|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1326-1514 |
4.98e-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: 4.98e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1326 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLGKKVI 1405
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1406 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKPVR 1485
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*....
gi 158518649 1486 IVGLSTALANARDLADWLNIKQMGLFNFR 1514
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
476-673 |
1.13e-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: 1.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 476 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFQQ-GVIKKNEFKIVYVAPMKALAAEMTDYFSRRL 554
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 555 EPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDVALSQIVRLLILDEVHLLHEDRGPVLESIVARTLRQ 634
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 158518649 635 VESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFFFD 673
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
978-1286 |
2.57e-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: 2.57e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 978 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNfCELSTPGGVENSYGKI 1057
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEK-VPIPVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1058 NILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSILPPHI 1137
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1138 LTRLEEKKLTV--DKLKDMRKDEIGHILHHVNIGLKVKQCVHQIPSVMMEASIQPITRTVLRVTLSIYADFTWNDQVHGT 1215
Cdd:pfam02889 160 IKKLEKKGVESvrDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158518649 1216 VgEPWWIWVEDPTNDHIYHSEYFLALKKQVISkeAQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIIN 1286
Cdd:pfam02889 240 S-EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
975-1288 |
4.03e-113 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 362.35 E-value: 4.03e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 975 YFSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNFCELSTPGGVENSY 1054
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1055 GKINILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSILP 1134
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1135 PHILTRLEEKK-LTVDKLKDMRKDEIGHILHHVN-IGLKVKQCVHQIPSVMMEASIQPITRTVLRVTLSIYADFTWNDQV 1212
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLGLLDaEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158518649 1213 HGTVgEPWWIWVEDPTNDHIYHSEYFLALKKQVIskEAQLLVFTIPIFEPLPsQYYIRAVSDRWLGAEAVCIINFQ 1288
Cdd:smart00611 241 HGKQ-EGWWLVIGDSDGNELLHIERFSLNKKNVS--EEVKLDFTAPATEGNY-QYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1809-2178 |
3.92e-100 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 324.98 E-value: 3.92e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1809 SIEPLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPHSFDSPH 1888
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1889 TKAHLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWLKDSSLLTLPNIE 1968
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1969 NHHLHLFKKWKpimkgphargRTSIESLPELIHAcgGKDHVFSSMVeselhaAKTKQAWNFLSHLPVINVGISVKGSwDD 2048
Cdd:smart00611 161 EEILKRLEKKK----------VLSLEDLLELEDE--ERGELLGLLD------AEGERVYKVLSRLPKLNIEISLEPI-TR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 2049 LVEGHNELSVSTLTADKRDDnkwiklhadqeyvlqvslqrvhfgfhkgkpescavtprfpkSKDEGWFLILGEVDKRELI 2128
Cdd:smart00611 222 TVLGVEVTLTVDLTWDDEIH-----------------------------------------GKQEGWWLVIGDSDGNELL 260
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 158518649 2129 ALKRVGYIRNH--HVASLSFYTPEIPGRYIYTLYFMSDCYLGLDQQYDIYLN 2178
Cdd:smart00611 261 HIERFSLNKKNvsEEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1327-1849 |
1.04e-95 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 320.69 E-value: 1.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1327 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKVRIEEkLGKKVIE 1406
Cdd:COG1204 23 LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEE-LGIKVGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1407 LTGDVTPDMKSIAKADLIVTTPEKWDGVSRswQNRNYVQQVTILIIDEIHLLG-EERGPVLEVIVSRtnfiSSHTEKPVR 1485
Cdd:COG1204 100 STGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTLEVLLAR----LRRLNPEAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1486 IVGLSTALANARDLADWLNIKqmglfNFRPSVRPVPLE--VHIQG---FPGQHYCPRmasmnKPAFQAIRSHSPA-KPVL 1559
Cdd:COG1204 174 IVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSK-----DPTLALALDLLEEgGQVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1560 IFVSSRRQTRLTALELIAFLA---TEEDPKQWLNMDEREMEniIATVRDSNLKLT--LAFGIGMHHAGLHERDRKTVEEL 1634
Cdd:COG1204 244 VFVSSRRDAESLAKKLADELKrrlTPEEREELEELAEELLE--VSEETHTNEKLAdcLEKGVAFHHAGLPSELRRLVEDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1635 FVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGktrryVDFPITDVLQMMGRAGRPQFDDQGKAVILVHDIK---KD 1711
Cdd:COG1204 322 FREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDeadEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1712 FYKKFLYEPFPVESSLLGVLSD--HLNAEIAGGTITSKQDALDYITWTYFFRRlimnPSYYNLGDVshdsVNKFLSHLIE 1789
Cdd:COG1204 397 FERYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQ----YDKGDLEEV----VDDALEFLLE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158518649 1790 KSLIElelsycieigEDNRSIEPLTYGRIASYYYLKHQTVKMFKDRLK---PECSTEELLSIL 1849
Cdd:COG1204 469 NGFIE----------EDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadEEFTDLGLLHLI 521
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
460-1015 |
8.23e-94 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 315.30 E-value: 8.23e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 460 IQDLDE---IGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFqqgvikknefKIVYV 536
Cdd:COG1204 3 VAELPLekvIEFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 537 APMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGdvALSQIvRLLILDEVHLL 616
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDV-DLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 617 H-EDRGPVLESIVARtLRQVESTqsmIRILGLSATLPNYLDVATFLHVNPyiglffFDGRFRPVPLgqtFLGIKCANKmq 695
Cdd:COG1204 150 DdESRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGV-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 696 qlNNMDEVCYEN-------VLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNCGHIPFFFPTQGHDYVLAEKQVQRSRN 768
Cdd:COG1204 215 --LRFDDGSRRSkdptlalALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 769 KQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTqiyaaKRGSFVDLGILDVMQ 848
Cdd:COG1204 293 EKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-----KRGGMVPIPVLEFKQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 849 IFGRAGRPQFDKFGEGIIIT-THDKLSH--YLTLLTQRNPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWISYTYLY 923
Cdd:COG1204 368 MAGRAGRPGYDPYGEAILVAkSSDEADElfERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTFYA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 924 VRMRANPLaygishkayqidptlrkhrEQLVIEVGRKLDKAQMIrfEERTGYFSSTDLGRTASHYYIKYNTIETFNELFD 1003
Cdd:COG1204 448 YQYDKGDL-------------------EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAELVDGLR 506
|
570
....*....|..
gi 158518649 1004 AHKTEGDIFAIV 1015
Cdd:COG1204 507 KADEEFTDLGLL 518
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1812-2175 |
3.07e-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: 3.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1812 PLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPhSFDSPHTKA 1891
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKG-DIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1892 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWLKDSSLLTLPNIENHH 1971
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1972 LHLFKKwkpimkgphaRGRTSIESL-----PELIHACGGKDHVFssmveselhaaktKQAWNFLSHLPVINVgisvkgsw 2046
Cdd:pfam02889 160 IKKLEK----------KGVESVRDIlelddAEELGELIRNPKMG-------------KDIAQFVNRFPKIEI-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 2047 ddlveghnELSVSTLTADkrddnkwiklhadqeyVLQVSLQrvhfgfhkgkpescaVTPRFPKSKD-----EGWFLILGE 2121
Cdd:pfam02889 209 --------EAEVQPITRS----------------VLRVEVT---------------ITPDFPWDKRvhgksEGFWLVVGD 249
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 158518649 2122 VDKRELIALKRV--GYIRNHHVASLSFYTPEI-PGRYIYTLYFMSDCYLGLDQQYDI 2175
Cdd:pfam02889 250 SDGNEILHIERFtlTKRTLAGEHKLEFTVPPSdPGPPQLFVRLISDSWLGADQEVPI 306
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1518-1706 |
1.86e-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: 1.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1518 RPVPLEVHIQGFPGQHYCPRMASMNK-----PAFQAIRSHSPAKPVLIFVSSRRQTRLTALELIaflateedpkqwlnmd 1592
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1593 eremeniiatvrdsnlkltlafGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKT 1672
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 158518649 1673 RRYvdFPITDVLQMMGRAGRPQFDDQGKAVILVH 1706
Cdd:cd18795 123 YRE--LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1344-1872 |
7.41e-61 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 224.31 E-value: 7.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFrvfNKYPTS--KAVYIAPLKALVRER---MDDWkvrieEKLGKKVIELTGDVTPDMKSI 1418
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMV---NKLLREggKAVYLVPLKALAEEKyreFKDW-----EKLGLRVAMTTGDYDSTDEWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1419 AKADLIVTTPEKWDGVSR---SWqnrnyVQQVTILIIDEIHLLGE-ERGPVLEVIVSrtnfissHTEKPVRIVGLSTALA 1494
Cdd:PRK00254 113 GKYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSyDRGATLEMILT-------HMLGRAQILGLSATVG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1495 NARDLADWLNIKQMglfnfRPSVRPVPLE--VHIQGF------PGQHYcprMASMNKPAFQAIRShspAKPVLIFVSSRR 1566
Cdd:PRK00254 181 NAEELAEWLNAELV-----VSDWRPVKLRkgVFYQGFlfwedgKIERF---PNSWESLVYDAVKK---GKGALVFVNTRR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1567 QTRLTALELIAFLATEEDPKQwlnmdEREMENIIATVRD--SNLKLTLAF--GIGMHHAGLHERDRKTVEELFVNCKVQV 1642
Cdd:PRK00254 250 SAEKEALELAKKIKRFLTKPE-----LRALKELADSLEEnpTNEKLKKALrgGVAFHHAGLGRTERVLIEDAFREGLIKV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1643 LIATSTLAWGVNFPAHLVIIKGTEYYDGKTrrYVDFPITDVLQMMGRAGRPQFDDQGKAVILVH-DIKKDFYKKF----- 1716
Cdd:PRK00254 325 ITATPTLSAGINLPAFRVIIRDTKRYSNFG--WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERYifgkp 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1717 --LYEPFPVESSLLGvlsdHLNAEIAGGTITSKQDALDYITWTYFfrrlimnpsYYNLGDVSH--DSVNKFLSHLIEKSL 1792
Cdd:PRK00254 403 ekLFSMLSNESAFRS----QVLALITNFGVSNFKELVNFLERTFY---------AHQRKDLYSleEKAKEIVYFLLENEF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1793 IELELsycieigEDNrsIEPLTYGRIASYYYLKHQTVKMFKDRLkPECSTEE----LLSILSDAEEYTDLPVRHNEDHMN 1868
Cdd:PRK00254 470 IDIDL-------EDR--FIPLPLGIRTSQLYIDPLTAKKFKDAF-PKIEKNPnplgIFQLIASTPDMTPLNYSRKEMEDL 539
|
....
gi 158518649 1869 SELA 1872
Cdd:PRK00254 540 LDEA 543
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
493-1034 |
5.53e-53 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 200.43 E-value: 5.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 493 ENMLICAPTGAGKTNIAMLTVLHEIrqhFQQGvikkneFKIVYVAPMKALAAEMTDYFsRRLEPLGIIVKELTGDMQlSK 572
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKL---LREG------GKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYD-ST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 573 SEIL-RTQMLVTTPEKWDVVTRKSVgdvalSQI--VRLLILDEVHLL-HEDRGPVLESIVARTLRQVEstqsmirILGLS 648
Cdd:PRK00254 109 DEWLgKYDIIIATAEKFDSLLRHGS-----SWIkdVKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ-------ILGLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 649 ATLPNYLDVATFLHVNpyigLFFFDgrFRPVPL-----GQTFLGIKCANKMQQLNNMDEVCYEnvlkQVKAGHQVMVFVH 723
Cdd:PRK00254 177 ATVGNAEELAEWLNAE----LVVSD--WRPVKLrkgvfYQGFLFWEDGKIERFPNSWESLVYD----AVKKGKGALVFVN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 724 ARNATVRTAMSLIERAKNCghipFFFPTQGHDYVLAEKQVQRSRNKQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHI 803
Cdd:PRK00254 247 TRRSAEKEALELAKKIKRF----LTKPELRALKELADSLEENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 804 KVLVCTATLAWGVNLPAHAVIIKGTQIYAakRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDK----LSHYL-- 877
Cdd:PRK00254 323 KVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklMERYIfg 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 878 ------TLLTQRNPIESQFLesladnlnAEIALGTVTNVEEAVKWISYTYlYVRMRANPlaYGISHKAYQIDPTLrkhRE 951
Cdd:PRK00254 401 kpeklfSMLSNESAFRSQVL--------ALITNFGVSNFKELVNFLERTF-YAHQRKDL--YSLEEKAKEIVYFL---LE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 952 QLVIEvgrkldkaqmIRFEERtgyFSSTDLGRTASHYYIKYNTIETFNELFDahKTEGD-----IFAIVSKAEEFDQIKV 1026
Cdd:PRK00254 467 NEFID----------IDLEDR---FIPLPLGIRTSQLYIDPLTAKKFKDAFP--KIEKNpnplgIFQLIASTPDMTPLNY 531
|
....*...
gi 158518649 1027 REEEIEEL 1034
Cdd:PRK00254 532 SRKEMEDL 539
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
677-869 |
8.95e-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: 8.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 677 RPVPLGQTFLGIK----CANKMQQLNNMDEVCYENVLKQVKAGHQVMVFVHARNATVRTAMSLIerakncghipfffptq 752
Cdd:cd18795 1 RPVPLEEYVLGFNglgiKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 753 ghdyvlaekqvqrsrnkqvrelfpdGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYA 832
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 158518649 833 AKRgsFVDLGILDVMQIFGRAGRPQFDKFGEGIIITT 869
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
478-656 |
1.27e-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: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 478 NRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQhfqqgviKKNEFKIVYVAPMKALAAEMTDYFSRRLEPL 557
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK-------LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 558 GIIVKELTGDMQLSK--SEILRTQMLVTTPEKWDVVTRKSvgdVALSQiVRLLILDEVHLLHE-DRGPVLESIVARtlrq 634
Cdd:pfam00270 73 GLKVASLLGGDSRKEqlEKLKGPDILVGTPGRLLDLLQER---KLLKN-LKLLVLDEAHRLLDmGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|..
gi 158518649 635 vesTQSMIRILGLSATLPNYLD 656
Cdd:pfam00270 145 ---LPKKRQILLLSATLPRNLE 163
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1328-1499 |
1.78e-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: 125.05 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1328 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFN-KYPTSKAVYIAPLKALVRERMDDWKVRIeEKLGKKVIE 1406
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDkLDNGPQALVLAPTRELAEQIYEELKKLG-KGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1407 LTGDVTP--DMKSIAKADLIVTTPEKWDGVsrsWQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNfisshteKP 1483
Cdd:pfam00270 79 LLGGDSRkeQLEKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRRLP-------KK 148
|
170
....*....|....*..
