEKPV 1485
Cdd:cd17921 79 LLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI----NKNA 153
|
170 180 190
....*....|....*....|....*....|
gi 456367250 1486 RIVGLSTALANARDLADWLNIKqmGLFNFR 1515
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 ... |
1519-1707 |
1.58e-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: 1.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1519 RPVPLEVHIQGFPGQHYCPRMASMNK-----PAFQAIRSHSPAKPVLIFVSSRRQTRLTALELIaflateedpkqwlnmd 1593
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1594 eqemeniiatvrdsnlkltlafGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKT 1673
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 456367250 1674 RRYvdFPITDVLQMMGRAGRPQFDDQGKAVILVH 1707
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 ... |
1328-1520 |
1.19e-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: 1.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1328 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTS-----KAVYIAPLKALVRERMDDWKIRIeEKLG 1402
Cdd:cd18023 2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLpwgnrKVVYIAPIKALCSEKYDDWKEKF-GPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1403 KKVIELTGD-VTPDMKSIAKADLIVTTPEKWDGVSRSW-QNRSYVQQVNILIIDEIHLLGEERGPVLEVIVSRTNFISSH 1480
Cdd:cd18023 81 LSCAELTGDtEMDDTFEIQDADIILTTPEKWDSMTRRWrDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSSS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 456367250 1481 TEK------PVRIVGLSTALANARDLADWLNIKQMGLFNFRPSVRP 1520
Cdd:cd18023 161 SELrgstvrPMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1345-1865 |
9.67e-60 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 220.84 E-value: 9.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFrvfNKYPTS--KAVYIAPLKALVRER---MDDWkirieEKLGKKVIELTGDVTPDMKSI 1419
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMV---NKLLREggKAVYLVPLKALAEEKyreFKDW-----EKLGLRVAMTTGDYDSTDEWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1420 AKADLIVTTPEKWDGVSRswQNRSYVQQVNILIIDEIHLLGE-ERGPVLEVIVSrtnfissHTEKPVRIVGLSTALANAR 1498
Cdd:PRK00254 113 GKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSyDRGATLEMILT-------HMLGRAQILGLSATVGNAE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1499 DLADWLNIKQMglfnfRPSVRPVPLE--VHIQGF------PGQHYcprMASMNKPAFQAIRShspAKPVLIFVSSRRQTR 1570
Cdd:PRK00254 184 ELAEWLNAELV-----VSDWRPVKLRkgVFYQGFlfwedgKIERF---PNSWESLVYDAVKK---GKGALVFVNTRRSAE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1571 LTALELIAFLateedpKQWLNMDEQEMENIIATVRDSN-----LKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLI 1645
Cdd:PRK00254 253 KEALELAKKI------KRFLTKPELRALKELADSLEENptnekLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVIT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1646 ATSTLAWGVNFPAHLVIIKGTEYYDGKTrrYVDFPITDVLQMMGRAGRPQFDDQGKAVILVH-DIKKDFYKKF------- 1717
Cdd:PRK00254 327 ATPTLSAGINLPAFRVIIRDTKRYSNFG--WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERYifgkpek 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1718 LYEPFPVESSLLGvlsdHLNAEIAGGTITSKQDALDYITWTYFfrrlimnpsYYNLGDVS--QDAINKFLSHLIGQSLVE 1795
Cdd:PRK00254 405 LFSMLSNESAFRS----QVLALITNFGVSNFKELVNFLERTFY---------AHQRKDLYslEEKAKEIVYFLLENEFID 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 456367250 1796 LELshcievgEDNrsIEPLTCGRIASYYYLKHKTVKMFKDRLkPECSTEE----LLSILSDAEEYTDLPVRHNE 1865
Cdd:PRK00254 472 IDL-------EDR--FIPLPLGIRTSQLYIDPLTAKKFKDAF-PKIEKNPnplgIFQLIASTPDMTPLNYSRKE 535
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
478-674 |
7.39e-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: 195.17 E-value: 7.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 478 LNRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHfhqgvlkknEFKIVYVAPMKALAAEMTNYFSKRLEP 557
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS---------GGKAVYIAPTRALVNQKEADLRERFGP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 558 LGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDvaLSQIVKLLILDEVHLLH-EDRGPVLESIVARTLRQv 636
Cdd:cd17921 73 LGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER--LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI- 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 456367250 637 estQSMIRILGLSATLPNYLDVATFLHVnpyIGLFYFD 674
Cdd:cd17921 150 ---NKNARFVGLSATLPNAEDLAEWLGV---EDLIRFD 181
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
494-1035 |
2.05e-56 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 210.83 E-value: 2.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 494 ENMLICAPTGAGKTNIAMLTVLHEIRQhfhQGvlkkneFKIVYVAPMKALAAEMTNYFsKRLEPLGIVVKELTGDMQlSK 573
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKLLR---EG------GKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYD-ST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 574 SEIL-RTQMLVTTPEKWDVVTRKSVgdvalSQI--VKLLILDEVHLL-HEDRGPVLESIVARTLRQVEstqsmirILGLS 649
Cdd:PRK00254 109 DEWLgKYDIIIATAEKFDSLLRHGS-----SWIkdVKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ-------ILGLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 650 ATLPNYLDVATFLHVNpyigLFYFDgrFRPVPL-----GQTFLGIKSANKMQQLNNMDEVCYESVlkqvKAGHQVMVFVH 724
Cdd:PRK00254 177 ATVGNAEELAEWLNAE----LVVSD--WRPVKLrkgvfYQGFLFWEDGKIERFPNSWESLVYDAV----KKGKGALVFVN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 725 ARNATVRTAMSLieraknSGQISCFLPTqgPEYgHALKQVQKS-----RNKQVRELFSDGFSIHHAGMLRQDRNLVENLF 799
Cdd:PRK00254 247 TRRSAEKEALEL------AKKIKRFLTK--PEL-RALKELADSleenpTNEKLKKALRGGVAFHHAGLGRTERVLIEDAF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 800 SNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYAakRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDK----LS 875
Cdd:PRK00254 318 REGLIKVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklME 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 876 HYL--------SLLTQQNPIESQFLesladnlnAEIALGTVTNVEEAVKWMSYTYlYVRMRANPlaYGISHKAYQMDPTL 947
Cdd:PRK00254 396 RYIfgkpeklfSMLSNESAFRSQVL--------ALITNFGVSNFKELVNFLERTF-YAHQRKDL--YSLEEKAKEIVYFL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 948 rkhREQLLIEvgqkldkarmIRFEERtgyFSSTDLGRTASHYYIKYNTIETFNELFDahKTEGD-----IFAIVSKAEEF 1022
Cdd:PRK00254 465 ---LENEFID----------IDLEDR---FIPLPLGIRTSQLYIDPLTAKKFKDAFP--KIEKNpnplgIFQLIASTPDM 526
|
570
....*....|...
gi 456367250 1023 DQIKVREEEIEEL 1035
Cdd:PRK00254 527 TPLNYSRKEMEDL 539
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
479-679 |
9.00e-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: 193.34 E-value: 9.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 479 NRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQhfhQGVLKKNEFKIVYVAPMKALAAEMTNYFSKRLEPL 558
Cdd:cd18023 3 NRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKE---RNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 559 GIVVKELTGDMQLSKS-EILRTQMLVTTPEKWDVVTRKSVGDVALSQIVKLLILDEVHLLHEDRGPVLESIVARTLRQVE 637
Cdd:cd18023 80 GLSCAELTGDTEMDDTfEIQDADIILTTPEKWDSMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 456367250 638 STQSM------IRILGLSATLPNYLDVATFLHVNPyIGLFYFDGRFRP 679
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 ... |
1318-1514 |
6.97e-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: 185.27 E-value: 6.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1318 AYEALYNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKY--PTS-------KAVYIAPLKALVRE 1388
Cdd:cd18019 8 AQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHrnPDGtinldafKIVYIAPMKALVQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1389 RMDDWKIRIEEkLGKKVIELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIHLLGEERGPVLE 1468
Cdd:cd18019 88 MVGNFSKRLAP-YGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDDRGPVLE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 456367250 1469 VIVSRTNFISSHTEKPVRIVGLSTALANARDLADWLNIK-QMGLFNF 1514
Cdd:cd18019 167 SIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDpKKGLFYF 213
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
678-870 |
3.24e-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: 180.83 E-value: 3.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 678 RPVPLGQTFLGIKS----ANKMQQLNNMDEVCYESVLKQVKAGHQVMVFVHARNATVRTAMSLIeraknsgqiscflptq 753
Cdd:cd18795 1 RPVPLEEYVLGFNGlgikLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 754 gpeyghalkqvqksrnkqvrelfsdGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYA 833
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 456367250 834 AKRgsFVDLGILDVMQIFGRAGRPQFDKFGEGIIITT 870
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1345-1761 |
1.19e-51 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 195.49 E-value: 1.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWkIRIEEkLGKKVIELTGDV--TPDMksIAKA 1422
Cdd:PRK01172 39 NVIVSVPTAAGKTLIAYSAIYETFLA--GLKSIYIVPLRSLAMEKYEEL-SRLRS-LGMRVKISIGDYddPPDF--IKRY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1423 DLIVTTPEKWDgvSRSWQNRSYVQQVNILIIDEIHLLGEE-RGPVLEVIVSRTNFISSHTekpvRIVGLSTALANARDLA 1501
Cdd:PRK01172 113 DVVILTSEKAD--SLIHHDPYIINDVGLIVADEIHIIGDEdRGPTLETVLSSARYVNPDA----RILALSATVSNANELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1502 DWLNIKQMglfnfRPSVRPVPLEVHIQgFPGQHYCPRMASMNKPAFQAIRSH-SPAKPVLIFVSSRRQTRLTALELIAFL 1580
Cdd:PRK01172 187 QWLNASLI-----KSNFRPVPLKLGIL-YRKRLILDGYERSQVDINSLIKETvNDGGQVLVFVSSRKNAEDYAEMLIQHF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1581 ATEEDPKqwLNMDEqemeniiATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHL 1660
Cdd:PRK01172 261 PEFNDFK--VSSEN-------NNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1661 VIIKG-TEYYDGKTRryvdfPIT--DVLQMMGRAGRPQFDDQGKAVILV-----HDIKKDFYKKflyEPFPVESSLLGVL 1732
Cdd:PRK01172 332 VIVRDiTRYGNGGIR-----YLSnmEIKQMIGRAGRPGYDQYGIGYIYAaspasYDAAKKYLSG---EPEPVISYMGSQR 403
|
410 420 430
....*....|....*....|....*....|.
