|
Name |
Accession |
Description |
Interval |
E-value |
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
121-653 |
6.24e-108 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 349.19 E-value: 6.24e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 121 LSTTILPDSFRGvFKFTEFNKMQSEAFPSIYESNENCIISSPTGSGKTVLFELAILRLIKetnsdtNNTKIIYIAPTKSL 200
Cdd:COG1204 6 LPLEKVIEFLKE-RGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALL------NGGKALYIVPLRAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 201 CYEMY---KNWFPSFvNLSVGMLTSDTsFLETEKAKKCNIIITTPEKWDLLTRRwsDYSRLFElVKLVLVDEIHTIK-EK 276
Cdd:COG1204 79 ASEKYrefKRDFEEL-GIKVGVSTGDY-DSDDEWLGRYDILVATPEKLDSLLRN--GPSWLRD-VDLVVVDEAHLIDdES 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 277 RGASLEVILTRMNTMCQNIRFVALSATVPNIEDLALWLktNNELpanilsFDESYRQVQLTKFVYgysFNCKNDF-QKDA 355
Cdd:COG1204 154 RGPTLEVLLARLRRLNPEAQIVALSATIGNAEEIAEWL--DAEL------VKSDWRPVPLNEGVL---YDGVLRFdDGSR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 356 IYNSKLIEIIEKH-ADNRPVLIFCPTRASTISTAKFL---LNNHIFSKSKKRCN-----------HNPSDKILNECMQQG 420
Cdd:COG1204 223 RSKDPTLALALDLlEEGGQVLVFVSSRRDAESLAKKLadeLKRRLTPEEREELEelaeellevseETHTNEKLADCLEKG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 421 IAFHHAGISLEDRTAVEKEFLAGSINILCSTSTLAVGVNLPAYLVIIKGTKSWNSSEIqeySDLDVLQMIGRAGRPQFET 500
Cdd:COG1204 303 VAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGMVPI---PVLEFKQMAGRAGRPGYDP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 501 HGCAVIMTDSK--MKQTYENLIHG-TDVLESSLH--LNLIEHLAAETSLETVYSIETAVNWLRNTFFYVRFGKnpaayQE 575
Cdd:COG1204 380 YGEAILVAKSSdeADELFERYILGePEPIRSKLAneSALRTHLLALIASGFANSREELLDFLENTFYAYQYDK-----GD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 576 VNRYvsfhsVEDSqinqfcqylLDTLVKVKIIDISNGEYKSTAYGNAMTRHYISFESMKQFI----NAKKFLSLQGILNL 651
Cdd:COG1204 455 LEEV-----VDDA---------LEFLLENGFIEEDGDRLRATKLGKLVSRLYIDPLTAAELVdglrKADEEFTDLGLLHL 520
|
..
gi 9755332 652 LA 653
Cdd:COG1204 521 IL 522
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
138-333 |
1.14e-104 |
|
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: 328.16 E-value: 1.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 138 EFNKMQSEAFPSIYESNENCIISSPTGSGKTVLFELAILRLIKETNS-DTNNTKIIYIAPTKSLCYEMYKNWFPSF--VN 214
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPlPWGNRKVVYIAPIKALCSEKYDDWKEKFgpLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 215 LSVGMLTSDTSFLETEKAKKCNIIITTPEKWDLLTRRWSDYSRLFELVKLVLVDEIHTIKEKRGASLEVILTRMNTM--- 291
Cdd:cd18023 81 LSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLsss 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9755332 292 -------CQNIRFVALSATVPNIEDLALWLKTNnelPANILSFDESYRQ 333
Cdd:cd18023 161 selrgstVRPMRFVAVSATIPNIEDLAEWLGDN---PAGCFSFGESFRP 206
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
613-953 |
4.60e-75 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 251.41 E-value: 4.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 613 EYKSTAYGNAMTRHYISFESMKQFINAKK-FLSLQGILNLLATSEEFSVMRVRHNEKKLFKEINLSPLLKYPFltekkqs 691
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKpKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLEN------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 692 QIIDRVSQKVSLLIQYELGGLEFPSyegasklhQTLVQDKFLVFRHCFRLLKCMVDTFIEKSDGTSLKNTLFLLRSLNGH 771
Cdd:smart00611 74 PSLDDPHVKANLLLQAHLSRLKLPS--------FALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 772 CWEnTPMVLRQLKTIGLVSVRRLIRHGITNLEEMGHLSDTQIEYYLNLKIGNGIKIKNDISLLPCLNIRTKLENCKIENE 851
Cdd:smart00611 146 LWP-TDSPLLQLPHLPEEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLEPITRTVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 852 ELWLTFKVEISATFKSSiwhgqhlsldietEKSSGELIDFRRLQVNKLQSPRGFRISAKISPKLEKIEFSIHCQEIAgLG 931
Cdd:smart00611 225 GVEVTLTVDLTWDDEIH-------------GKQEGWWLVIGDSDGNELLHIERFSLNKKNVSEEVKLDFTAPATEGN-YQ 290
|
330 340
....*....|....*....|..
gi 9755332 932 KTIVYSTDHLASQFSAKTPNIR 953
Cdd:smart00611 291 YTLRLVSDSYLGCDQEYPLSFD 312
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
131-673 |
3.50e-59 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 217.76 E-value: 3.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 131 RGVfkfTEFNKMQSEAFPSIYESNENCIISSPTGSGKTVLFELAIL-RLIKETNsdtnntKIIYIAPTKSLCYEMY---K 206
Cdd:PRK00254 19 RGI---EELYPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVnKLLREGG------KAVYLVPLKALAEEKYrefK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 207 NWfpSFVNLSVGMLTSDTSFLEtEKAKKCNIIITTPEKWDLLTRRWSDYSRLfelVKLVLVDEIHTIKEK-RGASLEVIL 285
Cdd:PRK00254 90 DW--EKLGLRVAMTTGDYDSTD-EWLGKYDIIIATAEKFDSLLRHGSSWIKD---VKLVVADEIHLIGSYdRGATLEMIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 286 TRMNTMCQnirFVALSATVPNIEDLALWLktNNELpanILSfdeSYRQVQLTKFVYGYSFNCKNDFQKDAIYNSKLIEII 365
Cdd:PRK00254 164 THMLGRAQ---ILGLSATVGNAEELAEWL--NAEL---VVS---DWRPVKLRKGVFYQGFLFWEDGKIERFPNSWESLVY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 366 EKHADNRPVLIFCPTRASTISTAKFL---LNNHIFSKSKKRCNH-------NPSDKILNECMQQGIAFHHAGISLEDRTA 435
Cdd:PRK00254 233 DAVKKGKGALVFVNTRRSAEKEALELakkIKRFLTKPELRALKEladsleeNPTNEKLKKALRGGVAFHHAGLGRTERVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 436 VEKEFLAGSINILCSTSTLAVGVNLPAYLVIIKGTKSWNSSEIQEYSDLDVLQMIGRAGRPQFETHGCAVIM-TDSKMKQ 514
Cdd:PRK00254 313 IEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVaTTEEPSK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 515 TYENLIHGTDVlesslhlNLIEHLAAETSLET----------VYSIETAVNWLRNTFFYVRfGKNPAAYQEVNRYVSFHS 584
Cdd:PRK00254 393 LMERYIFGKPE-------KLFSMLSNESAFRSqvlalitnfgVSNFKELVNFLERTFYAHQ-RKDLYSLEEKAKEIVYFL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 585 VEdsqiNQFcqylldtlvkvkiIDIS-NGEYKSTAYGNAMTRHYISFESMKQFINA----KKFLSLQGILNLLATSEEFS 659
Cdd:PRK00254 465 LE----NEF-------------IDIDlEDRFIPLPLGIRTSQLYIDPLTAKKFKDAfpkiEKNPNPLGIFQLIASTPDMT 527
|
570
....*....|....
gi 9755332 660 VMRVRHNEKKLFKE 673
Cdd:PRK00254 528 PLNYSRKEMEDLLD 541
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
332-509 |
5.66e-57 |
|
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: 193.54 E-value: 5.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 332 RQVQLTKFVYGYS--FNCKN-DFQKDAIYNSKLIEIIEKHADNRPVLIFCPTRASTISTAKFLLnnhifskskkrcnhnp 408
Cdd:cd18795 1 RPVPLEEYVLGFNglGIKLRvDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 409 sdkilnecmqqGIAFHHAGISLEDRTAVEKEFLAGSINILCSTSTLAVGVNLPAYLVIIKGTKSWNSSEIQEYSDLDVLQ 488
Cdd:cd18795 65 -----------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELSPLEYLQ 133
|
170 180
....*....|....*....|.
gi 9755332 489 MIGRAGRPQFETHGCAVIMTD 509
Cdd:cd18795 134 MIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
138-318 |
7.38e-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: 191.71 E-value: 7.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 138 EFNKMQSEAFPSIYESNENCIISSPTGSGKTVLFELAILRLIKetnsdTNNTKIIYIAPTKSLCYEMYKNWFPSFVNL-- 215
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALA-----TSGGKAVYIAPTRALVNQKEADLRERFGPLgk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 216 SVGMLTSDTSFLETEKAKkCNIIITTPEKWDLLTRRWSDysRLFELVKLVLVDEIHTIK-EKRGASLEVILTRMNTMCQN 294
Cdd:cd17921 76 NVGLLTGDPSVNKLLLAE-ADILVATPEKLDLLLRNGGE--RLIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRINKN 152
|
170 180
....*....|....*....|....
gi 9755332 295 IRFVALSATVPNIEDLALWLKTNN 318
Cdd:cd17921 153 ARFVGLSATLPNAEDLAEWLGVED 176
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
616-937 |
1.11e-52 |
|
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: 187.57 E-value: 1.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 616 STAYGNAMTRHYISFESMKQFI-NAKKFLSLQGILNLLATSEEFSVMRVRHNEKKLFKEINLSPLLKYPfltekkqSQII 694
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNqSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVK-------EGII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 695 DRVSQKVSLLIQYELGGLEFPSYegasklhqTLVQDKFLVFRHCFRLLKCMVDTFIEKSDGTSLKNTLFLLRSLNGHCWE 774
Cdd:smart00973 74 DSPHAKVNLLLQAHLSRLPLPDF--------DLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 775 NTPMVLRQLKTIGLVSVRRLI--RHGITNLEEMGHLSDTQIEYYLNLKIGNGIKIKNDISLLPCLNIRTKLENCKIeneE 852
Cdd:smart00973 146 DSDSPLKQLPHFLIEDVYDKLelKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITR---D 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 853 LWLTFKVEISATFKS--SIWHGQHLSLDIETEKSSG-ELIDFRRLQVNKLQSPRGFRISAKI---SPKLEKIEFSIHCQE 926
Cdd:smart00973 223 LTLRVELEITPVFAWdlPRHKGKSESWWLVVGDSDTnELLAIKRVTLRKKKKSNEVKLDFTVplsEPGPENYTVYLISDS 302
|
330
....*....|.
