|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1331-1519 |
5.12e-134 |
|
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: 416.39 E-value: 5.12e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1331 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLGKKVI 1410
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1411 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKPVR 1490
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*....
gi 767941789 1491 IVGLSTALANARDLADWLNIKQMGLFNFR 1519
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
481-678 |
1.41e-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: 1.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 481 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFQQ-GVIKKNEFKIVYVAPMKALAAEMTDYFSRRL 559
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 560 EPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDVALSQIVRLLILDEVHLLHEDRGPVLESIVARTLRQ 639
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 767941789 640 VESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFFFD 678
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
983-1291 |
2.68e-124 |
|
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: 393.87 E-value: 2.68e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 983 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNfCELSTPGGVENSYGKI 1062
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEK-VPIPVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1063 NILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSILPPHI 1142
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1143 LTRLEEKKLTV--DKLKDMRKDEIGHILHHVNIGLKVKQCVHQIPSVMMEASIQPITRTVLRVTLSIYADFTWNDQVHGT 1220
Cdd:pfam02889 160 IKKLEKKGVESvrDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767941789 1221 VgEPWWIWVEDPTNDHIYHSEYFLALKKQVISkeAQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIIN 1291
Cdd:pfam02889 240 S-EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
980-1293 |
4.58e-113 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 361.96 E-value: 4.58e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 980 YFSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNFCELSTPGGVENSY 1059
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1060 GKINILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSILP 1139
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1140 PHILTRLEEKK-LTVDKLKDMRKDEIGHILHHVN-IGLKVKQCVHQIPSVMMEASIQPITRTVLRVTLSIYADFTWNDQV 1217
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLGLLDaEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767941789 1218 HGTVgEPWWIWVEDPTNDHIYHSEYFLALKKQVIskEAQLLVFTIPIFEPLPsQYYIRAVSDRWLGAEAVCIINFQ 1293
Cdd:smart00611 241 HGKQ-EGWWLVIGDSDGNELLHIERFSLNKKNVS--EEVKLDFTAPATEGNY-QYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1814-2183 |
4.59e-100 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 324.60 E-value: 4.59e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1814 SIEPLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPHSFDSPH 1893
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1894 TKAHLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWLKDSSLLTLPNIE 1973
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1974 NHHLHLFKKWKpimkgphargRTSIESLPELIHAcgGKDHVFSSMVeselhaAKTKQAWNFLSHLPVINVGISVKGSwDD 2053
Cdd:smart00611 161 EEILKRLEKKK----------VLSLEDLLELEDE--ERGELLGLLD------AEGERVYKVLSRLPKLNIEISLEPI-TR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 2054 LVEGHNELSVSTLTADKRDDnkwiklhadqeyvlqvslqrvhfgfhkgkpescavtprfpkSKDEGWFLILGEVDKRELI 2133
Cdd:smart00611 222 TVLGVEVTLTVDLTWDDEIH-----------------------------------------GKQEGWWLVIGDSDGNELL 260
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 767941789 2134 ALKRVGYIRNH--HVASLSFYTPEIPGRYIYTLYFMSDCYLGLDQQYDIYLN 2183
Cdd:smart00611 261 HIERFSLNKKNvsEEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1332-1854 |
1.17e-95 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 320.69 E-value: 1.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1332 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKVRIEEkLGKKVIE 1411
Cdd:COG1204 23 LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEE-LGIKVGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1412 LTGDVTPDMKSIAKADLIVTTPEKWDGVSRswQNRNYVQQVTILIIDEIHLLG-EERGPVLEVIVSRtnfiSSHTEKPVR 1490
Cdd:COG1204 100 STGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTLEVLLAR----LRRLNPEAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1491 IVGLSTALANARDLADWLNIKqmglfNFRPSVRPVPLE--VHIQG---FPGQHYCPRmasmnKPAFQAIRSHSPA-KPVL 1564
Cdd:COG1204 174 IVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSK-----DPTLALALDLLEEgGQVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1565 IFVSSRRQTRLTALELIAFLA---TEEDPKQWLNMDEREMEniIATVRDSNLKLT--LAFGIGMHHAGLHERDRKTVEEL 1639
Cdd:COG1204 244 VFVSSRRDAESLAKKLADELKrrlTPEEREELEELAEELLE--VSEETHTNEKLAdcLEKGVAFHHAGLPSELRRLVEDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1640 FVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGktrryVDFPITDVLQMMGRAGRPQFDDQGKAVILVHDIK---KD 1716
Cdd:COG1204 322 FREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDeadEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1717 FYKKFLYEPFPVESSLLGVLSD--HLNAEIAGGTITSKQDALDYITWTYFFRRlimnPSYYNLGDVshdsVNKFLSHLIE 1794
Cdd:COG1204 397 FERYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQ----YDKGDLEEV----VDDALEFLLE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767941789 1795 KSLIElelsycieigEDNRSIEPLTYGRIASYYYLKHQTVKMFKDRLK---PECSTEELLSIL 1854
Cdd:COG1204 469 NGFIE----------EDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadEEFTDLGLLHLI 521
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
465-1020 |
9.71e-94 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 314.91 E-value: 9.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 465 IQDLDE---IGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFqqgvikknefKIVYV 541
Cdd:COG1204 3 VAELPLekvIEFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 542 APMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGdvALSQIvRLLILDEVHLL 621
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDV-DLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 622 H-EDRGPVLESIVARtLRQVESTqsmIRILGLSATLPNYLDVATFLHVNPyiglffFDGRFRPVPLgqtFLGIKCANKmq 700
Cdd:COG1204 150 DdESRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGV-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 701 qlNNMDEVCYEN-------VLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNCGHIPFFFPTQGHDYVLAEKQVQRSRN 773
Cdd:COG1204 215 --LRFDDGSRRSkdptlalALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 774 KQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTqiyaaKRGSFVDLGILDVMQ 853
Cdd:COG1204 293 EKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-----KRGGMVPIPVLEFKQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 854 IFGRAGRPQFDKFGEGIIIT-THDKLSH--YLTLLTQRNPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWISYTYLY 928
Cdd:COG1204 368 MAGRAGRPGYDPYGEAILVAkSSDEADElfERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTFYA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 929 VRMRANPLaygishkayqidptlrkhrEQLVIEVGRKLDKAQMIrfEERTGYFSSTDLGRTASHYYIKYNTIETFNELFD 1008
Cdd:COG1204 448 YQYDKGDL-------------------EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAELVDGLR 506
|
570
....*....|..
gi 767941789 1009 AHKTEGDIFAIV 1020
Cdd:COG1204 507 KADEEFTDLGLL 518
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1817-2180 |
3.23e-70 |
|
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: 238.64 E-value: 3.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1817 PLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPhSFDSPHTKA 1896
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKG-DIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1897 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWLKDSSLLTLPNIENHH 1976
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1977 LHLFKKwkpimkgphaRGRTSIESL-----PELIHACGGKDHVFssmveselhaaktKQAWNFLSHLPVINVgisvkgsw 2051
Cdd:pfam02889 160 IKKLEK----------KGVESVRDIlelddAEELGELIRNPKMG-------------KDIAQFVNRFPKIEI-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 2052 ddlveghnELSVSTLTADkrddnkwiklhadqeyVLQVSLQrvhfgfhkgkpescaVTPRFPKSKD-----EGWFLILGE 2126
Cdd:pfam02889 209 --------EAEVQPITRS----------------VLRVEVT---------------ITPDFPWDKRvhgksEGFWLVVGD 249
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 767941789 2127 VDKRELIALKRV--GYIRNHHVASLSFYTPEI-PGRYIYTLYFMSDCYLGLDQQYDI 2180
Cdd:pfam02889 250 SDGNEILHIERFtlTKRTLAGEHKLEFTVPPSdPGPPQLFVRLISDSWLGADQEVPI 306
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1523-1711 |
1.85e-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: 221.66 E-value: 1.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1523 RPVPLEVHIQGFPGQHYCPRMASMNK-----PAFQAIRSHSPAKPVLIFVSSRRQTRLTALELIaflateedpkqwlnmd 1597
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1598 eremeniiatvrdsnlkltlafGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKT 1677
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 767941789 1678 RRYvdFPITDVLQMMGRAGRPQFDDQGKAVILVH 1711
Cdd:cd18795 123 YRE--LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1349-1877 |
7.37e-61 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 224.31 E-value: 7.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFrvfNKYPTS--KAVYIAPLKALVRER---MDDWkvrieEKLGKKVIELTGDVTPDMKSI 1423
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMV---NKLLREggKAVYLVPLKALAEEKyreFKDW-----EKLGLRVAMTTGDYDSTDEWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1424 AKADLIVTTPEKWDGVSR---SWqnrnyVQQVTILIIDEIHLLGE-ERGPVLEVIVSrtnfissHTEKPVRIVGLSTALA 1499
Cdd:PRK00254 113 GKYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSyDRGATLEMILT-------HMLGRAQILGLSATVG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1500 NARDLADWLNIKQMglfnfRPSVRPVPLE--VHIQGF------PGQHYcprMASMNKPAFQAIRShspAKPVLIFVSSRR 1571
Cdd:PRK00254 181 NAEELAEWLNAELV-----VSDWRPVKLRkgVFYQGFlfwedgKIERF---PNSWESLVYDAVKK---GKGALVFVNTRR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1572 QTRLTALELIAFLATEEDPKQwlnmdEREMENIIATVRD--SNLKLTLAF--GIGMHHAGLHERDRKTVEELFVNCKVQV 1647
Cdd:PRK00254 250 SAEKEALELAKKIKRFLTKPE-----LRALKELADSLEEnpTNEKLKKALrgGVAFHHAGLGRTERVLIEDAFREGLIKV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1648 LIATSTLAWGVNFPAHLVIIKGTEYYDGKTrrYVDFPITDVLQMMGRAGRPQFDDQGKAVILVH-DIKKDFYKKF----- 1721
Cdd:PRK00254 325 ITATPTLSAGINLPAFRVIIRDTKRYSNFG--WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERYifgkp 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1722 --LYEPFPVESSLLGvlsdHLNAEIAGGTITSKQDALDYITWTYFfrrlimnpsYYNLGDVSH--DSVNKFLSHLIEKSL 1797
Cdd:PRK00254 403 ekLFSMLSNESAFRS----QVLALITNFGVSNFKELVNFLERTFY---------AHQRKDLYSleEKAKEIVYFLLENEF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1798 IELELsycieigEDNrsIEPLTYGRIASYYYLKHQTVKMFKDRLkPECSTEE----LLSILSDAEEYTDLPVRHNEDHMN 1873
Cdd:PRK00254 470 IDIDL-------EDR--FIPLPLGIRTSQLYIDPLTAKKFKDAF-PKIEKNPnplgIFQLIASTPDMTPLNYSRKEMEDL 539
|
....
gi 767941789 1874 SELA 1877
Cdd:PRK00254 540 LDEA 543
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
498-1039 |
5.35e-53 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 200.43 E-value: 5.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 498 ENMLICAPTGAGKTNIAMLTVLHEIrqhFQQGvikkneFKIVYVAPMKALAAEMTDYFsRRLEPLGIIVKELTGDMQlSK 577
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKL---LREG------GKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYD-ST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 578 SEIL-RTQMLVTTPEKWDVVTRKSVgdvalSQI--VRLLILDEVHLL-HEDRGPVLESIVARTLRQVEstqsmirILGLS 653
Cdd:PRK00254 109 DEWLgKYDIIIATAEKFDSLLRHGS-----SWIkdVKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ-------ILGLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 654 ATLPNYLDVATFLHVNpyigLFFFDgrFRPVPL-----GQTFLGIKCANKMQQLNNMDEVCYEnvlkQVKAGHQVMVFVH 728
Cdd:PRK00254 177 ATVGNAEELAEWLNAE----LVVSD--WRPVKLrkgvfYQGFLFWEDGKIERFPNSWESLVYD----AVKKGKGALVFVN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 729 ARNATVRTAMSLIERAKNCghipFFFPTQGHDYVLAEKQVQRSRNKQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHI 808
Cdd:PRK00254 247 TRRSAEKEALELAKKIKRF----LTKPELRALKELADSLEENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 809 KVLVCTATLAWGVNLPAHAVIIKGTQIYAakRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDK----LSHYL-- 882
Cdd:PRK00254 323 KVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklMERYIfg 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 883 ------TLLTQRNPIESQFLesladnlnAEIALGTVTNVEEAVKWISYTYlYVRMRANPlaYGISHKAYQIDPTLrkhRE 956
Cdd:PRK00254 401 kpeklfSMLSNESAFRSQVL--------ALITNFGVSNFKELVNFLERTF-YAHQRKDL--YSLEEKAKEIVYFL---LE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 957 QLVIEvgrkldkaqmIRFEERtgyFSSTDLGRTASHYYIKYNTIETFNELFDahKTEGD-----IFAIVSKAEEFDQIKV 1031
Cdd:PRK00254 467 NEFID----------IDLEDR---FIPLPLGIRTSQLYIDPLTAKKFKDAFP--KIEKNpnplgIFQLIASTPDMTPLNY 531
|
....*...
gi 767941789 1032 REEEIEEL 1039
Cdd:PRK00254 532 SRKEMEDL 539
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
682-874 |
8.89e-53 |
|
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: 182.37 E-value: 8.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 682 RPVPLGQTFLGIK----CANKMQQLNNMDEVCYENVLKQVKAGHQVMVFVHARNATVRTAMSLIerakncghipfffptq 757
Cdd:cd18795 1 RPVPLEEYVLGFNglgiKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 758 ghdyvlaekqvqrsrnkqvrelfpdGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYA 837
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 767941789 838 AKRgsFVDLGILDVMQIFGRAGRPQFDKFGEGIIITT 874
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
483-661 |
1.32e-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: 125.43 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 483 NRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQhfqqgviKKNEFKIVYVAPMKALAAEMTDYFSRRLEPL 562
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK-------LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 563 GIIVKELTGDMQLSK--SEILRTQMLVTTPEKWDVVTRKSvgdVALSQiVRLLILDEVHLLHE-DRGPVLESIVARtlrq 639
Cdd:pfam00270 73 GLKVASLLGGDSRKEqlEKLKGPDILVGTPGRLLDLLQER---KLLKN-LKLLVLDEAHRLLDmGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|..
gi 767941789 640 vesTQSMIRILGLSATLPNYLD 661
Cdd:pfam00270 145 ---LPKKRQILLLSATLPRNLE 163
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1333-1504 |
1.87e-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: 124.66 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1333 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFN-KYPTSKAVYIAPLKALVRERMDDWKVRIeEKLGKKVIE 1411
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDkLDNGPQALVLAPTRELAEQIYEELKKLG-KGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1412 LTGDVTP--DMKSIAKADLIVTTPEKWDGVsrsWQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNfisshteKP 1488
Cdd:pfam00270 79 LLGGDSRkeQLEKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRRLP-------KK 148
|
170
....*....|....*..
