|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1228-1416 |
3.25e-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: 416.77 E-value: 3.25e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1228 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLGKKVI 1307
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1308 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKPVR 1387
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*....
gi 2462605685 1388 IVGLSTALANARDLADWLNIKQMGLFNFR 1416
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
378-575 |
7.47e-125 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350778 [Multi-domain] Cd Length: 199 Bit Score: 390.64 E-value: 7.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 378 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFQQ-GVIKKNEFKIVYVAPMKALAAEMTDYFSRRL 456
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 457 EPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDVALSQIVRLLILDEVHLLHEDRGPVLESIVARTLRQ 536
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462605685 537 VESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFFFD 575
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
880-1188 |
1.81e-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: 394.26 E-value: 1.81e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 880 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNfCELSTPGGVENSYGKI 959
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEK-VPIPVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 960 NILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSILPPHI 1039
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1040 LTRLEEKKLTV--DKLKDMRKDEIGHILHHVNIGLKVKQCVHQIPSVMMEASIQPITRTVLRVTLSIYADFTWNDQVHGT 1117
Cdd:pfam02889 160 IKKLEKKGVESvrDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462605685 1118 VgEPWWIWVEDPTNDHIYHSEYFLALKKQVISkeAQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIIN 1188
Cdd:pfam02889 240 S-EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
877-1190 |
2.55e-113 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 362.73 E-value: 2.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 877 YFSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNFCELSTPGGVENSY 956
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 957 GKINILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSILP 1036
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1037 PHILTRLEEKK-LTVDKLKDMRKDEIGHILHHVN-IGLKVKQCVHQIPSVMMEASIQPITRTVLRVTLSIYADFTWNDQV 1114
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLGLLDaEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462605685 1115 HGTVgEPWWIWVEDPTNDHIYHSEYFLALKKQVIskEAQLLVFTIPIFEPLPsQYYIRAVSDRWLGAEAVCIINFQ 1190
Cdd:smart00611 241 HGKQ-EGWWLVIGDSDGNELLHIERFSLNKKNVS--EEVKLDFTAPATEGNY-QYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1711-2080 |
6.68e-101 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 326.91 E-value: 6.68e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1711 SIEPLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPHSFDSPH 1790
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1791 TKAHLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWLKDSSLLTLPNIE 1870
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1871 NHHLHLFKKWKpimkgphargRTSIECLPELIHAcgGKDHVFSSMVeselhaAKTKQAWNFLSHLPVINVGISVKGSwDD 1950
Cdd:smart00611 161 EEILKRLEKKK----------VLSLEDLLELEDE--ERGELLGLLD------AEGERVYKVLSRLPKLNIEISLEPI-TR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1951 LVEGHNELSVSTLTADKRDDnkwiklhadqeyvlqvslqrvhfgfhkgkpescavtprfpkSKDEGWFLILGEVDKRELI 2030
Cdd:smart00611 222 TVLGVEVTLTVDLTWDDEIH-----------------------------------------GKQEGWWLVIGDSDGNELL 260
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2462605685 2031 ALKRVGYIRNH--HVASLSFYTPEIPGRYIYTLYFMSDCYLGLDQQYDIYLN 2080
Cdd:smart00611 261 HIERFSLNKKNvsEEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1229-1751 |
5.85e-96 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 321.46 E-value: 5.85e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1229 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKVRIEEkLGKKVIE 1308
Cdd:COG1204 23 LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEE-LGIKVGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1309 LTGDVTPDMKSIAKADLIVTTPEKWDGVSRswQNRNYVQQVTILIIDEIHLLG-EERGPVLEVIVSRtnfiSSHTEKPVR 1387
Cdd:COG1204 100 STGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTLEVLLAR----LRRLNPEAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1388 IVGLSTALANARDLADWLNIKqmglfNFRPSVRPVPLE--VHIQG---FPGQHYCPRmasmnKPAFQAIRSHSPA-KPVL 1461
Cdd:COG1204 174 IVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSK-----DPTLALALDLLEEgGQVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1462 IFVSSRRQTRLTALELIAFLA---TEEDPKQWLNMDEREMEniIATVRDSNLKLT--LAFGIGMHHAGLHERDRKTVEEL 1536
Cdd:COG1204 244 VFVSSRRDAESLAKKLADELKrrlTPEEREELEELAEELLE--VSEETHTNEKLAdcLEKGVAFHHAGLPSELRRLVEDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1537 FVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGktrryVDFPITDVLQMMGRAGRPQFDDQGKAVILVHDIK---KD 1613
Cdd:COG1204 322 FREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDeadEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1614 FYKKFLYEPFPVESSLLGVLSD--HLNAEIAGGTITSKQDALDYITWTYFFRRlimnPSYYNLGDVshdsVNKFLSHLIE 1691
Cdd:COG1204 397 FERYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQ----YDKGDLEEV----VDDALEFLLE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462605685 1692 KSLIElelsycieigEDNRSIEPLTYGRIASYYYLKHQTVKMFKDRLK---PECSTEELLSIL 1751
Cdd:COG1204 469 NGFIE----------EDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadEEFTDLGLLHLI 521
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
362-917 |
4.81e-94 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 315.68 E-value: 4.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 362 IQDLDE---IGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFqqgvikknefKIVYV 438
Cdd:COG1204 3 VAELPLekvIEFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 439 APMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGdvALSQIvRLLILDEVHLL 518
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDV-DLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 519 H-EDRGPVLESIVARtLRQVESTqsmIRILGLSATLPNYLDVATFLHVNPyiglffFDGRFRPVPLgqtFLGIKCANKmq 597
Cdd:COG1204 150 DdESRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGV-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 598 qlNNMDEVCYEN-------VLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNCGHIPFFFPTQGHDYVLAEKQVQRSRN 670
Cdd:COG1204 215 --LRFDDGSRRSkdptlalALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 671 KQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTqiyaaKRGSFVDLGILDVMQ 750
Cdd:COG1204 293 EKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-----KRGGMVPIPVLEFKQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 751 IFGRAGRPQFDKFGEGIIIT-THDKLSH--YLTLLTQRNPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWISYTYLY 825
Cdd:COG1204 368 MAGRAGRPGYDPYGEAILVAkSSDEADElfERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTFYA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 826 VRMRANPLaygishkayqidptlrkhrEQLVIEVGRKLDKAQMIrfEERTGYFSSTDLGRTASHYYIKYNTIETFNELFD 905
Cdd:COG1204 448 YQYDKGDL-------------------EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAELVDGLR 506
|
570
....*....|..
gi 2462605685 906 AHKTEGDIFAIV 917
Cdd:COG1204 507 KADEEFTDLGLL 518
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1714-2077 |
5.10e-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: 238.25 E-value: 5.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1714 PLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPhSFDSPHTKA 1793
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKG-DIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1794 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWLKDSSLLTLPNIENHH 1873
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1874 LHLFKKwkpimkgphaRGRTSIECL-----PELIHACGGKDHVFssmveselhaaktKQAWNFLSHLPVINVgisvkgsw 1948
Cdd:pfam02889 160 IKKLEK----------KGVESVRDIlelddAEELGELIRNPKMG-------------KDIAQFVNRFPKIEI-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1949 ddlveghnELSVSTLTADkrddnkwiklhadqeyVLQVSLQrvhfgfhkgkpescaVTPRFPKSKD-----EGWFLILGE 2023
Cdd:pfam02889 209 --------EAEVQPITRS----------------VLRVEVT---------------ITPDFPWDKRvhgksEGFWLVVGD 249
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605685 2024 VDKRELIALKRV--GYIRNHHVASLSFYTPEI-PGRYIYTLYFMSDCYLGLDQQYDI 2077
Cdd:pfam02889 250 SDGNEILHIERFtlTKRTLAGEHKLEFTVPPSdPGPPQLFVRLISDSWLGADQEVPI 306
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1420-1608 |
2.03e-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: 2.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1420 RPVPLEVHIQGFPGQHYCPRMASMNK-----PAFQAIRSHSPAKPVLIFVSSRRQTRLTALELIaflateedpkqwlnmd 1494
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1495 eremeniiatvrdsnlkltlafGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKT 1574
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 2462605685 1575 RRYvdFPITDVLQMMGRAGRPQFDDQGKAVILVH 1608
Cdd:cd18795 123 YRE--LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1246-1774 |
2.86e-61 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 225.47 E-value: 2.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFrvfNKYPTS--KAVYIAPLKALVRER---MDDWkvrieEKLGKKVIELTGDVTPDMKSI 1320
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMV---NKLLREggKAVYLVPLKALAEEKyreFKDW-----EKLGLRVAMTTGDYDSTDEWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1321 AKADLIVTTPEKWDGVSR---SWqnrnyVQQVTILIIDEIHLLGE-ERGPVLEVIVSrtnfissHTEKPVRIVGLSTALA 1396
Cdd:PRK00254 113 GKYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSyDRGATLEMILT-------HMLGRAQILGLSATVG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1397 NARDLADWLNIKQMglfnfRPSVRPVPLE--VHIQGF------PGQHYcprMASMNKPAFQAIRShspAKPVLIFVSSRR 1468
Cdd:PRK00254 181 NAEELAEWLNAELV-----VSDWRPVKLRkgVFYQGFlfwedgKIERF---PNSWESLVYDAVKK---GKGALVFVNTRR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1469 QTRLTALELIAFLATEEDPKQwlnmdEREMENIIATVRD--SNLKLTLAF--GIGMHHAGLHERDRKTVEELFVNCKVQV 1544
Cdd:PRK00254 250 SAEKEALELAKKIKRFLTKPE-----LRALKELADSLEEnpTNEKLKKALrgGVAFHHAGLGRTERVLIEDAFREGLIKV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1545 LIATSTLAWGVNFPAHLVIIKGTEYYDGKTrrYVDFPITDVLQMMGRAGRPQFDDQGKAVILVH-DIKKDFYKKF----- 1618
Cdd:PRK00254 325 ITATPTLSAGINLPAFRVIIRDTKRYSNFG--WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERYifgkp 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1619 --LYEPFPVESSLLGvlsdHLNAEIAGGTITSKQDALDYITWTYFfrrlimnpsYYNLGDVSH--DSVNKFLSHLIEKSL 1694
Cdd:PRK00254 403 ekLFSMLSNESAFRS----QVLALITNFGVSNFKELVNFLERTFY---------AHQRKDLYSleEKAKEIVYFLLENEF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1695 IELELsycieigEDNrsIEPLTYGRIASYYYLKHQTVKMFKDRLkPECSTEE----LLSILSDAEEYTDLPVRHNEDHMN 1770
Cdd:PRK00254 470 IDIDL-------EDR--FIPLPLGIRTSQLYIDPLTAKKFKDAF-PKIEKNPnplgIFQLIASTPDMTPLNYSRKEMEDL 539
|
....
gi 2462605685 1771 SELA 1774
Cdd:PRK00254 540 LDEA 543
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
395-936 |
2.59e-53 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 201.20 E-value: 2.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 395 ENMLICAPTGAGKTNIAMLTVLHEIrqhFQQGvikkneFKIVYVAPMKALAAEMTDYFsRRLEPLGIIVKELTGDMQlSK 474
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKL---LREG------GKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYD-ST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 475 SEIL-RTQMLVTTPEKWDVVTRKSVgdvalSQI--VRLLILDEVHLL-HEDRGPVLESIVARTLRQVEstqsmirILGLS 550
Cdd:PRK00254 109 DEWLgKYDIIIATAEKFDSLLRHGS-----SWIkdVKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ-------ILGLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 551 ATLPNYLDVATFLHVNpyigLFFFDgrFRPVPL-----GQTFLGIKCANKMQQLNNMDEVCYEnvlkQVKAGHQVMVFVH 625
Cdd:PRK00254 177 ATVGNAEELAEWLNAE----LVVSD--WRPVKLrkgvfYQGFLFWEDGKIERFPNSWESLVYD----AVKKGKGALVFVN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 626 ARNATVRTAMSLIERAKNCghipFFFPTQGHDYVLAEKQVQRSRNKQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHI 705
Cdd:PRK00254 247 TRRSAEKEALELAKKIKRF----LTKPELRALKELADSLEENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 706 KVLVCTATLAWGVNLPAHAVIIKGTQIYAakRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDK----LSHYL-- 779
Cdd:PRK00254 323 KVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklMERYIfg 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 780 ------TLLTQRNPIESQFLesladnlnAEIALGTVTNVEEAVKWISYTYlYVRMRANPlaYGISHKAYQIDPTLrkhRE 853
Cdd:PRK00254 401 kpeklfSMLSNESAFRSQVL--------ALITNFGVSNFKELVNFLERTF-YAHQRKDL--YSLEEKAKEIVYFL---LE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 854 QLVIEvgrkldkaqmIRFEERtgyFSSTDLGRTASHYYIKYNTIETFNELFDahKTEGD-----IFAIVSKAEEFDQIKV 928
Cdd:PRK00254 467 NEFID----------IDLEDR---FIPLPLGIRTSQLYIDPLTAKKFKDAFP--KIEKNpnplgIFQLIASTPDMTPLNY 531
|
....*...
gi 2462605685 929 REEEIEEL 936
Cdd:PRK00254 532 SRKEMEDL 539
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
579-771 |
9.22e-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: 9.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 579 RPVPLGQTFLGIK----CANKMQQLNNMDEVCYENVLKQVKAGHQVMVFVHARNATVRTAMSLIerakncghipfffptq 654
Cdd:cd18795 1 RPVPLEEYVLGFNglgiKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 655 ghdyvlaekqvqrsrnkqvrelfpdGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYA 734
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462605685 735 AKRgsFVDLGILDVMQIFGRAGRPQFDKFGEGIIITT 771
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
380-558 |
1.12e-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: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 380 NRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQhfqqgviKKNEFKIVYVAPMKALAAEMTDYFSRRLEPL 459
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK-------LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 460 GIIVKELTGDMQLSK--SEILRTQMLVTTPEKWDVVTRKSvgdVALSQiVRLLILDEVHLLHE-DRGPVLESIVARtlrq 536
Cdd:pfam00270 73 GLKVASLLGGDSRKEqlEKLKGPDILVGTPGRLLDLLQER---KLLKN-LKLLVLDEAHRLLDmGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|..
gi 2462605685 537 vesTQSMIRILGLSATLPNYLD 558
Cdd:pfam00270 145 ---LPKKRQILLLSATLPRNLE 163
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1230-1401 |
1.54e-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: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1230 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFN-KYPTSKAVYIAPLKALVRERMDDWKVRIeEKLGKKVIE 1308
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDkLDNGPQALVLAPTRELAEQIYEELKKLG-KGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1309 LTGDVTP--DMKSIAKADLIVTTPEKWDGVsrsWQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNfisshteKP 1385
Cdd:pfam00270 79 LLGGDSRkeQLEKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRRLP-------KK 148
|
170
....*....|....*..
