|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
141-526 |
1.03e-165 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 478.87 E-value: 1.03e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 141 ITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSesfKTGPSpqpesqgsfy 220
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQ---RLDPS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 221 qRKAYPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANV 300
Cdd:COG0513 68 -RPRAPQALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 301 KYLVLDEADRMLDMGFEPQIRHIVedcDMTPVgERQTLMFSATFPADIQHLARDFLSDYIFLSVGRVGSTSENITQKVLY 380
Cdd:COG0513 147 ETLVLDEADRMLDMGFIEDIERIL---KLLPK-ERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 381 VENQDKKSALLDLLSASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVAA 460
Cdd:COG0513 223 VDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAA 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1705_300A 461 RGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFFNSENsniVKGLHEILTEANQEVP 526
Cdd:COG0513 303 RGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDE---RRLLRAIEKLIGQKIE 365
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
144-368 |
2.43e-156 |
|
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: 447.32 E-value: 2.43e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 144 FTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTGPSPQPesqgsFYQRK 223
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVG-----RGRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 224 AYPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYL 303
Cdd:cd17967 77 AYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1705_300A 304 VLDEADRMLDMGFEPQIRHIVEDCDMTPVGERQTLMFSATFPADIQHLARDFLSDYIFLSVGRVG 368
Cdd:cd17967 157 VLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
122-369 |
1.01e-152 |
|
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: 439.09 E-value: 1.01e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 122 FDNYDDIPVDASGKDVPEPITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVL 201
Cdd:cd18051 1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 202 SESFKTGPSPQPESQGSFYQ-RKAYPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLV 280
Cdd:cd18051 81 SQIYEQGPGESLPSESGYYGrRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 281 ATPGRLNDLLERGKISLANVKYLVLDEADRMLDMGFEPQIRHIVEDCDMTPVGERQTLMFSATFPADIQHLARDFLSDYI 360
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYI 240
|
....*....
1705_300A 361 FLSVGRVGS 369
Cdd:cd18051 241 FLAVGRVGS 249
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
95-368 |
4.18e-140 |
|
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: 407.43 E-value: 4.18e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 95 PAPRNEKAeiaIFGVPEdpnfqsSGINFDNYDDIPVDASGKDVPEPITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVP 174
Cdd:cd18052 5 PPPEDEDE---IFATIQ------TGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 175 IVANGRDLKACAQTGSGKTGGFLFPVLSESFKTGpspqpeSQGSFYQRKAYPTAVIMAPTRELATQIFDEAKKFTYRSWV 254
Cdd:cd18052 76 IILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEG------LTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 255 KACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRMLDMGFEPQIRHIVEDCDMTPVGE 334
Cdd:cd18052 150 RPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKED 229
|
250 260 270
....*....|....*....|....*....|....*
1705_300A 335 RQTLMFSATFPADIQHLARDFL-SDYIFLSVGRVG 368
Cdd:cd18052 230 RQTLMFSATFPEEIQRLAAEFLkEDYLFLTVGRVG 264
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
134-553 |
3.13e-123 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 374.88 E-value: 3.13e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 134 GKDVPEPITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESfktgpSPQP 213
Cdd:PTZ00110 122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI-----NAQP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 214 esqgsfYQRKAY-PTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLER 292
Cdd:PTZ00110 197 ------LLRYGDgPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLES 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 293 GKISLANVKYLVLDEADRMLDMGFEPQIRHIVEDcdMTPvgERQTLMFSATFPADIQHLARDFLSDY-IFLSVGRVG-ST 370
Cdd:PTZ00110 271 NVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQ--IRP--DRQTLMWSATWPKEVQSLARDLCKEEpVHVNVGSLDlTA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 371 SENITQKVLYVENQDKKSALLDLLSA--STDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSG 448
Cdd:PTZ00110 347 CHNIKQEVFVVEEHEKRGKLKMLLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTG 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 449 AATLLVATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFFNSENSNIVKGLHEILTEANQEVPSF 528
Cdd:PTZ00110 427 KSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPE 506
|
410 420
....*....|....*....|....*
1705_300A 529 LKDAMMSAPGSRSNSRRGGFGRNNN 553
Cdd:PTZ00110 507 LEKLSNERSNGTERRRWGGYGRFSN 531
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
142-518 |
4.73e-101 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 314.43 E-value: 4.73e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 142 TEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSE----SFKTgpspqpesqg 217
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKldvkRFRV---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 218 sfyQrkayptAVIMAPTRELATQIFDEAKK---FTYRswVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGK 294
Cdd:PRK11776 74 ---Q------ALVLCPTRELADQVAKEIRRlarFIPN--IKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 295 ISLANVKYLVLDEADRMLDMGFEPQIRHIVEDCDmtpvGERQTLMFSATFPADIQHLARDFLSDYIFLSVGRVGSTSEnI 374
Cdd:PRK11776 143 LDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAP----ARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-I 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 375 TQKVLYVENQDKKSALLDLLS----ASTdgltLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAA 450
Cdd:PRK11776 218 EQRFYEVSPDERLPALQRLLLhhqpESC----VVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSC 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1705_300A 451 TLLVATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFFNSENSNIVKGLHEIL 518
Cdd:PRK11776 294 SVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYL 361
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
142-558 |
4.95e-91 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 287.25 E-value: 4.95e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 142 TEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTgpsPQPESQgsfyq 221
Cdd:PRK04837 8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSH---PAPEDR----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 222 RKAYPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVK 301
Cdd:PRK04837 80 KVNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 302 YLVLDEADRMLDMGFEPQIRHIVEDcdMTPVGERQTLMFSATFPADIQHLARDFLSDYIFLSVGRVGSTSENITQKVLYV 381
Cdd:PRK04837 160 VVVLDEADRMFDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 382 ENQDKKSALLDLLSASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVAAR 461
Cdd:PRK04837 238 SNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 462 GLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFFNSEnsnIVKGLHEILTEANQEVP--SFLKDAMMS---- 535
Cdd:PRK04837 318 GLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE---YALNLPAIETYIGHSIPvsKYDSDALLTdlpk 394
|
410 420
....*....|....*....|....*...
1705_300A 536 -----APGSRSNSRRGGFGRNNNRDYRK 558
Cdd:PRK04837 395 plrltRPRTGNGPRRSGAPRNRRRRKRS 422
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
128-558 |
3.11e-90 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 288.22 E-value: 3.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 128 IPVDASGKDVPEPITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKT 207
Cdd:PLN00206 107 LEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 208 gpspqpESQGSFYQRKayPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLN 287
Cdd:PLN00206 187 ------RSGHPSEQRN--PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 288 DLLERGKISLANVKYLVLDEADRMLDMGFEPQIRHIVEDCDMTpvgerQTLMFSATFPADIQHLARDFLSDYIFLSVGRV 367
Cdd:PLN00206 259 DLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAKDIILISIGNP 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 368 GSTSENITQKVLYVENQDKKSALLDLLSASTDGL--TLIFVETKRMADQLTDFL-IMQNFRATAIHGDRTQSERERALAA 444
Cdd:PLN00206 334 NRPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKS 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 445 FRSGAATLLVATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFFNSENSNIVKGLHEILTEANQE 524
Cdd:PLN00206 414 FLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAA 493
|
410 420 430
....*....|....*....|....*....|....