gi 767941789 1489 VRIVGLS-TALANARDL 1504
Cdd:pfam00270 149 RQILLLSaTLPRNLEDL 165
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1334-1710 |
7.21e-26 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 116.53 E-value: 7.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1334 PVQT-QIFHTLYHTDcNVLLGAPTGSGKTVAAELA-IFRVFNKypTSKAVYIAPLKALVRERMDDWKVRIEEKLgkKVIE 1411
Cdd:COG1202 212 PVQSlAVENGLLEGK-DQLVVSATATGKTLIGELAgIKNALEG--KGKMLFLVPLVALANQKYEDFKDRYGDGL--DVSI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1412 LTGDV---TPDMKSIAKADLIVTTPEKWDGVSRSwqnRNYVQQVTILIIDEIHLLGE-ERGPVLEVIVSRTNFISSHTEk 1487
Cdd:COG1202 287 RVGASrirDDGTRFDPNADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEVHMLEDpERGHRLDGLIARLKYYCPGAQ- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1488 pvrIVGLSTALANARDLADWLNIKQMgLFNfrpsVRPVPLEVHIQGFPGQHYCPRMASMNKPAFQAIRSHSPAKPVLIFV 1567
Cdd:COG1202 363 ---WIYLSATVGNPEELAKKLGAKLV-EYE----ERPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1568 SSRRQTRltaleliaflateedpkqwlnmderemeniiatvrdsnlKLTLAFGIGM--HHAGLHERDRKTVEELFVNCKV 1645
Cdd:COG1202 435 NSRRRCH---------------------------------------EIARALGYKAapYHAGLDYGERKKVERRFADQEL 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767941789 1646 QVLIATSTLAWGVNFPAHLVIIK----GTEYydgktrryvdFPITDVLQMMGRAGRPQFDDQGKAVILV 1710
Cdd:COG1202 476 AAVVTTAALAAGVDFPASQVIFDslamGIEW----------LSVQEFHQMLGRAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
474-685 |
1.03e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.81 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 474 LAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRqhfqqgviKKNEFKIVYVAPMKALAAEMTD 553
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALK--------RGKGGRVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 554 YFSRRLEPLGIIVKELTGD----MQLSKSEILRTQMLVTTPEKWDVVTRKsvGDVALSQiVRLLILDEVH-LLHEDRGPV 628
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRLLDLLEN--DKLSLSN-VDLVILDEAHrLLDGGFGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767941789 629 LESIVARTLRqvestqsMIRILGLSATLPNYLDVATFLHVNpyiGLFFFDGRFRPVP 685
Cdd:smart00487 150 LEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1327-1526 |
1.21e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 103.73 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1327 YNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLG 1406
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1407 KKVIELTGDVT-PDMKSIAK--ADLIVTTPEKWDGVSRswQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNfis 1482
Cdd:smart00487 84 KVVGLYGGDSKrEQLRKLESgkTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767941789 1483 shteKPVRIVGLS-TALANARDLADWLNIkqmGLFNFRPSVRPVP 1526
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 ... |
1351-1666 |
8.99e-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: 83.76 E-value: 8.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1351 LLGAPTGSGKTVAAELAIFRVFNKYPTSK-----AVYIAPLKALVRErmddwkvrIEEKLGKKVIEL---------TGDV 1416
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKekglhTLYITPLRALAVD--------IARNLQAPIEELglpirvetrTGDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1417 TPDMKSIAKA---DLIVTTPEkwdgvsrSWQ-------NRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNFISSHt 1485
Cdd:TIGR04121 104 SSSERARQRKkppDILLTTPE-------SLAlllsypdAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1486 ekpVRIVGLSTALANARDLADWLnikqMGLFNFRPSV------RPVPLEV----HIQGFP-GQHYCPRMASmnkPAFQAI 1554
Cdd:TIGR04121 176 ---LRRWGLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISllpeSEERFPwAGHLGLRALP---EVYAEI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1555 RSHspaKPVLIFVSSRRQTRLTALELIAFLAteedpkqwlnmderemeniiatvrDSNLKltlafgIGMHHAGLHERDRK 1634
Cdd:TIGR04121 246 DQA---RTTLVFTNTRSQAELWFQALWEANP------------------------EFALP------IALHHGSLDREQRR 292
|
330 340 350
....*....|....*....|....*....|...
gi 767941789 1635 TVEELFVNCKVQVLIATSTLAWGVNF-PAHLVI 1666
Cdd:TIGR04121 293 WVEAAMAAGRLRAVVCTSSLDLGVDFgPVDLVI 325
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
493-861 |
5.89e-15 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 81.06 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 493 AYNTNENMLICAPTGAGKTNIAMLTVLheIRQHFQQGViKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVK-EL-T 570
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSL--IDLAGPEAP-KEKGLHTLYITPLRALAVDIARNLQAPIEELGLPIRvETrT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 571 GDMQLSKSEILRTQM---LVTTPEKWDVVTrkSVGDVA-LSQIVRLLILDEVH-LLHEDRGPVLESIVARtLRQvesTQS 645
Cdd:TIGR04121 101 GDTSSSERARQRKKPpdiLLTTPESLALLL--SYPDAArLFKDLRCVVVDEWHeLAGSKRGDQLELALAR-LRR---LAP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 646 MIRILGLSATLPNyLDVA--TFLHVNPYIGLFFFDGRFRPVPL-------GQTF-----LGIKCAnkmqqlnnmdevcyE 711
Cdd:TIGR04121 175 GLRRWGLSATIGN-LEEArrVLLGVGGAPAVLVRGKLPKAIEVisllpesEERFpwaghLGLRAL--------------P 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 712 NVLKQVKAGHQVMVFVHARNATVRTAMSLIErakncghipfffptqghdyvlaekqvqrsrnkqVRELFPDGFSIHHAGM 791
Cdd:TIGR04121 240 EVYAEIDQARTTLVFTNTRSQAELWFQALWE---------------------------------ANPEFALPIALHHGSL 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767941789 792 LRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIkgtQIYAAKrgsfvdlGILDVMQIFGRAG-RP 861
Cdd:TIGR04121 287 DREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSPK-------GVARLLQRAGRSNhRP 347
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1619-1698 |
1.13e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 71.09 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1619 FGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryVDFPITDVLQMMGRAGR 1697
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVII-----YD------LPWSPASYIQRIGRAGR 80
|
.
gi 767941789 1698 P 1698
Cdd:smart00490 81 A 81
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
783-861 |
9.04e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 65.70 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 783 GFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIKGtqiyaakrgsfVDLGILDVMQIFGRAGRP 861
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASYIQRIGRAGRA 81
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
497-824 |
7.35e-11 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 67.60 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 497 NENMLICAPTGAGKTNIAMLTVLHEIrqhFQQGVIKKNEFKI--VYVAPMKALAAEMtdyfsRR--LEPLGIIVKEL--- 569
Cdd:PRK13767 47 GKNVLISSPTGSGKTLAAFLAIIDEL---FRLGREGELEDKVycLYVSPLRALNNDI-----HRnlEEPLTEIREIAker 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 570 ------------TGDM-QLSKSEILRT--QMLVTTPEKWDVVT-----RKSVGDvalsqiVRLLILDEVHLLHED-RGPV 628
Cdd:PRK13767 119 geelpeirvairTGDTsSYEKQKMLKKppHILITTPESLAILLnspkfREKLRT------VKWVIVDEIHSLAENkRGVH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 629 LesivARTLRQVES--TQSMIRIlGLSATLPNYLDVATFLhvnpyiGLFFFDGRFRPVPLGQT-F---LGIKCANKMQQL 702
Cdd:PRK13767 193 L----SLSLERLEElaGGEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDCEIVDArFvkpFDIKVISPVDDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 703 -----NNMDEVCYENVLKQVKAGHQVMVFVHARNATVRTAMSLierakncghipfffptqghdyvlaekqvqrsrnkqvR 777
Cdd:PRK13767 262 ihtpaEEISEALYETLHELIKEHRTTLIFTNTRSGAERVLYNL------------------------------------R 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 767941789 778 ELFPDGFSI-----HHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP 824
Cdd:PRK13767 306 KRFPEEYDEdnigaHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG 357
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1603-1697 |
4.62e-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: 58.76 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1603 NIIATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryV 1681
Cdd:pfam00271 23 QTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YD------L 91
|
90
....*....|....*.
gi 767941789 1682 DFPITDVLQMMGRAGR 1697
Cdd:pfam00271 92 PWNPASYIQRIGRAGR 107
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1329-1495 |
1.30e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 63.75 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1329 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAI----FRVFNK-------YptskAVYIAPLKAL---VRERM 1394
Cdd:PRK13767 30 FGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREgeledkvY----CLYVSPLRALnndIHRNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1395 DDWKVRIEEKLGKKVIEL--------TGDVTPDMKS--------IakadLIvTTPEKWDGVSRSWQNRNYVQQVTILIID 1458
Cdd:PRK13767 105 EEPLTEIREIAKERGEELpeirvairTGDTSSYEKQkmlkkpphI----LI-TTPESLAILLNSPKFREKLRTVKWVIVD 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 767941789 1459 EIHLLGE-ERGPVLEVIVSRTNFISSHteKPVRIvGLS 1495
Cdd:PRK13767 180 EIHSLAEnKRGVHLSLSLERLEELAGG--EFVRI-GLS 214
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
497-619 |
4.70e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.12 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 497 NENMLICAPTGAGKTNIAMLTVLHeirqhfqqgVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLS 576
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE---------RLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767941789 577 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivrLLILDEVH 619
Cdd:COG1111 88 KRKELweKARIIVATPQviENDLIAgRIDLDDVS------LLIFDEAH 129
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
784-860 |
1.94e-06 |
|
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: 48.36 E-value: 1.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767941789 784 FSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIkgtqiyaakrgSFVDLGILDVMQIFGRAGR 860
Cdd:pfam00271 41 VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----------YDLPWNPASYIQRIGRAGR 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; ... |
1331-1519 |
5.12e-134 |
|
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: 416.39 E-value: 5.12e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1331 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLGKKVI 1410
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1411 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKPVR 1490
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*....
gi 767941789 1491 IVGLSTALANARDLADWLNIKQMGLFNFR 1519
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
481-678 |
1.41e-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: 1.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 481 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFQQ-GVIKKNEFKIVYVAPMKALAAEMTDYFSRRL 559
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 560 EPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDVALSQIVRLLILDEVHLLHEDRGPVLESIVARTLRQ 639
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 767941789 640 VESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFFFD 678
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
983-1291 |
2.68e-124 |
|
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: 393.87 E-value: 2.68e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 983 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNfCELSTPGGVENSYGKI 1062
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEK-VPIPVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1063 NILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSILPPHI 1142
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1143 LTRLEEKKLTV--DKLKDMRKDEIGHILHHVNIGLKVKQCVHQIPSVMMEASIQPITRTVLRVTLSIYADFTWNDQVHGT 1220
Cdd:pfam02889 160 IKKLEKKGVESvrDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767941789 1221 VgEPWWIWVEDPTNDHIYHSEYFLALKKQVISkeAQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIIN 1291
Cdd:pfam02889 240 S-EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
980-1293 |
4.58e-113 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 361.96 E-value: 4.58e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 980 YFSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNFCELSTPGGVENSY 1059
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1060 GKINILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSILP 1139
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1140 PHILTRLEEKK-LTVDKLKDMRKDEIGHILHHVN-IGLKVKQCVHQIPSVMMEASIQPITRTVLRVTLSIYADFTWNDQV 1217
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLGLLDaEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767941789 1218 HGTVgEPWWIWVEDPTNDHIYHSEYFLALKKQVIskEAQLLVFTIPIFEPLPsQYYIRAVSDRWLGAEAVCIINFQ 1293
Cdd:smart00611 241 HGKQ-EGWWLVIGDSDGNELLHIERFSLNKKNVS--EEVKLDFTAPATEGNY-QYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
465-678 |
3.01e-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: 355.52 E-value: 3.01e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 465 IQDLDEIGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHF-QQGVIKKNEFKIVYVAP 543
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRnPDGTINLDAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 544 MKALAAEMTDYFSRRLEPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSvGDVALSQIVRLLILDEVHLLHE 623
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKS-GDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767941789 624 DRGPVLESIVARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFFFD 678
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1814-2183 |
4.59e-100 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 324.60 E-value: 4.59e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1814 SIEPLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPHSFDSPH 1893
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1894 TKAHLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWLKDSSLLTLPNIE 1973
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1974 NHHLHLFKKWKpimkgphargRTSIESLPELIHAcgGKDHVFSSMVeselhaAKTKQAWNFLSHLPVINVGISVKGSwDD 2053
Cdd:smart00611 161 EEILKRLEKKK----------VLSLEDLLELEDE--ERGELLGLLD------AEGERVYKVLSRLPKLNIEISLEPI-TR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 2054 LVEGHNELSVSTLTADKRDDnkwiklhadqeyvlqvslqrvhfgfhkgkpescavtprfpkSKDEGWFLILGEVDKRELI 2133
Cdd:smart00611 222 TVLGVEVTLTVDLTWDDEIH-----------------------------------------GKQEGWWLVIGDSDGNELL 260
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 767941789 2134 ALKRVGYIRNH--HVASLSFYTPEIPGRYIYTLYFMSDCYLGLDQQYDIYLN 2183
Cdd:smart00611 261 HIERFSLNKKNvsEEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1332-1854 |
1.17e-95 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 320.69 E-value: 1.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1332 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKVRIEEkLGKKVIE 1411
Cdd:COG1204 23 LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEE-LGIKVGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1412 LTGDVTPDMKSIAKADLIVTTPEKWDGVSRswQNRNYVQQVTILIIDEIHLLG-EERGPVLEVIVSRtnfiSSHTEKPVR 1490
Cdd:COG1204 100 STGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTLEVLLAR----LRRLNPEAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1491 IVGLSTALANARDLADWLNIKqmglfNFRPSVRPVPLE--VHIQG---FPGQHYCPRmasmnKPAFQAIRSHSPA-KPVL 1564
Cdd:COG1204 174 IVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSK-----DPTLALALDLLEEgGQVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1565 IFVSSRRQTRLTALELIAFLA---TEEDPKQWLNMDEREMEniIATVRDSNLKLT--LAFGIGMHHAGLHERDRKTVEEL 1639
Cdd:COG1204 244 VFVSSRRDAESLAKKLADELKrrlTPEEREELEELAEELLE--VSEETHTNEKLAdcLEKGVAFHHAGLPSELRRLVEDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1640 FVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGktrryVDFPITDVLQMMGRAGRPQFDDQGKAVILVHDIK---KD 1716
Cdd:COG1204 322 FREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDeadEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1717 FYKKFLYEPFPVESSLLGVLSD--HLNAEIAGGTITSKQDALDYITWTYFFRRlimnPSYYNLGDVshdsVNKFLSHLIE 1794
Cdd:COG1204 397 FERYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQ----YDKGDLEEV----VDDALEFLLE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767941789 1795 KSLIElelsycieigEDNRSIEPLTYGRIASYYYLKHQTVKMFKDRLK---PECSTEELLSIL 1854
Cdd:COG1204 469 NGFIE----------EDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadEEFTDLGLLHLI 521
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
465-1020 |
9.71e-94 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 314.91 E-value: 9.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 465 IQDLDE---IGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFqqgvikknefKIVYV 541
Cdd:COG1204 3 VAELPLekvIEFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 542 APMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGdvALSQIvRLLILDEVHLL 621
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDV-DLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 622 H-EDRGPVLESIVARtLRQVESTqsmIRILGLSATLPNYLDVATFLHVNPyiglffFDGRFRPVPLgqtFLGIKCANKmq 700
Cdd:COG1204 150 DdESRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGV-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 701 qlNNMDEVCYEN-------VLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNCGHIPFFFPTQGHDYVLAEKQVQRSRN 773
Cdd:COG1204 215 --LRFDDGSRRSkdptlalALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 774 KQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTqiyaaKRGSFVDLGILDVMQ 853
Cdd:COG1204 293 EKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-----KRGGMVPIPVLEFKQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 854 IFGRAGRPQFDKFGEGIIIT-THDKLSH--YLTLLTQRNPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWISYTYLY 928
Cdd:COG1204 368 MAGRAGRPGYDPYGEAILVAkSSDEADElfERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTFYA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 929 VRMRANPLaygishkayqidptlrkhrEQLVIEVGRKLDKAQMIrfEERTGYFSSTDLGRTASHYYIKYNTIETFNELFD 1008
Cdd:COG1204 448 YQYDKGDL-------------------EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAELVDGLR 506
|
570
....*....|..
