|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
58-428 |
1.34e-162 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 464.24 E-value: 1.34e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHelelGRPQVVIVSP 137
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 138 TRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLD 217
Cdd:COG0513 80 TRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 218 MGFSEDMRRIMTHvtMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFVAIGIVGGACSDVKQTIYEVNKYAKRSKLIEIL- 296
Cdd:COG0513 160 MGFIEDIERILKL--LPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 297 SEQADGTIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIKNIKHVINYD 376
Cdd:COG0513 238 DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYD 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
2DB3_D 377 MPSKIDDYVHRIGRTGRVGNNGRATSFFDPEKDRAIAadlvKILEGSGQTVP 428
Cdd:COG0513 318 LPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLR----AIEKLIGQKIE 365
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
58-270 |
9.21e-140 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 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: 350725 [Multi-domain] Cd Length: 221 Bit Score: 398.78 E-value: 9.21e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGR-----PQV 132
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 133 VIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEA 212
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 213 DRMLDMGFSEDMRRIMTHVTMRP--EHQTLMFSATFPEEIQRMAGEFLKNYVFVAIGIVG 270
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHPDMPPkgERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
13-270 |
2.59e-135 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are 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: 350810 [Multi-domain] Cd Length: 264 Bit Score: 388.94 E-value: 2.59e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 13 YIPPEPSNDAIEIFSSgIASGIHFSKYNNIPVKVTGSDVPQPIQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISS 92
Cdd:cd18052 1 YIPPPPPEDEDEIFAT-IQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 93 GRDLMACAQTGSGKTAAFLLPILSKL----LEDPHELELGRPQVVIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTS 168
Cdd:cd18052 80 GRDLMACAQTGSGKTAAFLLPVLTGMmkegLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 169 FRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMRRIMTHVTMRP--EHQTLMFSATF 246
Cdd:cd18052 160 VGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSkeDRQTLMFSATF 239
|
250 260
....*....|....*....|....*
2DB3_D 247 PEEIQRMAGEFLK-NYVFVAIGIVG 270
Cdd:cd18052 240 PEEIQRLAAEFLKeDYLFLTVGRVG 264
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
46-428 |
5.51e-127 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 378.35 E-value: 5.51e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 46 VTGSDVPQPIQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHeL 125
Cdd:PTZ00110 120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPL-L 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 126 ELGR-PQVVIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDT 204
Cdd:PTZ00110 199 RYGDgPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 205 RFVVLDEADRMLDMGFSEDMRRIMTHVtmRPEHQTLMFSATFPEEIQRMAGEFLKNY-VFVAIGIVG-GACSDVKQTIYE 282
Cdd:PTZ00110 279 TYLVLDEADRMLDMGFEPQIRKIVSQI--RPDRQTLMWSATWPKEVQSLARDLCKEEpVHVNVGSLDlTACHNIKQEVFV 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 283 VNKYAKRSKLIEILSE---QADGTIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSV 359
Cdd:PTZ00110 357 VEEHEKRGKLKMLLQRimrDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDV 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2DB3_D 360 ASRGLDIKNIKHVINYDMPSKIDDYVHRIGRTGRVGNNGRATSFFDPEKDRaIAADLVKILEGSGQTVP 428
Cdd:PTZ00110 437 ASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYR-LARDLVKVLREAKQPVP 504
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
36-270 |
4.85e-108 |
|
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 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: 350809 [Multi-domain] Cd Length: 249 Bit Score: 319.29 E-value: 4.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 36 FSKYNNIPVKVTGSDVPQPIQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPIL 115
Cdd:cd18051 1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 116 SKLLED-PHELEL------GR----PQVVIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVI 184
Cdd:cd18051 81 SQIYEQgPGESLPsesgyyGRrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 185 ATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMRRIMTHVTMRP--EHQTLMFSATFPEEIQRMAGEFLKNYV 262
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPtgERQTLMFSATFPKEIQMLARDFLDNYI 240
|
....*...
2DB3_D 263 FVAIGIVG 270
Cdd:cd18051 241 FLAVGRVG 248
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
58-414 |
1.54e-106 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 322.91 E-value: 1.54e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLleDPHELelgRPQVVIVSP 137
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--DVKRF---RVQALVLCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 138 TRELAIQIFNEARKFA-FESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRML 216
Cdd:PRK11776 81 TRELADQVAKEIRRLArFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 217 DMGFSEDMRRIMTHvtMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFVAIGIVGGAcSDVKQTIYEVNKYAKRSKLIEIL 296
Cdd:PRK11776 161 DMGFQDAIDAIIRQ--APARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEVSPDERLPALQRLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 297 SE-QADGTIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIKNIKHVINY 375
Cdd:PRK11776 238 LHhQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINY 317
|
330 340 350
....*....|....*....|....*....|....*....
2DB3_D 376 DMPSKIDDYVHRIGRTGRVGNNGRATSFFDPEKDRAIAA 414
Cdd:PRK11776 318 ELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANA 356
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
67-264 |
7.83e-99 |
|
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: 293.58 E-value: 7.83e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELElGRPQVVIVSPTRELAIQIF 146
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKG-RGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 147 NEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMRR 226
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*...
2DB3_D 227 IMTHvtMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd00268 160 ILSA--LPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
58-403 |
2.24e-96 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 296.08 E-value: 2.24e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHElELGRPQVVIVSP 137
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRR-KSGPPRILILTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 138 TRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLD 217
Cdd:PRK11192 82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 218 MGFSEDMRRIMTHVTMRpeHQTLMFSATFP-EEIQRMAGEFLKNYVFVaigivggacsDVK----------QTIYEV-NK 285
Cdd:PRK11192 162 MGFAQDIETIAAETRWR--KQTLLFSATLEgDAVQDFAERLLNDPVEV----------EAEpsrrerkkihQWYYRAdDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 286 YAKRSKLIEILS-EQADGTIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGL 364
Cdd:PRK11192 230 EHKTALLCHLLKqPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGI 309
|
330 340 350
....*....|....*....|....*....|....*....
2DB3_D 365 DIKNIKHVINYDMPSKIDDYVHRIGRTGRVGNNGRATSF 403
Cdd:PRK11192 310 DIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
58-402 |
2.84e-94 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 291.33 E-value: 2.84e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGRP-QVVIVS 136
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPvRALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 137 PTRELAIQIFNEARKFAfeSYLKIG--IVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADR 214
Cdd:PRK10590 83 PTRELAAQIGENVRDYS--KYLNIRslVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 215 MLDMGFSEDMRRIMThvTMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFVAIGIVGGACSDVKQTIYEVNKYAKRSKLIE 294
Cdd:PRK10590 161 MLDMGFIHDIRRVLA--KLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 295 ILSEQA-DGTIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIKNIKHVI 373
Cdd:PRK10590 239 MIGKGNwQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340
....*....|....*....|....*....
2DB3_D 374 NYDMPSKIDDYVHRIGRTGRVGNNGRATS 402
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALS 347
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
20-428 |
5.39e-88 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 277.05 E-value: 5.39e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 20 NDAIEIFSSGIASGIHFSKYN----NIPVKVTGSDVPQPIQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRD 95
Cdd:PLN00206 81 DECFYVRDPGSTSGLSSSQAEllrrKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 96 LMACAQTGSGKTAAFLLPILSK--LLEDPHELELGRPQVVIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQN 173
Cdd:PLN00206 161 LLVSADTGSGKTASFLVPIISRccTIRSGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 174 ECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEdmrRIMTHVTMRPEHQTLMFSATFPEEIQRM 253
Cdd:PLN00206 241 YRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRD---QVMQIFQALSQPQVLLFSATVSPEVEKF 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 254 AGEFLKNYVFVAIGIVGGACSDVKQTIYEVNKYAKRSKLIEILSEQADGT---IVFVETKRGADFLASFLSE-KEFPTTS 329
Cdd:PLN00206 318 ASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKppaVVFVSSRLGADLLANAITVvTGLKALS 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 330 IHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIKNIKHVINYDMPSKIDDYVHRIGRTGRVGNNGRATSFFDpEKD 409
Cdd:PLN00206 398 IHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVN-EED 476
|
410
....*....|....*....