gi 158518649 1484 VRIVGLS-TALANARDL 1499
Cdd:pfam00270 149 RQILLLSaTLPRNLEDL 165
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1329-1705 |
7.00e-26 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 116.53 E-value: 7.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1329 PVQT-QIFHTLYHTDcNVLLGAPTGSGKTVAAELA-IFRVFNKypTSKAVYIAPLKALVRERMDDWKVRIEEKLgkKVIE 1406
Cdd:COG1202 212 PVQSlAVENGLLEGK-DQLVVSATATGKTLIGELAgIKNALEG--KGKMLFLVPLVALANQKYEDFKDRYGDGL--DVSI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1407 LTGDV---TPDMKSIAKADLIVTTPEKWDGVSRSwqnRNYVQQVTILIIDEIHLLGE-ERGPVLEVIVSRTNFISSHTEk 1482
Cdd:COG1202 287 RVGASrirDDGTRFDPNADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEVHMLEDpERGHRLDGLIARLKYYCPGAQ- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1483 pvrIVGLSTALANARDLADWLNIKQMgLFNfrpsVRPVPLEVHIQGFPGQHYCPRMASMNKPAFQAIRSHSPAKPVLIFV 1562
Cdd:COG1202 363 ---WIYLSATVGNPEELAKKLGAKLV-EYE----ERPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1563 SSRRQTRltaleliaflateedpkqwlnmderemeniiatvrdsnlKLTLAFGIGM--HHAGLHERDRKTVEELFVNCKV 1640
Cdd:COG1202 435 NSRRRCH---------------------------------------EIARALGYKAapYHAGLDYGERKKVERRFADQEL 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158518649 1641 QVLIATSTLAWGVNFPAHLVIIK----GTEYydgktrryvdFPITDVLQMMGRAGRPQFDDQGKAVILV 1705
Cdd:COG1202 476 AAVVTTAALAAGVDFPASQVIFDslamGIEW----------LSVQEFHQMLGRAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
469-680 |
9.65e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.81 E-value: 9.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 469 LAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRqhfqqgviKKNEFKIVYVAPMKALAAEMTD 548
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALK--------RGKGGRVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 549 YFSRRLEPLGIIVKELTGD----MQLSKSEILRTQMLVTTPEKWDVVTRKsvGDVALSQiVRLLILDEVH-LLHEDRGPV 623
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRLLDLLEN--DKLSLSN-VDLVILDEAHrLLDGGFGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 158518649 624 LESIVARTLRqvestqsMIRILGLSATLPNYLDVATFLHVNpyiGLFFFDGRFRPVP 680
Cdd:smart00487 150 LEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1322-1521 |
1.17e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 103.73 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1322 YNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLG 1401
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1402 KKVIELTGDVT-PDMKSIAK--ADLIVTTPEKWDGVSRswQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNfis 1477
Cdd:smart00487 84 KVVGLYGGDSKrEQLRKLESgkTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 158518649 1478 shteKPVRIVGLS-TALANARDLADWLNIkqmGLFNFRPSVRPVP 1521
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 ... |
1346-1661 |
8.96e-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: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1346 LLGAPTGSGKTVAAELAIFRVFNKYPTSK-----AVYIAPLKALVRErmddwkvrIEEKLGKKVIEL---------TGDV 1411
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKekglhTLYITPLRALAVD--------IARNLQAPIEELglpirvetrTGDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1412 TPDMKSIAKA---DLIVTTPEkwdgvsrSWQ-------NRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNFISSHt 1480
Cdd:TIGR04121 104 SSSERARQRKkppDILLTTPE-------SLAlllsypdAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1481 ekpVRIVGLSTALANARDLADWLnikqMGLFNFRPSV------RPVPLEV----HIQGFP-GQHYCPRMASmnkPAFQAI 1549
Cdd:TIGR04121 176 ---LRRWGLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISllpeSEERFPwAGHLGLRALP---EVYAEI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1550 RSHspaKPVLIFVSSRRQTRLTALELIAFLAteedpkqwlnmderemeniiatvrDSNLKltlafgIGMHHAGLHERDRK 1629
Cdd:TIGR04121 246 DQA---RTTLVFTNTRSQAELWFQALWEANP------------------------EFALP------IALHHGSLDREQRR 292
|
330 340 350
....*....|....*....|....*....|...
gi 158518649 1630 TVEELFVNCKVQVLIATSTLAWGVNF-PAHLVI 1661
Cdd:TIGR04121 293 WVEAAMAAGRLRAVVCTSSLDLGVDFgPVDLVI 325
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
488-856 |
5.73e-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: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 488 AYNTNENMLICAPTGAGKTNIAMLTVLheIRQHFQQGViKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVK-EL-T 565
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSL--IDLAGPEAP-KEKGLHTLYITPLRALAVDIARNLQAPIEELGLPIRvETrT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 566 GDMQLSKSEILRTQM---LVTTPEKWDVVTrkSVGDVA-LSQIVRLLILDEVH-LLHEDRGPVLESIVARtLRQvesTQS 640
Cdd:TIGR04121 101 GDTSSSERARQRKKPpdiLLTTPESLALLL--SYPDAArLFKDLRCVVVDEWHeLAGSKRGDQLELALAR-LRR---LAP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 641 MIRILGLSATLPNyLDVA--TFLHVNPYIGLFFFDGRFRPVPL-------GQTF-----LGIKCAnkmqqlnnmdevcyE 706
Cdd:TIGR04121 175 GLRRWGLSATIGN-LEEArrVLLGVGGAPAVLVRGKLPKAIEVisllpesEERFpwaghLGLRAL--------------P 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 707 NVLKQVKAGHQVMVFVHARNATVRTAMSLIErakncghipfffptqghdyvlaekqvqrsrnkqVRELFPDGFSIHHAGM 786
Cdd:TIGR04121 240 EVYAEIDQARTTLVFTNTRSQAELWFQALWE---------------------------------ANPEFALPIALHHGSL 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158518649 787 LRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIkgtQIYAAKrgsfvdlGILDVMQIFGRAG-RP 856
Cdd:TIGR04121 287 DREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSPK-------GVARLLQRAGRSNhRP 347
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1614-1693 |
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 158518649 1614 FGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryVDFPITDVLQMMGRAGR 1692
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVII-----YD------LPWSPASYIQRIGRAGR 80
|
.
gi 158518649 1693 P 1693
Cdd:smart00490 81 A 81
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
778-856 |
9.01e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 65.70 E-value: 9.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 778 GFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIKGtqiyaakrgsfVDLGILDVMQIFGRAGRP 856
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASYIQRIGRAGRA 81
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
492-819 |
6.90e-11 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 67.99 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 492 NENMLICAPTGAGKTNIAMLTVLHEIrqhFQQGVIKKNEFKI--VYVAPMKALAAEMtdyfsRR--LEPLGIIVKEL--- 564
Cdd:PRK13767 47 GKNVLISSPTGSGKTLAAFLAIIDEL---FRLGREGELEDKVycLYVSPLRALNNDI-----HRnlEEPLTEIREIAker 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 565 ------------TGDM-QLSKSEILRT--QMLVTTPEKWDVVT-----RKSVGDvalsqiVRLLILDEVHLLHED-RGPV 623
Cdd:PRK13767 119 geelpeirvairTGDTsSYEKQKMLKKppHILITTPESLAILLnspkfREKLRT------VKWVIVDEIHSLAENkRGVH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 624 LesivARTLRQVES--TQSMIRIlGLSATLPNYLDVATFLhvnpyiGLFFFDGRFRPVPLGQT-F---LGIKCANKMQQL 697
Cdd:PRK13767 193 L----SLSLERLEElaGGEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDCEIVDArFvkpFDIKVISPVDDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 698 -----NNMDEVCYENVLKQVKAGHQVMVFVHARNATVRTAMSLierakncghipfffptqghdyvlaekqvqrsrnkqvR 772
Cdd:PRK13767 262 ihtpaEEISEALYETLHELIKEHRTTLIFTNTRSGAERVLYNL------------------------------------R 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 158518649 773 ELFPDGFSI-----HHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP 819
Cdd:PRK13767 306 KRFPEEYDEdnigaHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG 357
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1598-1692 |
4.57e-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: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1598 NIIATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryV 1676
Cdd:pfam00271 23 QTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YD------L 91
|
90
....*....|....*.
gi 158518649 1677 DFPITDVLQMMGRAGR 1692
Cdd:pfam00271 92 PWNPASYIQRIGRAGR 107
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1324-1490 |
1.24e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 63.75 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1324 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAI----FRVFNK-------YptskAVYIAPLKAL---VRERM 1389
Cdd:PRK13767 30 FGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREgeledkvY----CLYVSPLRALnndIHRNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1390 DDWKVRIEEKLGKKVIEL--------TGDVTPDMKS--------IakadLIvTTPEKWDGVSRSWQNRNYVQQVTILIID 1453
Cdd:PRK13767 105 EEPLTEIREIAKERGEELpeirvairTGDTSSYEKQkmlkkpphI----LI-TTPESLAILLNSPKFREKLRTVKWVIVD 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 158518649 1454 EIHLLGE-ERGPVLEVIVSRTNFISSHteKPVRIvGLS 1490
Cdd:PRK13767 180 EIHSLAEnKRGVHLSLSLERLEELAGG--EFVRI-GLS 214
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
492-614 |
4.61e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.12 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 492 NENMLICAPTGAGKTNIAMLTVLHeirqhfqqgVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLS 571
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE---------RLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 158518649 572 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivrLLILDEVH 614
Cdd:COG1111 88 KRKELweKARIIVATPQviENDLIAgRIDLDDVS------LLIFDEAH 129
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
779-855 |
1.91e-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: 1.91e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158518649 779 FSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIkgtqiyaakrgSFVDLGILDVMQIFGRAGR 855
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; ... |
1326-1514 |
4.98e-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: 4.98e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1326 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLGKKVI 1405
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1406 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKPVR 1485
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*....
gi 158518649 1486 IVGLSTALANARDLADWLNIKQMGLFNFR 1514
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
476-673 |
1.13e-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: 1.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 476 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFQQ-GVIKKNEFKIVYVAPMKALAAEMTDYFSRRL 554
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 555 EPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDVALSQIVRLLILDEVHLLHEDRGPVLESIVARTLRQ 634
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 158518649 635 VESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFFFD 673
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
978-1286 |
2.57e-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: 2.57e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 978 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNfCELSTPGGVENSYGKI 1057
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEK-VPIPVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1058 NILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSILPPHI 1137
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1138 LTRLEEKKLTV--DKLKDMRKDEIGHILHHVNIGLKVKQCVHQIPSVMMEASIQPITRTVLRVTLSIYADFTWNDQVHGT 1215
Cdd:pfam02889 160 IKKLEKKGVESvrDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158518649 1216 VgEPWWIWVEDPTNDHIYHSEYFLALKKQVISkeAQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIIN 1286
Cdd:pfam02889 240 S-EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
975-1288 |
4.03e-113 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 362.35 E-value: 4.03e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 975 YFSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNFCELSTPGGVENSY 1054
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1055 GKINILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSILP 1134
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1135 PHILTRLEEKK-LTVDKLKDMRKDEIGHILHHVN-IGLKVKQCVHQIPSVMMEASIQPITRTVLRVTLSIYADFTWNDQV 1212
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLGLLDaEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158518649 1213 HGTVgEPWWIWVEDPTNDHIYHSEYFLALKKQVIskEAQLLVFTIPIFEPLPsQYYIRAVSDRWLGAEAVCIINFQ 1288
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 ... |
460-673 |
2.89e-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: 2.89e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 460 IQDLDEIGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHF-QQGVIKKNEFKIVYVAP 538
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRnPDGTINLDAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 539 MKALAAEMTDYFSRRLEPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSvGDVALSQIVRLLILDEVHLLHE 618
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKS-GDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 158518649 619 DRGPVLESIVARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFFFD 673
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1809-2178 |
3.92e-100 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 324.98 E-value: 3.92e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1809 SIEPLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPHSFDSPH 1888
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1889 TKAHLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWLKDSSLLTLPNIE 1968
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1969 NHHLHLFKKWKpimkgphargRTSIESLPELIHAcgGKDHVFSSMVeselhaAKTKQAWNFLSHLPVINVGISVKGSwDD 2048
Cdd:smart00611 161 EEILKRLEKKK----------VLSLEDLLELEDE--ERGELLGLLD------AEGERVYKVLSRLPKLNIEISLEPI-TR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 2049 LVEGHNELSVSTLTADKRDDnkwiklhadqeyvlqvslqrvhfgfhkgkpescavtprfpkSKDEGWFLILGEVDKRELI 2128
Cdd:smart00611 222 TVLGVEVTLTVDLTWDDEIH-----------------------------------------GKQEGWWLVIGDSDGNELL 260
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 158518649 2129 ALKRVGYIRNH--HVASLSFYTPEIPGRYIYTLYFMSDCYLGLDQQYDIYLN 2178
Cdd:smart00611 261 HIERFSLNKKNvsEEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1327-1849 |
1.04e-95 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 320.69 E-value: 1.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1327 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKVRIEEkLGKKVIE 1406
Cdd:COG1204 23 LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEE-LGIKVGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1407 LTGDVTPDMKSIAKADLIVTTPEKWDGVSRswQNRNYVQQVTILIIDEIHLLG-EERGPVLEVIVSRtnfiSSHTEKPVR 1485
Cdd:COG1204 100 STGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTLEVLLAR----LRRLNPEAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1486 IVGLSTALANARDLADWLNIKqmglfNFRPSVRPVPLE--VHIQG---FPGQHYCPRmasmnKPAFQAIRSHSPA-KPVL 1559
Cdd:COG1204 174 IVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSK-----DPTLALALDLLEEgGQVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1560 IFVSSRRQTRLTALELIAFLA---TEEDPKQWLNMDEREMEniIATVRDSNLKLT--LAFGIGMHHAGLHERDRKTVEEL 1634
Cdd:COG1204 244 VFVSSRRDAESLAKKLADELKrrlTPEEREELEELAEELLE--VSEETHTNEKLAdcLEKGVAFHHAGLPSELRRLVEDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1635 FVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGktrryVDFPITDVLQMMGRAGRPQFDDQGKAVILVHDIK---KD 1711
Cdd:COG1204 322 FREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDeadEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1712 FYKKFLYEPFPVESSLLGVLSD--HLNAEIAGGTITSKQDALDYITWTYFFRRlimnPSYYNLGDVshdsVNKFLSHLIE 1789
Cdd:COG1204 397 FERYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQ----YDKGDLEEV----VDDALEFLLE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158518649 1790 KSLIElelsycieigEDNRSIEPLTYGRIASYYYLKHQTVKMFKDRLK---PECSTEELLSIL 1849
Cdd:COG1204 469 NGFIE----------EDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadEEFTDLGLLHLI 521
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
460-1015 |
8.23e-94 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 315.30 E-value: 8.23e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 460 IQDLDE---IGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFqqgvikknefKIVYV 536
Cdd:COG1204 3 VAELPLekvIEFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 537 APMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGdvALSQIvRLLILDEVHLL 616
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDV-DLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 617 H-EDRGPVLESIVARtLRQVESTqsmIRILGLSATLPNYLDVATFLHVNPyiglffFDGRFRPVPLgqtFLGIKCANKmq 695
Cdd:COG1204 150 DdESRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGV-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 696 qlNNMDEVCYEN-------VLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNCGHIPFFFPTQGHDYVLAEKQVQRSRN 768
Cdd:COG1204 215 --LRFDDGSRRSkdptlalALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 769 KQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTqiyaaKRGSFVDLGILDVMQ 848
Cdd:COG1204 293 EKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-----KRGGMVPIPVLEFKQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 849 IFGRAGRPQFDKFGEGIIIT-THDKLSH--YLTLLTQRNPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWISYTYLY 923
Cdd:COG1204 368 MAGRAGRPGYDPYGEAILVAkSSDEADElfERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTFYA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 924 VRMRANPLaygishkayqidptlrkhrEQLVIEVGRKLDKAQMIrfEERTGYFSSTDLGRTASHYYIKYNTIETFNELFD 1003
Cdd:COG1204 448 YQYDKGDL-------------------EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAELVDGLR 506
|
570
....*....|..
gi 158518649 1004 AHKTEGDIFAIV 1015
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 ... |
978-1287 |
9.56e-94 |
|
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl domain) protein in which it was found. This protein is required for assembly of functional endoplasmic reticulum translocons. Other yeast proteins containing this domain include pre-mRNA splicing helicase BRR2, HFM1 protein and putative helicases.