gi 456367250 1733 SDHLN--AEIAGGTITSKQDALDYITWTYFF 1761
Cdd:PRK01172 404 KVRFNtlAAISMGLASSMEDLILFYNETLMA 434
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1345-1863 |
1.70e-50 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 193.25 E-value: 1.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKIRieEKLGKKVIELTGDVTPDMKSIAKADL 1424
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAMLKAIAR--GGKALYIVPLRALASEKFEEFERF--EELGVRVGISTGDYDSRDEWLGDNDI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1425 IVTTPEKWDGVSRswqNR-SYVQQVNILIIDEIHLLG-EERGPVLEVIVS---RTNfisshtekP-VRIVGLSTALANAR 1498
Cdd:PRK02362 117 IVATSEKVDSLLR---NGaPWLDDITCVVVDEVHLIDsANRGPTLEVTLAklrRLN--------PdLQVVALSATIGNAD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1499 DLADWLNIK-----------QMGLF-----NFRPSVRPVP-----------LEVHIQGfpGQhyCprmasmnkpafqair 1551
Cdd:PRK02362 186 ELADWLDAElvdsewrpidlREGVFyggaiHFDDSQREVEvpskddtlnlvLDTLEEG--GQ--C--------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1552 shspakpvLIFVSSRRQTRLTALELIAFLateedpKQWLNMDEQ-EMENIIATVRDS-------NLKLTLAFGIGMHHAG 1623
Cdd:PRK02362 247 --------LVFVSSRRNAEGFAKRAASAL------KKTLTAAERaELAELAEEIREVsdtetskDLADCVAKGAAFHHAG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1624 LHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGkTRRYVDFPITDVLQMMGRAGRPQFDDQGKAV 1703
Cdd:PRK02362 313 LSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDG-GAGMQPIPVLEYHQMAGRAGRPGLDPYGEAV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1704 ILV--HDIKKDFYKKFLY-EPFPVESSLL--GVLSDHLNAEIAGGTITSKQDALDYITWTYFFrrlimnpsyynlgdvSQ 1778
Cdd:PRK02362 392 LLAksYDELDELFERYIWaDPEDVRSKLAtePALRTHVLSTIASGFARTRDGLLEFLEATFYA---------------TQ 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1779 DAINKFLSHLIGQSLVELELSHCIEvgEDNRSIEPLTCGRIASYYYlkhktvkmfkdrLKPeCSTEELLSILSDAEEYTD 1858
Cdd:PRK02362 457 TDDTGRLERVVDDVLDFLERNGMIE--EDGETLEATELGHLVSRLY------------IDP-LSAAEIIDGLEAAKKPTD 521
|
....*
gi 456367250 1859 LPVRH 1863
Cdd:PRK02362 522 LGLLH 526
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
479-674 |
6.61e-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: 172.94 E-value: 6.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 479 NRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFHqgvlkkneFKIVYVAPMKALAAEMTNYFSKRL-EP 557
Cdd:cd18022 3 NPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPG--------SKVVYIAPLKALVRERVDDWKKRFeEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 558 LGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVV-----TRKSVgdvalsQIVKLLILDEVHLLHEDRGPVLESIVART 632
Cdd:cd18022 75 LGKKVVELTGDVTPDMKALADADIIITTPEKWDGIsrswqTREYV------QQVSLIIIDEIHLLGSDRGPVLEVIVSRM 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 456367250 633 LRQVESTQSMIRILGLSATLPNYLDVATFLHVNPyIGLFYFD 674
Cdd:cd18022 149 NYISSQTEKPVRLVGLSTALANAGDLANWLGIKK-MGLFNFR 189
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
493-991 |
7.02e-48 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 185.16 E-value: 7.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNIAMLTVLHEIrqhfhqgvlkKNEFKIVYVAPMKALAAEMTNYFSkRLEPLGIVVKELTGDMQlS 572
Cdd:PRK02362 39 GKNLLAAIPTASGKTLIAELAMLKAI----------ARGGKALYIVPLRALASEKFEEFE-RFEELGVRVGISTGDYD-S 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 573 KSEIL-RTQMLVTTPEKWDVVTRKsvGDVALSQIvKLLILDEVHLL-HEDRGPVLESIVARTLRQVESTQsmirILGLSA 650
Cdd:PRK02362 107 RDEWLgDNDIIVATSEKVDSLLRN--GAPWLDDI-TCVVVDEVHLIdSANRGPTLEVTLAKLRRLNPDLQ----VVALSA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 651 TLPNYLDVATFLH----------VNPYIGLFY-----FDGRFRPVPlgqtflgikSANKMQQLNnmdevcyeSVLKQVKA 715
Cdd:PRK02362 180 TIGNADELADWLDaelvdsewrpIDLREGVFYggaihFDDSQREVE---------VPSKDDTLN--------LVLDTLEE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 716 GHQVMVFVHARnatvRTAMSLIERAKNSGQiscflPTQGPEYGHALKQVQK-----SRNKQVRELFS---DGFSIHHAGM 787
Cdd:PRK02362 243 GGQCLVFVSSR----RNAEGFAKRAASALK-----KTLTAAERAELAELAEeirevSDTETSKDLADcvaKGAAFHHAGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 788 LRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYAAKRGSfVDLGILDVMQIFGRAGRPQFDKFGEGII 867
Cdd:PRK02362 314 SREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAGM-QPIPVLEYHQMAGRAGRPGLDPYGEAVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 868 IT-THDKLS----HYLSLLTQqnPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWMSYTyLYvrmranplaygishkA 940
Cdd:PRK02362 393 LAkSYDELDelfeRYIWADPE--DVRSKLATepALRTHVLSTIASGFARTRDGLLEFLEAT-FY---------------A 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 456367250 941 YQMDPTLRKHReqLLIEVGQKLDKARMIrfEERTGYFSSTDLGRTASHYYI 991
Cdd:PRK02362 455 TQTDDTGRLER--VVDDVLDFLERNGMI--EEDGETLEATELGHLVSRLYI 501
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1345-1727 |
8.64e-47 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 182.06 E-value: 8.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKirieEKLGK-KVIELTGDVT--PDmksiak 1421
Cdd:COG4581 42 SVLVAAPTGSGKTLVAEFAIFLALAR--GRRSFYTAPIKALSNQKFFDLV----ERFGAeNVGLLTGDASvnPD------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1422 ADLIVTTPEkwdgVSRswqNRSY--------VQQVnilIIDEIHLLGE-ERGPVLEVIVsrtnfIssHTEKPVRIVGLST 1492
Cdd:COG4581 110 APIVVMTTE----ILR---NMLYregadledVGVV---VMDEFHYLADpDRGWVWEEPI-----I--HLPARVQLVLLSA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1493 ALANARDLADWLNikqmglfnfrpSV-----------RPVPLEvhiqgfpgQHYC--PRMASMNKPAFQAIRSHSPAK-- 1557
Cdd:COG4581 173 TVGNAEEFAEWLT-----------RVrgetavvvseeRPVPLE--------FHYLvtPRLFPLFRVNPELLRPPSRHEvi 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1558 ---------PVLIFVSSRRQTRLTALELIAFLATEEDPKQWLNMDEQEMENIIATVRDSNLKLTLAFGIGMHHAGLHERD 1628
Cdd:COG4581 234 eeldrggllPAIVFIFSRRGCDEAAQQLLSARLTTKEERAEIREAIDEFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPKY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1629 RKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKTRRyvdfPIT--DVLQMMGRAGRPQFDDQGKAVILV 1706
Cdd:COG4581 314 RRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHR----PLTarEFHQIAGRAGRRGIDTEGHVVVLA 389
|
410 420
....*....|....*....|....*
gi 456367250 1707 HDiKKDFyKKFLY----EPFPVESS 1727
Cdd:COG4581 390 PE-HDDP-KKFARlasaRPEPLRSS 412
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
493-1031 |
3.00e-46 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 179.31 E-value: 3.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNIAMltvlHEIRQHFHQGVlkknefKIVYVAPMKALAAEMTNYFSkRLEPLGIVVKELTGDMQLS 572
Cdd:PRK01172 37 GENVIVSVPTAAGKTLIAY----SAIYETFLAGL------KSIYIVPLRSLAMEKYEELS-RLRSLGMRVKISIGDYDDP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 573 KSEILRTQMLVTTPEKWDVVTRKsvgDVALSQIVKLLILDEVHLLH-EDRGPVLESiVARTLRQVESTqsmIRILGLSAT 651
Cdd:PRK01172 106 PDFIKRYDVVILTSEKADSLIHH---DPYIINDVGLIVADEIHIIGdEDRGPTLET-VLSSARYVNPD---ARILALSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 652 LPNYLDVATFLHVNPYIGlfyfdgRFRPVPLGqtfLGIKSANKM----QQLNNMDEVcyeSVLKQ-VKAGHQVMVFVHAR 726
Cdd:PRK01172 179 VSNANELAQWLNASLIKS------NFRPVPLK---LGILYRKRLildgYERSQVDIN---SLIKEtVNDGGQVLVFVSSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 727 NATVRTAMSLIERAknsGQISCFLPTQGPEYGHalkqvqksrNKQVRELFSDGFSIHHAGMLRQDRNLVENLFSNGHIKV 806
Cdd:PRK01172 247 KNAEDYAEMLIQHF---PEFNDFKVSSENNNVY---------DDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 807 LVCTATLAWGVNLPAHAVIIKGTQIYAAKRGSFvdLGILDVMQIFGRAGRPQFDKFGEGIII----TTHDKLSHYLSllT 882
Cdd:PRK01172 315 IVATPTLAAGVNLPARLVIVRDITRYGNGGIRY--LSNMEIKQMIGRAGRPGYDQYGIGYIYaaspASYDAAKKYLS--G 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 883 QQNPIESQF--LESLADNLNAEIALGTVTNVEEAVKWMSYTYLYVRMRANPLAYGISHKAYqmdptlrkhreqLLIEVGq 960
Cdd:PRK01172 391 EPEPVISYMgsQRKVRFNTLAAISMGLASSMEDLILFYNETLMAIQNGVDEIDYYIESSLK------------FLKENG- 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456367250 961 kldkarmirFEERTGYFSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEE 1031
Cdd:PRK01172 458 ---------FIKGDVTLRATRLGKLTSDLYIDPESALILKSAFDHDYDEDLALYYISLCREIIPANTRDDY 519
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1329-1514 |
2.28e-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: 162.98 E-value: 2.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1329 NPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTS---------KAVYIAPLKALVRERMDDWKIRIEe 1399
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQggvikkddfKIVYIAPMKALAAEMVEKFSKRLA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1400 KLGKKVIELTGDVTPDMKSIAKADLIVTTPEKWDGVSR-SWQNRSYVQQVNILIIDEIHLLGEERGPVLEVIVSRTNFIS 1478
Cdd:cd18020 82 PLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRkSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQV 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 456367250 1479 SHTEKPVRIVGLSTALANARDLADWLNIKQM-GLFNF 1514
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 ... |
476-666 |
2.40e-41 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 151.26 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 476 KRLNRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHeirqHFHQGvlkkNEFKIVYVAPMKALAAEMTNYFSKRL 555
Cdd:cd18021 2 KFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLR----HWRQN----PKGRAVYIAPMQELVDARYKDWRAKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 556 EP-LGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVV-----TRKSVgdvalsQIVKLLILDEVHLLHEDRGPVLESIV 629
Cdd:cd18021 74 GPlLGKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLsrrwkQRKNV------QSVELFIADELHLIGGENGPVYEVVV 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 456367250 630 ARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNP 666
Cdd:cd18021 148 SRMRYISSQLEKPIRIVGLSSSLANARDVGEWLGASK 184
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
1328-1507 |
4.43e-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: 141.32 E-value: 4.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1328 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIfrVFNKYPTSKAVYIAPLKALVRERMDDWKIRieEKLGKKVIE 1407
Cdd:cd18028 2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAM--VNTLLEGGKALYLVPLRALASEKYEEFKKL--EEIGLKVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1408 LTGDVTPDMKSIAKADLIVTTPEKWDGVsrsWQNR-SYVQQVNILIIDEIHLLG-EERGPVLEVIVSRTNfissHTEKPV 1485
Cdd:cd18028 78 STGDYDEDDEWLGDYDIIVATYEKFDSL---LRHSpSWLRDVGVVVVDEIHLISdEERGPTLESIVARLR----RLNPNT 150
|
170 180
....*....|....*....|..