gi 2462605685 1386 VRIVGLS-TALANARDL 1401
Cdd:pfam00270 149 RQILLLSaTLPRNLEDL 165
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1231-1607 |
5.37e-26 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 116.91 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1231 PVQT-QIFHTLYHTDcNVLLGAPTGSGKTVAAELA-IFRVFNKypTSKAVYIAPLKALVRERMDDWKVRIEEKLgkKVIE 1308
Cdd:COG1202 212 PVQSlAVENGLLEGK-DQLVVSATATGKTLIGELAgIKNALEG--KGKMLFLVPLVALANQKYEDFKDRYGDGL--DVSI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1309 LTGDV---TPDMKSIAKADLIVTTPEKWDGVSRSwqnRNYVQQVTILIIDEIHLLGE-ERGPVLEVIVSRTNFISSHTEk 1384
Cdd:COG1202 287 RVGASrirDDGTRFDPNADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEVHMLEDpERGHRLDGLIARLKYYCPGAQ- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1385 pvrIVGLSTALANARDLADWLNIKQMgLFNfrpsVRPVPLEVHIQGFPGQHYCPRMASMNKPAFQAIRSHSPAKPVLIFV 1464
Cdd:COG1202 363 ---WIYLSATVGNPEELAKKLGAKLV-EYE----ERPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1465 SSRRQTRltaleliaflateedpkqwlnmderemeniiatvrdsnlKLTLAFGIGM--HHAGLHERDRKTVEELFVNCKV 1542
Cdd:COG1202 435 NSRRRCH---------------------------------------EIARALGYKAapYHAGLDYGERKKVERRFADQEL 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462605685 1543 QVLIATSTLAWGVNFPAHLVIIK----GTEYydgktrryvdFPITDVLQMMGRAGRPQFDDQGKAVILV 1607
Cdd:COG1202 476 AAVVTTAALAAGVDFPASQVIFDslamGIEW----------LSVQEFHQMLGRAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
371-582 |
8.27e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.81 E-value: 8.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 371 LAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRqhfqqgviKKNEFKIVYVAPMKALAAEMTD 450
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALK--------RGKGGRVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 451 YFSRRLEPLGIIVKELTGD----MQLSKSEILRTQMLVTTPEKWDVVTRKsvGDVALSQiVRLLILDEVH-LLHEDRGPV 525
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRLLDLLEN--DKLSLSN-VDLVILDEAHrLLDGGFGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605685 526 LESIVARTLRqvestqsMIRILGLSATLPNYLDVATFLHVNpyiGLFFFDGRFRPVP 582
Cdd:smart00487 150 LEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1224-1423 |
9.89e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 103.73 E-value: 9.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1224 YNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLG 1303
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1304 KKVIELTGDVT-PDMKSIAK--ADLIVTTPEKWDGVSRswQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNfis 1379
Cdd:smart00487 84 KVVGLYGGDSKrEQLRKLESgkTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462605685 1380 shteKPVRIVGLS-TALANARDLADWLNIkqmGLFNFRPSVRPVP 1423
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 ... |
1248-1563 |
8.27e-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: 8.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1248 LLGAPTGSGKTVAAELAIFRVFNKYPTSK-----AVYIAPLKALVRErmddwkvrIEEKLGKKVIEL---------TGDV 1313
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKekglhTLYITPLRALAVD--------IARNLQAPIEELglpirvetrTGDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1314 TPDMKSIAKA---DLIVTTPEkwdgvsrSWQ-------NRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNFISSHt 1382
Cdd:TIGR04121 104 SSSERARQRKkppDILLTTPE-------SLAlllsypdAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1383 ekpVRIVGLSTALANARDLADWLnikqMGLFNFRPSV------RPVPLEV----HIQGFP-GQHYCPRMASmnkPAFQAI 1451
Cdd:TIGR04121 176 ---LRRWGLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISllpeSEERFPwAGHLGLRALP---EVYAEI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1452 RSHspaKPVLIFVSSRRQTRLTALELIAFLAteedpkqwlnmderemeniiatvrDSNLKltlafgIGMHHAGLHERDRK 1531
Cdd:TIGR04121 246 DQA---RTTLVFTNTRSQAELWFQALWEANP------------------------EFALP------IALHHGSLDREQRR 292
|
330 340 350
....*....|....*....|....*....|...
gi 2462605685 1532 TVEELFVNCKVQVLIATSTLAWGVNF-PAHLVI 1563
Cdd:TIGR04121 293 WVEAAMAAGRLRAVVCTSSLDLGVDFgPVDLVI 325
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
390-758 |
5.33e-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: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 390 AYNTNENMLICAPTGAGKTNIAMLTVLheIRQHFQQGViKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVK-EL-T 467
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSL--IDLAGPEAP-KEKGLHTLYITPLRALAVDIARNLQAPIEELGLPIRvETrT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 468 GDMQLSKSEILRTQM---LVTTPEKWDVVTrkSVGDVA-LSQIVRLLILDEVH-LLHEDRGPVLESIVARtLRQvesTQS 542
Cdd:TIGR04121 101 GDTSSSERARQRKKPpdiLLTTPESLALLL--SYPDAArLFKDLRCVVVDEWHeLAGSKRGDQLELALAR-LRR---LAP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 543 MIRILGLSATLPNyLDVA--TFLHVNPYIGLFFFDGRFRPVPL-------GQTF-----LGIKCAnkmqqlnnmdevcyE 608
Cdd:TIGR04121 175 GLRRWGLSATIGN-LEEArrVLLGVGGAPAVLVRGKLPKAIEVisllpesEERFpwaghLGLRAL--------------P 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 609 NVLKQVKAGHQVMVFVHARNATVRTAMSLIErakncghipfffptqghdyvlaekqvqrsrnkqVRELFPDGFSIHHAGM 688
Cdd:TIGR04121 240 EVYAEIDQARTTLVFTNTRSQAELWFQALWE---------------------------------ANPEFALPIALHHGSL 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462605685 689 LRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIkgtQIYAAKrgsfvdlGILDVMQIFGRAG-RP 758
Cdd:TIGR04121 287 DREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSPK-------GVARLLQRAGRSNhRP 347
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1516-1595 |
1.03e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 71.09 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1516 FGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryVDFPITDVLQMMGRAGR 1594
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVII-----YD------LPWSPASYIQRIGRAGR 80
|
.
gi 2462605685 1595 P 1595
Cdd:smart00490 81 A 81
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
680-758 |
8.20e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 65.70 E-value: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 680 GFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIKGtqiyaakrgsfVDLGILDVMQIFGRAGRP 758
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-----------LPWSPASYIQRIGRAGRA 81
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
394-721 |
5.82e-11 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 67.99 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 394 NENMLICAPTGAGKTNIAMLTVLHEIrqhFQQGVIKKNEFKI--VYVAPMKALAAEMtdyfsRR--LEPLGIIVKEL--- 466
Cdd:PRK13767 47 GKNVLISSPTGSGKTLAAFLAIIDEL---FRLGREGELEDKVycLYVSPLRALNNDI-----HRnlEEPLTEIREIAker 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 467 ------------TGDM-QLSKSEILRT--QMLVTTPEKWDVVT-----RKSVGDvalsqiVRLLILDEVHLLHED-RGPV 525
Cdd:PRK13767 119 geelpeirvairTGDTsSYEKQKMLKKppHILITTPESLAILLnspkfREKLRT------VKWVIVDEIHSLAENkRGVH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 526 LesivARTLRQVES--TQSMIRIlGLSATLPNYLDVATFLhvnpyiGLFFFDGRFRPVPLGQT-F---LGIKCANKMQQL 599
Cdd:PRK13767 193 L----SLSLERLEElaGGEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDCEIVDArFvkpFDIKVISPVDDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 600 -----NNMDEVCYENVLKQVKAGHQVMVFVHARNATVRTAMSLierakncghipfffptqghdyvlaekqvqrsrnkqvR 674
Cdd:PRK13767 262 ihtpaEEISEALYETLHELIKEHRTTLIFTNTRSGAERVLYNL------------------------------------R 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2462605685 675 ELFPDGFSI-----HHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP 721
Cdd:PRK13767 306 KRFPEEYDEdnigaHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG 357
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1500-1594 |
4.11e-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: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1500 NIIATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryV 1578
Cdd:pfam00271 23 QTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YD------L 91
|
90
....*....|....*.
gi 2462605685 1579 DFPITDVLQMMGRAGR 1594
Cdd:pfam00271 92 PWNPASYIQRIGRAGR 107
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1226-1392 |
1.15e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 63.75 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1226 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAI----FRVFNK-------YptskAVYIAPLKAL---VRERM 1291
Cdd:PRK13767 30 FGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREgeledkvY----CLYVSPLRALnndIHRNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1292 DDWKVRIEEKLGKKVIEL--------TGDVTPDMKS--------IakadLIvTTPEKWDGVSRSWQNRNYVQQVTILIID 1355
Cdd:PRK13767 105 EEPLTEIREIAKERGEELpeirvairTGDTSSYEKQkmlkkpphI----LI-TTPESLAILLNSPKFREKLRTVKWVIVD 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462605685 1356 EIHLLGE-ERGPVLEVIVSRTNFISSHteKPVRIvGLS 1392
Cdd:PRK13767 180 EIHSLAEnKRGVHLSLSLERLEELAGG--EFVRI-GLS 214
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
394-516 |
3.64e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.51 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 394 NENMLICAPTGAGKTNIAMLTVLHeirqhfqqgVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLS 473
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE---------RLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462605685 474 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivrLLILDEVH 516
Cdd:COG1111 88 KRKELweKARIIVATPQviENDLIAgRIDLDDVS------LLIFDEAH 129
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
681-757 |
1.71e-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: 1.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462605685 681 FSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIkgtqiyaakrgSFVDLGILDVMQIFGRAGR 757
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; ... |
1228-1416 |
3.25e-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: 416.77 E-value: 3.25e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1228 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLGKKVI 1307
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1308 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKPVR 1387
Cdd:cd18022 81 ELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPVR 160
|
170 180
....*....|....*....|....*....
gi 2462605685 1388 IVGLSTALANARDLADWLNIKQMGLFNFR 1416
Cdd:cd18022 161 LVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
378-575 |
7.47e-125 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350778 [Multi-domain] Cd Length: 199 Bit Score: 390.64 E-value: 7.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 378 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFQQ-GVIKKNEFKIVYVAPMKALAAEMTDYFSRRL 456
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 457 EPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDVALSQIVRLLILDEVHLLHEDRGPVLESIVARTLRQ 536
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462605685 537 VESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFFFD 575
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
880-1188 |
1.81e-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: 394.26 E-value: 1.81e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 880 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNfCELSTPGGVENSYGKI 959
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEK-VPIPVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 960 NILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSILPPHI 1039
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1040 LTRLEEKKLTV--DKLKDMRKDEIGHILHHVNIGLKVKQCVHQIPSVMMEASIQPITRTVLRVTLSIYADFTWNDQVHGT 1117
Cdd:pfam02889 160 IKKLEKKGVESvrDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462605685 1118 VgEPWWIWVEDPTNDHIYHSEYFLALKKQVISkeAQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIIN 1188
Cdd:pfam02889 240 S-EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
877-1190 |
2.55e-113 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 362.73 E-value: 2.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 877 YFSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNFCELSTPGGVENSY 956
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 957 GKINILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSILP 1036
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1037 PHILTRLEEKK-LTVDKLKDMRKDEIGHILHHVN-IGLKVKQCVHQIPSVMMEASIQPITRTVLRVTLSIYADFTWNDQV 1114
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLGLLDaEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462605685 1115 HGTVgEPWWIWVEDPTNDHIYHSEYFLALKKQVIskEAQLLVFTIPIFEPLPsQYYIRAVSDRWLGAEAVCIINFQ 1190
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 ... |
362-575 |
2.37e-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: 2.37e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 362 IQDLDEIGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHF-QQGVIKKNEFKIVYVAP 440
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRnPDGTINLDAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 441 MKALAAEMTDYFSRRLEPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSvGDVALSQIVRLLILDEVHLLHE 520
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKS-GDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462605685 521 DRGPVLESIVARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFFFD 575
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1711-2080 |
6.68e-101 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 326.91 E-value: 6.68e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1711 SIEPLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPHSFDSPH 1790
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1791 TKAHLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWLKDSSLLTLPNIE 1870
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1871 NHHLHLFKKWKpimkgphargRTSIECLPELIHAcgGKDHVFSSMVeselhaAKTKQAWNFLSHLPVINVGISVKGSwDD 1950
Cdd:smart00611 161 EEILKRLEKKK----------VLSLEDLLELEDE--ERGELLGLLD------AEGERVYKVLSRLPKLNIEISLEPI-TR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1951 LVEGHNELSVSTLTADKRDDnkwiklhadqeyvlqvslqrvhfgfhkgkpescavtprfpkSKDEGWFLILGEVDKRELI 2030
Cdd:smart00611 222 TVLGVEVTLTVDLTWDDEIH-----------------------------------------GKQEGWWLVIGDSDGNELL 260
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2462605685 2031 ALKRVGYIRNH--HVASLSFYTPEIPGRYIYTLYFMSDCYLGLDQQYDIYLN 2080
Cdd:smart00611 261 HIERFSLNKKNvsEEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1229-1751 |
5.85e-96 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 321.46 E-value: 5.85e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1229 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKVRIEEkLGKKVIE 1308
Cdd:COG1204 23 LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDFEE-LGIKVGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1309 LTGDVTPDMKSIAKADLIVTTPEKWDGVSRswQNRNYVQQVTILIIDEIHLLG-EERGPVLEVIVSRtnfiSSHTEKPVR 1387
Cdd:COG1204 100 STGDYDSDDEWLGRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTLEVLLAR----LRRLNPEAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1388 IVGLSTALANARDLADWLNIKqmglfNFRPSVRPVPLE--VHIQG---FPGQHYCPRmasmnKPAFQAIRSHSPA-KPVL 1461
Cdd:COG1204 174 IVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSK-----DPTLALALDLLEEgGQVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1462 IFVSSRRQTRLTALELIAFLA---TEEDPKQWLNMDEREMEniIATVRDSNLKLT--LAFGIGMHHAGLHERDRKTVEEL 1536
Cdd:COG1204 244 VFVSSRRDAESLAKKLADELKrrlTPEEREELEELAEELLE--VSEETHTNEKLAdcLEKGVAFHHAGLPSELRRLVEDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1537 FVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGktrryVDFPITDVLQMMGRAGRPQFDDQGKAVILVHDIK---KD 1613
Cdd:COG1204 322 FREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDeadEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1614 FYKKFLYEPFPVESSLLGVLSD--HLNAEIAGGTITSKQDALDYITWTYFFRRlimnPSYYNLGDVshdsVNKFLSHLIE 1691
Cdd:COG1204 397 FERYILGEPEPIRSKLANESALrtHLLALIASGFANSREELLDFLENTFYAYQ----YDKGDLEEV----VDDALEFLLE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462605685 1692 KSLIElelsycieigEDNRSIEPLTYGRIASYYYLKHQTVKMFKDRLK---PECSTEELLSIL 1751
Cdd:COG1204 469 NGFIE----------EDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadEEFTDLGLLHLI 521
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
362-917 |
4.81e-94 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 315.68 E-value: 4.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 362 IQDLDE---IGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFqqgvikknefKIVYV 438
Cdd:COG1204 3 VAELPLekvIEFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----------KALYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 439 APMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGdvALSQIvRLLILDEVHLL 518
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS--WLRDV-DLVVVDEAHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 519 H-EDRGPVLESIVARtLRQVESTqsmIRILGLSATLPNYLDVATFLHVNPyiglffFDGRFRPVPLgqtFLGIKCANKmq 597
Cdd:COG1204 150 DdESRGPTLEVLLAR-LRRLNPE---AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPL---NEGVLYDGV-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 598 qlNNMDEVCYEN-------VLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNCGHIPFFFPTQGHDYVLAEKQVQRSRN 670
Cdd:COG1204 215 --LRFDDGSRRSkdptlalALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLEVSEETHTN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 671 KQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTqiyaaKRGSFVDLGILDVMQ 750
Cdd:COG1204 293 EKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-----KRGGMVPIPVLEFKQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 751 IFGRAGRPQFDKFGEGIIIT-THDKLSH--YLTLLTQRNPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWISYTYLY 825
Cdd:COG1204 368 MAGRAGRPGYDPYGEAILVAkSSDEADElfERYILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTFYA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 826 VRMRANPLaygishkayqidptlrkhrEQLVIEVGRKLDKAQMIrfEERTGYFSSTDLGRTASHYYIKYNTIETFNELFD 905
Cdd:COG1204 448 YQYDKGDL-------------------EEVVDDALEFLLENGFI--EEDGDRLRATKLGKLVSRLYIDPLTAAELVDGLR 506
|
570
....*....|..