Pssm-ID: 214946 Cd Length: 314 Bit Score: 306.59 E-value: 9.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 978 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNfCELSTPGGVENS-YGK 1056
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-VPIPVKEGIIDSpHAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1057 INILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLW-GWASPLRQF-SILP 1134
Cdd:smart00973 80 VNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWeDSDSPLKQLpHFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1135 PHILTRLEEKKL--TVDKLKDMRKDEIGHILH-HVNIGLKVKQCVHQIPSVMMEASIQPITRTV-LRVTLSIYADFTWND 1210
Cdd:smart00973 160 EDVYDKLELKDGsrSFELLLDMNAAELGEFLNrLPPNGRLIYELLRRFPKIEVEAEVLPITRDLtLRVELEITPVFAWDL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158518649 1211 QVHGTVGEPWWIWVEDPTNDHIYHSEYFLALKKQVISKeaQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIINF 1287
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 ... |
1324-1514 |
9.23e-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: 9.23e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1324 FSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLGKK 1403
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPLLGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1404 VIELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKP 1483
Cdd:cd18021 81 VVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 158518649 1484 VRIVGLSTALANARDLADWLNIKQMGLFNFR 1514
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 ... |
1812-2177 |
5.76e-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: 5.76e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1812 PLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPHSFDSPHTKA 1891
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1892 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWL-KDSSLLTLPNIEnh 1970
Cdd:smart00973 81 NLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEdSDSPLKQLPHFL-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1971 hlhlfkkwkpimkgphargrtsiesLPELIHACGGKDHVFSSMVESELHAAKTKQAWNFLSHLPVINVGISVKGSWDDLv 2050
Cdd:smart00973 159 -------------------------IEDVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEV- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 2051 eghnELSVSTLTADkrddnKWIKLHADQEYVLQVSLQRvhfgfhkgkpescavtprfPKSKDEGWFLILGEVDKRELIAL 2130
Cdd:smart00973 213 ----EAEVLPITRD-----LTLRVELEITPVFAWDLPR-------------------HKGKSESWWLVVGDSDTNELLAI 264
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 158518649 2131 KRV----GYIRNHHVASLSFYTPEiPGRYIYTLYFMSDCYLGLDQQYDIYL 2177
Cdd:smart00973 265 KRVtlrkKKKSNEVKLDFTVPLSE-PGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1812-2175 |
3.07e-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: 3.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1812 PLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPhSFDSPHTKA 1891
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKG-DIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1892 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWLKDSSLLTLPNIENHH 1971
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1972 LHLFKKwkpimkgphaRGRTSIESL-----PELIHACGGKDHVFssmveselhaaktKQAWNFLSHLPVINVgisvkgsw 2046
Cdd:pfam02889 160 IKKLEK----------KGVESVRDIlelddAEELGELIRNPKMG-------------KDIAQFVNRFPKIEI-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 2047 ddlveghnELSVSTLTADkrddnkwiklhadqeyVLQVSLQrvhfgfhkgkpescaVTPRFPKSKD-----EGWFLILGE 2121
Cdd:pfam02889 209 --------EAEVQPITRS----------------VLRVEVT---------------ITPDFPWDKRvhgksEGFWLVVGD 249
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 158518649 2122 VDKRELIALKRV--GYIRNHHVASLSFYTPEI-PGRYIYTLYFMSDCYLGLDQQYDI 2175
Cdd:pfam02889 250 SDGNEILHIERFtlTKRTLAGEHKLEFTVPPSdPGPPQLFVRLISDSWLGADQEVPI 306
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
1326-1514 |
1.55e-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: 1.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1326 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDDWKVRIEEkLGKKVI 1405
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSG-GKAVYIAPTRALVNQKEADLRERFGP-LGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1406 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRnYVQQVTILIIDEIHLLG-EERGPVLEVIVSRTNFIsshtEKPV 1484
Cdd:cd17921 79 LLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI----NKNA 153
|
170 180 190
....*....|....*....|....*....|
gi 158518649 1485 RIVGLSTALANARDLADWLNIKqmGLFNFR 1514
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 ... |
1518-1706 |
1.86e-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: 1.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1518 RPVPLEVHIQGFPGQHYCPRMASMNK-----PAFQAIRSHSPAKPVLIFVSSRRQTRLTALELIaflateedpkqwlnmd 1592
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1593 eremeniiatvrdsnlkltlafGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKT 1672
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 158518649 1673 RRYvdFPITDVLQMMGRAGRPQFDDQGKAVILVH 1706
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 ... |
1327-1519 |
4.18e-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: 4.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1327 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTS-----KAVYIAPLKALVRERMDDWKVRIeEKLG 1401
Cdd:cd18023 2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLpwgnrKVVYIAPIKALCSEKYDDWKEKF-GPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1402 KKVIELTGD-VTPDMKSIAKADLIVTTPEKWDGVSRSW-QNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFISSH 1479
Cdd:cd18023 81 LSCAELTGDtEMDDTFEIQDADIILTTPEKWDSMTRRWrDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSSS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 158518649 1480 TEK------PVRIVGLSTALANARDLADWLNIKQMGLFNFRPSVRP 1519
Cdd:cd18023 161 SELrgstvrPMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1344-1872 |
7.41e-61 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 224.31 E-value: 7.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFrvfNKYPTS--KAVYIAPLKALVRER---MDDWkvrieEKLGKKVIELTGDVTPDMKSI 1418
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMV---NKLLREggKAVYLVPLKALAEEKyreFKDW-----EKLGLRVAMTTGDYDSTDEWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1419 AKADLIVTTPEKWDGVSR---SWqnrnyVQQVTILIIDEIHLLGE-ERGPVLEVIVSrtnfissHTEKPVRIVGLSTALA 1494
Cdd:PRK00254 113 GKYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSyDRGATLEMILT-------HMLGRAQILGLSATVG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1495 NARDLADWLNIKQMglfnfRPSVRPVPLE--VHIQGF------PGQHYcprMASMNKPAFQAIRShspAKPVLIFVSSRR 1566
Cdd:PRK00254 181 NAEELAEWLNAELV-----VSDWRPVKLRkgVFYQGFlfwedgKIERF---PNSWESLVYDAVKK---GKGALVFVNTRR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1567 QTRLTALELIAFLATEEDPKQwlnmdEREMENIIATVRD--SNLKLTLAF--GIGMHHAGLHERDRKTVEELFVNCKVQV 1642
Cdd:PRK00254 250 SAEKEALELAKKIKRFLTKPE-----LRALKELADSLEEnpTNEKLKKALrgGVAFHHAGLGRTERVLIEDAFREGLIKV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1643 LIATSTLAWGVNFPAHLVIIKGTEYYDGKTrrYVDFPITDVLQMMGRAGRPQFDDQGKAVILVH-DIKKDFYKKF----- 1716
Cdd:PRK00254 325 ITATPTLSAGINLPAFRVIIRDTKRYSNFG--WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERYifgkp 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1717 --LYEPFPVESSLLGvlsdHLNAEIAGGTITSKQDALDYITWTYFfrrlimnpsYYNLGDVSH--DSVNKFLSHLIEKSL 1792
Cdd:PRK00254 403 ekLFSMLSNESAFRS----QVLALITNFGVSNFKELVNFLERTFY---------AHQRKDLYSleEKAKEIVYFLLENEF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1793 IELELsycieigEDNrsIEPLTYGRIASYYYLKHQTVKMFKDRLkPECSTEE----LLSILSDAEEYTDLPVRHNEDHMN 1868
Cdd:PRK00254 470 IDIDL-------EDR--FIPLPLGIRTSQLYIDPLTAKKFKDAF-PKIEKNPnplgIFQLIASTPDMTPLNYSRKEMEDL 539
|
....
gi 158518649 1869 SELA 1872
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 ... |
478-678 |
1.01e-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: 1.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 478 NRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQhfqQGVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPL 557
Cdd:cd18023 3 NRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKE---RNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 558 GIIVKELTGDMQLSKS-EILRTQMLVTTPEKWDVVTRKSVGDVALSQIVRLLILDEVHLLHEDRGPVLESIVARTLRQVE 636
Cdd:cd18023 80 GLSCAELTGDTEMDDTfEIQDADIILTTPEKWDSMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 158518649 637 STQSM------IRILGLSATLPNYLDVATFLHVNPyIGLFFFDGRFRP 678
Cdd:cd18023 160 SSELRgstvrpMRFVAVSATIPNIEDLAEWLGDNP-AGCFSFGESFRP 206
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
477-668 |
6.40e-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: 6.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 477 LNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHfqqgvikknEFKIVYVAPMKALAAEMTDYFSRRLEP 556
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS---------GGKAVYIAPTRALVNQKEADLRERFGP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 557 LGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDvaLSQIVRLLILDEVHLLH-EDRGPVLESIVARTLRQv 635
Cdd:cd17921 73 LGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER--LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI- 149
|
170 180 190
....*....|....*....|....*....|...
gi 158518649 636 estQSMIRILGLSATLPNYLDVATFLHVNPYIG 668
Cdd:cd17921 150 ---NKNARFVGLSATLPNAEDLAEWLGVEDLIR 179
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
493-1034 |
5.53e-53 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 200.43 E-value: 5.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 493 ENMLICAPTGAGKTNIAMLTVLHEIrqhFQQGvikkneFKIVYVAPMKALAAEMTDYFsRRLEPLGIIVKELTGDMQlSK 572
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKL---LREG------GKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYD-ST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 573 SEIL-RTQMLVTTPEKWDVVTRKSVgdvalSQI--VRLLILDEVHLL-HEDRGPVLESIVARTLRQVEstqsmirILGLS 648
Cdd:PRK00254 109 DEWLgKYDIIIATAEKFDSLLRHGS-----SWIkdVKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ-------ILGLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 649 ATLPNYLDVATFLHVNpyigLFFFDgrFRPVPL-----GQTFLGIKCANKMQQLNNMDEVCYEnvlkQVKAGHQVMVFVH 723
Cdd:PRK00254 177 ATVGNAEELAEWLNAE----LVVSD--WRPVKLrkgvfYQGFLFWEDGKIERFPNSWESLVYD----AVKKGKGALVFVN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 724 ARNATVRTAMSLIERAKNCghipFFFPTQGHDYVLAEKQVQRSRNKQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHI 803
Cdd:PRK00254 247 TRRSAEKEALELAKKIKRF----LTKPELRALKELADSLEENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 804 KVLVCTATLAWGVNLPAHAVIIKGTQIYAakRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDK----LSHYL-- 877
Cdd:PRK00254 323 KVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklMERYIfg 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 878 ------TLLTQRNPIESQFLesladnlnAEIALGTVTNVEEAVKWISYTYlYVRMRANPlaYGISHKAYQIDPTLrkhRE 951
Cdd:PRK00254 401 kpeklfSMLSNESAFRSQVL--------ALITNFGVSNFKELVNFLERTF-YAHQRKDL--YSLEEKAKEIVYFL---LE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 952 QLVIEvgrkldkaqmIRFEERtgyFSSTDLGRTASHYYIKYNTIETFNELFDahKTEGD-----IFAIVSKAEEFDQIKV 1026
Cdd:PRK00254 467 NEFID----------IDLEDR---FIPLPLGIRTSQLYIDPLTAKKFKDAFP--KIEKNpnplgIFQLIASTPDMTPLNY 531
|
....*...
gi 158518649 1027 REEEIEEL 1034
Cdd:PRK00254 532 SRKEMEDL 539
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
677-869 |
8.95e-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: 8.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 677 RPVPLGQTFLGIK----CANKMQQLNNMDEVCYENVLKQVKAGHQVMVFVHARNATVRTAMSLIerakncghipfffptq 752
Cdd:cd18795 1 RPVPLEEYVLGFNglgiKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 753 ghdyvlaekqvqrsrnkqvrelfpdGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYA 832
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 158518649 833 AKRgsFVDLGILDVMQIFGRAGRPQFDKFGEGIIITT 869
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1344-1862 |
9.08e-53 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 200.18 E-value: 9.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKVRieEKLGKKVIELTGDVTPDMKSIAKADL 1423
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAMLKAIAR--GGKALYIVPLRALASEKFEEFERF--EELGVRVGISTGDYDSRDEWLGDNDI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1424 IVTTPEKWDGVSR---SWqnrnyVQQVTILIIDEIHLLG-EERGPVLEVIVS---RTNfisshtekP-VRIVGLSTALAN 1495
Cdd:PRK02362 117 IVATSEKVDSLLRngaPW-----LDDITCVVVDEVHLIDsANRGPTLEVTLAklrRLN--------PdLQVVALSATIGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1496 ARDLADWLNIK-----------QMGLF-----NFRPSVRPVP-----------LEVHIQGfpGQhyCprmasmnkpafqa 1548
Cdd:PRK02362 184 ADELADWLDAElvdsewrpidlREGVFyggaiHFDDSQREVEvpskddtlnlvLDTLEEG--GQ--C------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1549 irshspakpvLIFVSSRRQTRLTALELIAFLateedpKQWLNMDER-EMENIIATVRDS-------NLKLTLAFGIGMHH 1620
Cdd:PRK02362 247 ----------LVFVSSRRNAEGFAKRAASAL------KKTLTAAERaELAELAEEIREVsdtetskDLADCVAKGAAFHH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1621 AGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGkTRRYVDFPITDVLQMMGRAGRPQFDDQGK 1700
Cdd:PRK02362 311 AGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDG-GAGMQPIPVLEYHQMAGRAGRPGLDPYGE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1701 AVILV--HDIKKDFYKKFLY-EPFPVESSLL--GVLSDHLNAEIAGGTITSKQDALDYITWTYFFRRlimNPSYYNLGDV 1775
Cdd:PRK02362 390 AVLLAksYDELDELFERYIWaDPEDVRSKLAtePALRTHVLSTIASGFARTRDGLLEFLEATFYATQ---TDDTGRLERV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1776 shdsVNKFLSHLIEKSLIElelsycieigEDNRSIEPLTYGRIASYYYlkhqtvkmfkdrLKPeCSTEELLSILSDAEEY 1855
Cdd:PRK02362 467 ----VDDVLDFLERNGMIE----------EDGETLEATELGHLVSRLY------------IDP-LSAAEIIDGLEAAKKP 519
|
....*..
gi 158518649 1856 TDLPVRH 1862
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 ... |
1310-1513 |
2.43e-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: 2.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1310 ITALGCKAYEALYNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKY--PTS-------KAVYIAP 1380
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHrnPDGtinldafKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1381 LKALVRERMDDWKVRIEEkLGKKVIELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGE 1460
Cdd:cd18019 81 MKALVQEMVGNFSKRLAP-YGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 158518649 1461 ERGPVLEVIVSRTNFISSHTEKPVRIVGLSTALANARDLADWLNIK-QMGLFNF 1513
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDpKKGLFYF 213
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1344-1822 |
2.53e-51 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 194.72 E-value: 2.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWkVRIEEkLGKKVIELTGDV--TPDMksIAKA 1421
Cdd:PRK01172 39 NVIVSVPTAAGKTLIAYSAIYETFLA--GLKSIYIVPLRSLAMEKYEEL-SRLRS-LGMRVKISIGDYddPPDF--IKRY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1422 DLIVTTPEKWDgvSRSWQNRNYVQQVTILIIDEIHLLGEE-RGPVLEVIVSRTNFISSHTekpvRIVGLSTALANARDLA 1500
Cdd:PRK01172 113 DVVILTSEKAD--SLIHHDPYIINDVGLIVADEIHIIGDEdRGPTLETVLSSARYVNPDA----RILALSATVSNANELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1501 DWLNIKQMglfnfRPSVRPVPLEVHIQgFPGQHYCPRMASMNKPAFQAIRSH-SPAKPVLIFVSSRRQTRLTALELIAFL 1579
Cdd:PRK01172 187 QWLNASLI-----KSNFRPVPLKLGIL-YRKRLILDGYERSQVDINSLIKETvNDGGQVLVFVSSRKNAEDYAEMLIQHF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1580 ATEEDPKqwLNMDEremeniiATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHL 1659
Cdd:PRK01172 261 PEFNDFK--VSSEN-------NNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1660 VIIKG-TEYYDGKTRryvdfPIT--DVLQMMGRAGRPQFDDQGKAVILV-----HDIKKDFYKKflyEPFPVESSLLGVL 1731
Cdd:PRK01172 332 VIVRDiTRYGNGGIR-----YLSnmEIKQMIGRAGRPGYDQYGIGYIYAaspasYDAAKKYLSG---EPEPVISYMGSQR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1732 SDHLN--AEIAGGTITSKQDALDYITWTYFFRRlimnpsyyNLGDVSHDSVNKFLSHLIEKSLIELELSY-CIEIGE--D 1806
Cdd:PRK01172 404 KVRFNtlAAISMGLASSMEDLILFYNETLMAIQ--------NGVDEIDYYIESSLKFLKENGFIKGDVTLrATRLGKltS 475
|
490
....*....|....*.