gi 456367250 1486 RIVGLSTALANARDLADWLNIK 1507
Cdd:cd18028 151 QIIGLSATIGNPDELAEWLNAE 172
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
489-891 |
2.29e-35 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 146.62 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 489 AYNTNENMLICAPTGAGKTNIAMltvlHEIRQHFHQGVlkknefKIVYVAPMKALAAEmtNYF--SKRL--EPLGIvvke 564
Cdd:COG4581 36 ALEAGRSVLVAAPTGSGKTLVAE----FAIFLALARGR------RSFYTAPIKALSNQ--KFFdlVERFgaENVGL---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 565 LTGDMQL--------SKSEILRTQMLVTTPEKWDVvtrksvgDVAlsqivkllILDEVHLLHE-DRGPVLE-SIVARTLR 634
Cdd:COG4581 100 LTGDASVnpdapivvMTTEILRNMLYREGADLEDV-------GVV--------VMDEFHYLADpDRGWVWEePIIHLPAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 635 qvestqsmIRILGLSATLPNYLDVATFLH--------VnpyiglfyfDGRFRPVPLGQTFLGIKSANKMQQLNNMDEVCY 706
Cdd:COG4581 165 --------VQLVLLSATVGNAEEFAEWLTrvrgetavV---------VSEERPVPLEFHYLVTPRLFPLFRVNPELLRPP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 707 E--SVLKQVKAGHQ--VMVFVHARNATVRTAMSLI--------ERAKNSGQISCFLPTQGPEYGHALkqvqksrnkqvRE 774
Cdd:COG4581 228 SrhEVIEELDRGGLlpAIVFIFSRRGCDEAAQQLLsarlttkeERAEIREAIDEFAEDFSVLFGKTL-----------SR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 775 LFSDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGtqiyAAKR--GSFVDLGILDVMQIFG 852
Cdd:COG4581 297 LLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTK----LSKFdgERHRPLTAREFHQIAG 372
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 456367250 853 RAGRPQFDKFGEGIIITT-HDKLSHYLSLLTQQ-NPIESQF 891
Cdd:COG4581 373 RAGRRGIDTEGHVVVLAPeHDDPKKFARLASARpEPLRSSF 413
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
479-657 |
4.49e-33 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 126.59 E-value: 4.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 479 NRIQSIVFDTAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQhfhqgvlKKNEFKIVYVAPMKALAAEMTNYFSKRLEPL 558
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK-------LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 559 GIVVKELTGDMQLSK--SEILRTQMLVTTPEKWDVVTRKSvgdVALSQiVKLLILDEVHLLHE-DRGPVLESIVARtlrq 635
Cdd:pfam00270 73 GLKVASLLGGDSRKEqlEKLKGPDILVGTPGRLLDLLQER---KLLKN-LKLLVLDEAHRLLDmGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|..
gi 456367250 636 vesTQSMIRILGLSATLPNYLD 657
Cdd:pfam00270 145 ---LPKKRQILLLSATLPRNLE 163
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1329-1500 |
3.17e-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: 3.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1329 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFN-KYPTSKAVYIAPLKALVRERMDDWKiRIEEKLGKKVIE 1407
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDkLDNGPQALVLAPTRELAEQIYEELK-KLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1408 LTGDVTP--DMKSIAKADLIVTTPEKWDGVsrsWQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNfisshteKP 1484
Cdd:pfam00270 79 LLGGDSRkeQLEKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRRLP-------KK 148
|
170
....*....|....*..
gi 456367250 1485 VRIVGLS-TALANARDL 1500
Cdd:pfam00270 149 RQILLLSaTLPRNLEDL 165
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
477-662 |
1.02e-28 |
|
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: 114.74 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 477 RLNRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHEIrqhfhqgvLKKNefKIVYVAPMKALAAEMTNYFSKrLE 556
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTL--------LEGG--KALYLVPLRALASEKYEEFKK-LE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 557 PLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSvgdVALSQIVKLLILDEVHLLH-EDRGPVLESIVARTLRQ 635
Cdd:cd18028 70 EIGLKVGISTGDYDEDDEWLGDYDIIVATYEKFDSLLRHS---PSWLRDVGVVVVDEIHLISdEERGPTLESIVARLRRL 146
|
170 180
....*....|....*....|....*..
gi 456367250 636 VESTQsmirILGLSATLPNYLDVATFL 662
Cdd:cd18028 147 NPNTQ----IIGLSATIGNPDELAEWL 169
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
470-681 |
6.76e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 107.19 E-value: 6.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 470 LAFKGMKRLNRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFHQGVLkknefkivYVAPMKALAAEMTN 549
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVL--------VLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 550 YFSKRLEPLGIVVKELTGD----MQLSKSEILRTQMLVTTPEKWDVVTRKsvGDVALSQiVKLLILDEVH-LLHEDRGPV 624
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRLLDLLEN--DKLSLSN-VDLVILDEAHrLLDGGFGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 456367250 625 LESIVARTLRqvestqsMIRILGLSATLPNYLDVATFLHVNpyiGLFYFDGRFRPVP 681
Cdd:smart00487 150 LEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1330-1706 |
1.06e-25 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 115.76 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1330 PVQT-QIFHTLYHTDcNVLLGAPTGSGKTVAAELA-IFRVFNKypTSKAVYIAPLKALVRERMDDWKIRIEEKLgkKVIE 1407
Cdd:COG1202 212 PVQSlAVENGLLEGK-DQLVVSATATGKTLIGELAgIKNALEG--KGKMLFLVPLVALANQKYEDFKDRYGDGL--DVSI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1408 LTGDV---TPDMKSIAKADLIVTTPEKWDGVSRSwqnRSYVQQVNILIIDEIHLLGE-ERGPVLEVIVSRTNFISSHTEk 1483
Cdd:COG1202 287 RVGASrirDDGTRFDPNADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEVHMLEDpERGHRLDGLIARLKYYCPGAQ- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1484 pvrIVGLSTALANARDLADWLNIKQMgLFNfrpsVRPVPLEVHIQGFPGQHYCPRMASMNKPAFQAIRSHSPAKPVLIFV 1563
Cdd:COG1202 363 ---WIYLSATVGNPEELAKKLGAKLV-EYE----ERPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1564 SSRRQTRltaleliaflateedpkqwlnmdeqemeniiatvrdsnlKLTLAFGIGM--HHAGLHERDRKTVEELFVNCKV 1641
Cdd:COG1202 435 NSRRRCH---------------------------------------EIARALGYKAapYHAGLDYGERKKVERRFADQEL 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456367250 1642 QVLIATSTLAWGVNFPAHLVIIK----GTEYydgktrryvdFPITDVLQMMGRAGRPQFDDQGKAVILV 1706
Cdd:COG1202 476 AAVVTTAALAAGVDFPASQVIFDslamGIEW----------LSVQEFHQMLGRAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1323-1522 |
4.86e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 104.88 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1323 YNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLG 1402
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1403 KKVIELTGDVT-PDMKSIAK--ADLIVTTPEKWDGVSRswQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNfis 1478
Cdd:smart00487 84 KVVGLYGGDSKrEQLRKLESgkTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 456367250 1479 shteKPVRIVGLS-TALANARDLADWLNIkqmGLFNFRPSVRPVP 1522
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 ... |
1343-1516 |
1.45e-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: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1343 DCNVLLGAPTGSGKTVAAELAIFRVF--NKyptSKAVYIAPLKALVRERMDdWKIRIEEKLGKKVIELTGDVTPDM-KSI 1419
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLleRR---KKALFVLPYVSIVQEKVD-ALSPLFEELGFRVEGYAGNKGRSPpKRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1420 AKADLIVTTPEKWDG-VSRSWQNRSyVQQVNILIIDEIHLLGEE-RGPVLEVIVSRtnfISSHTEKPVRIVGLSTALANA 1497
Cdd:cd18026 109 KSLSVAVCTIEKANSlVNSLIEEGR-LDELGLVVVDELHMLGDGhRGALLELLLTK---LLYAAQKNIQIVGMSATLPNL 184
|
170 180
....*....|....*....|.
gi 456367250 1498 RDLADWLNIKqmgLF--NFRP 1516
Cdd:cd18026 185 EELASWLRAE---LYttNFRP 202
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
1345-1504 |
2.03e-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: 93.03 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKYPTS--KAVYIAPLKALVRermdDWKIRIEE-----KLGKKVIELTGDVTPDMK 1417
Cdd:cd17922 3 NVLIAAPTGSGKTEAAFLPALSSLADEPEKgvQVLYISPLKALIN----DQERRLEEpldeiDLEIPVAVRHGDTSQSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1418 SIAKA---DLIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRtnfISSHTEKPVRIVGLSTA 1493
Cdd:cd17922 79 AKQLKnppGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHaLLGSKRGVQLELLLER---LRKLTGRPLRRIGLSAT 155
|
170
....*....|.
gi 456367250 1494 LANARDLADWL 1504
Cdd:cd17922 156 LGNLEEAAAFL 166
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
493-662 |
1.78e-20 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 90.34 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNIAMLTVLHEIRQHFHQGVlkknefKIVYVAPMKALAAEMTnyfsKRLE------PLGIVVKELT 566
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV------QVLYISPLKALINDQE----RRLEepldeiDLEIPVAVRH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 567 GDM-QLSKSEILRT--QMLVTTPEKWDVVTRKSVGDVALSQiVKLLILDEVH-LLHEDRGPVLESIVARtLRQVESTQsm 642
Cdd:cd17922 71 GDTsQSEKAKQLKNppGILITTPESLELLLVNKKLRELFAG-LRYVVVDEIHaLLGSKRGVQLELLLER-LRKLTGRP-- 146
|
170 180
....*....|....*....|
gi 456367250 643 IRILGLSATLPNYLDVATFL 662
Cdd:cd17922 147 LRRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
493-679 |
3.57e-20 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 90.74 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNIAMLTVLHEIRQhfhqgvlkkNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDmqLS 572
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLLE---------RRKKALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGN--KG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 573 KSEILR---TQMLVTTPEKWDVVTRKSVGDVALSQIvKLLILDEVHLLHE-DRGPVLESIVARTLRqveSTQSMIRILGL 648
Cdd:cd18026 102 RSPPKRrksLSVAVCTIEKANSLVNSLIEEGRLDEL-GLVVVDELHMLGDgHRGALLELLLTKLLY---AAQKNIQIVGM 177
|
170 180 190
....*....|....*....|....*....|.