2DB3_D 410 RAIAADLVKILEGSGQTVP 428
Cdd:PLN00206 477 RNLFPELVALLKSSGAAIP 495
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
58-410 |
2.90e-86 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 275.57 E-value: 2.90e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLleDPhelELGRPQVVIVSP 137
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DP---ELKAPQILVLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 138 TRELAIQIFNEARKFAfESYLKIGIV--YGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRM 215
Cdd:PRK11634 83 TRELAVQVAEAMTDFS-KHMRGVNVValYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 216 LDMGFSEDMRRIMTHVTmrPEHQTLMFSATFPEEIQRMAGEFLKNYVFVAIGIVGGACSDVKQTIYEVNKYAKRSKLIEI 295
Cdd:PRK11634 162 LRMGFIEDVETIMAQIP--EGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 296 L-SEQADGTIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIKNIKHVIN 374
Cdd:PRK11634 240 LeAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVN 319
|
330 340 350
....*....|....*....|....*....|....*.
2DB3_D 375 YDMPSKIDDYVHRIGRTGRVGNNGRATSFFDPEKDR 410
Cdd:PRK11634 320 YDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERR 355
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
49-403 |
4.21e-84 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 268.36 E-value: 4.21e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 49 SDVPQPIQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPH--ELE 126
Cdd:PRK04537 2 SDKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPAlaDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 127 LGRPQVVIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDR-TFITFEDTR 205
Cdd:PRK04537 82 PEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 206 FVVLDEADRMLDMGFSEDMRRIMTHVTMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFVAIGIVGGACSDVKQTIYEVNK 285
Cdd:PRK04537 162 ICVLDEADRMFDLGFIKDIRFLLRRMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 286 YAKRSKLIEILSeQADG--TIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRG 363
Cdd:PRK04537 242 EEKQTLLLGLLS-RSEGarTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
2DB3_D 364 LDIKNIKHVINYDMPSKIDDYVHRIGRTGRVGNNGRATSF 403
Cdd:PRK04537 321 LHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
56-403 |
3.84e-81 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 256.44 E-value: 3.84e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 56 QHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLL--EDPHELELGRPQVV 133
Cdd:PRK04837 8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLshPAPEDRKVNQPRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 134 IVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEAD 213
Cdd:PRK04837 88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 214 RMLDMGFSEDMR---RIMTHVTMRpehQTLMFSATFPEEIQRMAGEFLKNYVFVAIGIVGGACSDVKQTI-YEVN--KYA 287
Cdd:PRK04837 168 RMFDLGFIKDIRwlfRRMPPANQR---LNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELfYPSNeeKMR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 288 KRSKLIEilSEQADGTIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIK 367
Cdd:PRK04837 245 LLQTLIE--EEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIP 322
|
330 340 350
....*....|....*....|....*....|....*.
2DB3_D 368 NIKHVINYDMPSKIDDYVHRIGRTGRVGNNGRATSF 403
Cdd:PRK04837 323 AVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
75-403 |
1.57e-80 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 256.38 E-value: 1.57e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 75 GYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELE--LGRPQVVIVSPTRELAIQIFNEARKF 152
Cdd:PRK01297 106 GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKEryMGEPRALIIAPTRELVVQIAKDAAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 153 AFESYLKIGIVYGGTSFRHQNECI-TRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMRRIMTHV 231
Cdd:PRK01297 186 TKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQT 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 232 TMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFVAIGIVGGACSDVKQTIYEVNKYAKRSKLIEILSEQA-DGTIVFVETK 310
Cdd:PRK01297 266 PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNLVTQNPwERVMVFANRK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 311 RGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIKNIKHVINYDMPSKIDDYVHRIGR 390
Cdd:PRK01297 346 DEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGR 425
|
330
....*....|...
2DB3_D 391 TGRVGNNGRATSF 403
Cdd:PRK01297 426 TGRAGASGVSISF 438
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
67-264 |
1.75e-69 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 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: 350724 [Multi-domain] Cd Length: 197 Bit Score: 218.39 E-value: 1.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHeLELGR-PQVVIVSPTRELAIQI 145
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPP-LERGDgPIVLVLAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 146 FNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMR 225
Cdd:cd17966 80 QQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*....
2DB3_D 226 RIMTHVtmRPEHQTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17966 160 KIVDQI--RPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
67-264 |
1.49e-65 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 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: 350703 [Multi-domain] Cd Length: 220 Bit Score: 209.10 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGR---PQVVIVSPTRELAI 143
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKddgPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 144 QIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSED 223
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
2DB3_D 224 MRRIMTHVT---MRPEH---------------QTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17945 161 VTKILDAMPvsnKKPDTeeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
67-264 |
3.53e-65 |
|
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: 207.27 E-value: 3.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPhELELGR-PQVVIVSPTRELAIQI 145
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQR-ELEKGEgPIAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 146 FNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMR 225
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*....
2DB3_D 226 RIMTHVtmRPEHQTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17952 160 SIVGHV--RPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
80-252 |
7.69e-65 |
|
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: 205.55 E-value: 7.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 80 TPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLledphELELGRPQVVIVSPTRELAIQIFNEARKFAFESYLK 159
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL-----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 160 IGIVYGGTSFRHQNECItRGCHVVIATPGRLLDFVDRTFiTFEDTRFVVLDEADRMLDMGFSEDMRRIMTHvtMRPEHQT 239
Cdd:pfam00270 76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LPKKRQI 151
|
170
....*....|...
2DB3_D 240 LMFSATFPEEIQR 252
Cdd:pfam00270 152 LLLSATLPRNLED 164
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
45-262 |
1.76e-63 |
|
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: 204.15 E-value: 1.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 45 KVTGSDVPQPIQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHE 124
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 125 LELGRPQVVIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFV---DRTFITF 201
Cdd:cd17953 81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
2DB3_D 202 EDTRFVVLDEADRMLDMGFSEDMRRIMTHVtmRPEHQTLMFSATFPEEIQRMAGEFLKNYV 262
Cdd:cd17953 161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNI--RPDRQTVLFSATFPRKVEALARKVLHKPI 219
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
67-267 |
5.42e-63 |
|
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: 201.66 E-value: 5.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHElelGRPQVVIVSPTRELAIQIF 146
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKK---KGLRALILAPTRELASQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 147 NEARKFAFESYLKIGIVYGGT--SFRHQNECITRgCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDM 224
Cdd:cd17957 78 RELLKLSKGTGLRIVLLSKSLeaKAKDGPKSITK-YDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
2DB3_D 225 RRIMTHVTmRPEHQTLMFSATFPEEIQRMAGEFLKNYVFVAIG 267
Cdd:cd17957 157 DEILAACT-NPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
55-407 |
1.91e-62 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 206.99 E-value: 1.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 55 IQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLledphELELGRPQVVI 134
Cdd:PTZ00424 27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI-----DYDLNACQALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 135 VSPTRELAIQIfnEARKFAFESYLKIGI--VYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEA 212
Cdd:PTZ00424 102 LAPTRELAQQI--QKVVLALGDYLKVRChaCVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 213 DRMLDMGFSEDMRRIMTHvtMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFVAIGIVGGACSDVKQTIYEVN----KYAK 288
Cdd:PTZ00424 180 DEMLSRGFKGQIYDVFKK--LPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEkeewKFDT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 289 RSKLIEILS-EQAdgtIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIK 367
Cdd:PTZ00424 258 LCDLYETLTiTQA---IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
|
330 340 350 360
....*....|....*....|....*....|....*....|
2DB3_D 368 NIKHVINYDMPSKIDDYVHRIGRTGRVGNNGRATSFFDPE 407
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPD 374
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
67-264 |
3.87e-60 |
|
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: 194.72 E-value: 3.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVI-SSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGRPQVVIVSPTRELAIQI 145
Cdd:cd17964 5 LLKALTRMGFETMTPVQQKTLKPIlSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTRELALQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 146 FNEARKF-AFESYLKIGIVYGGTSFRHQ-NECITRGCHVVIATPGRLLDFVD--RTFITFEDTRFVVLDEADRMLDMGFS 221
Cdd:cd17964 85 AAEAKKLlQGLRKLRVQSAVGGTSRRAElNRLRRGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLDMGFR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
2DB3_D 222 EDMRRIMTHVTMRPEH--QTLMFSATFPEEIQRMAGEFL-KNYVFV 264
Cdd:cd17964 165 PDLEQILRHLPEKNADprQTLLFSATVPDEVQQIARLTLkKDYKFI 210
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
75-264 |
2.39e-59 |
|
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: 192.47 E-value: 2.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 75 GYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGRpqVVIVSPTRELAIQIFNEARKFAF 154
Cdd:cd17947 9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATR--VLVLVPTRELAMQCFSVLQQLAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 155 ESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTF-ITFEDTRFVVLDEADRMLDMGFSEDMRRIMTHVtm 233
Cdd:cd17947 87 FTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADELKEILRLC-- 164
|
170 180 190
....*....|....*....|....*....|..