1705_300A 525 VPSFLkdammsapgsrSNSRRGGFGRNNNRDYRK 558
Cdd:PLN00206 494 IPREL-----------ANSRYLGSGRKRKKKRRY 516
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
144-582 |
1.94e-89 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 284.39 E-value: 1.94e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 144 FTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLsesfKTGPSPQPESQGSFYQRk 223
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLL----QHLITRQPHAKGRRPVR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 224 ayptAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYL 303
Cdd:PRK10590 78 ----ALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 304 VLDEADRMLDMGFEPQIRHIVEDCDmtpvGERQTLMFSATFPADIQHLARDFLSDYIFLSVGRVGSTSENITQKVLYVEN 383
Cdd:PRK10590 154 VLDEADRMLDMGFIHDIRRVLAKLP----AKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 384 QDKKSALLDLLSASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVAARGL 463
Cdd:PRK10590 230 KRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 464 DIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFFNSENSNIVKGLHEIL--------TEANQEVPSFLKDAMMS 535
Cdd:PRK10590 310 DIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLkkeipriaIPGYEPDPSIKAEPIQN 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
1705_300A 536 APGSRSNSRRG-GFGRNNNRDYRKAGGASAGGWGSSRSRDNSFRGGSG 582
Cdd:PRK10590 390 GRQQRGGGGRGqGGGRGQQQGQPRRGEGGAKSASAKPAEKPSRRLGDA 437
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
137-508 |
6.16e-87 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 278.33 E-value: 6.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 137 VPEPI---TEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTgPSPQP 213
Cdd:PRK01297 79 VVEPQegkTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQT-PPPKE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 214 ESQGSfyqrkayPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIE-RGCDLLVATPGRLNDLLER 292
Cdd:PRK01297 158 RYMGE-------PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQR 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 293 GKISLANVKYLVLDEADRMLDMGFEPQIRHIVEDCdmTPVGERQTLMFSATFPADIQHLARDFLSDYIFLSVGRVGSTSE 372
Cdd:PRK01297 231 GEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASD 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 373 NITQKVLYVENQDKKSALLDLLSASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATL 452
Cdd:PRK01297 309 TVEQHVYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRV 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
1705_300A 453 LVATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFFNSENS 508
Cdd:PRK01297 389 LVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDA 444
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
153-363 |
1.17e-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: 1.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLS----ESFKTGPSPQpesqgsfyqrkayptA 228
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEkllpEPKKKGRGPQ---------------A 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 229 VIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEA 308
Cdd:cd00268 66 LVLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
1705_300A 309 DRMLDMGFEPQIRHIVedcDMTPvGERQTLMFSATFPADIQHLARDFLSDYIFLS 363
Cdd:cd00268 146 DRMLDMGFEEDVEKIL---SALP-KDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
149-502 |
8.54e-86 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 274.13 E-value: 8.54e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 149 LDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFktgpspqpesqgSFYQRKAYPTA 228
Cdd:PRK11192 8 LDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLL------------DFPRRKSGPPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 229 V-IMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDE 307
Cdd:PRK11192 76 IlILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 308 ADRMLDMGFEPQIRHIVEDCdmtpVGERQTLMFSATFPAD-IQHLARDFLSDYIFLSVGrvGSTSE--NITQKVLYVENQ 384
Cdd:PRK11192 156 ADRMLDMGFAQDIETIAAET----RWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAE--PSRRErkKIHQWYYRADDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 385 DKKSALL-DLLSASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVAARGL 463
Cdd:PRK11192 230 EHKTALLcHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGI 309
|
330 340 350
....*....|....*....|....*....|....*....
1705_300A 464 DIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAF 502
Cdd:PRK11192 310 DIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
153-363 |
3.01e-77 |
|
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: 243.43 E-value: 3.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESfktgpSPQPesqgsFYQRKAYPTAVIMA 232
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI-----NAQP-----PLERGDGPIVLVLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 233 PTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRML 312
Cdd:cd17966 71 PTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRML 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
1705_300A 313 DMGFEPQIRHIVEdcDMTPvgERQTLMFSATFPADIQHLARDFLSDYIFLS 363
Cdd:cd17966 151 DMGFEPQIRKIVD--QIRP--DRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
139-541 |
8.61e-75 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 249.48 E-value: 8.61e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 139 EPITE--FTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFktgpspqpeSQ 216
Cdd:PRK04537 4 KPLTDltFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLL---------SR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 217 GSFYQRKAY-PTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKI 295
Cdd:PRK04537 75 PALADRKPEdPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 296 -SLANVKYLVLDEADRMLDMGFEPQIRHIVEDcdMTPVGERQTLMFSATFPADIQHLARDFLSDYIFLSVGRVGSTSENI 374
Cdd:PRK04537 155 vSLHACEICVLDEADRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 375 TQKVLYVENQDKKSALLDLLSASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLV 454
Cdd:PRK04537 233 RQRIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 455 ATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFfnsENSNIVKGLHEILTEANQEVPSFLKDAMM 534
Cdd:PRK04537 313 ATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF---ACERYAMSLPDIEAYIEQKIPVEPVTAEL 389
|
....*..
1705_300A 535 SAPGSRS 541
Cdd:PRK04537 390 LTPLPRP 396
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
142-502 |
7.74e-69 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 234.74 E-value: 7.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 142 TEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTGPSPQpesqgsfyq 221
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQ--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 222 rkayptAVIMAPTRELATQIFDEAKKFT-YRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANV 300
Cdd:PRK11634 77 ------ILVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 301 KYLVLDEADRMLDMGFEPQIRHIvedcdMTPV-GERQTLMFSATFPADIQHLARDFLSDYIFLSVGRVGSTSENITQKVL 379
Cdd:PRK11634 151 SGLVLDEADEMLRMGFIEDVETI-----MAQIpEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 380 YVENQDKKSALLDLLSASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVA 459
Cdd:PRK11634 226 TVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|...