gi 2462605685 906 AHKTEGDIFAIV 917
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 ... |
880-1189 |
6.54e-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: 306.98 E-value: 6.54e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 880 STDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDTLLSNfCELSTPGGVENS-YGK 958
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-VPIPVKEGIIDSpHAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 959 INILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLW-GWASPLRQF-SILP 1036
Cdd:smart00973 80 VNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWeDSDSPLKQLpHFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1037 PHILTRLEEKKL--TVDKLKDMRKDEIGHILH-HVNIGLKVKQCVHQIPSVMMEASIQPITRTV-LRVTLSIYADFTWND 1112
Cdd:smart00973 160 EDVYDKLELKDGsrSFELLLDMNAAELGEFLNrLPPNGRLIYELLRRFPKIEVEAEVLPITRDLtLRVELEITPVFAWDL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605685 1113 QVHGTVGEPWWIWVEDPTNDHIYHSEYFLALKKQVISKeaQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIINF 1189
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 ... |
1226-1416 |
7.68e-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: 290.31 E-value: 7.68e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1226 FSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLGKK 1305
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPLLGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1306 VIELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKP 1385
Cdd:cd18021 81 VVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 2462605685 1386 VRIVGLSTALANARDLADWLNIKQMGLFNFR 1416
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 ... |
1714-2079 |
1.45e-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: 268.84 E-value: 1.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1714 PLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPHSFDSPHTKA 1793
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1794 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWL-KDSSLLTLPNIenh 1872
Cdd:smart00973 81 NLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEdSDSPLKQLPHF--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1873 hlhlfkkwkpimkgphargrtsieCLPELIHACGGKDHVFSSMVESELHAAKTKQAWNFLSHLPVINVGISVKGSWDDLv 1952
Cdd:smart00973 158 ------------------------LIEDVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEV- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1953 eghnELSVSTLTADkrddnKWIKLHADQEYVLQVSLQRvhfgfhkgkpescavtprfPKSKDEGWFLILGEVDKRELIAL 2032
Cdd:smart00973 213 ----EAEVLPITRD-----LTLRVELEITPVFAWDLPR-------------------HKGKSESWWLVVGDSDTNELLAI 264
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2462605685 2033 KRV----GYIRNHHVASLSFYTPEiPGRYIYTLYFMSDCYLGLDQQYDIYL 2079
Cdd:smart00973 265 KRVtlrkKKKSNEVKLDFTVPLSE-PGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1714-2077 |
5.10e-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: 238.25 E-value: 5.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1714 PLTYGRIASYYYLKHQTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHMNSELAKCLPIESNPhSFDSPHTKA 1793
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPIPVKG-DIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1794 HLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAANQGWLVTVLNITNLIQMVIQGRWLKDSSLLTLPNIENHH 1873
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1874 LHLFKKwkpimkgphaRGRTSIECL-----PELIHACGGKDHVFssmveselhaaktKQAWNFLSHLPVINVgisvkgsw 1948
Cdd:pfam02889 160 IKKLEK----------KGVESVRDIlelddAEELGELIRNPKMG-------------KDIAQFVNRFPKIEI-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1949 ddlveghnELSVSTLTADkrddnkwiklhadqeyVLQVSLQrvhfgfhkgkpescaVTPRFPKSKD-----EGWFLILGE 2023
Cdd:pfam02889 209 --------EAEVQPITRS----------------VLRVEVT---------------ITPDFPWDKRvhgksEGFWLVVGD 249
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605685 2024 VDKRELIALKRV--GYIRNHHVASLSFYTPEI-PGRYIYTLYFMSDCYLGLDQQYDI 2077
Cdd:pfam02889 250 SDGNEILHIERFtlTKRTLAGEHKLEFTVPPSdPGPPQLFVRLISDSWLGADQEVPI 306
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
1228-1416 |
1.28e-66 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 223.29 E-value: 1.28e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1228 HFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDDWKVRIEEkLGKKVI 1307
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSG-GKAVYIAPTRALVNQKEADLRERFGP-LGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1308 ELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRnYVQQVTILIIDEIHLLG-EERGPVLEVIVSRTNFIsshtEKPV 1386
Cdd:cd17921 79 LLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI----NKNA 153
|
170 180 190
....*....|....*....|....*....|
gi 2462605685 1387 RIVGLSTALANARDLADWLNIKqmGLFNFR 1416
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 ... |
1420-1608 |
2.03e-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: 2.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1420 RPVPLEVHIQGFPGQHYCPRMASMNK-----PAFQAIRSHSPAKPVLIFVSSRRQTRLTALELIaflateedpkqwlnmd 1494
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdsdiIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1495 eremeniiatvrdsnlkltlafGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKT 1574
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKG 122
|
170 180 190
....*....|....*....|....*....|....
gi 2462605685 1575 RRYvdFPITDVLQMMGRAGRPQFDDQGKAVILVH 1608
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 ... |
1229-1421 |
3.87e-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: 3.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1229 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTS-----KAVYIAPLKALVRERMDDWKVRIeEKLG 1303
Cdd:cd18023 2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLpwgnrKVVYIAPIKALCSEKYDDWKEKF-GPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1304 KKVIELTGD-VTPDMKSIAKADLIVTTPEKWDGVSRSW-QNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFISSH 1381
Cdd:cd18023 81 LSCAELTGDtEMDDTFEIQDADIILTTPEKWDSMTRRWrDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSSS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462605685 1382 TEK------PVRIVGLSTALANARDLADWLNIKQMGLFNFRPSVRP 1421
Cdd:cd18023 161 SELrgstvrPMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1246-1774 |
2.86e-61 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 225.47 E-value: 2.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFrvfNKYPTS--KAVYIAPLKALVRER---MDDWkvrieEKLGKKVIELTGDVTPDMKSI 1320
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMV---NKLLREggKAVYLVPLKALAEEKyreFKDW-----EKLGLRVAMTTGDYDSTDEWL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1321 AKADLIVTTPEKWDGVSR---SWqnrnyVQQVTILIIDEIHLLGE-ERGPVLEVIVSrtnfissHTEKPVRIVGLSTALA 1396
Cdd:PRK00254 113 GKYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSyDRGATLEMILT-------HMLGRAQILGLSATVG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1397 NARDLADWLNIKQMglfnfRPSVRPVPLE--VHIQGF------PGQHYcprMASMNKPAFQAIRShspAKPVLIFVSSRR 1468
Cdd:PRK00254 181 NAEELAEWLNAELV-----VSDWRPVKLRkgVFYQGFlfwedgKIERF---PNSWESLVYDAVKK---GKGALVFVNTRR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1469 QTRLTALELIAFLATEEDPKQwlnmdEREMENIIATVRD--SNLKLTLAF--GIGMHHAGLHERDRKTVEELFVNCKVQV 1544
Cdd:PRK00254 250 SAEKEALELAKKIKRFLTKPE-----LRALKELADSLEEnpTNEKLKKALrgGVAFHHAGLGRTERVLIEDAFREGLIKV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1545 LIATSTLAWGVNFPAHLVIIKGTEYYDGKTrrYVDFPITDVLQMMGRAGRPQFDDQGKAVILVH-DIKKDFYKKF----- 1618
Cdd:PRK00254 325 ITATPTLSAGINLPAFRVIIRDTKRYSNFG--WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERYifgkp 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1619 --LYEPFPVESSLLGvlsdHLNAEIAGGTITSKQDALDYITWTYFfrrlimnpsYYNLGDVSH--DSVNKFLSHLIEKSL 1694
Cdd:PRK00254 403 ekLFSMLSNESAFRS----QVLALITNFGVSNFKELVNFLERTFY---------AHQRKDLYSleEKAKEIVYFLLENEF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1695 IELELsycieigEDNrsIEPLTYGRIASYYYLKHQTVKMFKDRLkPECSTEE----LLSILSDAEEYTDLPVRHNEDHMN 1770
Cdd:PRK00254 470 IDIDL-------EDR--FIPLPLGIRTSQLYIDPLTAKKFKDAF-PKIEKNPnplgIFQLIASTPDMTPLNYSRKEMEDL 539
|
....
gi 2462605685 1771 SELA 1774
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 ... |
380-580 |
9.65e-57 |
|
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: 9.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 380 NRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQhfqQGVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPL 459
Cdd:cd18023 3 NRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKE---RNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 460 GIIVKELTGDMQLSKS-EILRTQMLVTTPEKWDVVTRKSVGDVALSQIVRLLILDEVHLLHEDRGPVLESIVARTLRQVE 538
Cdd:cd18023 80 GLSCAELTGDTEMDDTfEIQDADIILTTPEKWDSMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462605685 539 STQSM------IRILGLSATLPNYLDVATFLHVNPyIGLFFFDGRFRP 580
Cdd:cd18023 160 SSELRgstvrpMRFVAVSATIPNIEDLAEWLGDNP-AGCFSFGESFRP 206
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
379-570 |
5.54e-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: 192.86 E-value: 5.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 379 LNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHfqqgvikknEFKIVYVAPMKALAAEMTDYFSRRLEP 458
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS---------GGKAVYIAPTRALVNQKEADLRERFGP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 459 LGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDvaLSQIVRLLILDEVHLLH-EDRGPVLESIVARTLRQv 537
Cdd:cd17921 73 LGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER--LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI- 149
|
170 180 190
....*....|....*....|....*....|...
gi 2462605685 538 estQSMIRILGLSATLPNYLDVATFLHVNPYIG 570
Cdd:cd17921 150 ---NKNARFVGLSATLPNAEDLAEWLGVEDLIR 179
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
395-936 |
2.59e-53 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 201.20 E-value: 2.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 395 ENMLICAPTGAGKTNIAMLTVLHEIrqhFQQGvikkneFKIVYVAPMKALAAEMTDYFsRRLEPLGIIVKELTGDMQlSK 474
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKL---LREG------GKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYD-ST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 475 SEIL-RTQMLVTTPEKWDVVTRKSVgdvalSQI--VRLLILDEVHLL-HEDRGPVLESIVARTLRQVEstqsmirILGLS 550
Cdd:PRK00254 109 DEWLgKYDIIIATAEKFDSLLRHGS-----SWIkdVKLVVADEIHLIgSYDRGATLEMILTHMLGRAQ-------ILGLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 551 ATLPNYLDVATFLHVNpyigLFFFDgrFRPVPL-----GQTFLGIKCANKMQQLNNMDEVCYEnvlkQVKAGHQVMVFVH 625
Cdd:PRK00254 177 ATVGNAEELAEWLNAE----LVVSD--WRPVKLrkgvfYQGFLFWEDGKIERFPNSWESLVYD----AVKKGKGALVFVN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 626 ARNATVRTAMSLIERAKNCghipFFFPTQGHDYVLAEKQVQRSRNKQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHI 705
Cdd:PRK00254 247 TRRSAEKEALELAKKIKRF----LTKPELRALKELADSLEENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 706 KVLVCTATLAWGVNLPAHAVIIKGTQIYAakRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDK----LSHYL-- 779
Cdd:PRK00254 323 KVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklMERYIfg 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 780 ------TLLTQRNPIESQFLesladnlnAEIALGTVTNVEEAVKWISYTYlYVRMRANPlaYGISHKAYQIDPTLrkhRE 853
Cdd:PRK00254 401 kpeklfSMLSNESAFRSQVL--------ALITNFGVSNFKELVNFLERTF-YAHQRKDL--YSLEEKAKEIVYFL---LE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 854 QLVIEvgrkldkaqmIRFEERtgyFSSTDLGRTASHYYIKYNTIETFNELFDahKTEGD-----IFAIVSKAEEFDQIKV 928
Cdd:PRK00254 467 NEFID----------IDLEDR---FIPLPLGIRTSQLYIDPLTAKKFKDAFP--KIEKNpnplgIFQLIASTPDMTPLNY 531
|
....*...
gi 2462605685 929 REEEIEEL 936
Cdd:PRK00254 532 SRKEMEDL 539
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1246-1764 |
5.75e-53 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 200.57 E-value: 5.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKVRieEKLGKKVIELTGDVTPDMKSIAKADL 1325
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAMLKAIAR--GGKALYIVPLRALASEKFEEFERF--EELGVRVGISTGDYDSRDEWLGDNDI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1326 IVTTPEKWDGVSR---SWqnrnyVQQVTILIIDEIHLLG-EERGPVLEVIVS---RTNfisshtekP-VRIVGLSTALAN 1397
Cdd:PRK02362 117 IVATSEKVDSLLRngaPW-----LDDITCVVVDEVHLIDsANRGPTLEVTLAklrRLN--------PdLQVVALSATIGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1398 ARDLADWLNIK-----------QMGLF-----NFRPSVRPVP-----------LEVHIQGfpGQhyCprmasmnkpafqa 1450
Cdd:PRK02362 184 ADELADWLDAElvdsewrpidlREGVFyggaiHFDDSQREVEvpskddtlnlvLDTLEEG--GQ--C------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1451 irshspakpvLIFVSSRRQTRLTALELIAFLateedpKQWLNMDER-EMENIIATVRDS-------NLKLTLAFGIGMHH 1522
Cdd:PRK02362 247 ----------LVFVSSRRNAEGFAKRAASAL------KKTLTAAERaELAELAEEIREVsdtetskDLADCVAKGAAFHH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1523 AGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGkTRRYVDFPITDVLQMMGRAGRPQFDDQGK 1602
Cdd:PRK02362 311 AGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDG-GAGMQPIPVLEYHQMAGRAGRPGLDPYGE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1603 AVILV--HDIKKDFYKKFLY-EPFPVESSLL--GVLSDHLNAEIAGGTITSKQDALDYITWTYFFRRlimNPSYYNLGDV 1677
Cdd:PRK02362 390 AVLLAksYDELDELFERYIWaDPEDVRSKLAtePALRTHVLSTIASGFARTRDGLLEFLEATFYATQ---TDDTGRLERV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1678 shdsVNKFLSHLIEKSLIElelsycieigEDNRSIEPLTYGRIASYYYlkhqtvkmfkdrLKPeCSTEELLSILSDAEEY 1757
Cdd:PRK02362 467 ----VDDVLDFLERNGMIE----------EDGETLEATELGHLVSRLY------------IDP-LSAAEIIDGLEAAKKP 519
|
....*..
gi 2462605685 1758 TDLPVRH 1764
Cdd:PRK02362 520 TDLGLLH 526
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
579-771 |
9.22e-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: 9.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 579 RPVPLGQTFLGIK----CANKMQQLNNMDEVCYENVLKQVKAGHQVMVFVHARNATVRTAMSLIerakncghipfffptq 654
Cdd:cd18795 1 RPVPLEEYVLGFNglgiKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 655 ghdyvlaekqvqrsrnkqvrelfpdGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYA 734
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462605685 735 AKRgsFVDLGILDVMQIFGRAGRPQFDKFGEGIIITT 771
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
1212-1415 |
2.18e-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: 2.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1212 ITALGCKAYEALYNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKY--PTS-------KAVYIAP 1282
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHrnPDGtinldafKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1283 LKALVRERMDDWKVRIEEkLGKKVIELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGE 1362
Cdd:cd18019 81 MKALVQEMVGNFSKRLAP-YGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462605685 1363 ERGPVLEVIVSRTNFISSHTEKPVRIVGLSTALANARDLADWLNIK-QMGLFNF 1415
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDpKKGLFYF 213
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1246-1724 |
1.66e-51 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 195.10 E-value: 1.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWkVRIEEkLGKKVIELTGDV--TPDMksIAKA 1323
Cdd:PRK01172 39 NVIVSVPTAAGKTLIAYSAIYETFLA--GLKSIYIVPLRSLAMEKYEEL-SRLRS-LGMRVKISIGDYddPPDF--IKRY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1324 DLIVTTPEKWDgvSRSWQNRNYVQQVTILIIDEIHLLGEE-RGPVLEVIVSRTNFISSHTekpvRIVGLSTALANARDLA 1402
Cdd:PRK01172 113 DVVILTSEKAD--SLIHHDPYIINDVGLIVADEIHIIGDEdRGPTLETVLSSARYVNPDA----RILALSATVSNANELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1403 DWLNIKQMglfnfRPSVRPVPLEVHIQgFPGQHYCPRMASMNKPAFQAIRSH-SPAKPVLIFVSSRRQTRLTALELIAFL 1481
Cdd:PRK01172 187 QWLNASLI-----KSNFRPVPLKLGIL-YRKRLILDGYERSQVDINSLIKETvNDGGQVLVFVSSRKNAEDYAEMLIQHF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1482 ATEEDPKqwLNMDEremeniiATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHL 1561
Cdd:PRK01172 261 PEFNDFK--VSSEN-------NNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1562 VIIKG-TEYYDGKTRryvdfPIT--DVLQMMGRAGRPQFDDQGKAVILV-----HDIKKDFYKKflyEPFPVESSLLGVL 1633
Cdd:PRK01172 332 VIVRDiTRYGNGGIR-----YLSnmEIKQMIGRAGRPGYDQYGIGYIYAaspasYDAAKKYLSG---EPEPVISYMGSQR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1634 SDHLN--AEIAGGTITSKQDALDYITWTYFFRRlimnpsyyNLGDVSHDSVNKFLSHLIEKSLIELELSY-CIEIGE--D 1708
Cdd:PRK01172 404 KVRFNtlAAISMGLASSMEDLILFYNETLMAIQ--------NGVDEIDYYIESSLKFLKENGFIKGDVTLrATRLGKltS 475
|
490
....*....|....*.