2DB3_D 234 rPEH-QTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17947 165 -PRTrQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
276-404 |
3.43e-58 |
|
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: 186.94 E-value: 3.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 276 VKQTIYEVNKYAKRSKLIEILSEQADG--TIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKV 353
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPgkAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
2DB3_D 354 LIATSVASRGLDIKNIKHVINYDMPSKIDDYVHRIGRTGRVGNNGRATSFF 404
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
58-264 |
1.97e-57 |
|
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: 187.51 E-value: 1.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEdpHELELGrPQVVIVSP 137
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKA--HSPTVG-ARALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 138 TRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLD 217
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
2DB3_D 218 MGFSEDMRRIMTHvtMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17959 160 MGFAEQLHEILSR--LPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
35-267 |
4.20e-57 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 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: 350807 [Multi-domain] Cd Length: 234 Bit Score: 187.91 E-value: 4.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 35 HFSKYNNIPVKvtGSDVPQPIQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPI 114
Cdd:cd18049 5 QYRRSKEITVR--GHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 115 LSKLLEDPHeLELGR-PQVVIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDF 193
Cdd:cd18049 83 IVHINHQPF-LERGDgPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2DB3_D 194 VDRTFITFEDTRFVVLDEADRMLDMGFSEDMRRIMTHVtmRPEHQTLMFSATFPEEIQRMAGEFLKNYVFVAIG 267
Cdd:cd18049 162 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI--RPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
67-264 |
7.57e-57 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 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: 350716 [Multi-domain] Cd Length: 197 Bit Score: 185.75 E-value: 7.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELEL-GRPQVVIVSPTRELAIQI 145
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQrNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 146 FNEARKFAFESYlKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMR 225
Cdd:cd17958 81 EAECSKYSYKGL-KSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*....
2DB3_D 226 RIMTHVtmRPEHQTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17958 160 KILLDI--RPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
71-278 |
1.29e-56 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 185.39 E-value: 1.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 71 VNKSGYKIPTPIQKCSIPVISSG-RDLMACAQTGSGKTAAFLLPILSKLLEDPHelelgrPQVVIVSPTRELAIQIFNEA 149
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKG------GRVLVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 150 RKFAFESYLKIGIVYGGTSFRHQNECITRGC-HVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMRRIM 228
Cdd:smart00487 75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
2DB3_D 229 THvtMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFVAIGIvgGACSDVKQ 278
Cdd:smart00487 155 KL--LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQ 200
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
44-267 |
7.58e-56 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 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: 350808 [Multi-domain] Cd Length: 271 Bit Score: 185.98 E-value: 7.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 44 VKVTGSDVPQPIQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPH 123
Cdd:cd18050 50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 124 eLELGR-PQVVIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFE 202
Cdd:cd18050 130 -LERGDgPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLR 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
2DB3_D 203 DTRFVVLDEADRMLDMGFSEDMRRIMTHVtmRPEHQTLMFSATFPEEIQRMAGEFLKNYVFVAIG 267
Cdd:cd18050 209 RCTYLVLDEADRMLDMGFEPQIRKIVDQI--RPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
58-263 |
1.46e-54 |
|
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: 180.11 E-value: 1.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHElelgrPQVVIVSP 137
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYG-----IFALVLTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 138 TRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFV---DRTFITFEDTRFVVLDEADR 214
Cdd:cd17955 76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLrssDDTTKVLSRVKFLVLDEADR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
2DB3_D 215 MLDMGFSEDMRRIMTHVTmrPEHQTLMFSATFPEEIQRMAGEFLKNYVF 263
Cdd:cd17955 156 LLTGSFEDDLATILSALP--PKRQTLLFSATLTDALKALKELFGNKPFF 202
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
72-264 |
6.32e-54 |
|
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: 178.25 E-value: 6.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 72 NKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGRpQVVIVSPTRELAIQIFNEARK 151
Cdd:cd17941 6 KEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGL-GALIISPTRELAMQIFEVLRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 152 FAFESYLKIGIVYGGTSFRHQNECITRgCHVVIATPGRLLDFVDRT-FITFEDTRFVVLDEADRMLDMGFSEDMRRIMTH 230
Cdd:cd17941 85 VGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDAIVEN 163
|
170 180 190
....*....|....*....|....*....|....
2DB3_D 231 vtMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17941 164 --LPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
71-264 |
1.96e-53 |
|
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: 177.78 E-value: 1.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 71 VNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHEL--ELGrPQVVIVSPTRELAIQIFNE 148
Cdd:cd17949 6 KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVdrSDG-TLALVLVPTRELALQIYEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 149 ARKF-AFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRT-FITFEDTRFVVLDEADRMLDMGFSEDMRR 226
Cdd:cd17949 85 LEKLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTqSFDVSNLRWLVLDEADRLLDMGFEKDITK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
2DB3_D 227 IMTHV-----------TMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17949 165 ILELLddkrskaggekSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
67-264 |
2.53e-53 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 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: 350709 [Multi-domain] Cd Length: 206 Bit Score: 177.15 E-value: 2.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGR---PQVVIVSPTRELAI 143
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLPFIKgegPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 144 QIFNE----ARKFAFESY--LKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLD 217
Cdd:cd17951 81 QTHEVieyyCKALQEGGYpqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
2DB3_D 218 MGFSEDMRRIMTHVTmrPEHQTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17951 161 MGFEEDIRTIFSYFK--GQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
58-265 |
3.34e-50 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 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: 350712 [Multi-domain] Cd Length: 203 Bit Score: 168.65 E-value: 3.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELelgrpQVVIVSP 137
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRF-----FALVLAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 138 TRELAIQIFNEarkfaFESY-----LKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRT--FiTFEDTRFVVLD 210
Cdd:cd17954 77 TRELAQQISEQ-----FEALgssigLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTkgF-SLKSLKFLVMD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
2DB3_D 211 EADRMLDMGFSEDMRRIMTHVtmrP-EHQTLMFSATFPEEIQRMAGEFLKNYVFVA 265
Cdd:cd17954 151 EADRLLNMDFEPEIDKILKVI---PrERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
67-264 |
1.95e-49 |
|
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: 166.60 E-value: 1.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDphELELGRPQV--VIVSPTRELAIQ 144
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKR--KANLKKGQVgaLIISPTRELATQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 145 IFNEARKFA--FESYLKIGIVYGGTSFRHQNECITR-GCHVVIATPGRLLDFVDR--TFITFEDTRFVVLDEADRMLDMG 219
Cdd:cd17960 79 IYEVLQSFLehHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDEADRLLDLG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
2DB3_D 220 FSEDMRRIMTHVtmrP-EHQTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17960 159 FEADLNRILSKL---PkQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
70-264 |
3.64e-49 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 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: 350720 [Multi-domain] Cd Length: 193 Bit Score: 165.80 E-value: 3.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 70 NVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEdphelELGRPQVVIVSPTRELAIQIFNEA 149
Cdd:cd17962 4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT-----EHRNPSALILTPTRELAVQIEDQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 150 RKFAF-ESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMRRIM 228
Cdd:cd17962 79 KELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
|
170 180 190
....*....|....*....|....*....|....*.
2DB3_D 229 THVTmrPEHQTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17962 159 ENIS--HDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
58-260 |
6.00e-48 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, 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: 350698 [Multi-domain] Cd Length: 201 Bit Score: 162.85 E-value: 6.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLledphELELGRPQVVIVSP 137
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-----DPKKDVIQALILVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 138 TRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLD 217
Cdd:cd17940 76 TRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
2DB3_D 218 MGFSEDMRRIMTHvtMRPEHQTLMFSATFPEEIQRMAGEFLKN 260
Cdd:cd17940 156 QDFQPIIEKILNF--LPKERQILLFSATFPLTVKNFMDRHMHN 196
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
73-246 |
5.30e-45 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 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: 350704 [Multi-domain] Cd Length: 235 Bit Score: 156.25 E-value: 5.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 73 KSGYKIPTPIQKCSIPV-ISSGRDLMACAQTGSGKTAAFLLPILSKLLED----PHELELGRPQVVIVSPTRELAIQIFN 147
Cdd:cd17946 7 DLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQkssnGVGGKQKPLRALILTPTRELAVQVKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 148 EARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFV--DRTFIT-FEDTRFVVLDEADRMLDMGFSEDM 224
Cdd:cd17946 87 HLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIqeGNEHLAnLKSLRFLVLDEADRMLEKGHFAEL 166
|
170 180
....*....|....*....|....*..