gi 456367250 649 SATLPNYLDVATFLHVnpyiglFYFDGRFRP 679
Cdd:cd18026 178 SATLPNLEELASWLRA------ELYTTNFRP 202
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1325-1662 |
8.38e-19 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 93.63 E-value: 8.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1325 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAIF-RVFNKYPTSKA------VYIAPLKAL---VRERMDDWK 1394
Cdd:COG1201 22 FGAPTPPQREAW-PAIAAGESTLLIAPTGSGKTLAAFLPALdELARRPRPGELpdglrvLYISPLKALandIERNLRAPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1395 IRIEEKLGKKVIEL-----TGDVTPDMKSIAKA---DLIVTTPE---------KWdgvsrswqnRSYVQQVNILIIDEIH 1457
Cdd:COG1201 101 EEIGEAAGLPLPEIrvgvrTGDTPASERQRQRRrppHILITTPEslallltspDA---------RELLRGVRTVIVDEIH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1458 -LLGEERGPVLEVIVSRtnfISSHTEKPVRIVGLSTALANARDLADWLnikqMGLFNFRPS--VRP-----------VPL 1523
Cdd:COG1201 172 aLAGSKRGVHLALSLER---LRALAPRPLQRIGLSATVGPLEEVARFL----VGYEDPRPVtiVDAgagkkpdlevlVPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1524 EVHIQGFP-----GQHYCPRMAsmnkpafQAIRSHspaKPVLIFVSSRRQTRLTALELIAFLATEEDPkqwlnmdeqeme 1598
Cdd:COG1201 245 EDLIERFPwaghlWPHLYPRVL-------DLIEAH---RTTLVFTNTRSQAERLFQRLNELNPEDALP------------ 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456367250 1599 niiatvrdsnlkltlafgIGMHHAGL-HERdRKTVEELFVNCKVQVLIATSTLAWGVNFPA-HLVI 1662
Cdd:COG1201 303 ------------------IAAHHGSLsREQ-RLEVEEALKAGELRAVVATSSLELGIDIGDvDLVI 349
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
470-878 |
1.41e-16 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 86.43 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 470 LAFKGMKRLNRIQSIVFDTAYNtNENMLICAPTGAGKTNIAMLTVLHEIrqhfhqgvLKKNEFKIVYVAPMKALAA---- 545
Cdd:COG1205 49 LKKRGIERLYSHQAEAIEAARA-GKNVVIATPTASGKSLAYLLPVLEAL--------LEDPGATALYLYPTKALARdqlr 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 546 EMTNYFSKRlePLGIVVKELTGDMQLS-KSEILRT-QMLVTTP-----------EKWDVVTRKsvgdvalsqiVKLLILD 612
Cdd:COG1205 120 RLRELAEAL--GLGVRVATYDGDTPPEeRRWIREHpDIVLTNPdmlhygllphhTRWARFFRN----------LRYVVID 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 613 EVHLLhedRGpVLESIVA----RTLRQVESTQSMIRILGLSATLPNYLDVA---------------------TFLHVNPY 667
Cdd:COG1205 188 EAHTY---RG-VFGSHVAnvlrRLRRICRHYGSDPQFILASATIGNPAEHAerltgrpvtvvdedgsprgerTFVLWNPP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 668 IglfYFDGRFRpvplgqtflgikSANKmqqlnnmdEVCYesVLKQ-VKAGHQVMVFVHARNATVRTAMSLIERAKNsgqi 746
Cdd:COG1205 264 L---VDDGIRR------------SALA--------EAAR--LLADlVREGLRTLVFTRSRRGAELLARYARRALRE---- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 747 scflptqgPEYGHALkqvqksrnkqvrelfsdgfSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPA-HAVI 825
Cdd:COG1205 315 --------PDLADRV-------------------AAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVV 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 456367250 826 IKGtqiYAAKRGSFVdlgildvmQIFGRAGRPQFDkfGEGIIITTHDKLSHYL 878
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 ... |
1347-1662 |
3.20e-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: 85.30 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1347 LLGAPTGSGKTVAAELAIFRVFNKYPTSK-----AVYIAPLKALVR----------ERMdDWKIRIEEKlgkkvielTGD 1411
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKekglhTLYITPLRALAVdiarnlqapiEEL-GLPIRVETR--------TGD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1412 VTPDMKSIAKA---DLIVTTPEkwdgvsrSWQ-------NRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNFISSH 1480
Cdd:TIGR04121 103 TSSSERARQRKkppDILLTTPE-------SLAlllsypdAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1481 tekpVRIVGLSTALANARDLADWLnikqMGLFNFRPSV------RPVPLEV----HIQGFP-GQHYCPRMASmnkPAFQA 1549
Cdd:TIGR04121 176 ----LRRWGLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISllpeSEERFPwAGHLGLRALP---EVYAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1550 IRSHspaKPVLIFVSSRRQTRLTALELIAFLAteedpkqwlnmdeqemeniiatvrDSNLKltlafgIGMHHAGLHERDR 1629
Cdd:TIGR04121 245 IDQA---RTTLVFTNTRSQAELWFQALWEANP------------------------EFALP------IALHHGSLDREQR 291
|
330 340 350
....*....|....*....|....*....|....
gi 456367250 1630 KTVEELFVNCKVQVLIATSTLAWGVNF-PAHLVI 1662
Cdd:TIGR04121 292 RWVEAAMAAGRLRAVVCTSSLDLGVDFgPVDLVI 325
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
1345-1491 |
7.09e-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: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDdwKIRIEEKLGKKVIELTGDVTP---DMKSIAK 1421
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKG-KKVLVLVPTKALALQTAE--RLRELFGPGIRVAVLVGGSSAeerEKNKLGD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456367250 1422 ADLIVTTPEKWDGVSRSwQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTnfissHTEKPVRIVGLS 1491
Cdd:cd00046 80 ADIIIATPDMLLNLLLR-EDRLFLKDLKLIIVDEAHaLLIDSRGALILDLAVRK-----AGLKNAQVILLS 144
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
455-859 |
2.44e-15 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 82.25 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 455 EEKPVYIQDLDEVGQlaFKGM-----KRLNRIQSIVFDTAYNTNENMLICAPTGAGKTNIAMLTVLHEIrqhfhqgvlKK 529
Cdd:COG1202 184 EVDTVPVDDLDLPPE--LKDLlegrgEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAGIKNA---------LE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 530 NEFKIVYVAPMKALAAEMTNYFSKRLEPlGIVVKELTGDMQLSKSE---ILRTQMLVTTPEKWDVVTR--KSVGDVALsq 604
Cdd:COG1202 253 GKGKMLFLVPLVALANQKYEDFKDRYGD-GLDVSIRVGASRIRDDGtrfDPNADIIVGTYEGIDHALRtgRDLGDIGT-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 605 ivklLILDEVHLLHE-DRGPVLESIVARtLRQV-ESTQsmirILGLSATLPNYLDVATFLHVNpyigLFYFDGRfrPVPL 682
Cdd:COG1202 330 ----VVIDEVHMLEDpERGHRLDGLIAR-LKYYcPGAQ----WIYLSATVGNPEELAKKLGAK----LVEYEER--PVPL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 683 GQ--TFlgiksANKMQQLNNMDEVCYESVLKQVKAGH--QVMVFVHARnatvrtamslieraKNSGQISCFLPTQGPEYg 758
Cdd:COG1202 395 ERhlTF-----ADGREKIRIINKLVKREFDTKSSKGYrgQTIIFTNSR--------------RRCHEIARALGYKAAPY- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 759 halkqvqksrnkqvrelfsdgfsihHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIikgtqiyaakrgs 838
Cdd:COG1202 455 -------------------------HAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVI------------- 496
|
410 420
....*....|....*....|....*...
gi 456367250 839 FVDL--GI--LDV---MQIFGRAGRPQF 859
Cdd:COG1202 497 FDSLamGIewLSVqefHQMLGRAGRPDY 524
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1615-1694 |
7.73e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 71.47 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1615 FGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryVDFPITDVLQMMGRAGR 1693
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVII-----YD------LPWSPASYIQRIGRAGR 80
|
.
gi 456367250 1694 P 1694
Cdd:smart00490 81 A 81
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
489-857 |
9.45e-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: 80.29 E-value: 9.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 489 AYNTNENMLICAPTGAGKTNIAMLTVLHEIrqhFHQGVLKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLG--IVVKELT 566
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSLIDL---AGPEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGlpIRVETRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 567 GDMQLSKSEILRTQM---LVTTPEKWDVVTrkSVGDVA-LSQIVKLLILDEVH-LLHEDRGPVLESIVARtLRQvesTQS 641
Cdd:TIGR04121 101 GDTSSSERARQRKKPpdiLLTTPESLALLL--SYPDAArLFKDLRCVVVDEWHeLAGSKRGDQLELALAR-LRR---LAP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 642 MIRILGLSATLPNyLDVA--TFLHVNPYIGLFYFDGRFRPVPL-------GQTF-----LGIKSAnkmqqlnnmdevcyE 707
Cdd:TIGR04121 175 GLRRWGLSATIGN-LEEArrVLLGVGGAPAVLVRGKLPKAIEVisllpesEERFpwaghLGLRAL--------------P 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 708 SVLKQVKAGHQVMVFVHARNATVRTAMSLIEraknsgqiscflptqgpeyghalkqvqksrnkqVRELFSDGFSIHHAGM 787
Cdd:TIGR04121 240 EVYAEIDQARTTLVFTNTRSQAELWFQALWE---------------------------------ANPEFALPIALHHGSL 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456367250 788 LRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIkgtQIYAAKrgsfvdlGILDVMQIFGRAG-RP 857
Cdd:TIGR04121 287 DREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSPK-------GVARLLQRAGRSNhRP 347
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1290-1736 |
1.30e-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: 79.88 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1290 HLILPERHPPHTELLD-LQPLPVTALGCKAYEALYnfSHfnpvQTQIFHtLYHTDCNVLLGAPTGSGKTVAAELAIFRVF 1368
Cdd:COG1205 24 VRTIPAREARYAPWPDwLPPELRAALKKRGIERLY--SH----QAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1369 NKYPTSKAVYIAPLKALVRERMDDWKiRIEEKLGK--KVIELTGDVTPDMKS--IAKADLIVTTP-----------EKWd 1433
Cdd:COG1205 97 LEDPGATALYLYPTKALARDQLRRLR-ELAEALGLgvRVATYDGDTPPEERRwiREHPDIVLTNPdmlhygllphhTRW- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1434 gvSRSWQNRSYVqqvnilIIDEIHLLgeeRGpvleV-------IVSRTNFISSHTEKPVRIVGLSTALANARDLAdwlni 1506
Cdd:COG1205 175 --ARFFRNLRYV------VIDEAHTY---RG----VfgshvanVLRRLRRICRHYGSDPQFILASATIGNPAEHA----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1507 kqMGLFNfrpsvRPVpleVHIQG----FPGQHycprMASMNKPAFQAIRSHSPAK--------------PVLIFVSSRRQ 1568
Cdd:COG1205 235 --ERLTG-----RPV---TVVDEdgspRGERT----FVLWNPPLVDDGIRRSALAeaarlladlvreglRTLVFTRSRRG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1569 TRLTALELIAFLATEEDPkqwlnmdeqemENIIAtvrdsnlkltlafgigmHHAGLHERDRKTVEELFVNCKVQVLIATS 1648
Cdd:COG1205 301 AELLARYARRALREPDLA-----------DRVAA-----------------YRAGYLPEERREIERGLRSGELLGVVSTN 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1649 TLAWGVNFPA-HLVIIKGteyydgktrryvdFP--ITDVLQMMGRAGRpqfDDQGKAVILV--HDIKKDFYKK---FLYE 1720
Cdd:COG1205 353 ALELGIDIGGlDAVVLAG-------------YPgtRASFWQQAGRAGR---RGQDSLVVLVagDDPLDQYYVRhpeELFE 416
|
490 500
....*....|....*....|.
gi 456367250 1721 PfPVESSLLG-----VLSDHL 1736
Cdd:COG1205 417 R-PPEAAVIDpdnpyVLAPHL 436
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
494-871 |
1.37e-14 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 79.76 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 494 ENMLICAPTGAGKTNIAMLTVLHEIRQHFHQGVLkKNEFKIVYVAPMKALA-----------AEMTNYFSKRLEPLGIVV 562
Cdd:COG1201 40 ESTLLIAPTGSGKTLAAFLPALDELARRPRPGEL-PDGLRVLYISPLKALAndiernlraplEEIGEAAGLPLPEIRVGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 563 KelTGDMqlSKSEilRTQM-------LVTTPE---------KWdvvtRKSVGDvalsqiVKLLILDEVHLLHED-RGPVL 625
Cdd:COG1201 119 R--TGDT--PASE--RQRQrrrpphiLITTPEslallltspDA----RELLRG------VRTVIVDEIHALAGSkRGVHL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 626 ESIVARtLRQVeSTQSMIRIlGLSATLPNYLDVATFLhvnpyIGlfyfDGRFRPVPLGQTFLG----IKS-------ANK 694
Cdd:COG1201 183 ALSLER-LRAL-APRPLQRI-GLSATVGPLEEVARFL-----VG----YEDPRPVTIVDAGAGkkpdLEVlvpvedlIER 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 695 MQQLNNMDEVCYESVLKQVKAGHQVMVFVHARNATVRTAMSLIERAknsgqiscflptqgPEYGHALKqvqksrnkqvre 774
Cdd:COG1201 251 FPWAGHLWPHLYPRVLDLIEAHRTTLVFTNTRSQAERLFQRLNELN--------------PEDALPIA------------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 775 lfsdgfsIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLA----WG-VNLpahaVIikgtQIYAAK---RGsfvdlgild 846
Cdd:COG1201 305 -------AHHGSLSREQRLEVEEALKAGELRAVVATSSLElgidIGdVDL----VI----QVGSPKsvaRL--------- 360
|
410 420
....*....|....*....|....*
gi 456367250 847 vMQIFGRAGRpQFDKFGEGIIITTH 871
Cdd:COG1201 361 -LQRIGRAGH-RVGEVSKGRLVPTH 383
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
493-654 |
1.93e-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: 73.94 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNI---AMLTVLHEirqhfhqgvlkKNEFKIVYVAPMKAL----AAEMTNYFSKRLEPLGIVV-KE 564
Cdd:cd18025 16 RESALIVAPTSSGKTFIsyyCMEKVLRE-----------SDDGVVVYVAPTKALvnqvVAEVYARFSKKYPPSGKSLwGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 565 LTGDMQLskSEILRTQMLVTTPEKWDVVTRkSVGDVALSQIVKLLILDEVHLL-HEDRGPVLESIVArtlrqvestqsMI 643
Cdd:cd18025 85 FTRDYRH--NNPMNCQVLITVPECLEILLL-SPHNASWVPRIKYVIFDEIHSIgQSEDGAVWEQLLL-----------LI 150
|
170
....*....|...