gi 2462605685 1709 NRSIEPLTYGRIASYY 1724
Cdd:PRK01172 476 DLYIDPESALILKSAF 491
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
380-575 |
6.01e-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: 6.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 380 NRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFQqgvikkneFKIVYVAPMKALAAE-MTDYFSRRLEP 458
Cdd:cd18022 3 NPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPG--------SKVVYIAPLKALVRErVDDWKKRFEEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 459 LGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVV-----TRKSVgdvalsQIVRLLILDEVHLLHEDRGPVLESIVART 533
Cdd:cd18022 75 LGKKVVELTGDVTPDMKALADADIIITTPEKWDGIsrswqTREYV------QQVSLIIIDEIHLLGSDRGPVLEVIVSRM 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462605685 534 LRQVESTQSMIRILGLSATLPNYLDVATFLHVNPyIGLFFFD 575
Cdd:cd18022 149 NYISSQTEKPVRLVGLSTALANAGDLANWLGIKK-MGLFNFR 189
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
394-892 |
2.04e-47 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 183.62 E-value: 2.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 394 NENMLICAPTGAGKTNIAMLTVLHEIrqhfqqgvikKNEFKIVYVAPMKALAAEMTDYFSRrLEPLGIIVKELTGDMQlS 473
Cdd:PRK02362 39 GKNLLAAIPTASGKTLIAELAMLKAI----------ARGGKALYIVPLRALASEKFEEFER-FEELGVRVGISTGDYD-S 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 474 KSEIL-RTQMLVTTPEKWDVVTRKsvGDVALSQIVrLLILDEVHLL-HEDRGPVLESIVARTLRQVESTQsmirILGLSA 551
Cdd:PRK02362 107 RDEWLgDNDIIVATSEKVDSLLRN--GAPWLDDIT-CVVVDEVHLIdSANRGPTLEVTLAKLRRLNPDLQ----VVALSA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 552 TLPNYLDVATFLHVNpyiglfFFDGRFRPVPLGQ-TFLG--IKCANKMQQLNNM--DEVcyEN-VLKQVKAGHQVMVFVH 625
Cdd:PRK02362 180 TIGNADELADWLDAE------LVDSEWRPIDLREgVFYGgaIHFDDSQREVEVPskDDT--LNlVLDTLEEGGQCLVFVS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 626 AR-NA---------TVRTAMSLIERAKNCGhipfffptqghdyvLAEKQVQRSRNKQVREL---FPDGFSIHHAGMLRQD 692
Cdd:PRK02362 252 SRrNAegfakraasALKKTLTAAERAELAE--------------LAEEIREVSDTETSKDLadcVAKGAAFHHAGLSREH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 693 RNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGTQIYAAKRGSfVDLGILDVMQIFGRAGRPQFDKFGEGIIIT-T 771
Cdd:PRK02362 318 RELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAGM-QPIPVLEYHQMAGRAGRPGLDPYGEAVLLAkS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 772 HDKLS----HYLTLLTQrnPIESQFLE--SLADNLNAEIALGTVTNVEEAVKWISYTyLYvrmranplaygishkAYQID 845
Cdd:PRK02362 397 YDELDelfeRYIWADPE--DVRSKLATepALRTHVLSTIASGFARTRDGLLEFLEAT-FY---------------ATQTD 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2462605685 846 PTLRKHReqLVIEVGRKLDKAQMIrfEERTGYFSSTDLGRTASHYYI 892
Cdd:PRK02362 459 DTGRLER--VVDDVLDFLERNGMI--EEDGETLEATELGHLVSRLYI 501
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
394-932 |
3.79e-47 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 182.00 E-value: 3.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 394 NENMLICAPTGAGKTNIAMltvlHEIRQHFQQGVikknefKIVYVAPMKALAAEMTDYFSRrLEPLGIIVKELTGDMQLS 473
Cdd:PRK01172 37 GENVIVSVPTAAGKTLIAY----SAIYETFLAGL------KSIYIVPLRSLAMEKYEELSR-LRSLGMRVKISIGDYDDP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 474 KSEILRTQMLVTTPEKWDVVTRKsvgDVALSQIVRLLILDEVHLLH-EDRGPVLESiVARTLRQVESTqsmIRILGLSAT 552
Cdd:PRK01172 106 PDFIKRYDVVILTSEKADSLIHH---DPYIINDVGLIVADEIHIIGdEDRGPTLET-VLSSARYVNPD---ARILALSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 553 LPNYLDVATFLHVNpyiglfFFDGRFRPVPLGqtfLGIKCANKMQQLNNMDEVCYENVL--KQVKAGHQVMVFVHARNAT 630
Cdd:PRK01172 179 VSNANELAQWLNAS------LIKSNFRPVPLK---LGILYRKRLILDGYERSQVDINSLikETVNDGGQVLVFVSSRKNA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 631 VRTAMSLIErakncgHIPFFfptqgHDYVLAEKQVQrSRNKQVRELFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVC 710
Cdd:PRK01172 250 EDYAEMLIQ------HFPEF-----NDFKVSSENNN-VYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 711 TATLAWGVNLPAHAVIIKGTQIYAAKRGSFvdLGILDVMQIFGRAGRPQFDKFGEGIII----TTHDKLSHYLTllTQRN 786
Cdd:PRK01172 318 TPTLAAGVNLPARLVIVRDITRYGNGGIRY--LSNMEIKQMIGRAGRPGYDQYGIGYIYaaspASYDAAKKYLS--GEPE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 787 PIESQF--LESLADNLNAEIALGTVTNVEEAVKWISYTYLYVRMRANPLAYGIShkayqidptlrkhreqlvievgrkld 864
Cdd:PRK01172 394 PVISYMgsQRKVRFNTLAAISMGLASSMEDLILFYNETLMAIQNGVDEIDYYIE-------------------------- 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462605685 865 kaQMIRFEERTGY------FSSTDLGRTASHYYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEE 932
Cdd:PRK01172 448 --SSLKFLKENGFikgdvtLRATRLGKLTSDLYIDPESALILKSAFDHDYDEDLALYYISLCREIIPANTRDDY 519
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1246-1628 |
1.20e-46 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 181.68 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDWKvrieEKLGK-KVIELTGDVT--PDmksiak 1322
Cdd:COG4581 42 SVLVAAPTGSGKTLVAEFAIFLALAR--GRRSFYTAPIKALSNQKFFDLV----ERFGAeNVGLLTGDASvnPD------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1323 ADLIVTTPEkwdgVSRswqNRNY--------VQQVtilIIDEIHLLGE-ERGPVLEVIVsrtnfIssHTEKPVRIVGLST 1393
Cdd:COG4581 110 APIVVMTTE----ILR---NMLYregadledVGVV---VMDEFHYLADpDRGWVWEEPI-----I--HLPARVQLVLLSA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1394 ALANARDLADWLNikqmglfnfrpSV-----------RPVPLEvhiqgfpgQHYC--PRMASMNKPAFQAIRSHSPAK-- 1458
Cdd:COG4581 173 TVGNAEEFAEWLT-----------RVrgetavvvseeRPVPLE--------FHYLvtPRLFPLFRVNPELLRPPSRHEvi 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1459 ---------PVLIFVSSRRQTRLTALELIAFLATEEDPKQWLNMDEREMENIIATVRDSNLKLTLAFGIGMHHAGLHERD 1529
Cdd:COG4581 234 eeldrggllPAIVFIFSRRGCDEAAQQLLSARLTTKEERAEIREAIDEFAEDFSVLFGKTLSRLLRRGIAVHHAGMLPKY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1530 RKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKTRRyvdfPIT--DVLQMMGRAGRPQFDDQGKAVILV 1607
Cdd:COG4581 314 RRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHR----PLTarEFHQIAGRAGRRGIDTEGHVVVLA 389
|
410 420
....*....|....*....|....*
gi 2462605685 1608 HDiKKDFyKKFLY----EPFPVESS 1628
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; ... |
1230-1415 |
5.93e-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: 5.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1230 NPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTS---------KAVYIAPLKALVRERMDDWKVRIEe 1300
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQggvikkddfKIVYIAPMKALAAEMVEKFSKRLA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1301 KLGKKVIELTGDVTPDMKSIAKADLIVTTPEKWDGVSR-SWQNRNYVQQVTILIIDEIHLLGEERGPVLEVIVSRTNFIS 1379
Cdd:cd18020 82 PLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRkSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQV 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462605685 1380 SHTEKPVRIVGLSTALANARDLADWLNIKQM-GLFNF 1415
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 ... |
377-567 |
4.09e-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: 4.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 377 KRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHeirqHFQQGvikkNEFKIVYVAPMKALAAEMTDYFSRRL 456
Cdd:cd18021 2 KFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLR----HWRQN----PKGRAVYIAPMQELVDARYKDWRAKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 457 EP-LGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVV-----TRKSVgdvalsQIVRLLILDEVHLLHEDRGPVLESIV 530
Cdd:cd18021 74 GPlLGKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLsrrwkQRKNV------QSVELFIADELHLIGGENGPVYEVVV 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462605685 531 ARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNP 567
Cdd:cd18021 148 SRMRYISSQLEKPIRIVGLSSSLANARDVGEWLGASK 184
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
1229-1408 |
3.58e-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: 138.62 E-value: 3.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1229 FNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIfrVFNKYPTSKAVYIAPLKALVRERMDDWKVRieEKLGKKVIE 1308
Cdd:cd18028 2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAM--VNTLLEGGKALYLVPLRALASEKYEEFKKL--EEIGLKVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1309 LTGDVTPDMKSIAKADLIVTTPEKWDGVsrsWQNR-NYVQQVTILIIDEIHLLG-EERGPVLEVIVSRTNfissHTEKPV 1386
Cdd:cd18028 78 STGDYDEDDEWLGDYDIIVATYEKFDSL---LRHSpSWLRDVGVVVVDEIHLISdEERGPTLESIVARLR----RLNPNT 150
|
170 180
....*....|....*....|..
gi 2462605685 1387 RIVGLSTALANARDLADWLNIK 1408
Cdd:cd18028 151 QIIGLSATIGNPDELAEWLNAE 172
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
390-865 |
6.08e-35 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 145.08 E-value: 6.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 390 AYNTNENMLICAPTGAGKTNIAMltvlHEIRQHFQQGVikknefKIVYVAPMKALAAEMTDYFSRRL--EPLGIivkeLT 467
Cdd:COG4581 36 ALEAGRSVLVAAPTGSGKTLVAE----FAIFLALARGR------RSFYTAPIKALSNQKFFDLVERFgaENVGL----LT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 468 GDMQL--------SKSEILRTQMLVTTPEKWDVvtrksvgDVAlsqivrllILDEVHLLHE-DRGPVLE-SIVARTLRqv 537
Cdd:COG4581 102 GDASVnpdapivvMTTEILRNMLYREGADLEDV-------GVV--------VMDEFHYLADpDRGWVWEePIIHLPAR-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 538 estqsmIRILGLSATLPNYLDVATFLH--------VnpyiglfffDGRFRPVPLGQTFLGIKCANKMQQLNNMDEVCYE- 608
Cdd:COG4581 165 ------VQLVLLSATVGNAEEFAEWLTrvrgetavV---------VSEERPVPLEFHYLVTPRLFPLFRVNPELLRPPSr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 609 -NVLKQVKAGHQ--VMVFVHARNATVrtamsliERAKNCGHIPFFFPTQGH--DYVLAEKQVQRS--RNKQVRELFPDGF 681
Cdd:COG4581 230 hEVIEELDRGGLlpAIVFIFSRRGCD-------EAAQQLLSARLTTKEERAeiREAIDEFAEDFSvlFGKTLSRLLRRGI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 682 SIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIKGtqiyAAKR--GSFVDLGILDVMQIFGRAGRPQ 759
Cdd:COG4581 303 AVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTK----LSKFdgERHRPLTAREFHQIAGRAGRRG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 760 FDKFGEGIIITT-HDKLSHYLTLLTQR-NPIESQFlesladnlnaEIALGTVTNVeeaVKWISYTylyvRMRAnplAYGI 837
Cdd:COG4581 379 IDTEGHVVVLAPeHDDPKKFARLASARpEPLRSSF----------RPSYNMVLNL---LARPGLE----RARE---LLED 438
|
490 500
....*....|....*....|....*...
gi 2462605685 838 SHKAYQIDPTLRKHREQlVIEVGRKLDK 865
Cdd:COG4581 439 SFAQFQADRSVVGLARR-ARELERALAG 465
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
380-558 |
1.12e-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: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 380 NRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQhfqqgviKKNEFKIVYVAPMKALAAEMTDYFSRRLEPL 459
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDK-------LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 460 GIIVKELTGDMQLSK--SEILRTQMLVTTPEKWDVVTRKSvgdVALSQiVRLLILDEVHLLHE-DRGPVLESIVARtlrq 536
Cdd:pfam00270 73 GLKVASLLGGDSRKEqlEKLKGPDILVGTPGRLLDLLQER---KLLKN-LKLLVLDEAHRLLDmGFGPDLEEILRR---- 144
|
170 180
....*....|....*....|..
gi 2462605685 537 vesTQSMIRILGLSATLPNYLD 558
Cdd:pfam00270 145 ---LPKKRQILLLSATLPRNLE 163
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1230-1401 |
1.54e-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: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1230 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFN-KYPTSKAVYIAPLKALVRERMDDWKVRIeEKLGKKVIE 1308
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEALDkLDNGPQALVLAPTRELAEQIYEELKKLG-KGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1309 LTGDVTP--DMKSIAKADLIVTTPEKWDGVsrsWQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNfisshteKP 1385
Cdd:pfam00270 79 LLGGDSRkeQLEKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRRLP-------KK 148
|
170
....*....|....*..
gi 2462605685 1386 VRIVGLS-TALANARDL 1401
Cdd:pfam00270 149 RQILLLSaTLPRNLEDL 165
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
378-563 |
6.13e-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: 112.43 E-value: 6.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 378 RLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHfqqgvikkneFKIVYVAPMKALAAEMTDYFSrRLE 457
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEG----------GKALYLVPLRALASEKYEEFK-KLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 458 PLGIIVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSvgdVALSQIVRLLILDEVHLLH-EDRGPVLESIVARTLRQ 536
Cdd:cd18028 70 EIGLKVGISTGDYDEDDEWLGDYDIIVATYEKFDSLLRHS---PSWLRDVGVVVVDEIHLISdEERGPTLESIVARLRRL 146
|
170 180
....*....|....*....|....*..
