|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
171-550 |
9.41e-165 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 477.72 E-value: 9.41e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 171 FTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLafdkgpaavpVDQDagmgyr 250
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQR----------LDPS------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 251 pRKAYPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANI 330
Cdd:COG0513 68 -RPRAPQALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 331 KFLVLDEADRMLDMGFEPQIRHIVEGADmtsvEERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRVGSTSENITQKVVH 410
Cdd:COG0513 147 ETLVLDEADRMLDMGFIEDIERILKLLP----KERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 411 VEDSEKRSYLLDILHTLPPEgLTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATAVA 490
Cdd:COG0513 223 VDKRDKLELLRRLLRDEDPE-RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVA 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 491 SRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAFFNRNNKGIAKELIELLQ 550
Cdd:COG0513 302 ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIG 361
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
171-398 |
1.25e-155 |
|
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: 446.55 E-value: 1.25e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 171 FTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKGPAAVpvdqdagmGYR 250
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSV--------GRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 251 PRKAYPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANI 330
Cdd:cd17967 74 RRKAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075533 331 KFLVLDEADRMLDMGFEPQIRHIVEGADMTSVEERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRVG 398
Cdd:cd17967 154 KFLVLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
150-399 |
1.36e-144 |
|
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: 419.44 E-value: 1.36e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 150 FEKYDDIPVEVSGGDI-EPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPIL 228
Cdd:cd18051 1 FDKYEDIPVEATGENCpPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 229 SLAFDKGPAAVPVDQdaGMGYRPRKAYPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDL 308
Cdd:cd18051 81 SQIYEQGPGESLPSE--SGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 309 LSATPGRLVDLIDRGRISLANIKFLVLDEADRMLDMGFEPQIRHIVEGADMTSVEERQTLMFSATFPRDIQLLARDFLKD 388
Cdd:cd18051 159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238
|
250
....*....|.
gi 19075533 389 YVFLSVGRVGS 399
Cdd:cd18051 239 YIFLAVGRVGS 249
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
131-398 |
9.52e-131 |
|
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: 384.70 E-value: 9.52e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 131 ERQLFGAVAdgtkvsTGINFEKYDDIPVEVSGGDI-EPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDL 209
Cdd:cd18052 10 EDEIFATIQ------TGINFDKYDEIPVEVTGRNPpPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 210 MACAQTGSGKTAGFLFPILSLAFDKGPAAVPVDQdagmgyrprKAYPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAV 289
Cdd:cd18052 84 MACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSE---------VQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 290 YGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEADRMLDMGFEPQIRHIVEGADMTSVEERQTLM 369
Cdd:cd18052 155 YGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLM 234
|
250 260 270
....*....|....*....|....*....|
gi 19075533 370 FSATFPRDIQLLARDFLK-DYVFLSVGRVG 398
Cdd:cd18052 235 FSATFPEEIQRLAAEFLKeDYLFLTVGRVG 264
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
68-568 |
1.29e-127 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 387.21 E-value: 1.29e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 68 SSNYGGRREYNRGGHYGGGEGR--QNNYRGGREGGYSNGGGYRnnrGFGQWRDGQHVIGAR------NTL----LERQLF 135
Cdd:PTZ00110 18 SNNYNSYGPYPDSSNPYGNYQAnhQDNYGGFRPGYGNYSGGYG---GFGMNSYGSSTLGKRlqpidwKSInlvpFEKNFY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 136 GAVADGTKVSTginfEKYDDIPVE-----VSGGDI-EPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDL 209
Cdd:PTZ00110 95 KEHPEVSALSS----KEVDEIRKEkeitiIAGENVpKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 210 MACAQTGSGKTAGFLFPilslafdkgpAAVPVDQDAGMGYRPRkayPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAV 289
Cdd:PTZ00110 171 IGIAETGSGKTLAFLLP----------AIVHINAQPLLRYGDG---PIVLVLAPTRELAEQIREQCNKFGASSKIRNTVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 290 YGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEADRMLDMGFEPQIRHIVEGADmtsvEERQTLM 369
Cdd:PTZ00110 238 YGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIR----PDRQTLM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 370 FSATFPRDIQLLARDFLKDY-VFLSVGRVG-STSENITQKVVHVEDSEKRSYLLDILHTL-PPEGLTLIFVETKRMADTL 446
Cdd:PTZ00110 314 WSATWPKEVQSLARDLCKEEpVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRImRDGDKILIFVETKKGADFL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 447 TDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGN 526
Cdd:PTZ00110 394 TKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGA 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 19075533 527 TGQAVAFFNRNNKGIAKELIELLQEANQECPSFLIAMARESS 568
Cdd:PTZ00110 474 KGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERS 515
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
169-550 |
3.45e-101 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 315.97 E-value: 3.45e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 169 NEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSlafdkgpaavPVDqdagmg 248
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQ----------KLD------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 249 yrPRKAYPTTLILAPTRELVCQIHEESRKF------------CyrswvrpcavyGGADIRAQIRQIDQGCDLLSATPGRL 316
Cdd:PRK11776 68 --VKRFRVQALVLCPTRELADQVAKEIRRLarfipnikvltlC-----------GGVPMGPQIDSLEHGAHIIVGTPGRI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 317 VDLIDRGRISLANIKFLVLDEADRMLDMGFEPQIRHIVEGADmtsvEERQTLMFSATFPRDIQLLARDFLKDYVFLSVGR 396
Cdd:PRK11776 135 LDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAP----ARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 397 VGSTSEnITQKVVHVEDSEKRSYLLDILHTLPPEGlTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELF 476
Cdd:PRK11776 211 THDLPA-IEQRFYEVSPDERLPALQRLLLHHQPES-CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRF 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075533 477 RSGRTSIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAFFNRNNKGIAKELIELLQ 550
Cdd:PRK11776 289 ANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLG 362
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
171-532 |
9.85e-93 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 294.02 E-value: 9.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 171 FTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKGPAAvpvdqdagMGYR 250
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHA--------KGRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 251 PRKAypttLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANI 330
Cdd:PRK10590 75 PVRA----LILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 331 KFLVLDEADRMLDMGFEPQIRHIVegADMTSveERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRVGSTSENITQKVVH 410
Cdd:PRK10590 151 EILVLDEADRMLDMGFIHDIRRVL--AKLPA--KRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 411 VEDSEKRsyllDILHTLPPEG---LTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVAT 487
Cdd:PRK10590 227 VDKKRKR----ELLSQMIGKGnwqQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVAT 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 19075533 488 AVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVA 532
Cdd:PRK10590 303 DIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALS 347
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
180-393 |
2.41e-86 |
|
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: 267.77 E-value: 2.41e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLafdkgpaavpVDQDAgmgyRPRKAYPTTL 259
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEK----------LLPEP----KKKGRGPQAL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 260 ILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEAD 339
Cdd:cd00268 67 VLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEAD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19075533 340 RMLDMGFEPQIRHIVegaDMTSvEERQTLMFSATFPRDIQLLARDFLKDYVFLS 393
Cdd:cd00268 147 RMLDMGFEEDVEKIL---SALP-KDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
156-561 |
2.60e-86 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 278.98 E-value: 2.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 156 IPVEVSGGDI-EPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDK 234
Cdd:PLN00206 107 LEIHVKGEAVpPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 235 GPAAVPVDQDagmgyrprkayPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPG 314
Cdd:PLN00206 187 RSGHPSEQRN-----------PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 315 RLVDLIDRGRISLANIKFLVLDEADRMLDMGFEPQIRHIVEgadmtSVEERQTLMFSATFPRDIQLLARDFLKDYVFLSV 394
Cdd:PLN00206 256 RLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQ-----ALSQPQVLLFSATVSPEVEKFASSLAKDIILISI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 395 GRVGSTSENITQKVVHVEDSEKRSYLLDIL----HTLPPeglTLIFVETKRMADTLTDYL-LNSNFPATSIHGDRTQRER 469
Cdd:PLN00206 331 GNPNRPNKAVKQLAIWVETKQKKQKLFDILkskqHFKPP---AVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKER 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 470 ERALELFRSGRTSIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAFFNRNNKGIAKELIELL 549
Cdd:PLN00206 408 REVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALL 487
|
410
....*....|..