gi 9755332 927 IAGLGKTIVYS 937
Cdd:smart00973 303 YLGCDQEVSFS 313
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
121-510 |
1.55e-51 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 193.95 E-value: 1.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 121 LSTTILPDSFRGVFKFTEFN--KMQSEAFPSIyESNENCIISSPTGSGKTVLFELAILRLIKEtnsdtnNTKIIYIAPTK 198
Cdd:PRK01172 3 ISDLGYDDEFLNLFTGNDFElyDHQRMAIEQL-RKGENVIVSVPTAAGKTLIAYSAIYETFLA------GLKSIYIVPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 199 SLCYEMYKNW-----FPSFVNLSVGMLTSDTSFLetekaKKCNIIITTPEKWDLLTRRWSDysrLFELVKLVLVDEIHTI 273
Cdd:PRK01172 76 SLAMEKYEELsrlrsLGMRVKISIGDYDDPPDFI-----KRYDVVILTSEKADSLIHHDPY---IINDVGLIVADEIHII 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 274 -KEKRGASLEVILTRMNTMCQNIRFVALSATVPNIEDLALWLktnnelpaNILSFDESYRQVQL-TKFVYGYSFNCKNDF 351
Cdd:PRK01172 148 gDEDRGPTLETVLSSARYVNPDARILALSATVSNANELAQWL--------NASLIKSNFRPVPLkLGILYRKRLILDGYE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 352 QKDAIYNSKLIEIIEkhaDNRPVLIFCPTRASTISTAKFLLN-----NHIFSKSKkrcNHNPSDKILNECMQQGIAFHHA 426
Cdd:PRK01172 220 RSQVDINSLIKETVN---DGGQVLVFVSSRKNAEDYAEMLIQhfpefNDFKVSSE---NNNVYDDSLNEMLPHGVAFHHA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 427 GISLEDRTAVEKEFLAGSINILCSTSTLAVGVNLPAYLVIIKGTKSWNSSEIQEYSDLDVLQMIGRAGRPQFETHGCAVI 506
Cdd:PRK01172 294 GLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYI 373
|
....
gi 9755332 507 MTDS 510
Cdd:PRK01172 374 YAAS 377
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
126-674 |
2.00e-47 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 182.46 E-value: 2.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 126 LPDSFRGVFK---FTEFNKMQSEAFPSIYESNENCIISSPTGSGKTVLFELAILRLIKetnsdtNNTKIIYIAPTKSLCY 202
Cdd:PRK02362 8 LPEGVIEFYEaegIEELYPPQAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIA------RGGKALYIVPLRALAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 203 EMYKNW--FPSF---VNLSVGMLTSDTSFLETEkakkcNIIITTPEKWDLLTR---RW-SDYSrlfelvkLVLVDEIHTI 273
Cdd:PRK02362 82 EKFEEFerFEELgvrVGISTGDYDSRDEWLGDN-----DIIVATSEKVDSLLRngaPWlDDIT-------CVVVDEVHLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 274 -KEKRGASLEVILT---RMNTMCQnirFVALSATVPNIEDLALWLKTnnELpanilsFDESYRQVQLTKFV-YGYSFNCK 348
Cdd:PRK02362 150 dSANRGPTLEVTLAklrRLNPDLQ---VVALSATIGNADELADWLDA--EL------VDSEWRPIDLREGVfYGGAIHFD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 349 NDfqkdaiynSKLIEIIEKHADNRPV----------LIFCPTRASTISTAKFLLnnhifSKSKKRCNHNPSD-------- 410
Cdd:PRK02362 219 DS--------QREVEVPSKDDTLNLVldtleeggqcLVFVSSRRNAEGFAKRAA-----SALKKTLTAAERAelaelaee 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 411 ----------KILNECMQQGIAFHHAGISLEDRTAVEKEFLAGSINILCSTSTLAVGVNLPAYLVIIKGTKSWNSSE-IQ 479
Cdd:PRK02362 286 irevsdtetsKDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAgMQ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 480 EYSDLDVLQMIGRAGRPQFETHGCAVIMTDSkmkqtYENLihgTDVLEsslhlNLIE--------HLAAETSLET----- 546
Cdd:PRK02362 366 PIPVLEYHQMAGRAGRPGLDPYGEAVLLAKS-----YDEL---DELFE-----RYIWadpedvrsKLATEPALRThvlst 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 547 -----VYSIETAVNWLRNTFFyvrfgknpaAYQEVNrYVSFHSVEDSqinqfcqyLLDTLVKVKIIDISNGEYKSTAYGN 621
Cdd:PRK02362 433 iasgfARTRDGLLEFLEATFY---------ATQTDD-TGRLERVVDD--------VLDFLERNGMIEEDGETLEATELGH 494
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 9755332 622 AMTRHYI---SFESMKQFINAKKFLSLQGILNLLATSEEFSVMRVRHNEKKLFKEI 674
Cdd:PRK02362 495 LVSRLYIdplSAAEIIDGLEAAKKPTDLGLLHLVCSTPDMYELYLRSGDYEWLNEY 550
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
136-328 |
2.42e-47 |
|
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: 167.82 E-value: 2.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 136 FTEFNKMQSEAFPSIYESNENCIISSPTGSGKTVLFELAILRLIKetnsDTNNTKIIYIAPTKSLCYEMYKNW---FPSF 212
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWR----QNPKGRAVYIAPMQELVDARYKDWrakFGPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 213 VNLSVGMLTSDTSfLETEKAKKCNIIITTPEKWDLLTRRWSDYSRLfELVKLVLVDEIHTIKEKRGASLEVILTRMNTMC 292
Cdd:cd18021 77 LGKKVVKLTGETS-TDLKLLAKSDVILATPEQWDVLSRRWKQRKNV-QSVELFIADELHLIGGENGPVYEVVVSRMRYIS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9755332 293 ----QNIRFVALSATVPNIEDLALWLKTNnelPANILSFD 328
Cdd:cd18021 155 sqleKPIRIVGLSSSLANARDVGEWLGAS---KSTIFNFH 191
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
126-317 |
1.07e-43 |
|
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: 157.92 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 126 LPDSFRGVFK-FTEFNKMQSEAFPSIYESNENCIISSPTGSGKTVLFELAILRLI-KETNSDT----NNTKIIYIAPTKS 199
Cdd:cd18019 4 LPDWAQPAFEgFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIgKHRNPDGtinlDAFKIVYIAPMKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 200 LCYEMYKNwFPS---FVNLSVGMLTSDTSfLETEKAKKCNIIITTPEKWDLLTRRWSDYSRLfELVKLVLVDEIHTIKEK 276
Cdd:cd18019 84 LVQEMVGN-FSKrlaPYGITVAELTGDQQ-LTKEQISETQIIVTTPEKWDIITRKSGDRTYT-QLVRLIIIDEIHLLHDD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9755332 277 RGASLEVILTR----MNTMCQNIRFVALSATVPNIEDLALWLKTN 317
Cdd:cd18019 161 RGPVLESIVARtirqIEQTQEYVRLVGLSATLPNYEDVATFLRVD 205
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
138-319 |
9.60e-42 |
|
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: 151.37 E-value: 9.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 138 EFNKMQSEAFPSIYESNENCIISSPTGSGKTVLFELAILRLIKetnsDTNNTKIIYIAPTKSLCYEMYKNWFPSFVN--- 214
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFN----KYPGSKVVYIAPLKALVRERVDDWKKRFEEklg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 215 LSVGMLTSDTSfLETEKAKKCNIIITTPEKWDLLTRRWSdySRLF-ELVKLVLVDEIHTIKEKRGASLEVILTRMNTMC- 292
Cdd:cd18022 77 KKVVELTGDVT-PDMKALADADIIITTPEKWDGISRSWQ--TREYvQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISs 153
|
170 180 190
....*....|....*....|....*....|
gi 9755332 293 ---QNIRFVALSATVPNIEDLALWLKTNNE 319
Cdd:cd18022 154 qteKPVRLVGLSTALANAGDLANWLGIKKM 183
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
138-314 |
4.95e-39 |
|
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: 143.24 E-value: 4.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 138 EFNKMQSEAFPSIYESNENCIISSPTGSGKTVLFELAILrliketNSDTNNTKIIYIAPTKSLCYEMYKNwFPSF----- 212
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMV------NTLLEGGKALYLVPLRALASEKYEE-FKKLeeigl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 213 -VNLSVGMLTSDTSFLetekaKKCNIIITTPEKWDLLTR-RWSdysrLFELVKLVLVDEIHTI-KEKRGASLEVILTRMN 289
Cdd:cd18028 74 kVGISTGDYDEDDEWL-----GDYDIIVATYEKFDSLLRhSPS----WLRDVGVVVVDEIHLIsDEERGPTLESIVARLR 144
|
170 180
....*....|....*....|....*
gi 9755332 290 TMCQNIRFVALSATVPNIEDLALWL 314
Cdd:cd18028 145 RLNPNTQIIGLSATIGNPDELAEWL 169
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
138-317 |
5.48e-39 |
|
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: 144.11 E-value: 5.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 138 EFNKMQSEAFPSIYESNENCIISSPTGSGKTVLFELAILRLIKE-----TNSDTNNTKIIYIAPTKSLCYEMYKNWFPS- 211
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQhvnqgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 212 -FVNLSVGMLTSDTSFLETEKAKKcNIIITTPEKWDLLTRRWSDYSRLFELVKLVLVDEIHTIKEKRGASLEVILTR--- 287
Cdd:cd18020 81 aPLGIKVKELTGDMQLTKKEIAET-QIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARtlr 159
|
170 180 190
....*....|....*....|....*....|.
gi 9755332 288 -MNTMCQNIRFVALSATVPNIEDLALWLKTN 317
Cdd:cd18020 160 qVESTQSMIRIVGLSATLPNYLDVADFLRVN 190
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
140-310 |
2.93e-36 |
|
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: 135.06 E-value: 2.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 140 NKMQSEAFPSIYEsNENCIISSPTGSGKTVLFELAILRLIKETNsdtNNTKIIYIAPTKSLCYEMYKNW--FPSFVNLSV 217
Cdd:pfam00270 1 TPIQAEAIPAILE-GRDVLVQAPTGSGKTLAFLLPALEALDKLD---NGPQALVLAPTRELAEQIYEELkkLGKGLGLKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 218 GMLTSDTSFLET-EKAKKCNIIITTPEKWDLLTRRwsdySRLFELVKLVLVDEIHTIKEK-RGASLEVILTRMNtmcQNI 295
Cdd:pfam00270 77 ASLLGGDSRKEQlEKLKGPDILVGTPGRLLDLLQE----RKLLKNLKLLVLDEAHRLLDMgFGPDLEEILRRLP---KKR 149
|
170
....*....|....*.