gi 456367250 644 R--ILGLSATLPN 654
Cdd:cd18025 151 PcpFLALSATIGN 163
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
493-651 |
1.89e-13 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 69.74 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNIAMLTVLHEirqhfhqgvLKKNEFKIVYVAPMKALAAEMTNYFsKRLEPLGIVVKELTGDM--- 569
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLL---------LLKKGKKVLVLVPTKALALQTAERL-RELFGPGIRVAVLVGGSsae 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 570 QLSKSEILRTQMLVTTPEKwdvVTRKSVGDVALSQI-VKLLILDEVH-LLHEDRGPVLESIVARTLRQVEStqsmiRILG 647
Cdd:cd00046 71 EREKNKLGDADIIIATPDM---LLNLLLREDRLFLKdLKLIIVDEAHaLLIDSRGALILDLAVRKAGLKNA-----QVIL 142
|
....
gi 456367250 648 LSAT 651
Cdd:cd00046 143 LSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
779-857 |
6.47e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 66.08 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 779 GFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIKGtqiyaakrgsfVDLGILDVMQIFGRAGRP 857
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASYIQRIGRAGRA 81
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
494-651 |
8.14e-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: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 494 ENMLICAPTGAGKTNIAMLtvlheIRQHFHQGVLKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLSK 573
Cdd:cd17927 18 KNTIICLPTGSGKTFVAVL-----ICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 574 S---EILRTQMLVTTPEKWdVVTRKSVGDVALSqIVKLLILDEVHllHEDRGPVLESIVARTLRQ-VESTQSMIRILGLS 649
Cdd:cd17927 93 SveqIVESSDVIIVTPQIL-VNDLKSGTIVSLS-DFSLLVFDECH--NTTKNHPYNEIMFRYLDQkLGSSGPLPQILGLT 168
|
..
gi 456367250 650 AT 651
Cdd:cd17927 169 AS 170
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
1346-1504 |
7.20e-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: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1346 VLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDwkirIEEKLGKkVIELTGDVT--PDmksiakAD 1423
Cdd:cd18024 50 VLVSAHTSAGKTVVAEYAIAQSLRD--KQRVIYTSPIKALSNQKYRE----LQEEFGD-VGLMTGDVTinPN------AS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1424 LIVTTPEkwdgVSRS--WQNRSYVQQVNILIIDEIHLLGE-ERGPVLEvivsRTNFISSHTekpVRIVGLSTALANARDL 1500
Cdd:cd18024 117 CLVMTTE----ILRSmlYRGSEIMREVAWVIFDEIHYMRDkERGVVWE----ETIILLPDK---VRYVFLSATIPNARQF 185
|
....
gi 456367250 1501 ADWL 1504
Cdd:cd18024 186 AEWI 189
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1350-1692 |
7.31e-11 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 68.03 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1350 APTGSGKTVAAEL-AIFRVF----------NKYPTSKAVYIAPLKALVRERMDDWKIRIE------EKLGKKVIELT-GD 1411
Cdd:PRK09751 3 APTGSGKTLAAFLyALDRLFreggedtreaHKRKTSRILYISPIKALGTDVQRNLQIPLKgiaderRRRGETEVNLRvGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1412 VTPDMKSIAKA-------DLIVTTPEKWDGVSRSwQNRSYVQQVNILIIDEIH-LLGEERGPVLEVIVSRTNFIsSHTek 1483
Cdd:PRK09751 83 RTGDTPAQERSkltrnppDILITTPESLYLMLTS-RARETLRGVETVIIDEVHaVAGSKRGAHLALSLERLDAL-LHT-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1484 PVRIVGLSTALANARDLADWLNIKQMGLFNFRPSVR--------PVPLEVHIQGFPGQH----YCPRMASMnKPAFQA-- 1549
Cdd:PRK09751 159 SAQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRhpqirivvPVANMDDVSSVASGTgedsHAGREGSI-WPYIETgi 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1550 IRSHSPAKPVLIFVSSRRQT-RLTAL--ELIA--FLATEEDPKqwlnmDEQEMENIIATV--RDSNLKLTLAFGigmHHA 1622
Cdd:PRK09751 238 LDEVLRHRSTIVFTNSRGLAeKLTARlnELYAarLQRSPSIAV-----DAAHFESTSGATsnRVQSSDVFIARS---HHG 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456367250 1623 GLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKgteyydgktrryVDFP--ITDVLQMMGRAG 1692
Cdd:PRK09751 310 SVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQ------------VATPlsVASGLQRIGRAG 369
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
1334-1709 |
3.30e-10 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 65.05 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1334 QIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTskaVYIAPLKALVRermdDWKIRIEEKLGKkvIELTGDVT 1413
Cdd:COG1061 91 ALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV---LVLVPRRELLE----QWAEELRRFLGD--PLAGGGKK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1414 PDmksiaKADLIVTTpekWDGVSRSWQNRSYVQQVNILIIDEIHLLGeerGPVLEVIVSRTNfisshtekPVRIVGLS-T 1492
Cdd:COG1061 162 DS-----DAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHAG---APSYRRILEAFP--------AAYRLGLTaT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1493 AlanardladwlnikqmglfnFRPSVRPVPLEVhiqgFPGQHYcprmasmNKPAFQAIRSHSPAKPVLIfvssRRQTRLT 1572
Cdd:COG1061 223 P--------------------FRSDGREILLFL----FDGIVY-------EYSLKEAIEDGYLAPPEYY----GIRVDLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1573 AlELIAFLATEEDPKQWLNMDEQEMENIIATVRDSNLKL--TLAFGIGMHHA-------------------GLHERDRKT 1631
Cdd:COG1061 268 D-ERAEYDALSERLREALAADAERKDKILRELLREHPDDrkTLVFCSSVDHAealaellneagiraavvtgDTPKKEREE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1632 VEELFVNCKVQVLIATSTLAWGVNFPA--HLVIIKGTeyydgKTRRYvdfpitdVLQMMGRAGRPqfdDQGKAVILVHDI 1709
Cdd:COG1061 347 ILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPT-----GSPRE-------FIQRLGRGLRP---APGKEDALVYDF 411
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1599-1693 |
3.44e-10 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 59.15 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1599 NIIATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryV 1677
Cdd:pfam00271 23 QTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YD------L 91
|
90
....*....|....*.
gi 456367250 1678 DFPITDVLQMMGRAGR 1693
Cdd:pfam00271 92 PWNPASYIQRIGRAGR 107
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1329-1512 |
4.06e-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: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1329 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIfrVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEklgkkVIEL 1408
Cdd:cd18027 10 DVFQKQAILHLEAGD-SVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGD-----VGLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1409 TGDVT--PDMKSiakadLIVTTPekwdgVSRS--WQNRSYVQQVNILIIDEIHLLGE-ERGPVLEVIVSrtnFISSHtek 1483
Cdd:cd18027 82 TGDVQlnPEASC-----LIMTTE-----ILRSmlYNGSDVIRDLEWVIFDEVHYINDaERGVVWEEVLI---MLPDH--- 145
|
170 180 190
....*....|....*....|....*....|
gi 456367250 1484 pVRIVGLSTALANARDLADWLN-IKQMGLF 1512
Cdd:cd18027 146 -VSIILLSATVPNTVEFADWIGrIKKKNIY 174
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1346-1505 |
4.07e-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: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1346 VLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLGKKVIELTGDVTPD--MKSIAKAD 1423
Cdd:cd18025 19 ALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYPPSGKSLWGVFTRDyrHNNPMNCQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1424 LIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIHLLG-EERGPVLEVIVsrtnfisshTEKPVRIVGLSTALANARDLAD 1502
Cdd:cd18025 99 VLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGqSEDGAVWEQLL---------LLIPCPFLALSATIGNPQKFHE 169
|
...
gi 456367250 1503 WLN 1505
Cdd:cd18025 170 WLQ 172
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
493-820 |
5.14e-10 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 64.91 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNIAMLTVLHEIRQHFHQGVLkKNEFKIVYVAPMKALAAEMtnyfsKR--LEPL-GI--VVKEL-- 565
Cdd:PRK13767 47 GKNVLISSPTGSGKTLAAFLAIIDELFRLGREGEL-EDKVYCLYVSPLRALNNDI-----HRnlEEPLtEIreIAKERge 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 566 ----------TGDM-QLSKSEILRT--QMLVTTPEKWDVVT-----RKSVGDvalsqiVKLLILDEVHLLHED-RGPVLe 626
Cdd:PRK13767 121 elpeirvairTGDTsSYEKQKMLKKppHILITTPESLAILLnspkfREKLRT------VKWVIVDEIHSLAENkRGVHL- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 627 sivARTLRQVES--TQSMIRIlGLSATLPNYLDVATFLhvnpyiGLFYFDGRFRPVPLGQT-F---LGIK---------- 690
Cdd:PRK13767 194 ---SLSLERLEElaGGEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDCEIVDArFvkpFDIKvispvddlih 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 691 -SANKMQqlnnmdEVCYESVLKQVKAGHQVMVFVHARNATVRTAMSLieraknsgqiscflptqgpeyghalkqvqksrn 769
Cdd:PRK13767 264 tPAEEIS------EALYETLHELIKEHRTTLIFTNTRSGAERVLYNL--------------------------------- 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 456367250 770 kqvRELFSDGFSI-----HHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP 820
Cdd:PRK13767 305 ---RKRFPEEYDEdnigaHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG 357
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
494-659 |
1.31e-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: 59.52 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 494 ENMLICAPTGAGKTNIAMLTVLHEIrqhfhqgvLKKNEFKIVYVAPMKALAAEMTNYFSKRLEPL--GIVVKELTGDMQL 571
Cdd:cd17923 16 RSVVVTTGTASGKSLCYQLPILEAL--------LRDPGSRALYLYPTKALAQDQLRSLRELLEQLglGIRVATYDGDTPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 572 SKSEILRTQ---MLVTTPEKWDV-VTRKSVGDVALSQIVKLLILDEVHLLhedRGpVLESIVA----RTLRQVESTQSMI 643
Cdd:cd17923 88 EERRAIIRNpprILLTNPDMLHYaLLPHHDRWARFLRNLRYVVLDEAHTY---RG-VFGSHVAlllrRLRRLCRRYGADP 163
|
170
....*....|....*.