gi 19075533 550 QEANQECPSFLI 561
Cdd:PLN00206 488 KSSGAAIPRELA 499
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
165-533 |
3.12e-84 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 272.17 E-value: 3.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 165 IEPV---NEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDkgpaaVPV 241
Cdd:PRK01297 80 VEPQegkTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQ-----TPP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 242 DQDAGMGYrprkayPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQID-QGCDLLSATPGRLVDLI 320
Cdd:PRK01297 155 PKERYMGE------PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFN 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 321 DRGRISLANIKFLVLDEADRMLDMGFEPQIRHIVEGADMTSveERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRVGST 400
Cdd:PRK01297 229 QRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRKE--ERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 401 SENITQKVVHVEDSEKRSYLLDILHTLPPEGLtLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGR 480
Cdd:PRK01297 307 SDTVEQHVYAVAGSDKYKLLYNLVTQNPWERV-MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGK 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 19075533 481 TSIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAF 533
Cdd:PRK01297 386 IRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
176-533 |
2.70e-82 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 265.65 E-value: 2.70e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 176 LNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILS--LAFdkgpaavpvdqdagmgyrPRK 253
Cdd:PRK11192 8 LDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQhlLDF------------------PRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 254 --AYPTTLILAPTRELVCQIHEESRKFcyrswvrpcAVYGGADI-----------RAQIRQIDQgcDLLSATPGRLVDLI 320
Cdd:PRK11192 70 ksGPPRILILTPTRELAMQVADQAREL---------AKHTHLDIatitggvaymnHAEVFSENQ--DIVVATPGRLLQYI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 321 DRGRISLANIKFLVLDEADRMLDMGFEPQIRHIvegadmtSVEER---QTLMFSATFP-RDIQLLARDFLKDYVFLSVGr 396
Cdd:PRK11192 139 KEENFDCRAVETLILDEADRMLDMGFAQDIETI-------AAETRwrkQTLLFSATLEgDAVQDFAERLLNDPVEVEAE- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 397 vGSTSE--NITQKVVHVEDSEKRSYLLdiLHTLPPEGLT--LIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERA 472
Cdd:PRK11192 211 -PSRRErkKIHQWYYRADDLEHKTALL--CHLLKQPEVTrsIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEA 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075533 473 LELFRSGRTSIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAF 533
Cdd:PRK11192 288 IKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
171-533 |
9.45e-78 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 253.74 E-value: 9.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 171 FTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILS-LAFDKGPAAVPVDQdagmgy 249
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHyLLSHPAPEDRKVNQ------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 250 rprkayPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLAN 329
Cdd:PRK04837 84 ------PRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 330 IKFLVLDEADRMLDMGFEPQIRHIVEgaDMTSVEERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRVGSTSENITQKVV 409
Cdd:PRK04837 158 IQVVVLDEADRMFDLGFIKDIRWLFR--RMPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 410 HVEDSEKRSYLLDILHTLPPEGlTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATAV 489
Cdd:PRK04837 236 YPSNEEKMRLLQTLIEEEWPDR-AIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 19075533 490 ASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAF 533
Cdd:PRK04837 315 AARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
180-393 |
4.07e-74 |
|
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: 236.11 E-value: 4.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPilslafdkgpAAVPVDQDAgmgYRPRKAYPTTL 259
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLP----------AIVHINAQP---PLERGDGPIVL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 260 ILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEAD 339
Cdd:cd17966 68 VLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19075533 340 RMLDMGFEPQIRHIVEGADmtsvEERQTLMFSATFPRDIQLLARDFLKDYVFLS 393
Cdd:cd17966 148 RMLDMGFEPQIRKIVDQIR----PDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
171-533 |
1.71e-71 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 241.39 E-value: 1.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 171 FTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKgPAAV---PVDqdagm 247
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSR-PALAdrkPED----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 248 gyrprkayPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRI-S 326
Cdd:PRK04537 85 --------PRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 327 LANIKFLVLDEADRMLDMGFEPQIRHIVEgaDMTSVEERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRVGSTSENITQ 406
Cdd:PRK04537 157 LHACEICVLDEADRMFDLGFIKDIRFLLR--RMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 407 KVVHVEDSEKRSYLLDILHTlpPEGL-TLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMV 485
Cdd:PRK04537 235 RIYFPADEEKQTLLLGLLSR--SEGArTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILV 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 19075533 486 ATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAF 533
Cdd:PRK04537 313 ATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
171-533 |
4.71e-70 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 238.98 E-value: 4.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 171 FTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSlafdkgpaavpvdqdagmGYR 250
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLH------------------NLD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 251 PRKAYPTTLILAPTRELVCQIHEESRKFC-YRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLAN 329
Cdd:PRK11634 70 PELKAPQILVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 330 IKFLVLDEADRMLDMGFEPQIRHIvegadMTSV-EERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRVGSTSENITQKV 408
Cdd:PRK11634 150 LSGLVLDEADEMLRMGFIEDVETI-----MAQIpEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 409 VHVEDSEKRSYLLDILHTLPPEGlTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATA 488
Cdd:PRK11634 225 WTVWGMRKNEALVRFLEAEDFDA-AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATD 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 19075533 489 VASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAF 533
Cdd:PRK11634 304 VAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
180-388 |
9.95e-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: 211.50 E-value: 9.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKgPAAVPVDQdagmgyrprkayPTTL 259
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ-RELEKGEG------------PIAV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 260 ILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEAD 339
Cdd:cd17952 68 IVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEAD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19075533 340 RMLDMGFEPQIRHIVEGADmtsvEERQTLMFSATFPRDIQLLARDFLKD 388
Cdd:cd17952 148 RMFDMGFEYQVRSIVGHVR----PDRQTLLFSATFKKKIEQLARDILSD 192
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
166-533 |
1.09e-63 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 215.85 E-value: 1.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 166 EPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLafdkgpaavpVDQDa 245
Cdd:PTZ00424 25 EIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQL----------IDYD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 246 gmgYRPRKAypttLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRI 325
Cdd:PTZ00424 94 ---LNACQA----LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 326 SLANIKFLVLDEADRMLDMGFEPQIRHIVEgadmTSVEERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRVGSTSENIT 405
Cdd:PTZ00424 167 RVDDLKLFILDEADEMLSRGFKGQIYDVFK----KLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 406 QKVVHVEDSE-KRSYLLDILHTLPPEGlTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIM 484
Cdd:PTZ00424 243 QFYVAVEKEEwKFDTLCDLYETLTITQ-AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVL 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 19075533 485 VATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAF 533
Cdd:PTZ00424 322 ITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINF 370
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
404-534 |
3.97e-63 |
|
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: 204.66 E-value: 3.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 404 ITQKVVHVEDSEKRSYLLDILHTLPPEGLTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSI 483
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 19075533 484 MVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAFF 534
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
160-388 |
6.16e-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: 207.61 E-value: 6.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 160 VSGGDI-EPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKGPAA 238