gi 767941789 1009 AHKTEGDIFAIV 1020
Cdd:COG1204 507 KADEEFTDLGLL 518
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
983-1292 |
1.06e-93 |
|
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: 306.59 E-value: 1.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 983 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNfCELSTPGGVENS-YGK 1061
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-VPIPVKEGIIDSpHAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1062 INILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLW-GWASPLRQF-SILP 1139
Cdd:smart00973 80 VNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWeDSDSPLKQLpHFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1140 PHILTRLEEKKL--TVDKLKDMRKDEIGHILH-HVNIGLKVKQCVHQIPSVMMEASIQPITRTV-LRVTLSIYADFTWND 1215
Cdd:smart00973 160 EDVYDKLELKDGsrSFELLLDMNAAELGEFLNrLPPNGRLIYELLRRFPKIEVEAEVLPITRDLtLRVELEITPVFAWDL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767941789 1216 QVHGTVGEPWWIWVEDPTNDHIYHSEYFLALKKQVISKeaQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIINF 1292
Cdd:smart00973 240 PRHKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSNE--VKLDFTVPLSEPGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1329-1519 |
9.62e-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: 289.93 E-value: 9.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1329 FSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLGKK 1408
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPLLGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1409 VIELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKP 1488
Cdd:cd18021 81 VVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 767941789 1489 VRIVGLSTALANARDLADWLNIKQMGLFNFR 1519
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 ... |
1817-2182 |
6.17e-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: 6.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1817 PLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPHSFDSPHTKA 1896
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1897 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWL-KDSSLLTLPNIEnh 1975
Cdd:smart00973 81 NLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEdSDSPLKQLPHFL-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1976 hlhlfkkwkpimkgphargrtsiesLPELIHACGGKDHVFSSMVESELHAAKTKQAWNFLSHLPVINVGISVKGSWDDLv 2055
Cdd:smart00973 159 -------------------------IEDVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEV- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 2056 eghnELSVSTLTADkrddnKWIKLHADQEYVLQVSLQRvhfgfhkgkpescavtprfPKSKDEGWFLILGEVDKRELIAL 2135
Cdd:smart00973 213 ----EAEVLPITRD-----LTLRVELEITPVFAWDLPR-------------------HKGKSESWWLVVGDSDTNELLAI 264
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767941789 2136 KRV----GYIRNHHVASLSFYTPEiPGRYIYTLYFMSDCYLGLDQQYDIYL 2182
Cdd:smart00973 265 KRVtlrkKKKSNEVKLDFTVPLSE-PGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1817-2180 |
3.23e-70 |
|
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: 238.64 E-value: 3.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1817 PLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPhSFDSPHTKA 1896
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKG-DIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1897 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWLKDSSLLTLPNIENHH 1976
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1977 LHLFKKwkpimkgphaRGRTSIESL-----PELIHACGGKDHVFssmveselhaaktKQAWNFLSHLPVINVgisvkgsw 2051
Cdd:pfam02889 160 IKKLEK----------KGVESVRDIlelddAEELGELIRNPKMG-------------KDIAQFVNRFPKIEI-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 2052 ddlveghnELSVSTLTADkrddnkwiklhadqeyVLQVSLQrvhfgfhkgkpescaVTPRFPKSKD-----EGWFLILGE 2126
Cdd:pfam02889 209 --------EAEVQPITRS----------------VLRVEVT---------------ITPDFPWDKRvhgksEGFWLVVGD 249
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 767941789 2127 VDKRELIALKRV--GYIRNHHVASLSFYTPEI-PGRYIYTLYFMSDCYLGLDQQYDI 2180
Cdd:pfam02889 250 SDGNEILHIERFtlTKRTLAGEHKLEFTVPPSdPGPPQLFVRLISDSWLGADQEVPI 306
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
1331-1519 |
1.60e-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: 222.91 E-value: 1.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1331 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDDWKVRIEEkLGKKVI 1410
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSG-GKAVYIAPTRALVNQKEADLRERFGP-LGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1411 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRnYVQQVTILIIDEIHLLG-EERGPVLEVIVSRTNFIsshtEKPV 1489
Cdd:cd17921 79 LLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI----NKNA 153
|
170 180 190
....*....|....*....|....*....|
gi 767941789 1490 RIVGLSTALANARDLADWLNIKqmGLFNFR 1519
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 ... |
1523-1711 |
1.85e-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: 221.66 E-value: 1.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1523 RPVPLEVHIQGFPGQHYCPRMASMNK-----PAFQAIRSHSPAKPVLIFVSSRRQTRLTALELIaflateedpkqwlnmd 1597
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1598 eremeniiatvrdsnlkltlafGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKT 1677
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 767941789 1678 RRYvdFPITDVLQMMGRAGRPQFDDQGKAVILVH 1711
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 ... |
1332-1524 |
4.36e-66 |
|
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: 223.00 E-value: 4.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1332 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTS-----KAVYIAPLKALVRERMDDWKVRIeEKLG 1406
Cdd:cd18023 2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLpwgnrKVVYIAPIKALCSEKYDDWKEKF-GPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1407 KKVIELTGD-VTPDMKSIAKADLIVTTPEKWDGVSRSW-QNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFISSH 1484
Cdd:cd18023 81 LSCAELTGDtEMDDTFEIQDADIILTTPEKWDSMTRRWrDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSSS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767941789 1485 TEK------PVRIVGLSTALANARDLADWLNIKQMGLFNFRPSVRP 1524
Cdd:cd18023 161 SELrgstvrPMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1349-1877 |
7.37e-61 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 224.31 E-value: 7.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFrvfNKYPTS--KAVYIAPLKALVRER---MDDWkvrieEKLGKKVIELTGDVTPDMKSI 1423
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMV---NKLLREggKAVYLVPLKALAEEKyreFKDW-----EKLGLRVAMTTGDYDSTDEWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1424 AKADLIVTTPEKWDGVSR---SWqnrnyVQQVTILIIDEIHLLGE-ERGPVLEVIVSrtnfissHTEKPVRIVGLSTALA 1499
Cdd:PRK00254 113 GKYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSyDRGATLEMILT-------HMLGRAQILGLSATVG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1500 NARDLADWLNIKQMglfnfRPSVRPVPLE--VHIQGF------PGQHYcprMASMNKPAFQAIRShspAKPVLIFVSSRR 1571
Cdd:PRK00254 181 NAEELAEWLNAELV-----VSDWRPVKLRkgVFYQGFlfwedgKIERF---PNSWESLVYDAVKK---GKGALVFVNTRR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1572 QTRLTALELIAFLATEEDPKQwlnmdEREMENIIATVRD--SNLKLTLAF--GIGMHHAGLHERDRKTVEELFVNCKVQV 1647
Cdd:PRK00254 250 SAEKEALELAKKIKRFLTKPE-----LRALKELADSLEEnpTNEKLKKALrgGVAFHHAGLGRTERVLIEDAFREGLIKV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1648 LIATSTLAWGVNFPAHLVIIKGTEYYDGKTrrYVDFPITDVLQMMGRAGRPQFDDQGKAVILVH-DIKKDFYKKF----- 1721
Cdd:PRK00254 325 ITATPTLSAGINLPAFRVIIRDTKRYSNFG--WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERYifgkp 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1722 --LYEPFPVESSLLGvlsdHLNAEIAGGTITSKQDALDYITWTYFfrrlimnpsYYNLGDVSH--DSVNKFLSHLIEKSL 1797
Cdd:PRK00254 403 ekLFSMLSNESAFRS----QVLALITNFGVSNFKELVNFLERTFY---------AHQRKDLYSleEKAKEIVYFLLENEF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1798 IELELsycieigEDNrsIEPLTYGRIASYYYLKHQTVKMFKDRLkPECSTEE----LLSILSDAEEYTDLPVRHNEDHMN 1873
Cdd:PRK00254 470 IDIDL-------EDR--FIPLPLGIRTSQLYIDPLTAKKFKDAF-PKIEKNPnplgIFQLIASTPDMTPLNYSRKEMEDL 539
|
....
gi 767941789 1874 SELA 1877
Cdd:PRK00254 540 LDEA 543
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
483-683 |
1.06e-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: 196.04 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 483 NRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQhfqQGVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPL 562
Cdd:cd18023 3 NRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKE---RNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 563 GIIVKELTGDMQLSKS-EILRTQMLVTTPEKWDVVTRKSVGDVALSQIVRLLILDEVHLLHEDRGPVLESIVARTLRQVE 641
Cdd:cd18023 80 GLSCAELTGDTEMDDTfEIQDADIILTTPEKWDSMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767941789 642 STQSM------IRILGLSATLPNYLDVATFLHVNPyIGLFFFDGRFRP 683
Cdd:cd18023 160 SSELRgstvrpMRFVAVSATIPNIEDLAEWLGDNP-AGCFSFGESFRP 206
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
482-673 |
6.73e-56 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 192.48 E-value: 6.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 482 LNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHfqqgvikknEFKIVYVAPMKALAAEMTDYFSRRLEP 561
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS---------GGKAVYIAPTRALVNQKEADLRERFGP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 562 LGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDvaLSQIVRLLILDEVHLLH-EDRGPVLESIVARTLRQv 640
Cdd:cd17921 73 LGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER--LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI- 149
|
170 180 190
....*....|....*....|....*....|...
gi 767941789 641 estQSMIRILGLSATLPNYLDVATFLHVNPYIG 673
Cdd:cd17921 150 ---NKNARFVGLSATLPNAEDLAEWLGVEDLIR 179
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
498-1039 |
5.35e-53 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 200.43 E-value: 5.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 498 ENMLICAPTGAGKTNIAMLTVLHEIrqhFQQGvikkneFKIVYVAPMKALAAEMTDYFsRRLEPLGIIVKELTGDMQlSK 577
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKL---LREG------GKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYD-ST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 578 SEIL-RTQMLVTTPEKWDVVTRKSVgdvalSQI--VRLLILDEVHLL-HEDRGPVLESIVARTLRQVEstqsmirILGLS 653
Cdd:PRK00254 109 DEWLgKYDIIIATAEKFDSLLRHGS-----SWIkdVKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ-------ILGLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 654 ATLPNYLDVATFLHVNpyigLFFFDgrFRPVPL-----GQTFLGIKCANKMQQLNNMDEVCYEnvlkQVKAGHQVMVFVH 728
Cdd:PRK00254 177 ATVGNAEELAEWLNAE----LVVSD--WRPVKLrkgvfYQGFLFWEDGKIERFPNSWESLVYD----AVKKGKGALVFVN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 729 ARNATVRTAMSLIERAKNCghipFFFPTQGHDYVLAEKQVQRSRNKQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHI 808
Cdd:PRK00254 247 TRRSAEKEALELAKKIKRF----LTKPELRALKELADSLEENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 809 KVLVCTATLAWGVNLPAHAVIIKGTQIYAakRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDK----LSHYL-- 882
Cdd:PRK00254 323 KVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklMERYIfg 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 883 ------TLLTQRNPIESQFLesladnlnAEIALGTVTNVEEAVKWISYTYlYVRMRANPlaYGISHKAYQIDPTLrkhRE 956
Cdd:PRK00254 401 kpeklfSMLSNESAFRSQVL--------ALITNFGVSNFKELVNFLERTF-YAHQRKDL--YSLEEKAKEIVYFL---LE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 957 QLVIEvgrkldkaqmIRFEERtgyFSSTDLGRTASHYYIKYNTIETFNELFDahKTEGD-----IFAIVSKAEEFDQIKV 1031
Cdd:PRK00254 467 NEFID----------IDLEDR---FIPLPLGIRTSQLYIDPLTAKKFKDAFP--KIEKNpnplgIFQLIASTPDMTPLNY 531
|
....*...
gi 767941789 1032 REEEIEEL 1039
Cdd:PRK00254 532 SRKEMEDL 539
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
682-874 |
8.89e-53 |
|
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: 182.37 E-value: 8.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 682 RPVPLGQTFLGIK----CANKMQQLNNMDEVCYENVLKQVKAGHQVMVFVHARNATVRTAMSLIerakncghipfffptq 757
Cdd:cd18795 1 RPVPLEEYVLGFNglgiKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 758 ghdyvlaekqvqrsrnkqvrelfpdGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYA 837
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 767941789 838 AKRgsFVDLGILDVMQIFGRAGRPQFDKFGEGIIITT 874
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1349-1867 |
9.71e-53 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 200.18 E-value: 9.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKVRieEKLGKKVIELTGDVTPDMKSIAKADL 1428
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAMLKAIAR--GGKALYIVPLRALASEKFEEFERF--EELGVRVGISTGDYDSRDEWLGDNDI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1429 IVTTPEKWDGVSR---SWqnrnyVQQVTILIIDEIHLLG-EERGPVLEVIVS---RTNfisshtekP-VRIVGLSTALAN 1500
Cdd:PRK02362 117 IVATSEKVDSLLRngaPW-----LDDITCVVVDEVHLIDsANRGPTLEVTLAklrRLN--------PdLQVVALSATIGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1501 ARDLADWLNIK-----------QMGLF-----NFRPSVRPVP-----------LEVHIQGfpGQhyCprmasmnkpafqa 1553
Cdd:PRK02362 184 ADELADWLDAElvdsewrpidlREGVFyggaiHFDDSQREVEvpskddtlnlvLDTLEEG--GQ--C------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1554 irshspakpvLIFVSSRRQTRLTALELIAFLateedpKQWLNMDER-EMENIIATVRDS-------NLKLTLAFGIGMHH 1625
Cdd:PRK02362 247 ----------LVFVSSRRNAEGFAKRAASAL------KKTLTAAERaELAELAEEIREVsdtetskDLADCVAKGAAFHH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1626 AGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGkTRRYVDFPITDVLQMMGRAGRPQFDDQGK 1705
Cdd:PRK02362 311 AGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDG-GAGMQPIPVLEYHQMAGRAGRPGLDPYGE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1706 AVILV--HDIKKDFYKKFLY-EPFPVESSLL--GVLSDHLNAEIAGGTITSKQDALDYITWTYFFRRlimNPSYYNLGDV 1780
Cdd:PRK02362 390 AVLLAksYDELDELFERYIWaDPEDVRSKLAtePALRTHVLSTIASGFARTRDGLLEFLEATFYATQ---TDDTGRLERV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1781 shdsVNKFLSHLIEKSLIElelsycieigEDNRSIEPLTYGRIASYYYlkhqtvkmfkdrLKPeCSTEELLSILSDAEEY 1860
Cdd:PRK02362 467 ----VDDVLDFLERNGMIE----------EDGETLEATELGHLVSRLY------------IDP-LSAAEIIDGLEAAKKP 519
|
....*..
gi 767941789 1861 TDLPVRH 1867
Cdd:PRK02362 520 TDLGLLH 526
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
1315-1518 |
2.50e-52 |
|
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: 183.73 E-value: 2.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1315 ITALGCKAYEALYNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKY--PTS-------KAVYIAP 1385
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHrnPDGtinldafKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1386 LKALVRERMDDWKVRIEEkLGKKVIELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGE 1465
Cdd:cd18019 81 MKALVQEMVGNFSKRLAP-YGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767941789 1466 ERGPVLEVIVSRTNFISSHTEKPVRIVGLSTALANARDLADWLNIK-QMGLFNF 1518
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDpKKGLFYF 213
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1349-1827 |
2.56e-51 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 194.72 E-value: 2.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWkVRIEEkLGKKVIELTGDV--TPDMksIAKA 1426
Cdd:PRK01172 39 NVIVSVPTAAGKTLIAYSAIYETFLA--GLKSIYIVPLRSLAMEKYEEL-SRLRS-LGMRVKISIGDYddPPDF--IKRY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1427 DLIVTTPEKWDgvSRSWQNRNYVQQVTILIIDEIHLLGEE-RGPVLEVIVSRTNFISSHTekpvRIVGLSTALANARDLA 1505
Cdd:PRK01172 113 DVVILTSEKAD--SLIHHDPYIINDVGLIVADEIHIIGDEdRGPTLETVLSSARYVNPDA----RILALSATVSNANELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1506 DWLNIKQMglfnfRPSVRPVPLEVHIQgFPGQHYCPRMASMNKPAFQAIRSH-SPAKPVLIFVSSRRQTRLTALELIAFL 1584
Cdd:PRK01172 187 QWLNASLI-----KSNFRPVPLKLGIL-YRKRLILDGYERSQVDINSLIKETvNDGGQVLVFVSSRKNAEDYAEMLIQHF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1585 ATEEDPKqwLNMDEremeniiATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHL 1664
Cdd:PRK01172 261 PEFNDFK--VSSEN-------NNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1665 VIIKG-TEYYDGKTRryvdfPIT--DVLQMMGRAGRPQFDDQGKAVILV-----HDIKKDFYKKflyEPFPVESSLLGVL 1736
Cdd:PRK01172 332 VIVRDiTRYGNGGIR-----YLSnmEIKQMIGRAGRPGYDQYGIGYIYAaspasYDAAKKYLSG---EPEPVISYMGSQR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1737 SDHLN--AEIAGGTITSKQDALDYITWTYFFRRlimnpsyyNLGDVSHDSVNKFLSHLIEKSLIELELSY-CIEIGE--D 1811
Cdd:PRK01172 404 KVRFNtlAAISMGLASSMEDLILFYNETLMAIQ--------NGVDEIDYYIESSLKFLKENGFIKGDVTLrATRLGKltS 475
|
490
....*....|....*.