2DB3_D 225 RRI--MTHVTMRPEH---QTLMFSATF 246
Cdd:cd17946 167 EKIleLLNKDRAGKKrkrQTFVFSATL 193
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
75-264 |
2.67e-42 |
|
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: 147.72 E-value: 2.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 75 GYKIPTPIQKCSIPVISSG--RDLMACAQTGSGKTAAFLLPILSKLledphELELGRPQVVIVSPTRELAIQIFNEARKF 152
Cdd:cd17963 13 GFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-----DPTLKSPQALCLAPTRELARQIGEVVEKM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 153 AFESYLKIGIVYGGTSFRhQNECITRgcHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDM-GFSEDMRRIMTHv 231
Cdd:cd17963 88 GKFTGVKVALAVPGNDVP-RGKKITA--QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQSIRIKRM- 163
|
170 180 190
....*....|....*....|....*....|...
2DB3_D 232 tMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17963 164 -LPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
75-254 |
4.20e-42 |
|
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: 147.51 E-value: 4.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 75 GYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLledpHELELgRPQ----VVIVSPTRELAIQIFNEAR 150
Cdd:cd17942 9 GFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELL----YKLKF-KPRngtgVIIISPTRELALQIYGVAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 151 KFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRT--FItFEDTRFVVLDEADRMLDMGFSEDMRRIM 228
Cdd:cd17942 84 ELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTkgFL-YKNLQCLIIDEADRILEIGFEEEMRQII 162
|
170 180
....*....|....*....|....*.
2DB3_D 229 THVTMRpeHQTLMFSATFPEEIQRMA 254
Cdd:cd17942 163 KLLPKR--RQTMLFSATQTRKVEDLA 186
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
75-262 |
3.75e-40 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins 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: 350697 [Multi-domain] Cd Length: 199 Bit Score: 142.46 E-value: 3.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 75 GYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLledphELELGRPQVVIVSPTRELAIQIFNEARKFAF 154
Cdd:cd17939 16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI-----DTTVRETQALVLAPTRELAQQIQKVVKALGD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 155 ESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMRRIMTHVTmr 234
Cdd:cd17939 91 YMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLP-- 168
|
170 180
....*....|....*....|....*...
2DB3_D 235 PEHQTLMFSATFPEEIQRMAGEFLKNYV 262
Cdd:cd17939 169 PETQVVLFSATMPHEVLEVTKKFMRDPV 196
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
67-264 |
5.82e-40 |
|
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: 142.07 E-value: 5.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILsklledphelelgrpQVV---IVSPTRELAI 143
Cdd:cd17938 10 LIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL---------------QIVvalILEPSRELAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 144 QIFNEARKFAfeSYLK-----IGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDM 218
Cdd:cd17938 75 QTYNCIENFK--KYLDnpklrVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
2DB3_D 219 GFSEDMRRIMTHVtmrPEH-------QTLMFSATF-PEEIQRMAGEFLKNYVFV 264
Cdd:cd17938 153 GNLETINRIYNRI---PKItsdgkrlQVIVCSATLhSFEVKKLADKIMHFPTWV 203
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
71-260 |
6.17e-40 |
|
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: 141.95 E-value: 6.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 71 VNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGR-PQVVIVSPTRELAIQIFNEA 149
Cdd:cd17961 9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQgTRALILVPTRELAQQVSKVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 150 RKFA--FESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDR-TFITFEDTRFVVLDEADRMLDMGFSEDMRR 226
Cdd:cd17961 89 EQLTayCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESgSLLLLSTLKYLVIDEADLVLSYGYEEDLKS 168
|
170 180 190
....*....|....*....|....*....|....
2DB3_D 227 IMTHVTMRpeHQTLMFSATFPEEIQRMAGEFLKN 260
Cdd:cd17961 169 LLSYLPKN--YQTFLMSATLSEDVEALKKLVLHN 200
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
68-259 |
5.02e-39 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both 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. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 139.60 E-value: 5.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 68 IDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGR-PQVVIVSPTRELAIQIF 146
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRaPKVLVLAPTRELANQVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 147 NEARKFAFEsyLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMRR 226
Cdd:cd17944 82 KDFKDITRK--LSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159
|
170 180 190
....*....|....*....|....*....|....*..
2DB3_D 227 IMtHVTMR--PEH--QTLMFSATFPEEIQRMAGEFLK 259
Cdd:cd17944 160 IL-SVSYKkdSEDnpQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
67-264 |
2.28e-38 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 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: 350701 [Multi-domain] Cd Length: 192 Bit Score: 137.40 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLedpheLELGRPQVVIVSPTRELAIQIF 146
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD-----LERRHPQVLILAPTREIAVQIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 147 NEARKFA-FESYLKIGIVYGGTSFRhQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMR 225
Cdd:cd17943 76 DVFKKIGkKLEGLKCEVFIGGTPVK-EDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154
|
170 180 190
....*....|....*....|....*....|....*....
2DB3_D 226 RIMTHvtMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFV 264
Cdd:cd17943 155 WIFSS--LPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
63-260 |
2.23e-36 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 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: 350708 [Multi-domain] Cd Length: 208 Bit Score: 132.47 E-value: 2.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 63 LRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHELelgrpQVVIVSPTRELA 142
Cdd:cd17950 9 LKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQV-----SVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 143 IQIFNEARKFAfeSYL---KIGIVYGGTSFRHQNECI-TRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDm 218
Cdd:cd17950 84 FQISNEYERFS--KYMpnvKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
2DB3_D 219 gfSEDMRR-IMTHVTMRP-EHQTLMFSATFPEEIQRMAGEFLKN 260
Cdd:cd17950 161 --QLDMRRdVQEIFRATPhDKQVMMFSATLSKEIRPVCKKFMQD 202
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
58-262 |
2.71e-36 |
|
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: 132.18 E-value: 2.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLledphELELGRPQVVIVSP 137
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI-----DTSLKATQALVLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 138 TRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLD 217
Cdd:cd18046 76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
2DB3_D 218 MGFSEDMRRIMThvTMRPEHQTLMFSATFPEEIQRMAGEFLKNYV 262
Cdd:cd18046 156 RGFKDQIYDIFQ--KLPPDTQVVLLSATMPNDVLEVTTKFMRDPI 198
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
67-248 |
2.76e-36 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 132.88 E-value: 2.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPH--ELELGRPQVVIVSPTRELAIQ 144
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLlaEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 145 IFNEARKFAFESYLKIGIVYGGTSFR-----HQNEcitrgCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRMLDMG 219
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRqirnpHFEE-----VDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
2DB3_D 220 FSEDMRRIM--THVTMRPEH---------QTLMFSATFPE 248
Cdd:cd17948 156 FNEKLSHFLrrFPLASRRSEntdgldpgtQLVLVSATMPS 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
287-395 |
1.21e-35 |
|
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: 127.33 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 287 AKRSKLIEILSEQADG-TIVFVETKRGADfLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLD 365
Cdd:pfam00271 1 EKLEALLELLKKERGGkVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
2DB3_D 366 IKNIKHVINYDMPSKIDDYVHRIGRTGRVG 395
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
58-262 |
4.73e-35 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 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: 350803 [Multi-domain] Cd Length: 201 Bit Score: 128.74 E-value: 4.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKLledphELELGRPQVVIVSP 137
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL-----DIQVRETQALILSP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 138 TRELAIQIFNEArkFAFESYLKIGI--VYGGTSFRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADRM 215
Cdd:cd18045 76 TRELAVQIQKVL--LALGDYMNVQChaCIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
2DB3_D 216 LDMGFSEDMRRIMTHVTmrPEHQTLMFSATFPEEIQRMAGEFLKNYV 262
Cdd:cd18045 154 LNKGFKEQIYDVYRYLP--PATQVVLVSATLPQDILEMTNKFMTDPI 198
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
67-253 |
6.23e-31 |
|
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: 118.50 E-value: 6.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIPVI---------SSGRDLMACAQTGSGKTAAFLLPILSKLLEDPHElelgRPQVVIVSP 137