gi 158518649 1807 NRSIEPLTYGRIASYY 1822
Cdd:PRK01172 476 DLYIDPESALILKSAF 491
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
478-673 |
7.01e-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: 7.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 478 NRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFQqgvikkneFKIVYVAPMKALAAE-MTDYFSRRLEP 556
Cdd:cd18022 3 NPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPG--------SKVVYIAPLKALVRErVDDWKKRFEEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 557 LGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVV-----TRKSVgdvalsQIVRLLILDEVHLLHEDRGPVLESIVART 631
Cdd:cd18022 75 LGKKVVELTGDVTPDMKALADADIIITTPEKWDGIsrswqTREYV------QQVSLIIIDEIHLLGSDRGPVLEVIVSRM 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 158518649 632 LRQVESTQSMIRILGLSATLPNYLDVATFLHVNPyIGLFFFD 673
Cdd:cd18022 149 NYISSQTEKPVRLVGLSTALANAGDLANWLGIKK-MGLFNFR 189
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
492-990 |
2.96e-47 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 183.24 E-value: 2.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 492 NENMLICAPTGAGKTNIAMLTVLHEIrqhfqqgvikKNEFKIVYVAPMKALAAEMTDYFSRrLEPLGIIVKELTGDMQlS 571
Cdd:PRK02362 39 GKNLLAAIPTASGKTLIAELAMLKAI----------ARGGKALYIVPLRALASEKFEEFER-FEELGVRVGISTGDYD-S 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 572 KSEIL-RTQMLVTTPEKWDVVTRKsvGDVALSQIVrLLILDEVHLL-HEDRGPVLESIVARTLRQVESTQsmirILGLSA 649
Cdd:PRK02362 107 RDEWLgDNDIIVATSEKVDSLLRN--GAPWLDDIT-CVVVDEVHLIdSANRGPTLEVTLAKLRRLNPDLQ----VVALSA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 650 TLPNYLDVATFLHVNpyiglfFFDGRFRPVPLGQ-TFLG--IKCANKMQQLNNM--DEVcyEN-VLKQVKAGHQVMVFVH 723
Cdd:PRK02362 180 TIGNADELADWLDAE------LVDSEWRPIDLREgVFYGgaIHFDDSQREVEVPskDDT--LNlVLDTLEEGGQCLVFVS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 724 AR-NA---------TVRTAMSLIERAKNCGhipfffptqghdyvLAEKQVQRSRNKQVREL---FPDGFSIHHAGMLRQD 790
Cdd:PRK02362 252 SRrNAegfakraasALKKTLTAAERAELAE--------------LAEEIREVSDTETSKDLadcVAKGAAFHHAGLSREH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 791 RNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYAAKRGSfVDLGILDVMQIFGRAGRPQFDKFGEGIIIT-T 869
Cdd:PRK02362 318 RELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAGM-QPIPVLEYHQMAGRAGRPGLDPYGEAVLLAkS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 870 HDKLS----HYLTLLTQrnPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWISYTyLYvrmranplaygishkAYQID 943
Cdd:PRK02362 397 YDELDelfeRYIWADPE--DVRSKLATepALRTHVLSTIASGFARTRDGLLEFLEAT-FY---------------ATQTD 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 158518649 944 PTLRKHReqLVIEVGRKLDKAQMIrfEERTGYFSSTDLGRTASHYYI 990
Cdd:PRK02362 459 DTGRLER--VVDDVLDFLERNGMI--EEDGETLEATELGHLVSRLYI 501
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
492-1030 |
5.66e-47 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 181.23 E-value: 5.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 492 NENMLICAPTGAGKTNIAMltvlHEIRQHFQQGVikknefKIVYVAPMKALAAEMTDYFSRrLEPLGIIVKELTGDMQLS 571
Cdd:PRK01172 37 GENVIVSVPTAAGKTLIAY----SAIYETFLAGL------KSIYIVPLRSLAMEKYEELSR-LRSLGMRVKISIGDYDDP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 572 KSEILRTQMLVTTPEKWDVVTRKsvgDVALSQIVRLLILDEVHLLH-EDRGPVLESiVARTLRQVESTqsmIRILGLSAT 650
Cdd:PRK01172 106 PDFIKRYDVVILTSEKADSLIHH---DPYIINDVGLIVADEIHIIGdEDRGPTLET-VLSSARYVNPD---ARILALSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 651 LPNYLDVATFLHVNpyiglfFFDGRFRPVPLGqtfLGIKCANKMQQLNNMDEVCYENVL--KQVKAGHQVMVFVHARNAT 728
Cdd:PRK01172 179 VSNANELAQWLNAS------LIKSNFRPVPLK---LGILYRKRLILDGYERSQVDINSLikETVNDGGQVLVFVSSRKNA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 729 VRTAMSLIErakncgHIPFFfptqgHDYVLAEKQVQrSRNKQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVC 808
Cdd:PRK01172 250 EDYAEMLIQ------HFPEF-----NDFKVSSENNN-VYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 809 TATLAWGVNLPAHAVIIKGTQIYAAKRGSFvdLGILDVMQIFGRAGRPQFDKFGEGIII----TTHDKLSHYLTllTQRN 884
Cdd:PRK01172 318 TPTLAAGVNLPARLVIVRDITRYGNGGIRY--LSNMEIKQMIGRAGRPGYDQYGIGYIYaaspASYDAAKKYLS--GEPE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 885 PIESQF--LESLADNLNAEIALGTVTNVEEAVKWISYTYLYVRMRANPLAYGIShkayqidptlrkhreqlvievgrkld 962
Cdd:PRK01172 394 PVISYMgsQRKVRFNTLAAISMGLASSMEDLILFYNETLMAIQNGVDEIDYYIE-------------------------- 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158518649 963 kaQMIRFEERTGY------FSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEE 1030
Cdd:PRK01172 448 --SSLKFLKENGFikgdvtLRATRLGKLTSDLYIDPESALILKSAFDHDYDEDLALYYISLCREIIPANTRDDY 519
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1344-1726 |
1.22e-46 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 181.68 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKvrieEKLGK-KVIELTGDVT--PDmksiak 1420
Cdd:COG4581 42 SVLVAAPTGSGKTLVAEFAIFLALAR--GRRSFYTAPIKALSNQKFFDLV----ERFGAeNVGLLTGDASvnPD------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1421 ADLIVTTPEkwdgVSRswqNRNY--------VQQVtilIIDEIHLLGE-ERGPVLEVIVsrtnfIssHTEKPVRIVGLST 1491
Cdd:COG4581 110 APIVVMTTE----ILR---NMLYregadledVGVV---VMDEFHYLADpDRGWVWEEPI-----I--HLPARVQLVLLSA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1492 ALANARDLADWLNikqmglfnfrpSV-----------RPVPLEvhiqgfpgQHYC--PRMASMNKPAFQAIRSHSPAK-- 1556
Cdd:COG4581 173 TVGNAEEFAEWLT-----------RVrgetavvvseeRPVPLE--------FHYLvtPRLFPLFRVNPELLRPPSRHEvi 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1557 ---------PVLIFVSSRRQTRLTALELIAFLATEEDPKQWLNMDEREMENIIATVRDSNLKLTLAFGIGMHHAGLHERD 1627
Cdd:COG4581 234 eeldrggllPAIVFIFSRRGCDEAAQQLLSARLTTKEERAEIREAIDEFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPKY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1628 RKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKTRRyvdfPIT--DVLQMMGRAGRPQFDDQGKAVILV 1705
Cdd:COG4581 314 RRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHR----PLTarEFHQIAGRAGRRGIDTEGHVVVLA 389
|
410 420
....*....|....*....|....*
gi 158518649 1706 HDiKKDFyKKFLY----EPFPVESS 1726
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; ... |
1328-1513 |
6.99e-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: 161.83 E-value: 6.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1328 NPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTS---------KAVYIAPLKALVRERMDDWKVRIEe 1398
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQggvikkddfKIVYIAPMKALAAEMVEKFSKRLA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1399 KLGKKVIELTGDVTPDMKSIAKADLIVTTPEKWDGVSR-SWQNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFIS 1477
Cdd:cd18020 82 PLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRkSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQV 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 158518649 1478 SHTEKPVRIVGLSTALANARDLADWLNIKQM-GLFNF 1513
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 ... |
475-665 |
4.73e-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: 4.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 475 KRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHeirqHFQQGvikkNEFKIVYVAPMKALAAEMTDYFSRRL 554
Cdd:cd18021 2 KFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLR----HWRQN----PKGRAVYIAPMQELVDARYKDWRAKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 555 EP-LGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVV-----TRKSVgdvalsQIVRLLILDEVHLLHEDRGPVLESIV 628
Cdd:cd18021 74 GPlLGKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLsrrwkQRKNV------QSVELFIADELHLIGGENGPVYEVVV 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 158518649 629 ARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNP 665
Cdd:cd18021 148 SRMRYISSQLEKPIRIVGLSSSLANARDVGEWLGASK 184
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
1327-1506 |
4.83e-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: 4.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1327 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIfrVFNKYPTSKAVYIAPLKALVRERMDDWKVRieEKLGKKVIE 1406
Cdd:cd18028 2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAM--VNTLLEGGKALYLVPLRALASEKYEEFKKL--EEIGLKVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1407 LTGDVTPDMKSIAKADLIVTTPEKWDGVsrsWQNR-NYVQQVTILIIDEIHLLG-EERGPVLEVIVSRTNfissHTEKPV 1484
Cdd:cd18028 78 STGDYDEDDEWLGDYDIIVATYEKFDSL---LRHSpSWLRDVGVVVVDEIHLISdEERGPTLESIVARLR----RLNPNT 150
|
170 180
....*....|....*....|..
gi 158518649 1485 RIVGLSTALANARDLADWLNIK 1506
Cdd:cd18028 151 QIIGLSATIGNPDELAEWLNAE 172
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
488-963 |
6.47e-35 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 145.08 E-value: 6.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 488 AYNTNENMLICAPTGAGKTNIAMltvlHEIRQHFQQGVikknefKIVYVAPMKALAAEMTDYFSRRL--EPLGIivkeLT 565
Cdd:COG4581 36 ALEAGRSVLVAAPTGSGKTLVAE----FAIFLALARGR------RSFYTAPIKALSNQKFFDLVERFgaENVGL----LT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 566 GDMQL--------SKSEILRTQMLVTTPEKWDVvtrksvgDVAlsqivrllILDEVHLLHE-DRGPVLE-SIVARTLRqv 635
Cdd:COG4581 102 GDASVnpdapivvMTTEILRNMLYREGADLEDV-------GVV--------VMDEFHYLADpDRGWVWEePIIHLPAR-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 636 estqsmIRILGLSATLPNYLDVATFLH--------VnpyiglfffDGRFRPVPLGQTFLGIKCANKMQQLNNMDEVCYE- 706
Cdd:COG4581 165 ------VQLVLLSATVGNAEEFAEWLTrvrgetavV---------VSEERPVPLEFHYLVTPRLFPLFRVNPELLRPPSr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 707 -NVLKQVKAGHQ--VMVFVHARNATVrtamsliERAKNCGHIPFFFPTQGH--DYVLAEKQVQRS--RNKQVRELFPDGF 779
Cdd:COG4581 230 hEVIEELDRGGLlpAIVFIFSRRGCD-------EAAQQLLSARLTTKEERAeiREAIDEFAEDFSvlFGKTLSRLLRRGI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 780 SIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGtqiyAAKR--GSFVDLGILDVMQIFGRAGRPQ 857
Cdd:COG4581 303 AVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTK----LSKFdgERHRPLTAREFHQIAGRAGRRG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 858 FDKFGEGIIITT-HDKLSHYLTLLTQR-NPIESQFlesladnlnaEIALGTVTNVeeaVKWISYTylyvRMRAnplAYGI 935
Cdd:COG4581 379 IDTEGHVVVLAPeHDDPKKFARLASARpEPLRSSF----------RPSYNMVLNL---LARPGLE----RARE---LLED 438
|
490 500
....*....|....*....|....*...
gi 158518649 936 SHKAYQIDPTLRKHREQlVIEVGRKLDK 963
Cdd:COG4581 439 SFAQFQADRSVVGLARR-ARELERALAG 465
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
478-656 |
1.27e-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: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 478 NRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQhfqqgviKKNEFKIVYVAPMKALAAEMTDYFSRRLEPL 557
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK-------LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 558 GIIVKELTGDMQLSK--SEILRTQMLVTTPEKWDVVTRKSvgdVALSQiVRLLILDEVHLLHE-DRGPVLESIVARtlrq 634
Cdd:pfam00270 73 GLKVASLLGGDSRKEqlEKLKGPDILVGTPGRLLDLLQER---KLLKN-LKLLVLDEAHRLLDmGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|..
gi 158518649 635 vesTQSMIRILGLSATLPNYLD 656
Cdd:pfam00270 145 ---LPKKRQILLLSATLPRNLE 163
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1328-1499 |
1.78e-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: 125.05 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1328 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFN-KYPTSKAVYIAPLKALVRERMDDWKVRIeEKLGKKVIE 1406
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDkLDNGPQALVLAPTRELAEQIYEELKKLG-KGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1407 LTGDVTP--DMKSIAKADLIVTTPEKWDGVsrsWQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNfisshteKP 1483
Cdd:pfam00270 79 LLGGDSRkeQLEKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRRLP-------KK 148
|
170
....*....|....*..
gi 158518649 1484 VRIVGLS-TALANARDL 1499
Cdd:pfam00270 149 RQILLLSaTLPRNLEDL 165
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
476-661 |
8.26e-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: 8.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 476 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHfqqgvikkneFKIVYVAPMKALAAEMTDYFSrRLE 555
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEG----------GKALYLVPLRALASEKYEEFK-KLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 556 PLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSvgdVALSQIVRLLILDEVHLLH-EDRGPVLESIVARTLRQ 634
Cdd:cd18028 70 EIGLKVGISTGDYDEDDEWLGDYDIIVATYEKFDSLLRHS---PSWLRDVGVVVVDEIHLISdEERGPTLESIVARLRRL 146
|
170 180
....*....|....*....|....*..