1705_300A 460 ARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAF 502
Cdd:PRK11634 306 ARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
132-360 |
1.29e-68 |
|
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: 221.87 E-value: 1.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 132 ASGKDVPEPITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSEsFKTGPSP 211
Cdd:cd17953 2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRH-IKDQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 212 QPEsQGsfyqrkayPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLL- 290
Cdd:cd17953 81 KPG-EG--------PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILt 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1705_300A 291 -ERGKI-SLANVKYLVLDEADRMLDMGFEPQIRHIVEdcDMTPvgERQTLMFSATFPADIQHLARDFLSDYI 360
Cdd:cd17953 152 aNNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIVN--NIRP--DRQTVLFSATFPRKVEALARKVLHKPI 219
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
130-365 |
1.21e-66 |
|
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: 217.18 E-value: 1.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 130 VDASGKDVPEPITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESfktgp 209
Cdd:cd18049 12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 210 SPQPesqgsFYQRKAYPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDL 289
Cdd:cd18049 87 NHQP-----FLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1705_300A 290 LERGKISLANVKYLVLDEADRMLDMGFEPQIRHIVEdcDMTPvgERQTLMFSATFPADIQHLARDFLSDYIFLSVG 365
Cdd:cd18049 162 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD--QIRP--DRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
153-360 |
2.93e-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: 212.28 E-value: 2.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESfktgpSPQPEsqgsfYQRKAYPTAVIMA 232
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI-----MDQRE-----LEKGEGPIAVIVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 233 PTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRML 312
Cdd:cd17952 71 PTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMF 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
1705_300A 313 DMGFEPQIRHIVEdcDMTPvgERQTLMFSATFPADIQHLARDFLSDYI 360
Cdd:cd17952 151 DMGFEYQVRSIVG--HVRP--DRQTLLFSATFKKKIEQLARDILSDPI 194
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
149-363 |
4.99e-63 |
|
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: 206.67 E-value: 4.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 149 LDGLLLENIKLARFTKPTPVQKYSV-PIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTGPSPQPESQGsfyqrkaypt 227
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 228 AVIMAPTRELATQIFDEAKKFTYRSW-VKACVVYGGSPIGNQLREIER-GCDLLVATPGRLNDLLE--RGKISLANVKYL 303
Cdd:cd17964 71 ALIISPTRELALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1705_300A 304 VLDEADRMLDMGFEPQIRHIVEDCDMTPVGERQTLMFSATFPADIQHLARDFL-SDYIFLS 363
Cdd:cd17964 151 VLDEADRLLDMGFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLkKDYKFID 211
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
124-533 |
9.13e-63 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 212.38 E-value: 9.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 124 NYDDIpVDAsgkdvpepiteFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLse 203
Cdd:PTZ00424 22 NYDEI-VDS-----------FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 204 sfktgpspqpesqgsfyQRKAYP----TAVIMAPTRELATQIFDEAKKFTYRSWVK--ACVvyGGSPIGNQLREIERGCD 277
Cdd:PTZ00424 88 -----------------QLIDYDlnacQALILAPTRELAQQIQKVVLALGDYLKVRchACV--GGTVVRDDINKLKAGVH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 278 LLVATPGRLNDLLERGKISLANVKYLVLDEADRMLDMGFEPQIRHIVEDcdMTPvgERQTLMFSATFPADIQHLARDFLS 357
Cdd:PTZ00424 149 MVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKK--LPP--DVQVALFSATMPNEILELTTKFMR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 358 DYIFLSVGRVGSTSENITQKVLYVENQDKK-SALLDLLSASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQS 436
Cdd:PTZ00424 225 DPKRILVKKDELTLEGIRQFYVAVEKEEWKfDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 437 ERERALAAFRSGAATLLVATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFFNSENSNIVKGLHE 516
Cdd:PTZ00424 305 DRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
|
410
....*....|....*..
1705_300A 517 ILTEANQEVPSFLKDAM 533
Cdd:PTZ00424 385 HYNTQIEEMPMEVADYL 401
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
134-365 |
1.55e-62 |
|
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: 207.56 E-value: 1.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 134 GKDVPEPITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESfktgpSPQP 213
Cdd:cd18050 54 GVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI-----NHQP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 214 esqgsFYQRKAYPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERG 293
Cdd:cd18050 129 -----YLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAG 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1705_300A 294 KISLANVKYLVLDEADRMLDMGFEPQIRHIVEdcDMTPvgERQTLMFSATFPADIQHLARDFLSDYIFLSVG 365
Cdd:cd18050 204 KTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD--QIRP--DRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
374-503 |
1.83e-62 |
|
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: 202.35 E-value: 1.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 374 ITQKVLYVENQDKKSALL-DLLSASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATL 452
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
1705_300A 453 LVATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFF 503
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
153-358 |
6.72e-59 |
|
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: 195.38 E-value: 6.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESfktgpspqpESQGSFYQRKAYPTAVIMA 232
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHL---------DLQPIPREQRNGPGVLVLT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 233 PTRELATQIFDEAKKFTYRSwVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRML 312
Cdd:cd17958 72 PTRELALQIEAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRML 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
1705_300A 313 DMGFEPQIRHIVedCDMTPvgERQTLMFSATFPADIQHLARDFLSD 358
Cdd:cd17958 151 DMGFEPQIRKIL--LDIRP--DRQTIMTSATWPDGVRRLAQSYLKD 192
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
153-356 |
2.62e-58 |
|
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: 194.85 E-value: 2.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTGPSP-QPESQGsfyqrkayPTAVIM 231
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeETKDDG--------PYALIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 232 APTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRM 311
Cdd:cd17945 73 APTRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1705_300A 312 LDMGFEPQIRHIVEDCDMTPVGE----------------RQTLMFSATFPADIQHLARDFL 356
Cdd:cd17945 153 IDMGFEPQVTKILDAMPVSNKKPdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYL 213
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
153-365 |
4.83e-58 |
|
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: 193.19 E-value: 4.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESfktgpsPQPESQGSFYqrkayptAVIMA 232
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKL------GKPRKKKGLR-------ALILA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 233 PTRELATQIFDEAKKFTYRSWVKACVVYGGS-PIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRM 311
Cdd:cd17957 68 PTRELASQIYRELLKLSKGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
1705_300A 312 LDMGFEPQIRHIVEDCDMTPVgerQTLMFSATFPADIQHLARDFLSDYIFLSVG 365
Cdd:cd17957 148 FEPGFREQTDEILAACTNPNL---QRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
162-353 |
1.05e-54 |
|
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: 184.38 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 162 FTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLsESFKTGPSpqpesqgsfyqRKAYPTAVIMAPTRELATQI 241
Cdd:cd17947 10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPIL-ERLLYRPK-----------KKAATRVLVLVPTRELAMQC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 242 FDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGK-ISLANVKYLVLDEADRMLDMGFEPQI 320
Cdd:cd17947 78 FSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADEL 157
|
170 180 190
....*....|....*....|....*....|...
1705_300A 321 RHIVEDCDMTpvgeRQTLMFSATFPADIQHLAR 353
Cdd:cd17947 158 KEILRLCPRT----RQTMLFSATMTDEVKDLAK 186
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
166-351 |
1.06e-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: 183.21 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 166 TPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTGPSPQpesqgsfyqrkayptAVIMAPTRELATQIFDEA 245
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQ---------------ALVLAPTRELAEQIYEEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 246 KKFTYRSWVKACVVYGGSPIGNQLREIeRGCDLLVATPGRLNDLLERGKiSLANVKYLVLDEADRMLDMGFEPQIRHIVE 325
Cdd:pfam00270 66 KKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILR 143
|
170 180
....*....|....*....|....*.