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLlpsskstppYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVP----RLRALIVVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 138 TRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQNECITRGCH--------VVIATPGRLLDFVDRT-FITFEDTRFVV 208
Cdd:cd17956 77 TKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTpGFTLKHLRFLV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
2DB3_D 209 LDEADRMLDMGF-------------SEDMRRIMTHVTMRPEH-----QTLMFSATF---PEEIQRM 253
Cdd:cd17956 157 IDEADRLLNQSFqdwletvmkalgrPTAPDLGSFGDANLLERsvrplQKLLFSATLtrdPEKLSSL 222
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
314-395 |
3.80e-29 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 108.84 E-value: 3.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 314 DFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIKNIKHVINYDMPSKIDDYVHRIGRTGR 393
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
2DB3_D 394 VG 395
Cdd:smart00490 81 AG 82
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
62-265 |
3.42e-25 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 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: 350723 [Multi-domain] Cd Length: 251 Bit Score: 103.61 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 62 DLRDIIID-----NVNKSGYKIPTPIQKCSIPVISSGR----------------DLMACAQTGSGKTAAFLLPILSKL-- 118
Cdd:cd17965 9 SVREAIIKeilkgSNKTDEEIKPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLkr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 119 ------LEDPHELEL----GRPQVVIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQ--NECITRGCHVVIAT 186
Cdd:cd17965 89 qeqepfEEAEEEYESakdtGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQrlQLAFKGRIDILVTT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2DB3_D 187 PGRLLDFVDRTFITFEDTRFVVLDEADRMLDMGFSEDMRRIMTHvtMRPEHQTLMFSATFPEEIQRMAGEFLKNYVFVA 265
Cdd:cd17965 169 PGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APKLKHLILCSATIPKEFDKTLRKLFPDVVRIA 245
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
44-254 |
7.28e-23 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) 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: 350806 [Multi-domain] Cd Length: 229 Bit Score: 96.24 E-value: 7.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 44 VKVTGSDVPQP---IQHFTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVISSG--RDLMACAQTGSGKTAAFLLPILSKL 118
Cdd:cd18048 3 VEVLQRDPTSPlfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 119 leDPHELelgRPQVVIVSPTRELAIQ---IFNEARKFAfesyLKIGIVYGGTSFRhqnecITRGC----HVVIATPGRLL 191
Cdd:cd18048 83 --DALKL---YPQCLCLSPTFELALQtgkVVEEMGKFC----VGIQVIYAIRGNR-----PGKGTdieaQIVIGTPGTVL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
2DB3_D 192 DFVDR-TFITFEDTRFVVLDEADRMLDM-GFSEDMRRIMThvTMRPEHQTLMFSATFPEEIQRMA 254
Cdd:cd18048 149 DWCFKlRLIDVTNISVFVLDEADVMINVqGHSDHSVRVKR--SMPKECQMLLFSATFEDSVWAFA 211
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
93-416 |
4.83e-22 |
|
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: 4.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 93 GRDLMACAQTGSGKTAAFLLpILSKLLEdphelelgRPQVVIVSPTRELAIQIFNEARKFafesyLKIGIVYGGTSFRHq 172
Cdd:COG1061 100 GGRGLVVAPTGTGKTVLALA-LAAELLR--------GKRVLVLVPRRELLEQWAEELRRF-----LGDPLAGGGKKDSD- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 173 necitrgCHVVIATPGRL-----LDFVDRTFitfedtRFVVLDEADRMLDMGFsedmRRIMTHvtMRPEHqTLMFSAT-- 245
Cdd:COG1061 165 -------APITVATYQSLarrahLDELGDRF------GLVIIDEAHHAGAPSY----RRILEA--FPAAY-RLGLTATpf 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 246 ----FPEEIQR-------------MAGEFLKNYVFVAIGI-------VGGACSDVKQTIYEVNKYAKRSKLIEILSEQAD 301
Cdd:COG1061 225 rsdgREILLFLfdgivyeyslkeaIEDGYLAPPEYYGIRVdltderaEYDALSERLREALAADAERKDKILRELLREHPD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 302 G--TIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIKNIKHVInYDMP- 378
Cdd:COG1061 305 DrkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPt 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....
2DB3_D 379 -SKIdDYVHRIGRTGRVGNNGRATSFFD-----PEKDRAIAADL 416
Cdd:COG1061 384 gSPR-EFIQRLGRGLRPAPGKEDALVYDfvgndVPVLEELAKDL 426
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
93-245 |
3.78e-20 |
|
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: 86.30 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 93 GRDLMACAQTGSGKTAAFLLPILsklledpHELELGRPQVVIVSPTRELAIQIFNEARKFAFESYlKIGIVYGGTSFRHQ 172
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAAL-------LLLLKKGKKVLVLVPTKALALQTAERLRELFGPGI-RVAVLVGGSSAEER 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2DB3_D 173 NECITRGCHVVIATPGRLLDFVDRTF-ITFEDTRFVVLDEADRMLDMGFSEDMRRIMTHVTMRPEHQTLMFSAT 245
Cdd:cd00046 73 EKNKLGDADIIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
90-404 |
2.73e-18 |
|
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: 87.58 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 90 ISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPhelelgRPQVVIVSPTRELA------IQIFNEarkfAFESYLKIGIV 163
Cdd:COG1205 68 ARAGKNVVIATPTASGKSLAYLLPVLEALLEDP------GATALYLYPTKALArdqlrrLRELAE----ALGLGVRVATY 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 164 YGGTSfRHQNECITRGCHVVIATPgrllDFVDRTFI--------TFEDTRFVVLDEA---------------DRmldmgf 220
Cdd:COG1205 138 DGDTP-PEERRWIREHPDIVLTNP----DMLHYGLLphhtrwarFFRNLRYVVIDEAhtyrgvfgshvanvlRR------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 221 sedMRRIMTHVTMRPehQTLMFSATF--PEEI-QRMAGEflknyVFVAIGIVGGACSDVKQTIYE---VNKYAKRSKL-- 292
Cdd:COG1205 207 ---LRRICRHYGSDP--QFILASATIgnPAEHaERLTGR-----PVTVVDEDGSPRGERTFVLWNpplVDDGIRRSALae 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 293 -IEILSEQADG---TIVFVETKRGADFLASFLSE---KEFPTTSI---HGDRLQSQREQALRDFKNGSMKVLIATSVASR 362
Cdd:COG1205 277 aARLLADLVREglrTLVFTRSRRGAELLARYARRalrEPDLADRVaayRAGYLPEERREIERGLRSGELLGVVSTNALEL 356
|
330 340 350 360
....*....|....*....|....*....|....*....|..
2DB3_D 363 GLDIKNIKHVINYDMPSKIDDYVHRIGRTGRVGNngRATSFF 404
Cdd:COG1205 357 GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQ--DSLVVL 396
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
288-399 |
2.22e-17 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 84.40 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 288 KRSKLIEILSEQADG-----TIVFVETKRGADFLASFLSEKEFPTT------SIHGDRLQSQREQ--ALRDFKNGSMKVL 354
Cdd:COG1111 336 KLSKLREILKEQLGTnpdsrIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKGLTQKEQieILERFRAGEFNVL 415
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
2DB3_D 355 IATSVASRGLDIKNIKHVINYD-MPSKIdDYVHRIGRTGRvGNNGR 399
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEpVPSEI-RSIQRKGRTGR-KREGR 459
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
58-254 |
1.36e-16 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 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: 350805 [Multi-domain] Cd Length: 205 Bit Score: 78.22 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 58 FTSADLRDIIIDNVNKSGYKIPTPIQKCSIPVI--SSGRDLMACAQTGSGKTAAFLLPILSKLleDPhelELGRPQVVIV 135
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMlaEPPQNLIAQSQSGTGKTAAFVLAMLSQV--EP---ANKYPQCLCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 136 SPTRELAIQ---IFNEARKFafesYLKIGIVYGGTSFRHQNECITRGcHVVIATPGRLLDF-VDRTFITFEDTRFVVLDE 211
Cdd:cd18047 78 SPTYELALQtgkVIEQMGKF----YPELKLAYAVRGNKLERGQKISE-QIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
2DB3_D 212 ADRML-DMGFSEDMRRIMthvTMRPEH-QTLMFSATFPEEIQRMA 254
Cdd:cd18047 153 ADVMIaTQGHQDQSIRIQ---RMLPRNcQMLLFSATFEDSVWKFA 194
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
281-412 |
1.17e-15 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 78.64 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 281 YEVNK---YAKRSKLIEILSEQADGT-IVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIA 356
Cdd:COG0514 207 LEVVPkppDDKLAQLLDFLKEHPGGSgIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVA 286
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
2DB3_D 357 TSVASRGLDIKNIKHVINYDMPSKIDDYVHRIGRTGRVGNNGRATSFFDPEkDRAI 412
Cdd:COG0514 287 TIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE-DVAI 341
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
275-399 |
5.24e-15 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 77.22 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 275 DVKQTIYEVNKYA----KRSKLIEILSEQADG-----TIVFVETKRGADFLASFLSEKEFPT------TSIHGDRLQSQR 339
Cdd:PRK13766 331 RFRKAVRKAKELDiehpKLEKLREIVKEQLGKnpdsrIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKGMSQK 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
2DB3_D 340 EQ--ALRDFKNGSMKVLIATSVASRGLDIKNIKHVINYD-MPSKIdDYVHRIGRTGRvGNNGR 399
Cdd:PRK13766 411 EQieILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGR 471
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
288-390 |
5.05e-13 |
|
C-terminal helicase domain of the 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. Dicer exists throughout eukaryotes, and a subset has 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 helicase domains 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: 350189 [Multi-domain] Cd Length: 142 Bit Score: 66.08 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 288 KRSKLIEILSEQADGT-----IVFVETKRGADFLASFLSEKEFPTTSIHGDRL-------------QSQREQ--ALRDFK 347
Cdd:cd18802 8 KLQKLIEILREYFPKTpdfrgIIFVERRATAVVLSRLLKEHPSTLAFIRCGFLigrgnssqrkrslMTQRKQkeTLDKFR 87
|
90 100 110 120
....*....|....*....|....*....|....*....|...