gi 158518649 635 VESTQsmirILGLSATLPNYLDVATFL 661
Cdd:cd18028 147 NPNTQ----IIGLSATIGNPDELAEWL 169
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1329-1705 |
7.00e-26 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 116.53 E-value: 7.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1329 PVQT-QIFHTLYHTDcNVLLGAPTGSGKTVAAELA-IFRVFNKypTSKAVYIAPLKALVRERMDDWKVRIEEKLgkKVIE 1406
Cdd:COG1202 212 PVQSlAVENGLLEGK-DQLVVSATATGKTLIGELAgIKNALEG--KGKMLFLVPLVALANQKYEDFKDRYGDGL--DVSI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1407 LTGDV---TPDMKSIAKADLIVTTPEKWDGVSRSwqnRNYVQQVTILIIDEIHLLGE-ERGPVLEVIVSRTNFISSHTEk 1482
Cdd:COG1202 287 RVGASrirDDGTRFDPNADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEVHMLEDpERGHRLDGLIARLKYYCPGAQ- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1483 pvrIVGLSTALANARDLADWLNIKQMgLFNfrpsVRPVPLEVHIQGFPGQHYCPRMASMNKPAFQAIRSHSPAKPVLIFV 1562
Cdd:COG1202 363 ---WIYLSATVGNPEELAKKLGAKLV-EYE----ERPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1563 SSRRQTRltaleliaflateedpkqwlnmderemeniiatvrdsnlKLTLAFGIGM--HHAGLHERDRKTVEELFVNCKV 1640
Cdd:COG1202 435 NSRRRCH---------------------------------------EIARALGYKAapYHAGLDYGERKKVERRFADQEL 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158518649 1641 QVLIATSTLAWGVNFPAHLVIIK----GTEYydgktrryvdFPITDVLQMMGRAGRPQFDDQGKAVILV 1705
Cdd:COG1202 476 AAVVTTAALAAGVDFPASQVIFDslamGIEW----------LSVQEFHQMLGRAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
469-680 |
9.65e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.81 E-value: 9.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 469 LAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRqhfqqgviKKNEFKIVYVAPMKALAAEMTD 548
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALK--------RGKGGRVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 549 YFSRRLEPLGIIVKELTGD----MQLSKSEILRTQMLVTTPEKWDVVTRKsvGDVALSQiVRLLILDEVH-LLHEDRGPV 623
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRLLDLLEN--DKLSLSN-VDLVILDEAHrLLDGGFGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 158518649 624 LESIVARTLRqvestqsMIRILGLSATLPNYLDVATFLHVNpyiGLFFFDGRFRPVP 680
Cdd:smart00487 150 LEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1322-1521 |
1.17e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 103.73 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1322 YNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLG 1401
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1402 KKVIELTGDVT-PDMKSIAK--ADLIVTTPEKWDGVSRswQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNfis 1477
Cdd:smart00487 84 KVVGLYGGDSKrEQLRKLESgkTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 158518649 1478 shteKPVRIVGLS-TALANARDLADWLNIkqmGLFNFRPSVRPVP 1521
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 ... |
1342-1515 |
2.55e-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: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1342 DCNVLLGAPTGSGKTVAAELAIFRVF--NKyptSKAVYIAPLKALVRERMDdWKVRIEEKLGKKVIELTGDVTPDM-KSI 1418
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLleRR---KKALFVLPYVSIVQEKVD-ALSPLFEELGFRVEGYAGNKGRSPpKRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1419 AKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGEE-RGPVLEVIVSRtnfISSHTEKPVRIVGLSTALANAR 1497
Cdd:cd18026 109 KSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDGhRGALLELLLTK---LLYAAQKNIQIVGMSATLPNLE 185
|
170 180
....*....|....*....|
gi 158518649 1498 DLADWLNIKqmgLF--NFRP 1515
Cdd:cd18026 186 ELASWLRAE---LYttNFRP 202
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
1344-1503 |
1.22e-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: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKYPTS--KAVYIAPLKALVRermdDWKVRIEE-----KLGKKVIELTGDVTPDMK 1416
Cdd:cd17922 3 NVLIAAPTGSGKTEAAFLPALSSLADEPEKgvQVLYISPLKALIN----DQERRLEEpldeiDLEIPVAVRHGDTSQSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1417 SIAKA---DLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRtnfISSHTEKPVRIVGLSTA 1492
Cdd:cd17922 79 AKQLKnppGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHaLLGSKRGVQLELLLER---LRKLTGRPLRRIGLSAT 155
|
170
....*....|.
gi 158518649 1493 LANARDLADWL 1503
Cdd:cd17922 156 LGNLEEAAAFL 166
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
492-661 |
1.34e-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: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 492 NENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGVikknefKIVYVAPMKALAAEMTdyfsRRLE------PLGIIVKELT 565
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV------QVLYISPLKALINDQE----RRLEepldeiDLEIPVAVRH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 566 GDM-QLSKSEILRT--QMLVTTPEKWDVVTRKSVGDVALSQiVRLLILDEVH-LLHEDRGPVLESIVARtLRQVESTQsm 641
Cdd:cd17922 71 GDTsQSEKAKQLKNppGILITTPESLELLLVNKKLRELFAG-LRYVVVDEIHaLLGSKRGVQLELLLER-LRKLTGRP-- 146
|
170 180
....*....|....*....|
gi 158518649 642 IRILGLSATLPNYLDVATFL 661
Cdd:cd17922 147 LRRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
492-678 |
1.31e-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: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 492 NENMLICAPTGAGKTNIAMLTVLHEIRQhfqqgvikkNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDmqLS 571
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLLE---------RRKKALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGN--KG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 572 KSEILR---TQMLVTTPEKWDVVTRKSVGDVALSQIvRLLILDEVHLLHE-DRGPVLESIVARTLRqveSTQSMIRILGL 647
Cdd:cd18026 102 RSPPKRrksLSVAVCTIEKANSLVNSLIEEGRLDEL-GLVVVDELHMLGDgHRGALLELLLTKLLY---AAQKNIQIVGM 177
|
170 180 190
....*....|....*....|....*....|.
gi 158518649 648 SATLPNYLDVATFLHVnpyiglFFFDGRFRP 678
Cdd:cd18026 178 SATLPNLEELASWLRA------ELYTTNFRP 202
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1324-1661 |
6.95e-19 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 94.01 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1324 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAIF-RVFNKYPTSKA------VYIAPLKAL---VRERMDDWK 1393
Cdd:COG1201 22 FGAPTPPQREAW-PAIAAGESTLLIAPTGSGKTLAAFLPALdELARRPRPGELpdglrvLYISPLKALandIERNLRAPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1394 VRIEEKLGKKVIEL-----TGDVTPDMKSIAKA---DLIVTTPE---------KWdgvsrswqnRNYVQQVTILIIDEIH 1456
Cdd:COG1201 101 EEIGEAAGLPLPEIrvgvrTGDTPASERQRQRRrppHILITTPEslallltspDA---------RELLRGVRTVIVDEIH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1457 -LLGEERGPVLEVIVSRtnfISSHTEKPVRIVGLSTALANARDLADWLnikqMGLFNFRPS--VRP-----------VPL 1522
Cdd:COG1201 172 aLAGSKRGVHLALSLER---LRALAPRPLQRIGLSATVGPLEEVARFL----VGYEDPRPVtiVDAgagkkpdlevlVPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1523 EVHIQGFP-----GQHYCPRMAsmnkpafQAIRSHspaKPVLIFVSSRRQTRLTALELIAFLATEEDPkqwlnmdereme 1597
Cdd:COG1201 245 EDLIERFPwaghlWPHLYPRVL-------DLIEAH---RTTLVFTNTRSQAERLFQRLNELNPEDALP------------ 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158518649 1598 niiatvrdsnlkltlafgIGMHHAGL-HERdRKTVEELFVNCKVQVLIATSTLAWGVNFPA-HLVI 1661
Cdd:COG1201 303 ------------------IAAHHGSLsREQ-RLEVEEALKAGELRAVVATSSLELGIDIGDvDLVI 349
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
469-877 |
4.38e-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: 4.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 469 LAFKGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQHfqqgvikkNEFKIVYVAPMKALAA---- 544
Cdd:COG1205 49 LKKRGIERLYSHQAEAIEAARA-GKNVVIATPTASGKSLAYLLPVLEALLED--------PGATALYLYPTKALARdqlr 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 545 EMTDYFSRRlePLGIIVKELTGDMQLS-KSEILRT-QMLVTTP-----------EKWDVVTRKsvgdvalsqiVRLLILD 611
Cdd:COG1205 120 RLRELAEAL--GLGVRVATYDGDTPPEeRRWIREHpDIVLTNPdmlhygllphhTRWARFFRN----------LRYVVID 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 612 EVHLLhedRGpVLESIVA----RTLRQVESTQSMIRILGLSATLPNYLDVA---------------------TFLHVNPY 666
Cdd:COG1205 188 EAHTY---RG-VFGSHVAnvlrRLRRICRHYGSDPQFILASATIGNPAEHAerltgrpvtvvdedgsprgerTFVLWNPP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 667 IGLfffDGRFRPVPLgqtflgikcankmqqlnnmdEVCYenVLKQ-VKAGHQVMVFVHARNATVRTAMSLIERAKncghi 745
Cdd:COG1205 264 LVD---DGIRRSALA--------------------EAAR--LLADlVREGLRTLVFTRSRRGAELLARYARRALR----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 746 pfffptqghdyvlaekqvqrsrnkqvRELFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPA-HAVI 824
Cdd:COG1205 314 --------------------------EPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVV 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 158518649 825 IKGtqiYAAKRGSFVdlgildvmQIFGRAGRPQFDkfGEGIIITTHDKLSHYL 877
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 ... |
1346-1661 |
8.96e-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: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1346 LLGAPTGSGKTVAAELAIFRVFNKYPTSK-----AVYIAPLKALVRErmddwkvrIEEKLGKKVIEL---------TGDV 1411
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKekglhTLYITPLRALAVD--------IARNLQAPIEELglpirvetrTGDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1412 TPDMKSIAKA---DLIVTTPEkwdgvsrSWQ-------NRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNFISSHt 1480
Cdd:TIGR04121 104 SSSERARQRKkppDILLTTPE-------SLAlllsypdAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1481 ekpVRIVGLSTALANARDLADWLnikqMGLFNFRPSV------RPVPLEV----HIQGFP-GQHYCPRMASmnkPAFQAI 1549
Cdd:TIGR04121 176 ---LRRWGLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISllpeSEERFPwAGHLGLRALP---EVYAEI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1550 RSHspaKPVLIFVSSRRQTRLTALELIAFLAteedpkqwlnmderemeniiatvrDSNLKltlafgIGMHHAGLHERDRK 1629
Cdd:TIGR04121 246 DQA---RTTLVFTNTRSQAELWFQALWEANP------------------------EFALP------IALHHGSLDREQRR 292
|
330 340 350
....*....|....*....|....*....|...
gi 158518649 1630 TVEELFVNCKVQVLIATSTLAWGVNF-PAHLVI 1661
Cdd:TIGR04121 293 WVEAAMAAGRLRAVVCTSSLDLGVDFgPVDLVI 325
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
493-870 |
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 158518649 493 ENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGViKKNEFKIVYVAPMKALAAEMtdyfSRRLE-PL-------GIIVKEL 564
Cdd:COG1201 40 ESTLLIAPTGSGKTLAAFLPALDELARRPRPGE-LPDGLRVLYISPLKALANDI----ERNLRaPLeeigeaaGLPLPEI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 565 -----TGDMqlSKSEilRTQM-------LVTTPE---------KWdvvtRKSVGDvalsqiVRLLILDEVHLLHED-RGP 622
Cdd:COG1201 115 rvgvrTGDT--PASE--RQRQrrrpphiLITTPEslallltspDA----RELLRG------VRTVIVDEIHALAGSkRGV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 623 VLESIVARtLRQVeSTQSMIRIlGLSATLPNYLDVATFLhvnpyIGlfffDGRFRPV-----PLGQTF-LGIKCANKmqq 696
Cdd:COG1201 181 HLALSLER-LRAL-APRPLQRI-GLSATVGPLEEVARFL-----VG----YEDPRPVtivdaGAGKKPdLEVLVPVE--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 697 lnNMDEVC----------YENVLKQVKAGHQVMVFVHARNatvrtamslierakncghipfffptqghdyvLAEKQVQRs 766
Cdd:COG1201 246 --DLIERFpwaghlwphlYPRVLDLIEAHRTTLVFTNTRS-------------------------------QAERLFQR- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 767 rnkqVRELFPDGFS---IHHAGMLRQDRNLVENLFSNGHIKVLVCTATLA----WG-VNLpahaVIikgtQIYAAK---R 835
Cdd:COG1201 292 ----LNELNPEDALpiaAHHGSLSREQRLEVEEALKAGELRAVVATSSLElgidIGdVDL----VI----QVGSPKsvaR 359
|
410 420 430
....*....|....*....|....*....|....*
gi 158518649 836 GsfvdlgildvMQIFGRAGRpQFDKFGEGIIITTH 870
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 ... |
1344-1490 |
1.85e-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: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDdwKVRIEEKLGKKVIELTGDVTP---DMKSIAK 1420
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKG-KKVLVLVPTKALALQTAE--RLRELFGPGIRVAVLVGGSSAeerEKNKLGD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158518649 1421 ADLIVTTPEKWDGVSRSwQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTnfissHTEKPVRIVGLS 1490
Cdd:cd00046 80 ADIIIATPDMLLNLLLR-EDRLFLKDLKLIIVDEAHaLLIDSRGALILDLAVRK-----AGLKNAQVILLS 144
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
454-858 |
2.42e-15 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 82.25 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 454 EEKPVYIQDLDEIGQlaFKGM-----KRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIrqhfqqgviKK 528
Cdd:COG1202 184 EVDTVPVDDLDLPPE--LKDLlegrgEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAGIKNA---------LE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 529 NEFKIVYVAPMKALAAEMTDYFSRRLEPlGIIVKELTGDMQLSKSE---ILRTQMLVTTPEKWDVVTR--KSVGDVALsq 603
Cdd:COG1202 253 GKGKMLFLVPLVALANQKYEDFKDRYGD-GLDVSIRVGASRIRDDGtrfDPNADIIVGTYEGIDHALRtgRDLGDIGT-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 604 ivrlLILDEVHLLHE-DRGPVLESIVARtLRQV-ESTQsmirILGLSATLPNYLDVATFLHVNpyigLFFFDGRfrPVPL 681
Cdd:COG1202 330 ----VVIDEVHMLEDpERGHRLDGLIAR-LKYYcPGAQ----WIYLSATVGNPEELAKKLGAK----LVEYEER--PVPL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 682 GQ--TFlgikcANKMQQLNNMDEVCYENVLKQVKAGH--QVMVFVHARnatvrtamslieraKNCghipfffptqghdYV 757
Cdd:COG1202 395 ERhlTF-----ADGREKIRIINKLVKREFDTKSSKGYrgQTIIFTNSR--------------RRC-------------HE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 758 LAEKqvqrsrnkqvrelFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIikgtqiyaakrgs 837
Cdd:COG1202 443 IARA-------------LGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVI------------- 496
|
410 420
....*....|....*....|....*...
gi 158518649 838 FVDL--GI--LDV---MQIFGRAGRPQF 858
Cdd:COG1202 497 FDSLamGIewLSVqefHQMLGRAGRPDY 524
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
488-856 |
5.73e-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: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 488 AYNTNENMLICAPTGAGKTNIAMLTVLheIRQHFQQGViKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVK-EL-T 565
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSL--IDLAGPEAP-KEKGLHTLYITPLRALAVDIARNLQAPIEELGLPIRvETrT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 566 GDMQLSKSEILRTQM---LVTTPEKWDVVTrkSVGDVA-LSQIVRLLILDEVH-LLHEDRGPVLESIVARtLRQvesTQS 640
Cdd:TIGR04121 101 GDTSSSERARQRKKPpdiLLTTPESLALLL--SYPDAArLFKDLRCVVVDEWHeLAGSKRGDQLELALAR-LRR---LAP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 641 MIRILGLSATLPNyLDVA--TFLHVNPYIGLFFFDGRFRPVPL-------GQTF-----LGIKCAnkmqqlnnmdevcyE 706
Cdd:TIGR04121 175 GLRRWGLSATIGN-LEEArrVLLGVGGAPAVLVRGKLPKAIEVisllpesEERFpwaghLGLRAL--------------P 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 707 NVLKQVKAGHQVMVFVHARNATVRTAMSLIErakncghipfffptqghdyvlaekqvqrsrnkqVRELFPDGFSIHHAGM 786
Cdd:TIGR04121 240 EVYAEIDQARTTLVFTNTRSQAELWFQALWE---------------------------------ANPEFALPIALHHGSL 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158518649 787 LRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIkgtQIYAAKrgsfvdlGILDVMQIFGRAG-RP 856
Cdd:TIGR04121 287 DREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSPK-------GVARLLQRAGRSNhRP 347
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1614-1693 |
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 158518649 1614 FGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryVDFPITDVLQMMGRAGR 1692
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVII-----YD------LPWSPASYIQRIGRAGR 80
|
.