gi 9755332 296 RFVALSATVP-NIEDL 310
Cdd:pfam00270 150 QILLLSATLPrNLEDL 165
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
143-550 |
2.55e-34 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 142.00 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 143 QSEAFPSIyESNENCIISSPTGSGKTVLFELAILRLIKEtnsdtnNTKIIYIAPTKSLCYEMYKNwfpsFVNL----SVG 218
Cdd:COG4581 30 QEEAILAL-EAGRSVLVAAPTGSGKTLVAEFAIFLALAR------GRRSFYTAPIKALSNQKFFD----LVERfgaeNVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 219 MLTSDTSFletekakkcN----IIITTPEkwdLLTRRWSDYSRLFELVKLVLVDEIHTIKEK-RGASLEVILTrmnTMCQ 293
Cdd:COG4581 99 LLTGDASV---------NpdapIVVMTTE---ILRNMLYREGADLEDVGVVVMDEFHYLADPdRGWVWEEPII---HLPA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 294 NIRFVALSATVPNIEDLALWLKTNNELPANILSFDesyRQVQLTkfvygYSFNCKNDFQKDAIYNSKLI------EIIEK 367
Cdd:COG4581 164 RVQLVLLSATVGNAEEFAEWLTRVRGETAVVVSEE---RPVPLE-----FHYLVTPRLFPLFRVNPELLrppsrhEVIEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 368 --HADNRPVLIFCPTRASTISTAKFLLNNHIFSKSKKRCN-----------HNPSDKILNECMQQGIAFHHAGISLEDRT 434
Cdd:COG4581 236 ldRGGLLPAIVFIFSRRGCDEAAQQLLSARLTTKEERAEIreaidefaedfSVLFGKTLSRLLRRGIAVHHAGMLPKYRR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 435 AVEKEFLAGSINILCSTSTLAVGVNLPAYLVIIKGTKSWNSseiQEYSDL---DVLQMIGRAGRPQFETHGCAVIMTDSK 511
Cdd:COG4581 316 LVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDG---ERHRPLtarEFHQIAGRAGRRGIDTEGHVVVLAPEH 392
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 9755332 512 M-KQTYENLIHG-TDVLESSLHL--NLIEHLAAETSLETVYSI 550
Cdd:COG4581 393 DdPKKFARLASArPEPLRSSFRPsyNMVLNLLARPGLERAREL 435
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
616-898 |
1.79e-31 |
|
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: 125.78 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 616 STAYGNAMTRHYISFESMKQFI-NAKKFLSLQGILNLLATSEEFSVMRVRHNEKKLFKEINlsplLKYPFlteKKQSQII 694
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNqSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLL----EKVPI---PVKGDIE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 695 DRvSQKVSLLIQYELGGLEFPSYEgasklhqtLVQDKFLVFRHCFRLLKCMVDTFIEKSDGTSLKNTLFLLRSLNGHCWe 774
Cdd:pfam02889 74 DP-HAKVNILLQAYISRLKLPGFA--------LVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMW- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 775 NTPMVLRQLKTIGLVSVRRLIRHGITNLEEMGHLSDTQIEYYLNLKIGNGIKIKNDISLLPCLNIRTKLEncKIENEElw 854
Cdd:pfam02889 144 DSDSPLRQFPGIPPELIKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQ--PITRSV-- 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 9755332 855 LTFKVEISATF-KSSIWHGQHLSLDIETEKSSG-ELIDFRRLQVNK 898
Cdd:pfam02889 220 LRVEVTITPDFpWDKRVHGKSEGFWLVVGDSDGnEILHIERFTLTK 265
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
134-314 |
3.20e-31 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 121.83 E-value: 3.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 134 FKFTEFNKMQSEAFPSIYESNENCIISSPTGSGKTVLFELAILRLIKEtnsdTNNTKIIYIAPTKSLCYEMY---KNWFP 210
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKR----GKGGRVLVLVPTRELAEQWAeelKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 211 SFVNLSVGMLTSDTSFLETEKAKK--CNIIITTPEKwdlLTRRWSDYSRLFELVKLVLVDEIHTIKEK-RGASLEVILTR 287
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESgkTDILVTTPGR---LLDLLENDKLSLSNVDLVILDEAHRLLDGgFGDQLEKLLKL 156
|
170 180
....*....|....*....|....*..
gi 9755332 288 MNtmcQNIRFVALSATVPNIEDLALWL 314
Cdd:smart00487 157 LP---KNVQLLLLSATPPEEIENLLEL 180
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
154-314 |
6.62e-26 |
|
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: 105.36 E-value: 6.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 154 NENCIISSPTGSGKTVLFELAILRLIKETNSDTnnTKIIYIAPTKSLCYEMYKN------WFPsfVNLSVGMLTSDTSfl 227
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKG--VQVLYISPLKALINDQERRleepldEID--LEIPVAVRHGDTS-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 228 ETEKAKKC----NIIITTPEKWD-LLTRRwsDYSRLFELVKLVLVDEIHT-IKEKRGASLEVILTRMNTM-CQNIRFVAL 300
Cdd:cd17922 75 QSEKAKQLknppGILITTPESLElLLVNK--KLRELFAGLRYVVVDEIHAlLGSKRGVQLELLLERLRKLtGRPLRRIGL 152
|
170
....*....|....
gi 9755332 301 SATVPNIEDLALWL 314
Cdd:cd17922 153 SATLGNLEEAAAFL 166
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
130-494 |
7.45e-26 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 115.20 E-value: 7.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 130 FRGVFK-FTEFnkmQSEAFPSIyESNENCIISSPTGSGKTvlfeLA-----ILRLIKETNSDT--NNTKIIYIAPTKSLC 201
Cdd:COG1201 18 FAARFGaPTPP---QREAWPAI-AAGESTLLIAPTGSGKT----LAaflpaLDELARRPRPGElpDGLRVLYISPLKALA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 202 YEMYKN-----------WFPSFVNLSVGMLTSDTSflETEKAK----KCNIIITTPEkw-dLLTRRwsDYSRLFELVKLV 265
Cdd:COG1201 90 NDIERNlrapleeigeaAGLPLPEIRVGVRTGDTP--ASERQRqrrrPPHILITTPEslalLLTSP--DARELLRGVRTV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 266 LVDEIHTIKE-KRGASLEVILTRMNTMC-QNIRFVALSATVPNIEDLALWL-KTNNELPANILSFDESyRQVQLT----- 337
Cdd:COG1201 166 IVDEIHALAGsKRGVHLALSLERLRALApRPLQRIGLSATVGPLEEVARFLvGYEDPRPVTIVDAGAG-KKPDLEvlvpv 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 338 -----KFVYGYSFNckndfqkDAIYNsKLIEIIEKHadnRPVLIFCPTRASTistakfllnNHIFSKSKKRcnhNPSDKI 412
Cdd:COG1201 245 edlieRFPWAGHLW-------PHLYP-RVLDLIEAH---RTTLVFTNTRSQA---------ERLFQRLNEL---NPEDAL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 413 LnecmqqgIAFHHAGISLEDRTAVEKEFLAGSINILCSTSTLAVGVNLPAY-LVI-IKGTKSwnsseiqeysdldV---L 487
Cdd:COG1201 302 P-------IAAHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDVdLVIqVGSPKS-------------VarlL 361
|
....*..
gi 9755332 488 QMIGRAG 494
Cdd:COG1201 362 QRIGRAG 368
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
135-494 |
2.33e-24 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 110.36 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 135 KFTEFNKMQSEAFPSIYEsNENCIISSPTGSGKTVLFELAIL-RLIKETNSDTNNTKI--IYIAPTKSLCYEMYKNWF-- 209
Cdd:PRK13767 29 KFGTFTPPQRYAIPLIHE-GKNVLISSPTGSGKTLAAFLAIIdELFRLGREGELEDKVycLYVSPLRALNNDIHRNLEep 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 210 ------------PSFVNLSVGMLTSDTSFLETEK-AKKC-NIIITTPEKWDLLTRRwSDYSRLFELVKLVLVDEIHTIKE 275
Cdd:PRK13767 108 lteireiakergEELPEIRVAIRTGDTSSYEKQKmLKKPpHILITTPESLAILLNS-PKFREKLRTVKWVIVDEIHSLAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 276 -KRGASLEVILTRMNTMCQN--IRfVALSATVPNIEDLALWLKTNNElpanilsfDESYRQVQL--TKFVYGYS------ 344
Cdd:PRK13767 187 nKRGVHLSLSLERLEELAGGefVR-IGLSATIEPLEEVAKFLVGYED--------DGEPRDCEIvdARFVKPFDikvisp 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 345 ----FNCKNDFQKDAIYNsKLIEIIEKHadnRPVLIFCPTRASTISTAKFLlnnhifsksKKRcnhnpSDKILNEcmqQG 420
Cdd:PRK13767 258 vddlIHTPAEEISEALYE-TLHELIKEH---RTTLIFTNTRSGAERVLYNL---------RKR-----FPEEYDE---DN 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9755332 421 IAFHHAGISLEDRTAVEKEFLAGSINILCSTSTLAVGVNLPaY--LVIIKGT-KSWNSseiqeysdldVLQMIGRAG 494
Cdd:PRK13767 317 IGAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG-YidLVVLLGSpKSVSR----------LLQRIGRAG 382
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
93-507 |
3.40e-24 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 109.98 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 93 FDHDLEQTPDEEAKKPKKVTIRksakkcLSTTILPDSFRGVF--KFTEFNKMQSEAFPSIYESNENCIISSPTGSGKTVL 170
Cdd:COG1202 168 LDPDLTKFDEISATTDEVDTVP------VDDLDLPPELKDLLegRGEELLPVQSLAVENGLLEGKDQLVVSATATGKTLI 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 171 FELA-ILRLIKetnsdtNNTKIIYIAPTKSLC---YEMYKNWFPSFVNLS--VGMltSDTSFLETEKAKKCNIIITTPEK 244
Cdd:COG1202 242 GELAgIKNALE------GKGKMLFLVPLVALAnqkYEDFKDRYGDGLDVSirVGA--SRIRDDGTRFDPNADIIVGTYEG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 245 WDLLTRRWSDYSRlfelVKLVLVDEIHTIKEK-RGASLEVILTRMNTMCQNIRFVALSATVPNIEDLAlwlktnNELPAN 323
Cdd:COG1202 314 IDHALRTGRDLGD----IGTVVIDEVHMLEDPeRGHRLDGLIARLKYYCPGAQWIYLSATVGNPEELA------KKLGAK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 324 ILSFDEsyRQVQltkfvygysfnckndfqkdaiynsklieiIEKHadnrpvLIFCPTR-------------ASTISTAKF 390