2DB3_D 348 NGSMKVLIATSVASRGLDIKNIKHVINYDMPSKIDDYVHRIGR 390
Cdd:cd18802 88 DGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
67-395 |
8.00e-12 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 66.84 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 67 IIDNVNKSGYKIPTPIQKCSIP-VISSGRDLMACAQTGSGKTAAFLLPILSKLLEDphelelGRpqVVIVSPTRELAIQI 145
Cdd:COG1204 11 VIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNG------GK--ALYIVPLRALASEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 146 FNEARKFaFESY-LKIGIVYGGtsfRHQNECITRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEAdRMLDmgfseDM 224
Cdd:COG1204 83 YREFKRD-FEELgIKVGVSTGD---YDSDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLID-----DE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 225 RR------IMTHVTMR-PEHQTLMFSATF--PEEIQR-MAGEFLK-NYVFVA--IGIVggacsdVKQTIYEVNKYAKRSK 291
Cdd:COG1204 153 SRgptlevLLARLRRLnPEAQIVALSATIgnAEEIAEwLDAELVKsDWRPVPlnEGVL------YDGVLRFDDGSRRSKD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 292 ----LIEILSEQADGTIVFVETKRGA--------DFLASFLSEKEFPTTSIHGDRLQSQRE------------------- 340
Cdd:COG1204 227 ptlaLALDLLEEGGQVLVFVSSRRDAeslakklaDELKRRLTPEEREELEELAEELLEVSEethtnekladclekgvafh 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2DB3_D 341 -----QALRD-----FKNGSMKVLIATS-------VASRGLDIKNIKHVINYDMPskIDDYVHRIGRTGRVG 395
Cdd:COG1204 307 haglpSELRRlvedaFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIP--VLEFKQMAGRAGRPG 376
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
80-212 |
9.91e-12 |
|
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: 63.43 E-value: 9.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 80 TPIQKCSI-PVISSGRDLMACAQTGSGKTAAFLLPILSKLLEdphelelGRPQVVIVSPTRELAIQIFNEARKFAFESYL 158
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALAT-------SGGKAVYIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
2DB3_D 159 KIGIVYGGTSFRHQNEcitRGCHVVIATPGRlLDFVDRTFIT--FEDTRFVVLDEA 212
Cdd:cd17921 76 NVGLLTGDPSVNKLLL---AEADILVATPEK-LDLLLRNGGErlIQDVRLVVVDEA 127
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
76-395 |
1.39e-11 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 66.66 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 76 YKIPTPIQKCSIPVISSGRDLMACAQTGSGKT-AAFlLPILSKLLEDPHELELGRP-QVVIVSPTRELAIQIF------- 146
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGlRVLYISPLKALANDIErnlrapl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 147 NEARKFAFES--YLKIGIVYGGTSfrhQNE---CITRGCHVVIATPGRLldfvdrtFI---------TFEDTRFVVLDEA 212
Cdd:COG1201 101 EEIGEAAGLPlpEIRVGVRTGDTP---ASErqrQRRRPPHILITTPESL-------ALlltspdareLLRGVRTVIVDEI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 213 -------------------DRMLDmgfsEDMRRIMTHVTMRPehqtlmfsatfPEEIQR--MAGEFLKNYVFVAIGIV-- 269
Cdd:COG1201 171 halagskrgvhlalslerlRALAP----RPLQRIGLSATVGP-----------LEEVARflVGYEDPRPVTIVDAGAGkk 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 270 --------GGACSDVKQTIYEVNKYAKRsKLIEILsEQADGTIVFVETKRGADFLASFLSEK-EFPTTSI---HG--DRl 335
Cdd:COG1201 236 pdlevlvpVEDLIERFPWAGHLWPHLYP-RVLDLI-EAHRTTLVFTNTRSQAERLFQRLNELnPEDALPIaahHGslSR- 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
2DB3_D 336 qSQR---EQALrdfKNGSMKVLIATSVASRGLDIKNIKHVINYDMPSKIDDYVHRIGRTG-RVG 395
Cdd:COG1201 313 -EQRlevEEAL---KAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVG 372
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
103-394 |
1.85e-11 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 66.02 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 103 GSGKTA---AFLLpilsklledpHELELGRPQ-VVIVSPTReLAIQIFNEARKFAFEsyLKIGIVYGGTSfRHQNECITR 178
Cdd:COG0553 270 GLGKTIqalALLL----------ELKERGLARpVLIVAPTS-LVGNWQRELAKFAPG--LRVLVLDGTRE-RAKGANPFE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 179 GCHVVIATpgrlLDFVDRTFITFEDTRF--VVLDEADRM----------------------------------------L 216
Cdd:COG0553 336 DADLVITS----YGLLRRDIELLAAVDWdlVILDEAQHIknpatkrakavralkarhrlaltgtpvenrleelwslldfL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 217 DMG-------FSED------------------------MRR-------------IMTH-VTMRPEHQTL--MFSATFPEE 249
Cdd:COG0553 412 NPGllgslkaFRERfarpiekgdeealerlrrllrpflLRRtkedvlkdlpektEETLyVELTPEQRALyeAVLEYLRRE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 250 IQRMAGEFLKNYVFVAIGIVGGACSDVKQTIYEVNKYAKRS----KLIEILSEQADG---TIVFVETKRGADFLASFLSE 322
Cdd:COG0553 492 LEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGRSakleALLELLEELLAEgekVLVFSQFTDTLDLLEERLEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 323 KEFPTTSIHGDRLQSQREQALRDFKNGS--MKVLIATSVASRGLDIKNIKHVINYDM---PSKID---DYVHRIGRTGRV 394
Cdd:COG0553 572 RGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLwwnPAVEEqaiDRAHRIGQTRDV 651
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
287-389 |
2.11e-11 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. 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: 350180 [Multi-domain] Cd Length: 135 Bit Score: 61.34 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 287 AKRSKLIEILSEQADGT---IVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMK--VLIATSVAS 361
Cdd:cd18793 11 GKLEALLELLEELREPGekvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGG 90
|
90 100 110
....*....|....*....|....*....|....
2DB3_D 362 RGLDIKNIKHVINYDM---PSKID---DYVHRIG 389
Cdd:cd18793 91 VGLNLTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
281-395 |
4.21e-11 |
|
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: 60.30 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 281 YEVNKYAKRSKLI----EILSEQADG-TIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLI 355
Cdd:cd18794 6 YSVRPKDKKDEKLdllkRIKVEHLGGsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIV 85
|
90 100 110 120
....*....|....*....|....*....|....*....|
2DB3_D 356 ATSVASRGLDIKNIKHVINYDMPSKIDDYVHRIGRTGRVG 395
Cdd:cd18794 86 ATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
90-212 |
7.55e-11 |
|
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: 60.68 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 90 ISSGRDLMACAQTGSGKTAAFLLPILSKLLEDPhelelgRPQVVIVSPTRELAIQIFNEARKFAFESYLKIGI-VYGG-T 167
Cdd:cd17923 12 ARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQDQLRSLRELLEQLGLGIRVaTYDGdT 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
2DB3_D 168 SFRHQNECITRGCHVVIATPGRL----LDFVDRTFITFEDTRFVVLDEA 212
Cdd:cd17923 86 PREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
288-399 |
9.78e-11 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; 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. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain] Cd Length: 143 Bit Score: 59.68 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 288 KRSKLIEILSEQADGT--------IVFVETKRGADFLASFLSEKEF---PTTSI-----HGDRLQSQREQ--ALRDFKNG 349
Cdd:cd18801 10 KLEKLEEIVKEHFKKKqegsdtrvIIFSEFRDSAEEIVNFLSKIRPgirATRFIgqasgKSSKGMSQKEQkeVIEQFRKG 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
2DB3_D 350 SMKVLIATSVASRGLDIKNIKHVINYD-MPSKIdDYVHRIGRTGRvGNNGR 399
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR-KRQGR 138
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
298-393 |
4.44e-10 |
|
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: 57.66 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 298 EQADGTIVFVETKRGADFLAS---FLSEKEFPTTSI---HGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDIKNIKH 371
Cdd:cd18796 36 ERHKSTLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDL 115
|
90 100
....*....|....*....|..