Cdd:cd17953 2 VRGKDCpKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 239 vpvdqdAGMGyrprkayPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVD 318
Cdd:cd17953 82 ------PGEG-------PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMID 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075533 319 LI--DRGRI-SLANIKFLVLDEADRMLDMGFEPQIRHIVegadMTSVEERQTLMFSATFPRDIQLLARDFLKD 388
Cdd:cd17953 149 ILtaNNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIV----NNIRPDRQTVLFSATFPRKVEALARKVLHK 217
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
180-395 |
9.40e-60 |
|
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: 198.20 E-value: 9.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILslafdkgpaavpvdqdAGMGYRPRKAYPTTL 259
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPIL----------------QKLGKPRKKKGLRAL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 260 ILAPTRELVCQIHEESRKFCYRSWVRPCAVYGG-ADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEA 338
Cdd:cd17957 65 ILAPTRELASQIYRELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19075533 339 DRMLDMGFEPQIRHIVEGADMTSVeerQTLMFSATFPRDIQLLARDFLKDYVFLSVG 395
Cdd:cd17957 145 DKLFEPGFREQTDEILAACTNPNL---QRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
180-393 |
5.49e-59 |
|
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: 197.16 E-value: 5.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSlAFDKGPAAVPVDQDAGmgyrprkayPTTL 259
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLV-YISRLPPLDEETKDDG---------PYAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 260 ILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEAD 339
Cdd:cd17945 71 ILAPTRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEAD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 340 RMLDMGFEPQIRHIVE--GADMTSVEE--------------RQTLMFSATFPRDIQLLARDFLKDYVFLS 393
Cdd:cd17945 151 RMIDMGFEPQVTKILDamPVSNKKPDTeeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
166-395 |
1.13e-58 |
|
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: 196.77 E-value: 1.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 166 EPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPilslafdkgpAAVPVDQDA 245
Cdd:cd18049 21 KPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLP----------AIVHINHQP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 246 gmgYRPRKAYPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRI 325
Cdd:cd18049 91 ---FLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 326 SLANIKFLVLDEADRMLDMGFEPQIRHIVEGADmtsvEERQTLMFSATFPRDIQLLARDFLKDYVFLSVG 395
Cdd:cd18049 168 NLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR----PDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
180-387 |
9.21e-57 |
|
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: 190.16 E-value: 9.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLafdkgpaavpvdqdagMGYRPRKaYPTT- 258
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILER----------------LLYRPKK-KAATr 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 259 -LILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGR-ISLANIKFLVLD 336
Cdd:cd17947 64 vLVLVPTRELAMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19075533 337 EADRMLDMGFEPQIRHIVEgadmTSVEERQTLMFSATFPRDIQLLARDFLK 387
Cdd:cd17947 144 EADRMLEEGFADELKEILR----LCPRTRQTMLFSATMTDEVKDLAKLSLN 190
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
180-388 |
1.58e-54 |
|
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: 184.59 E-value: 1.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILsLAFDKGPAAvpvdqdagmgyRPRKAYPTTL 259
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF-IHLDLQPIP-----------REQRNGPGVL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 260 ILAPTRELVCQIHEESRKFCYRSWVRPCaVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEAD 339
Cdd:cd17958 69 VLTPTRELALQIEAECSKYSYKGLKSVC-VYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19075533 340 RMLDMGFEPQIRHIvegadMTSVE-ERQTLMFSATFPRDIQLLARDFLKD 388
Cdd:cd17958 148 RMLDMGFEPQIRKI-----LLDIRpDRQTIMTSATWPDGVRRLAQSYLKD 192
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
166-395 |
5.50e-54 |
|
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: 185.60 E-value: 5.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 166 EPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPilslafdkgpAAVPVDQDA 245
Cdd:cd18050 59 KPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLP----------AIVHINHQP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 246 gmgYRPRKAYPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRI 325
Cdd:cd18050 129 ---YLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 326 SLANIKFLVLDEADRMLDMGFEPQIRHIVEGADmtsvEERQTLMFSATFPRDIQLLARDFLKDYVFLSVG 395
Cdd:cd18050 206 NLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR----PDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
176-393 |
7.15e-54 |
|
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: 183.17 E-value: 7.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 176 LNSHLLQNIKLSGYTQPTPVQKNSI-PIVTSGRDLMACAQTGSGKTAGFLFPILslafdkgpaavpvdQDAGMGYRPRKA 254
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAI--------------QSLLNTKPAGRR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 255 YPT-TLILAPTRELVCQIHEESRKFCY--RSWVRPCAVyGGADIRAQI-RQIDQGCDLLSATPGRLVDLID--RGRISLA 328
Cdd:cd17964 67 SGVsALIISPTRELALQIAAEAKKLLQglRKLRVQSAV-GGTSRRAELnRLRRGRPDILVATPGRLIDHLEnpGVAKAFT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19075533 329 NIKFLVLDEADRMLDMGFEPQIRHIVEGADMTSVEERQTLMFSATFPRDIQLLARDFL-KDYVFLS 393
Cdd:cd17964 146 DLDYLVLDEADRLLDMGFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLkKDYKFID 211
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
193-381 |
9.98e-54 |
|
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: 180.90 E-value: 9.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 193 TPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAfdkgpaavpvdqdagmgyRPRKAYPTTLILAPTRELVCQIH 272
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL------------------DKLDNGPQALVLAPTRELAEQIY 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 273 EESRKFCYRSWVRPCAVYGGADIRAQIRQIdQGCDLLSATPGRLVDLIDRgRISLANIKFLVLDEADRMLDMGFEPQIRH 352
Cdd:pfam00270 63 EELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEE 140
|
170 180
....*....|....*....|....*....
gi 19075533 353 IVEGADmtsvEERQTLMFSATFPRDIQLL 381
Cdd:pfam00270 141 ILRRLP----KKRQILLLSATLPRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
184-407 |
6.70e-53 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 180.38 E-value: 6.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 184 IKLSGYTQPTPVQKNSIPIVTSG-RDLMACAQTGSGKTAGFLFPILSLAFdkgpaavpvdqdagmgyrpRKAYPTTLILA 262
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-------------------RGKGGRVLVLV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 263 PTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGC-DLLSATPGRLVDLIDRGRISLANIKFLVLDEADRM 341
Cdd:smart00487 62 PTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19075533 342 LDMGFEPQIRHIVEGADmtsvEERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRvgSTSENITQK 407
Cdd:smart00487 142 LDGGFGDQLEKLLKLLP----KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
176-393 |
3.34e-49 |
|
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: 170.84 E-value: 3.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 176 LNSHLLQNiklSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSlafDKGPAAVPVDQDAGmgyrprkay 255
Cdd:cd17949 1 LVSHLKSK---MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQ---RLLSLEPRVDRSDG--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 256 PTTLILAPTRELVCQIHEESRKFC-YRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGR-ISLANIKFL 333
Cdd:cd17949 66 TLALVLVPTRELALQIYEVLEKLLkPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075533 334 VLDEADRMLDMGFEPQIRHIVE---------GADMTSVEERQTLMFSATFPRDIQLLARDFLKDYVFLS 393
Cdd:cd17949 146 VLDEADRLLDMGFEKDITKILEllddkrskaGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
180-392 |
6.51e-49 |
|
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: 169.44 E-value: 6.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAfdkgpaavpVDQDAGMGYRPRKAyPTTL 259
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFA---------LEQEKKLPFIKGEG-PYGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 260 ILAPTRELVCQIHEESRKFCYR------SWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFL 333
Cdd:cd17951 71 IVCPSRELARQTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19075533 334 VLDEADRMLDMGFEPQIRHIVEgaDMTSveERQTLMFSATFPRDIQLLARDFLKDYVFL 392
Cdd:cd17951 151 CLDEADRMIDMGFEEDIRTIFS--YFKG--QRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
171-393 |
1.03e-48 |
|
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: 168.94 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 171 FTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPIL-SLAFDK-GPAAvpvdqdagmg 248
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILqRLSEDPyGIFA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 249 yrprkaypttLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLI---DRGRI 325