gi 456367250 644 RILGLSATLPNYLDVA 659
Cdd:cd17923 164 QFILTSATIGNPAEHA 179
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1325-1491 |
1.37e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 63.75 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1325 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAI----FRVFNK-------YptskAVYIAPLKAL---VRERM 1390
Cdd:PRK13767 30 FGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREgeledkvY----CLYVSPLRALnndIHRNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1391 DDWKIRIEEKLGKKVIEL--------TGDVTPDMKS--------IakadLIvTTPEKWDGVSRSWQNRSYVQQVNILIID 1454
Cdd:PRK13767 105 EEPLTEIREIAKERGEELpeirvairTGDTSSYEKQkmlkkpphI----LI-TTPESLAILLNSPKFREKLRTVKWVIVD 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 456367250 1455 EIHLLGE-ERGPVLEVIVSRTNFISSHteKPVRIvGLS 1491
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 ... |
1345-1501 |
2.36e-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: 58.75 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVR---ERMDDWKIRIEEKLgkKVIELTGDvTP--DMKSI 1419
Cdd:cd17923 17 SVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQdqlRSLRELLEQLGLGI--RVATYDGD-TPreERRAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1420 AK--ADLIVTTP-----------EKWDGVSRSWQnrsYVqqvnilIIDEIH----LLGEERGPVLEVIVSRTNFISSHte 1482
Cdd:cd17923 94 IRnpPRILLTNPdmlhyallphhDRWARFLRNLR---YV------VLDEAHtyrgVFGSHVALLLRRLRRLCRRYGAD-- 162
|
170
....*....|....*....
gi 456367250 1483 kpVRIVGLSTALANARDLA 1501
Cdd:cd17923 163 --PQFILTSATIGNPAEHA 179
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
498-855 |
7.51e-09 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 61.48 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 498 ICAPTGAGKTNIAMltvLHEIRQHFHQGVL------KKNEFKIVYVAPMKALAAEMTNYFSKRLEPLG------------ 559
Cdd:PRK09751 1 VIAPTGSGKTLAAF---LYALDRLFREGGEdtreahKRKTSRILYISPIKALGTDVQRNLQIPLKGIAderrrrgetevn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 560 IVVKELTGDMQLS-KSEILRT--QMLVTTPEKWDVV----TRKSVGDvalsqiVKLLILDEVHLLH-EDRGPVLesivAR 631
Cdd:PRK09751 78 LRVGIRTGDTPAQeRSKLTRNppDILITTPESLYLMltsrARETLRG------VETVIIDEVHAVAgSKRGAHL----AL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 632 TLRQVEST--QSMIRIlGLSATLPNYLDVATFLhvnpyiglfyfdGRFRPV----PLGQTFLGIKSANKMQQLNNMDEVC 705
Cdd:PRK09751 148 SLERLDALlhTSAQRI-GLSATVRSASDVAAFL------------GGDRPVtvvnPPAMRHPQIRIVVPVANMDDVSSVA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 706 YE-------------------SVLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNSGQISCFLPTQGPEY----GHALK 762
Cdd:PRK09751 215 SGtgedshagregsiwpyietGILDEVLRHRSTIVFTNSRGLAEKLTARLNELYAARLQRSPSIAVDAAHFestsGATSN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 763 QVQKSRNKQVRElfsdgfsiHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIkgtQIYAAkrgsfvdL 842
Cdd:PRK09751 295 RVQSSDVFIARS--------HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVI---QVATP-------L 356
|
410
....*....|...
gi 456367250 843 GILDVMQIFGRAG 855
Cdd:PRK09751 357 SVASGLQRIGRAG 369
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
482-650 |
1.20e-08 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 57.28 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 482 QSIVFDTAynTNENMLICAPTGAGKTNIA-MLtvlheIRQHFHQGVLKKNEFKI-VYVAPMKALAAEMTNYFSKRLEPLg 559
Cdd:cd18034 7 QLELFEAA--LKRNTIVVLPTGSGKTLIAvML-----IKEMGELNRKEKNPKKRaVFLVPTVPLVAQQAEAIRSHTDLK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 560 ivVKELTGDMQLS-------KSEILRTQMLVTTPEKW-DVVTRksvGDVALSQIvKLLILDEVHL---LHEDRGpvlesi 628
Cdd:cd18034 79 --VGEYSGEMGVDkwtkerwKEELEKYDVLVMTAQILlDALRH---GFLSLSDI-NLLIFDECHHatgDHPYAR------ 146
|
170 180
....*....|....*....|..
gi 456367250 629 VARTLRQVESTQSMIRILGLSA 650
Cdd:cd18034 147 IMKEFYHLEGRTSRPRILGLTA 168
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1345-1457 |
1.53e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 56.14 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLgKKVIELTGDvtPDMKSIAKADL 1424
Cdd:pfam04851 25 RGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYV-EIGEIISGD--KKDESVDDNKI 101
|
90 100 110
....*....|....*....|....*....|...
gi 456367250 1425 IVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIH 1457
Cdd:pfam04851 102 VVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
1345-1458 |
5.59e-08 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 55.13 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKYP---TSKAVYIAPLKALVRERMDDWKiRIEEKLGKKVIELTGDVTPDM---KS 1418
Cdd:cd17927 19 NTIICLPTGSGKTFVAVLICEHHLKKFPagrKGKVVFLANKVPLVEQQKEVFR-KHFERPGYKVTGLSGDTSENVsveQI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 456367250 1419 IAKADLIVTTPEKWDGVSRSWQNRSyVQQVNILIIDEIHL 1458
Cdd:cd17927 98 VESSDVIIVTPQILVNDLKSGTIVS-LSDFSLLVFDECHN 136
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
493-615 |
5.80e-08 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 58.20 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNIAMLTVLHeirqhfhqgVLKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLS 572
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE---------RLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 456367250 573 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivkLLILDEVH 615
Cdd:COG1111 88 KRKELweKARIIVATPQviENDLIAgRIDLDDVS------LLIFDEAH 129
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
493-613 |
5.96e-08 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 55.29 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNIAMLTVLHEIRQHFHQGvlkknEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLS 572
Cdd:cd17957 27 GRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK-----GLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEAK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 456367250 573 KSE----ILRTQMLVTTPEKwdVVTRKSVGDVALSQiVKLLILDE 613
Cdd:cd17957 102 AKDgpksITKYDILVSTPLR--LVFLLKQGPIDLSS-VEYLVLDE 143
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
1350-1476 |
6.15e-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: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1350 APTGSGKTVAAELAIFRVFNKyptsKAVYIAPLKALVrermDDWKIRIEEKLGKKVI-ELTGDVTpdmKSIAKADLIVTT 1428
Cdd:cd17926 25 LPTGSGKTLTALALIAYLKEL----RTLIVVPTDALL----DQWKERFEDFLGDSSIgLIGGGKK---KDFDDANVVVAT 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 456367250 1429 PEkwdgvSRSWQN---RSYVQQVNILIIDEIHLLGeerGPVLEVIVSRTNF 1476
Cdd:cd17926 94 YQ-----SLSNLAeeeKDLFDQFGLLIVDEAHHLP---AKTFSEILKELNA 136
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
493-659 |
7.21e-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: 55.14 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNIAMLTVLHEIRqhfhqgvlkkNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVvkelTGDMQLS 572
Cdd:cd18024 47 NESVLVSAHTSAGKTVVAEYAIAQSLR----------DKQRVIYTSPIKALSNQKYRELQEEFGDVGLM----TGDVTIN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 573 KS--------EILRTqMLVTTPEkwdvVTRKsvgdvalsqiVKLLILDEVHLLHE-DRGPVLE-SIVArtlrqvesTQSM 642
Cdd:cd18024 113 PNasclvmttEILRS-MLYRGSE----IMRE----------VAWVIFDEIHYMRDkERGVVWEeTIIL--------LPDK 169
|
170
....*....|....*..
gi 456367250 643 IRILGLSATLPNYLDVA 659
Cdd:cd18024 170 VRYVFLSATIPNARQFA 186
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
454-861 |
7.85e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 57.34 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 454 FEEKPVYIQDLDEvGQLAFKGMKRLNRIQSIVFDTAYNT----NENMLICAPTGAGKTNIAMLTvlheIRQHFHQGvlkk 529
Cdd:COG1061 58 TERELAEAEALEA-GDEASGTSFELRPYQQEALEALLAAlergGGRGLVVAPTGTGKTVLALAL----AAELLRGK---- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 530 nefKIVYVAPMKAL----AAEMTNYFSKRLEPLGivVKELTGDmqlskseilrtqMLVTTpekWDVVTRKSVGDvALSQI 605
Cdd:COG1061 129 ---RVLVLVPRRELleqwAEELRRFLGDPLAGGG--KKDSDAP------------ITVAT---YQSLARRAHLD-ELGDR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 606 VKLLILDEVHLLhedrgpvlesiVARTLRQVESTQSMIRILGLSATlPNYLDVATFLHVNpYIGLFY--------FDGRF 677
Cdd:COG1061 188 FGLVIIDEAHHA-----------GAPSYRRILEAFPAAYRLGLTAT-PFRSDGREILLFL-FDGIVYeyslkeaiEDGYL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 678 RPVplgqTFLGIKSanKMQQLNNMDEVCYESVLKQVKAGHQvmvfvharnATVRTAMSLIERAKNSGQISCFLPTQgpey 757
Cdd:COG1061 255 APP----EYYGIRV--DLTDERAEYDALSERLREALAADAE---------RKDKILRELLREHPDDRKTLVFCSSV---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 758 GHAlkqvqksrnKQVRELFSD-GFSIH--HAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIikgtqIYAA 834
Cdd:COG1061 316 DHA---------EALAELLNEaGIRAAvvTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVA-----ILLR 381
|
410 420
....*....|....*....|....*..
gi 456367250 835 KRGSfvdLGILdvMQIFGRAGRPQFDK 861
Cdd:COG1061 382 PTGS---PREF--IQRLGRGLRPAPGK 403
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
492-652 |
8.44e-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: 54.83 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 492 TNENMLICAPTGAGKTNIAMLTVLHEIRQhFHQGvlKKNefKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDMQL 571
Cdd:cd18073 16 KGKNTIICAPTGCGKTFVSLLICEHHLKK-FPQG--QKG--KVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGATAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 572 SKSE---ILRTQMLVTTPEKwdVVTRKSVGDVALSQIVKLLILDEVHllHEDRGPVLESIVARTLRQ--VESTQSMIRIL 646
Cdd:cd18073 91 NVPVeqiIENNDIIILTPQI--LVNNLKKGTIPSLSIFTLMIFDECH--NTSGNHPYNMIMFRYLDQklGGSSGPLPQII 166
|
....*.
gi 456367250 647 GLSATL 652
Cdd:cd18073 167 GLTASV 172
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
495-615 |
1.26e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.19 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 495 NMLICAPTGAGKTNIAMLTVLheirqhfhqGVLKKNEFKIVYVAPMKALAAEMTNYFSK--RLEPLGIVVkeLTGDMQLS 572
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIA---------ERLHKKGGKVLILAPTKPLVEQHAEFFRKflNIPEEKIVV--FTGEVSPE 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 456367250 573 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivkLLILDEVH 615
Cdd:PRK13766 100 KRAELweKAKVIVATPQviENDLIAgRISLEDVS------LLIFDEAH 141
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
473-664 |
2.55e-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: 53.91 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 473 KGMKRLNRIQSIVFDTAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQHFHQGVLKKNEFKIVYVAPMKALAAEMTNYFS 552
Cdd:cd17948 8 QGITKPTTVQKQGIPSILR-GRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNAPRGLVITPSRELAEQIGSVAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 553 KRLEPLGIVVKELTGDMqlSKSEILRTQM-----LVTTPEK-WDVVTRksvGDVALSQiVKLLILDEVH-LLHEDRGPVL 625
Cdd:cd17948 87 SLTEGLGLKVKVITGGR--TKRQIRNPHFeevdiLVATPGAlSKLLTS---RIYSLEQ-LRHLVLDEADtLLDDSFNEKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 456367250 626 ESIVART---LRQVESTQSMIR---ILGLSATLPNYL--------DVATFLHV 664
Cdd:cd17948 161 SHFLRRFplaSRRSENTDGLDPgtqLVLVSATMPSGVgevlskviDVDSIETV 213
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
1345-1497 |
3.05e-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: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRV-----FNKYPTSKAVYIAPLKALVRERMddwkIRIEEKLGKKVIELTGDVTPDMKS- 1418
Cdd:cd18034 18 NTIVVLPTGSGKTLIAVMLIKEMgelnrKEKNPKKRAVFLVPTVPLVAQQA----EAIRSHTDLKVGEYSGEMGVDKWTk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1419 ------IAKADLIVTTPEkwdgVSRSWQNRSYVQ--QVNILIIDEIHLLGEERgpVLEVIVSRTNFISSHTEKPvRIVGL 1490
Cdd:cd18034 94 erwkeeLEKYDVLVMTAQ----ILLDALRHGFLSlsDINLLIFDECHHATGDH--PYARIMKEFYHLEGRTSRP-RILGL 166
|
....*..