Cdd:COG1202 384 LVEYEE--RPVP-----------------------------LERH------LTFADGRekiriinklvkreFDTKSSKGY 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 391 LLNNHIFSKSKKRCnHNPSDKIlnecmqqGI--AFHHAGISLEDRTAVEKEFLAGSINILCSTSTLAVGVNLPAYLVI-- 466
Cdd:COG1202 427 RGQTIIFTNSRRRC-HEIARAL-------GYkaAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIfd 498
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 9755332 467 -----IKgtksWNSseIQEYSdldvlQMIGRAGRPQFETHGCAVIM 507
Cdd:COG1202 499 slamgIE----WLS--VQEFH-----QMLGRAGRPDYHDRGKVYLL 533
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
151-496 |
5.73e-24 |
|
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: 109.18 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 151 YESNENCIISSPTGSGKTV-LFELAILRLIKETNSDTNNTKIIYIAPTKSLCYEMYKN-----------WfpsfvnlSVG 218
Cdd:TIGR04121 25 ALEGRSGLLIAPTGSGKTLaGFLPSLIDLAGPEAPKEKGLHTLYITPLRALAVDIARNlqapieelglpI-------RVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 219 MLTSDTSFLETEKAKKC--NIIITTPEKWDLLTrRWSDYSRLFELVKLVLVDEIHT-IKEKRGASLEVILTRMNTMCQNI 295
Cdd:TIGR04121 98 TRTGDTSSSERARQRKKppDILLTTPESLALLL-SYPDAARLFKDLRCVVVDEWHElAGSKRGDQLELALARLRRLAPGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 296 RFVALSATVPNIEDLALWL-KTNNELPANILSFDESYRQV------QLTKFVYG-----YSFnckndfqkdaiynSKLIE 363
Cdd:TIGR04121 177 RRWGLSATIGNLEEARRVLlGVGGAPAVLVRGKLPKAIEVisllpeSEERFPWAghlglRAL-------------PEVYA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 364 IIEKHadnRPVLIFCPTRASTISTAKFLLnnhifskskkrcNHNPSDKILnecmqqgIAFHHAGISLEDRTAVEKEFLAG 443
Cdd:TIGR04121 244 EIDQA---RTTLVFTNTRSQAELWFQALW------------EANPEFALP-------IALHHGSLDREQRRWVEAAMAAG 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 9755332 444 SINILCSTSTLAVGVN-LPAYLVI-IKGTKswNSSEIqeysdldvLQMIGRAG-RP 496
Cdd:TIGR04121 302 RLRAVVCTSSLDLGVDfGPVDLVIqIGSPK--GVARL--------LQRAGRSNhRP 347
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
131-495 |
1.26e-21 |
|
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: 101.45 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 131 RGVFKFTEFnkmQSEAFPSIYEsNENCIISSPTGSGKTVLFELAILRLIKEtnsdTNNTKIIYIAPTKSLCYEMYKNW-- 208
Cdd:COG1205 52 RGIERLYSH---QAEAIEAARA-GKNVVIATPTASGKSLAYLLPVLEALLE----DPGATALYLYPTKALARDQLRRLre 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 209 --FPSFVNLSVGMLTSDTSFLETEKA-KKCNIIITTPEKWDL-LTRRWSDYSRLFELVKLVLVDEIHTIkekR---GASL 281
Cdd:COG1205 124 laEALGLGVRVATYDGDTPPEERRWIrEHPDIVLTNPDMLHYgLLPHHTRWARFFRNLRYVVIDEAHTY---RgvfGSHV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 282 EVILTRMNTMCQ----NIRFVALSATVPNIEDLALWLkTNneLPANILSFDESYRQvqltkfvygysfncKNDFqkdAIY 357
Cdd:COG1205 201 ANVLRRLRRICRhygsDPQFILASATIGNPAEHAERL-TG--RPVTVVDEDGSPRG--------------ERTF---VLW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 358 NsklieiiekhadnrPVLIFCPTRASTISTAKFLLNNHI--------FSKSKK-------RCNHNPSDKILNECmqqgIA 422
Cdd:COG1205 261 N--------------PPLVDDGIRRSALAEAARLLADLVreglrtlvFTRSRRgaellarYARRALREPDLADR----VA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 423 FHHAGISLEDRTAVEKEFLAGSINILCSTSTLAVGVNLPaylviikgtkswnsseiqeysDLDV-------------LQM 489
Cdd:COG1205 323 AYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIG---------------------GLDAvvlagypgtrasfWQQ 381
|
....*.
gi 9755332 490 IGRAGR 495
Cdd:COG1205 382 AGRAGR 387
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
138-496 |
5.15e-21 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 98.56 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 138 EFNKMQSEA----FPSIYESNENCIISSPTGSGKTVLFELAILRLIketnsdtNNTKIIYIAPTKSLC---YEMYKNWFP 210
Cdd:COG1061 80 ELRPYQQEAlealLAALERGGGRGLVVAPTGTGKTVLALALAAELL-------RGKRVLVLVPRRELLeqwAEELRRFLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 211 sfvnlsvgmltsDTSFLETEKAKKCNIIITTpekWDLLTRRwSDYSRLFELVKLVLVDEIHTIkekRGASLEVILTRMnt 290
Cdd:COG1061 153 ------------DPLAGGGKKDSDAPITVAT---YQSLARR-AHLDELGDRFGLVIIDEAHHA---GAPSYRRILEAF-- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 291 mcQNIRFVALSATvPNIEDlalwlktNNELPANILS---FDESYRQVQ----LTKF-VYGYSFNCKNDFQKDAIYNSK-- 360
Cdd:COG1061 212 --PAAYRLGLTAT-PFRSD-------GREILLFLFDgivYEYSLKEAIedgyLAPPeYYGIRVDLTDERAEYDALSERlr 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 361 -------------LIEIIEKHADNRPVLIFCPtrasTISTAKFLLnnhifskskkrcnhnpsdKILNEcMQQGIAFHHAG 427
Cdd:COG1061 282 ealaadaerkdkiLRELLREHPDDRKTLVFCS----SVDHAEALA------------------ELLNE-AGIRAAVVTGD 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9755332 428 ISLEDRTAVEKEFLAGSINILCSTSTLAVGVNLPA--YLVIIKGTKSwnsseIQEYsdldvLQMIGRAGRP 496
Cdd:COG1061 339 TPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPTGS-----PREF-----IQRLGRGLRP 399
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
126-315 |
2.85e-19 |
|
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: 87.27 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 126 LPDSFRGVFKFTEFNKM---QSEAF--PSIYEsNENCIISSPTGSGKTVLFELAILRLIKETNSdtnntKIIYIAPTKSL 200
Cdd:cd18026 1 LPDAVREAYAKKGIKKLydwQKECLslPGLLE-GRNLVYSLPTSGGKTLVAEILMLKRLLERRK-----KALFVLPYVSI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 201 CYEMYKnWFPSFVnlsvgmltSDTSFLETEKA-----------KKCNIIITTPEKWDLLTRRWSDYSRLFELvKLVLVDE 269
Cdd:cd18026 75 VQEKVD-ALSPLF--------EELGFRVEGYAgnkgrsppkrrKSLSVAVCTIEKANSLVNSLIEEGRLDEL-GLVVVDE 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9755332 270 IHTIKEK-RGASLEVILTRMNTMCQ-NIRFVALSATVPNIEDLALWLK 315
Cdd:cd18026 145 LHMLGDGhRGALLELLLTKLLYAAQkNIQIVGMSATLPNLEELASWLR 192
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
161-494 |
7.02e-19 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 93.07 E-value: 7.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 161 SPTGSGKTVL-FELAILRLIKETNSDTNN------TKIIYIAPTKSLCYEMYKNW-FP-------------SFVNLSVGM 219
Cdd:PRK09751 3 APTGSGKTLAaFLYALDRLFREGGEDTREahkrktSRILYISPIKALGTDVQRNLqIPlkgiaderrrrgeTEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 220 LTSDTSFLETEK--AKKCNIIITTPEK-WDLLTRRWSDYSRlfeLVKLVLVDEIHTIK-EKRGASLEVILTRMN----TM 291
Cdd:PRK09751 83 RTGDTPAQERSKltRNPPDILITTPESlYLMLTSRARETLR---GVETVIIDEVHAVAgSKRGAHLALSLERLDallhTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 292 CQNIrfvALSATVPNIEDLALWLktNNELPANILSfDESYRQVQLTKFV-----------YGYSFNCKNDFQKDAIYNSK 360
Cdd:PRK09751 160 AQRI---GLSATVRSASDVAAFL--GGDRPVTVVN-PPAMRHPQIRIVVpvanmddvssvASGTGEDSHAGREGSIWPYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 361 LIEIIEKHADNRPVLIFCPTRASTIS-TAKFllnNHIFSKSKKRCNHNPSDKILNECMQ-------QG----IA-FHHAG 427
Cdd:PRK09751 234 ETGILDEVLRHRSTIVFTNSRGLAEKlTARL---NELYAARLQRSPSIAVDAAHFESTSgatsnrvQSsdvfIArSHHGS 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 428 ISLEDRTAVEKEFLAGSINILCSTSTLAVGVNLPAYLVIikgtkswnsseIQEYSDLDV---LQMIGRAG 494
Cdd:PRK09751 311 VSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLV-----------IQVATPLSVasgLQRIGRAG 369
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
154-303 |
2.35e-17 |
|
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: 80.14 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 154 NENCIISSPTGSGKTVLFELAILRLIketnsDTNNTKIIYIAPTKSLCYEMYKNW-FPSFVNLSVGMLTSDTSFLETEKA 232
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLL-----LKKGKKVLVLVPTKALALQTAERLrELFGPGIRVAVLVGGSSAEEREKN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9755332 233 KKCN--IIITTPEKwdLLTRRWSDYSRLFELVKLVLVDEIHTIKEKRGASLEVILTRMNTMCQNIRFVALSAT 303
Cdd:cd00046 76 KLGDadIIIATPDM--LLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
143-311 |
2.88e-17 |
|
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: 81.09 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 143 QSEAFPSIyESNENCIISSPTGSGKTVLFELAIL-RLIKETNSdtnntKIIYIAPTKSLCY---EMYKNWFPSFV-NLSV 217
Cdd:cd17923 5 QAEAIEAA-RAGRSVVVTTGTASGKSLCYQLPILeALLRDPGS-----RALYLYPTKALAQdqlRSLRELLEQLGlGIRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 218 GMLTSDTSFLETEKAKK--CNIIITTPEKWD-LLTRRWSDYSRLFELVKLVLVDEIHTIKEKRGASLEVILTRMNTMCQ- 293
Cdd:cd17923 79 ATYDGDTPREERRAIIRnpPRILLTNPDMLHyALLPHHDRWARFLRNLRYVVLDEAHTYRGVFGSHVALLLRRLRRLCRr 158
|
170 180
....*....|....*....|.