2DB3_D 372 VINYDMPSKIDDYVHRIGRTGR 393
Cdd:cd18796 116 VIQIGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
94-212 |
9.80e-10 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 58.05 E-value: 9.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 94 RDLMACAQTGSGKT--AAFLLPILSkllEDPHELELGRPQVVIVSPTRELAIQifnEARKFAFESYLKIGIVYGGT---- 167
Cdd:cd18034 17 RNTIVVLPTGSGKTliAVMLIKEMG---ELNRKEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGEMgvdk 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
2DB3_D 168 -SFRHQNECItRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEA 212
Cdd:cd18034 91 wTKERWKEEL-EKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
93-211 |
4.90e-09 |
|
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: 55.28 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 93 GRDLMACAQTGSGKTAAFLLPILSKLLEDPheleLGRPQVVIVSPTRELAIQIFNEARKFA--FESYLKIGIVYGGTSFR 170
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEP----EKGVQVLYISPLKALINDQERRLEEPLdeIDLEIPVAVRHGDTSQS 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
2DB3_D 171 HQNECITRGCHVVIATPGRL-LDFVDRTFI-TFEDTRFVVLDE 211
Cdd:cd17922 77 EKAKQLKNPPGILITTPESLeLLLVNKKLReLFAGLRYVVVDE 119
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
79-245 |
5.07e-09 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the 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: 350676 [Multi-domain] Cd Length: 180 Bit Score: 55.50 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 79 PTPIQKCSIPVISSG------RDLMACAQTGSGKTAAFLLPILSKLledphelELGRpQVVIVSPTRELAIQIFNEARKF 152
Cdd:cd17918 16 LTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAY-------KNGK-QVAILVPTEILAHQHYEEARKF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 153 AfeSYLKIGIVYGGTSfrhqnECITRGCHVVIATPGRLldFVDRtfiTFEDTRFVVLDEADRMldmgFSEDMRRIMthvT 232
Cdd:cd17918 88 L--PFINVELVTGGTK-----AQILSGISLLVGTHALL--HLDV---KFKNLDLVIVDEQHRF----GVAQREALY---N 148
|
170
....*....|...
2DB3_D 233 MRPEHqTLMFSAT 245
Cdd:cd17918 149 LGATH-FLEATAT 160
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
280-398 |
5.44e-09 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain] Cd Length: 174 Bit Score: 55.39 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 280 IYEVNKYAKRsKLIEILSEQADGTIVFVETKRG---ADFLASFLSEKEFPTTSIHgdrlqSQREQALRDFKNGSMKVLIA 356
Cdd:cd18798 5 VYIEDSDSLE-KLLELVKKLGDGGLIFVSIDYGkeyAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIG 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
2DB3_D 357 TS----VASRGLDI-KNIKHVINYDMPSKidDYVHRIGRTGRVGNNG 398
Cdd:cd18798 79 VAsyygVLVRGIDLpERIKYAIFYGVPVT--TYIQASGRTSRLYAGG 123
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
82-211 |
5.93e-09 |
|
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: 55.83 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 82 IQKCSIP-VISSGRDLMACAQTGSGKTAAFLLPILsKLLEDPHELELGRPQVVIVSPTRELAIQIFNEARkfafESYLKI 160
Cdd:cd18023 5 IQSEVFPdLLYSDKNFVVSAPTGSGKTVLFELAIL-RLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWK----EKFGPL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
2DB3_D 161 GI----VYGGTSFRHQNEciTRGCHVVIATPGRlLDFVDRTFIT----FEDTRFVVLDE 211
Cdd:cd18023 80 GLscaeLTGDTEMDDTFE--IQDADIILTTPEK-WDSMTRRWRDngnlVQLVALVLIDE 135
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
350-393 |
1.11e-08 |
|
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: 51.55 E-value: 1.11e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
2DB3_D 350 SMKVLIATSVASRGLDIKNIKHVINYDMPSKIDDYVHRIGRTGR 393
Cdd:cd18785 22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
73-142 |
2.18e-07 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 53.35 E-value: 2.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2DB3_D 73 KSGYKIPTPIQKCSIPVISSGRDLMACAQTGSGKTAAFLLPILSKL--LEDPHELElGRPQVVIVSPTRELA 142
Cdd:PRK13767 27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELfrLGREGELE-DKVYCLYVSPLRALN 97
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
100-417 |
8.70e-07 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 51.46 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 100 AQTGSGKT-AAFLLPILSKLLEDPHELELGRP----QVVIVSPTRELA--IQ---------IFNE-ARKFAFESYLKIGI 162
Cdd:PRK09751 3 APTGSGKTlAAFLYALDRLFREGGEDTREAHKrktsRILYISPIKALGtdVQrnlqiplkgIADErRRRGETEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 163 VYGGTSFRHQNECITRGCHVVIATPGRL-LDFVDRTFITFEDTRFVVLDEADRM---------------LDMGFSEDMRR 226
Cdd:PRK09751 83 RTGDTPAQERSKLTRNPPDILITTPESLyLMLTSRARETLRGVETVIIDEVHAVagskrgahlalslerLDALLHTSAQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 227 IMTHVTMRPEHQTLMF-------SATFPEEIQRMAgefLKNYVFVA----IGIVGGACSDVKQTIYE--VNKYAKRSKLI 293
Cdd:PRK09751 163 IGLSATVRSASDVAAFlggdrpvTVVNPPAMRHPQ---IRIVVPVAnmddVSSVASGTGEDSHAGREgsIWPYIETGILD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 294 EILSEQAdgTIVFVETKRGADFLASFLSE---------------------------------KEFPTTSIHGDRLQSQR- 339
Cdd:PRK09751 240 EVLRHRS--TIVFTNSRGLAEKLTARLNElyaarlqrspsiavdaahfestsgatsnrvqssDVFIARSHHGSVSKEQRa 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 340 --EQALrdfKNGSMKVLIATSVASRGLDIKNIKHVINYDMPSKIDDYVHRIGRTG-RVGnnGRATSFFDPEKDRaiaaDL 416
Cdd:PRK09751 318 itEQAL---KSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGhQVG--GVSKGLFFPRTRR----DL 388
|
.
2DB3_D 417 V 417
Cdd:PRK09751 389 V 389
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
95-429 |
9.13e-07 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 50.51 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 95 DLMACAQTGSGKTAAFLLpILSKLLEDPHELelgrpQVVIVSPTRELAIQIFNEARK-FAFESYLKIGIVYGGTSFRHQN 173
Cdd:cd09639 1 LLVIEAPTGYGKTEAALL-WALHSLKSQKAD-----RVIIALPTRATINAMYRRAKEaFGETGLYHSSILSSRIKEMGDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 174 ECITRGCH-------------VVIATPGRLLDFVDRTFITFEDTRF------VVLDEADRMLD--MGFSEDMRRIMthvt 232
Cdd:cd09639 75 EEFEHLFPlyihsndtlfldpITVCTIDQVLKSVFGEFGHYEFTLAsianslLIFDEVHFYDEytLALILAVLEVL---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 233 MRPEHQTLMFSATFPEeiqrmageFLKNYvFVAIGIV----GGACSDVKQtiYEVNKYAKRSK----LIEILSEQADG-- 302
Cdd:cd09639 151 KDNDVPILLMSATLPK--------FLKEY-AEKIGYVeenePLDLKPNER--APFIKIESDKVgeisSLERLLEFIKKgg 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 303 -TIVFVETKRGADFLASFLSEK--EFPTTSIHGDRLQSQR----EQALRDFKNGSMKVLIATSVASRGLDiknIKHVINY 375
Cdd:cd09639 220 sVAIIVNTVDRAQEFYQQLKEKgpEEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLD---ISVDVMI 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
2DB3_D 376 DMPSKIDDYVHRIGRTGRVGnngratsffdpEKDRAIAADLVKILEGSGQTVPD 429
Cdd:cd09639 297 TELAPIDSLIQRLGRLHRYG-----------EKNGEEVYIITDAPDGKGQKPYP 339
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
92-250 |
4.80e-06 |
|
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: 46.56 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 92 SGRDLMACAQTGSGKTAAFLLPILSKLLEdphelelGRPQVVIVsPTRELAIQIFNEARKFAfESYLKIGIVYGgtSFRH 171
Cdd:cd18028 16 KGENLLISIPTASGKTLIAEMAMVNTLLE-------GGKALYLV-PLRALASEKYEEFKKLE-EIGLKVGISTG--DYDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 172 QNECITRgCHVVIATPGRlLDFVDRTFITF-EDTRFVVLDEAdRMLDmgfseDMRR------IMTHV-TMRPEHQTLMFS 243
Cdd:cd18028 85 DDEWLGD-YDIIVATYEK-FDSLLRHSPSWlRDVGVVVVDEI-HLIS-----DEERgptlesIVARLrRLNPNTQIIGLS 156
|
....*....