gi 767941789 1812 NRSIEPLTYGRIASYY 1827
Cdd:PRK01172 476 DLYIDPESALILKSAF 491
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
483-678 |
6.96e-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: 6.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 483 NRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFQqgvikkneFKIVYVAPMKALAAE-MTDYFSRRLEP 561
Cdd:cd18022 3 NPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPG--------SKVVYIAPLKALVRErVDDWKKRFEEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 562 LGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVV-----TRKSVgdvalsQIVRLLILDEVHLLHEDRGPVLESIVART 636
Cdd:cd18022 75 LGKKVVELTGDVTPDMKALADADIIITTPEKWDGIsrswqTREYV------QQVSLIIIDEIHLLGSDRGPVLEVIVSRM 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767941789 637 LRQVESTQSMIRILGLSATLPNYLDVATFLHVNPyIGLFFFD 678
Cdd:cd18022 149 NYISSQTEKPVRLVGLSTALANAGDLANWLGIKK-MGLFNFR 189
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
497-995 |
3.25e-47 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 183.24 E-value: 3.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 497 NENMLICAPTGAGKTNIAMLTVLHEIrqhfqqgvikKNEFKIVYVAPMKALAAEMTDYFSRrLEPLGIIVKELTGDMQlS 576
Cdd:PRK02362 39 GKNLLAAIPTASGKTLIAELAMLKAI----------ARGGKALYIVPLRALASEKFEEFER-FEELGVRVGISTGDYD-S 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 577 KSEIL-RTQMLVTTPEKWDVVTRKsvGDVALSQIVrLLILDEVHLL-HEDRGPVLESIVARTLRQVESTQsmirILGLSA 654
Cdd:PRK02362 107 RDEWLgDNDIIVATSEKVDSLLRN--GAPWLDDIT-CVVVDEVHLIdSANRGPTLEVTLAKLRRLNPDLQ----VVALSA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 655 TLPNYLDVATFLHVNpyiglfFFDGRFRPVPLGQ-TFLG--IKCANKMQQLNNM--DEVcyEN-VLKQVKAGHQVMVFVH 728
Cdd:PRK02362 180 TIGNADELADWLDAE------LVDSEWRPIDLREgVFYGgaIHFDDSQREVEVPskDDT--LNlVLDTLEEGGQCLVFVS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 729 AR-NA---------TVRTAMSLIERAKNCGhipfffptqghdyvLAEKQVQRSRNKQVREL---FPDGFSIHHAGMLRQD 795
Cdd:PRK02362 252 SRrNAegfakraasALKKTLTAAERAELAE--------------LAEEIREVSDTETSKDLadcVAKGAAFHHAGLSREH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 796 RNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYAAKRGSfVDLGILDVMQIFGRAGRPQFDKFGEGIIIT-T 874
Cdd:PRK02362 318 RELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAGM-QPIPVLEYHQMAGRAGRPGLDPYGEAVLLAkS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 875 HDKLS----HYLTLLTQrnPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWISYTyLYvrmranplaygishkAYQID 948
Cdd:PRK02362 397 YDELDelfeRYIWADPE--DVRSKLATepALRTHVLSTIASGFARTRDGLLEFLEAT-FY---------------ATQTD 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 767941789 949 PTLRKHReqLVIEVGRKLDKAQMIrfEERTGYFSSTDLGRTASHYYI 995
Cdd:PRK02362 459 DTGRLER--VVDDVLDFLERNGMI--EEDGETLEATELGHLVSRLYI 501
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
497-1035 |
5.78e-47 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 181.23 E-value: 5.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 497 NENMLICAPTGAGKTNIAMltvlHEIRQHFQQGVikknefKIVYVAPMKALAAEMTDYFSRrLEPLGIIVKELTGDMQLS 576
Cdd:PRK01172 37 GENVIVSVPTAAGKTLIAY----SAIYETFLAGL------KSIYIVPLRSLAMEKYEELSR-LRSLGMRVKISIGDYDDP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 577 KSEILRTQMLVTTPEKWDVVTRKsvgDVALSQIVRLLILDEVHLLH-EDRGPVLESiVARTLRQVESTqsmIRILGLSAT 655
Cdd:PRK01172 106 PDFIKRYDVVILTSEKADSLIHH---DPYIINDVGLIVADEIHIIGdEDRGPTLET-VLSSARYVNPD---ARILALSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 656 LPNYLDVATFLHVNpyiglfFFDGRFRPVPLGqtfLGIKCANKMQQLNNMDEVCYENVL--KQVKAGHQVMVFVHARNAT 733
Cdd:PRK01172 179 VSNANELAQWLNAS------LIKSNFRPVPLK---LGILYRKRLILDGYERSQVDINSLikETVNDGGQVLVFVSSRKNA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 734 VRTAMSLIErakncgHIPFFfptqgHDYVLAEKQVQrSRNKQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVC 813
Cdd:PRK01172 250 EDYAEMLIQ------HFPEF-----NDFKVSSENNN-VYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 814 TATLAWGVNLPAHAVIIKGTQIYAAKRGSFvdLGILDVMQIFGRAGRPQFDKFGEGIII----TTHDKLSHYLTllTQRN 889
Cdd:PRK01172 318 TPTLAAGVNLPARLVIVRDITRYGNGGIRY--LSNMEIKQMIGRAGRPGYDQYGIGYIYaaspASYDAAKKYLS--GEPE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 890 PIESQF--LESLADNLNAEIALGTVTNVEEAVKWISYTYLYVRMRANPLAYGIShkayqidptlrkhreqlvievgrkld 967
Cdd:PRK01172 394 PVISYMgsQRKVRFNTLAAISMGLASSMEDLILFYNETLMAIQNGVDEIDYYIE-------------------------- 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767941789 968 kaQMIRFEERTGY------FSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEE 1035
Cdd:PRK01172 448 --SSLKFLKENGFikgdvtLRATRLGKLTSDLYIDPESALILKSAFDHDYDEDLALYYISLCREIIPANTRDDY 519
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1349-1731 |
1.24e-46 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 181.68 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKvrieEKLGK-KVIELTGDVT--PDmksiak 1425
Cdd:COG4581 42 SVLVAAPTGSGKTLVAEFAIFLALAR--GRRSFYTAPIKALSNQKFFDLV----ERFGAeNVGLLTGDASvnPD------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1426 ADLIVTTPEkwdgVSRswqNRNY--------VQQVtilIIDEIHLLGE-ERGPVLEVIVsrtnfIssHTEKPVRIVGLST 1496
Cdd:COG4581 110 APIVVMTTE----ILR---NMLYregadledVGVV---VMDEFHYLADpDRGWVWEEPI-----I--HLPARVQLVLLSA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1497 ALANARDLADWLNikqmglfnfrpSV-----------RPVPLEvhiqgfpgQHYC--PRMASMNKPAFQAIRSHSPAK-- 1561
Cdd:COG4581 173 TVGNAEEFAEWLT-----------RVrgetavvvseeRPVPLE--------FHYLvtPRLFPLFRVNPELLRPPSRHEvi 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1562 ---------PVLIFVSSRRQTRLTALELIAFLATEEDPKQWLNMDEREMENIIATVRDSNLKLTLAFGIGMHHAGLHERD 1632
Cdd:COG4581 234 eeldrggllPAIVFIFSRRGCDEAAQQLLSARLTTKEERAEIREAIDEFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPKY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1633 RKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKTRRyvdfPIT--DVLQMMGRAGRPQFDDQGKAVILV 1710
Cdd:COG4581 314 RRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHR----PLTarEFHQIAGRAGRRGIDTEGHVVVLA 389
|
410 420
....*....|....*....|....*
gi 767941789 1711 HDiKKDFyKKFLY----EPFPVESS 1731
Cdd:COG4581 390 PE-HDDP-KKFARlasaRPEPLRSS 412
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1333-1518 |
8.18e-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: 161.44 E-value: 8.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1333 NPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTS---------KAVYIAPLKALVRERMDDWKVRIEe 1403
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQggvikkddfKIVYIAPMKALAAEMVEKFSKRLA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1404 KLGKKVIELTGDVTPDMKSIAKADLIVTTPEKWDGVSR-SWQNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFIS 1482
Cdd:cd18020 82 PLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRkSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQV 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 767941789 1483 SHTEKPVRIVGLSTALANARDLADWLNIKQM-GLFNF 1518
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 ... |
480-670 |
4.88e-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: 150.49 E-value: 4.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 480 KRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHeirqHFQQGvikkNEFKIVYVAPMKALAAEMTDYFSRRL 559
Cdd:cd18021 2 KFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLR----HWRQN----PKGRAVYIAPMQELVDARYKDWRAKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 560 EP-LGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVV-----TRKSVgdvalsQIVRLLILDEVHLLHEDRGPVLESIV 633
Cdd:cd18021 74 GPlLGKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLsrrwkQRKNV------QSVELFIADELHLIGGENGPVYEVVV 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 767941789 634 ARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNP 670
Cdd:cd18021 148 SRMRYISSQLEKPIRIVGLSSSLANARDVGEWLGASK 184
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
1332-1511 |
5.13e-37 |
|
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: 138.24 E-value: 5.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1332 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIfrVFNKYPTSKAVYIAPLKALVRERMDDWKVRieEKLGKKVIE 1411
Cdd:cd18028 2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAM--VNTLLEGGKALYLVPLRALASEKYEEFKKL--EEIGLKVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1412 LTGDVTPDMKSIAKADLIVTTPEKWDGVsrsWQNR-NYVQQVTILIIDEIHLLG-EERGPVLEVIVSRTNfissHTEKPV 1489
Cdd:cd18028 78 STGDYDEDDEWLGDYDIIVATYEKFDSL---LRHSpSWLRDVGVVVVDEIHLISdEERGPTLESIVARLR----RLNPNT 150
|
170 180
....*....|....*....|..
gi 767941789 1490 RIVGLSTALANARDLADWLNIK 1511
Cdd:cd18028 151 QIIGLSATIGNPDELAEWLNAE 172
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
493-968 |
6.43e-35 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 145.08 E-value: 6.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 493 AYNTNENMLICAPTGAGKTNIAMltvlHEIRQHFQQGVikknefKIVYVAPMKALAAEMTDYFSRRL--EPLGIivkeLT 570
Cdd:COG4581 36 ALEAGRSVLVAAPTGSGKTLVAE----FAIFLALARGR------RSFYTAPIKALSNQKFFDLVERFgaENVGL----LT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 571 GDMQL--------SKSEILRTQMLVTTPEKWDVvtrksvgDVAlsqivrllILDEVHLLHE-DRGPVLE-SIVARTLRqv 640
Cdd:COG4581 102 GDASVnpdapivvMTTEILRNMLYREGADLEDV-------GVV--------VMDEFHYLADpDRGWVWEePIIHLPAR-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 641 estqsmIRILGLSATLPNYLDVATFLH--------VnpyiglfffDGRFRPVPLGQTFLGIKCANKMQQLNNMDEVCYE- 711
Cdd:COG4581 165 ------VQLVLLSATVGNAEEFAEWLTrvrgetavV---------VSEERPVPLEFHYLVTPRLFPLFRVNPELLRPPSr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 712 -NVLKQVKAGHQ--VMVFVHARNATVrtamsliERAKNCGHIPFFFPTQGH--DYVLAEKQVQRS--RNKQVRELFPDGF 784
Cdd:COG4581 230 hEVIEELDRGGLlpAIVFIFSRRGCD-------EAAQQLLSARLTTKEERAeiREAIDEFAEDFSvlFGKTLSRLLRRGI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 785 SIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGtqiyAAKR--GSFVDLGILDVMQIFGRAGRPQ 862
Cdd:COG4581 303 AVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTK----LSKFdgERHRPLTAREFHQIAGRAGRRG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 863 FDKFGEGIIITT-HDKLSHYLTLLTQR-NPIESQFlesladnlnaEIALGTVTNVeeaVKWISYTylyvRMRAnplAYGI 940
Cdd:COG4581 379 IDTEGHVVVLAPeHDDPKKFARLASARpEPLRSSF----------RPSYNMVLNL---LARPGLE----RARE---LLED 438
|
490 500
....*....|....*....|....*...
gi 767941789 941 SHKAYQIDPTLRKHREQlVIEVGRKLDK 968
Cdd:COG4581 439 SFAQFQADRSVVGLARR-ARELERALAG 465
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
483-661 |
1.32e-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: 125.43 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 483 NRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQhfqqgviKKNEFKIVYVAPMKALAAEMTDYFSRRLEPL 562
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK-------LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 563 GIIVKELTGDMQLSK--SEILRTQMLVTTPEKWDVVTRKSvgdVALSQiVRLLILDEVHLLHE-DRGPVLESIVARtlrq 639
Cdd:pfam00270 73 GLKVASLLGGDSRKEqlEKLKGPDILVGTPGRLLDLLQER---KLLKN-LKLLVLDEAHRLLDmGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|..
gi 767941789 640 vesTQSMIRILGLSATLPNYLD 661
Cdd:pfam00270 145 ---LPKKRQILLLSATLPRNLE 163
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1333-1504 |
1.87e-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: 124.66 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1333 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFN-KYPTSKAVYIAPLKALVRERMDDWKVRIeEKLGKKVIE 1411
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDkLDNGPQALVLAPTRELAEQIYEELKKLG-KGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1412 LTGDVTP--DMKSIAKADLIVTTPEKWDGVsrsWQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNfisshteKP 1488
Cdd:pfam00270 79 LLGGDSRkeQLEKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRRLP-------KK 148
|
170
....*....|....*..
gi 767941789 1489 VRIVGLS-TALANARDL 1504
Cdd:pfam00270 149 RQILLLSaTLPRNLEDL 165
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
481-666 |
8.69e-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: 112.04 E-value: 8.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 481 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHfqqgvikkneFKIVYVAPMKALAAEMTDYFSrRLE 560
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEG----------GKALYLVPLRALASEKYEEFK-KLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 561 PLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSvgdVALSQIVRLLILDEVHLLH-EDRGPVLESIVARTLRQ 639
Cdd:cd18028 70 EIGLKVGISTGDYDEDDEWLGDYDIIVATYEKFDSLLRHS---PSWLRDVGVVVVDEIHLISdEERGPTLESIVARLRRL 146
|
170 180
....*....|....*....|....*..