gi 158518649 1693 P 1693
Cdd:smart00490 81 A 81
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1289-1735 |
3.97e-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: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1289 HLILPERHPPHTELLD-LQPLPITALGCKAYEALYnfSHfnpvQTQIFHtLYHTDCNVLLGAPTGSGKTVAAELAIFRVF 1367
Cdd:COG1205 24 VRTIPAREARYAPWPDwLPPELRAALKKRGIERLY--SH----QAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1368 NKYPTSKAVYIAPLKALVRERMDDWKvRIEEKLGK--KVIELTGDVTPDMKS--IAKADLIVTTP-----------EKWd 1432
Cdd:COG1205 97 LEDPGATALYLYPTKALARDQLRRLR-ELAEALGLgvRVATYDGDTPPEERRwiREHPDIVLTNPdmlhygllphhTRW- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1433 gvSRSWQNRNYVqqvtilIIDEIHLLgeeRGpvleV-------IVSRTNFISSHTEKPVRIVGLSTALANARDLAdwlni 1505
Cdd:COG1205 175 --ARFFRNLRYV------VIDEAHTY---RG----VfgshvanVLRRLRRICRHYGSDPQFILASATIGNPAEHA----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1506 kqMGLFNfRPsvrpvplevhiqgfpgqhycprmasmnkpaFQAI-RSHSPA--------KPVLIFVSSRRQTRLTALELI 1576
Cdd:COG1205 235 --ERLTG-RP------------------------------VTVVdEDGSPRgertfvlwNPPLVDDGIRRSALAEAARLL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1577 AFLAtEEDPKQWLNMDEREM-ENIIATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNF 1655
Cdd:COG1205 282 ADLV-REGLRTLVFTRSRRGaELLARYARRALREPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1656 PA-HLVIIKGteyydgktrryvdFP--ITDVLQMMGRAGRpqfDDQGKAVILV--HDIKKDFYKK---FLYEPfPVESSL 1727
Cdd:COG1205 361 GGlDAVVLAG-------------YPgtRASFWQQAGRAGR---RGQDSLVVLVagDDPLDQYYVRhpeELFER-PPEAAV 423
|
490
....*....|...
gi 158518649 1728 LG-----VLSDHL 1735
Cdd:COG1205 424 IDpdnpyVLAPHL 436
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
492-650 |
4.82e-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: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 492 NENMLICAPTGAGKTNIAMLTVLHEIRqhfqqgvikKNEFKIVYVAPMKALAAEMTDYFsRRLEPLGIIVKELTGDM--- 568
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLL---------KKGKKVLVLVPTKALALQTAERL-RELFGPGIRVAVLVGGSsae 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 569 QLSKSEILRTQMLVTTPEKwdvVTRKSVGDVALSQI-VRLLILDEVH-LLHEDRGPVLESIVARTLRQVEStqsmiRILG 646
Cdd:cd00046 71 EREKNKLGDADIIIATPDM---LLNLLLREDRLFLKdLKLIIVDEAHaLLIDSRGALILDLAVRKAGLKNA-----QVIL 142
|
....
gi 158518649 647 LSAT 650
Cdd:cd00046 143 LSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
778-856 |
9.01e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 65.70 E-value: 9.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 778 GFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIKGtqiyaakrgsfVDLGILDVMQIFGRAGRP 856
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 ... |
492-653 |
9.68e-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: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 492 NENMLICAPTGAGKTNI---AMLTVLHEirqhfqqgvikKNEFKIVYVAPMKAL----AAEMTDYFSRRLEPLGI-IVKE 563
Cdd:cd18025 16 RESALIVAPTSSGKTFIsyyCMEKVLRE-----------SDDGVVVYVAPTKALvnqvVAEVYARFSKKYPPSGKsLWGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 564 LTGDMQLskSEILRTQMLVTTPEKWDVVTRkSVGDVALSQIVRLLILDEVHLL-HEDRGPVLESIVArtlrqvestqsMI 642
Cdd:cd18025 85 FTRDYRH--NNPMNCQVLITVPECLEILLL-SPHNASWVPRIKYVIFDEIHSIgQSEDGAVWEQLLL-----------LI 150
|
170
....*....|...
gi 158518649 643 R--ILGLSATLPN 653
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 ... |
493-650 |
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 158518649 493 ENMLICAPTGAGKTNIAMLtvlheIRQHFQQGVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLSK 572
Cdd:cd17927 18 KNTIICLPTGSGKTFVAVL-----ICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 573 S---EILRTQMLVTTPEKWdVVTRKSVGDVALSqIVRLLILDEVHllHEDRGPVLESIVARTLRQ-VESTQSMIRILGLS 648
Cdd:cd17927 93 SveqIVESSDVIIVTPQIL-VNDLKSGTIVSLS-DFSLLVFDECH--NTTKNHPYNEIMFRYLDQkLGSSGPLPQILGLT 168
|
..
gi 158518649 649 AT 650
Cdd:cd17927 169 AS 170
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
492-819 |
6.90e-11 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 67.99 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 492 NENMLICAPTGAGKTNIAMLTVLHEIrqhFQQGVIKKNEFKI--VYVAPMKALAAEMtdyfsRR--LEPLGIIVKEL--- 564
Cdd:PRK13767 47 GKNVLISSPTGSGKTLAAFLAIIDEL---FRLGREGELEDKVycLYVSPLRALNNDI-----HRnlEEPLTEIREIAker 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 565 ------------TGDM-QLSKSEILRT--QMLVTTPEKWDVVT-----RKSVGDvalsqiVRLLILDEVHLLHED-RGPV 623
Cdd:PRK13767 119 geelpeirvairTGDTsSYEKQKMLKKppHILITTPESLAILLnspkfREKLRT------VKWVIVDEIHSLAENkRGVH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 624 LesivARTLRQVES--TQSMIRIlGLSATLPNYLDVATFLhvnpyiGLFFFDGRFRPVPLGQT-F---LGIKCANKMQQL 697
Cdd:PRK13767 193 L----SLSLERLEElaGGEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDCEIVDArFvkpFDIKVISPVDDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 698 -----NNMDEVCYENVLKQVKAGHQVMVFVHARNATVRTAMSLierakncghipfffptqghdyvlaekqvqrsrnkqvR 772
Cdd:PRK13767 262 ihtpaEEISEALYETLHELIKEHRTTLIFTNTRSGAERVLYNL------------------------------------R 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 158518649 773 ELFPDGFSI-----HHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP 819
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 ... |
1345-1503 |
9.30e-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: 9.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1345 VLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDwkvrIEEKLGKkVIELTGDVT--PDmksiakAD 1422
Cdd:cd18024 50 VLVSAHTSAGKTVVAEYAIAQSLRD--KQRVIYTSPIKALSNQKYRE----LQEEFGD-VGLMTGDVTinPN------AS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1423 LIVTTPEkwdgVSRS--WQNRNYVQQVTILIIDEIHLLGE-ERGPVLEvivsRTNFISSHTekpVRIVGLSTALANARDL 1499
Cdd:cd18024 117 CLVMTTE----ILRSmlYRGSEIMREVAWVIFDEIHYMRDkERGVVWE----ETIILLPDK---VRYVFLSATIPNARQF 185
|
....
gi 158518649 1500 ADWL 1503
Cdd:cd18024 186 AEWI 189
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
1333-1708 |
1.23e-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: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1333 QIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTskaVYIAPLKALVRermdDWKVRIEEKLGKkvIELTGDVT 1412
Cdd:COG1061 91 ALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV---LVLVPRRELLE----QWAEELRRFLGD--PLAGGGKK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1413 PDmksiaKADLIVTTpekWDGVSRSWQNRNYVQQVTILIIDEIHLLGeerGPVLEVIVSRTNfisshtekPVRIVGLS-T 1491
Cdd:COG1061 162 DS-----DAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHAG---APSYRRILEAFP--------AAYRLGLTaT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1492 AlanardladwlnikqmglfnFRPSVRPVPLEVhiqgFPGQHYcprmasmNKPAFQAIRSHSPAKPVLIfvssRRQTRLT 1571
Cdd:COG1061 223 P--------------------FRSDGREILLFL----FDGIVY-------EYSLKEAIEDGYLAPPEYY----GIRVDLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1572 AlELIAFLATEEDPKQWLNMDEREMENIIATVRDSNLKL--TLAFGIGMHHA-------------------GLHERDRKT 1630
Cdd:COG1061 268 D-ERAEYDALSERLREALAADAERKDKILRELLREHPDDrkTLVFCSSVDHAealaellneagiraavvtgDTPKKEREE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1631 VEELFVNCKVQVLIATSTLAWGVNFPA--HLVIIKGTeyydgKTRRYvdfpitdVLQMMGRAGRPqfdDQGKAVILVHDI 1708
Cdd:COG1061 347 ILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPT-----GSPRE-------FIQRLGRGLRP---APGKEDALVYDF 411
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1349-1691 |
2.20e-10 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 66.49 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1349 APTGSGKTVAAEL-AIFRVF----------NKYPTSKAVYIAPLKALVRERMDDWKVRIE------EKLGKKVIELT-GD 1410
Cdd:PRK09751 3 APTGSGKTLAAFLyALDRLFreggedtreaHKRKTSRILYISPIKALGTDVQRNLQIPLKgiaderRRRGETEVNLRvGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1411 VTPDMKSIAKA-------DLIVTTPEKWDGVSRSwQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNFIsSHTek 1482
Cdd:PRK09751 83 RTGDTPAQERSkltrnppDILITTPESLYLMLTS-RARETLRGVETVIIDEVHaVAGSKRGAHLALSLERLDAL-LHT-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1483 PVRIVGLSTALANARDLADWLNIKQMGLFNFRPSVR--------PVPLEVHIQGFPGQH----YCPRMASMnKPAFQA-- 1548
Cdd:PRK09751 159 SAQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRhpqirivvPVANMDDVSSVASGTgedsHAGREGSI-WPYIETgi 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1549 IRSHSPAKPVLIFVSSRRQT-RLTAL--ELIA--FLATEEDPKqwlnmDEREMENIIATV--RDSNLKLTLAFGigmHHA 1621
Cdd:PRK09751 238 LDEVLRHRSTIVFTNSRGLAeKLTARlnELYAarLQRSPSIAV-----DAAHFESTSGATsnRVQSSDVFIARS---HHG 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158518649 1622 GLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKgteyydgktrryVDFP--ITDVLQMMGRAG 1691
Cdd:PRK09751 310 SVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQ------------VATPlsVASGLQRIGRAG 369
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1598-1692 |
4.57e-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: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1598 NIIATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryV 1676
Cdd:pfam00271 23 QTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YD------L 91
|
90
....*....|....*.
gi 158518649 1677 DFPITDVLQMMGRAGR 1692
Cdd:pfam00271 92 PWNPASYIQRIGRAGR 107
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1345-1504 |
4.61e-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: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1345 VLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLGKKVIELTGDVTPD--MKSIAKAD 1422
Cdd:cd18025 19 ALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYPPSGKSLWGVFTRDyrHNNPMNCQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1423 LIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLG-EERGPVLEVIVsrtnfisshTEKPVRIVGLSTALANARDLAD 1501
Cdd:cd18025 99 VLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGqSEDGAVWEQLL---------LLIPCPFLALSATIGNPQKFHE 169
|
...
gi 158518649 1502 WLN 1504
Cdd:cd18025 170 WLQ 172
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1328-1511 |
7.47e-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: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1328 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIfrVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEklgkkVIEL 1407
Cdd:cd18027 10 DVFQKQAILHLEAGD-SVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGD-----VGLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1408 TGDVT--PDMKSiakadLIVTTPekwdgVSRS--WQNRNYVQQVTILIIDEIHLLGE-ERGPVLEVIVSrtnFISSHtek 1482
Cdd:cd18027 82 TGDVQlnPEASC-----LIMTTE-----ILRSmlYNGSDVIRDLEWVIFDEVHYINDaERGVVWEEVLI---MLPDH--- 145
|
170 180 190
....*....|....*....|....*....|
gi 158518649 1483 pVRIVGLSTALANARDLADWLN-IKQMGLF 1511
Cdd:cd18027 146 -VSIILLSATVPNTVEFADWIGrIKKKNIY 174
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1324-1490 |
1.24e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 63.75 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1324 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAI----FRVFNK-------YptskAVYIAPLKAL---VRERM 1389
Cdd:PRK13767 30 FGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREgeledkvY----CLYVSPLRALnndIHRNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1390 DDWKVRIEEKLGKKVIEL--------TGDVTPDMKS--------IakadLIvTTPEKWDGVSRSWQNRNYVQQVTILIID 1453
Cdd:PRK13767 105 EEPLTEIREIAKERGEELpeirvairTGDTSSYEKQkmlkkpphI----LI-TTPESLAILLNSPKFREKLRTVKWVIVD 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 158518649 1454 EIHLLGE-ERGPVLEVIVSRTNFISSHteKPVRIvGLS 1490
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 ... |
1344-1500 |
1.63e-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: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVR---ERMDDWKVRIEEKLgkKVIELTGDvTP--DMKSI 1418
Cdd:cd17923 17 SVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQdqlRSLRELLEQLGLGI--RVATYDGD-TPreERRAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1419 AK--ADLIVTTP-----------EKWDGVSRSWQnrnYVqqvtilIIDEIH----LLGEERGPVLEVIVSRTNFISSHte 1481
Cdd:cd17923 94 IRnpPRILLTNPdmlhyallphhDRWARFLRNLR---YV------VLDEAHtyrgVFGSHVALLLRRLRRLCRRYGAD-- 162
|
170
....*....|....*....
gi 158518649 1482 kpVRIVGLSTALANARDLA 1500
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 ... |
493-658 |
3.05e-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: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 493 ENMLICAPTGAGKTNIAMLTVLHEIrqhfqqgvIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPL--GIIVKELTGDMQL 570
Cdd:cd17923 16 RSVVVTTGTASGKSLCYQLPILEAL--------LRDPGSRALYLYPTKALAQDQLRSLRELLEQLglGIRVATYDGDTPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 571 SKSEILRTQ---MLVTTPEKWDV-VTRKSVGDVALSQIVRLLILDEVHLLhedRGpVLESIVA----RTLRQVESTQSMI 642
Cdd:cd17923 88 EERRAIIRNpprILLTNPDMLHYaLLPHHDRWARFLRNLRYVVLDEAHTY---RG-VFGSHVAlllrRLRRLCRRYGADP 163
|
170
....*....|....*.
gi 158518649 643 RILGLSATLPNYLDVA 658
Cdd:cd17923 164 QFILTSATIGNPAEHA 179
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
481-649 |
3.14e-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: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 481 QSIVFETAynTNENMLICAPTGAGKTNIA-MLtvlheIRQ-HFQQGVIKKNEFKIVYVAPMKALAAEMTDYFsRRLEPLG 558
Cdd:cd18034 7 QLELFEAA--LKRNTIVVLPTGSGKTLIAvML-----IKEmGELNRKEKNPKKRAVFLVPTVPLVAQQAEAI-RSHTDLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 559 iiVKELTGDMQLS-------KSEILRTQMLVTTPEKW-DVVTRksvGDVALSQIvRLLILDEVHL---LHEDRGpvlesi 627
Cdd:cd18034 79 --VGEYSGEMGVDkwtkerwKEELEKYDVLVMTAQILlDALRH---GFLSLSDI-NLLIFDECHHatgDHPYAR------ 146
|
170 180
....*....|....*....|..