gi 2462605685 537 VESTQsmirILGLSATLPNYLDVATFL 563
Cdd:cd18028 147 NPNTQ----IIGLSATIGNPDELAEWL 169
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1231-1607 |
5.37e-26 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 116.91 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1231 PVQT-QIFHTLYHTDcNVLLGAPTGSGKTVAAELA-IFRVFNKypTSKAVYIAPLKALVRERMDDWKVRIEEKLgkKVIE 1308
Cdd:COG1202 212 PVQSlAVENGLLEGK-DQLVVSATATGKTLIGELAgIKNALEG--KGKMLFLVPLVALANQKYEDFKDRYGDGL--DVSI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1309 LTGDV---TPDMKSIAKADLIVTTPEKWDGVSRSwqnRNYVQQVTILIIDEIHLLGE-ERGPVLEVIVSRTNFISSHTEk 1384
Cdd:COG1202 287 RVGASrirDDGTRFDPNADIIVGTYEGIDHALRT---GRDLGDIGTVVIDEVHMLEDpERGHRLDGLIARLKYYCPGAQ- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1385 pvrIVGLSTALANARDLADWLNIKQMgLFNfrpsVRPVPLEVHIQGFPGQHYCPRMASMNKPAFQAIRSHSPAKPVLIFV 1464
Cdd:COG1202 363 ---WIYLSATVGNPEELAKKLGAKLV-EYE----ERPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1465 SSRRQTRltaleliaflateedpkqwlnmderemeniiatvrdsnlKLTLAFGIGM--HHAGLHERDRKTVEELFVNCKV 1542
Cdd:COG1202 435 NSRRRCH---------------------------------------EIARALGYKAapYHAGLDYGERKKVERRFADQEL 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462605685 1543 QVLIATSTLAWGVNFPAHLVIIK----GTEYydgktrryvdFPITDVLQMMGRAGRPQFDDQGKAVILV 1607
Cdd:COG1202 476 AAVVTTAALAAGVDFPASQVIFDslamGIEW----------LSVQEFHQMLGRAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
371-582 |
8.27e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.81 E-value: 8.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 371 LAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRqhfqqgviKKNEFKIVYVAPMKALAAEMTD 450
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALK--------RGKGGRVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 451 YFSRRLEPLGIIVKELTGD----MQLSKSEILRTQMLVTTPEKWDVVTRKsvGDVALSQiVRLLILDEVH-LLHEDRGPV 525
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGdskrEQLRKLESGKTDILVTTPGRLLDLLEN--DKLSLSN-VDLVILDEAHrLLDGGFGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605685 526 LESIVARTLRqvestqsMIRILGLSATLPNYLDVATFLHVNpyiGLFFFDGRFRPVP 582
Cdd:smart00487 150 LEKLLKLLPK-------NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLE 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1224-1423 |
9.89e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 103.73 E-value: 9.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1224 YNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLG 1303
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1304 KKVIELTGDVT-PDMKSIAK--ADLIVTTPEKWDGVSRswQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNfis 1379
Cdd:smart00487 84 KVVGLYGGDSKrEQLRKLESgkTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLLP--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462605685 1380 shteKPVRIVGLS-TALANARDLADWLNIkqmGLFNFRPSVRPVP 1423
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 ... |
1244-1417 |
2.29e-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: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1244 DCNVLLGAPTGSGKTVAAELAIFRVF--NKyptSKAVYIAPLKALVRERMDdWKVRIEEKLGKKVIELTGDVTPDM-KSI 1320
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLleRR---KKALFVLPYVSIVQEKVD-ALSPLFEELGFRVEGYAGNKGRSPpKRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1321 AKADLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLGEE-RGPVLEVIVSRtnfISSHTEKPVRIVGLSTALANAR 1399
Cdd:cd18026 109 KSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDGhRGALLELLLTK---LLYAAQKNIQIVGMSATLPNLE 185
|
170 180
....*....|....*....|
gi 2462605685 1400 DLADWLNIKqmgLF--NFRP 1417
Cdd:cd18026 186 ELASWLRAE---LYttNFRP 202
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
1246-1405 |
9.28e-22 |
|
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: 94.19 E-value: 9.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKYPTS--KAVYIAPLKALVRermdDWKVRIEE-----KLGKKVIELTGDVTPDMK 1318
Cdd:cd17922 3 NVLIAAPTGSGKTEAAFLPALSSLADEPEKgvQVLYISPLKALIN----DQERRLEEpldeiDLEIPVAVRHGDTSQSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1319 SIAKA---DLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRtnfISSHTEKPVRIVGLSTA 1394
Cdd:cd17922 79 AKQLKnppGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHaLLGSKRGVQLELLLER---LRKLTGRPLRRIGLSAT 155
|
170
....*....|.
gi 2462605685 1395 LANARDLADWL 1405
Cdd:cd17922 156 LGNLEEAAAFL 166
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
394-563 |
1.04e-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: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 394 NENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGVikknefKIVYVAPMKALAAEMTdyfsRRLE------PLGIIVKELT 467
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV------QVLYISPLKALINDQE----RRLEepldeiDLEIPVAVRH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 468 GDM-QLSKSEILRT--QMLVTTPEKWDVVTRKSVGDVALSQiVRLLILDEVH-LLHEDRGPVLESIVARtLRQVESTQsm 543
Cdd:cd17922 71 GDTsQSEKAKQLKNppGILITTPESLELLLVNKKLRELFAG-LRYVVVDEIHaLLGSKRGVQLELLLER-LRKLTGRP-- 146
|
170 180
....*....|....*....|
gi 2462605685 544 IRILGLSATLPNYLDVATFL 563
Cdd:cd17922 147 LRRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
394-580 |
1.20e-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: 92.28 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 394 NENMLICAPTGAGKTNIAMLTVLHEIRQhfqqgvikkNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDmqLS 473
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLLE---------RRKKALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGN--KG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 474 KSEILR---TQMLVTTPEKWDVVTRKSVGDVALSQIvRLLILDEVHLLHE-DRGPVLESIVARTLRqveSTQSMIRILGL 549
Cdd:cd18026 102 RSPPKRrksLSVAVCTIEKANSLVNSLIEEGRLDEL-GLVVVDELHMLGDgHRGALLELLLTKLLY---AAQKNIQIVGM 177
|
170 180 190
....*....|....*....|....*....|.
gi 2462605685 550 SATLPNYLDVATFLHVnpyiglFFFDGRFRP 580
Cdd:cd18026 178 SATLPNLEELASWLRA------ELYTTNFRP 202
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1226-1563 |
6.74e-19 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 94.01 E-value: 6.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1226 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAIF-RVFNKYPTSKA------VYIAPLKAL---VRERMDDWK 1295
Cdd:COG1201 22 FGAPTPPQREAW-PAIAAGESTLLIAPTGSGKTLAAFLPALdELARRPRPGELpdglrvLYISPLKALandIERNLRAPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1296 VRIEEKLGKKVIEL-----TGDVTPDMKSIAKA---DLIVTTPE---------KWdgvsrswqnRNYVQQVTILIIDEIH 1358
Cdd:COG1201 101 EEIGEAAGLPLPEIrvgvrTGDTPASERQRQRRrppHILITTPEslallltspDA---------RELLRGVRTVIVDEIH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1359 -LLGEERGPVLEVIVSRtnfISSHTEKPVRIVGLSTALANARDLADWLnikqMGLFNFRPS--VRP-----------VPL 1424
Cdd:COG1201 172 aLAGSKRGVHLALSLER---LRALAPRPLQRIGLSATVGPLEEVARFL----VGYEDPRPVtiVDAgagkkpdlevlVPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1425 EVHIQGFP-----GQHYCPRMAsmnkpafQAIRSHspaKPVLIFVSSRRQTRLTALELIAFLATEEDPkqwlnmdereme 1499
Cdd:COG1201 245 EDLIERFPwaghlWPHLYPRVL-------DLIEAH---RTTLVFTNTRSQAERLFQRLNELNPEDALP------------ 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462605685 1500 niiatvrdsnlkltlafgIGMHHAGL-HERdRKTVEELFVNCKVQVLIATSTLAWGVNFPA-HLVI 1563
Cdd:COG1201 303 ------------------IAAHHGSLsREQ-RLEVEEALKAGELRAVVATSSLELGIDIGDvDLVI 349
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
371-779 |
4.14e-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: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 371 LAFKGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQHfqqgvikkNEFKIVYVAPMKALAA---- 446
Cdd:COG1205 49 LKKRGIERLYSHQAEAIEAARA-GKNVVIATPTASGKSLAYLLPVLEALLED--------PGATALYLYPTKALARdqlr 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 447 EMTDYFSRRlePLGIIVKELTGDMQLS-KSEILRT-QMLVTTP-----------EKWDVVTRKsvgdvalsqiVRLLILD 513
Cdd:COG1205 120 RLRELAEAL--GLGVRVATYDGDTPPEeRRWIREHpDIVLTNPdmlhygllphhTRWARFFRN----------LRYVVID 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 514 EVHLLhedRGpVLESIVA----RTLRQVESTQSMIRILGLSATLPNYLDVA---------------------TFLHVNPY 568
Cdd:COG1205 188 EAHTY---RG-VFGSHVAnvlrRLRRICRHYGSDPQFILASATIGNPAEHAerltgrpvtvvdedgsprgerTFVLWNPP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 569 IGLfffDGRFRPVPLgqtflgikcankmqqlnnmdEVCYenVLKQ-VKAGHQVMVFVHARNATVRTAMSLIERAKncghi 647
Cdd:COG1205 264 LVD---DGIRRSALA--------------------EAAR--LLADlVREGLRTLVFTRSRRGAELLARYARRALR----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 648 pfffptqghdyvlaekqvqrsrnkqvRELFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPA-HAVI 726
Cdd:COG1205 314 --------------------------EPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVV 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2462605685 727 IKGtqiYAAKRGSFVdlgildvmQIFGRAGRPQFDkfGEGIIITTHDKLSHYL 779
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 ... |
1248-1563 |
8.27e-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: 8.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1248 LLGAPTGSGKTVAAELAIFRVFNKYPTSK-----AVYIAPLKALVRErmddwkvrIEEKLGKKVIEL---------TGDV 1313
Cdd:TIGR04121 32 LLIAPTGSGKTLAGFLPSLIDLAGPEAPKekglhTLYITPLRALAVD--------IARNLQAPIEELglpirvetrTGDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1314 TPDMKSIAKA---DLIVTTPEkwdgvsrSWQ-------NRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNFISSHt 1382
Cdd:TIGR04121 104 SSSERARQRKkppDILLTTPE-------SLAlllsypdAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAPG- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1383 ekpVRIVGLSTALANARDLADWLnikqMGLFNFRPSV------RPVPLEV----HIQGFP-GQHYCPRMASmnkPAFQAI 1451
Cdd:TIGR04121 176 ---LRRWGLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISllpeSEERFPwAGHLGLRALP---EVYAEI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1452 RSHspaKPVLIFVSSRRQTRLTALELIAFLAteedpkqwlnmderemeniiatvrDSNLKltlafgIGMHHAGLHERDRK 1531
Cdd:TIGR04121 246 DQA---RTTLVFTNTRSQAELWFQALWEANP------------------------EFALP------IALHHGSLDREQRR 292
|
330 340 350
....*....|....*....|....*....|...
gi 2462605685 1532 TVEELFVNCKVQVLIATSTLAWGVNF-PAHLVI 1563
Cdd:TIGR04121 293 WVEAAMAAGRLRAVVCTSSLDLGVDFgPVDLVI 325
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
395-772 |
9.54e-16 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 83.61 E-value: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 395 ENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGViKKNEFKIVYVAPMKALAAEMtdyfSRRLE-PL-------GIIVKEL 466
Cdd:COG1201 40 ESTLLIAPTGSGKTLAAFLPALDELARRPRPGE-LPDGLRVLYISPLKALANDI----ERNLRaPLeeigeaaGLPLPEI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 467 -----TGDMqlSKSEilRTQM-------LVTTPE---------KWdvvtRKSVGDvalsqiVRLLILDEVHLLHED-RGP 524
Cdd:COG1201 115 rvgvrTGDT--PASE--RQRQrrrpphiLITTPEslallltspDA----RELLRG------VRTVIVDEIHALAGSkRGV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 525 VLESIVARtLRQVeSTQSMIRIlGLSATLPNYLDVATFLhvnpyIGlfffDGRFRPV-----PLGQTF-LGIKCANKmqq 598
Cdd:COG1201 181 HLALSLER-LRAL-APRPLQRI-GLSATVGPLEEVARFL-----VG----YEDPRPVtivdaGAGKKPdLEVLVPVE--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 599 lnNMDEVC----------YENVLKQVKAGHQVMVFVHARNatvrtamslierakncghipfffptqghdyvLAEKQVQRs 668
Cdd:COG1201 246 --DLIERFpwaghlwphlYPRVLDLIEAHRTTLVFTNTRS-------------------------------QAERLFQR- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 669 rnkqVRELFPDGFS---IHHAGMLRQDRNLVENLFSNGHIKVLVCTATLA----WG-VNLpahaVIikgtQIYAAK---R 737
Cdd:COG1201 292 ----LNELNPEDALpiaAHHGSLSREQRLEVEEALKAGELRAVVATSSLElgidIGdVDL----VI----QVGSPKsvaR 359
|
410 420 430
....*....|....*....|....*....|....*
gi 2462605685 738 GsfvdlgildvMQIFGRAGRpQFDKFGEGIIITTH 772
Cdd:COG1201 360 L----------LQRIGRAGH-RVGEVSKGRLVPTH 383
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
356-760 |
1.76e-15 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 82.63 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 356 EEKPVYIQDLDEIGQlaFKGM-----KRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTVLHEIrqhfqqgviKK 430
Cdd:COG1202 184 EVDTVPVDDLDLPPE--LKDLlegrgEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAGIKNA---------LE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 431 NEFKIVYVAPMKALAAEMTDYFSRRLEPlGIIVKELTGDMQLSKSE---ILRTQMLVTTPEKWDVVTR--KSVGDVALsq 505
Cdd:COG1202 253 GKGKMLFLVPLVALANQKYEDFKDRYGD-GLDVSIRVGASRIRDDGtrfDPNADIIVGTYEGIDHALRtgRDLGDIGT-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 506 ivrlLILDEVHLLHE-DRGPVLESIVARtLRQV-ESTQsmirILGLSATLPNYLDVATFLHVNpyigLFFFDGRfrPVPL 583
Cdd:COG1202 330 ----VVIDEVHMLEDpERGHRLDGLIAR-LKYYcPGAQ----WIYLSATVGNPEELAKKLGAK----LVEYEER--PVPL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 584 GQ--TFlgikcANKMQQLNNMDEVCYENVLKQVKAGH--QVMVFVHARnatvrtamslieraKNCghipfffptqghdYV 659
Cdd:COG1202 395 ERhlTF-----ADGREKIRIINKLVKREFDTKSSKGYrgQTIIFTNSR--------------RRC-------------HE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 660 LAEKqvqrsrnkqvrelFPDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIikgtqiyaakrgs 739
Cdd:COG1202 443 IARA-------------LGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVI------------- 496
|
410 420
....*....|....*....|....*...
gi 2462605685 740 FVDL--GI--LDV---MQIFGRAGRPQF 760
Cdd:COG1202 497 FDSLamGIewLSVqefHQMLGRAGRPDY 524
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
1246-1392 |
1.76e-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: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDdwKVRIEEKLGKKVIELTGDVTP---DMKSIAK 1322
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKG-KKVLVLVPTKALALQTAE--RLRELFGPGIRVAVLVGGSSAeerEKNKLGD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462605685 1323 ADLIVTTPEKWDGVSRSwQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTnfissHTEKPVRIVGLS 1392
Cdd:cd00046 80 ADIIIATPDMLLNLLLR-EDRLFLKDLKLIIVDEAHaLLIDSRGALILDLAVRK-----AGLKNAQVILLS 144
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
390-758 |
5.33e-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: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 390 AYNTNENMLICAPTGAGKTNIAMLTVLheIRQHFQQGViKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVK-EL-T 467
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSL--IDLAGPEAP-KEKGLHTLYITPLRALAVDIARNLQAPIEELGLPIRvETrT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 468 GDMQLSKSEILRTQM---LVTTPEKWDVVTrkSVGDVA-LSQIVRLLILDEVH-LLHEDRGPVLESIVARtLRQvesTQS 542
Cdd:TIGR04121 101 GDTSSSERARQRKKPpdiLLTTPESLALLL--SYPDAArLFKDLRCVVVDEWHeLAGSKRGDQLELALAR-LRR---LAP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 543 MIRILGLSATLPNyLDVA--TFLHVNPYIGLFFFDGRFRPVPL-------GQTF-----LGIKCAnkmqqlnnmdevcyE 608
Cdd:TIGR04121 175 GLRRWGLSATIGN-LEEArrVLLGVGGAPAVLVRGKLPKAIEVisllpesEERFpwaghLGLRAL--------------P 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 609 NVLKQVKAGHQVMVFVHARNATVRTAMSLIErakncghipfffptqghdyvlaekqvqrsrnkqVRELFPDGFSIHHAGM 688
Cdd:TIGR04121 240 EVYAEIDQARTTLVFTNTRSQAELWFQALWE---------------------------------ANPEFALPIALHHGSL 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462605685 689 LRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIkgtQIYAAKrgsfvdlGILDVMQIFGRAG-RP 758
Cdd:TIGR04121 287 DREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVI---QIGSPK-------GVARLLQRAGRSNhRP 347
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1516-1595 |
1.03e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 71.09 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1516 FGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryVDFPITDVLQMMGRAGR 1594
Cdd:smart00490 12 IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVII-----YD------LPWSPASYIQRIGRAGR 80
|
.