gi 9755332 294 ---NIRFVALSATVPNIEDLA 311
Cdd:cd17923 159 ygaDPQFILTSATIGNPAEHA 179
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
134-332 |
3.50e-17 |
|
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: 81.34 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 134 FKFTeFNKMQSEAFPSIyESNENCIISSPTGSGKTVLFELAILRLIKetnsdtNNTKIIYIAPTKSLCYEMYKNWFPSFV 213
Cdd:cd18024 29 YPFT-LDPFQKTAIACI-ERNESVLVSAHTSAGKTVVAEYAIAQSLR------DKQRVIYTSPIKALSNQKYRELQEEFG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 214 NlsVGMLTSDTSFLETekaKKCnIIITTPEKWDLLTRRwsdySRLFELVKLVLVDEIHTIKEK-RGASLE--VILtrmnt 290
Cdd:cd18024 101 D--VGLMTGDVTINPN---ASC-LVMTTEILRSMLYRG----SEIMREVAWVIFDEIHYMRDKeRGVVWEetIIL----- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9755332 291 MCQNIRFVALSATVPNIEDLALWLKTNNELPANILSFDesYR 332
Cdd:cd18024 166 LPDKVRYVFLSATIPNARQFAEWICKIHKQPCHVVYTD--YR 205
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
137-495 |
9.23e-16 |
|
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: 82.05 E-value: 9.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 137 TEFNKMQSEAFPSIYESNEN----CIISSPTGSGKTvlfeLAILRLIKETNSDTNNTKIIYIAPTKSLC---YEMYKNWF 209
Cdd:COG1203 126 TPINPLQNEALELALEAAEEepglFILTAPTGGGKT----EAALLFALRLAAKHGGRRIIYALPFTSIInqtYDRLRDLF 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 210 PSfvnlSVGMLTSDTSFLETEKAKKCN----------------IIITTPekwD-----LLTRRWSDYSRLFELV-KLVLV 267
Cdd:COG1203 202 GE----DVLLHHSLADLDLLEEEEEYEsearwlkllkelwdapVVVTTI---DqlfesLFSNRKGQERRLHNLAnSVIIL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 268 DEIHTIKEKRGASLEVILTRMNTMcqNIRFVALSATVPNIEDLALwLKTNNELPANILSFDESYRQvqltkfvygysFNC 347
Cdd:COG1203 275 DEVQAYPPYMLALLLRLLEWLKNL--GGSVILMTATLPPLLREEL-LEAYELIPDEPEELPEYFRA-----------FVR 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 348 KN-DFQKDAIYNSKLIE-IIEKHADNRPVLIFCPTRASTISTAKFLlnnhifskskkrcnhnpSDKILNEcmqqGIAFHH 425
Cdd:COG1203 341 KRvELKEGPLSDEELAElILEALHKGKSVLVIVNTVKDAQELYEAL-----------------KEKLPDE----EVYLLH 399
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9755332 426 AGISLEDRTAVEKE----FLAGSINILCSTSTLAVGVNLPAYLVIIkgtkswnsseiqEYSDLD-VLQmigRAGR 495
Cdd:COG1203 400 SRFCPADRSEIEKEikerLERGKPCILVSTQVVEAGVDIDFDVVIR------------DLAPLDsLIQ---RAGR 459
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
411-496 |
3.60e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 71.47 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 411 KILNECMQQ---GIAFHHAGISLEDRTAVEKEFLAGSINILCSTSTLAVGVNLP-AYLVIIKGTkSWNSSeiqeysdlDV 486
Cdd:smart00490 1 EELAELLKElgiKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL-PWSPA--------SY 71
|
90
....*....|
gi 9755332 487 LQMIGRAGRP 496
Cdd:smart00490 72 IQRIGRAGRA 81
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
136-311 |
2.00e-14 |
|
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: 73.24 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 136 FTEFNKMQSEAFPSIYeSNENCIISSPTGSGKTVLFELAIL-RLIKETNSDTNNTKIIYIAPTKSLC---YEMYKNWFpS 211
Cdd:cd00268 10 FEKPTPIQAQAIPLIL-SGRDVIGQAQTGSGKTLAFLLPILeKLLPEPKKKGRGPQALVLAPTRELAmqiAEVARKLG-K 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 212 FVNLSVGMLTSDTSFLETEKA--KKCNIIITTPEK-WDLLTRRwsdySRLFELVKLVLVDE---------IHTIKEkrga 279
Cdd:cd00268 88 GTGLKVAAIYGGAPIKKQIEAlkKGPDIVVGTPGRlLDLIERG----KLDLSNVKYLVLDEadrmldmgfEEDVEK---- 159
|
170 180 190
....*....|....*....|....*....|...
gi 9755332 280 slevILTRMNTMCQNIRFvalSATVPN-IEDLA 311
Cdd:cd00268 160 ----ILSALPKDRQTLLF---SATLPEeVKELA 185
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
150-315 |
2.96e-14 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350783 [Multi-domain] Cd Length: 192 Bit Score: 72.40 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 150 IYESNENCIISSPTGSGKTVLFELAILRLIKETNSDTnntkIIYIAPTKSLCYEMY--------KNWFPSFVNLsVGMLT 221
Cdd:cd18025 12 IVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDGV----VVYVAPTKALVNQVVaevyarfsKKYPPSGKSL-WGVFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 222 SDTSFletEKAKKCNIIITTPEKWD--LLTR---RWSDysrlfeLVKLVLVDEIHTI-KEKRGASLEVILTRMNtmCQni 295
Cdd:cd18025 87 RDYRH---NNPMNCQVLITVPECLEilLLSPhnaSWVP------RIKYVIFDEIHSIgQSEDGAVWEQLLLLIP--CP-- 153
|
170 180
....*....|....*....|
gi 9755332 296 rFVALSATVPNIEDLALWLK 315
Cdd:cd18025 154 -FLALSATIGNPQKFHEWLQ 172
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
359-495 |
2.77e-13 |
|
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: 67.24 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 359 SKLIEIIEKHADNRpVLIFCPTRAStiSTAKFLLNNHIFSkskkrcnhnpsdkilnecmqqgIAFHHAGISLEDRTAVEK 438
Cdd:pfam00271 4 EALLELLKKERGGK-VLIFSQTKKT--LEAELLLEKEGIK----------------------VARLHGDLSQEEREEILE 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 9755332 439 EFLAGSINILCSTSTLAVGVNLP-AYLVIIKGTkSWNSSEIqeysdldvLQMIGRAGR 495
Cdd:pfam00271 59 DFRKGKIDVLVATDVAERGLDLPdVDLVINYDL-PWNPASY--------IQRIGRAGR 107
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
138-314 |
3.12e-13 |
|
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: 69.22 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 138 EFNKMQSEAFPSIyESNENCIISSPTGSGKTVLFELAIlrlikeTNSDTNNTKIIYIAPTKSLCYEMYKNWFPSFVNlsV 217
Cdd:cd18027 8 ELDVFQKQAILHL-EAGDSVFVAAHTSAGKTVVAEYAI------ALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGD--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 218 GMLTSDTSfLETEkakkCNIIITTPEKWDLLTRRWSDYSRLFELVklvLVDEIHTIKE-KRGASLEVILTRMNtmcQNIR 296
Cdd:cd18027 79 GLITGDVQ-LNPE----ASCLIMTTEILRSMLYNGSDVIRDLEWV---IFDEVHYINDaERGVVWEEVLIMLP---DHVS 147
|
170
....*....|....*...
gi 9755332 297 FVALSATVPNIEDLALWL 314
Cdd:cd18027 148 IILLSATVPNTVEFADWI 165
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
142-303 |
3.89e-12 |
|
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: 65.02 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 142 MQSEAFPSIYESNEN--CIISSPTGSGKTVLfELAILRLIKEtnsdtnnTKIIYIAPTKSLCYEMYKNWFPSFVNLSVGM 219
Cdd:cd17926 4 YQEEALEAWLAHKNNrrGILVLPTGSGKTLT-ALALIAYLKE-------LRTLIVVPTDALLDQWKERFEDFLGDSSIGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 220 LTSDtsflETEKAKKCNIIITTPEKWDLLTRRWSDYSRLFElvkLVLVDEIHTIkekrGA-SLEVILTRMNTMCQnirfV 298
Cdd:cd17926 76 IGGG----KKKDFDDANVVVATYQSLSNLAEEEKDLFDQFG---LLIVDEAHHL----PAkTFSEILKELNAKYR----L 140
|
....*
gi 9755332 299 ALSAT 303
Cdd:cd17926 141 GLTAT 145
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
158-312 |
2.02e-10 |
|
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: 61.15 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 158 IISSPTGSGKTvlfeLAILRLIKETNSDTNNTKIIYIAPTKSLC---YEMYKNWFPSFV-NLSVGMLTSDTSF-LETEKA 232
Cdd:cd17930 5 ILEAPTGSGKT----EAALLWALKLAARGGKRRIIYALPTRATInqmYERIREILGRLDdEDKVLLLHSKAALeLLESDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 233 KKCNIIITTPEKWDLLTRRWSD-----------YS---------RLFELV-KLVLVDEIHTIKEKRGA----SLEVILTR 287
Cdd:cd17930 81 EPDDDPVEAVDWALLLKRSWLApivvttidqllESllkykhferRLHGLAnSVVVLDEVQAYDPEYMAlllkALLELLGE 160
|
170 180
....*....|....*....|....*
gi 9755332 288 MNTmcqniRFVALSATVPNIEDLAL 312
Cdd:cd17930 161 LGG-----PVVLMTATLPALLRDEL 180
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
136-451 |
5.13e-10 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 63.24 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 136 FTEFNKMQSEAFPSIyESNENCIISSPTGSGKTVLFELAILRLIKETNSdtNNTKIIYIAPTKSLC---YEMYKnWFPSF 212
Cdd:COG0513 22 YTTPTPIQAQAIPLI-LAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP--RAPQALILAPTRELAlqvAEELR-KLAKY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 213 VNLSVGMLTSDTSFLETEKA--KKCNIIITTPekwdlltrrwsdySRLFELVK-----------LVLvDE---------I 270
Cdd:COG0513 98 LGLRVATVYGGVSIGRQIRAlkRGVDIVVATP-------------GRLLDLIErgaldlsgvetLVL-DEadrmldmgfI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 271 HTIKEkrgaslevILTRMNTMCQNIRFvalSATVPN-IEDLA-LWLKTnnelPANIlSFDESYRQVQLTKFVYgysFNCK 348
Cdd:COG0513 164 EDIER--------ILKLLPKERQTLLF---SATMPPeIRKLAkRYLKN----PVRI-EVAPENATAETIEQRY---YLVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 349 NDfQKDAIynskLIEIIEKHADNRpVLIFCPTRASTISTAKFLLNNHIfskskkrcnhnPSDKIlnecmqqgiafhHAGI 428
Cdd:COG0513 225 KR-DKLEL----LRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGI-----------SAAAL------------HGDL 275
|
330 340
....*....|....*....|...