1705_300A 326 DCDmtpvGERQTLMFSATFPADIQHL 351
Cdd:pfam00270 144 RLP----KKRQILLLSATLPRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
157-377 |
3.17e-53 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 180.38 E-value: 3.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 157 IKLARFTKPTPVQKYSVPIVANG-RDLKACAQTGSGKTGGFLFPVLSesfktgpspqpesqgsFYQRKAYPTAVIMAPTR 235
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALE----------------ALKRGKGGRVLVLVPTR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 236 ELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGC-DLLVATPGRLNDLLERGKISLANVKYLVLDEADRMLDM 314
Cdd:smart00487 65 ELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
1705_300A 315 GFEPQIRHIVEDCDmtpvGERQTLMFSATFPADIQHLARDFLSDYIFLSVGRvgSTSENITQK 377
Cdd:smart00487 145 GFGDQLEKLLKLLP----KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
149-362 |
4.91e-50 |
|
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: 172.14 E-value: 4.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 149 LDGLLLENIKlarftKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFktgpspQPESQGSFYQRKAyPTA 228
Cdd:cd17951 2 LKGLKKKGIK-----KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFAL------EQEKKLPFIKGEG-PYG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 229 VIMAPTRELATQIFDEAKKFTYR------SWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKY 302
Cdd:cd17951 70 LIVCPSRELARQTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 303 LVLDEADRMLDMGFEPQIRHIVEDCDmtpvGERQTLMFSATFPADIQHLARDFLSDYIFL 362
Cdd:cd17951 150 LCLDEADRMIDMGFEEDIRTIFSYFK----GQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
161-363 |
1.38e-47 |
|
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: 165.84 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 161 RFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESfktgpspqpESQGSFYQRKAYPTAVIMAPTRELATQ 240
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRL---------LSLEPRVDRSDGTLALVLVPTRELALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 241 IFDEAKKFT-YRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGK-ISLANVKYLVLDEADRMLDMGFEP 318
Cdd:cd17949 81 IYEVLEKLLkPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
1705_300A 319 QIRHIVE---------DCDMTPVGERQTLMFSATFPADIQHLARDFLSDYIFLS 363
Cdd:cd17949 161 DITKILEllddkrskaGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
153-358 |
3.64e-47 |
|
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: 164.41 E-value: 3.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKtgpSPQPesqgsFYqrkayptAVIMA 232
Cdd:cd17954 11 LCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLE---NPQR-----FF-------ALVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 233 PTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGK-ISLANVKYLVLDEADRM 311
Cdd:cd17954 76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
1705_300A 312 LDMGFEPQIRHIVEdcdMTPvGERQTLMFSATFPADIQHLARDFLSD 358
Cdd:cd17954 156 LNMDFEPEIDKILK---VIP-RERTTYLFSATMTTKVAKLQRASLKN 198
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
144-362 |
6.25e-47 |
|
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: 163.63 E-value: 6.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 144 FTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLsESFKtGPSPQPESQgsfyqrk 223
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMI-EKLK-AHSPTVGAR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 224 ayptAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYL 303
Cdd:cd17959 74 ----ALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
1705_300A 304 VLDEADRMLDMGFEPQIRHIVEDCDMTpvgeRQTLMFSATFPADIQHLARDFLSDYIFL 362
Cdd:cd17959 150 VFDEADRLFEMGFAEQLHEILSRLPEN----RQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
144-363 |
2.31e-45 |
|
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: 159.31 E-value: 2.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 144 FTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLsESFKTGPSpqpesqGSFyqrk 223
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-QRLSEDPY------GIF---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 224 ayptAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLE---RGKISLANV 300
Cdd:cd17955 70 ----ALVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
1705_300A 301 KYLVLDEADRMLDMGFEPQIRHIVEDCdmtPvGERQTLMFSATFPADIQHLARDFLSDYIFLS 363
Cdd:cd17955 146 KFLVLDEADRLLTGSFEDDLATILSAL---P-PKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
153-363 |
2.63e-45 |
|
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: 158.87 E-value: 2.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFktgpspqpesqgsFYQRKayPTAVIMA 232
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL-------------TEHRN--PSALILT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 233 PTRELATQIFDEAKKFTY-RSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRM 311
Cdd:cd17962 66 PTRELAVQIEDQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTM 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
1705_300A 312 LDMGFEPQIRHIVEDCDMTPvgerQTLMFSATFPADIQHLARDFLSDYIFLS 363
Cdd:cd17962 146 LKMGFQQQVLDILENISHDH----QTILVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
160-364 |
8.99e-44 |
|
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: 155.14 E-value: 8.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 160 ARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSesfktgpspqpesqgSFYQRKAYPT----AVIMAPTR 235
Cdd:cd17941 8 AGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLE---------------KLYRERWTPEdglgALIISPTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 236 ELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERgCDLLVATPGR-LNDLLERGKISLANVKYLVLDEADRMLDM 314
Cdd:cd17941 73 ELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRlLQHMDETPGFDTSNLQMLVLDEADRILDM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
1705_300A 315 GFEPQIRHIVEDcdmTPvGERQTLMFSATFPADIQHLARDFLSDYIFLSV 364
Cdd:cd17941 152 GFKETLDAIVEN---LP-KSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
153-356 |
5.42e-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: 150.14 E-value: 5.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTGPSPQpesqgsfyqrkayptAVIMA 232
Cdd:cd17940 10 LLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQ---------------ALILV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 233 PTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRML 312
Cdd:cd17940 75 PTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
1705_300A 313 DMGFEPQIRHIVedcDMTPvGERQTLMFSATFPADIQHLARDFL 356
Cdd:cd17940 155 SQDFQPIIEKIL---NFLP-KERQILLFSATFPLTVKNFMDRHM 194
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
153-356 |
3.45e-41 |
|
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: 148.11 E-value: 3.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTGPSPQpesqgsfyqrKAYPTAVIMA 232
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLK----------KGQVGALIIS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 233 PTRELATQIFDEAKKFTYRSWVK---ACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLER--GKISLANVKYLVLDE 307
Cdd:cd17960 71 PTRELATQIYEVLQSFLEHHLPKlkcQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
1705_300A 308 ADRMLDMGFEPQIRHIVEdcdMTPvGERQTLMFSATFPADIQHLARDFL 356
Cdd:cd17960 151 ADRLLDLGFEADLNRILS---KLP-KQRRTGLFSATQTDAVEELIKAGL 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
385-494 |
1.33e-39 |
|
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: 140.42 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 385 DKKSALLDLLSASTDGLTLIFVETKRMADqLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVAARGLD 464
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
1705_300A 465 IPNVTHVINYDLPSDVDDYVHRIGRTGRAG 494
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
161-344 |
1.72e-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: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 161 RFTKPTPVQKYSVP-IVANGRDLKACAQTGSGKTGGFLFPVLsESFKtgpspQPESQGSFYQRKAYPTAVIMAPTRELAT 239
Cdd:cd17946 9 GFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPIL-ERLL-----SQKSSNGVGGKQKPLRALILTPTRELAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 240 QI---FDEAKKFTYrswVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGK---ISLANVKYLVLDEADRMLD 313
Cdd:cd17946 83 QVkdhLKAIAKYTN---IKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEADRMLE 159
|
170 180 190
....*....|....*....|....*....|....*
1705_300A 314 MG-FEpQIRHIVE---DCDMTPVGERQTLMFSATF 344
Cdd:cd17946 160 KGhFA-ELEKILEllnKDRAGKKRKRQTFVFSATL 193
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
165-352 |
1.02e-36 |
|
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: 135.91 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 165 PTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSesfktgpspqpesqgsfyqrkaYPTAVIMAPTRELATQIFDE 244
Cdd:cd17938 22 PTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ----------------------IVVALILEPSRELAEQTYNC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 245 AKKFTY---RSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRMLDMGFEPQIR 321
Cdd:cd17938 80 IENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETIN 159
|
170 180 190
....*....|....*....|....*....|....