gi 2462605685 1595 P 1595
Cdd:smart00490 81 A 81
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1191-1637 |
3.76e-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: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1191 HLILPERHPPHTELLD-LQPLPITALGCKAYEALYnfSHfnpvQTQIFHtLYHTDCNVLLGAPTGSGKTVAAELAIFRVF 1269
Cdd:COG1205 24 VRTIPAREARYAPWPDwLPPELRAALKKRGIERLY--SH----QAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1270 NKYPTSKAVYIAPLKALVRERMDDWKvRIEEKLGK--KVIELTGDVTPDMKS--IAKADLIVTTP-----------EKWd 1334
Cdd:COG1205 97 LEDPGATALYLYPTKALARDQLRRLR-ELAEALGLgvRVATYDGDTPPEERRwiREHPDIVLTNPdmlhygllphhTRW- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1335 gvSRSWQNRNYVqqvtilIIDEIHLLgeeRGpvleV-------IVSRTNFISSHTEKPVRIVGLSTALANARDLAdwlni 1407
Cdd:COG1205 175 --ARFFRNLRYV------VIDEAHTY---RG----VfgshvanVLRRLRRICRHYGSDPQFILASATIGNPAEHA----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1408 kqMGLFNfRPsvrpvplevhiqgfpgqhycprmasmnkpaFQAI-RSHSPA--------KPVLIFVSSRRQTRLTALELI 1478
Cdd:COG1205 235 --ERLTG-RP------------------------------VTVVdEDGSPRgertfvlwNPPLVDDGIRRSALAEAARLL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1479 AFLAtEEDPKQWLNMDEREM-ENIIATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNF 1557
Cdd:COG1205 282 ADLV-REGLRTLVFTRSRRGaELLARYARRALREPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1558 PA-HLVIIKGteyydgktrryvdFP--ITDVLQMMGRAGRpqfDDQGKAVILV--HDIKKDFYKK---FLYEPfPVESSL 1629
Cdd:COG1205 361 GGlDAVVLAG-------------YPgtRASFWQQAGRAGR---RGQDSLVVLVagDDPLDQYYVRhpeELFER-PPEAAV 423
|
490
....*....|...
gi 2462605685 1630 LG-----VLSDHL 1637
Cdd:COG1205 424 IDpdnpyVLAPHL 436
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
394-552 |
4.51e-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: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 394 NENMLICAPTGAGKTNIAMLTVLHEIRqhfqqgvikKNEFKIVYVAPMKALAAEMTDYFsRRLEPLGIIVKELTGDM--- 470
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLL---------KKGKKVLVLVPTKALALQTAERL-RELFGPGIRVAVLVGGSsae 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 471 QLSKSEILRTQMLVTTPEKwdvVTRKSVGDVALSQI-VRLLILDEVH-LLHEDRGPVLESIVARTLRQVEStqsmiRILG 548
Cdd:cd00046 71 EREKNKLGDADIIIATPDM---LLNLLLREDRLFLKdLKLIIVDEAHaLLIDSRGALILDLAVRKAGLKNA-----QVIL 142
|
....
gi 2462605685 549 LSAT 552
Cdd:cd00046 143 LSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
680-758 |
8.20e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 65.70 E-value: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 680 GFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIKGtqiyaakrgsfVDLGILDVMQIFGRAGRP 758
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 ... |
394-555 |
9.22e-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: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 394 NENMLICAPTGAGKTNI---AMLTVLHEirqhfqqgvikKNEFKIVYVAPMKAL----AAEMTDYFSRRLEPLGI-IVKE 465
Cdd:cd18025 16 RESALIVAPTSSGKTFIsyyCMEKVLRE-----------SDDGVVVYVAPTKALvnqvVAEVYARFSKKYPPSGKsLWGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 466 LTGDMQLskSEILRTQMLVTTPEKWDVVTRkSVGDVALSQIVRLLILDEVHLL-HEDRGPVLESIVArtlrqvestqsMI 544
Cdd:cd18025 85 FTRDYRH--NNPMNCQVLITVPECLEILLL-SPHNASWVPRIKYVIFDEIHSIgQSEDGAVWEQLLL-----------LI 150
|
170
....*....|...
gi 2462605685 545 R--ILGLSATLPN 555
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 ... |
395-552 |
1.97e-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: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 395 ENMLICAPTGAGKTNIAMLtvlheIRQHFQQGVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLSK 474
Cdd:cd17927 18 KNTIICLPTGSGKTFVAVL-----ICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 475 S---EILRTQMLVTTPEKWdVVTRKSVGDVALSqIVRLLILDEVHllHEDRGPVLESIVARTLRQ-VESTQSMIRILGLS 550
Cdd:cd17927 93 SveqIVESSDVIIVTPQIL-VNDLKSGTIVSLS-DFSLLVFDECH--NTTKNHPYNEIMFRYLDQkLGSSGPLPQILGLT 168
|
..
gi 2462605685 551 AT 552
Cdd:cd17927 169 AS 170
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
394-721 |
5.82e-11 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 67.99 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 394 NENMLICAPTGAGKTNIAMLTVLHEIrqhFQQGVIKKNEFKI--VYVAPMKALAAEMtdyfsRR--LEPLGIIVKEL--- 466
Cdd:PRK13767 47 GKNVLISSPTGSGKTLAAFLAIIDEL---FRLGREGELEDKVycLYVSPLRALNNDI-----HRnlEEPLTEIREIAker 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 467 ------------TGDM-QLSKSEILRT--QMLVTTPEKWDVVT-----RKSVGDvalsqiVRLLILDEVHLLHED-RGPV 525
Cdd:PRK13767 119 geelpeirvairTGDTsSYEKQKMLKKppHILITTPESLAILLnspkfREKLRT------VKWVIVDEIHSLAENkRGVH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 526 LesivARTLRQVES--TQSMIRIlGLSATLPNYLDVATFLhvnpyiGLFFFDGRFRPVPLGQT-F---LGIKCANKMQQL 599
Cdd:PRK13767 193 L----SLSLERLEElaGGEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDCEIVDArFvkpFDIKVISPVDDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 600 -----NNMDEVCYENVLKQVKAGHQVMVFVHARNATVRTAMSLierakncghipfffptqghdyvlaekqvqrsrnkqvR 674
Cdd:PRK13767 262 ihtpaEEISEALYETLHELIKEHRTTLIFTNTRSGAERVLYNL------------------------------------R 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2462605685 675 ELFPDGFSI-----HHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP 721
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 ... |
1247-1405 |
8.86e-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: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1247 VLLGAPTGSGKTVAAELAIFRVFNKypTSKAVYIAPLKALVRERMDDwkvrIEEKLGKkVIELTGDVT--PDmksiakAD 1324
Cdd:cd18024 50 VLVSAHTSAGKTVVAEYAIAQSLRD--KQRVIYTSPIKALSNQKYRE----LQEEFGD-VGLMTGDVTinPN------AS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1325 LIVTTPEkwdgVSRS--WQNRNYVQQVTILIIDEIHLLGE-ERGPVLEvivsRTNFISSHTekpVRIVGLSTALANARDL 1401
Cdd:cd18024 117 CLVMTTE----ILRSmlYRGSEIMREVAWVIFDEIHYMRDkERGVVWE----ETIILLPDK---VRYVFLSATIPNARQF 185
|
....
gi 2462605685 1402 ADWL 1405
Cdd:cd18024 186 AEWI 189
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
1235-1610 |
9.95e-11 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 66.97 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1235 QIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTskaVYIAPLKALVRermdDWKVRIEEKLGKkvIELTGDVT 1314
Cdd:COG1061 91 ALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV---LVLVPRRELLE----QWAEELRRFLGD--PLAGGGKK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1315 PDmksiaKADLIVTTpekWDGVSRSWQNRNYVQQVTILIIDEIHLLGeerGPVLEVIVSRTNfisshtekPVRIVGLS-T 1393
Cdd:COG1061 162 DS-----DAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHAG---APSYRRILEAFP--------AAYRLGLTaT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1394 AlanardladwlnikqmglfnFRPSVRPVPLEVhiqgFPGQHYcprmasmNKPAFQAIRSHSPAKPVLIfvssRRQTRLT 1473
Cdd:COG1061 223 P--------------------FRSDGREILLFL----FDGIVY-------EYSLKEAIEDGYLAPPEYY----GIRVDLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1474 AlELIAFLATEEDPKQWLNMDEREMENIIATVRDSNLKL--TLAFGIGMHHA-------------------GLHERDRKT 1532
Cdd:COG1061 268 D-ERAEYDALSERLREALAADAERKDKILRELLREHPDDrkTLVFCSSVDHAealaellneagiraavvtgDTPKKEREE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1533 VEELFVNCKVQVLIATSTLAWGVNFPA--HLVIIKGTeyydgKTRRYvdfpitdVLQMMGRAGRPqfdDQGKAVILVHDI 1610
Cdd:COG1061 347 ILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPT-----GSPRE-------FIQRLGRGLRP---APGKEDALVYDF 411
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1251-1593 |
2.09e-10 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 66.49 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1251 APTGSGKTVAAEL-AIFRVF----------NKYPTSKAVYIAPLKALVRERMDDWKVRIE------EKLGKKVIELT-GD 1312
Cdd:PRK09751 3 APTGSGKTLAAFLyALDRLFreggedtreaHKRKTSRILYISPIKALGTDVQRNLQIPLKgiaderRRRGETEVNLRvGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1313 VTPDMKSIAKA-------DLIVTTPEKWDGVSRSwQNRNYVQQVTILIIDEIH-LLGEERGPVLEVIVSRTNFIsSHTek 1384
Cdd:PRK09751 83 RTGDTPAQERSkltrnppDILITTPESLYLMLTS-RARETLRGVETVIIDEVHaVAGSKRGAHLALSLERLDAL-LHT-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1385 PVRIVGLSTALANARDLADWLNIKQMGLFNFRPSVR--------PVPLEVHIQGFPGQH----YCPRMASMnKPAFQA-- 1450
Cdd:PRK09751 159 SAQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRhpqirivvPVANMDDVSSVASGTgedsHAGREGSI-WPYIETgi 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1451 IRSHSPAKPVLIFVSSRRQT-RLTAL--ELIA--FLATEEDPKqwlnmDEREMENIIATV--RDSNLKLTLAFGigmHHA 1523
Cdd:PRK09751 238 LDEVLRHRSTIVFTNSRGLAeKLTARlnELYAarLQRSPSIAV-----DAAHFESTSGATsnRVQSSDVFIARS---HHG 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462605685 1524 GLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKgteyydgktrryVDFP--ITDVLQMMGRAG 1593
Cdd:PRK09751 310 SVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQ------------VATPlsVASGLQRIGRAG 369
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1500-1594 |
4.11e-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: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1500 NIIATVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-AHLVIIkgteyYDgktrryV 1578
Cdd:pfam00271 23 QTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----YD------L 91
|
90
....*....|....*.
gi 2462605685 1579 DFPITDVLQMMGRAGR 1594
Cdd:pfam00271 92 PWNPASYIQRIGRAGR 107
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1247-1406 |
4.39e-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: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1247 VLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEKLGKKVIELTGDVTPD--MKSIAKAD 1324
Cdd:cd18025 19 ALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYPPSGKSLWGVFTRDyrHNNPMNCQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1325 LIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIHLLG-EERGPVLEVIVsrtnfisshTEKPVRIVGLSTALANARDLAD 1403
Cdd:cd18025 99 VLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGqSEDGAVWEQLL---------LLIPCPFLALSATIGNPQKFHE 169
|
...
gi 2462605685 1404 WLN 1406
Cdd:cd18025 170 WLQ 172
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1230-1413 |
7.12e-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: 7.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1230 NPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIfrVFNKYPTSKAVYIAPLKALVRERMDDWKVRIEEklgkkVIEL 1309
Cdd:cd18027 10 DVFQKQAILHLEAGD-SVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGD-----VGLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1310 TGDVT--PDMKSiakadLIVTTPekwdgVSRS--WQNRNYVQQVTILIIDEIHLLGE-ERGPVLEVIVSrtnFISSHtek 1384
Cdd:cd18027 82 TGDVQlnPEASC-----LIMTTE-----ILRSmlYNGSDVIRDLEWVIFDEVHYINDaERGVVWEEVLI---MLPDH--- 145
|
170 180 190
....*....|....*....|....*....|
gi 2462605685 1385 pVRIVGLSTALANARDLADWLN-IKQMGLF 1413
Cdd:cd18027 146 -VSIILLSATVPNTVEFADWIGrIKKKNIY 174
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1226-1392 |
1.15e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 63.75 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1226 FSHFNPVQTQIFhTLYHTDCNVLLGAPTGSGKTVAAELAI----FRVFNK-------YptskAVYIAPLKAL---VRERM 1291
Cdd:PRK13767 30 FGTFTPPQRYAI-PLIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREgeledkvY----CLYVSPLRALnndIHRNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1292 DDWKVRIEEKLGKKVIEL--------TGDVTPDMKS--------IakadLIvTTPEKWDGVSRSWQNRNYVQQVTILIID 1355
Cdd:PRK13767 105 EEPLTEIREIAKERGEELpeirvairTGDTSSYEKQkmlkkpphI----LI-TTPESLAILLNSPKFREKLRTVKWVIVD 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462605685 1356 EIHLLGE-ERGPVLEVIVSRTNFISSHteKPVRIvGLS 1392
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 ... |
1246-1402 |
1.66e-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: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVR---ERMDDWKVRIEEKLgkKVIELTGDvTP--DMKSI 1320
Cdd:cd17923 17 SVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQdqlRSLRELLEQLGLGI--RVATYDGD-TPreERRAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1321 AK--ADLIVTTP-----------EKWDGVSRSWQnrnYVqqvtilIIDEIH----LLGEERGPVLEVIVSRTNFISSHte 1383
Cdd:cd17923 94 IRnpPRILLTNPdmlhyallphhDRWARFLRNLR---YV------VLDEAHtyrgVFGSHVALLLRRLRRLCRRYGAD-- 162
|
170
....*....|....*....
gi 2462605685 1384 kpVRIVGLSTALANARDLA 1402
Cdd:cd17923 163 --PQFILTSATIGNPAEHA 179
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
383-551 |
2.94e-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: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 383 QSIVFETAynTNENMLICAPTGAGKTNIA-MLtvlheIRQ-HFQQGVIKKNEFKIVYVAPMKALAAEMTDYFsRRLEPLG 460
Cdd:cd18034 7 QLELFEAA--LKRNTIVVLPTGSGKTLIAvML-----IKEmGELNRKEKNPKKRAVFLVPTVPLVAQQAEAI-RSHTDLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 461 iiVKELTGDMQLS-------KSEILRTQMLVTTPEKW-DVVTRksvGDVALSQIvRLLILDEVHL---LHEDRGpvlesi 529
Cdd:cd18034 79 --VGEYSGEMGVDkwtkerwKEELEKYDVLVMTAQILlDALRH---GFLSLSDI-NLLIFDECHHatgDHPYAR------ 146
|
170 180
....*....|....*....|..
gi 2462605685 530 VARTLRQVESTQSMIRILGLSA 551
Cdd:cd18034 147 IMKEFYHLEGRTSRPRILGLTA 168
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
395-560 |
3.02e-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: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 395 ENMLICAPTGAGKTNIAMLTVLHEIrqhfqqgvIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPL--GIIVKELTGDMQL 472
Cdd:cd17923 16 RSVVVTTGTASGKSLCYQLPILEAL--------LRDPGSRALYLYPTKALAQDQLRSLRELLEQLglGIRVATYDGDTPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 473 SKSEILRTQ---MLVTTPEKWDV-VTRKSVGDVALSQIVRLLILDEVHLLhedRGpVLESIVA----RTLRQVESTQSMI 544
Cdd:cd17923 88 EERRAIIRNpprILLTNPDMLHYaLLPHHDRWARFLRNLRYVVLDEAHTY---RG-VFGSHVAlllrRLRRLCRRYGADP 163
|
170
....*....|....*.