2DB3_D 244 ATF--PEEI 250
Cdd:cd18028 157 ATIgnPDEL 165
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
303-373 |
2.29e-05 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 43.32 E-value: 2.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2DB3_D 303 TIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQRE-QALRDFKNGSMKVLIATSVA--SRGLDIKNIKHVI 373
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGELKPPILVTVDllTTGVDIPEVDNVV 82
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
102-248 |
2.79e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.20 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 102 TGSGKT--AAFLLPILSKLLEDPHelelgrpqVVIVSPTRELAIQIFNEARKFaFESYLKIGIVYGGTSFRHQNEcitrG 179
Cdd:pfam04851 32 TGSGKTltAAKLIARLFKKGPIKK--------VLFLVPRKDLLEQALEEFKKF-LPNYVEIGEIISGDKKDESVD----D 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2DB3_D 180 CHVVIATPGRLLDFVDRTFITFEDTRFVVL--DEADRmldmGFSEDMRRIMTHVtmrpEHQTLM-FSATFPE 248
Cdd:pfam04851 99 NKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHR----SGASSYRNILEYF----KPAFLLgLTATPER 162
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
284-404 |
3.38e-05 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350176 [Multi-domain] Cd Length: 153 Bit Score: 43.78 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 284 NKYAKRSKLIEILsEQADGTIVFVETKrgadFLASFLSEKeFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRG 363
Cdd:cd18789 34 NKLRALEELLKRH-EQGDKIIVFTDNV----EALYRYAKR-LLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEG 107
|
90 100 110 120
....*....|....*....|....*....|....*....|...
2DB3_D 364 LDI--KNIKHVINYDMPSKiDDYVHRIGRTGRVGNNGRATSFF 404
Cdd:cd18789 108 IDLpeANVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
283-406 |
3.80e-05 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 45.86 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 283 VNKYAKRSKLIEILSEQ-ADGTIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVAS 361
Cdd:PRK11057 218 VEKFKPLDQLMRYVQEQrGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFG 297
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
2DB3_D 362 RGLDIKNIKHVINYDMPSKIDDYVHRIGRTGRVGNNGRATSFFDP 406
Cdd:PRK11057 298 MGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDP 342
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
97-214 |
4.16e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 44.04 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 97 MACAQTGSGKTAAFLLPILSKLledphelELGRPQVVIVSPTRELAIQIFNEARKFaFESYLKIGIVYGGTSFRHQNEcI 176
Cdd:cd18035 20 LIVLPTGLGKTIIAILVAADRL-------TKKGGKVLILAPSRPLVEQHAENLKRV-LNIPDKITSLTGEVKPEERAE-R 90
|
90 100 110
....*....|....*....|....*....|....*...
2DB3_D 177 TRGCHVVIATPGRLLDFVDRTFITFEDTRFVVLDEADR 214
Cdd:cd18035 91 WDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
290-396 |
5.22e-05 |
|
C-terminal helicase domain of HrQ family helicases; 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. HrQ 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: 350184 [Multi-domain] Cd Length: 146 Bit Score: 43.01 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 290 SKLIEILSEQADGTIVFVETKRGADFLASF----LSEKEFPTTSIHGDR---LQSQREQALRDFKNGSMKVLIATSVASR 362
Cdd:cd18797 25 ARLFADLVRAGVKTIVFCRSRKLAELLLRYlkarLVEEGPLASKVASYRagyLAEDRREIEAELFNGELLGVVATNALEL 104
|
90 100 110
....*....|....*....|....*....|....
2DB3_D 363 GLDIKNIKHVINYDMPSKIDDYVHRIGRTGRVGN 396
Cdd:cd18797 105 GIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGK 138
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
93-214 |
2.12e-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: 42.03 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 93 GRDLMACAQTGSGKTAAFLLpILSKLLEDPHELELGRpqVVIVSPTRELAIQIFNEARKFAFESYLKIGIVYGGTSFRHQ 172
Cdd:cd17927 17 GKNTIICLPTGSGKTFVAVL-ICEHHLKKFPAGRKGK--VVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENVS 93
|
90 100 110 120
....*....|....*....|....*....|....*....|...
2DB3_D 173 NECITRGCHVVIATPGRLL-DFVDRTFITFEDTRFVVLDEADR 214
Cdd:cd17927 94 VEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
93-187 |
1.43e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 39.77 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 93 GRDLMACAQTGSGKTAAFLLPILSKLLEDPHELELGRpqVVIVSPTRELAIQifnEARKFA--FESYLKIGIVYGGTSFR 170
Cdd:cd18036 17 GKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGR--VVVLVNKVPLVEQ---QLEKFFkyFRKGYKVTGLSGDSSHK 91
|
90
....*....|....*..
2DB3_D 171 HQNECITRGCHVVIATP 187
Cdd:cd18036 92 VSFGQIVKASDVIICTP 108
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
258-393 |
2.01e-03 |
|
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: 38.69 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 258 LKNYVFVAIGIvgGACSDVKQTIYEVNKYAKrskLIEILSEQADG-TIVFVETKRGADFLASFLSEKEFpttsIHGDRLQ 336
Cdd:cd18795 5 LEEYVLGFNGL--GIKLRVDVMNKFDSDIIV---LLKIETVSEGKpVLVFCSSRKECEKTAKDLAGIAF----HHAGLTR 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
2DB3_D 337 SQREQALRDFKNGSMKVLIATSVASRGLD-------IKNIKHVINYDM-PSKIDDYVHRIGRTGR 393
Cdd:cd18795 76 EDRELVEELFREGLIKVLVATSTLAAGVNlpartviIKGTQRYDGKGYrELSPLEYLQMIGRAGR 140
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
293-366 |
4.09e-03 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB 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: 350177 [Multi-domain] Cd Length: 171 Bit Score: 38.00 E-value: 4.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2DB3_D 293 IEILSEQADGTIVFVETKRGADFLASFLSEKEFPTTSIHGDRLQSQREQALRDFKNGSMKVLIATSVASRGLDI 366
Cdd:cd18790 20 IRKRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDL 93
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
93-166 |
4.78e-03 |
|
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: 38.04 E-value: 4.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2DB3_D 93 GRDLMACAQTGSGKTAAFLLPILsKLLEDPhelelGRPQVVIVSPTRELAIQIFNEARKFA--FESYLKIGIVYGG 166
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWAL-KLAARG-----GKRRIIYALPTRATINQMYERIREILgrLDDEDKVLLLHSK 70
|
|
| DEXDc_ComFA |
cd17925 |
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ... |
90-213 |
5.69e-03 |
|
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon protein 1) is part of the complex mediating the binding and uptake of single-stranded DNA. ComFA is required for DNA uptake but not for binding. It 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: 350683 [Multi-domain] Cd Length: 143 Bit Score: 37.28 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DB3_D 90 ISSGRDLMACAQTGSGKTaAFLLPILSKLLEDphelelGRpQVVIVSP----TRELAIQIfnearKFAFESyLKIGIVYG 165
Cdd:cd17925 13 IDAKEDLLVWAVTGAGKT-EMLFPAIAQALRQ------GG-RVAIASPridvCLELAPRL-----KAAFPG-AAIVLLHG 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
2DB3_D 166 GTSFRHQNEcitrgcHVVIATPGRLLDFvDRTFitfedtRFVVLDEAD 213
Cdd:cd17925 79 GSEDQYQRS------PLVIATTHQLLRF-YRAF------DLLIIDEVD 113
|
|
| |