gi 158518649 628 VARTLRQVESTQSMIRILGLSA 649
Cdd:cd18034 147 IMKEFYHLEGRTSRPRILGLTA 168
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
452-860 |
3.58e-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: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 452 SFEEKPVYIQDLDEiGQLAFKGMKRLNRIQSIVFETAYNT----NENMLICAPTGAGKTNIAMLTvlheIRQHFQQGvik 527
Cdd:COG1061 57 DTERELAEAEALEA-GDEASGTSFELRPYQQEALEALLAAlergGGRGLVVAPTGTGKTVLALAL----AAELLRGK--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 528 knefKIVYVAPMKAL----AAEMTDYFSRRLEPLGiiVKELTGDmqlskseilrtqMLVTTpekWDVVTRKSVGDvALSQ 603
Cdd:COG1061 129 ----RVLVLVPRRELleqwAEELRRFLGDPLAGGG--KKDSDAP------------ITVAT---YQSLARRAHLD-ELGD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 604 IVRLLILDEVHLLhedrgpvlesiVARTLRQVESTQSMIRILGLSATlPNYLDVATflhvnpyIGLFFFDG-RFRpVPLG 682
Cdd:COG1061 187 RFGLVIIDEAHHA-----------GAPSYRRILEAFPAAYRLGLTAT-PFRSDGRE-------ILLFLFDGiVYE-YSLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 683 Q----------TFLGIKcaNKMQQLNNMDEVCYENVLKQVKAGHQvmvfvharnATVRTAMSLIERAKNCGHIPFFFPTQ 752
Cdd:COG1061 247 EaiedgylappEYYGIR--VDLTDERAEYDALSERLREALAADAE---------RKDKILRELLREHPDDRKTLVFCSSV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 753 GHDYVLAEkqvqrsrnkqvrELFPDGFSIH--HAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIikgtqI 830
Cdd:COG1061 316 DHAEALAE------------LLNEAGIRAAvvTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVA-----I 378
|
410 420 430
....*....|....*....|....*....|
gi 158518649 831 YAAKRGSfvdLGILdvMQIFGRAGRPQFDK 860
Cdd:COG1061 379 LLRPTGS---PREF--IQRLGRGLRPAPGK 403
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
497-854 |
4.52e-08 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 58.78 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 497 ICAPTGAGKTNIAMltvLHEIRQHFQQGVI------KKNEFKIVYVAPMKALAAEMTDYFSRRLEPLG------------ 558
Cdd:PRK09751 1 VIAPTGSGKTLAAF---LYALDRLFREGGEdtreahKRKTSRILYISPIKALGTDVQRNLQIPLKGIAderrrrgetevn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 559 IIVKELTGDMQLS-KSEILRT--QMLVTTPEKWDVV----TRKSVGDVAlsqivrLLILDEVHLLH-EDRGPVLesivAR 630
Cdd:PRK09751 78 LRVGIRTGDTPAQeRSKLTRNppDILITTPESLYLMltsrARETLRGVE------TVIIDEVHAVAgSKRGAHL----AL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 631 TLRQVEST--QSMIRIlGLSATLPNYLDVATFLhvnpyiglfffdGRFRPV----PLGQTFLGIKCANKMQQLNNMDEVC 704
Cdd:PRK09751 148 SLERLDALlhTSAQRI-GLSATVRSASDVAAFL------------GGDRPVtvvnPPAMRHPQIRIVVPVANMDDVSSVA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 705 YE-------------------NVLKQVKAGHQVMVFVHARNATVRTAMSLIE--RAKNCGHIPFFFPTQGHDYVLA--EK 761
Cdd:PRK09751 215 SGtgedshagregsiwpyietGILDEVLRHRSTIVFTNSRGLAEKLTARLNElyAARLQRSPSIAVDAAHFESTSGatSN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 762 QVQRSRNKQVRElfpdgfsiHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIkgtQIYAAkrgsfvdL 841
Cdd:PRK09751 295 RVQSSDVFIARS--------HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVI---QVATP-------L 356
|
410
....*....|...
gi 158518649 842 GILDVMQIFGRAG 854
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 ... |
1344-1457 |
5.09e-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: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKYP---TSKAVYIAPLKALVRERMDDWKvRIEEKLGKKVIELTGDVTPDM---KS 1417
Cdd:cd17927 19 NTIICLPTGSGKTFVAVLICEHHLKKFPagrKGKVVFLANKVPLVEQQKEVFR-KHFERPGYKVTGLSGDTSENVsveQI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 158518649 1418 IAKADLIVTTP-------EKWDGVSRSwqnrnyvqQVTILIIDEIHL 1457
Cdd:cd17927 98 VESSDVIIVTPqilvndlKSGTIVSLS--------DFSLLVFDECHN 136
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1344-1456 |
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 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKvrieeKLGKKVIELTGDVTPDMKSIAK--A 1421
Cdd:pfam04851 25 RGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFK-----KFLPNYVEIGEIISGDKKDESVddN 99
|
90 100 110
....*....|....*....|....*....|....*
gi 158518649 1422 DLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIH 1456
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 ... |
491-651 |
1.17e-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: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 491 TNENMLICAPTGAGKTNIAMLTVLHEIRQhFQQGviKKNefKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQL 570
Cdd:cd18073 16 KGKNTIICAPTGCGKTFVSLLICEHHLKK-FPQG--QKG--KVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGATAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 571 SKSE---ILRTQMLVTTPEKwdVVTRKSVGDVALSQIVRLLILDEVHllHEDRGPVLESIVARTLRQ--VESTQSMIRIL 645
Cdd:cd18073 91 NVPVeqiIENNDIIILTPQI--LVNNLKKGTIPSLSIFTLMIFDECH--NTSGNHPYNMIMFRYLDQklGGSSGPLPQII 166
|
....*.
gi 158518649 646 GLSATL 651
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 ... |
440-658 |
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 158518649 440 EVRIPYS-EPMPLSFEEKPV-----YIQDLDEIGQLAFKGMKRlnriqsivfetayntNENMLICAPTGAGKTNIAMLTV 513
Cdd:cd18024 4 EVALPPDyDYTPISAHKPPGnpartYPFTLDPFQKTAIACIER---------------NESVLVSAHTSAGKTVVAEYAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 514 LHEIRqhfqqgvikkNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIvkelTGDMQLSKS--------EILRTqMLVTTP 585
Cdd:cd18024 69 AQSLR----------DKQRVIYTSPIKALSNQKYRELQEEFGDVGLM----TGDVTINPNasclvmttEILRS-MLYRGS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158518649 586 EkwdvVTRKsvgdvalsqiVRLLILDEVHLLHE-DRGPVLE-SIVArtlrqvesTQSMIRILGLSATLPNYLDVA 658
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 ... |
492-612 |
1.59e-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: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 492 NENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGvikknEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLS 571
Cdd:cd17957 27 GRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK-----GLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEAK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 158518649 572 KSE----ILRTQMLVTTPEKwdVVTRKSVGDVALSQiVRLLILDE 612
Cdd:cd17957 102 AKDgpksITKYDILVSTPLR--LVFLLKQGPIDLSS-VEYLVLDE 143
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
1349-1475 |
2.23e-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: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1349 APTGSGKTVAAELAIFRVFNKyptsKAVYIAPLKALVrermDDWKVRIEEKLGKKVI-ELTGDVTpdmKSIAKADLIVTT 1427
Cdd:cd17926 25 LPTGSGKTLTALALIAYLKEL----RTLIVVPTDALL----DQWKERFEDFLGDSSIgLIGGGKK---KDFDDANVVVAT 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 158518649 1428 PEkwdgvSRSWQN---RNYVQQVTILIIDEIHLLGeerGPVLEVIVSRTNF 1475
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 ... |
493-652 |
2.28e-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: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 493 ENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGvikkNEFKIVYVAPMKALAAEMTDYFSRRLEPlGIIVKELTGDMQLSK 572
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAG----EKGRVVVLVNKVPLVEQQLEKFFKYFRK-GYKVTGLSGDSSHKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 573 S---EILRTQMLVTTPEKWDVVTRKSVGDVALS-QIVRLLILDEVHllHEDRGPVLESIVARTLRQ-VESTQSMIRILGL 647
Cdd:cd18036 93 SfgqIVKASDVIICTPQILINNLLSGREEERVYlSDFSLLIFDECH--HTQKEHPYNKIMRMYLDKkLSSQGPLPQILGL 170
|
....*
gi 158518649 648 SATLP 652
Cdd:cd18036 171 TASPG 175
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
492-614 |
4.61e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.12 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 492 NENMLICAPTGAGKTNIAMLTVLHeirqhfqqgVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLS 571
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE---------RLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 158518649 572 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivrLLILDEVH 614
Cdd:COG1111 88 KRKELweKARIIVATPQviENDLIAgRIDLDDVS------LLIFDEAH 129
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
475-809 |
5.67e-07 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 54.70 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 475 KRLNRIQSIVFETAYNTNEN----MLICAPTGAGKTNIAMLTVLHEIRQHFQQGVIkknefkivYVAPMKAL----AAEM 546
Cdd:COG1203 126 TPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKHGGRRII--------YALPFTSIinqtYDRL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 547 TDYF--------SRRLEPLGIIVKELTGDMQLSK--SEILRTQMLVTTPekwD-----VVTRKSvgdvalSQIVRL---- 607
Cdd:COG1203 198 RDLFgedvllhhSLADLDLLEEEEEYESEARWLKllKELWDAPVVVTTI---DqlfesLFSNRK------GQERRLhnla 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 608 ---LILDEVHLL-HEDRGPVLesivaRTLRQVESTQSmiRILGLSATLPNYLDVATF------LHVNPYIGLFFFDGRFR 677
Cdd:COG1203 269 nsvIILDEVQAYpPYMLALLL-----RLLEWLKNLGG--SVILMTATLPPLLREELLeayeliPDEPEELPEYFRAFVRK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 678 PVplgqtflgikcanKMQQLNNMDEVCYENVLKQVKAGHQVMVFVharnATVRTAMSLierakncghipfffptqghdYv 757
Cdd:COG1203 342 RV-------------ELKEGPLSDEELAELILEALHKGKSVLVIV----NTVKDAQEL--------------------Y- 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 158518649 758 laekqvqrsrnKQVRELFPDGFSIH-HAGMLRQDRNLVEN----LFSNGHIKVLVCT 809
Cdd:COG1203 384 -----------EALKEKLPDEEVYLlHSRFCPADRSEIEKeikeRLERGKPCILVST 429
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
705-855 |
5.97e-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: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 705 YENVLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNcghipfffptqghdyvlaekqvqrsrnkqvrELFPDGFSIHHA 784
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPD-------------------------------RVPPDFIALHHG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158518649 785 GMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPA-HAVIikgtQIYAAKrgsfvdlGILDVMQIFGRAGR 855
Cdd:cd18796 77 SLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDvDLVI----QIGSPK-------SVARLLQRLGRSGH 137
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1300-1518 |
6.02e-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: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1300 TELLDLQPLPITALGCKAYEALYNF-----SHFNPVQTQIFHTLYHTDCN----VLLGAPTGSGKTVAAELAIFRVFNKY 1370
Cdd:COG1203 96 SANFDMARQALDHLLAERLERLLPKkskprTPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKH 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1371 PTSKAVYIAPLKALVrERMDDwkvRIEEKLGKKVIELTGDVTPDMKSIAK-----------------ADLIVTTPEK-WD 1432
Cdd:COG1203 176 GGRRIIYALPFTSII-NQTYD---RLRDLFGEDVLLHHSLADLDLLEEEEeyesearwlkllkelwdAPVVVTTIDQlFE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1433 GV--SRSWQNRNYVQQVT-ILIIDEIHLLGEERGPVLEvivsrtNFISSHTEKPVRIVgLSTA---------LANARDLA 1500
Cdd:COG1203 252 SLfsNRKGQERRLHNLANsVIILDEVQAYPPYMLALLL------RLLEWLKNLGGSVI-LMTAtlppllreeLLEAYELI 324
|
250
....*....|....*...
gi 158518649 1501 DWLNIKQMGLFNFRPSVR 1518
Cdd:COG1203 325 PDEPEELPEYFRAFVRKR 342
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
1344-1470 |
6.63e-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: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVR---ERMDDW--KVRIEEKLGkkviELTGDVTPDM--K 1416
Cdd:cd17930 3 LVILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINqmyERIREIlgRLDDEDKVL----LLHSKAALELleS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1417 SIAKADLIVTTPEKWDGVSRSWqNRNYVqqVT-------------------------ILIIDEIHLLGEER-GPVLEVIV 1470
Cdd:cd17930 79 DEEPDDDPVEAVDWALLLKRSW-LAPIV--VTtidqllesllkykhferrlhglansVVVLDEVQAYDPEYmALLLKALL 155
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
496-744 |
1.23e-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: 53.20 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 496 LICAPTGAGKTNIAMLTVLHEIRQhfqqgvikKNEFKIVYVAPMKALAAEMTDYFSRRL-EPLGIIVKELTGD--MQLSK 572
Cdd:cd09639 3 VIEAPTGYGKTEAALLWALHSLKS--------QKADRVIIALPTRATINAMYRRAKEAFgETGLYHSSILSSRikEMGDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 573 SEILR--------------TQMLVTTPEKWDVVTRKSVG--DVALSQIVR-LLILDEVHLLHEDrgpVLESIVA--RTLR 633
Cdd:cd09639 75 EEFEHlfplyihsndtlflDPITVCTIDQVLKSVFGEFGhyEFTLASIANsLLIFDEVHFYDEY---TLALILAvlEVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 634 QVEstqsmIRILGLSATLPNYLDvATFLHVNPYIGLFFFDGRFRpvplgQTFLGIKCANKMqqlnNMDEVCYENVLKQVK 713
Cdd:cd09639 152 DND-----VPILLMSATLPKFLK-EYAEKIGYVEENEPLDLKPN-----ERAPFIKIESDK----VGEISSLERLLEFIK 216
|
250 260 270
....*....|....*....|....*....|.
gi 158518649 714 AGHQVMVFVHarnaTVRTAMSLIERAKNCGH 744
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 ... |
481-650 |
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 158518649 481 QSIVFETAYNtneNMLICAPTGAGKTNIAMLTVLHEIRQhFQQGvikknefKIVYVAPMKALAAEMTDYFsrrLEPLGI- 559
Cdd:cd18033 8 FTIVQKALFQ---NTLVALPTGLGKTFIAAVVMLNYYRW-FPKG-------KIVFMAPTKPLVSQQIEAC---YKITGIp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 560 --IVKELTGDMQLSK-SEILRT-QMLVTTPEKwdVVTRKSVGDVALSQIVrLLILDEVhllHEDRGPVLESIVARTLRQV 635
Cdd:cd18033 74 ssQTAELTGSVPPTKrAELWASkRVFFLTPQT--LENDLKEGDCDPKSIV-CLVIDEA---HRATGNYAYCQVVRELMRY 147
|
170
....*....|....*
gi 158518649 636 ESTqsmIRILGLSAT 650
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 ... |
1327-1456 |
1.53e-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: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1327 FNPVQTQIFHtlyhtdcNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKvRIEEKLGKKVIE 1406
Cdd:cd18033 8 FTIVQKALFQ-------NTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACY-KITGIPSSQTAE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 158518649 1407 LTGDVTPDMKSI--AKADLIVTTPEKWDGVSRSwqNRNYVQQVTILIIDEIH 1456
Cdd:cd18033 80 LTGSVPPTKRAElwASKRVFFLTPQTLENDLKE--GDCDPKSIVCLVIDEAH 129
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
779-855 |
1.91e-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: 1.91e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158518649 779 FSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIkgtqiyaakrgSFVDLGILDVMQIFGRAGR 855
Cdd:pfam00271 41 VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----------YDLPWNPASYIQRIGRAGR 107
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
494-614 |
2.04e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 52.95 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 494 NMLICAPTGAGKTNIAMLTVLheirqhfqqGVIKKNEFKIVYVAPMKALAAEMTDYFSR--RLEPLGIIVkeLTGDMQLS 571
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIA---------ERLHKKGGKVLILAPTKPLVEQHAEFFRKflNIPEEKIVV--FTGEVSPE 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 158518649 572 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivrLLILDEVH 614
Cdd:PRK13766 100 KRAELweKAKVIVATPQviENDLIAgRISLEDVS------LLIFDEAH 141
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
1344-1456 |
2.28e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 52.81 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKyPTSKAVYIAPLKALVRERMDDWKvRIEEKLGKKVIELTGDVTPD--MKSIAKA 1421
Cdd:COG1111 19 NTLVVLPTGLGKTAVALLVIAERLHK-KGGKVLFLAPTKPLVEQHAEFFK-EALNIPEDEIVVFTGEVSPEkrKELWEKA 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 158518649 1422 DLIVTTPE--KWDGVSrswqNRNYVQQVTILIIDEIH 1456
Cdd:COG1111 97 RIIVATPQviENDLIA----GRIDLDDVSLLIFDEAH 129
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
493-661 |
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 158518649 493 ENMLICAPTGAGKTNIAMLTVlheirqhfqqGVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIvkelTGDMQLS- 571
Cdd:cd18027 24 DSVFVAAHTSAGKTVVAEYAI----------ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGLI----TGDVQLNp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 572 -------KSEILRTqMLVTTPEkwdvVTRKsvgdvalsqiVRLLILDEVHLLHE-DRGPVLESIVARTLRQVestqsmiR 643
Cdd:cd18027 90 easclimTTEILRS-MLYNGSD----VIRD----------LEWVIFDEVHYINDaERGVVWEEVLIMLPDHV-------S 147
|
170
....*....|....*...