gi 2462605685 545 RILGLSATLPNYLDVA 560
Cdd:cd17923 164 QFILTSATIGNPAEHA 179
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
354-762 |
2.77e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 58.88 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 354 SFEEKPVYIQDLDEiGQLAFKGMKRLNRIQSIVFETAYNT----NENMLICAPTGAGKTNIAMLTvlheIRQHFQQGvik 429
Cdd:COG1061 57 DTERELAEAEALEA-GDEASGTSFELRPYQQEALEALLAAlergGGRGLVVAPTGTGKTVLALAL----AAELLRGK--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 430 knefKIVYVAPMKAL----AAEMTDYFSRRLEPLGiiVKELTGDmqlskseilrtqMLVTTpekWDVVTRKSVGDvALSQ 505
Cdd:COG1061 129 ----RVLVLVPRRELleqwAEELRRFLGDPLAGGG--KKDSDAP------------ITVAT---YQSLARRAHLD-ELGD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 506 IVRLLILDEVHLLhedrgpvlesiVARTLRQVESTQSMIRILGLSATlPNYLDVATflhvnpyIGLFFFDG-RFRpVPLG 584
Cdd:COG1061 187 RFGLVIIDEAHHA-----------GAPSYRRILEAFPAAYRLGLTAT-PFRSDGRE-------ILLFLFDGiVYE-YSLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 585 Q----------TFLGIKcaNKMQQLNNMDEVCYENVLKQVKAGHQvmvfvharnATVRTAMSLIERAKNCGHIPFFFPTQ 654
Cdd:COG1061 247 EaiedgylappEYYGIR--VDLTDERAEYDALSERLREALAADAE---------RKDKILRELLREHPDDRKTLVFCSSV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 655 GHDYVLAEkqvqrsrnkqvrELFPDGFSIH--HAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIikgtqI 732
Cdd:COG1061 316 DHAEALAE------------LLNEAGIRAAvvTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVA-----I 378
|
410 420 430
....*....|....*....|....*....|
gi 2462605685 733 YAAKRGSfvdLGILdvMQIFGRAGRPQFDK 762
Cdd:COG1061 379 LLRPTGS---PREF--IQRLGRGLRPAPGK 403
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
399-756 |
4.29e-08 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 58.78 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 399 ICAPTGAGKTNIAMltvLHEIRQHFQQGVI------KKNEFKIVYVAPMKALAAEMTDYFSRRLEPLG------------ 460
Cdd:PRK09751 1 VIAPTGSGKTLAAF---LYALDRLFREGGEdtreahKRKTSRILYISPIKALGTDVQRNLQIPLKGIAderrrrgetevn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 461 IIVKELTGDMQLS-KSEILRT--QMLVTTPEKWDVV----TRKSVGDVAlsqivrLLILDEVHLLH-EDRGPVLesivAR 532
Cdd:PRK09751 78 LRVGIRTGDTPAQeRSKLTRNppDILITTPESLYLMltsrARETLRGVE------TVIIDEVHAVAgSKRGAHL----AL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 533 TLRQVEST--QSMIRIlGLSATLPNYLDVATFLhvnpyiglfffdGRFRPV----PLGQTFLGIKCANKMQQLNNMDEVC 606
Cdd:PRK09751 148 SLERLDALlhTSAQRI-GLSATVRSASDVAAFL------------GGDRPVtvvnPPAMRHPQIRIVVPVANMDDVSSVA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 607 YE-------------------NVLKQVKAGHQVMVFVHARNATVRTAMSLIE--RAKNCGHIPFFFPTQGHDYVLA--EK 663
Cdd:PRK09751 215 SGtgedshagregsiwpyietGILDEVLRHRSTIVFTNSRGLAEKLTARLNElyAARLQRSPSIAVDAAHFESTSGatSN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 664 QVQRSRNKQVRElfpdgfsiHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVIIkgtQIYAAkrgsfvdL 743
Cdd:PRK09751 295 RVQSSDVFIARS--------HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVI---QVATP-------L 356
|
410
....*....|...
gi 2462605685 744 GILDVMQIFGRAG 756
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 ... |
1246-1359 |
4.76e-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: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKYP---TSKAVYIAPLKALVRERMDDWKvRIEEKLGKKVIELTGDVTPDM---KS 1319
Cdd:cd17927 19 NTIICLPTGSGKTFVAVLICEHHLKKFPagrKGKVVFLANKVPLVEQQKEVFR-KHFERPGYKVTGLSGDTSENVsveQI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462605685 1320 IAKADLIVTTP-------EKWDGVSRSwqnrnyvqQVTILIIDEIHL 1359
Cdd:cd17927 98 VESSDVIIVTPqilvndlKSGTIVSLS--------DFSLLVFDECHN 136
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1246-1358 |
9.13e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 53.83 E-value: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKvrieeKLGKKVIELTGDVTPDMKSIAK--A 1323
Cdd:pfam04851 25 RGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFK-----KFLPNYVEIGEIISGDKKDESVddN 99
|
90 100 110
....*....|....*....|....*....|....*
gi 2462605685 1324 DLIVTTPEKWDGVSRSWQNRNYVQQVTILIIDEIH 1358
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 ... |
393-553 |
1.14e-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: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 393 TNENMLICAPTGAGKTNIAMLTVLHEIRQhFQQGviKKNefKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQL 472
Cdd:cd18073 16 KGKNTIICAPTGCGKTFVSLLICEHHLKK-FPQG--QKG--KVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGATAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 473 SKSE---ILRTQMLVTTPEKwdVVTRKSVGDVALSQIVRLLILDEVHllHEDRGPVLESIVARTLRQ--VESTQSMIRIL 547
Cdd:cd18073 91 NVPVeqiIENNDIIILTPQI--LVNNLKKGTIPSLSIFTLMIFDECH--NTSGNHPYNMIMFRYLDQklGGSSGPLPQII 166
|
....*.
gi 2462605685 548 GLSATL 553
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 ... |
342-560 |
1.43e-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: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 342 EVRIPYS-EPMPLSFEEKPV-----YIQDLDEIGQLAFKGMKRlnriqsivfetayntNENMLICAPTGAGKTNIAMLTV 415
Cdd:cd18024 4 EVALPPDyDYTPISAHKPPGnpartYPFTLDPFQKTAIACIER---------------NESVLVSAHTSAGKTVVAEYAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 416 LHEIRqhfqqgvikkNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIvkelTGDMQLSKS--------EILRTqMLVTTP 487
Cdd:cd18024 69 AQSLR----------DKQRVIYTSPIKALSNQKYRELQEEFGDVGLM----TGDVTINPNasclvmttEILRS-MLYRGS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462605685 488 EkwdvVTRKsvgdvalsqiVRLLILDEVHLLHE-DRGPVLE-SIVArtlrqvesTQSMIRILGLSATLPNYLDVA 560
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 ... |
394-514 |
1.48e-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: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 394 NENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGvikknEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLS 473
Cdd:cd17957 27 GRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK-----GLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEAK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462605685 474 KSE----ILRTQMLVTTPEKwdVVTRKSVGDVALSQiVRLLILDE 514
Cdd:cd17957 102 AKDgpksITKYDILVSTPLR--LVFLLKQGPIDLSS-VEYLVLDE 143
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
1251-1377 |
2.01e-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: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1251 APTGSGKTVAAELAIFRVFNKyptsKAVYIAPLKALVrermDDWKVRIEEKLGKKVI-ELTGDVTpdmKSIAKADLIVTT 1329
Cdd:cd17926 25 LPTGSGKTLTALALIAYLKEL----RTLIVVPTDALL----DQWKERFEDFLGDSSIgLIGGGKK---KDFDDANVVVAT 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462605685 1330 PEkwdgvSRSWQN---RNYVQQVTILIIDEIHLLGeerGPVLEVIVSRTNF 1377
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 ... |
395-554 |
2.22e-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: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 395 ENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGvikkNEFKIVYVAPMKALAAEMTDYFSRRLEPlGIIVKELTGDMQLSK 474
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAG----EKGRVVVLVNKVPLVEQQLEKFFKYFRK-GYKVTGLSGDSSHKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 475 S---EILRTQMLVTTPEKWDVVTRKSVGDVALS-QIVRLLILDEVHllHEDRGPVLESIVARTLRQ-VESTQSMIRILGL 549
Cdd:cd18036 93 SfgqIVKASDVIICTPQILINNLLSGREEERVYlSDFSLLIFDECH--HTQKEHPYNKIMRMYLDKkLSSQGPLPQILGL 170
|
....*
gi 2462605685 550 SATLP 554
Cdd:cd18036 171 TASPG 175
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
394-516 |
3.64e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.51 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 394 NENMLICAPTGAGKTNIAMLTVLHeirqhfqqgVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDMQLS 473
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE---------RLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462605685 474 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivrLLILDEVH 516
Cdd:COG1111 88 KRKELweKARIIVATPQviENDLIAgRIDLDDVS------LLIFDEAH 129
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
377-711 |
4.70e-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: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 377 KRLNRIQSIVFETAYNTNEN----MLICAPTGAGKTNIAMLTVLHEIRQHFQQGVIkknefkivYVAPMKAL----AAEM 448
Cdd:COG1203 126 TPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKHGGRRII--------YALPFTSIinqtYDRL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 449 TDYF--------SRRLEPLGIIVKELTGDMQLSK--SEILRTQMLVTTPekwD-----VVTRKSvgdvalSQIVRL---- 509
Cdd:COG1203 198 RDLFgedvllhhSLADLDLLEEEEEYESEARWLKllKELWDAPVVVTTI---DqlfesLFSNRK------GQERRLhnla 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 510 ---LILDEVHLL-HEDRGPVLesivaRTLRQVESTQSmiRILGLSATLPNYLDVATF------LHVNPYIGLFFFDGRFR 579
Cdd:COG1203 269 nsvIILDEVQAYpPYMLALLL-----RLLEWLKNLGG--SVILMTATLPPLLREELLeayeliPDEPEELPEYFRAFVRK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 580 PVplgqtflgikcanKMQQLNNMDEVCYENVLKQVKAGHQVMVFVharnATVRTAMSLierakncghipfffptqghdYv 659
Cdd:COG1203 342 RV-------------ELKEGPLSDEELAELILEALHKGKSVLVIV----NTVKDAQEL--------------------Y- 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462605685 660 laekqvqrsrnKQVRELFPDGFSIH-HAGMLRQDRNLVEN----LFSNGHIKVLVCT 711
Cdd:COG1203 384 -----------EALKEKLPDEEVYLlHSRFCPADRSEIEKeikeRLERGKPCILVST 429
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1202-1420 |
4.86e-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: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1202 TELLDLQPLPITALGCKAYEALYNF-----SHFNPVQTQIFHTLYHTDCN----VLLGAPTGSGKTVAAELAIFRVFNKY 1272
Cdd:COG1203 96 SANFDMARQALDHLLAERLERLLPKkskprTPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALRLAAKH 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1273 PTSKAVYIAPLKALVrERMDDwkvRIEEKLGKKVIELTGDVTPDMKSIAK-----------------ADLIVTTPEK-WD 1334
Cdd:COG1203 176 GGRRIIYALPFTSII-NQTYD---RLRDLFGEDVLLHHSLADLDLLEEEEeyesearwlkllkelwdAPVVVTTIDQlFE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1335 GV--SRSWQNRNYVQQVT-ILIIDEIHLLGEERGPVLEvivsrtNFISSHTEKPVRIVgLSTA---------LANARDLA 1402
Cdd:COG1203 252 SLfsNRKGQERRLHNLANsVIILDEVQAYPPYMLALLL------RLLEWLKNLGGSVI-LMTAtlppllreeLLEAYELI 324
|
250
....*....|....*...
gi 2462605685 1403 DWLNIKQMGLFNFRPSVR 1420
Cdd:COG1203 325 PDEPEELPEYFRAFVRKR 342
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
607-757 |
5.64e-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: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 607 YENVLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNcghipfffptqghdyvlaekqvqrsrnkqvrELFPDGFSIHHA 686
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPD-------------------------------RVPPDFIALHHG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462605685 687 GMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPA-HAVIikgtQIYAAKrgsfvdlGILDVMQIFGRAGR 757
Cdd:cd18796 77 SLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDvDLVI----QIGSPK-------SVARLLQRLGRSGH 137
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
1246-1372 |
5.97e-07 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 51.91 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVR---ERMDDW--KVRIEEKLGkkviELTGDVTPDM--K 1318
Cdd:cd17930 3 LVILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINqmyERIREIlgRLDDEDKVL----LLHSKAALELleS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1319 SIAKADLIVTTPEKWDGVSRSWqNRNYVqqVT-------------------------ILIIDEIHLLGEER-GPVLEVIV 1372
Cdd:cd17930 79 DEEPDDDPVEAVDWALLLKRSW-LAPIV--VTtidqllesllkykhferrlhglansVVVLDEVQAYDPEYmALLLKALL 155
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
398-646 |
1.04e-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: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 398 LICAPTGAGKTNIAMLTVLHEIRQhfqqgvikKNEFKIVYVAPMKALAAEMTDYFSRRL-EPLGIIVKELTGD--MQLSK 474
Cdd:cd09639 3 VIEAPTGYGKTEAALLWALHSLKS--------QKADRVIIALPTRATINAMYRRAKEAFgETGLYHSSILSSRikEMGDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 475 SEILR--------------TQMLVTTPEKWDVVTRKSVG--DVALSQIVR-LLILDEVHLLHEDrgpVLESIVA--RTLR 535
Cdd:cd09639 75 EEFEHlfplyihsndtlflDPITVCTIDQVLKSVFGEFGhyEFTLASIANsLLIFDEVHFYDEY---TLALILAvlEVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 536 QVEstqsmIRILGLSATLPNYLDvATFLHVNPYIGLFFFDGRFRpvplgQTFLGIKCANKMqqlnNMDEVCYENVLKQVK 615
Cdd:cd09639 152 DND-----VPILLMSATLPKFLK-EYAEKIGYVEENEPLDLKPN-----ERAPFIKIESDK----VGEISSLERLLEFIK 216
|
250 260 270
....*....|....*....|....*....|.
gi 2462605685 616 AGHQVMVFVHarnaTVRTAMSLIERAKNCGH 646
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 ... |
383-552 |
1.50e-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: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 383 QSIVFETAYNtneNMLICAPTGAGKTNIAMLTVLHEIRQhFQQGvikknefKIVYVAPMKALAAEMTDYFsrrLEPLGI- 461
Cdd:cd18033 8 FTIVQKALFQ---NTLVALPTGLGKTFIAAVVMLNYYRW-FPKG-------KIVFMAPTKPLVSQQIEAC---YKITGIp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 462 --IVKELTGDMQLSK-SEILRT-QMLVTTPEKwdVVTRKSVGDVALSQIVrLLILDEVhllHEDRGPVLESIVARTLRQV 537
Cdd:cd18033 74 ssQTAELTGSVPPTKrAELWASkRVFFLTPQT--LENDLKEGDCDPKSIV-CLVIDEA---HRATGNYAYCQVVRELMRY 147
|
170
....*....|....*
gi 2462605685 538 ESTqsmIRILGLSAT 552
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 ... |
1229-1358 |
1.54e-06 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 50.40 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1229 FNPVQTQIFHtlyhtdcNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKvRIEEKLGKKVIE 1308
Cdd:cd18033 8 FTIVQKALFQ-------NTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACY-KITGIPSSQTAE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462605685 1309 LTGDVTPDMKSI--AKADLIVTTPEKWDGVSRSwqNRNYVQQVTILIIDEIH 1358
Cdd:cd18033 80 LTGSVPPTKRAElwASKRVFFLTPQTLENDLKE--GDCDPKSIVCLVIDEAH 129
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
681-757 |
1.71e-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: 1.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462605685 681 FSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLP-AHAVIIkgtqiyaakrgSFVDLGILDVMQIFGRAGR 757
Cdd:pfam00271 41 VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-----------YDLPWNPASYIQRIGRAGR 107
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
396-516 |
1.71e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 53.34 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 396 NMLICAPTGAGKTNIAMLTVLheirqhfqqGVIKKNEFKIVYVAPMKALAAEMTDYFSR--RLEPLGIIVkeLTGDMQLS 473
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIA---------ERLHKKGGKVLILAPTKPLVEQHAEFFRKflNIPEEKIVV--FTGEVSPE 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462605685 474 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivrLLILDEVH 516
Cdd:PRK13766 100 KRAELweKAKVIVATPQviENDLIAgRISLEDVS------LLIFDEAH 141
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
1246-1358 |
1.89e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 53.20 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKyPTSKAVYIAPLKALVRERMDDWKvRIEEKLGKKVIELTGDVTPD--MKSIAKA 1323
Cdd:COG1111 19 NTLVVLPTGLGKTAVALLVIAERLHK-KGGKVLFLAPTKPLVEQHAEFFK-EALNIPEDEIVVFTGEVSPEkrKELWEKA 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462605685 1324 DLIVTTPE--KWDGVSrswqNRNYVQQVTILIIDEIH 1358
Cdd:COG1111 97 RIIVATPQviENDLIA----GRIDLDDVSLLIFDEAH 129
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
395-563 |
2.33e-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: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 395 ENMLICAPTGAGKTNIAMLTVlheirqhfqqGVIKKNEFKIVYVAPMKALAAEMTDYFSRRLEPLGIIvkelTGDMQLS- 473
Cdd:cd18027 24 DSVFVAAHTSAGKTVVAEYAI----------ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGLI----TGDVQLNp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 474 -------KSEILRTqMLVTTPEkwdvVTRKsvgdvalsqiVRLLILDEVHLLHE-DRGPVLESIVARTLRQVestqsmiR 545
Cdd:cd18027 90 easclimTTEILRS-MLYNGSD----VIRD----------LEWVIFDEVHYINDaERGVVWEEVLIMLPDHV-------S 147
|
170
....*....|....*...