gi 9755332 429 SLEDRTAVEKEFLAGSINILCST 451
Cdd:COG0513 276 SQGQRERALDAFRNGKIRVLVAT 298
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
135-311 |
2.06e-09 |
|
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: 58.37 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 135 KFTEFNKMQSEAFPSIYEsNENCIISSPTGSGKTVLFELAILRLIKETNSDTNNTKIIyIAPTKSLCYEMYKNwfpsFVN 214
Cdd:cd17957 9 GYREPTPIQMQAIPILLH-GRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRALI-LAPTRELASQIYRE----LLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 215 LSVG-------MLTSDTSFLETEKA--KKCNIIITTP---------EKWDLLTRRW-----SDysRLFELVKLVLVDEIH 271
Cdd:cd17957 83 LSKGtglrivlLSKSLEAKAKDGPKsiTKYDILVSTPlrlvfllkqGPIDLSSVEYlvldeAD--KLFEPGFREQTDEIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 9755332 272 TIkekrgasleviltrmntmCQN--IRFVALSATVP-NIEDLA 311
Cdd:cd17957 161 AA------------------CTNpnLQRSLFSATIPsEVEELA 185
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
154-271 |
1.79e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.51 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 154 NENCIISSPTGSGKTVLFELAILRLIKETNSdtnntKIIYIAPTKSLC---YEMYKNwFPSFVNLSVGMLTSDTSFLETE 230
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAERLHKKGG-----KVLFLAPTKPLVeqhAEFFKE-ALNIPEDEIVVFTGEVSPEKRK 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 9755332 231 KA-KKCNIIITTPE--KWDLLTRRWSdysrlFELVKLVLVDEIH 271
Cdd:COG1111 91 ELwEKARIIVATPQviENDLIAGRID-----LDDVSLLIFDEAH 129
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
138-271 |
3.83e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 51.13 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 138 EFNKMQSEAFPSIYES----NENCIISSPTGSGKTVLFELAILRLIKETNSDtnntKIIYIAPTKSLCYEMYKNWFPSFV 213
Cdd:pfam04851 3 ELRPYQIEAIENLLESikngQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK----KVLFLVPRKDLLEQALEEFKKFLP 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 9755332 214 N-LSVGMLTSDTSFLETEKAKKcnIIITTPEKWDLLTRRWSDYSrLFELVKLVLVDEIH 271
Cdd:pfam04851 79 NyVEIGEIISGDKKDESVDDNK--IVVTTIQSLYKALELASLEL-LPDFFDVIIIDEAH 134
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
132-311 |
4.76e-07 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 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: 350707 [Multi-domain] Cd Length: 214 Bit Score: 51.82 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 132 GVFKFTEFNKMQSEAFPSIYeSNENCIISSPTGSGKTVLFELAIL-RLIKETNSDTNN--TKIIYIAPTKSLC---YEMY 205
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLL-QGRDVLVRSQTGSGKTLAYLLPIIqRLLSLEPRVDRSdgTLALVLVPTRELAlqiYEVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 206 KNWFPSFVNLSVGMLTSDTSfLETEKA---KKCNIIITTP----------EKWDLLTRRW-----SDysRLFEL-----V 262
Cdd:cd17949 86 EKLLKPFHWIVPGYLIGGEK-RKSEKArlrKGVNILIATPgrlldhlkntQSFDVSNLRWlvldeAD--RLLDMgfekdI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 9755332 263 KlVLVDEIHTIKEKRGASLEVILTRMNTMCqnirfvalSATV-PNIEDLA 311
Cdd:cd17949 163 T-KILELLDDKRSKAGGEKSKPSRRQTVLV--------SATLtDGVKRLA 203
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
134-311 |
6.46e-07 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 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: 350711 [Multi-domain] Cd Length: 222 Bit Score: 51.61 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 134 FKFTEFNKMQSEAFPSIYeSNENCIISSPTGSGKTVLFELAILRLIKETNSDTNNTKIIYI--APTKSLCYEMYKN--WF 209
Cdd:cd17953 30 LGYEKPTPIQAQALPAIM-SGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEGPIGLimAPTRELALQIYVEckKF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 210 PSFVNLSVGMLTSDTSFLE--TEKAKKCNIIITTPEKW-DLLT---RRWSDYSRlfelVKLVLVDEIhtikekrgaslev 283
Cdd:cd17953 109 SKALGLRVVCVYGGSGISEqiAELKRGAEIVVCTPGRMiDILTannGRVTNLRR----VTYVVLDEA------------- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9755332 284 ilTRMNTM---------CQNIR----FVALSATVPN-IEDLA 311
Cdd:cd17953 172 --DRMFDMgfepqimkiVNNIRpdrqTVLFSATFPRkVEALA 211
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
135-305 |
1.19e-06 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members 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: 350721 [Multi-domain] Cd Length: 196 Bit Score: 50.27 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 135 KFTEFNKMQSEAFPSIYES-NENCIISSPTGSGKTVLFELAILrlikeTNSDTNN--TKIIYIAPTKSLC---YEMYKNw 208
Cdd:cd17963 13 GFNKPSKIQETALPLILSDpPENLIAQSQSGTGKTAAFVLAML-----SRVDPTLksPQALCLAPTRELArqiGEVVEK- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 209 FPSFVNLSVGMLTSDTSFLETEKAKKcNIIITTPEK-WDLLTRRWSDYSRLfelvKLVLVDEIHTIKEKRGASlEVILTR 287
Cdd:cd17963 87 MGKFTGVKVALAVPGNDVPRGKKITA-QIVIGTPGTvLDWLKKRQLDLKKI----KILVLDEADVMLDTQGHG-DQSIRI 160
|
170
....*....|....*...
gi 9755332 288 MNTMCQNIRFVALSATVP 305
Cdd:cd17963 161 KRMLPRNCQILLFSATFP 178
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
154-271 |
1.42e-06 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 49.82 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 154 NENCIISSPTGSGKTVLFELAIL-RLIKEtnsdtnNTKIIYIAPTKSLCyEMYKNWFPSFVNLS--VGMLTSDTSFLETE 230
Cdd:cd18035 16 NGNTLIVLPTGLGKTIIAILVAAdRLTKK------GGKVLILAPSRPLV-EQHAENLKRVLNIPdkITSLTGEVKPEERA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 9755332 231 KA-KKCNIIITTPE--KWDLLTRRWSdysrlFELVKLVLVDEIH 271
Cdd:cd18035 89 ERwDASKIIVATPQviENDLLAGRIT-----LDDVSLLIFDEAH 127
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
143-271 |
1.52e-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: 49.96 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 143 QSEAFpsiYES-NENCIISSPTGSGKTVLFELAILRLIKETNSDTNNTKIIY-IAPTKSLCYEMYKnWFPSFVNLSVGML 220
Cdd:cd18034 7 QLELF---EAAlKRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNPKKRAVfLVPTVPLVAQQAE-AIRSHTDLKVGEY 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 9755332 221 TSD------TSFLETEKAKKCNIIITTPEKW-DLLTRRWSDysrlFELVKLVLVDEIH 271
Cdd:cd18034 83 SGEmgvdkwTKERWKEELEKYDVLVMTAQILlDALRHGFLS----LSDINLLIFDECH 136
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
143-269 |
1.85e-06 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 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: 350719 [Multi-domain] Cd Length: 206 Bit Score: 49.89 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 143 QSEAFPSIYESnENCIISSPTGSGKTVLFELAILRLI---KETNSDTNNTKIIYIAPTKSLCYEMYKNW---------FP 210
Cdd:cd17961 21 QSKAIPLALEG-KDILARARTGSGKTAAYALPIIQKIlkaKAESGEEQGTRALILVPTRELAQQVSKVLeqltaycrkDV 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 211 SFVNLSVGMLTSDTSFLETEKAkkcNIIITTPEK-WDLLTrrwSDYSRLFELVKLVLVDE 269
Cdd:cd17961 100 RVVNLSASSSDSVQRALLAEKP---DIVVSTPARlLSHLE---SGSLLLLSTLKYLVIDE 153
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
134-269 |
1.92e-06 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 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: 350718 [Multi-domain] Cd Length: 202 Bit Score: 49.88 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 134 FKFTEFNKMQSEAFPsIYESNENCIISSPTGSGKTVLFELAILRLI--KETNSDTNNTKIIYIAPTKSLCYEMYKNwFPS 211
Cdd:cd17960 8 LGFTSMTPVQAATIP-LFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkRKANLKKGQVGALIISPTRELATQIYEV-LQS 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9755332 212 FVN-----LSVGML---TSDTSFLETEKAKKCNIIITTPEKWDLLTRRWSDYSRLFELVKLVLvDE 269
Cdd:cd17960 86 FLEhhlpkLKCQLLiggTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKADKVKVKSLEVLVL-DE 150
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
361-495 |
3.86e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 48.03 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 361 LIEIIEKHADNRPVLIFCPTRASTISTAKFLlnnhifsksKKRC-NHNPSDKIlnecmqqgiAFHHAGISLEDRTAVEKE 439
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRL---------RELCpDRVPPDFI---------ALHHGSLSRELREEVEAA 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 9755332 440 FLAGSINILCSTSTLAVGVNLPAY-LVI-IKGTKSWNSseiqeysdldVLQMIGRAGR 495
Cdd:cd18796 90 LKRGDLKVVVATSSLELGIDIGDVdLVIqIGSPKSVAR----------LLQRLGRSGH 137
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
127-306 |
4.91e-06 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 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: 350717 [Multi-domain] Cd Length: 205 Bit Score: 48.84 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 127 PDSFRGVFK--FTEFNKMQSEAFPSIYESNEnCIISSPTGSGKTVLFELAILRLIKETnSDTNNTKIIYIAPTKSLCYEM 204
Cdd:cd17959 10 PPLLRAIKKkgYKVPTPIQRKTIPLILDGRD-VVAMARTGSGKTAAFLIPMIEKLKAH-SPTVGARALILSPTRELALQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 205 YK--NWFPSFVNLSVGMLTSDTSFLE--TEKAKKCNIIITTPekwdlltrrwsdySRLFEL----------VKLVLVDEI 270
Cdd:cd17959 88 LKvtKELGKFTDLRTALLVGGDSLEEqfEALASNPDIIIATP-------------GRLLHLlvemnlklssVEYVVFDEA 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 9755332 271 HTIKEKRGAS-LEVILTRMNTMCQNIRFvalSATVPN 306
Cdd:cd17959 155 DRLFEMGFAEqLHEILSRLPENRQTLLF---SATLPK 188
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
361-495 |
7.95e-06 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 49.75 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 361 LIEIIEKHADnRPVLIFCPTRASTISTAKFLlnnhifskskkrcnhnpsdkilnecMQQGI--AFHHAGISLEDRTAVEK 438
Cdd:COG0514 221 LLDFLKEHPG-GSGIVYCLSRKKVEELAEWL-------------------------REAGIraAAYHAGLDAEEREANQD 274
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9755332 439 EFLAGSINILCSTSTLAVGVN-----------LPaylviikgtKSwnsseIQEYsdldvLQMIGRAGR 495
Cdd:COG0514 275 RFLRDEVDVIVATIAFGMGIDkpdvrfvihydLP---------KS-----IEAY-----YQEIGRAGR 323
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
156-271 |
1.03e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 49.87 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 156 NCIISSPTGSGKTVLFELAILRLIKETNSdtnntKIIYIAPTKSLCyEMYKNWFPSFVNL---SVGMLTSDTSFLETEKA 232
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIAERLHKKGG-----KVLILAPTKPLV-EQHAEFFRKFLNIpeeKIVVFTGEVSPEKRAEL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 9755332 233 -KKCNIIITTPE--KWDLLTRRWSdysrlFELVKLVLVDEIH 271
Cdd:PRK13766 105 wEKAKVIVATPQviENDLIAGRIS-----LEDVSLLIFDEAH 141
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
159-242 |
1.14e-05 |
|
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: 48.01 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 159 ISSPTGSGKTVLFELAILRLIKETNSdtNNTKIIYIAPTKSLCYEMYK--NWFPSFVNLSVGMLTSDTSFLETEKA---- 232
Cdd:cd17956 41 VSAPTGSGKTLAYVLPIVQALSKRVV--PRLRALIVVPTKELVQQVYKvfESLCKGTGLKVVSLSGQKSFKKEQKLllvd 118
|
90
....*....|....*.