gi 456367250 1491 STALANA 1497
Cdd:cd18034 167 TASPVNG 173
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
1345-1471 |
4.67e-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: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDdwkiRIEEKLGK-----KVIELTGDVTPDM--K 1417
Cdd:cd17930 3 LVILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINQMYE----RIREILGRlddedKVLLLHSKAALELleS 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456367250 1418 SIAKADLIVTTPEKWDGVSRSWQNR----SYVQ------QVN------------ILIIDEIHLLGEER-GPVLEVIV 1471
Cdd:cd17930 79 DEEPDDDPVEAVDWALLLKRSWLAPivvtTIDQllesllKYKhferrlhglansVVVLDEVQAYDPEYmALLLKALL 155
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
476-810 |
5.29e-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: 54.70 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 476 KRLNRIQSIVFDTAYNTNEN----MLICAPTGAGKTNIAMLTVLHEIRQHFHQgvlkknefKIVYVAPMKAL----AAEM 547
Cdd:COG1203 126 TPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKHGGR--------RIIYALPFTSIinqtYDRL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 548 TNYF--------SKRLEPLGIVVKELTGDMQLSK--SEILRTQMLVTTPekwD-----VVTRKSvgdvalSQIVKL---- 608
Cdd:COG1203 198 RDLFgedvllhhSLADLDLLEEEEEYESEARWLKllKELWDAPVVVTTI---DqlfesLFSNRK------GQERRLhnla 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 609 ---LILDEVHLL-HEDRGPVLesivaRTLRQVESTQSmiRILGLSATLPNyLDVATFLHVNPYIGLFYFDGRFRPVPLGQ 684
Cdd:COG1203 269 nsvIILDEVQAYpPYMLALLL-----RLLEWLKNLGG--SVILMTATLPP-LLREELLEAYELIPDEPEELPEYFRAFVR 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 685 TFLGIKSANKmqqlnnMDEVCYESVLKQVKAGHQVMVFVharnATVRTAMSLieraknsgqiscflptqgpeYghalkqv 764
Cdd:COG1203 341 KRVELKEGPL------SDEELAELILEALHKGKSVLVIV----NTVKDAQEL--------------------Y------- 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 456367250 765 qksrnKQVRELFSDGFSIH-HAGMLRQDRNLVEN----LFSNGHIKVLVCT 810
Cdd:COG1203 384 -----EALKEKLPDEEVYLlHSRFCPADRSEIEKeikeRLERGKPCILVST 429
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1301-1519 |
6.17e-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: 54.70 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1301 TELLDLQPLPVTALGCKAYEALYNF-----SHFNPVQTQIFHTLYHTDCN----VLLGAPTGSGKTVAAELAIFRVFNKY 1371
Cdd:COG1203 96 SANFDMARQALDHLLAERLERLLPKkskprTPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKH 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1372 PTSKAVYIAPLKALVrERMDDwkiRIEEKLGKKVIELTGDVTPDMKSIAK-----------------ADLIVTTPEK-WD 1433
Cdd:COG1203 176 GGRRIIYALPFTSII-NQTYD---RLRDLFGEDVLLHHSLADLDLLEEEEeyesearwlkllkelwdAPVVVTTIDQlFE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1434 GV--SRSWQNRSYVQQVN-ILIIDEIHLLGEERGPVLEvivsrtNFISSHTEKPVRIVgLSTA---------LANARDLA 1501
Cdd:COG1203 252 SLfsNRKGQERRLHNLANsVIILDEVQAYPPYMLALLL------RLLEWLKNLGGSVI-LMTAtlppllreeLLEAYELI 324
|
250
....*....|....*...
gi 456367250 1502 DWLNIKQMGLFNFRPSVR 1519
Cdd:COG1203 325 PDEPEELPEYFRAFVRKR 342
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
482-651 |
7.60e-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: 51.55 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 482 QSIVFDTAYNtneNMLICAPTGAGKTNIAMLTVLHEIRQhFHQGvlkknefKIVYVAPMKALAAEMTNYFSKRLE-PLGI 560
Cdd:cd18033 8 FTIVQKALFQ---NTLVALPTGLGKTFIAAVVMLNYYRW-FPKG-------KIVFMAPTKPLVSQQIEACYKITGiPSSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 561 VVkELTGDMQLSK-SEILRT-QMLVTTPEkwdVVTRKSVGDVALSQIVKLLILDEVhllHEDRGPVLESIVARTLRQVES 638
Cdd:cd18033 77 TA-ELTGSVPPTKrAELWASkRVFFLTPQ---TLENDLKEGDCDPKSIVCLVIDEA---HRATGNYAYCQVVRELMRYNS 149
|
170
....*....|...
gi 456367250 639 TqsmIRILGLSAT 651
Cdd:cd18033 150 H---FRILALTAT 159
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
775-856 |
9.22e-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: 49.52 E-value: 9.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 775 LFSDGFSI--HHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIkgtqiyaakrgSFVDLGILDVMQIF 851
Cdd:pfam00271 34 LEKEGIKVarLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----------YDLPWNPASYIQRI 102
|
....*
gi 456367250 852 GRAGR 856
Cdd:pfam00271 103 GRAGR 107
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
494-662 |
1.10e-06 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 51.11 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 494 ENMLICAPTGAGKTNIAMLTVlheirqhfhqGVLKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIvvkeLTGDMQLS- 572
Cdd:cd18027 24 DSVFVAAHTSAGKTVVAEYAI----------ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGL----ITGDVQLNp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 573 -------KSEILRTqMLVTTPEkwdvVTRKsvgdvalsqiVKLLILDEVHLLHE-DRGPVLESIVARTLRQVestqsmiR 644
Cdd:cd18027 90 easclimTTEILRS-MLYNGSD----VIRD----------LEWVIFDEVHYINDaERGVVWEEVLIMLPDHV-------S 147
|
170
....*....|....*...
gi 456367250 645 ILGLSATLPNYLDVATFL 662
Cdd:cd18027 148 IILLSATVPNTVEFADWI 165
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
470-666 |
1.49e-06 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 50.90 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 470 LAFKGMKRLNRIQSIVFDTAYNtNENMLICAPTGAGKTnIA-MLTVLHEIRQhfhQGVLKKNEFKIVYVAPMKALA---A 545
Cdd:cd00268 5 LKKLGFEKPTPIQAQAIPLILS-GRDVIGQAQTGSGKT-LAfLLPILEKLLP---EPKKKGRGPQALVLAPTRELAmqiA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 546 EMTNYFSKrlePLGIVVKELTGDMQLSKSEIL---RTQMLVTTPEK-WDVVTRksvGDVALSQiVKLLILDEV-HLLHED 620
Cdd:cd00268 80 EVARKLGK---GTGLKVAAIYGGAPIKKQIEAlkkGPDIVVGTPGRlLDLIER---GKLDLSN-VKYLVLDEAdRMLDMG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 456367250 621 RGPVLESIVARTLRQvesTQSMIrilgLSATLPNYLD--VATFLHvNP 666
Cdd:cd00268 153 FEEDVEKILSALPKD---RQTLL----FSATLPEEVKelAKKFLK-NP 192
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
706-856 |
1.51e-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: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 706 YESVLKQVKAGHQVMVFVHARNATVRTAMSLIERAknsgqiscflptqgPEYGHALKqvqksrnkqvrelfsdgFSIHHA 785
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELC--------------PDRVPPDF-----------------IALHHG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456367250 786 GMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPA-HAVIikgtQIYAAKrgsfvdlGILDVMQIFGRAGR 856
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 ... |
1328-1457 |
1.71e-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: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1328 FNPVQTQIFHtlyhtdcNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKiRIEEKLGKKVIE 1407
Cdd:cd18033 8 FTIVQKALFQ-------NTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACY-KITGIPSSQTAE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 456367250 1408 LTGDVTPDMKSI--AKADLIVTTPEKWDGVSRSwqNRSYVQQVNILIIDEIH 1457
Cdd:cd18033 80 LTGSVPPTKRAElwASKRVFFLTPQTLENDLKE--GDCDPKSIVCLVIDEAH 129
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
494-657 |
2.09e-06 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 50.37 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 494 ENMLICAPTGAGKTNIAMLTVLHEIRQHFHQgvlkknefKIVYVAPMKALA----AEMTNYFSKRLEPLGIV-------V 562
Cdd:cd17930 2 GLVILEAPTGSGKTEAALLWALKLAARGGKR--------RIIYALPTRATInqmyERIREILGRLDDEDKVLllhskaaL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 563 KELTGDMQLSKSEILRTQMLVTTPEKWD---VVT----------------RKSVGdvaLSQivKLLILDEVHLLhedrGP 623
Cdd:cd17930 74 ELLESDEEPDDDPVEAVDWALLLKRSWLapiVVTtidqllesllkykhfeRRLHG---LAN--SVVVLDEVQAY----DP 144
|
170 180 190
....*....|....*....|....*....|....
gi 456367250 624 VLESIVARTLRQVESTQSmIRILGLSATLPNYLD 657
Cdd:cd17930 145 EYMALLLKALLELLGELG-GPVVLMTATLPALLR 177
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
494-653 |
2.11e-06 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 50.55 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 494 ENMLICAPTGAGKTNIAMLTVLHEIRQHFHQGvlkkNEFKIVYVAPMKALAAEMTNYFSKRLEPlGIVVKELTGDMQLSK 573
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAG----EKGRVVVLVNKVPLVEQQLEKFFKYFRK-GYKVTGLSGDSSHKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 574 S---EILRTQMLVTTPEKWDVVTRKSVGDVALS-QIVKLLILDEVHllHEDRGPVLESIVARTLRQ-VESTQSMIRILGL 648
Cdd:cd18036 93 SfgqIVKASDVIICTPQILINNLLSGREEERVYlSDFSLLIFDECH--HTQKEHPYNKIMRMYLDKkLSSQGPLPQILGL 170
|
....*
gi 456367250 649 SATLP 653
Cdd:cd18036 171 TASPG 175
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
1345-1457 |
2.65e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 52.81 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKyPTSKAVYIAPLKALVRERMDDWK--IRIEEklgKKVIELTGDVTPD--MKSIA 1420
Cdd:COG1111 19 NTLVVLPTGLGKTAVALLVIAERLHK-KGGKVLFLAPTKPLVEQHAEFFKeaLNIPE---DEIVVFTGEVSPEkrKELWE 94
|
90 100 110
....*....|....*....|....*....|....*....