Cdd:cd17955 71 ----------LVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLrssDDTTK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075533 326 SLANIKFLVLDEADRMLDMGFEPQIRHIVEgadmtSVE-ERQTLMFSATFPRDIQLLARDFLKDYVFLS 393
Cdd:cd17955 141 VLSRVKFLVLDEADRLLTGSFEDDLATILS-----ALPpKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
171-392 |
2.53e-48 |
|
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: 167.87 E-value: 2.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 171 FTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAfdKGPAAVpvdqdagMGYR 250
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--KAHSPT-------VGAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 251 prkayptTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANI 330
Cdd:cd17959 74 -------ALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075533 331 KFLVLDEADRMLDMGFEPQIRHIVEGADmtsvEERQTLMFSATFPRDIQLLARDFLKDYVFL 392
Cdd:cd17959 147 EYVVFDEADRLFEMGFAEQLHEILSRLP----ENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
180-393 |
5.73e-47 |
|
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: 163.87 E-value: 5.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKgpaavpvdqdagmgyrprKAYPTTL 259
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTE------------------HRNPSAL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 260 ILAPTRELVCQIHEESRKFCY-RSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEA 338
Cdd:cd17962 63 ILTPTRELAVQIEDQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19075533 339 DRMLDMGFEPQIRHIVEGADmtsvEERQTLMFSATFPRDIQLLARDFLKDYVFLS 393
Cdd:cd17962 143 DTMLKMGFQQQVLDILENIS----HDHQTILVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
171-390 |
1.31e-45 |
|
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: 160.56 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 171 FTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDkgpaavpvdqdagmgyR 250
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLE----------------N 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 251 PRKAYptTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGR-ISLAN 329
Cdd:cd17954 66 PQRFF--ALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075533 330 IKFLVLDEADRMLDMGFEPQIRHIVEgadmTSVEERQTLMFSATFPRDIQLLARDFLKDYV 390
Cdd:cd17954 144 LKFLVMDEADRLLNMDFEPEIDKILK----VIPRERTTYLFSATMTTKVAKLQRASLKNPV 200
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
176-387 |
2.31e-42 |
|
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: 151.68 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 176 LNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLafdkgpaavpVDqdagmgyrPRKAY 255
Cdd:cd17940 6 LKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEK----------ID--------PKKDV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 256 PTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVL 335
Cdd:cd17940 68 IQALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19075533 336 DEADRMLDMGFEPQIRHIVEgadmTSVEERQTLMFSATFPRDIQLLARDFLK 387
Cdd:cd17940 148 DEADKLLSQDFQPIIEKILN----FLPKERQILLFSATFPLTVKNFMDRHMH 195
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
187-394 |
1.28e-41 |
|
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: 149.36 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 187 SGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKGPAAvpvdqDAGMGyrprkayptTLILAPTRE 266
Cdd:cd17941 8 AGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTP-----EDGLG---------ALIISPTRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 267 LVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQgCDLLSATPGRLVDLIDRG-RISLANIKFLVLDEADRMLDMG 345
Cdd:cd17941 74 LAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19075533 346 FEPQIRHIVEgadmTSVEERQTLMFSATFPRDIQLLARDFLKDYVFLSV 394
Cdd:cd17941 153 FKETLDAIVE----NLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
180-387 |
1.80e-39 |
|
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: 144.69 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIP-IVTSGRDLMACAQTGSGKTAGFLFPIL-SLAfdkgpaavpvDQDAGMGYRPRKAYPT 257
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILeRLL----------SQKSSNGVGGKQKPLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 258 TLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGR---ISLANIKFLV 334
Cdd:cd17946 71 ALILTPTRELAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19075533 335 LDEADRMLDMG-FEpQIRHIVE---GADMTSVEERQTLMFSATFPRDIQLLARDFLK 387
Cdd:cd17946 151 LDEADRMLEKGhFA-ELEKILEllnKDRAGKKRKRQTFVFSATLTLDHQLPLKLNSK 206
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
180-373 |
6.00e-38 |
|
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: 139.38 E-value: 6.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAfdkgpaavpvdqdagmgyrprkaypTTL 259
Cdd:cd17938 10 LIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------------------------VAL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 260 ILAPTRELVCQIHEESRKFCY---RSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLD 336
Cdd:cd17938 65 ILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 19075533 337 EADRMLDMGFEPQIRHIVEGA-DMTSVEER-QTLMFSAT 373
Cdd:cd17938 145 EADRLLSQGNLETINRIYNRIpKITSDGKRlQVIVCSAT 183
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
180-386 |
1.00e-37 |
|
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: 138.86 E-value: 1.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILS-LAFDKgpaavpvdqdagmgYRPRKAYPTT 258
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEiLLKRK--------------ANLKKGQVGA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 259 LILAPTRELVCQIHEESRKFCYRSW--VRPCAVYGGADIRAQIRQID-QGCDLLSATPGRLVDLIDR--GRISLANIKFL 333
Cdd:cd17960 67 LIISPTRELATQIYEVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRkaDKVKVKSLEVL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19075533 334 VLDEADRMLDMGFEPQIRHIvegadMTSV-EERQTLMFSATFPRDIQLLARDFL 386
Cdd:cd17960 147 VLDEADRLLDLGFEADLNRI-----LSKLpKQRRTGLFSATQTDAVEELIKAGL 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
415-525 |
1.17e-37 |
|
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: 135.42 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 415 EKRSYLLDILHTLPPeGLTLIFVETKRMADTltDYLLNS-NFPATSIHGDRTQRERERALELFRSGRTSIMVATAVASRG 493
Cdd:pfam00271 1 EKLEALLELLKKERG-GKVLIFSQTKKTLEA--ELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 19075533 494 LDIPNVTHVINYDLPTDIDDYVHRIGRTGRAG 525
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
176-392 |
1.89e-37 |
|
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: 138.10 E-value: 1.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 176 LNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKgpaavpvDQDAGmgyrpRKAY 255
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKA-------KAESG-----EEQG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 256 PTTLILAPTRELVCQIHEESRKFCY--RSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISL-ANIKF 332
Cdd:cd17961 69 TRALILVPTRELAQQVSKVLEQLTAycRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKY 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075533 333 LVLDEADRMLDMGFEpqirhivegADMTSVEER-----QTLMFSATFPRDIQLLARDFLKDYVFL 392
Cdd:cd17961 149 LVIDEADLVLSYGYE---------EDLKSLLSYlpknyQTFLMSATLSEDVEALKKLVLHNPAIL 204
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
181-387 |
5.78e-37 |
|
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: 136.72 E-value: 5.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 181 LQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDkgpaavpvdqdagMGYRPRKAyPTTLI 260
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYK-------------LKFKPRNG-TGVII 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 261 LAPTRELVCQIHEESRKFC-YRSWVRPCaVYGGADIRAQIRQIDQGCDLLSATPGRLVD-LIDRGRISLANIKFLVLDEA 338
Cdd:cd17942 68 ISPTRELALQIYGVAKELLkYHSQTFGI-VIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19075533 339 DRMLDMGFEPQIRHIVEgadmTSVEERQTLMFSATFPRDIQLLARDFLK 387
Cdd:cd17942 147 DRILEIGFEEEMRQIIK----LLPKRRQTMLFSATQTRKVEDLARISLK 191
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
181-387 |
2.00e-34 |
|
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: 129.58 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 181 LQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSlafdkgpaavpvDQDAGMGYRPRKAYPTTLI 260
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIE------------KLQEDQQPRKRGRAPKVLV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 261 LAPTRELVCQIHEEsrkfcYRSWVRPCAV---YGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDE 337
Cdd:cd17944 70 LAPTRELANQVTKD-----FKDITRKLSVacfYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDE 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19075533 338 ADRMLDMGFEPQIRHIVEGADMTSVEER-QTLMFSATFPRDIQLLARDFLK 387
Cdd:cd17944 145 VDQMLDMGFAEQVEEILSVSYKKDSEDNpQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
176-392 |
4.39e-34 |
|
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: 128.46 E-value: 4.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 176 LNSHLLQNIKLSGYTQPTPVQKNSIPIVTSG--RDLMACAQTGSGKTAGFLFPILSlafdkgpaavPVDqdagmgyrPRK 253