1705_300A 322 HIVEDC-DMTPVGER-QTLMFSATFPA-DIQHLA 352
Cdd:cd17938 160 RIYNRIpKITSDGKRlQVIVCSATLHSfEVKKLA 193
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
154-353 |
1.25e-36 |
|
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: 135.57 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 154 LENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTGpspqpesqgsFYQRKAypTAVI-MA 232
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLK----------FKPRNG--TGVIiIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 233 PTRELATQIFDEAKKF-TYRSWVKACVVyGGSpigNQLREIER---GCDLLVATPGRLNDLLERGK-ISLANVKYLVLDE 307
Cdd:cd17942 70 PTRELALQIYGVAKELlKYHSQTFGIVI-GGA---NRKAEAEKlgkGVNILVATPGRLLDHLQNTKgFLYKNLQCLIIDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
1705_300A 308 ADRMLDMGFEPQIRHIVEdcdMTPvGERQTLMFSATFPADIQHLAR 353
Cdd:cd17942 146 ADRILEIGFEEEMRQIIK---LLP-KRRQTMLFSATQTRKVEDLAR 187
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
167-356 |
5.14e-36 |
|
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: 133.82 E-value: 5.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 167 PVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPvLSESFKTGPSPQpesqgsfyQRKAYPTAVIMAPTRELATQIFDEAK 246
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIP-LIEKLQEDQQPR--------KRGRAPKVLVLAPTRELANQVTKDFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 247 KFTYRSWVkACVvYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRMLDMGFEPQIRHIV-- 324
Cdd:cd17944 86 DITRKLSV-ACF-YGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsv 163
|
170 180 190
....*....|....*....|....*....|....*
1705_300A 325 ---EDCDMTPvgerQTLMFSATFPADIQHLARDFL 356
Cdd:cd17944 164 sykKDSEDNP----QTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
153-358 |
7.64e-35 |
|
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: 130.93 E-value: 7.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSEsfkTGPSPQPESqgsfyqrkayptAVIMA 232
Cdd:cd17950 13 LLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQ---LEPVDGQVS------------VLVIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 233 PTRELATQIFDEAKKFT-YRSWVKACVVYGGSPIGNQLREIERGC-DLLVATPGRLNDLLERGKISLANVKYLVLDEADR 310
Cdd:cd17950 78 HTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
1705_300A 311 M---LDMGfepqiRHIVEDCDMTPVgERQTLMFSATFPADIQHLARDFLSD 358
Cdd:cd17950 158 MleqLDMR-----RDVQEIFRATPH-DKQVMMFSATLSKEIRPVCKKFMQD 202
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
153-358 |
4.13e-34 |
|
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: 128.60 E-value: 4.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYS-VPIVaNGRDLKACAQTGSGKTGGFLFPVLSESFKTGPSPQpesqgsfyqrkayptAVIM 231
Cdd:cd17939 8 LLRGIYAYGFEKPSAIQQRAiVPII-KGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQ---------------ALVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 232 APTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRM 311
Cdd:cd17939 72 APTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
1705_300A 312 LDMGFEPQIRHIVEdcdMTPvGERQTLMFSATFPADIQHLARDFLSD 358
Cdd:cd17939 152 LSRGFKDQIYDIFQ---FLP-PETQVVLFSATMPHEVLEVTKKFMRD 194
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
153-360 |
6.79e-34 |
|
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: 129.02 E-value: 6.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVL-----SESFKTGPSPQPEsqgsfyqrkaypt 227
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIqrllrYKLLAEGPFNAPR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 228 AVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGnQLREIERG-CDLLVATPGRLNDLLERGKISLANVKYLVLD 306
Cdd:cd17948 68 GLVITPSRELAEQIGSVAQSLTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1705_300A 307 EADRMLDMGFEPQIRHIVEDCdmtPVGER------------QTLMFSATFPADiqhlARDFLSDYI 360
Cdd:cd17948 147 EADTLLDDSFNEKLSHFLRRF---PLASRrsentdgldpgtQLVLVSATMPSG----VGEVLSKVI 205
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
149-358 |
1.49e-33 |
|
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: 126.93 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 149 LDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTgpspqpESQGSFYQrkaYPTA 228
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKA------KAESGEEQ---GTRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 229 VIMAPTRELATQIFDEAKKFTY--RSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISL-ANVKYLVL 305
Cdd:cd17961 72 LILVPTRELAQQVSKVLEQLTAycRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
1705_300A 306 DEADRMLDMGFEPQIRHIVedcDMTPVGeRQTLMFSATFPADIQHLARDFLSD 358
Cdd:cd17961 152 DEADLVLSYGYEEDLKSLL---SYLPKN-YQTFLMSATLSEDVEALKKLVLHN 200
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
153-363 |
4.96e-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: 122.37 E-value: 4.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLsESFKtgpspqPESQGsfyqrkayPTAVIMA 232
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL-ESLD------LERRH--------PQVLILA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 233 PTRELATQIFDEAKKF-TYRSWVKACVVYGGSPIGNQLREIeRGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRM 311
Cdd:cd17943 66 PTREIAVQIHDVFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
1705_300A 312 LDMGFEPQIRHIVEdcdMTPVGeRQTLMFSATFPADIQHLARDFLSDYIFLS 363
Cdd:cd17943 145 MEGSFQKDVNWIFS---SLPKN-KQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
149-360 |
8.80e-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: 8.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 149 LDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTGPSPQpesqgsfyqrkayptA 228
Cdd:cd18046 6 LKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQ---------------A 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 229 VIMAPTRELATQIFD--EAKKFTYRSWVKACVvyGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLD 306
Cdd:cd18046 71 LVLAPTRELAQQIQKvvMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLD 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
1705_300A 307 EADRMLDMGFEPQIRHIVEdcdMTPVgERQTLMFSATFPADIQHLARDFLSDYI 360
Cdd:cd18046 149 EADEMLSRGFKDQIYDIFQ---KLPP-DTQVVLLSATMPNDVLEVTTKFMRDPI 198
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
153-362 |
6.80e-31 |
|
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: 119.22 E-value: 6.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIVANG--RDLKACAQTGSGKTGGFLFPVLSESFKTGPSPQpesqgsfyqrkayptAVI 230
Cdd:cd17963 5 LLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQ---------------ALC 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 231 MAPTRELATQIFDEAKKF------TYRSWVKACVVYGGSPIGNQLreiergcdlLVATPGRLNDLLERGKISLANVKYLV 304
Cdd:cd17963 70 LAPTRELARQIGEVVEKMgkftgvKVALAVPGNDVPRGKKITAQI---------VIGTPGTVLDWLKKRQLDLKKIKILV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
1705_300A 305 LDEADRMLDM-GFEPQIRHIV----EDCdmtpvgerQTLMFSATFPADIQHLARDFLSDYIFL 362
Cdd:cd17963 141 LDEADVMLDTqGHGDQSIRIKrmlpRNC--------QILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
413-494 |
3.31e-30 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 113.46 E-value: 3.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 413 DQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGR 492
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
1705_300A 493 AG 494
Cdd:smart00490 81 AG 82
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