gi 767941789 640 VESTQsmirILGLSATLPNYLDVATFL 666
Cdd:cd18028 147 NPNTQ----IIGLSATIGNPDELAEWL 169
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1334-1710 |
7.21e-26 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 116.53 E-value: 7.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1334 PVQT-QIFHTLYHTDcNVLLGAPTGSGKTVAAELA-IFRVFNKypTSKAVYIAPLKALVRERMDDWKVRIEEKLgkKVIE 1411
Cdd:COG1202 212 PVQSlAVENGLLEGK-DQLVVSATATGKTLIGELAgIKNALEG--KGKMLFLVPLVALANQKYEDFKDRYGDGL--DVSI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1412 LTGDV---TPDMKSIAKADLIVTTPEKWDGVSRSwqnRNYVQQVTILIIDEIHLLGE-ERGPVLEVIVSRTNFISSHTEk 1487
Cdd:COG1202 287 RVGASrirDDGTRFDPNADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEVHMLEDpERGHRLDGLIARLKYYCPGAQ- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1488 pvrIVGLSTALANARDLADWLNIKQMgLFNfrpsVRPVPLEVHIQGFPGQHYCPRMASMNKPAFQAIRSHSPAKPVLIFV 1567
Cdd:COG1202 363 ---WIYLSATVGNPEELAKKLGAKLV-EYE----ERPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1568 SSRRQTRltaleliaflateedpkqwlnmderemeniiatvrdsnlKLTLAFGIGM--HHAGLHERDRKTVEELFVNCKV 1645
Cdd:COG1202 435 NSRRRCH---------------------------------------EIARALGYKAapYHAGLDYGERKKVERRFADQEL 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767941789 1646 QVLIATSTLAWGVNFPAHLVIIK----GTEYydgktrryvdFPITDVLQMMGRAGRPQFDDQGKAVILV 1710
Cdd:COG1202 476 AAVVTTAALAAGVDFPASQVIFDslamGIEW----------LSVQEFHQMLGRAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
474-685 |
1.03e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.81 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 474 LAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRqhfqqgviKKNEFKIVYVAPMKALAAEMTD 553
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALK--------RGKGGRVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 554 YFSRRLEPLGIIVKELTGD----MQLSKSEILRTQMLVTTPEKWDVVTRKsvGDVALSQiVRLLILDEVH-LLHEDRGPV 628
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRLLDLLEN--DKLSLSN-VDLVILDEAHrLLDGGFGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767941789 629 LESIVARTLRqvestqsMIRILGLSATLPNYLDVATFLHVNpyiGLFFFDGRFRPVP 685
Cdd:smart00487 150 LEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1327-1526 |
1.21e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 103.73 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1327 YNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLG 1406
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1407 KKVIELTGDVT-PDMKSIAK--ADLIVTTPEKWDGVSRswQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNfis 1482
Cdd:smart00487 84 KVVGLYGGDSKrEQLRKLESgkTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767941789 1483 shteKPVRIVGLS-TALANARDLADWLNIkqmGLFNFRPSVRPVP 1526
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 ... |
1347-1520 |
2.66e-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: 96.90 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1347 DCNVLLGAPTGSGKTVAAELAIFRVF--NKyptSKAVYIAPLKALVRERMDdWKVRIEEKLGKKVIELTGDVTPDM-KSI 1423
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLleRR---KKALFVLPYVSIVQEKVD-ALSPLFEELGFRVEGYAGNKGRSPpKRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1424 AKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGEE-RGPVLEVIVSRtnfISSHTEKPVRIVGLSTALANAR 1502
Cdd:cd18026 109 KSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDGhRGALLELLLTK---LLYAAQKNIQIVGMSATLPNLE 185
|
170 180
....*....|....*....|
gi 767941789 1503 DLADWLNIKqmgLF--NFRP 1520
Cdd:cd18026 186 ELASWLRAE---LYttNFRP 202
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
1349-1508 |
1.25e-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: 93.80 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKYPTS--KAVYIAPLKALVRermdDWKVRIEE-----KLGKKVIELTGDVTPDMK 1421
Cdd:cd17922 3 NVLIAAPTGSGKTEAAFLPALSSLADEPEKgvQVLYISPLKALIN----DQERRLEEpldeiDLEIPVAVRHGDTSQSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1422 SIAKA---DLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRtnfISSHTEKPVRIVGLSTA 1497
Cdd:cd17922 79 AKQLKnppGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHaLLGSKRGVQLELLLER---LRKLTGRPLRRIGLSAT 155
|
170
....*....|.
gi 767941789 1498 LANARDLADWL 1508
Cdd:cd17922 156 LGNLEEAAAFL 166
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
497-666 |
1.38e-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: 93.80 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 497 NENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGVikknefKIVYVAPMKALAAEMTdyfsRRLE------PLGIIVKELT 570
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV------QVLYISPLKALINDQE----RRLEepldeiDLEIPVAVRH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 571 GDM-QLSKSEILRT--QMLVTTPEKWDVVTRKSVGDVALSQiVRLLILDEVH-LLHEDRGPVLESIVARtLRQVESTQsm 646
Cdd:cd17922 71 GDTsQSEKAKQLKNppGILITTPESLELLLVNKKLRELFAG-LRYVVVDEIHaLLGSKRGVQLELLLER-LRKLTGRP-- 146
|
170 180
....*....|....*....|
gi 767941789 647 IRILGLSATLPNYLDVATFL 666
Cdd:cd17922 147 LRRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
497-683 |
1.33e-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: 91.89 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 497 NENMLICAPTGAGKTNIAMLTVLHEIRQhfqqgvikkNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDmqLS 576
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLLE---------RRKKALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGN--KG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 577 KSEILR---TQMLVTTPEKWDVVTRKSVGDVALSQIvRLLILDEVHLLHE-DRGPVLESIVARTLRqveSTQSMIRILGL 652
Cdd:cd18026 102 RSPPKRrksLSVAVCTIEKANSLVNSLIEEGRLDEL-GLVVVDELHMLGDgHRGALLELLLTKLLY---AAQKNIQIVGM 177
|
170 180 190
....*....|....*....|....*....|.
gi 767941789 653 SATLPNYLDVATFLHVnpyiglFFFDGRFRP 683
Cdd:cd18026 178 SATLPNLEELASWLRA------ELYTTNFRP 202
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1329-1666 |
7.21e-19 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 94.01 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1329 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAIF-RVFNKYPTSKA------VYIAPLKAL---VRERMDDWK 1398
Cdd:COG1201 22 FGAPTPPQREAW-PAIAAGESTLLIAPTGSGKTLAAFLPALdELARRPRPGELpdglrvLYISPLKALandIERNLRAPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1399 VRIEEKLGKKVIEL-----TGDVTPDMKSIAKA---DLIVTTPE---------KWdgvsrswqnRNYVQQVTILIIDEIH 1461
Cdd:COG1201 101 EEIGEAAGLPLPEIrvgvrTGDTPASERQRQRRrppHILITTPEslallltspDA---------RELLRGVRTVIVDEIH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1462 -LLGEERGPVLEVIVSRtnfISSHTEKPVRIVGLSTALANARDLADWLnikqMGLFNFRPS--VRP-----------VPL 1527
Cdd:COG1201 172 aLAGSKRGVHLALSLER---LRALAPRPLQRIGLSATVGPLEEVARFL----VGYEDPRPVtiVDAgagkkpdlevlVPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1528 EVHIQGFP-----GQHYCPRMAsmnkpafQAIRSHspaKPVLIFVSSRRQTRLTALELIAFLATEEDPkqwlnmdereme 1602
Cdd:COG1201 245 EDLIERFPwaghlWPHLYPRVL-------DLIEAH---RTTLVFTNTRSQAERLFQRLNELNPEDALP------------ 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767941789 1603 niiatvrdsnlkltlafgIGMHHAGL-HERdRKTVEELFVNCKVQVLIATSTLAWGVNFPA-HLVI 1666
Cdd:COG1201 303 ------------------IAAHHGSLsREQ-RLEVEEALKAGELRAVVATSSLELGIDIGDvDLVI 349
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
474-882 |
4.39e-16 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 84.50 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 474 LAFKGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQHfqqgvikkNEFKIVYVAPMKALAA---- 549
Cdd:COG1205 49 LKKRGIERLYSHQAEAIEAARA-GKNVVIATPTASGKSLAYLLPVLEALLED--------PGATALYLYPTKALARdqlr 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 550 EMTDYFSRRlePLGIIVKELTGDMQLS-KSEILRT-QMLVTTP-----------EKWDVVTRKsvgdvalsqiVRLLILD 616
Cdd:COG1205 120 RLRELAEAL--GLGVRVATYDGDTPPEeRRWIREHpDIVLTNPdmlhygllphhTRWARFFRN----------LRYVVID 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 617 EVHLLhedRGpVLESIVA----RTLRQVESTQSMIRILGLSATLPNYLDVA---------------------TFLHVNPY 671
Cdd:COG1205 188 EAHTY---RG-VFGSHVAnvlrRLRRICRHYGSDPQFILASATIGNPAEHAerltgrpvtvvdedgsprgerTFVLWNPP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 672 IGLfffDGRFRPVPLgqtflgikcankmqqlnnmdEVCYenVLKQ-VKAGHQVMVFVHARNATVRTAMSLIERAKncghi 750
Cdd:COG1205 264 LVD---DGIRRSALA--------------------EAAR--LLADlVREGLRTLVFTRSRRGAELLARYARRALR----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 751 pfffptqghdyvlaekqvqrsrnkqvRELFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPA-HAVI 829
Cdd:COG1205 314 --------------------------EPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVV 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 767941789 830 IKGtqiYAAKRGSFVdlgildvmQIFGRAGRPQFDkfGEGIIITTHDKLSHYL 882
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 ... |
1351-1666 |
8.99e-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: 83.76 E-value: 8.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1351 LLGAPTGSGKTVAAELAIFRVFNKYPTSK-----AVYIAPLKALVRErmddwkvrIEEKLGKKVIEL---------TGDV 1416
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKekglhTLYITPLRALAVD--------IARNLQAPIEELglpirvetrTGDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1417 TPDMKSIAKA---DLIVTTPEkwdgvsrSWQ-------NRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNFISSHt 1485
Cdd:TIGR04121 104 SSSERARQRKkppDILLTTPE-------SLAlllsypdAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1486 ekpVRIVGLSTALANARDLADWLnikqMGLFNFRPSV------RPVPLEV----HIQGFP-GQHYCPRMASmnkPAFQAI 1554
Cdd:TIGR04121 176 ---LRRWGLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISllpeSEERFPwAGHLGLRALP---EVYAEI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1555 RSHspaKPVLIFVSSRRQTRLTALELIAFLAteedpkqwlnmderemeniiatvrDSNLKltlafgIGMHHAGLHERDRK 1634
Cdd:TIGR04121 246 DQA---RTTLVFTNTRSQAELWFQALWEANP------------------------EFALP------IALHHGSLDREQRR 292
|
330 340 350
....*....|....*....|....*....|...
gi 767941789 1635 TVEELFVNCKVQVLIATSTLAWGVNF-PAHLVI 1666
Cdd:TIGR04121 293 WVEAAMAAGRLRAVVCTSSLDLGVDFgPVDLVI 325
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
498-875 |
1.01e-15 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 83.61 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 498 ENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGViKKNEFKIVYVAPMKALAAEMtdyfSRRLE-PL-------GIIVKEL 569
Cdd:COG1201 40 ESTLLIAPTGSGKTLAAFLPALDELARRPRPGE-LPDGLRVLYISPLKALANDI----ERNLRaPLeeigeaaGLPLPEI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 570 -----TGDMqlSKSEilRTQM-------LVTTPE---------KWdvvtRKSVGDvalsqiVRLLILDEVHLLHED-RGP 627
Cdd:COG1201 115 rvgvrTGDT--PASE--RQRQrrrpphiLITTPEslallltspDA----RELLRG------VRTVIVDEIHALAGSkRGV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 628 VLESIVARtLRQVeSTQSMIRIlGLSATLPNYLDVATFLhvnpyIGlfffDGRFRPV-----PLGQTF-LGIKCANKmqq 701
Cdd:COG1201 181 HLALSLER-LRAL-APRPLQRI-GLSATVGPLEEVARFL-----VG----YEDPRPVtivdaGAGKKPdLEVLVPVE--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 702 lnNMDEVC----------YENVLKQVKAGHQVMVFVHARNatvrtamslierakncghipfffptqghdyvLAEKQVQRs 771
Cdd:COG1201 246 --DLIERFpwaghlwphlYPRVLDLIEAHRTTLVFTNTRS-------------------------------QAERLFQR- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 772 rnkqVRELFPDGFS---IHHAGMLRQDRNLVENLFSNGHIKVLVCTATLA----WG-VNLpahaVIikgtQIYAAK---R 840
Cdd:COG1201 292 ----LNELNPEDALpiaAHHGSLSREQRLEVEEALKAGELRAVVATSSLElgidIGdVDL----VI----QVGSPKsvaR 359
|
410 420 430
....*....|....*....|....*....|....*
gi 767941789 841 GsfvdlgildvMQIFGRAGRpQFDKFGEGIIITTH 875
Cdd:COG1201 360 L----------LQRIGRAGH-RVGEVSKGRLVPTH 383
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
1349-1495 |
1.93e-15 |
|
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: 75.52 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDdwKVRIEEKLGKKVIELTGDVTP---DMKSIAK 1425
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKG-KKVLVLVPTKALALQTAE--RLRELFGPGIRVAVLVGGSSAeerEKNKLGD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767941789 1426 ADLIVTTPEKWDGVSRSwQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTnfissHTEKPVRIVGLS 1495
Cdd:cd00046 80 ADIIIATPDMLLNLLLR-EDRLFLKDLKLIIVDEAHaLLIDSRGALILDLAVRK-----AGLKNAQVILLS 144
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
459-863 |
2.35e-15 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 82.25 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 459 EEKPVYIQDLDEIGQlaFKGM-----KRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIrqhfqqgviKK 533
Cdd:COG1202 184 EVDTVPVDDLDLPPE--LKDLlegrgEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAGIKNA---------LE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 534 NEFKIVYVAPMKALAAEMTDYFSRRLEPlGIIVKELTGDMQLSKSE---ILRTQMLVTTPEKWDVVTR--KSVGDVALsq 608
Cdd:COG1202 253 GKGKMLFLVPLVALANQKYEDFKDRYGD-GLDVSIRVGASRIRDDGtrfDPNADIIVGTYEGIDHALRtgRDLGDIGT-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 609 ivrlLILDEVHLLHE-DRGPVLESIVARtLRQV-ESTQsmirILGLSATLPNYLDVATFLHVNpyigLFFFDGRfrPVPL 686
Cdd:COG1202 330 ----VVIDEVHMLEDpERGHRLDGLIAR-LKYYcPGAQ----WIYLSATVGNPEELAKKLGAK----LVEYEER--PVPL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 687 GQ--TFlgikcANKMQQLNNMDEVCYENVLKQVKAGH--QVMVFVHARnatvrtamslieraKNCghipfffptqghdYV 762
Cdd:COG1202 395 ERhlTF-----ADGREKIRIINKLVKREFDTKSSKGYrgQTIIFTNSR--------------RRC-------------HE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 763 LAEKqvqrsrnkqvrelFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIikgtqiyaakrgs 842
Cdd:COG1202 443 IARA-------------LGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVI------------- 496
|
410 420
....*....|....*....|....*...
gi 767941789 843 FVDL--GI--LDV---MQIFGRAGRPQF 863
Cdd:COG1202 497 FDSLamGIewLSVqefHQMLGRAGRPDY 524
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
493-861 |
5.89e-15 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 81.06 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 493 AYNTNENMLICAPTGAGKTNIAMLTVLheIRQHFQQGViKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVK-EL-T 570
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSL--IDLAGPEAP-KEKGLHTLYITPLRALAVDIARNLQAPIEELGLPIRvETrT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 571 GDMQLSKSEILRTQM---LVTTPEKWDVVTrkSVGDVA-LSQIVRLLILDEVH-LLHEDRGPVLESIVARtLRQvesTQS 645
Cdd:TIGR04121 101 GDTSSSERARQRKKPpdiLLTTPESLALLL--SYPDAArLFKDLRCVVVDEWHeLAGSKRGDQLELALAR-LRR---LAP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 646 MIRILGLSATLPNyLDVA--TFLHVNPYIGLFFFDGRFRPVPL-------GQTF-----LGIKCAnkmqqlnnmdevcyE 711
Cdd:TIGR04121 175 GLRRWGLSATIGN-LEEArrVLLGVGGAPAVLVRGKLPKAIEVisllpesEERFpwaghLGLRAL--------------P 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 712 NVLKQVKAGHQVMVFVHARNATVRTAMSLIErakncghipfffptqghdyvlaekqvqrsrnkqVRELFPDGFSIHHAGM 791
Cdd:TIGR04121 240 EVYAEIDQARTTLVFTNTRSQAELWFQALWE---------------------------------ANPEFALPIALHHGSL 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767941789 792 LRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIkgtQIYAAKrgsfvdlGILDVMQIFGRAG-RP 861
Cdd:TIGR04121 287 DREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSPK-------GVARLLQRAGRSNhRP 347
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1619-1698 |
1.13e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 71.09 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1619 FGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryVDFPITDVLQMMGRAGR 1697
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVII-----YD------LPWSPASYIQRIGRAGR 80
|
.