gi 456367250 1421 KADLIVTTPE--KWDGVSrswqNRSYVQQVNILIIDEIH 1457
Cdd:COG1111 95 KARIIVATPQviENDLIA----GRIDLDDVSLLIFDEAH 129
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
493-615 |
6.93e-06 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 48.66 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 493 NENMLICAPTGAGKTNIAMLTVLheirqhfhqGVLKKNEFKIVYVAPMKALAAEMTNYFsKRLEPLGIVVKELTGDMQLS 572
Cdd:cd18035 16 NGNTLIVLPTGLGKTIIAILVAA---------DRLTKKGGKVLILAPSRPLVEQHAENL-KRVLNIPDKITSLTGEVKPE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 456367250 573 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivkLLILDEVH 615
Cdd:cd18035 86 ERAERwdASKIIVATPQviENDLLAgRITLDDVS------LLIFDEAH 127
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
497-744 |
1.38e-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: 49.74 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 497 LICAPTGAGKTNIAMLTVLHEIRQhfhqgvlkKNEFKIVYVAPMKALAAEMTNYFSKRL-EPLGIVVKELTGD--MQLSK 573
Cdd:cd09639 3 VIEAPTGYGKTEAALLWALHSLKS--------QKADRVIIALPTRATINAMYRRAKEAFgETGLYHSSILSSRikEMGDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 574 SEILR--------------TQMLVTTPEKWDVVTRKSVGDVALSQ---IVKLLILDEVHLLHEDrgpVLESIVA--RTLR 634
Cdd:cd09639 75 EEFEHlfplyihsndtlflDPITVCTIDQVLKSVFGEFGHYEFTLasiANSLLIFDEVHFYDEY---TLALILAvlEVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 635 QVEstqsmIRILGLSATLPNYLDvATFLHVNPYIGLFYFDGRFRpvplgQTFLGIKSANKMqqlnNMDEVCYESVLKQVK 714
Cdd:cd09639 152 DND-----VPILLMSATLPKFLK-EYAEKIGYVEENEPLDLKPN-----ERAPFIKIESDK----VGEISSLERLLEFIK 216
|
250 260 270
....*....|....*....|....*....|
gi 456367250 715 AGHQVMVFVHarnaTVRTAMSLIERAKNSG 744
Cdd:cd09639 217 KGGSVAIIVN----TVDRAQEFYQQLKEKG 242
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
1345-1457 |
4.72e-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: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKYpTSKAVYIAPLKALVRERMDDWK--IRIEEklgkKVIELTGDVTPDMKS--IA 1420
Cdd:cd18035 18 NTLIVLPTGLGKTIIAILVAADRLTKK-GGKVLILAPSRPLVEQHAENLKrvLNIPD----KITSLTGEVKPEERAerWD 92
|
90 100 110
....*....|....*....|....*....|....*..
gi 456367250 1421 KADLIVTTPEKWDgvSRSWQNRSYVQQVNILIIDEIH 1457
Cdd:cd18035 93 ASKIIVATPQVIE--NDLLAGRITLDDVSLLIFDEAH 127
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
491-651 |
8.47e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.97 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 491 NTNENMLICAPTGAGKTniamLTVLHEIRQHFHQGVLKknefKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDmq 570
Cdd:pfam04851 21 NGQKRGLIVMATGSGKT----LTAAKLIARLFKKGPIK----KVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 571 lSKSEILRT-QMLVTTPEKWDVVTRKSVGDVALSQIVkLLILDEVHllhedRGPvlesivARTLRQVESTQSMIRILGLS 649
Cdd:pfam04851 91 -KKDESVDDnKIVVTTIQSLYKALELASLELLPDFFD-VIIIDEAH-----RSG------ASSYRNILEYFKPAFLLGLT 157
|
..
gi 456367250 650 AT 651
Cdd:pfam04851 158 AT 159
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
1550-1693 |
1.95e-04 |
|
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: 43.79 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1550 IRSHSPAKPVLIFVSSRRQTrltaleliaflateedpkqwlnmdeqemENIIATVRDSNLKLTLAFGIGMHHAGLHERDR 1629
Cdd:cd18796 32 IFLLERHKSTLVFTNTRSQA----------------------------ERLAQRLRELCPDRVPPDFIALHHGSLSRELR 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 456367250 1630 KTVEELFVNCKVQVLIATSTLAWGVNFPA-HLVIIKGTEYydgktrryvdfPITDVLQMMGRAGR 1693
Cdd:cd18796 84 EEVEAALKRGDLKVVVATSSLELGIDIGDvDLVIQIGSPK-----------SVARLLQRLGRSGH 137
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
1345-1457 |
4.55e-04 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 45.63 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDDWK--IRIEEklgKKVIELTGDVTPD--MKSIA 1420
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIAERLHKKG-GKVLILAPTKPLVEQHAEFFRkfLNIPE---EKIVVFTGEVSPEkrAELWE 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 456367250 1421 KADLIVTTPE--KWDGVSrswqNRSYVQQVNILIIDEIH 1457
Cdd:PRK13766 107 KAKVIVATPQviENDLIA----GRISLEDVSLLIFDEAH 141
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
488-652 |
1.14e-03 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438711 [Multi-domain] Cd Length: 174 Bit Score: 41.93 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 488 TAYNTNENMLICAPTGAGKTNIAMLTVLHEirqhfhqgvLKKNEFKIVYVAP----MKALAAEMTnyfSKRLEPLGIVVK 563
Cdd:cd17990 12 AALDAGGQVVLEAPPGAGKTTRVPLALLAE---------LWIAGGKIIVLEPrrvaARAAARRLA---TLLGEAPGETVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 564 -ELTGDMQLSKseilRTQMLVTTPekwDVVTRKSVGDVALSQiVKLLILDEVHllheDRGPVLESIVARTLRQVESTQSM 642
Cdd:cd17990 80 yRVRGESRVGR----RTRVEVVTE---GVLLRRLQRDPELSG-VGAVILDEFH----ERSLDADLALALLLEVQQLLRDD 147
|
170
....*....|
gi 456367250 643 IRILGLSATL 652
Cdd:cd17990 148 LRLLAMSATL 157
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
1323-1482 |
1.44e-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: 42.35 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1323 YNFSHFNPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAV-YIAPLkALV----RERMDdwKIR- 1396
Cdd:cd17948 8 QGITKPTTVQKQGIPSILRGR-NTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpFNAPR-GLVitpsRELAE--QIGs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1397 ----IEEKLGKKVIELTGDVTpdMKSI-----AKADLIVTTPekwDGVSRSWQNRSY-VQQVNILIIDEIH-LLGEERGP 1465
Cdd:cd17948 84 vaqsLTEGLGLKVKVITGGRT--KRQIrnphfEEVDILVATP---GALSKLLTSRIYsLEQLRHLVLDEADtLLDDSFNE 158
|
170
....*....|....*..
gi 456367250 1466 VLEVIVSRTNFISSHTE 1482
Cdd:cd17948 159 KLSHFLRRFPLASRRSE 175
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
1621-1693 |
1.72e-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: 1.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456367250 1621 HAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-----AHLVIIKGTE-YYdgktrryvdfpitdvlQMMGRAGR 1693
Cdd:cd18794 61 HAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPdvrfvIHYSLPKSMEsYY----------------QESGRAGR 123
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
474-653 |
1.82e-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: 41.80 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 474 GMKRLNRIQSIVFDTAYNTNENMLICAPTGAGKTnIAML--TVLHEIRQHFHQgvlKKNEFKIVYVAPMKALAAEMTNYF 551
Cdd:cd17964 13 GFETMTPVQQKTLKPILSTGDDVLARAKTGTGKT-LAFLlpAIQSLLNTKPAG---RRSGVSALIISPTRELALQIAAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 552 SKRLEPL-GIVVKELTGDMQLSKSEI----LRTQMLVTTPEKW-DVVTRKSVGDVALSqiVKLLILDEV-HLLheDRG-- 622
Cdd:cd17964 89 KKLLQGLrKLRVQSAVGGTSRRAELNrlrrGRPDILVATPGRLiDHLENPGVAKAFTD--LDYLVLDEAdRLL--DMGfr 164
|
170 180 190
....*....|....*....|....*....|.
gi 456367250 623 PVLESIVaRTLRQVESTQsmIRILGLSATLP 653
Cdd:cd17964 165 PDLEQIL-RHLPEKNADP--RQTLLFSATVP 192
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
1325-1457 |
2.16e-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: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1325 FSHFNPVQTQ-IFHTLYHTDCNVLLgaPTGSGKTVAAELAIFrVFNKyPTskaVYIAPLKALvrerMDDWKIRIEEkLGK 1403
Cdd:cd17920 10 YDEFRPGQLEaINAVLAGRDVLVVM--PTGGGKSLCYQLPAL-LLDG-VT---LVVSPLISL----MQDQVDRLQQ-LGI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456367250 1404 KVIELTGDVTPDMKSIA-------KADLIVTTPEK--WDGVSRSWQNRSYVQQVNILIIDEIH 1457
Cdd:cd17920 78 RAAALNSTLSPEEKREVllrikngQYKLLYVTPERllSPDFLELLQRLPERKRLALIVVDEAH 140
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
489-652 |
2.70e-03 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 40.37 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 489 AYNTNENMLICAPTGAGKTNIAMLTVLHeirqhfhqgvLKknEFKIVYVAPMKAL----AAEMTNYFSKRleplgiVVKE 564
Cdd:cd17926 14 AHKNNRRGILVLPTGSGKTLTALALIAY----------LK--ELRTLIVVPTDALldqwKERFEDFLGDS------SIGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 565 LTGDmqlSKSEILRTQMLVTTPEK--WDVVTRKSVGDVALsqivkLLILDEVHllhedRGPvlesivARTLRQVESTQSM 642
Cdd:cd17926 76 IGGG---KKKDFDDANVVVATYQSlsNLAEEEKDLFDQFG-----LLIVDEAH-----HLP------AKTFSEILKELNA 136
|
170
....*....|
gi 456367250 643 IRILGLSATL 652
Cdd:cd17926 137 KYRLGLTATP 146
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
1330-1429 |
3.35e-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: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1330 PVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIF---RVFNKYPTSKAVYIAPLKAL----VRErmddwKIRIEEKLG 1402
Cdd:cd17957 15 PIQMQAIPILLHGR-DLLACAPTGSGKTLAFLIPILqklGKPRKKKGLRALILAPTRELasqiYRE-----LLKLSKGTG 88
|
90 100 110
....*....|....*....|....*....|.
gi 456367250 1403 KKVIELTGDVTP----DMKSIAKADLIVTTP 1429
Cdd:cd17957 89 LRIVLLSKSLEAkakdGPKSITKYDILVSTP 119
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
1345-1457 |
4.10e-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: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1345 NVLLGAPTGSGKTVAAELAIFRVFNKYP----TSKAVYIAPLKALVrERMDDWKIRIEEKlGKKVIELTGD--VTPDMKS 1418
Cdd:cd18036 19 NTIICAPTGSGKTRVAVYICRHHLEKRRsageKGRVVVLVNKVPLV-EQQLEKFFKYFRK-GYKVTGLSGDssHKVSFGQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 456367250 1419 IAKA-DLIVTTPEKWDGVSRS--WQNRSYVQQVNILIIDEIH 1457
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 ... |
1643-1693 |
6.66e-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: 6.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 456367250 1643 VLIATSTLAWGVNFPAHLVIIKGTEYYDGKTRRyvDFPITDVLQMMGRAGR 1693
Cdd:cd18805 73 VLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMR--PLSPSEVKQIAGRAGR 121
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
1324-1429 |
9.71e-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: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456367250 1324 NFSHFNPVQTQIFHTLYHTD--------CNVLLGAPTGSGKTVAAELAIFRVFNKYPTSK--AVYIAPLKAL---VRERM 1390
Cdd:cd17956 9 GITSAFPVQAAVIPWLLPSSkstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRlrALIVVPTKELvqqVYKVF 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 456367250 1391 DdwkiRIEEKLGKKVIELTG--DVTPDMKSIA---------KADLIVTTP 1429
Cdd:cd17956 89 E----SLCKGTGLKVVSLSGqkSFKKEQKLLLvdtsgrylsRVDILVATP 134
|
|
| |