144-358 |
2.46e-29 |
|
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: 115.26 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 144 FTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKTGGFLFPVLSESFKTGPSPQpesqgsfyqrk 223
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQ----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 224 ayptAVIMAPTRELATQIFDEA---KKFTYRSwVKACVvyGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANV 300
Cdd:cd18045 70 ----ALILSPTRELAVQIQKVLlalGDYMNVQ-CHACI--GGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
1705_300A 301 KYLVLDEADRMLDMGFEPQIRHIVEdcdMTPVGErQTLMFSATFPADIQHLARDFLSD 358
Cdd:cd18045 143 KMLVLDEADEMLNKGFKEQIYDVYR---YLPPAT-QVVLVSATLPQDILEMTNKFMTD 196
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
153-353 |
7.99e-26 |
|
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: 106.18 E-value: 7.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVP---------IVANGRDLKACAQTGSGKTGGFLFPVLsESFKTGPSPQPEsqgsfyqrk 223
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPwllpsskstPPYRPGDLCVSAPTGSGKTLAYVLPIV-QALSKRVVPRLR--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 224 ayptAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPI---GNQLREIERG-----CDLLVATPGRLNDLLERGK- 294
Cdd:cd17956 71 ----ALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFkkeQKLLLVDTSGrylsrVDILVATPGRLVDHLNSTPg 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1705_300A 295 ISLANVKYLVLDEADRMLDMGF--------EPQIRHIVEDCDMTPVGER--------QTLMFSATFPADIQHLAR 353
Cdd:cd17956 147 FTLKHLRFLVIDEADRLLNQSFqdwletvmKALGRPTAPDLGSFGDANLlersvrplQKLLFSATLTRDPEKLSS 221
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
269-506 |
4.28e-24 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 105.99 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 269 LREIERG-CDLLVATPGRLN-----DLLERGKISLanvkyLVLDEA--------DrmldmgFEP---QIRHIVEDCDMTP 331
Cdd:COG0514 100 LRALRAGeLKLLYVAPERLLnprflELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRERLPNVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 332 VgerqtLMFSATfpAD-------IQHLArdfLSD-YIFL-SVGRvgstsENITQKVLYVENQDKKSALLDLLSASTDGLT 402
Cdd:COG0514 169 V-----LALTAT--ATprvradiAEQLG---LEDpRVFVgSFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPGGSG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 403 LIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATaVA-ARGLDIPNVTHVINYDLPSDVD 481
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIE 312
|
250 260
....*....|....*....|....*
1705_300A 482 DYVHRIGRTGRAGNTGLATAFFNSE 506
Cdd:COG0514 313 AYYQEIGRAGRDGLPAEALLLYGPE 337
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
149-358 |
1.85e-20 |
|
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: 90.90 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 149 LDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLKA----------------CAQTGSGKTGGFLFPVLSeSFKTGPSPQ 212
Cdd:cd17965 15 IKEILKGSNKTDEEIKPSPIQTLAIKKLLKTLMRKVtkqtsneepklevfllAAETGSGKTLAYLAPLLD-YLKRQEQEP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 213 PESQGSFYQ---RKAYPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVV-YGGSPIGNQLRE-IERGCDLLVATPGRLN 287
Cdd:cd17965 94 FEEAEEEYEsakDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFsSGFGPSYQRLQLaFKGRIDILVTTPGKLA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1705_300A 288 DLLERGKISLANVKYLVLDEADRMLDMGFEPQIRHIVEdcDMTPVgeRQTLMFSATFPADIQHLARDFLSD 358
Cdd:cd17965 174 SLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIK--RAPKL--KHLILCSATIPKEFDKTLRKLFPD 240
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
188-472 |
4.07e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 94.32 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 188 TGSGKTGGFLFpvLSESFKTGPspqpesqgsfyqrkaypTAVIMAPTRELATQIFDEAKKFTYRswvkacvvyggspIGN 267
Cdd:COG1061 109 TGTGKTVLALA--LAAELLRGK-----------------RVLVLVPRRELLEQWAEELRRFLGD-------------PLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 268 QLREIERGCDLLVATPGRLNDLLERGKISlANVKYLVLDEA--------DRMLDMgFEPQIRhivedcdmtpvgerqtLM 339
Cdd:COG1061 157 GGGKKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAhhagapsyRRILEA-FPAAYR----------------LG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 340 FSAT------------------FPADIQHLARD-FLSDYIFLSV--------GRVGSTSENITQKVLYvENQDKKSALLD 392
Cdd:COG1061 219 LTATpfrsdgreillflfdgivYEYSLKEAIEDgYLAPPEYYGIrvdltderAEYDALSERLREALAA-DAERKDKILRE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 393 LLSASTDGL-TLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVAARGLDIPNVTHV 471
Cdd:COG1061 298 LLREHPDDRkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVA 377
|
.
1705_300A 472 I 472
Cdd:COG1061 378 I 378
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
386-494 |
4.65e-15 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 78.62 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 386 KKSALLDLLS----ASTDGLTLIFVETKRMADQLTDFLIMQNFRAT------AIHGDR--TQSERERALAAFRSGAATLL 453
Cdd:COG1111 336 KLSKLREILKeqlgTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGEFNVL 415
|
90 100 110 120
....*....|....*....|....*....|....*....|..
1705_300A 454 VATAVAARGLDIPNVTHVINYDL-PSDVdDYVHRIGRTGRAG 494
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGRKR 456
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
130-358 |
5.02e-15 |
|
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: 74.67 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 130 VDASGKDVPEP---ITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANG--RDLKACAQTGSGKTGGFLFPVLSEs 204
Cdd:cd18048 3 VEVLQRDPTSPlfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 205 fktgpspqpesqgsFYQRKAYPTAVIMAPTRELATQ---IFDEAKKFTYRSWVKACVVYGGSPIGNQLREiergcDLLVA 281
Cdd:cd18048 82 --------------VDALKLYPQCLCLSPTFELALQtgkVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEA-----QIVIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 282 TPGRLNDLLERGK-ISLANVKYLVLDEADRMLDM-GFEPQI----RHIVEDCDMtpvgerqtLMFSATFPADIQHLARDF 355
Cdd:cd18048 143 TPGTVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSvrvkRSMPKECQM--------LLFSATFEDSVWAFAERI 214
|
...
1705_300A 356 LSD 358
Cdd:cd18048 215 VPD 217
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
402-495 |
9.57e-14 |
|
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: 68.77 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 402 TLIFVETKRMADQL---------------TDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVAARGLDIP 466
Cdd:cd18802 28 GIIFVERRATAVVLsrllkehpstlafirCGFLIGRGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVP 107
|
90 100
....*....|....*....|....*....
1705_300A 467 NVTHVINYDLPSDVDDYVHRIGRtGRAGN 495
Cdd:cd18802 108 ACNLVIRFDLPKTLRSYIQSRGR-ARAPN 135
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
184-343 |
1.59e-13 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 68.20 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 184 ACAQTGSGKTGGFLFPVLSESFKTGPspqpesqgsfyqrkaypTAVIMAPTRELATQIFDEAKKFtYRSWVKACVVYGGS 263
Cdd:cd00046 6 ITAPTGSGKTLAALLAALLLLLKKGK-----------------KVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 264 PIGNQLREIERGCDLLVATPGRLNDLLER-GKISLANVKYLVLDEADRMLDMGFEPQIRHIVEDCDMTPVGerQTLMFSA 342
Cdd:cd00046 68 SAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNA--QVILLSA 145
|
.