gi 767941789 1698 P 1698
Cdd:smart00490 81 A 81
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1294-1740 |
3.98e-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: 78.34 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1294 HLILPERHPPHTELLD-LQPLPITALGCKAYEALYnfSHfnpvQTQIFHtLYHTDCNVLLGAPTGSGKTVAAELAIFRVF 1372
Cdd:COG1205 24 VRTIPAREARYAPWPDwLPPELRAALKKRGIERLY--SH----QAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1373 NKYPTSKAVYIAPLKALVRERMDDWKvRIEEKLGK--KVIELTGDVTPDMKS--IAKADLIVTTP-----------EKWd 1437
Cdd:COG1205 97 LEDPGATALYLYPTKALARDQLRRLR-ELAEALGLgvRVATYDGDTPPEERRwiREHPDIVLTNPdmlhygllphhTRW- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1438 gvSRSWQNRNYVqqvtilIIDEIHLLgeeRGpvleV-------IVSRTNFISSHTEKPVRIVGLSTALANARDLAdwlni 1510
Cdd:COG1205 175 --ARFFRNLRYV------VIDEAHTY---RG----VfgshvanVLRRLRRICRHYGSDPQFILASATIGNPAEHA----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1511 kqMGLFNfRPsvrpvplevhiqgfpgqhycprmasmnkpaFQAI-RSHSPA--------KPVLIFVSSRRQTRLTALELI 1581
Cdd:COG1205 235 --ERLTG-RP------------------------------VTVVdEDGSPRgertfvlwNPPLVDDGIRRSALAEAARLL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1582 AFLAtEEDPKQWLNMDEREM-ENIIATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNF 1660
Cdd:COG1205 282 ADLV-REGLRTLVFTRSRRGaELLARYARRALREPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1661 PA-HLVIIKGteyydgktrryvdFP--ITDVLQMMGRAGRpqfDDQGKAVILV--HDIKKDFYKK---FLYEPfPVESSL 1732
Cdd:COG1205 361 GGlDAVVLAG-------------YPgtRASFWQQAGRAGR---RGQDSLVVLVagDDPLDQYYVRhpeELFER-PPEAAV 423
|
490
....*....|...
gi 767941789 1733 LG-----VLSDHL 1740
Cdd:COG1205 424 IDpdnpyVLAPHL 436
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
497-655 |
5.07e-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: 68.58 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 497 NENMLICAPTGAGKTNIAMLTVLHEIRqhfqqgvikKNEFKIVYVAPMKALAAEMTDYFsRRLEPLGIIVKELTGDM--- 573
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLL---------KKGKKVLVLVPTKALALQTAERL-RELFGPGIRVAVLVGGSsae 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 574 QLSKSEILRTQMLVTTPEKwdvVTRKSVGDVALSQI-VRLLILDEVH-LLHEDRGPVLESIVARTLRQVEStqsmiRILG 651
Cdd:cd00046 71 EREKNKLGDADIIIATPDM---LLNLLLREDRLFLKdLKLIIVDEAHaLLIDSRGALILDLAVRKAGLKNA-----QVIL 142
|
....
gi 767941789 652 LSAT 655
Cdd:cd00046 143 LSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
783-861 |
9.04e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 65.70 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 783 GFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIKGtqiyaakrgsfVDLGILDVMQIFGRAGRP 861
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASYIQRIGRAGRA 81
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
497-658 |
9.70e-13 |
|
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: 68.93 E-value: 9.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 497 NENMLICAPTGAGKTNI---AMLTVLHEirqhfqqgvikKNEFKIVYVAPMKAL----AAEMTDYFSRRLEPLGI-IVKE 568
Cdd:cd18025 16 RESALIVAPTSSGKTFIsyyCMEKVLRE-----------SDDGVVVYVAPTKALvnqvVAEVYARFSKKYPPSGKsLWGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 569 LTGDMQLskSEILRTQMLVTTPEKWDVVTRkSVGDVALSQIVRLLILDEVHLL-HEDRGPVLESIVArtlrqvestqsMI 647
Cdd:cd18025 85 FTRDYRH--NNPMNCQVLITVPECLEILLL-SPHNASWVPRIKYVIFDEIHSIgQSEDGAVWEQLLL-----------LI 150
|
170
....*....|...
gi 767941789 648 R--ILGLSATLPN 658
Cdd:cd18025 151 PcpFLALSATIGN 163
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
498-655 |
2.11e-12 |
|
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: 68.23 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 498 ENMLICAPTGAGKTNIAMLtvlheIRQHFQQGVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLSK 577
Cdd:cd17927 18 KNTIICLPTGSGKTFVAVL-----ICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 578 S---EILRTQMLVTTPEKWdVVTRKSVGDVALSqIVRLLILDEVHllHEDRGPVLESIVARTLRQ-VESTQSMIRILGLS 653
Cdd:cd17927 93 SveqIVESSDVIIVTPQIL-VNDLKSGTIVSLS-DFSLLVFDECH--NTTKNHPYNEIMFRYLDQkLGSSGPLPQILGLT 168
|
..
gi 767941789 654 AT 655
Cdd:cd17927 169 AS 170
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
497-824 |
7.35e-11 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 67.60 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 497 NENMLICAPTGAGKTNIAMLTVLHEIrqhFQQGVIKKNEFKI--VYVAPMKALAAEMtdyfsRR--LEPLGIIVKEL--- 569
Cdd:PRK13767 47 GKNVLISSPTGSGKTLAAFLAIIDEL---FRLGREGELEDKVycLYVSPLRALNNDI-----HRnlEEPLTEIREIAker 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 570 ------------TGDM-QLSKSEILRT--QMLVTTPEKWDVVT-----RKSVGDvalsqiVRLLILDEVHLLHED-RGPV 628
Cdd:PRK13767 119 geelpeirvairTGDTsSYEKQKMLKKppHILITTPESLAILLnspkfREKLRT------VKWVIVDEIHSLAENkRGVH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 629 LesivARTLRQVES--TQSMIRIlGLSATLPNYLDVATFLhvnpyiGLFFFDGRFRPVPLGQT-F---LGIKCANKMQQL 702
Cdd:PRK13767 193 L----SLSLERLEElaGGEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDCEIVDArFvkpFDIKVISPVDDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 703 -----NNMDEVCYENVLKQVKAGHQVMVFVHARNATVRTAMSLierakncghipfffptqghdyvlaekqvqrsrnkqvR 777
Cdd:PRK13767 262 ihtpaEEISEALYETLHELIKEHRTTLIFTNTRSGAERVLYNL------------------------------------R 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 767941789 778 ELFPDGFSI-----HHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP 824
Cdd:PRK13767 306 KRFPEEYDEdnigaHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG 357
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
1350-1508 |
9.33e-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: 63.62 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1350 VLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDwkvrIEEKLGKkVIELTGDVT--PDmksiakAD 1427
Cdd:cd18024 50 VLVSAHTSAGKTVVAEYAIAQSLRD--KQRVIYTSPIKALSNQKYRE----LQEEFGD-VGLMTGDVTinPN------AS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1428 LIVTTPEkwdgVSRS--WQNRNYVQQVTILIIDEIHLLGE-ERGPVLEvivsRTNFISSHTekpVRIVGLSTALANARDL 1504
Cdd:cd18024 117 CLVMTTE----ILRSmlYRGSEIMREVAWVIFDEIHYMRDkERGVVWE----ETIILLPDK---VRYVFLSATIPNARQF 185
|
....
gi 767941789 1505 ADWL 1508
Cdd:cd18024 186 AEWI 189
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
1338-1713 |
1.29e-10 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 66.59 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1338 QIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTskaVYIAPLKALVRermdDWKVRIEEKLGKkvIELTGDVT 1417
Cdd:COG1061 91 ALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV---LVLVPRRELLE----QWAEELRRFLGD--PLAGGGKK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1418 PDmksiaKADLIVTTpekWDGVSRSWQNRNYVQQVTILIIDEIHLLGeerGPVLEVIVSRTNfisshtekPVRIVGLS-T 1496
Cdd:COG1061 162 DS-----DAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHAG---APSYRRILEAFP--------AAYRLGLTaT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1497 AlanardladwlnikqmglfnFRPSVRPVPLEVhiqgFPGQHYcprmasmNKPAFQAIRSHSPAKPVLIfvssRRQTRLT 1576
Cdd:COG1061 223 P--------------------FRSDGREILLFL----FDGIVY-------EYSLKEAIEDGYLAPPEYY----GIRVDLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1577 AlELIAFLATEEDPKQWLNMDEREMENIIATVRDSNLKL--TLAFGIGMHHA-------------------GLHERDRKT 1635
Cdd:COG1061 268 D-ERAEYDALSERLREALAADAERKDKILRELLREHPDDrkTLVFCSSVDHAealaellneagiraavvtgDTPKKEREE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1636 VEELFVNCKVQVLIATSTLAWGVNFPA--HLVIIKGTeyydgKTRRYvdfpitdVLQMMGRAGRPqfdDQGKAVILVHDI 1713
Cdd:COG1061 347 ILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPT-----GSPRE-------FIQRLGRGLRP---APGKEDALVYDF 411
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1354-1696 |
2.21e-10 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 66.49 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1354 APTGSGKTVAAEL-AIFRVF----------NKYPTSKAVYIAPLKALVRERMDDWKVRIE------EKLGKKVIELT-GD 1415
Cdd:PRK09751 3 APTGSGKTLAAFLyALDRLFreggedtreaHKRKTSRILYISPIKALGTDVQRNLQIPLKgiaderRRRGETEVNLRvGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1416 VTPDMKSIAKA-------DLIVTTPEKWDGVSRSwQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNFIsSHTek 1487
Cdd:PRK09751 83 RTGDTPAQERSkltrnppDILITTPESLYLMLTS-RARETLRGVETVIIDEVHaVAGSKRGAHLALSLERLDAL-LHT-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1488 PVRIVGLSTALANARDLADWLNIKQMGLFNFRPSVR--------PVPLEVHIQGFPGQH----YCPRMASMnKPAFQA-- 1553
Cdd:PRK09751 159 SAQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRhpqirivvPVANMDDVSSVASGTgedsHAGREGSI-WPYIETgi 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1554 IRSHSPAKPVLIFVSSRRQT-RLTAL--ELIA--FLATEEDPKqwlnmDEREMENIIATV--RDSNLKLTLAFGigmHHA 1626
Cdd:PRK09751 238 LDEVLRHRSTIVFTNSRGLAeKLTARlnELYAarLQRSPSIAV-----DAAHFESTSGATsnRVQSSDVFIARS---HHG 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767941789 1627 GLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKgteyydgktrryVDFP--ITDVLQMMGRAG 1696
Cdd:PRK09751 310 SVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQ------------VATPlsVASGLQRIGRAG 369
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1350-1509 |
4.62e-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: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1350 VLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLGKKVIELTGDVTPD--MKSIAKAD 1427
Cdd:cd18025 19 ALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYPPSGKSLWGVFTRDyrHNNPMNCQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1428 LIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLG-EERGPVLEVIVsrtnfisshTEKPVRIVGLSTALANARDLAD 1506
Cdd:cd18025 99 VLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGqSEDGAVWEQLL---------LLIPCPFLALSATIGNPQKFHE 169
|
...
gi 767941789 1507 WLN 1509
Cdd:cd18025 170 WLQ 172
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1603-1697 |
4.62e-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: 58.76 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1603 NIIATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryV 1681
Cdd:pfam00271 23 QTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YD------L 91
|
90
....*....|....*.
gi 767941789 1682 DFPITDVLQMMGRAGR 1697
Cdd:pfam00271 92 PWNPASYIQRIGRAGR 107
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1333-1516 |
7.49e-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: 60.36 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1333 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIfrVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEklgkkVIEL 1412
Cdd:cd18027 10 DVFQKQAILHLEAGD-SVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGD-----VGLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1413 TGDVT--PDMKSiakadLIVTTPekwdgVSRS--WQNRNYVQQVTILIIDEIHLLGE-ERGPVLEVIVSrtnFISSHtek 1487
Cdd:cd18027 82 TGDVQlnPEASC-----LIMTTE-----ILRSmlYNGSDVIRDLEWVIFDEVHYINDaERGVVWEEVLI---MLPDH--- 145
|
170 180 190
....*....|....*....|....*....|
gi 767941789 1488 pVRIVGLSTALANARDLADWLN-IKQMGLF 1516
Cdd:cd18027 146 -VSIILLSATVPNTVEFADWIGrIKKKNIY 174
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1329-1495 |
1.30e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 63.75 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1329 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAI----FRVFNK-------YptskAVYIAPLKAL---VRERM 1394
Cdd:PRK13767 30 FGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREgeledkvY----CLYVSPLRALnndIHRNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1395 DDWKVRIEEKLGKKVIEL--------TGDVTPDMKS--------IakadLIvTTPEKWDGVSRSWQNRNYVQQVTILIID 1458
Cdd:PRK13767 105 EEPLTEIREIAKERGEELpeirvairTGDTSSYEKQkmlkkpphI----LI-TTPESLAILLNSPKFREKLRTVKWVIVD 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 767941789 1459 EIHLLGE-ERGPVLEVIVSRTNFISSHteKPVRIvGLS 1495
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 ... |
1349-1505 |
1.62e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 59.14 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVR---ERMDDWKVRIEEKLgkKVIELTGDvTP--DMKSI 1423
Cdd:cd17923 17 SVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQdqlRSLRELLEQLGLGI--RVATYDGD-TPreERRAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1424 AK--ADLIVTTP-----------EKWDGVSRSWQnrnYVqqvtilIIDEIH----LLGEERGPVLEVIVSRTNFISSHte 1486
Cdd:cd17923 94 IRnpPRILLTNPdmlhyallphhDRWARFLRNLR---YV------VLDEAHtyrgVFGSHVALLLRRLRRLCRRYGAD-- 162
|
170
....*....|....*....
gi 767941789 1487 kpVRIVGLSTALANARDLA 1505
Cdd:cd17923 163 --PQFILTSATIGNPAEHA 179
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
498-663 |
3.03e-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: 58.37 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 498 ENMLICAPTGAGKTNIAMLTVLHEIrqhfqqgvIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPL--GIIVKELTGDMQL 575
Cdd:cd17923 16 RSVVVTTGTASGKSLCYQLPILEAL--------LRDPGSRALYLYPTKALAQDQLRSLRELLEQLglGIRVATYDGDTPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 576 SKSEILRTQ---MLVTTPEKWDV-VTRKSVGDVALSQIVRLLILDEVHLLhedRGpVLESIVA----RTLRQVESTQSMI 647
Cdd:cd17923 88 EERRAIIRNpprILLTNPDMLHYaLLPHHDRWARFLRNLRYVVLDEAHTY---RG-VFGSHVAlllrRLRRLCRRYGADP 163
|
170
....*....|....*.
gi 767941789 648 RILGLSATLPNYLDVA 663
Cdd:cd17923 164 QFILTSATIGNPAEHA 179
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
486-654 |
3.18e-09 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 58.82 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 486 QSIVFETAynTNENMLICAPTGAGKTNIA-MLtvlheIRQ-HFQQGVIKKNEFKIVYVAPMKALAAEMTDYFsRRLEPLG 563
Cdd:cd18034 7 QLELFEAA--LKRNTIVVLPTGSGKTLIAvML-----IKEmGELNRKEKNPKKRAVFLVPTVPLVAQQAEAI-RSHTDLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 564 iiVKELTGDMQLS-------KSEILRTQMLVTTPEKW-DVVTRksvGDVALSQIvRLLILDEVHL---LHEDRGpvlesi 632
Cdd:cd18034 79 --VGEYSGEMGVDkwtkerwKEELEKYDVLVMTAQILlDALRH---GFLSLSDI-NLLIFDECHHatgDHPYAR------ 146
|
170 180
....*....|....*....|..