gi 2462605685 546 ILGLSATLPNYLDVATFL 563
Cdd:cd18027 148 IILLSATVPNTVEFADWI 165
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
395-558 |
2.72e-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: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 395 ENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGVIkknefkivYVAPMKALA----AEMTDYFSRRLEPLGII-------V 463
Cdd:cd17930 2 GLVILEAPTGSGKTEAALLWALKLAARGGKRRII--------YALPTRATInqmyERIREILGRLDDEDKVLllhskaaL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 464 KELTGDMQLSKSEILRTQMLVTTPEKWD---VVTrksVGDVAL-------SQIVRL-------LILDEVHLLhedrGPVL 526
Cdd:cd17930 74 ELLESDEEPDDDPVEAVDWALLLKRSWLapiVVT---TIDQLLesllkykHFERRLhglansvVVLDEVQAY----DPEY 146
|
170 180 190
....*....|....*....|....*....|..
gi 2462605685 527 ESIVARTLRQVESTQSmIRILGLSATLPNYLD 558
Cdd:cd17930 147 MALLLKALLELLGELG-GPVVLMTATLPALLR 177
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
374-565 |
5.25e-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: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 374 KGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTNIAMLTVLHEIRQHFQQGVIKKNEFKIVYVAPMKALAAEMTDYFS 453
Cdd:cd17948 8 QGITKPTTVQKQGIPSILR-GRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNAPRGLVITPSRELAEQIGSVAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 454 RRLEPLGIIVKELTGDMqlSKSEILRTQM-----LVTTPEK-WDVVTRksvGDVALSQiVRLLILDEVH-LLHEDRGPVL 526
Cdd:cd17948 87 SLTEGLGLKVKVITGGR--TKRQIRNPHFeevdiLVATPGAlSKLLTS---RIYSLEQ-LRHLVLDEADtLLDDSFNEKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462605685 527 ESIVART---LRQVESTQSMIR---ILGLSATLPNYL--------DVATFLHV 565
Cdd:cd17948 161 SHFLRRFplaSRRSENTDGLDPgtqLVLVSATMPSGVgevlskviDVDSIETV 213
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
1246-1398 |
5.81e-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: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRV-----FNKYPTSKAVYIAPLKALVRERMDdwkvRIEEKLGKKVIELTGDVTPDMKS- 1319
Cdd:cd18034 18 NTIVVLPTGSGKTLIAVMLIKEMgelnrKEKNPKKRAVFLVPTVPLVAQQAE----AIRSHTDLKVGEYSGEMGVDKWTk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1320 ------IAKADLIVTTPEkwdgVSRSWQNRNYVQ--QVTILIIDEIHLLGEERgpVLEVIVSRTNFISSHTEKPvRIVGL 1391
Cdd:cd18034 94 erwkeeLEKYDVLVMTAQ----ILLDALRHGFLSlsDINLLIFDECHHATGDH--PYARIMKEFYHLEGRTSRP-RILGL 166
|
....*..
gi 2462605685 1392 STALANA 1398
Cdd:cd18034 167 TASPVNG 173
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
371-567 |
1.29e-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: 48.21 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 371 LAFKGMKRLNRIQSIVFETAYNtNENMLICAPTGAGKTnIA-MLTVLHEIRqhfQQGVIKKNEFKIVYVAPMKALAAEMT 449
Cdd:cd00268 5 LKKLGFEKPTPIQAQAIPLILS-GRDVIGQAQTGSGKT-LAfLLPILEKLL---PEPKKKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 450 DYFSRRLEPLGIIVKELTGDMQLSKSEIL---RTQMLVTTPEK-WDVVTRksvGDVALSQiVRLLILDEV-HLLHEDRGP 524
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEAlkkGPDIVVGTPGRlLDLIER---GKLDLSN-VKYLVLDEAdRMLDMGFEE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462605685 525 VLESIVARTLRQvesTQSMIrilgLSATLPNYLD--VATFLHvNP 567
Cdd:cd00268 156 DVEKILSALPKD---RQTLL----FSATLPEEVKelAKKFLK-NP 192
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
392-552 |
2.36e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.51 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 392 NTNENMLICAPTGAGKTniamLTVLHEIRQHFQQGVIKknefKIVYVAPMKALAAEMTDYFSRRLEPLGIIVKELTGDmq 471
Cdd:pfam04851 21 NGQKRGLIVMATGSGKT----LTAAKLIARLFKKGPIK----KVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 472 lSKSEILRT-QMLVTTPEKWDVVTRKSVGDVALSQIVrLLILDEVHllhedRGPvlesivARTLRQVESTQSMIRILGLS 550
Cdd:pfam04851 91 -KKDESVDDnKIVVTTIQSLYKALELASLELLPDFFD-VIIIDEAH-----RSG------ASSYRNILEYFKPAFLLGLT 157
|
..
gi 2462605685 551 AT 552
Cdd:pfam04851 158 AT 159
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
394-516 |
4.76e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 46.35 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 394 NENMLICAPTGAGKTNIAMLTVLheirqhfqqGVIKKNEFKIVYVAPMKALAAEMTDYFsRRLEPLGIIVKELTGDMQLS 473
Cdd:cd18035 16 NGNTLIVLPTGLGKTIIAILVAA---------DRLTKKGGKVLILAPSRPLVEQHAENL-KRVLNIPDKITSLTGEVKPE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462605685 474 KSEIL--RTQMLVTTPE--KWDVVT-RKSVGDVAlsqivrLLILDEVH 516
Cdd:cd18035 86 ERAERwdASKIIVATPQviENDLLAgRITLDDVS------LLIFDEAH 127
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
1246-1358 |
5.08e-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: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKYpTSKAVYIAPLKALVRERMDDWKVRIEEKLgkKVIELTGDVTPDMKS--IAKA 1323
Cdd:cd18035 18 NTLIVLPTGLGKTIIAILVAADRLTKK-GGKVLILAPSRPLVEQHAENLKRVLNIPD--KITSLTGEVKPEERAerWDAS 94
|
90 100 110
....*....|....*....|....*....|....*
gi 2462605685 1324 DLIVTTPEKWDgvSRSWQNRNYVQQVTILIIDEIH 1358
Cdd:cd18035 95 KIIVATPQVIE--NDLLAGRITLDDVSLLIFDEAH 127
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
1246-1358 |
1.06e-04 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 47.56 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKYPtSKAVYIAPLKALVRERMDDWK--VRIEEklgKKVIELTGDVTPD--MKSIA 1321
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIAERLHKKG-GKVLILAPTKPLVEQHAEFFRkfLNIPE---EKIVVFTGEVSPEkrAELWE 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462605685 1322 KADLIVTTPE--KWDGVSrswqNRNYVQQVTILIIDEIH 1358
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 ... |
1451-1594 |
1.92e-04 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 43.79 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1451 IRSHSPAKPVLIFVSSRRQTrltaleliaflateedpkqwlnmderemENIIATVRDSNLKLTLAFGIGMHHAGLHERDR 1530
Cdd:cd18796 32 IFLLERHKSTLVFTNTRSQA----------------------------ERLAQRLRELCPDRVPPDFIALHHGSLSRELR 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462605685 1531 KTVEELFVNCKVQVLIATSTLAWGVNFPA-HLVIIKGTEYydgktrryvdfPITDVLQMMGRAGR 1594
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 ... |
1226-1358 |
6.81e-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: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1226 FSHFNPVQTQ-IFHTLYHTDCNVLLgaPTGSGKTVAAELAIFrVFNKyPTskaVYIAPLKALvrerMDDwKVRIEEKLGK 1304
Cdd:cd17920 10 YDEFRPGQLEaINAVLAGRDVLVVM--PTGGGKSLCYQLPAL-LLDG-VT---LVVSPLISL----MQD-QVDRLQQLGI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462605685 1305 KVIELTGDVTPDMKSIA-------KADLIVTTPEK--WDGVSRSWQNRNYVQQVTILIIDEIH 1358
Cdd:cd17920 78 RAAALNSTLSPEEKREVllrikngQYKLLYVTPERllSPDFLELLQRLPERKRLALIVVDEAH 140
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
375-554 |
1.15e-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: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 375 GMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTnIAML--TVLHEIRQHFQQgviKKNEFKIVYVAPMKALAAEMTDYF 452
Cdd:cd17964 13 GFETMTPVQQKTLKPILSTGDDVLARAKTGTGKT-LAFLlpAIQSLLNTKPAG---RRSGVSALIISPTRELALQIAAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 453 SRRLEPL-GIIVKELTGDMQLSKSEI----LRTQMLVTTPEKW-DVVTRKSVGDVALSqiVRLLILDEV-HLLheDRG-- 523
Cdd:cd17964 89 KKLLQGLrKLRVQSAVGGTSRRAELNrlrrGRPDILVATPGRLiDHLENPGVAKAFTD--LDYLVLDEAdRLL--DMGfr 164
|
170 180 190
....*....|....*....|....*....|.
gi 2462605685 524 PVLESIVaRTLRQVESTQsmIRILGLSATLP 554
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 ... |
388-553 |
1.27e-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: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 388 ETAYNTNENMLICAPTGAGKTNIAMLTVLHEIRQHFQqgvikknefKIVYVAPMKALAAEMTDYFSR-RLEPLGIIVK-E 465
Cdd:cd17990 11 RAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGG---------KIIVLEPRRVAARAAARRLATlLGEAPGETVGyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 466 LTGDMQLSKseilRTQMLVTTPekwDVVTRKSVGDVALSQiVRLLILDEVHllheDRGPVLESIVARTLRQVESTQSMIR 545
Cdd:cd17990 82 VRGESRVGR----RTRVEVVTE---GVLLRRLQRDPELSG-VGAVILDEFH----ERSLDADLALALLLEVQQLLRDDLR 149
|
....*...
gi 2462605685 546 ILGLSATL 553
Cdd:cd17990 150 LLAMSATL 157
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
1246-1358 |
1.36e-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: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1246 NVLLGAPTGSGKTVAAELAIFRVFNKYP----TSKAVYIAPLKALVRERMDDWKVRIEEklGKKVIELTGD--VTPDMKS 1319
Cdd:cd18036 19 NTIICAPTGSGKTRVAVYICRHHLEKRRsageKGRVVVLVNKVPLVEQQLEKFFKYFRK--GYKVTGLSGDssHKVSFGQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462605685 1320 IAKA-DLIVTTPEKWDGVSRS--WQNRNYVQQVTILIIDEIH 1358
Cdd:cd18036 97 IVKAsDVIICTPQILINNLLSgrEEERVYLSDFSLLIFDECH 138
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
390-553 |
1.73e-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: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 390 AYNTNENMLICAPTGAGKTNIAMLtvlheirqhfqqgVIKKN-EFKIVYVAPMKALAAEMTDYFSRRLEPlgIIVKELTG 468
Cdd:cd17926 14 AHKNNRRGILVLPTGSGKTLTALA-------------LIAYLkELRTLIVVPTDALLDQWKERFEDFLGD--SSIGLIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 469 DmqlSKSEILRTQMLVTTPEK--WDVVTRKSVGDVALsqivrLLILDEVHllhedRGPvlesivARTLRQVESTQSMIRI 546
Cdd:cd17926 79 G---KKKDFDDANVVVATYQSlsNLAEEEKDLFDQFG-----LLIVDEAH-----HLP------AKTFSEILKELNAKYR 139
|
....*..
gi 2462605685 547 LGLSATL 553
Cdd:cd17926 140 LGLTATP 146
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
1231-1356 |
1.92e-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: 41.81 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1231 PVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIF---RVFNKYPTSKAVYIAPLKAL----VRErmddwKVRIEEKLG 1303
Cdd:cd17957 15 PIQMQAIPILLHGR-DLLACAPTGSGKTLAFLIPILqklGKPRKKKGLRALILAPTRELasqiYRE-----LLKLSKGTG 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462605685 1304 KKVIELTGDVTP----DMKSIAKADLIVTTPE------KWDGVSRSWqnrnyvqqVTILIIDE 1356
Cdd:cd17957 89 LRIVLLSKSLEAkakdGPKSITKYDILVSTPLrlvfllKQGPIDLSS--------VEYLVLDE 143
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
1522-1594 |
1.95e-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: 40.27 E-value: 1.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462605685 1522 HAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFP-----AHLVIIKGTE-YYdgktrryvdfpitdvlQMMGRAGR 1594
Cdd:cd18794 61 HAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPdvrfvIHYSLPKSMEsYY----------------QESGRAGR 123
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
1224-1383 |
2.59e-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: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1224 YNFSHFNPVQTQIFHTLYHTDcNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAV-YIAPLkALV----RERMDdwKVR- 1297
Cdd:cd17948 8 QGITKPTTVQKQGIPSILRGR-NTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpFNAPR-GLVitpsRELAE--QIGs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1298 ----IEEKLGKKVIELTGDVTpdMKSI-----AKADLIVTTPekwDGVSRSWQNRNY-VQQVTILIIDEIH-LLGEERGP 1366
Cdd:cd17948 84 vaqsLTEGLGLKVKVITGGRT--KRQIrnphfEEVDILVATP---GALSKLLTSRIYsLEQLRHLVLDEADtLLDDSFNE 158
|
170
....*....|....*..
gi 2462605685 1367 VLEVIVSRTNFISSHTE 1383
Cdd:cd17948 159 KLSHFLRRFPLASRRSE 175
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
383-517 |
5.48e-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: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 383 QSIVFETAYNTNEN-MLICAPTGAGKTNIAMLTVLHEirqhfqqgvikknEFKIVYVAPMKALA-------AEMTDYFSR 454
Cdd:cd09710 2 QVATFEALQSKDADiIFNTAPTGAGKTLAWLTPLLHG-------------ENKAIALYPTNALIedqteaiKEFVDDANP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 455 RLEPLGIIVKELT-----GDMQLSKSEIL-----------RTQMLVTTPEKWDVVTR-----KSVGDVALSQIVRLLILD 513
Cdd:cd09710 69 RHQVKSLSASDITlwpndKNVGSSKGEKLynllrndigtsTPIILLTNPDIFVYLTRfayidRGDIAAGFYTKFSTVIFD 148
|
....
gi 2462605685 514 EVHL 517
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 ... |
1544-1594 |
6.36e-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: 6.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2462605685 1544 VLIATSTLAWGVNFPAHLVIIKGTEYYDGKTRRyvDFPITDVLQMMGRAGR 1594
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 ... |
1225-1330 |
8.85e-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: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1225 NFSHFNPVQTQIFHTLYHTD--------CNVLLGAPTGSGKTVAAELAIFRVFNKYPTSK--AVYIAPLKAL---VRERM 1291
Cdd:cd17956 9 GITSAFPVQAAVIPWLLPSSkstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRlrALIVVPTKELvqqVYKVF 88
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462605685 1292 DdwkvRIEEKLGKKVIELTG--DVTPDMKSIA---------KADLIVTTP 1330
Cdd:cd17956 89 E----SLCKGTGLKVVSLSGqkSFKKEQKLLLvdtsgrylsRVDILVATP 134
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