gi 158518649 644 ILGLSATLPNYLDVATFL 661
Cdd:cd18027 148 IILLSATVPNTVEFADWI 165
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
493-656 |
2.99e-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: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 493 ENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGVIkknefkivYVAPMKALA----AEMTDYFSRRLEPLGII-------V 561
Cdd:cd17930 2 GLVILEAPTGSGKTEAALLWALKLAARGGKRRII--------YALPTRATInqmyERIREILGRLDDEDKVLllhskaaL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 562 KELTGDMQLSKSEILRTQMLVTTPEKWD---VVTrksVGDVAL-------SQIVRL-------LILDEVHLLhedrGPVL 624
Cdd:cd17930 74 ELLESDEEPDDDPVEAVDWALLLKRSWLapiVVT---TIDQLLesllkykHFERRLhglansvVVLDEVQAY----DPEY 146
|
170 180 190
....*....|....*....|....*....|..
gi 158518649 625 ESIVARTLRQVESTQSmIRILGLSATLPNYLD 656
Cdd:cd17930 147 MALLLKALLELLGELG-GPVVLMTATLPALLR 177
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
472-663 |
5.71e-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: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 472 KGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGVIKKNEFKIVYVAPMKALAAEMTDYFS 551
Cdd:cd17948 8 QGITKPTTVQKQGIPSILR-GRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNAPRGLVITPSRELAEQIGSVAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 552 RRLEPLGIIVKELTGDMqlSKSEILRTQM-----LVTTPEK-WDVVTRksvGDVALSQiVRLLILDEVH-LLHEDRGPVL 624
Cdd:cd17948 87 SLTEGLGLKVKVITGGR--TKRQIRNPHFeevdiLVATPGAlSKLLTS---RIYSLEQ-LRHLVLDEADtLLDDSFNEKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 158518649 625 ESIVART---LRQVESTQSMIR---ILGLSATLPNYL--------DVATFLHV 663
Cdd:cd17948 161 SHFLRRFplaSRRSENTDGLDPgtqLVLVSATMPSGVgevlskviDVDSIETV 213
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
1344-1496 |
6.21e-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: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRV-----FNKYPTSKAVYIAPLKALVRERMDdwkvRIEEKLGKKVIELTGDVTPDMKS- 1417
Cdd:cd18034 18 NTIVVLPTGSGKTLIAVMLIKEMgelnrKEKNPKKRAVFLVPTVPLVAQQAE----AIRSHTDLKVGEYSGEMGVDKWTk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1418 ------IAKADLIVTTPEkwdgVSRSWQNRNYVQ--QVTILIIDEIHLLGEERgpVLEVIVSRTNFISSHTEKPvRIVGL 1489
Cdd:cd18034 94 erwkeeLEKYDVLVMTAQ----ILLDALRHGFLSlsDINLLIFDECHHATGDH--PYARIMKEFYHLEGRTSRP-RILGL 166
|
....*..
gi 158518649 1490 STALANA 1496
Cdd:cd18034 167 TASPVNG 173
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
469-665 |
1.50e-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: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 469 LAFKGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTnIA-MLTVLHEIRqhfQQGVIKKNEFKIVYVAPMKALAAEMT 547
Cdd:cd00268 5 LKKLGFEKPTPIQAQAIPLILS-GRDVIGQAQTGSGKT-LAfLLPILEKLL---PEPKKKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 548 DYFSRRLEPLGIIVKELTGDMQLSKSEIL---RTQMLVTTPEK-WDVVTRksvGDVALSQiVRLLILDEV-HLLHEDRGP 622
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEAlkkGPDIVVGTPGRlLDLIER---GKLDLSN-VKYLVLDEAdRMLDMGFEE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 158518649 623 VLESIVARTLRQvesTQSMIrilgLSATLPNYLD--VATFLHvNP 665
Cdd:cd00268 156 DVEKILSALPKD---RQTLL----FSATLPEEVKelAKKFLK-NP 192
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
490-650 |
2.99e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.51 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 490 NTNENMLICAPTGAGKTniamLTVLHEIRQHFQQGVIKknefKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDmq 569
Cdd:pfam04851 21 NGQKRGLIVMATGSGKT----LTAAKLIARLFKKGPIK----KVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 570 lSKSEILRT-QMLVTTPEKWDVVTRKSVGDVALSQIVrLLILDEVHllhedRGPvlesivARTLRQVESTQSMIRILGLS 648
Cdd:pfam04851 91 -KKDESVDDnKIVVTTIQSLYKALELASLELLPDFFD-VIIIDEAH-----RSG------ASSYRNILEYFKPAFLLGLT 157
|
..
gi 158518649 649 AT 650
Cdd:pfam04851 158 AT 159
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
492-614 |
5.23e-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: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 492 NENMLICAPTGAGKTNIAMLTVLheirqhfqqGVIKKNEFKIVYVAPMKALAAEMTDYFsRRLEPLGIIVKELTGDMQLS 571
Cdd:cd18035 16 NGNTLIVLPTGLGKTIIAILVAA---------DRLTKKGGKVLILAPSRPLVEQHAENL-KRVLNIPDKITSLTGEVKPE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 158518649 572 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivrLLILDEVH 614
Cdd:cd18035 86 ERAERwdASKIIVATPQviENDLLAgRITLDDVS------LLIFDEAH 127
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
1344-1456 |
5.48e-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: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKYpTSKAVYIAPLKALVRERMDDWKVRIEEKLgkKVIELTGDVTPDMKS--IAKA 1421
Cdd:cd18035 18 NTLIVLPTGLGKTIIAILVAADRLTKK-GGKVLILAPSRPLVEQHAENLKRVLNIPD--KITSLTGEVKPEERAerWDAS 94
|
90 100 110
....*....|....*....|....*....|....*
gi 158518649 1422 DLIVTTPEKWDgvSRSWQNRNYVQQVTILIIDEIH 1456
Cdd:cd18035 95 KIIVATPQVIE--NDLLAGRITLDDVSLLIFDEAH 127
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
1344-1456 |
1.23e-04 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 47.18 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDDWK--VRIEEklgKKVIELTGDVTPD--MKSIA 1419
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIAERLHKKG-GKVLILAPTKPLVEQHAEFFRkfLNIPE---EKIVVFTGEVSPEkrAELWE 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 158518649 1420 KADLIVTTPE--KWDGVSrswqNRNYVQQVTILIIDEIH 1456
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 ... |
1549-1692 |
2.03e-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: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1549 IRSHSPAKPVLIFVSSRRQTrltaleliaflateedpkqwlnmderemENIIATVRDSNLKLTLAFGIGMHHAGLHERDR 1628
Cdd:cd18796 32 IFLLERHKSTLVFTNTRSQA----------------------------ERLAQRLRELCPDRVPPDFIALHHGSLSRELR 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158518649 1629 KTVEELFVNCKVQVLIATSTLAWGVNFPA-HLVIIKGTEYydgktrryvdfPITDVLQMMGRAGR 1692
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 ... |
1324-1456 |
7.01e-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: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1324 FSHFNPVQTQ-IFHTLYHTDCNVLLgaPTGSGKTVAAELAIFrVFNKyPTskaVYIAPLKALvrerMDDwKVRIEEKLGK 1402
Cdd:cd17920 10 YDEFRPGQLEaINAVLAGRDVLVVM--PTGGGKSLCYQLPAL-LLDG-VT---LVVSPLISL----MQD-QVDRLQQLGI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158518649 1403 KVIELTGDVTPDMKSIA-------KADLIVTTPEK--WDGVSRSWQNRNYVQQVTILIIDEIH 1456
Cdd:cd17920 78 RAAALNSTLSPEEKREVllrikngQYKLLYVTPERllSPDFLELLQRLPERKRLALIVVDEAH 140
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
473-652 |
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 158518649 473 GMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTnIAML--TVLHEIRQHFQQgviKKNEFKIVYVAPMKALAAEMTDYF 550
Cdd:cd17964 13 GFETMTPVQQKTLKPILSTGDDVLARAKTGTGKT-LAFLlpAIQSLLNTKPAG---RRSGVSALIISPTRELALQIAAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 551 SRRLEPL-GIIVKELTGDMQLSKSEI----LRTQMLVTTPEKW-DVVTRKSVGDVALSqiVRLLILDEV-HLLheDRG-- 621
Cdd:cd17964 89 KKLLQGLrKLRVQSAVGGTSRRAELNrlrrGRPDILVATPGRLiDHLENPGVAKAFTD--LDYLVLDEAdRLL--DMGfr 164
|
170 180 190
....*....|....*....|....*....|.
gi 158518649 622 PVLESIVaRTLRQVESTQsmIRILGLSATLP 652
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 ... |
486-651 |
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 158518649 486 ETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFQqgvikknefKIVYVAPMKALAAEMTDYFSR-RLEPLGIIVK-E 563
Cdd:cd17990 11 RAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGG---------KIIVLEPRRVAARAAARRLATlLGEAPGETVGyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 564 LTGDMQLSKseilRTQMLVTTPekwDVVTRKSVGDVALSQiVRLLILDEVHllheDRGPVLESIVARTLRQVESTQSMIR 643
Cdd:cd17990 82 VRGESRVGR----RTRVEVVTE---GVLLRRLQRDPELSG-VGAVILDEFH----ERSLDADLALALLLEVQQLLRDDLR 149
|
....*...
gi 158518649 644 ILGLSATL 651
Cdd:cd17990 150 LLAMSATL 157
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
1344-1456 |
1.41e-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: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1344 NVLLGAPTGSGKTVAAELAIFRVFNKYP----TSKAVYIAPLKALVRERMDDWKVRIEEklGKKVIELTGD--VTPDMKS 1417
Cdd:cd18036 19 NTIICAPTGSGKTRVAVYICRHHLEKRRsageKGRVVVLVNKVPLVEQQLEKFFKYFRK--GYKVTGLSGDssHKVSFGQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 158518649 1418 IAKA-DLIVTTPEKWDGVSRS--WQNRNYVQQVTILIIDEIH 1456
Cdd:cd18036 97 IVKAsDVIICTPQILINNLLSgrEEERVYLSDFSLLIFDECH 138
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
488-651 |
1.88e-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: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 488 AYNTNENMLICAPTGAGKTNIAMLtvlheirqhfqqgVIKKN-EFKIVYVAPMKALAAEMTDYFSRRLEPlgIIVKELTG 566
Cdd:cd17926 14 AHKNNRRGILVLPTGSGKTLTALA-------------LIAYLkELRTLIVVPTDALLDQWKERFEDFLGD--SSIGLIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 567 DmqlSKSEILRTQMLVTTPEK--WDVVTRKSVGDVALsqivrLLILDEVHllhedRGPvlesivARTLRQVESTQSMIRI 644
Cdd:cd17926 79 G---KKKDFDDANVVVATYQSlsNLAEEEKDLFDQFG-----LLIVDEAH-----HLP------AKTFSEILKELNAKYR 139
|
....*..
gi 158518649 645 LGLSATL 651
Cdd:cd17926 140 LGLTATP 146
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
1620-1692 |
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 158518649 1620 HAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-----AHLVIIKGTE-YYdgktrryvdfpitdvlQMMGRAGR 1692
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 ... |
1329-1454 |
2.15e-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: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1329 PVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIF---RVFNKYPTSKAVYIAPLKAL----VRErmddwKVRIEEKLG 1401
Cdd:cd17957 15 PIQMQAIPILLHGR-DLLACAPTGSGKTLAFLIPILqklGKPRKKKGLRALILAPTRELasqiYRE-----LLKLSKGTG 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158518649 1402 KKVIELTGDVTP----DMKSIAKADLIVTTPE------KWDGVSRSWqnrnyvqqVTILIIDE 1454
Cdd:cd17957 89 LRIVLLSKSLEAkakdGPKSITKYDILVSTPLrlvfllKQGPIDLSS--------VEYLVLDE 143
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
1322-1481 |
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 158518649 1322 YNFSHFNPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAV-YIAPLkALV----RERMDdwKVR- 1395
Cdd:cd17948 8 QGITKPTTVQKQGIPSILRGR-NTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpFNAPR-GLVitpsRELAE--QIGs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1396 ----IEEKLGKKVIELTGDVTpdMKSI-----AKADLIVTTPekwDGVSRSWQNRNY-VQQVTILIIDEIH-LLGEERGP 1464
Cdd:cd17948 84 vaqsLTEGLGLKVKVITGGRT--KRQIrnphfEEVDILVATP---GALSKLLTSRIYsLEQLRHLVLDEADtLLDDSFNE 158
|
170
....*....|....*..
gi 158518649 1465 VLEVIVSRTNFISSHTE 1481
Cdd:cd17948 159 KLSHFLRRFPLASRRSE 175
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
481-615 |
6.11e-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: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 481 QSIVFETAYNTNEN-MLICAPTGAGKTNIAMLTVLHEirqhfqqgvikknEFKIVYVAPMKALA-------AEMTDYFSR 552
Cdd:cd09710 2 QVATFEALQSKDADiIFNTAPTGAGKTLAWLTPLLHG-------------ENKAIALYPTNALIedqteaiKEFVDDANP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 553 RLEPLGIIVKELT-----GDMQLSKSEIL-----------RTQMLVTTPEKWDVVTR-----KSVGDVALSQIVRLLILD 611
Cdd:cd09710 69 RHQVKSLSASDITlwpndKNVGSSKGEKLynllrndigtsTPIILLTNPDIFVYLTRfayidRGDIAAGFYTKFSTVIFD 148
|
....
gi 158518649 612 EVHL 615
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 ... |
1642-1692 |
6.66e-03 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350192 [Multi-domain] Cd Length: 135 Bit Score: 39.08 E-value: 6.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 158518649 1642 VLIATSTLAWGVNFPAHLVIIKGTEYYDGKTRRyvDFPITDVLQMMGRAGR 1692
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 ... |
1323-1428 |
9.29e-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: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158518649 1323 NFSHFNPVQTQIFHTLYHTD--------CNVLLGAPTGSGKTVAAELAIFRVFNKYPTSK--AVYIAPLKAL---VRERM 1389
Cdd:cd17956 9 GITSAFPVQAAVIPWLLPSSkstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRlrALIVVPTKELvqqVYKVF 88
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 158518649 1390 DdwkvRIEEKLGKKVIELTG--DVTPDMKSIA---------KADLIVTTP 1428
Cdd:cd17956 89 E----SLCKGTGLKVVSLSGqkSFKKEQKLLLvdtsgrylsRVDILVATP 134
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