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLS----------RVD--------PTL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 254 AYPTTLILAPTRELVCQIHEESRK---------FCYrswVRPCAVYGGADIRAQIrqidqgcdlLSATPGRLVDLIDRGR 324
Cdd:cd17963 63 KSPQALCLAPTRELARQIGEVVEKmgkftgvkvALA---VPGNDVPRGKKITAQI---------VIGTPGTVLDWLKKRQ 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075533 325 ISLANIKFLVLDEADRMLDM-GFEPQIRHIVEGADMTSveerQTLMFSATFPRDIQLLARDFLKDYVFL 392
Cdd:cd17963 131 LDLKKIKILVLDEADVMLDTqGHGDQSIRIKRMLPRNC----QILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
176-388 |
3.84e-32 |
|
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: 123.61 E-value: 3.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 176 LNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSlafdkgpAAVPVDQDAgmgyrprkay 255
Cdd:cd17950 9 LKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQ-------QLEPVDGQV---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 256 pTTLILAPTRELVCQIHEESRKFC-YRSWVRPCAVYGGADIRAQIRQI-DQGCDLLSATPGRLVDLIDRGRISLANIKFL 333
Cdd:cd17950 72 -SVLVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19075533 334 VLDEADRM---LDMgfepqiRHIVEGADMTSVEERQTLMFSATFPRDIQLLARDFLKD 388
Cdd:cd17950 151 VLDECDKMleqLDM------RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQD 202
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
180-393 |
4.20e-32 |
|
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: 122.76 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTagFLFPILSLafdkgpaavpvdqdagMGYRPRKAYPTTL 259
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKT--LVFVVIAL----------------ESLDLERRHPQVL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 260 ILAPTRELVCQIHEESRKFC-YRSWVRPCAVYGGADIrAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEA 338
Cdd:cd17943 63 ILAPTREIAVQIHDVFKKIGkKLEGLKCEVFIGGTPV-KEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19075533 339 DRMLDMGFEPQIRHIVEGADmtsvEERQTLMFSATFPRD-IQLLARdFLKDYVFLS 393
Cdd:cd17943 142 DKLMEGSFQKDVNWIFSSLP----KNKQVIAFSATYPKNlDNLLAR-YMRKPVLVR 192
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
176-390 |
9.15e-32 |
|
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: 122.17 E-value: 9.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 176 LNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILslafdkgpaavpvdQDAGMGYRPRKAy 255
Cdd:cd18046 6 LKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISIL--------------QQIDTSLKATQA- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 256 pttLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVL 335
Cdd:cd18046 71 ---LVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19075533 336 DEADRMLDMGFEPQIRHIVEGADmtsvEERQTLMFSATFPRDIQLLARDFLKDYV 390
Cdd:cd18046 148 DEADEMLSRGFKDQIYDIFQKLP----PDTQVVLLSATMPNDVLEVTTKFMRDPI 198
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
175-390 |
1.29e-31 |
|
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: 121.66 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 175 PLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLfpILSLafdkgpaavpvdQDAGMGYRPRKA 254
Cdd:cd17939 3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFS--IGAL------------QRIDTTVRETQA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 255 ypttLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLV 334
Cdd:cd17939 69 ----LVLAPTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19075533 335 LDEADRMLDMGFEPQIRHIVEGADmtsvEERQTLMFSATFPRDIQLLARDFLKDYV 390
Cdd:cd17939 145 LDEADEMLSRGFKDQIYDIFQFLP----PETQVVLFSATMPHEVLEVTKKFMRDPV 196
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
171-390 |
1.18e-30 |
|
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: 119.11 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 171 FTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSlAFDkgpaavpvdqdagmgyr 250
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ-CLD----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 251 PRKAYPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANI 330
Cdd:cd18045 63 IQVRETQALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 331 KFLVLDEADRMLDMGFEPQIRHIVEGADMTSveerQTLMFSATFPRDIQLLARDFLKDYV 390
Cdd:cd18045 143 KMLVLDEADEMLNKGFKEQIYDVYRYLPPAT----QVVLVSATLPQDILEMTNKFMTDPI 198
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
444-525 |
5.64e-30 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 112.69 E-value: 5.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 444 DTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGR 523
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 19075533 524 AG 525
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
180-383 |
6.36e-30 |
|
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: 117.85 E-value: 6.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILS-LAFDKGPAAVPVDQdagmgyrprkayPTT 258
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQrLLRYKLLAEGPFNA------------PRG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 259 LILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRaQIRQIDQG-CDLLSATPGRLVDLIDRGRISLANIKFLVLDE 337
Cdd:cd17948 69 LVITPSRELAEQIGSVAQSLTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19075533 338 ADRMLDMGFEPQIRHIVE-------GADMTSVEER--QTLMFSATFPRDI-QLLAR 383
Cdd:cd17948 148 ADTLLDDSFNEKLSHFLRrfplasrRSENTDGLDPgtQLVLVSATMPSGVgEVLSK 203
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
180-383 |
3.98e-29 |
|
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: 115.81 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 180 LLQNIKLSGYTQPTPVQKNSIP---------IVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKgpaAVPvdqdagmgyR 250
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPwllpsskstPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKR---VVP---------R 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 251 PRkayptTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGC--------DLLSATPGRLVDLIDR 322
Cdd:cd17956 69 LR-----ALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDHLNS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075533 323 GR-ISLANIKFLVLDEADRMLDMGF----EPQIRHI--VEGADMTSVEER----------QTLMFSATFPRDIQLLAR 383
Cdd:cd17956 144 TPgFTLKHLRFLVIDEADRLLNQSFqdwlETVMKALgrPTAPDLGSFGDAnllersvrplQKLLFSATLTRDPEKLSS 221
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
293-547 |
6.38e-24 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 105.61 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 293 ADIRAQIRQIDQG-CDLLSATPGRL-----VDLIDRGRISLanikfLVLDEA--------DrmldmgFEP---QIRHIVE 355
Cdd:COG0514 94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 356 gadmtSVEERQTLMFSATFP----RDI--QLLARDflkDYVFL-SVGRvgstsENITQKVVHVEDSEKRSYLLDILHTLP 428
Cdd:COG0514 163 -----RLPNVPVLALTATATprvrADIaeQLGLED---PRVFVgSFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 429 PEGlTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATaVA-SRGLDIPNVTHVINYDL 507
Cdd:COG0514 230 GGS-GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDL 307
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19075533 508 PTDIDDYVHRIGRTGRAGNTGQAVAFFNRNNKGIAKELIE 547
Cdd:COG0514 308 PKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
206-503 |
4.30e-21 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 97.40 E-value: 4.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 206 GRDLMACAQTGSGKTAGFLFPILSLAFDKgpaavpvdqdagmgyrprkaypTTLILAPTRELVCQIHEEsrkfcYRSWVR 285
Cdd:COG1061 100 GGRGLVVAPTGTGKTVLALALAAELLRGK----------------------RVLVLVPRRELLEQWAEE-----LRRFLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 286 PCAVYGGADiraqirqiDQGCDLLSATPGRLVDLIDRGRISlANIKFLVLDEA--------DRMLDMgFEPQIRhivega 357
Cdd:COG1061 153 DPLAGGGKK--------DSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAhhagapsyRRILEA-FPAAYR------ 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 358 dmtsveerqtLMFSATFPRD-------------------IQLLARDFLKDYVFLSV--------GRVGSTSENITQKVVH 410
Cdd:COG1061 217 ----------LGLTATPFRSdgreillflfdgivyeyslKEAIEDGYLAPPEYYGIrvdltderAEYDALSERLREALAA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 411 vEDSEKRSYLLDILHTLPPEGLTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATAVA 490
Cdd:COG1061 287 -DAERKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVL 365
|
330
....*....|...
gi 19075533 491 SRGLDIPNVTHVI 503
Cdd:COG1061 366 NEGVDVPRLDVAI 378
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
158-388 |
1.27e-19 |
|
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: 88.15 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 158 VEVSGGD----IEPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSG--RDLMACAQTGSGKTAGFLFPILSLA 231
Cdd:cd18048 3 VEVLQRDptspLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 232 fdkgpaavpvdqDAgmgyrpRKAYPTTLILAPTRELVCQ---IHEESRKFCYRSWVRpCAVYG-----GADIRAQIrqid 303
Cdd:cd18048 83 ------------DA------LKLYPQCLCLSPTFELALQtgkVVEEMGKFCVGIQVI-YAIRGnrpgkGTDIEAQI---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 304 qgcdlLSATPGRLVDLIDRGR-ISLANIKFLVLDEADRMLDmgfepqirhiVEGADMTSV-------EERQTLMFSATFP 375
Cdd:cd18048 140 -----VIGTPGTVLDWCFKLRlIDVTNISVFVLDEADVMIN----------VQGHSDHSVrvkrsmpKECQMLLFSATFE 204
|
250
....*....|...