gi 9755332 233 ------KKCNIIITTP 242
Cdd:cd17956 119 tsgrylSRVDILVATP 134
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
361-495 |
1.37e-05 |
|
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: 46.05 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 361 LIEIIEKHADNRPVLIFCPTRASTISTAKFLlnnhifskskKRCNHNPsdkilnecmqqgiAFHHAGISLEDRTAVEKEF 440
Cdd:cd18794 20 LLKRIKVEHLGGSGIIYCLSRKECEQVAARL----------QSKGISA-------------AAYHAGLEPSDRRDVQRKW 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 9755332 441 LAGSINILCSTSTLAVGVNLP-AYLVIIKG-TKSwnsseIQEYsdldvLQMIGRAGR 495
Cdd:cd18794 77 LRDKIQVIVATVAFGMGIDKPdVRFVIHYSlPKS-----MESY-----YQESGRAGR 123
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
127-306 |
1.54e-05 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are 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: 350804 [Multi-domain] Cd Length: 201 Bit Score: 47.06 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 127 PDSFRGVFK--FTEFNKMQSEAFPSIYESNEnCIISSPTGSGKTVLFELAILRLIketNSDTNNTKIIYIAPTKSLCYEM 204
Cdd:cd18046 8 ESLLRGIYAygFEKPSAIQQRAIMPCIKGYD-VIAQAQSGTGKTATFSISILQQI---DTSLKATQALVLAPTRELAQQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 205 YK--NWFPSFVNLSVGMLTSDTSFLETEKAKK--CNIIITTPEK-WDLLTRRW--SDYSRLF------ELVKLVLVDEIH 271
Cdd:cd18046 84 QKvvMALGDYMGIKCHACIGGTSVRDDAQKLQagPHIVVGTPGRvFDMINRRYlrTDYIKMFvldeadEMLSRGFKDQIY 163
|
170 180 190
....*....|....*....|....*....|....*
gi 9755332 272 TIKEKRGASLEVILtrmntmcqnirfvaLSATVPN 306
Cdd:cd18046 164 DIFQKLPPDTQVVL--------------LSATMPN 184
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
135-242 |
2.69e-04 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 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: 350699 [Multi-domain] Cd Length: 198 Bit Score: 43.43 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 135 KFTEFNKMQSEAFPSIYESNEncII-SSPTGSGKTVLFELAIL-RLIKETNSDTNNTKIIYIAPTKSLCYEMYK--NWFP 210
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQGRD--ILgAAKTGSGKTLAFLVPLLeKLYRERWTPEDGLGALIISPTRELAMQIFEvlRKVG 86
|
90 100 110
....*....|....*....|....*....|...
gi 9755332 211 SFVNLSVGMLTSDTSF-LETEKAKKCNIIITTP 242
Cdd:cd17941 87 KYHSFSAGLIIGGKDVkEEKERINRMNILVCTP 119
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
151-310 |
3.04e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350677 [Multi-domain] Cd Length: 182 Bit Score: 42.94 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 151 YESNENCIISSPTGSGKTVLfELAILRLIKEtnSDTNNTKIIYIAPtKSLCY----EMyKNWFPsfvNLSVGMLTSDTS- 225
Cdd:cd17919 16 YENGPGGILADEMGLGKTLQ-AIAFLAYLLK--EGKERGPVLVVCP-LSVLEnwerEF-EKWTP---DLRVVVYHGSQRe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 226 ---FLETEKAKKCNIIITTPEkwdlltrRWSDYSRLFELVK--LVLVDEIHTIKEKRGASLEViLTRMNTMCqniRfVAL 300
Cdd:cd17919 88 raqIRAKEKLDKFDVVLTTYE-------TLRRDKASLRKFRwdLVVVDEAHRLKNPKSQLSKA-LKALRAKR---R-LLL 155
|
170
....*....|...
gi 9755332 301 SATvP---NIEDL 310
Cdd:cd17919 156 TGT-PlqnNLEEL 167
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
134-311 |
3.47e-04 |
|
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: 43.34 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 134 FKFTEFNKMQSEAFPSIYESNENCIISSPTGSGKTVLFEL-AILRLIKETNSDTNNT-KIIYIAPTKSLCYEMYK----- 206
Cdd:cd17964 12 MGFETMTPVQQKTLKPILSTGDDVLARAKTGTGKTLAFLLpAIQSLLNTKPAGRRSGvSALIISPTRELALQIAAeakkl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 207 -NWFPSF-VNLSVGMlTSDTSFLETEKAKKCNIIITTPEKW-DLLTR-RWSDYSRlfELVKLVLvDEIHTIKEKrG--AS 280
Cdd:cd17964 92 lQGLRKLrVQSAVGG-TSRRAELNRLRRGRPDILVATPGRLiDHLENpGVAKAFT--DLDYLVL-DEADRLLDM-GfrPD 166
|
170 180 190
....*....|....*....|....*....|...
gi 9755332 281 LEVILTRMNTMCQNIRFVAL-SATVP-NIEDLA 311
Cdd:cd17964 167 LEQILRHLPEKNADPRQTLLfSATVPdEVQQIA 199
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
155-306 |
4.30e-04 |
|
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: 42.80 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 155 ENCIISSPTGSGKTVLFELAILRLIKETNSdTNNTKIIYIAPTKSLcYEMYKNWFPSFVN---LSVGMLTSDTSFLET-- 229
Cdd:cd17927 18 KNTIICLPTGSGKTFVAVLICEHHLKKFPA-GRKGKVVFLANKVPL-VEQQKEVFRKHFErpgYKVTGLSGDTSENVSve 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 230 EKAKKCNIIITTPEKW--DLLTRRWSDYSRlfelVKLVLVDEIH-TIKEK--RGASLEVILTRMNTMCQNIRFVALSATV 304
Cdd:cd17927 96 QIVESSDVIIVTPQILvnDLKSGTIVSLSD----FSLLVFDECHnTTKNHpyNEIMFRYLDQKLGSSGPLPQILGLTASP 171
|
..
gi 9755332 305 PN 306
Cdd:cd17927 172 GV 173
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
421-515 |
4.35e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It 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: 350198 [Multi-domain] Cd Length: 159 Bit Score: 41.95 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 421 IAFHHAGISLEDRTAVEKEFLAGSINILCSTSTLAVGVNLP-AYLVIIKGTKSWNSSEIQeysdldvlQMIGRAGRPQFE 499
Cdd:cd18811 64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPnATVMVIEDAERFGLSQLH--------QLRGRVGRGDHQ 135
|
90
....*....|....*.
gi 9755332 500 THgcAVIMTDSKMKQT 515
Cdd:cd18811 136 SY--CLLVYKDPLTET 149
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
358-507 |
4.71e-04 |
|
C-terminal helicase domain of the 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. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain] Cd Length: 131 Bit Score: 41.34 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 358 NSKLIEIIEKHADNRPVLIFCPTRASTISTAKFLLNNHIfskskkrcnhnPSDKIlnecmqqgiafhHAGISLEDRTAVE 437
Cdd:cd18787 14 KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGI-----------KVAAL------------HGDLSQEERERAL 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9755332 438 KEFLAGSINILCSTSTLAVGVNLPAY-LVIikgtkswN---SSEIQEYsdldvLQMIGRAGRpqFETHGCAVIM 507
Cdd:cd18787 71 KKFRSGKVRVLVATDVAARGLDIPGVdHVI-------NydlPRDAEDY-----VHRIGRTGR--AGRKGTAITF 130
|
|
| DEAHc_XPD-like |
cd17915 |
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ... |
157-286 |
5.35e-04 |
|
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members are 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: 350673 [Multi-domain] Cd Length: 138 Bit Score: 41.26 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 157 CIISSPTGSGKTvlfeLAILRLIKETNSDTNNTKIIYIAPTKSLCYEMYKNW--FPSFVNLSVGMLTSdtsfletekaKK 234
Cdd:cd17915 4 VALESPTGSGKT----LSLLCSALSYQREFHKTKVLYCSRTHSQIEQIIRELrkLLEKRKIRALALSS----------RD 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 9755332 235 CNIIITTPEKwdLLTRRWSDYSRLFELVKLVLVDEIHTIKEKRgasleVILT 286
Cdd:cd17915 70 ADIVVLPYPY--LLDARIREFIGIDLREQVVIIDEAHNLDERS-----VIIT 114
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
136-242 |
6.31e-04 |
|
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 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: 350705 [Multi-domain] Cd Length: 196 Bit Score: 42.24 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 136 FTEFNKMQSEAFPSIYESNENCIiSSPTGSGKTVLFELAILRLIKETNSDTNNTKIIYIAPTKSL---CYEMYKNwFPSF 212
Cdd:cd17947 10 FTKPTPIQAAAIPLALLGKDICA-SAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELamqCFSVLQQ-LAQF 87
|
90 100 110
....*....|....*....|....*....|..