1705_300A 343 T 343
Cdd:cd00046 146 T 146
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
360-494 |
2.48e-13 |
|
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: 67.23 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 360 IFLSVGRVGSTSENITQKVLYVENQDKKSalldllsastdglTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERE 439
Cdd:cd18794 4 LFYSVRPKDKKDEKLDLLKRIKVEHLGGS-------------GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRR 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
1705_300A 440 RALAAFRSGAATLLVATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAG 494
Cdd:cd18794 71 DVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
386-488 |
1.26e-11 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 62.49 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 386 KKSALLDLLS---ASTDGLtLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAAT--LLVATAVAA 460
Cdd:cd18793 12 KLEALLELLEelrEPGEKV-LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGG 90
|
90 100 110
....*....|....*....|....*....|....
1705_300A 461 RGLDIPNVTHVINYDL---PSDVD---DYVHRIG 488
Cdd:cd18793 91 VGLNLTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
403-536 |
6.27e-11 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 65.28 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 403 LIFVETKRMADQLTDFLIMQNFRATAIHG--DR------TQSERERALAAFRSGAATLLVATAVAARGLDIPNVTHVINY 474
Cdd:PRK13766 369 IVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaSKdgdkgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFY 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1705_300A 475 D-LPSDVdDYVHRIGRTGRaGNTG----LAT------AFFNSENS------NIVKGLHEILTEANQEVPSFLKDAMMSA 536
Cdd:PRK13766 449 EpVPSEI-RSIQRKGRTGR-QEEGrvvvLIAkgtrdeAYYWSSRRkekkmkEELKNLKGILNKKLQELDEEQKGEEEEK 525
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
403-490 |
1.80e-10 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 63.71 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 403 LIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAAT--LLVATAVAARGLDIPNVTHVINYDL---P 477
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLwwnP 632
|
90
....*....|....*.
1705_300A 478 SDVD---DYVHRIGRT 490
Cdd:COG0553 633 AVEEqaiDRAHRIGQT 648
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
388-495 |
4.47e-10 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 58.43 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 388 SALLDLLSASTDglTLIFVETKRMADQLTD---FLIMQNFRATAI---HGDRTQSERERALAAFRSGAATLLVATAVAAR 461
Cdd:cd18796 29 AEVIFLLERHKS--TLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGSLSRELREEVEAALKRGDLKVVVATSSLEL 106
|
90 100 110
....*....|....*....|....*....|....
1705_300A 462 GLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGN 495
Cdd:cd18796 107 GIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
402-497 |
5.90e-10 |
|
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: 55.79 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 402 TLIFVETKRMADQLTDFLimqnfrataihgdrtqsereralaafrsgaaTLLVATAVAARGLDIPNVTHVINYDLPSDVD 481
Cdd:cd18785 6 IIVFTNSIEHAEEIASSL-------------------------------EILVATNVLGEGIDVPSLDTVIFFDPPSSAA 54
|
90
....*....|....*.
1705_300A 482 DYVHRIGRTGRAGNTG 497
Cdd:cd18785 55 SYIQRVGRAGRGGKDE 70
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
166-494 |
6.47e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 58.75 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 166 TPVQKYSVP-IVANGRDLKACAQTGSGKTggFL--FPVLSeSFKTGPspqpesqgsfyqrkaypTAVIMAPTRELATQIF 242
Cdd:COG1204 24 YPPQAEALEaGLLEGKNLVVSAPTASGKT--LIaeLAILK-ALLNGG-----------------KALYIVPLRALASEKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 243 DEAKKFtYRSW-VKACVVYGGSPIGnqLREIERgCDLLVATPGRLnDLLERGKIS-LANVKYLVLDEAdrmldmgfepqi 320
Cdd:COG1204 84 REFKRD-FEELgIKVGVSTGDYDSD--DEWLGR-YDILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA------------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 321 rHIVEDcdmtpvGER------------------QTLMFSATFPaDIQHLAR-----DFLSDY--IFLSVGRvgstsenIT 375
Cdd:COG1204 147 -HLIDD------ESRgptlevllarlrrlnpeaQIVALSATIG-NAEEIAEwldaeLVKSDWrpVPLNEGV-------LY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 376 QKVLYV--ENQDKKSALLDLL--SASTDGLTLIFVETKR----MADQLTDFL--------------IMQNFRATAI---- 429
Cdd:COG1204 212 DGVLRFddGSRRSKDPTLALAldLLEEGGQVLVFVSSRRdaesLAKKLADELkrrltpeereeleeLAEELLEVSEetht 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 430 ---------------HGDRTQSERERALAAFRSGAATLLVATAVAARGLDIPnVTHVI--------NYDLPsdVDDYVHR 486
Cdd:COG1204 292 nekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIirdtkrggMVPIP--VLEFKQM 368
|
....*...
1705_300A 487 IGRTGRAG 494
Cdd:COG1204 369 AGRAGRPG 376
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
153-358 |
6.80e-09 |
|
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: 56.27 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 153 LLENIKLARFTKPTPVQKYSVPIV--ANGRDLKACAQTGSGKTGGFLFPVLSEsfkTGPSPQpesqgsfyqrkaYPTAVI 230
Cdd:cd18047 12 LLQGVYAMGFNRPSKIQENALPLMlaEPPQNLIAQSQSGTGKTAAFVLAMLSQ---VEPANK------------YPQCLC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 231 MAPTRELATQ---IFDEAKKFtYRSWVKACVVYGgspignqlREIERGC----DLLVATPGRLNDLLERGK-ISLANVKY 302
Cdd:cd18047 77 LSPTYELALQtgkVIEQMGKF-YPELKLAYAVRG--------NKLERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIKV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
1705_300A 303 LVLDEADRML-DMGFEPQIRHIVEdcdMTPVGeRQTLMFSATFPADIQHLARDFLSD 358
Cdd:cd18047 148 FVLDEADVMIaTQGHQDQSIRIQR---MLPRN-CQMLLFSATFEDSVWKFAQKVVPD 200
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
176-499 |
8.17e-09 |
|
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: 58.69 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 176 VANGRDLKACAQTGSGKTGGFLFPVLsESFKTGPSpqpesqgsfyqrkayPTAVIMAPTRELAtqiFDEAKKFT--YRSW 253
Cdd:COG1205 68 ARAGKNVVIATPTASGKSLAYLLPVL-EALLEDPG---------------ATALYLYPTKALA---RDQLRRLRelAEAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 254 ---VKACVVYGGSPiGNQLREIERGCDLLVATPgrlnDLLERG------KIS--LANVKYLVLDEA-------------- 308
Cdd:COG1205 129 glgVRVATYDGDTP-PEERRWIREHPDIVLTNP----DMLHYGllphhtRWArfFRNLRYVVIDEAhtyrgvfgshvanv 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 309 -DRMldmgfepqiRHIVEDCDMTPvgerQTLMFSATF--PAdiQHLARdfLSDYIFLSVGRVGSTSENITQkVLY----V 381
Cdd:COG1205 204 lRRL---------RRICRHYGSDP----QFILASATIgnPA--EHAER--LTGRPVTVVDEDGSPRGERTF-VLWnpplV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 382 ENQDKKSALL---DLLSAST-DGL-TLIFV----ETKRMADQLTDFLIMQNF--RATAIHGDRTQSEReRAL-AAFRSGA 449
Cdd:COG1205 266 DDGIRRSALAeaaRLLADLVrEGLrTLVFTrsrrGAELLARYARRALREPDLadRVAAYRAGYLPEER-REIeRGLRSGE 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