gi 19075533 376 RDIQLLARDFLKD 388
Cdd:cd18048 205 DSVWAFAERIVPD 217
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
174-388 |
9.69e-19 |
|
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: 86.28 E-value: 9.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 174 PPLNSHLLQNIKL-----SGYTQPTPVQKNSIPI-----------VTSGRD------LMAcAQTGSGKTAGFLFPILSlA 231
Cdd:cd17965 8 PSVREAIIKEILKgsnktDEEIKPSPIQTLAIKKllktlmrkvtkQTSNEEpklevfLLA-AETGSGKTLAYLAPLLD-Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 232 FDKGPAAVPVDQDAGMGYRPRKAYPTTLILAPTRELVCQIHEESRKFCYRSW--VRPCAVYGGADIRAQIRQIDQGCDLL 309
Cdd:cd17965 86 LKRQEQEPFEEAEEEYESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKlgIKTFSSGFGPSYQRLQLAFKGRIDIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 310 SATPGRLVDLI-DRGRIsLANIKFLVLDEADRMLDMGFEPqirhivegaDMTSVEERQT----LMF-SATFPRDIQLLAR 383
Cdd:cd17965 166 VTTPGKLASLAkSRPKI-LSRVTHLVVDEADTLFDRSFLQ---------DTTSIIKRAPklkhLILcSATIPKEFDKTLR 235
|
....*
gi 19075533 384 DFLKD 388
Cdd:cd17965 236 KLFPD 240
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
420-526 |
2.60e-16 |
|
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: 76.09 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 420 LLDILH---TLPPEGLTLIFVETKRMADTL---------------TDYLLNSNFPATSIHGDRTQRERERALELFRSGRT 481
Cdd:cd18802 12 LIEILReyfPKTPDFRGIIFVERRATAVVLsrllkehpstlafirCGFLIGRGNSSQRKRSLMTQRKQKETLDKFRDGEL 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 19075533 482 SIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRtGRAGN 526
Cdd:cd18802 92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPN 135
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
429-531 |
2.29e-15 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 79.77 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 429 PEGLTLIFVETKRMADTLTDYLLNSNFPAT------SIHGDR--TQRERERALELFRSGRTSIMVATAVASRGLDIPNVT 500
Cdd:COG1111 352 PDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVD 431
|
90 100 110
....*....|....*....|....*....|..
gi 19075533 501 HVINYDL-PTDIdDYVHRIGRTGRaGNTGQAV 531
Cdd:COG1111 432 LVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
401-534 |
7.18e-15 |
|
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: 71.86 E-value: 7.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 401 SENITQKVVHVEDSEKRSYLLDILHTLPPEGLTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGR 480
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 19075533 481 TSIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAFF 534
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
406-519 |
3.48e-12 |
|
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: 64.03 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 406 QKVVHVEDSeKRSYLLDILHTLPPEGL-TLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTS-- 482
Cdd:cd18793 3 PKIEEVVSG-KLEALLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrv 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 19075533 483 IMVATAVASRGLDIPNVTHVINYDL---PTDID---DYVHRIG 519
Cdd:cd18793 82 FLLSTKAGGVGLNLTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
206-373 |
1.86e-11 |
|
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: 62.42 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 206 GRDLMACAQTGSGKTAGFLFPILSLAFDKGPaavpvdqdagmgyrprkaypTTLILAPTRELVCQIHEESRKfcYRSWVR 285
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGK--------------------KVLVLVPTKALALQTAERLRE--LFGPGI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 286 PCAV-YGGADIRAQIRQIDQGCDLLSATPGRLVDLIDR-GRISLANIKFLVLDEADRMLDMGFEPQIRHIVEGADMTSVE 363
Cdd:cd00046 59 RVAVlVGGSSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNA 138
|
170
....*....|
gi 19075533 364 erQTLMFSAT 373
Cdd:cd00046 139 --QVILLSAT 146
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
171-388 |
2.32e-11 |
|
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: 63.59 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 171 FTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSG--RDLMACAQTGSGKTAGFLFPILSlafdkgpaavPVDqdagmg 248
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLS----------QVE------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 249 yrPRKAYPTTLILAPTRELVCQ---IHEESRKFcYRSWVRPCAVYGGADIRAqIRQIDQgcdLLSATPGRLVD-LIDRGR 324
Cdd:cd18047 67 --PANKYPQCLCLSPTYELALQtgkVIEQMGKF-YPELKLAYAVRGNKLERG-QKISEQ---IVIGTPGTVLDwCSKLKF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075533 325 ISLANIKFLVLDEADRML-DMGFEPQI----RHIVEGADMtsveerqtLMFSATFPRDIQLLARDFLKD 388
Cdd:cd18047 140 IDPKKIKVFVLDEADVMIaTQGHQDQSiriqRMLPRNCQM--------LLFSATFEDSVWKFAQKVVPD 200
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
434-531 |
2.73e-11 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 66.82 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 434 LIFVETKRMADTLTDYLLNSNFPA------TSIHGDR--TQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHVINY 505
Cdd:PRK13766 369 IVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFY 448
|
90 100
....*....|....*....|....*..
gi 19075533 506 D-LPTDIdDYVHRIGRTGRaGNTGQAV 531
Cdd:PRK13766 449 EpVPSEI-RSIQRKGRTGR-QEEGRVV 473
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
412-521 |
5.37e-11 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 65.63 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 412 EDSEKRSYLLDILHTLPPEGL-TLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTS--IMVATA 488
Cdd:COG0553 530 GRSAKLEALLELLEELLAEGEkVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLK 609
|
90 100 110
....*....|....*....|....*....|....*....
gi 19075533 489 VASRGLDIPNVTHVINYDL---PTDID---DYVHRIGRT 521
Cdd:COG0553 610 AGGEGLNLTAADHVIHYDLwwnPAVEEqaiDRAHRIGQT 648
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
433-535 |
6.65e-11 |
|
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: 58.48 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 433 TLIFVETKRMADTLTDYLlnsnfpatsihgdrtqrereralelfrsgrtSIMVATAVASRGLDIPNVTHVINYDLPTDID 512
Cdd:cd18785 6 IIVFTNSIEHAEEIASSL-------------------------------EILVATNVLGEGIDVPSLDTVIFFDPPSSAA 54
|
90 100
....*....|....*....|...
gi 19075533 513 DYVHRIGRTGRAGNTGQAVAFFN 535
Cdd:cd18785 55 SYIQRVGRAGRGGKDEGEVILFV 77
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
162-531 |
1.62e-10 |
|
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: 64.09 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 162 GGDIEPVNEFTSPPLNSHLlqniKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSlAFDKGPAAvpv 241
Cdd:COG1205 31 EARYAPWPDWLPPELRAAL----KKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLE-ALLEDPGA--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 242 dqdagmgyrprkaypTTLILAPTRELvcqIHEESRKFcyRSWVRPC------AVYGG---ADIRAQIRqidQGCDLLSAT 312
Cdd:COG1205 103 ---------------TALYLYPTKAL---ARDQLRRL--RELAEALglgvrvATYDGdtpPEERRWIR---EHPDIVLTN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 313 PgrlvDLIDRG------RIS--LANIKFLVLDEAdrmldmgfepqirHI---VEGADMTSVEERqtlmfsatfprdIQLL 381
Cdd:COG1205 160 P----DMLHYGllphhtRWArfFRNLRYVVIDEA-------------HTyrgVFGSHVANVLRR------------LRRI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 382 ARDFLKD--YVFLS--VGRVGSTSENIT-QKVVHVEDS--------------------EKRSYLL---DILHTLPPEGL- 432
Cdd:COG1205 211 CRHYGSDpqFILASatIGNPAEHAERLTgRPVTVVDEDgsprgertfvlwnpplvddgIRRSALAeaaRLLADLVREGLr 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 433 TLIFVETKRMADTLTDYL---LNSNFPATSI---HGDRTQREReRALE-LFRSGRTSIMVATAVASRGLDIPNVTHVINY 505
Cdd:COG1205 291 TLVFTRSRRGAELLARYArraLREPDLADRVaayRAGYLPEER-REIErGLRSGELLGVVSTNALELGIDIGGLDAVVLA 369
|
410 420
....*....|....*....|....*.