gi 9755332 213 VNLSVGMLTSDTSFLETEKAKKCN--IIITTP 242
Cdd:cd17947 88 TDITFALAVGGLSLKAQEAALRARpdIVIATP 119
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
134-205 |
1.39e-03 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 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: 350700 [Multi-domain] Cd Length: 198 Bit Score: 41.19 E-value: 1.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9755332 134 FKFTEFNKMQSEAFPSIYESnENCIISSPTGSGKTVLFELAILRLIKETN-SDTNNTKIIYIAPTKSLCYEMY 205
Cdd:cd17942 8 MGFTKMTEIQAKSIPPLLEG-RDVLGAAKTGSGKTLAFLIPAIELLYKLKfKPRNGTGVIIISPTRELALQIY 79
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
155-303 |
1.42e-03 |
|
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: 41.15 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 155 ENCIISSPTGSGKTVLFELAILRLIKETNSdtnnTKIIYIAPTKSL-------CYEMyknwfpsfvnlsVGMLTSDTSFL 227
Cdd:cd18033 17 QNTLVALPTGLGKTFIAAVVMLNYYRWFPK----GKIVFMAPTKPLvsqqieaCYKI------------TGIPSSQTAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 228 --ETEKAKKC------NIIITTPEKWDlltrrwSDYSR---LFELVKLVLVDEIHTIKeKRGASLEVI--LTRMNTmcqN 294
Cdd:cd18033 81 tgSVPPTKRAelwaskRVFFLTPQTLE------NDLKEgdcDPKSIVCLVIDEAHRAT-GNYAYCQVVreLMRYNS---H 150
|
....*....
gi 9755332 295 IRFVALSAT 303
Cdd:cd18033 151 FRILALTAT 159
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
153-320 |
1.62e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 153 SNENCIISSPTGSGKTVLFeLAILRLIKETNSdtnntKIIYIAPTKSLCYEMYKNWFPSFvnlsvgmltsDTSFLETEKA 232
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLA-RALARELGPPGG-----GVIYIDGEDILEEVLDQLLLIIV----------GGKKASGSGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 233 KKCNIIITTPEKwdlltrrwsdysrlfELVKLVLVDEIHTIKEKRGASLEVILTRMNTM-----CQNIRFVALSATVPNI 307
Cdd:smart00382 65 LRLRLALALARK---------------LKPDVLILDEITSLLDAEQEALLLLLEELRLLlllksEKNLTVILTTNDEKDL 129
|
170
....*....|...
gi 9755332 308 EDLALWLKTNNEL 320
Cdd:smart00382 130 GPALLRRRFDRRI 142
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
155-271 |
1.64e-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: 41.31 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 155 ENCIISSPTGSGKTVLFELAILRLIKETNSDTNNTKIIYIAPTKSLcYEMYKNWFPSFVN--LSVGMLTSDTSFLET--E 230
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVNKVPL-VEQQLEKFFKYFRkgYKVTGLSGDSSHKVSfgQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 9755332 231 KAKKCNIIITTPEKWDLLTRRWSDYSRL-FELVKLVLVDEIH 271
Cdd:cd18036 97 IVKASDVIICTPQILINNLLSGREEERVyLSDFSLLIFDECH 138
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
130-311 |
1.92e-03 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 40.70 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 130 FRGVFKFTEFNKMQSEAFPSIYeSNENCIISSPTGSGKTVLFELAILRLIKETNSDTnntkiIYIAPTKSLCYEMYKNwF 209
Cdd:cd18018 4 LRRVFGHPSFRPGQEEAIARLL-SGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLT-----LVVSPLIALMKDQVDA-L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 210 PSFVNLSV--GMLTSDTSFLETEK--AKKCNIIITTPEKwdLLTRRWSDYSRLFELVKLVLVDEIHTIKEK----RGASL 281
Cdd:cd18018 77 PRAIKAAAlnSSLTREERRRILEKlrAGEVKILYVSPER--LVNESFRELLRQTPPISLLVVDEAHCISEWshnfRPDYL 154
|
170 180 190
....*....|....*....|....*....|...
gi 9755332 282 evILTRM-NTMCQNIRFVALSATVPN--IEDLA 311
Cdd:cd18018 155 --RLCRVlRELLGAPPVLALTATATKrvVEDIA 185
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
164-310 |
2.24e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 42.13 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 164 GSGKTVlfE-LAILRLIKETNsdtNNTKIIYIAPTkSLCY----EMYKnWFPSfvnLSVGMLTSDTS-FLETEKAKKCNI 237
Cdd:COG0553 270 GLGKTI--QaLALLLELKERG---LARPVLIVAPT-SLVGnwqrELAK-FAPG---LRVLVLDGTRErAKGANPFEDADL 339
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9755332 238 IITTpekWDLLTRRWSDYSRL-FELVklvLVDEIHTIKE---KRGASLEVILTRmntmcqniRFVALSAT-VPN-IEDL 310
Cdd:COG0553 340 VITS---YGLLRRDIELLAAVdWDLV---ILDEAQHIKNpatKRAKAVRALKAR--------HRLALTGTpVENrLEEL 404
|
|
| uvsW |
PHA02558 |
UvsW helicase; Provisional |
149-289 |
2.51e-03 |
|
UvsW helicase; Provisional
Pssm-ID: 222875 [Multi-domain] Cd Length: 501 Bit Score: 41.92 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 149 SIYES--NENCIISSPTGSGKTvLFELAILRLIKETNSdtnnTKIIYIAPTKSLCYEMYKN-----WFPSFVNLSVgmlt 221
Cdd:PHA02558 122 AVYEGlkNNRRLLNLPTSAGKS-LIQYLLSRYYLENYE----GKVLIIVPTTSLVTQMIDDfvdyrLFPREAMHKI---- 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9755332 222 sdtsFLETEKAKKCNIIITT-------PEKWdlltrrwsdysrlFELVKLVLVDEIHTIKEKrgaSLEVILTRMN 289
Cdd:PHA02558 193 ----YSGTAKDTDAPIVVSTwqsavkqPKEW-------------FDQFGMVIVDECHLFTGK---SLTSIITKLD 247
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
142-264 |
4.03e-03 |
|
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 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: 350710 [Multi-domain] Cd Length: 197 Bit Score: 39.71 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 142 MQSEAFPSIYeSNENCIISSPTGSGKTVLFELAILRLI---KETNSDTNNTKIIyIAPTKSLCYEMYK--NWFPSFVNLS 216
Cdd:cd17952 16 IQAQALPVAL-SGRDMIGIAKTGSGKTAAFIWPMLVHImdqRELEKGEGPIAVI-VAPTRELAQQIYLeaKKFGKAYNLR 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 9755332 217 VGMLTSDTSFLETEKAKK--CNIIITTPekwdlltrrwsdySRLFELVKL 264
Cdd:cd17952 94 VVAVYGGGSKWEQAKALQegAEIVVATP-------------GRLIDMVKK 130
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
364-495 |
4.15e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 41.42 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 364 IIEKHADNRPVLIFC---PTRASTISTAKFLLNNH------IFSKSKKRCnhnpsDKI---LNECMQQGiAFHHAGISLE 431
Cdd:PLN03137 644 VVFRQSFNRPNLWYSvvpKTKKCLEDIDKFIKENHfdecgiIYCLSRMDC-----EKVaerLQEFGHKA-AFYHGSMDPA 717
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9755332 432 DRTAVEKEFLAGSINILCSTSTLAVGVNLPAYLVIIKGT--KSwnsseIQEYSdldvlQMIGRAGR 495
Cdd:PLN03137 718 QRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSlpKS-----IEGYH-----QECGRAGR 773
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
143-269 |
4.57e-03 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) 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: 350713 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 143 QSEAFPSIYESnENCIISSPTGSGKTVLFELAILRLIKEtnsDTNNTKIIYIAPTKSLCYEMYK--NWFPSFVNLSVGML 220
Cdd:cd17955 26 QKLCIPEILAG-RDVIGGAKTGSGKTAAFALPILQRLSE---DPYGIFALVLTPTRELAYQIAEqfRALGAPLGLRCCVI 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 9755332 221 TSDTSFLETEK--AKKCNIIITTPEKW-DLLTRRwSDYSRLFELVKLVLVDE 269
Cdd:cd17955 102 VGGMDMVKQALelSKRPHIVVATPGRLaDHLRSS-DDTTKVLSRVKFLVLDE 152
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
143-269 |
5.47e-03 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 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: 350696 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 143 QSEAFPSIYESNEnCIISSPTGSGKTVLFELAILRLIKEtnsdtnntkiIYIAPTKSL------CYEMYKNWFPSfVNLS 216
Cdd:cd17938 26 QAEAIPLILGGGD-VLMAAETGSGKTGAFCLPVLQIVVA----------LILEPSRELaeqtynCIENFKKYLDN-PKLR 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 9755332 217 VGMLTSDTSFLETEKAKK--CNIIITTPEK-WDLLTRRWSDYSRlfelVKLVLVDE 269
Cdd:cd17938 94 VALLIGGVKAREQLKRLEsgVDIVVGTPGRlEDLIKTGKLDLSS----VRFFVLDE 145
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
444-496 |
7.72e-03 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The 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: 350172 [Multi-domain] Cd Length: 77 Bit Score: 36.53 E-value: 7.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 9755332 444 SINILCSTSTLAVGVNLP-AYLVIIKGTKSWNSSEIQeysdldvlqMIGRAGRP 496
Cdd:cd18785 22 SLEILVATNVLGEGIDVPsLDTVIFFDPPSSAASYIQ---------RVGRAGRG 66
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
145-321 |
9.37e-03 |
|
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 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: 350820 [Multi-domain] Cd Length: 251 Bit Score: 39.26 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 145 EAFPSIYESNENCIISSPTGSGKTVLFELAILRLIKETNSDTNNTKIIYIAPTKSLCYEmYKNWFPSFVNLSV-GMLTSD 223
Cdd:cd18062 33 EWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYE-FDKWAPSVVKVSYkGSPAAR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755332 224 TSFLETEKAKKCNIIITTPE-----KWDLLTRRWsdysrlfelvKLVLVDEIHTIKEKRGASLEViltrMNTMCQNIRFV 298
Cdd:cd18062 112 RAFVPQLRSGKFNVLLTTYEyiikdKQILAKIRW----------KYMIVDEGHRMKNHHCKLTQV----LNTHYVAPRRL 177
|
170 180
....*....|....*....|...
gi 9755332 299 ALSATVPNIEDLALWLKTNNELP 321
Cdd:cd18062 178 LLTGTPLQNKLPELWALLNFLLP 200
|
|
| |