gi 767941789 633 VARTLRQVESTQSMIRILGLSA 654
Cdd:cd18034 147 IMKEFYHLEGRTSRPRILGLTA 168
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
457-865 |
3.84e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 58.50 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 457 SFEEKPVYIQDLDEiGQLAFKGMKRLNRIQSIVFETAYNT----NENMLICAPTGAGKTNIAMLTvlheIRQHFQQGvik 532
Cdd:COG1061 57 DTERELAEAEALEA-GDEASGTSFELRPYQQEALEALLAAlergGGRGLVVAPTGTGKTVLALAL----AAELLRGK--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 533 knefKIVYVAPMKAL----AAEMTDYFSRRLEPLGiiVKELTGDmqlskseilrtqMLVTTpekWDVVTRKSVGDvALSQ 608
Cdd:COG1061 129 ----RVLVLVPRRELleqwAEELRRFLGDPLAGGG--KKDSDAP------------ITVAT---YQSLARRAHLD-ELGD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 609 IVRLLILDEVHLLhedrgpvlesiVARTLRQVESTQSMIRILGLSATlPNYLDVATflhvnpyIGLFFFDG-RFRpVPLG 687
Cdd:COG1061 187 RFGLVIIDEAHHA-----------GAPSYRRILEAFPAAYRLGLTAT-PFRSDGRE-------ILLFLFDGiVYE-YSLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 688 Q----------TFLGIKcaNKMQQLNNMDEVCYENVLKQVKAGHQvmvfvharnATVRTAMSLIERAKNCGHIPFFFPTQ 757
Cdd:COG1061 247 EaiedgylappEYYGIR--VDLTDERAEYDALSERLREALAADAE---------RKDKILRELLREHPDDRKTLVFCSSV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 758 GHDYVLAEkqvqrsrnkqvrELFPDGFSIH--HAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIikgtqI 835
Cdd:COG1061 316 DHAEALAE------------LLNEAGIRAAvvTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVA-----I 378
|
410 420 430
....*....|....*....|....*....|
gi 767941789 836 YAAKRGSfvdLGILdvMQIFGRAGRPQFDK 865
Cdd:COG1061 379 LLRPTGS---PREF--IQRLGRGLRPAPGK 403
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
502-859 |
4.53e-08 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 58.78 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 502 ICAPTGAGKTNIAMltvLHEIRQHFQQGVI------KKNEFKIVYVAPMKALAAEMTDYFSRRLEPLG------------ 563
Cdd:PRK09751 1 VIAPTGSGKTLAAF---LYALDRLFREGGEdtreahKRKTSRILYISPIKALGTDVQRNLQIPLKGIAderrrrgetevn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 564 IIVKELTGDMQLS-KSEILRT--QMLVTTPEKWDVV----TRKSVGDVAlsqivrLLILDEVHLLH-EDRGPVLesivAR 635
Cdd:PRK09751 78 LRVGIRTGDTPAQeRSKLTRNppDILITTPESLYLMltsrARETLRGVE------TVIIDEVHAVAgSKRGAHL----AL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 636 TLRQVEST--QSMIRIlGLSATLPNYLDVATFLhvnpyiglfffdGRFRPV----PLGQTFLGIKCANKMQQLNNMDEVC 709
Cdd:PRK09751 148 SLERLDALlhTSAQRI-GLSATVRSASDVAAFL------------GGDRPVtvvnPPAMRHPQIRIVVPVANMDDVSSVA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 710 YE-------------------NVLKQVKAGHQVMVFVHARNATVRTAMSLIE--RAKNCGHIPFFFPTQGHDYVLA--EK 766
Cdd:PRK09751 215 SGtgedshagregsiwpyietGILDEVLRHRSTIVFTNSRGLAEKLTARLNElyAARLQRSPSIAVDAAHFESTSGatSN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 767 QVQRSRNKQVRElfpdgfsiHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIkgtQIYAAkrgsfvdL 846
Cdd:PRK09751 295 RVQSSDVFIARS--------HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVI---QVATP-------L 356
|
410
....*....|...
gi 767941789 847 GILDVMQIFGRAG 859
Cdd:PRK09751 357 SVASGLQRIGRAG 369
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
1349-1462 |
5.06e-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: 55.52 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKYP---TSKAVYIAPLKALVRERMDDWKvRIEEKLGKKVIELTGDVTPDM---KS 1422
Cdd:cd17927 19 NTIICLPTGSGKTFVAVLICEHHLKKFPagrKGKVVFLANKVPLVEQQKEVFR-KHFERPGYKVTGLSGDTSENVsveQI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767941789 1423 IAKADLIVTTP-------EKWDGVSRSwqnrnyvqQVTILIIDEIHL 1462
Cdd:cd17927 98 VESSDVIIVTPqilvndlKSGTIVSLS--------DFSLLVFDECHN 136
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1349-1461 |
1.06e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 53.44 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKvrieeKLGKKVIELTGDVTPDMKSIAK--A 1426
Cdd:pfam04851 25 RGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFK-----KFLPNYVEIGEIISGDKKDESVddN 99
|
90 100 110
....*....|....*....|....*....|....*
gi 767941789 1427 DLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIH 1461
Cdd:pfam04851 100 KIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
496-656 |
1.18e-07 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350831 [Multi-domain] Cd Length: 202 Bit Score: 54.44 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 496 TNENMLICAPTGAGKTNIAMLTVLHEIRQhFQQGviKKNefKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQL 575
Cdd:cd18073 16 KGKNTIICAPTGCGKTFVSLLICEHHLKK-FPQG--QKG--KVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGATAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 576 SKSE---ILRTQMLVTTPEKwdVVTRKSVGDVALSQIVRLLILDEVHllHEDRGPVLESIVARTLRQ--VESTQSMIRIL 650
Cdd:cd18073 91 NVPVeqiIENNDIIILTPQI--LVNNLKKGTIPSLSIFTLMIFDECH--NTSGNHPYNMIMFRYLDQklGGSSGPLPQII 166
|
....*.
gi 767941789 651 GLSATL 656
Cdd:cd18073 167 GLTASV 172
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
445-663 |
1.50e-07 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350782 [Multi-domain] Cd Length: 205 Bit Score: 53.99 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 445 EVRIPYS-EPMPLSFEEKPV-----YIQDLDEIGQLAFKGMKRlnriqsivfetayntNENMLICAPTGAGKTNIAMLTV 518
Cdd:cd18024 4 EVALPPDyDYTPISAHKPPGnpartYPFTLDPFQKTAIACIER---------------NESVLVSAHTSAGKTVVAEYAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 519 LHEIRqhfqqgvikkNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIvkelTGDMQLSKS--------EILRTqMLVTTP 590
Cdd:cd18024 69 AQSLR----------DKQRVIYTSPIKALSNQKYRELQEEFGDVGLM----TGDVTINPNasclvmttEILRS-MLYRGS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767941789 591 EkwdvVTRKsvgdvalsqiVRLLILDEVHLLHE-DRGPVLE-SIVArtlrqvesTQSMIRILGLSATLPNYLDVA 663
Cdd:cd18024 134 E----IMRE----------VAWVIFDEIHYMRDkERGVVWEeTIIL--------LPDKVRYVFLSATIPNARQFA 186
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
497-617 |
1.60e-07 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 53.75 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 497 NENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGvikknEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLS 576
Cdd:cd17957 27 GRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK-----GLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEAK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767941789 577 KSE----ILRTQMLVTTPEKwdVVTRKSVGDVALSQiVRLLILDE 617
Cdd:cd17957 102 AKDgpksITKYDILVSTPLR--LVFLLKQGPIDLSS-VEYLVLDE 143
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
1354-1480 |
2.26e-07 |
|
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: 52.31 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1354 APTGSGKTVAAELAIFRVFNKyptsKAVYIAPLKALVrermDDWKVRIEEKLGKKVI-ELTGDVTpdmKSIAKADLIVTT 1432
Cdd:cd17926 25 LPTGSGKTLTALALIAYLKEL----RTLIVVPTDALL----DQWKERFEDFLGDSSIgLIGGGKK---KDFDDANVVVAT 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767941789 1433 PEkwdgvSRSWQN---RNYVQQVTILIIDEIHLLGeerGPVLEVIVSRTNF 1480
Cdd:cd17926 94 YQ-----SLSNLAeeeKDLFDQFGLLIVDEAHHLP---AKTFSEILKELNA 136
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
498-657 |
2.35e-07 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 53.63 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 498 ENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGvikkNEFKIVYVAPMKALAAEMTDYFSRRLEPlGIIVKELTGDMQLSK 577
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAG----EKGRVVVLVNKVPLVEQQLEKFFKYFRK-GYKVTGLSGDSSHKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 578 S---EILRTQMLVTTPEKWDVVTRKSVGDVALS-QIVRLLILDEVHllHEDRGPVLESIVARTLRQ-VESTQSMIRILGL 652
Cdd:cd18036 93 SfgqIVKASDVIICTPQILINNLLSGREEERVYlSDFSLLIFDECH--HTQKEHPYNKIMRMYLDKkLSSQGPLPQILGL 170
|
....*
gi 767941789 653 SATLP 657
Cdd:cd18036 171 TASPG 175
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
497-619 |
4.70e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.12 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 497 NENMLICAPTGAGKTNIAMLTVLHeirqhfqqgVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLS 576
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE---------RLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767941789 577 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivrLLILDEVH 619
Cdd:COG1111 88 KRKELweKARIIVATPQviENDLIAgRIDLDDVS------LLIFDEAH 129
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
710-860 |
5.99e-07 |
|
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: 51.11 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 710 YENVLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNcghipfffptqghdyvlaekqvqrsrnkqvrELFPDGFSIHHA 789
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPD-------------------------------RVPPDFIALHHG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767941789 790 GMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPA-HAVIikgtQIYAAKrgsfvdlGILDVMQIFGRAGR 860
Cdd:cd18796 77 SLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDvDLVI----QIGSPK-------SVARLLQRLGRSGH 137
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
480-814 |
6.03e-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: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 480 KRLNRIQSIVFETAYNTNEN----MLICAPTGAGKTNIAMLTVLHEIRQHFQQGVIkknefkivYVAPMKAL----AAEM 551
Cdd:COG1203 126 TPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKHGGRRII--------YALPFTSIinqtYDRL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 552 TDYF--------SRRLEPLGIIVKELTGDMQLSK--SEILRTQMLVTTPekwD-----VVTRKSvgdvalSQIVRL---- 612
Cdd:COG1203 198 RDLFgedvllhhSLADLDLLEEEEEYESEARWLKllKELWDAPVVVTTI---DqlfesLFSNRK------GQERRLhnla 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 613 ---LILDEVHLL-HEDRGPVLesivaRTLRQVESTQSmiRILGLSATLPNYLDVATF------LHVNPYIGLFFFDGRFR 682
Cdd:COG1203 269 nsvIILDEVQAYpPYMLALLL-----RLLEWLKNLGG--SVILMTATLPPLLREELLeayeliPDEPEELPEYFRAFVRK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 683 PVplgqtflgikcanKMQQLNNMDEVCYENVLKQVKAGHQVMVFVharnATVRTAMSLierakncghipfffptqghdYv 762
Cdd:COG1203 342 RV-------------ELKEGPLSDEELAELILEALHKGKSVLVIV----NTVKDAQEL--------------------Y- 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 767941789 763 laekqvqrsrnKQVRELFPDGFSIH-HAGMLRQDRNLVEN----LFSNGHIKVLVCT 814
Cdd:COG1203 384 -----------EALKEKLPDEEVYLlHSRFCPADRSEIEKeikeRLERGKPCILVST 429
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1305-1523 |
6.35e-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: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1305 TELLDLQPLPITALGCKAYEALYNF-----SHFNPVQTQIFHTLYHTDCN----VLLGAPTGSGKTVAAELAIFRVFNKY 1375
Cdd:COG1203 96 SANFDMARQALDHLLAERLERLLPKkskprTPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKH 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1376 PTSKAVYIAPLKALVrERMDDwkvRIEEKLGKKVIELTGDVTPDMKSIAK-----------------ADLIVTTPEK-WD 1437
Cdd:COG1203 176 GGRRIIYALPFTSII-NQTYD---RLRDLFGEDVLLHHSLADLDLLEEEEeyesearwlkllkelwdAPVVVTTIDQlFE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1438 GV--SRSWQNRNYVQQVT-ILIIDEIHLLGEERGPVLEvivsrtNFISSHTEKPVRIVgLSTA---------LANARDLA 1505
Cdd:COG1203 252 SLfsNRKGQERRLHNLANsVIILDEVQAYPPYMLALLL------RLLEWLKNLGGSVI-LMTAtlppllreeLLEAYELI 324
|
250
....*....|....*...
gi 767941789 1506 DWLNIKQMGLFNFRPSVR 1523
Cdd:COG1203 325 PDEPEELPEYFRAFVRKR 342
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
1349-1475 |
6.70e-07 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 51.91 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVR---ERMDDW--KVRIEEKLGkkviELTGDVTPDM--K 1421
Cdd:cd17930 3 LVILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINqmyERIREIlgRLDDEDKVL----LLHSKAALELleS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1422 SIAKADLIVTTPEKWDGVSRSWqNRNYVqqVT-------------------------ILIIDEIHLLGEER-GPVLEVIV 1475
Cdd:cd17930 79 DEEPDDDPVEAVDWALLLKRSW-LAPIV--VTtidqllesllkykhferrlhglansVVVLDEVQAYDPEYmALLLKALL 155
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
501-749 |
1.28e-06 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 52.82 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 501 LICAPTGAGKTNIAMLTVLHEIRQhfqqgvikKNEFKIVYVAPMKALAAEMTDYFSRRL-EPLGIIVKELTGD--MQLSK 577
Cdd:cd09639 3 VIEAPTGYGKTEAALLWALHSLKS--------QKADRVIIALPTRATINAMYRRAKEAFgETGLYHSSILSSRikEMGDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 578 SEILR--------------TQMLVTTPEKWDVVTRKSVG--DVALSQIVR-LLILDEVHLLHEDrgpVLESIVA--RTLR 638
Cdd:cd09639 75 EEFEHlfplyihsndtlflDPITVCTIDQVLKSVFGEFGhyEFTLASIANsLLIFDEVHFYDEY---TLALILAvlEVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 639 QVEstqsmIRILGLSATLPNYLDvATFLHVNPYIGLFFFDGRFRpvplgQTFLGIKCANKMqqlnNMDEVCYENVLKQVK 718
Cdd:cd09639 152 DND-----VPILLMSATLPKFLK-EYAEKIGYVEENEPLDLKPN-----ERAPFIKIESDK----VGEISSLERLLEFIK 216
|
250 260 270
....*....|....*....|....*....|.
gi 767941789 719 AGHQVMVFVHarnaTVRTAMSLIERAKNCGH 749
Cdd:cd09639 217 KGGSVAIIVN----TVDRAQEFYQQLKEKGP 243
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
486-655 |
1.46e-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: 50.78 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 486 QSIVFETAYNtneNMLICAPTGAGKTNIAMLTVLHEIRQhFQQGvikknefKIVYVAPMKALAAEMTDYFsrrLEPLGI- 564
Cdd:cd18033 8 FTIVQKALFQ---NTLVALPTGLGKTFIAAVVMLNYYRW-FPKG-------KIVFMAPTKPLVSQQIEAC---YKITGIp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 565 --IVKELTGDMQLSK-SEILRT-QMLVTTPEKwdVVTRKSVGDVALSQIVrLLILDEVhllHEDRGPVLESIVARTLRQV 640
Cdd:cd18033 74 ssQTAELTGSVPPTKrAELWASkRVFFLTPQT--LENDLKEGDCDPKSIV-CLVIDEA---HRATGNYAYCQVVRELMRY 147
|
170
....*....|....*
gi 767941789 641 ESTqsmIRILGLSAT 655
Cdd:cd18033 148 NSH---FRILALTAT 159
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
1332-1461 |
1.52e-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: 50.78 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1332 FNPVQTQIFHtlyhtdcNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKvRIEEKLGKKVIE 1411
Cdd:cd18033 8 FTIVQKALFQ-------NTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACY-KITGIPSSQTAE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767941789 1412 LTGDVTPDMKSI--AKADLIVTTPEKWDGVSRSwqNRNYVQQVTILIIDEIH 1461
Cdd:cd18033 80 LTGSVPPTKRAElwASKRVFFLTPQTLENDLKE--GDCDPKSIVCLVIDEAH 129
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
784-860 |
1.94e-06 |
|
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: 48.36 E-value: 1.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767941789 784 FSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIkgtqiyaakrgSFVDLGILDVMQIFGRAGR 860
Cdd:pfam00271 41 VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----------YDLPWNPASYIQRIGRAGR 107
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
499-619 |
2.07e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 52.95 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 499 NMLICAPTGAGKTNIAMLTVLheirqhfqqGVIKKNEFKIVYVAPMKALAAEMTDYFSR--RLEPLGIIVkeLTGDMQLS 576
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIA---------ERLHKKGGKVLILAPTKPLVEQHAEFFRKflNIPEEKIVV--FTGEVSPE 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767941789 577 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivrLLILDEVH 619
Cdd:PRK13766 100 KRAELweKAKVIVATPQviENDLIAgRISLEDVS------LLIFDEAH 141
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
1349-1461 |
2.32e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 52.81 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKyPTSKAVYIAPLKALVRERMDDWKvRIEEKLGKKVIELTGDVTPD--MKSIAKA 1426
Cdd:COG1111 19 NTLVVLPTGLGKTAVALLVIAERLHK-KGGKVLFLAPTKPLVEQHAEFFK-EALNIPEDEIVVFTGEVSPEkrKELWEKA 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 767941789 1427 DLIVTTPE--KWDGVSrswqNRNYVQQVTILIIDEIH 1461
Cdd:COG1111 97 RIIVATPQviENDLIA----GRIDLDDVSLLIFDEAH 129
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
498-666 |
2.45e-06 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 49.96 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 498 ENMLICAPTGAGKTNIAMLTVlheirqhfqqGVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIvkelTGDMQLS- 576
Cdd:cd18027 24 DSVFVAAHTSAGKTVVAEYAI----------ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGLI----TGDVQLNp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 577 -------KSEILRTqMLVTTPEkwdvVTRKsvgdvalsqiVRLLILDEVHLLHE-DRGPVLESIVARTLRQVestqsmiR 648
Cdd:cd18027 90 easclimTTEILRS-MLYNGSD----VIRD----------LEWVIFDEVHYINDaERGVVWEEVLIMLPDHV-------S 147
|
170
....*....|....*...