gi 19075533 506 DLPTDIDDYVHRIGRTGRAGNTGQAV 531
Cdd:COG1205 370 GYPGTRASFWQQAGRAGRRGQDSLVV 395
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
179-525 |
1.76e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 63.76 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 179 HLLQNIKLSGYTQPTPVQKNSIP-IVTSGRDLMACAQTGSGKTA-GFLFpILSLAFDKGPAavpvdqdagmgyrprkayp 256
Cdd:COG1204 10 KVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLiAELA-ILKALLNGGKA------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 257 ttLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAqiRQIDQgCDLLSATPGRLVDLIDRGRISLANIKFLVLD 336
Cdd:COG1204 70 --LYIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDD--EWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 337 EAdrmldmgfepqirHIVEGAD------------MTSVEERQTLMFSATF--PRDI-QLLARDFLK-DY--VFLSVGRvg 398
Cdd:COG1204 145 EA-------------HLIDDESrgptlevllarlRRLNPEAQIVALSATIgnAEEIaEWLDAELVKsDWrpVPLNEGV-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 399 stsenITQKVVHVEDSEKRS--YLLD-ILHTLPPEGLTLIFVETKR----MADTLTDYLLNS---------NFPATSI-- 460
Cdd:COG1204 210 -----LYDGVLRFDDGSRRSkdPTLAlALDLLEEGGQVLVFVSSRRdaesLAKKLADELKRRltpeereelEELAEELle 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 461 ----------------------HGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPnVTHVI------NYDLPTDID 512
Cdd:COG1204 285 vseethtnekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIirdtkrGGMVPIPVL 363
|
410
....*....|...
gi 19075533 513 DYVHRIGRTGRAG 525
Cdd:COG1204 364 EFKQMAGRAGRPG 376
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
465-523 |
2.04e-08 |
|
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: 53.51 E-value: 2.04e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 465 TQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHVINYD-LPTDIdDYVHRIGRTGR 523
Cdd:cd18801 75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
433-526 |
3.48e-07 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 49.96 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 433 TLIFVETKRMADTLTDYLLN---SNFPATSI---HG--DRTQRER-ERALelfRSGRTSIMVATAVASRGLDIPNVTHVI 503
Cdd:cd18796 41 TLVFTNTRSQAERLAQRLRElcpDRVPPDFIalhHGslSRELREEvEAAL---KRGDLKVVVATSSLELGIDIGDVDLVI 117
|
90 100
....*....|....*....|...
gi 19075533 504 NYDLPTDIDDYVHRIGRTGRAGN 526
Cdd:cd18796 118 QIGSPKSVARLLQRLGRSGHRPG 140
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
434-535 |
8.48e-07 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 52.02 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 434 LIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHVINYDLPTDIDD 513
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
90 100
....*....|....*....|..
gi 19075533 514 YVHRIGRTGRAGNTGQAVAFFN 535
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLFYD 341
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
433-503 |
1.00e-06 |
|
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: 47.94 E-value: 1.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075533 433 TLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERER-ALELFRSGRTSIMVATAVA--SRGLDIPNVTHVI 503
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLFFGELKPPILVTVDllTTGVDIPEVDNVV 82
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
208-525 |
1.76e-06 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 50.53 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 208 DLMACAQTGSGKT-AGFLF---PILSLAFDKGPAAVPVDQDA-GMGYRPRKAYPTTLILAPTRELVCQIHEESRKfcyRS 282
Cdd:TIGR01587 1 LLVIEAPTGYGKTeAALLWalhSIKSQKADRVIIALPTRATInAMYRRAKELFGSELVGLHHSSSFSRIKEMGDS---EE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 283 WVRPCAVYGGADIRA-----QIRQIDQGcdLLSATPGRLVDLIDRGRISLANIkflVLDEADrmldmGFEPQIRHIVEGA 357
Cdd:TIGR01587 78 FEHLFPLYIHSNDKLfldpiTVCTIDQV--LKSVFGEFGHYEFTLASIANSLL---IFDEVH-----FYDEYTLALILAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 358 DMTSVEERQTLM-FSATFPRDIQLLARDFlkDYVFLSVGRVGSTSENITQKVVHVEDSEKR---SYLLDILHTLPPEGLT 433
Cdd:TIGR01587 148 LEVLKDNDVPILlMSATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILIESDKVgeiSSLERLLEFIKKGGSI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 434 LIFVETKRMADTLTDYL--LNSNFPATSIHG-----DRTQRERERALELFRSGRTSIMVATAVASRGLDIpNVTHVINYD 506
Cdd:TIGR01587 226 AIIVNTVDRAQEFYQQLkeKAPEEEIILYHSrftekDRAKKEAELLREMKKSNEKFVIVATQVIEASLDI-SADVMITEL 304
|
330
....*....|....*....
gi 19075533 507 LPtdIDDYVHRIGRTGRAG 525
Cdd:TIGR01587 305 AP--IDSLIQRLGRLHRYG 321
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
433-534 |
1.30e-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: 45.70 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 433 TLIFVETKrmaDTLTDYLLNSNFPAtsIHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIP--NVTHVINYDLPTD 510
Cdd:cd18789 52 IIVFTDNV---EALYRYAKRLLKPF--ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPeaNVAIQISGHGGSR 126
|
90 100
....*....|....*....|....
gi 19075533 511 iDDYVHRIGRTGRAGNTGQAVAFF 534
Cdd:cd18789 127 -RQEAQRLGRILRPKKGGGKNAFF 149
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
460-533 |
1.51e-05 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 45.41 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 460 IHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHVINYD-----LPTdiddyVHRI-GRTGRAGNtgQAVAF 533
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDaerfgLSQ-----LHQLrGRVGRGDH--QSYCL 139
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
433-506 |
1.72e-05 |
|
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: 45.70 E-value: 1.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075533 433 TLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHVINYD 506
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
189-547 |
2.09e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 47.79 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 189 YTQPTPVQKNSIPIVTSGRDLMACAQTGSGKT-AGFLFPILSLAfdkgpaavpvdQDAGMGYRPRKAYptTLILAPTREL 267
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDELA-----------RRPRPGELPDGLR--VLYISPLKAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 268 VCQIH-------EEsrkfcyrswVRPCAVYGGADIRAQIR-----------QIDQGCDLLSATPGRLVDLI--DRGRISL 327
Cdd:COG1201 89 ANDIErnlraplEE---------IGEAAGLPLPEIRVGVRtgdtpaserqrQRRRPPHILITTPESLALLLtsPDARELL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 328 ANIKFLVLDE----AD--R--MLDMGFEpQIRHIVeGADMtsveerQTLMFSATFpRDIQLLARdFLkdyvflsVGRVGs 399
Cdd:COG1201 160 RGVRTVIVDEihalAGskRgvHLALSLE-RLRALA-PRPL------QRIGLSATV-GPLEEVAR-FL-------VGYED- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 400 tseniTQKVVHVEDSEKRSYLLDIL-------HTLPPEGL------------------TLIFVETKRMADTLTdYLLNSN 454
Cdd:COG1201 222 -----PRPVTIVDAGAGKKPDLEVLvpvedliERFPWAGHlwphlyprvldlieahrtTLVFTNTRSQAERLF-QRLNEL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 455 FPATSI-----HG--DRTQRER-ERALelfRSGRTSIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTG-RAG 525
Cdd:COG1201 296 NPEDALpiaahHGslSREQRLEvEEAL---KAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVG 372
|
410 420
....*....|....*....|...
gi 19075533 526 NTGQAVAF-FNRNnkgiakELIE 547
Cdd:COG1201 373 EVSKGRLVpTHRD------ELVE 389
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
460-534 |
3.06e-05 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain] Cd Length: 160 Bit Score: 44.57 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 460 IHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHVInydlptdIDD-------YVHRI-GRTGRAGNtgQAV 531
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMI-------IEDadrfglsQLHQLrGRVGRGKH--QSY 136
|
...
gi 19075533 532 AFF 534
Cdd:cd18792 137 CYL 139
|
|
| uvrb |
TIGR00631 |
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ... |
433-502 |
4.31e-05 |
|
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273185 [Multi-domain] Cd Length: 655 Bit Score: 46.52 E-value: 4.31e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 433 TLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHV 502
Cdd:TIGR00631 445 VLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLV 514
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
420-533 |
1.05e-04 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members 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: 350178 [Multi-domain] Cd Length: 171 Bit Score: 43.29 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 420 LLDILHTLPPEGLTLIFV----ETKRMADTLTDYLLNSNFPATSI---HGDRTQRERERALELFRSGRTSIMVATAVASR 492
Cdd:cd18791 33 LILQIHRTEEPGDILVFLpgqeEIERLCELLREELLSPDLGKLLVlplHSSLPPEEQQRVFEPPPPGVRKVVLATNIAET 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 19075533 493 GLDIPNVTHVI--------NYDLPTDIDDYV-HRIG------RTGRAGNTGQAVAF 533
Cdd:cd18791 113 SITIPGVVYVIdsglvkekVYDPRTGLSSLVtVWISkasaeqRAGRAGRTRPGKCY 168
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
206-340 |
1.65e-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: 43.19 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 206 GRDLMACAQTGSGKTagflFPILSLA---FDKGPAAvpvdqdagmgyrpRKAYptTLILAPTRELVCQIHEESRKFCYRS 282
Cdd:cd17927 17 GKNTIICLPTGSGKT----FVAVLICehhLKKFPAG-------------RKGK--VVFLANKVPLVEQQKEVFRKHFERP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 19075533 283 WVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRI-SLANIKFLVLDEADR 340
Cdd:cd17927 78 GYKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDECHN 136
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
196-338 |
1.83e-04 |
|
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: 42.57 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 196 QKNSIPIVTSGRDLMACAQTGSGKTAGFLFPIL-SLAFDKGPAAvpvdqdagmgyrprkaypttLILAPT---------- 264
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeALLRDPGSRA--------------------LYLYPTkalaqdqlrs 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 265 -RELVCQIHEESRkfcyrswvrpCAVYGG-ADIRAQIRQIDQGCDLLSATPGRLVDLI----DRGRISLANIKFLVLDEA 338
Cdd:cd17923 65 lRELLEQLGLGIR----------VATYDGdTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
208-525 |
1.84e-04 |
|
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: 43.96 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 208 DLMACAQTGSGKT-AGFLFPILSLA---FDKGPAAVPVDQDAGMGYRPRKAypttliLAPTRELVCQIHEESRKFCYRS- 282
Cdd:cd09639 1 LLVIEAPTGYGKTeAALLWALHSLKsqkADRVIIALPTRATINAMYRRAKE------AFGETGLYHSSILSSRIKEMGDs 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 283 --WVRPCAVYGGADIRA-----QIRQIDQGcdLLSATPGRLVDLIDRGRISLANIkflVLDEADrmldmGFEPQIRHIVE 355
Cdd:cd09639 75 eeFEHLFPLYIHSNDTLfldpiTVCTIDQV--LKSVFGEFGHYEFTLASIANSLL---IFDEVH-----FYDEYTLALIL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 356 GADMTSVEERQTLM-FSATFPRDIQLLARDFlkDYVFLSVGRVgsTSENITQKVVHVEDS--EKRSYLLDILHTLPPEGL 432
Cdd:cd09639 145 AVLEVLKDNDVPILlMSATLPKFLKEYAEKI--GYVEENEPLD--LKPNERAPFIKIESDkvGEISSLERLLEFIKKGGS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 433 TLIFVETKRMADTLTDYLLNSN--FPATSIHG-----DRTQRERERALELFRSGRtSIMVATAVASRGLDIpNVTHVINY 505
Cdd:cd09639 221 VAIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSrftekDRAKKEAELLLEFKKSEK-FVIVATQVIEASLDI-SVDVMITE 298
|
330 340
....*....|....*....|
gi 19075533 506 DLPtdIDDYVHRIGRTGRAG 525
Cdd:cd09639 299 LAP--IDSLIQRLGRLHRYG 316
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
247-340 |
5.59e-04 |
|
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: 41.35 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 247 MGYRPRKAYPTTLILAPTRELVCQiHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQgCDLLSATPGRLVDLIDRGRIS 326
Cdd:cd18035 37 AADRLTKKGGKVLILAPSRPLVEQ-HAENLKRVLNIPDKITSLTGEVKPEERAERWDA-SKIIVATPQVIENDLLAGRIT 114
|
90
....*....|....
gi 19075533 327 LANIKFLVLDEADR 340
Cdd:cd18035 115 LDDVSLLIFDEAHH 128
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
192-380 |
6.37e-04 |
|
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: 41.25 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 192 PTPVQKNSIPIVTSG------RDLMACAQTGSGKTAGFLFPILsLAFDKGpaavpvdqdagmgyrprkayPTTLILAPTR 265
Cdd:cd17918 16 LTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAAL-LAYKNG--------------------KQVAILVPTE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 266 ELVCQIHEESRKfcYRSWVRPCAVYGGADiraqiRQIDQGCDLLSATPGrlvdLIDRGRISLaNIKFLVLDEADRMldmg 345
Cdd:cd17918 75 ILAHQHYEEARK--FLPFINVELVTGGTK-----AQILSGISLLVGTHA----LLHLDVKFK-NLDLVIVDEQHRF---- 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 19075533 346 fepqirHIVEGADMTSVEERQTLMFSAT-FPRDIQL 380
Cdd:cd17918 139 ------GVAQREALYNLGATHFLEATATpIPRTLAL 168
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
464-531 |
8.57e-04 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350191 [Multi-domain] Cd Length: 238 Bit Score: 41.46 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 464 RTQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHV--INYDLPTDIDDY---------VHRI-GRTGRAGNTGQAV 531
Cdd:cd18804 128 RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADSGLNSPDFraserafqlLTQVsGRAGRGDKPGKVI 207
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
202-338 |
8.89e-04 |
|
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: 40.71 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 202 IVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKGPAAVpvdqdagmgYrprkaypttliLAPTRELVCQIHEESRKfCYR 281
Cdd:cd17921 13 LYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAV---------Y-----------IAPTRALVNQKEADLRE-RFG 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 19075533 282 SWVRPCAVYGGaDIRAQIRQIDQgCDLLSATPGRLVDLIDRGRI-SLANIKFLVLDEA 338
Cdd:cd17921 72 PLGKNVGLLTG-DPSVNKLLLAE-ADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
189-224 |
1.56e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 41.80 E-value: 1.56e-03
10 20 30
....*....|....*....|....*....|....*..
gi 19075533 189 YTQPTPVQKNSIPIVTSGRDLMACAQTGSGKT-AGFL 224
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL 66
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
327-496 |
3.37e-03 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 40.45 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 327 LANiKFLVLDEADrMLDMGFEPQIRHIVEGADM--TSVeerqTLMfSATFPRDIqllaRDFLKDYVFLSVGRVGSTSENI 404
Cdd:COG1203 267 LAN-SVIILDEVQ-AYPPYMLALLLRLLEWLKNlgGSV----ILM-TATLPPLL----REELLEAYELIPDEPEELPEYF 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 405 TQKVVH--------VEDSEKRSYLLDILHTlppEGLTLIFVETKRMADTLTD-----------YLLNSNFPAtsihGDRT 465
Cdd:COG1203 336 RAFVRKrvelkegpLSDEELAELILEALHK---GKSVLVIVNTVKDAQELYEalkeklpdeevYLLHSRFCP----ADRS 408
|
170 180 190
....*....|....*....|....*....|.
gi 19075533 466 QRERErALELFRSGRTSIMVATAVASRGLDI 496
Cdd:COG1203 409 EIEKE-IKERLERGKPCILVSTQVVEAGVDI 438
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
460-534 |
6.54e-03 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350197 [Multi-domain] Cd Length: 151 Bit Score: 37.71 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075533 460 IHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNV-THVINydlptDIDDY----VHRI-GRTGRAGNtgQAVAF 533
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNAnTIIIE-----RADKFglaqLYQLrGRVGRSKE--RAYAY 129
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.
gi 19075533 534 F 534
Cdd:cd18810 130 F 130
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| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
460-500 |
7.32e-03 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 39.36 E-value: 7.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 19075533 460 IHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNVT 500
Cdd:PRK10917 511 LHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNAT 551
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