gi 767941789 649 ILGLSATLPNYLDVATFL 666
Cdd:cd18027 148 IILLSATVPNTVEFADWI 165
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
498-661 |
3.03e-06 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 49.98 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 498 ENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGVIkknefkivYVAPMKALA----AEMTDYFSRRLEPLGII-------V 566
Cdd:cd17930 2 GLVILEAPTGSGKTEAALLWALKLAARGGKRRII--------YALPTRATInqmyERIREILGRLDDEDKVLllhskaaL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 567 KELTGDMQLSKSEILRTQMLVTTPEKWD---VVTrksVGDVAL-------SQIVRL-------LILDEVHLLhedrGPVL 629
Cdd:cd17930 74 ELLESDEEPDDDPVEAVDWALLLKRSWLapiVVT---TIDQLLesllkykHFERRLhglansvVVLDEVQAY----DPEY 146
|
170 180 190
....*....|....*....|....*....|..
gi 767941789 630 ESIVARTLRQVESTQSmIRILGLSATLPNYLD 661
Cdd:cd17930 147 MALLLKALLELLGELG-GPVVLMTATLPALLR 177
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
477-668 |
5.73e-06 |
|
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: 49.67 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 477 KGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGVIKKNEFKIVYVAPMKALAAEMTDYFS 556
Cdd:cd17948 8 QGITKPTTVQKQGIPSILR-GRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNAPRGLVITPSRELAEQIGSVAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 557 RRLEPLGIIVKELTGDMqlSKSEILRTQM-----LVTTPEK-WDVVTRksvGDVALSQiVRLLILDEVH-LLHEDRGPVL 629
Cdd:cd17948 87 SLTEGLGLKVKVITGGR--TKRQIRNPHFeevdiLVATPGAlSKLLTS---RIYSLEQ-LRHLVLDEADtLLDDSFNEKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767941789 630 ESIVART---LRQVESTQSMIR---ILGLSATLPNYL--------DVATFLHV 668
Cdd:cd17948 161 SHFLRRFplaSRRSENTDGLDPgtqLVLVSATMPSGVgevlskviDVDSIETV 213
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
1349-1501 |
6.35e-06 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 49.19 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRV-----FNKYPTSKAVYIAPLKALVRERMDdwkvRIEEKLGKKVIELTGDVTPDMKS- 1422
Cdd:cd18034 18 NTIVVLPTGSGKTLIAVMLIKEMgelnrKEKNPKKRAVFLVPTVPLVAQQAE----AIRSHTDLKVGEYSGEMGVDKWTk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1423 ------IAKADLIVTTPEkwdgVSRSWQNRNYVQ--QVTILIIDEIHLLGEERgpVLEVIVSRTNFISSHTEKPvRIVGL 1494
Cdd:cd18034 94 erwkeeLEKYDVLVMTAQ----ILLDALRHGFLSlsDINLLIFDECHHATGDH--PYARIMKEFYHLEGRTSRP-RILGL 166
|
....*..
gi 767941789 1495 STALANA 1501
Cdd:cd18034 167 TASPVNG 173
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
474-670 |
1.49e-05 |
|
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: 47.82 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 474 LAFKGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTnIA-MLTVLHEIRqhfQQGVIKKNEFKIVYVAPMKALAAEMT 552
Cdd:cd00268 5 LKKLGFEKPTPIQAQAIPLILS-GRDVIGQAQTGSGKT-LAfLLPILEKLL---PEPKKKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 553 DYFSRRLEPLGIIVKELTGDMQLSKSEIL---RTQMLVTTPEK-WDVVTRksvGDVALSQiVRLLILDEV-HLLHEDRGP 627
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEAlkkGPDIVVGTPGRlLDLIER---GKLDLSN-VKYLVLDEAdRMLDMGFEE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767941789 628 VLESIVARTLRQvesTQSMIrilgLSATLPNYLD--VATFLHvNP 670
Cdd:cd00268 156 DVEKILSALPKD---RQTLL----FSATLPEEVKelAKKFLK-NP 192
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
495-655 |
3.02e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.51 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 495 NTNENMLICAPTGAGKTniamLTVLHEIRQHFQQGVIKknefKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDmq 574
Cdd:pfam04851 21 NGQKRGLIVMATGSGKT----LTAAKLIARLFKKGPIK----KVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 575 lSKSEILRT-QMLVTTPEKWDVVTRKSVGDVALSQIVrLLILDEVHllhedRGPvlesivARTLRQVESTQSMIRILGLS 653
Cdd:pfam04851 91 -KKDESVDDnKIVVTTIQSLYKALELASLELLPDFFD-VIIIDEAH-----RSG------ASSYRNILEYFKPAFLLGLT 157
|
..
gi 767941789 654 AT 655
Cdd:pfam04851 158 AT 159
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
497-619 |
5.30e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 45.97 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 497 NENMLICAPTGAGKTNIAMLTVLheirqhfqqGVIKKNEFKIVYVAPMKALAAEMTDYFsRRLEPLGIIVKELTGDMQLS 576
Cdd:cd18035 16 NGNTLIVLPTGLGKTIIAILVAA---------DRLTKKGGKVLILAPSRPLVEQHAENL-KRVLNIPDKITSLTGEVKPE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767941789 577 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivrLLILDEVH 619
Cdd:cd18035 86 ERAERwdASKIIVATPQviENDLLAgRITLDDVS------LLIFDEAH 127
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
1349-1461 |
5.45e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 45.97 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKYpTSKAVYIAPLKALVRERMDDWKVRIEEKLgkKVIELTGDVTPDMKS--IAKA 1426
Cdd:cd18035 18 NTLIVLPTGLGKTIIAILVAADRLTKK-GGKVLILAPSRPLVEQHAENLKRVLNIPD--KITSLTGEVKPEERAerWDAS 94
|
90 100 110
....*....|....*....|....*....|....*
gi 767941789 1427 DLIVTTPEKWDgvSRSWQNRNYVQQVTILIIDEIH 1461
Cdd:cd18035 95 KIIVATPQVIE--NDLLAGRITLDDVSLLIFDEAH 127
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
1349-1461 |
1.24e-04 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 47.18 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDDWK--VRIEEklgKKVIELTGDVTPD--MKSIA 1424
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIAERLHKKG-GKVLILAPTKPLVEQHAEFFRkfLNIPE---EKIVVFTGEVSPEkrAELWE 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 767941789 1425 KADLIVTTPE--KWDGVSrswqNRNYVQQVTILIIDEIH 1461
Cdd:PRK13766 107 KAKVIVATPQviENDLIA----GRISLEDVSLLIFDEAH 141
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
1554-1697 |
2.04e-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: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1554 IRSHSPAKPVLIFVSSRRQTrltaleliaflateedpkqwlnmderemENIIATVRDSNLKLTLAFGIGMHHAGLHERDR 1633
Cdd:cd18796 32 IFLLERHKSTLVFTNTRSQA----------------------------ERLAQRLRELCPDRVPPDFIALHHGSLSRELR 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767941789 1634 KTVEELFVNCKVQVLIATSTLAWGVNFPA-HLVIIKGTEYydgktrryvdfPITDVLQMMGRAGR 1697
Cdd:cd18796 84 EEVEAALKRGDLKVVVATSSLELGIDIGDvDLVIQIGSPK-----------SVARLLQRLGRSGH 137
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
1329-1461 |
7.23e-04 |
|
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: 42.91 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1329 FSHFNPVQTQ-IFHTLYHTDCNVLLgaPTGSGKTVAAELAIFrVFNKyPTskaVYIAPLKALvrerMDDwKVRIEEKLGK 1407
Cdd:cd17920 10 YDEFRPGQLEaINAVLAGRDVLVVM--PTGGGKSLCYQLPAL-LLDG-VT---LVVSPLISL----MQD-QVDRLQQLGI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767941789 1408 KVIELTGDVTPDMKSIA-------KADLIVTTPEK--WDGVSRSWQNRNYVQQVTILIIDEIH 1461
Cdd:cd17920 78 RAAALNSTLSPEEKREVllrikngQYKLLYVTPERllSPDFLELLQRLPERKRLALIVVDEAH 140
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
478-657 |
1.29e-03 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 42.57 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 478 GMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTnIAML--TVLHEIRQHFQQgviKKNEFKIVYVAPMKALAAEMTDYF 555
Cdd:cd17964 13 GFETMTPVQQKTLKPILSTGDDVLARAKTGTGKT-LAFLlpAIQSLLNTKPAG---RRSGVSALIISPTRELALQIAAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 556 SRRLEPL-GIIVKELTGDMQLSKSEI----LRTQMLVTTPEKW-DVVTRKSVGDVALSqiVRLLILDEV-HLLheDRG-- 626
Cdd:cd17964 89 KKLLQGLrKLRVQSAVGGTSRRAELNrlrrGRPDILVATPGRLiDHLENPGVAKAFTD--LDYLVLDEAdRLL--DMGfr 164
|
170 180 190
....*....|....*....|....*....|.
gi 767941789 627 PVLESIVaRTLRQVESTQsmIRILGLSATLP 657
Cdd:cd17964 165 PDLEQIL-RHLPEKNADP--RQTLLFSATVP 192
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
491-656 |
1.33e-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: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 491 ETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFQqgvikknefKIVYVAPMKALAAEMTDYFSR-RLEPLGIIVK-E 568
Cdd:cd17990 11 RAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGG---------KIIVLEPRRVAARAAARRLATlLGEAPGETVGyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 569 LTGDMQLSKseilRTQMLVTTPekwDVVTRKSVGDVALSQiVRLLILDEVHllheDRGPVLESIVARTLRQVESTQSMIR 648
Cdd:cd17990 82 VRGESRVGR----RTRVEVVTE---GVLLRRLQRDPELSG-VGAVILDEFH----ERSLDADLALALLLEVQQLLRDDLR 149
|
....*...
gi 767941789 649 ILGLSATL 656
Cdd:cd17990 150 LLAMSATL 157
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
1349-1461 |
1.43e-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: 42.08 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1349 NVLLGAPTGSGKTVAAELAIFRVFNKYP----TSKAVYIAPLKALVRERMDDWKVRIEEklGKKVIELTGD--VTPDMKS 1422
Cdd:cd18036 19 NTIICAPTGSGKTRVAVYICRHHLEKRRsageKGRVVVLVNKVPLVEQQLEKFFKYFRK--GYKVTGLSGDssHKVSFGQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767941789 1423 IAKA-DLIVTTPEKWDGVSRS--WQNRNYVQQVTILIIDEIH 1461
Cdd:cd18036 97 IVKAsDVIICTPQILINNLLSgrEEERVYLSDFSLLIFDECH 138
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
493-656 |
1.90e-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: 40.75 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 493 AYNTNENMLICAPTGAGKTNIAMLtvlheirqhfqqgVIKKN-EFKIVYVAPMKALAAEMTDYFSRRLEPlgIIVKELTG 571
Cdd:cd17926 14 AHKNNRRGILVLPTGSGKTLTALA-------------LIAYLkELRTLIVVPTDALLDQWKERFEDFLGD--SSIGLIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 572 DmqlSKSEILRTQMLVTTPEK--WDVVTRKSVGDVALsqivrLLILDEVHllhedRGPvlesivARTLRQVESTQSMIRI 649
Cdd:cd17926 79 G---KKKDFDDANVVVATYQSlsNLAEEEKDLFDQFG-----LLIVDEAH-----HLP------AKTFSEILKELNAKYR 139
|
....*..
gi 767941789 650 LGLSATL 656
Cdd:cd17926 140 LGLTATP 146
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
1625-1697 |
1.97e-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: 1.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767941789 1625 HAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-----AHLVIIKGTE-YYdgktrryvdfpitdvlQMMGRAGR 1697
Cdd:cd18794 61 HAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPdvrfvIHYSLPKSMEsYY----------------QESGRAGR 123
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
1334-1459 |
2.10e-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: 41.42 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1334 PVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIF---RVFNKYPTSKAVYIAPLKAL----VRErmddwKVRIEEKLG 1406
Cdd:cd17957 15 PIQMQAIPILLHGR-DLLACAPTGSGKTLAFLIPILqklGKPRKKKGLRALILAPTRELasqiYRE-----LLKLSKGTG 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767941789 1407 KKVIELTGDVTP----DMKSIAKADLIVTTPE------KWDGVSRSWqnrnyvqqVTILIIDE 1459
Cdd:cd17957 89 LRIVLLSKSLEAkakdGPKSITKYDILVSTPLrlvfllKQGPIDLSS--------VEYLVLDE 143
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
1327-1486 |
2.77e-03 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 41.58 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1327 YNFSHFNPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAV-YIAPLkALV----RERMDdwKVR- 1400
Cdd:cd17948 8 QGITKPTTVQKQGIPSILRGR-NTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpFNAPR-GLVitpsRELAE--QIGs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1401 ----IEEKLGKKVIELTGDVTpdMKSI-----AKADLIVTTPekwDGVSRSWQNRNY-VQQVTILIIDEIH-LLGEERGP 1469
Cdd:cd17948 84 vaqsLTEGLGLKVKVITGGRT--KRQIrnphfEEVDILVATP---GALSKLLTSRIYsLEQLRHLVLDEADtLLDDSFNE 158
|
170
....*....|....*..
gi 767941789 1470 VLEVIVSRTNFISSHTE 1486
Cdd:cd17948 159 KLSHFLRRFPLASRRSE 175
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
486-620 |
6.13e-03 |
|
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; 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; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D
Pssm-ID: 187841 [Multi-domain] Cd Length: 353 Bit Score: 41.40 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 486 QSIVFETAYNTNEN-MLICAPTGAGKTNIAMLTVLHEirqhfqqgvikknEFKIVYVAPMKALA-------AEMTDYFSR 557
Cdd:cd09710 2 QVATFEALQSKDADiIFNTAPTGAGKTLAWLTPLLHG-------------ENKAIALYPTNALIedqteaiKEFVDDANP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 558 RLEPLGIIVKELT-----GDMQLSKSEIL-----------RTQMLVTTPEKWDVVTR-----KSVGDVALSQIVRLLILD 616
Cdd:cd09710 69 RHQVKSLSASDITlwpndKNVGSSKGEKLynllrndigtsTPIILLTNPDIFVYLTRfayidRGDIAAGFYTKFSTVIFD 148
|
....
gi 767941789 617 EVHL 620
Cdd:cd09710 149 EFHL 152
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
1647-1697 |
6.68e-03 |
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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: 6.68e-03
10 20 30 40 50
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gi 767941789 1647 VLIATSTLAWGVNFPAHLVIIKGTEYYDGKTRRyvDFPITDVLQMMGRAGR 1697
Cdd:cd18805 73 VLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMR--PLSPSEVKQIAGRAGR 121
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| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
1328-1433 |
9.31e-03 |
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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: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941789 1328 NFSHFNPVQTQIFHTLYHTD--------CNVLLGAPTGSGKTVAAELAIFRVFNKYPTSK--AVYIAPLKAL---VRERM 1394
Cdd:cd17956 9 GITSAFPVQAAVIPWLLPSSkstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRlrALIVVPTKELvqqVYKVF 88
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767941789 1395 DdwkvRIEEKLGKKVIELTG--DVTPDMKSIA---------KADLIVTTP 1433
Cdd:cd17956 89 E----SLCKGTGLKVVSLSGqkSFKKEQKLLLvdtsgrylsRVDILVATP 134
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