1705_300A 450 ATLLVAT-AVAArGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLA 499
Cdd:COG1205 345 LLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
403-492 |
1.41e-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: 53.90 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 403 LIFVETKRMADQLTDFL--IMQNFRATAIHGDR--------TQSERERALAAFRSGAATLLVATAVAARGLDIPNVTHVI 472
Cdd:cd18801 34 IIFSEFRDSAEEIVNFLskIRPGIRATRFIGQAsgksskgmSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLII 113
|
90 100
....*....|....*....|
1705_300A 473 NYDLPSDVDDYVHRIGRTGR 492
Cdd:cd18801 114 CYDASPSPIRMIQRMGRTGR 133
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
375-503 |
1.75e-08 |
|
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: 53.79 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 375 TQKVLYVENQDKKSALLDLLSASTDG-LTLIFVETKrmaDQLTDflIMQNFRATAIHGDRTQSERERALAAFRSGAATLL 453
Cdd:cd18789 24 KRRLLAAMNPNKLRALEELLKRHEQGdKIIVFTDNV---EALYR--YAKRLLKPFITGETPQSEREEILQNFREGEYNTL 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
1705_300A 454 VATAVAARGLDIP--NVTHVINYDLPSDvDDYVHRIGRTGRAGNTGLATAFF 503
Cdd:cd18789 99 VVSKVGDEGIDLPeaNVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
170-333 |
1.94e-07 |
|
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: 51.66 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 170 KYSVPIVA---NGRDLKACAQTGSGKTggFLFPVLSESFktgpspqpesqgsFYQRKAYPTA--VIMAPTRELATQIFDE 244
Cdd:cd17927 5 NYQLELAQpalKGKNTIICLPTGSGKT--FVAVLICEHH-------------LKKFPAGRKGkvVFLANKVPLVEQQKEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 245 AKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRL-NDLLERGKISLANVKYLVLDEADRMLDMGFEPQIRHI 323
Cdd:cd17927 70 FRKHFERPGYKVTGLSGDTSENVSVEQIVESSDVIIVTPQILvNDLKSGTIVSLSDFSLLVFDECHNTTKNHPYNEIMFR 149
|
170
....*....|
1705_300A 324 VEDCDMTPVG 333
Cdd:cd17927 150 YLDQKLGSSG 159
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
373-498 |
2.39e-07 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 51.15 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 373 NITQkvLYVENQDKKSALLDLLSASTDGlTLIFVET---KRMADQLTDFLIMQNFRATAIHgdrtqSERERALAAFRSGA 449
Cdd:cd18798 1 NIVD--VYIEDSDSLEKLLELVKKLGDG-GLIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGE 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
1705_300A 450 ATLLVATA----VAARGLDIPN-VTHVINYDLPsdVDDYVHRIGRTGRAGNTGL 498
Cdd:cd18798 73 IDVLIGVAsyygVLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSRLYAGGL 124
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
381-492 |
3.53e-07 |
|
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: 50.32 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 381 VENQDKKSALLDLLS-----ASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVA 455
Cdd:cd18790 4 IEVRPTEGQVDDLLGeirkrVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVG 83
|
90 100 110 120
....*....|....*....|....*....|....*....|..
1705_300A 456 TAVAARGLDIPNVTHVINYD-----LPSDVDDYVHRIGRTGR 492
Cdd:cd18790 84 INLLREGLDLPEVSLVAILDadkegFLRSETSLIQTIGRAAR 125
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
377-475 |
7.74e-07 |
|
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: 49.19 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 377 KVLYVENQDKKSALLDLLSAStdgltlifvetkRMADQLTDflIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVAT 456
Cdd:cd18792 28 QVYYVYPRIEESEKLDLKSIE------------ALAEELKE--LVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVST 93
|
90
....*....|....*....
1705_300A 457 AVAARGLDIPNVTHVINYD 475
Cdd:cd18792 94 TVIEVGIDVPNANTMIIED 112
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
185-308 |
8.02e-07 |
|
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: 49.57 E-value: 8.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 185 CAQTGSGKTggflfpVLSE-----SFKTGPSpqpesqgsfyqrkaypTAVIMAPTRELATQIFDEAKKfTYRSWVKACVV 259
Cdd:cd17921 23 SAPTSSGKT------LIAElailrALATSGG----------------KAVYIAPTRALVNQKEADLRE-RFGPLGKNVGL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
1705_300A 260 YGGSPIGNQLREIErgCDLLVATPGRLNDLLERGKI-SLANVKYLVLDEA 308
Cdd:cd17921 80 LTGDPSVNKLLLAE--ADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
374-504 |
4.45e-06 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 49.71 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 374 ITQKVLYVENQDKKSALldllsastdgltlIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLL 453
Cdd:PRK11057 224 LDQLMRYVQEQRGKSGI-------------IYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIV 290
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
1705_300A 454 VATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFFN 504
Cdd:PRK11057 291 VATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
411-475 |
7.03e-06 |
|
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: 46.57 E-value: 7.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
1705_300A 411 MADQLTDfLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVAARGLDIPNVTHVINYD 475
Cdd:cd18811 50 MYEYLKE-RFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED 113
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
160-214 |
3.86e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 46.63 E-value: 3.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
1705_300A 160 ARFTKPTPVQKYSVPIVANGRDLKACAQTGSGKT-GGFLfPVLSESFKTGPSPQPE 214
Cdd:COG1201 20 ARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFL-PALDELARRPRPGELP 74
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
176-308 |
1.11e-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: 43.34 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 176 VANGRDLKACAQTGSGKTGGFLFPVLSESFKtgpspQPESqgsfyqrkaypTAVIMAPTRELATqifDEAKKFtyRSWVK 255
Cdd:cd17923 12 ARAGRSVVVTTGTASGKSLCYQLPILEALLR-----DPGS-----------RALYLYPTKALAQ---DQLRSL--RELLE 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
1705_300A 256 ACV------VYGG-SPIGNQLREIERGCDLLVATPGRLNDLL----ERGKISLANVKYLVLDEA 308
Cdd:cd17923 71 QLGlgirvaTYDGdTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
402-472 |
1.90e-04 |
|
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: 41.39 E-value: 1.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1705_300A 402 TLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERER-ALAAFRSGAATLLVATAVA--ARGLDIPNVTHVI 472
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLFFGELKPPILVTVDllTTGVDIPEVDNVV 82
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
184-308 |
3.36e-04 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 42.25 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 184 ACAQTGSGKTggfLFPVL---SESFKTGPSPQPESQgsfyqrkayptAVIMAPTRELATQIFDEAKKFTYRSwVKACVVY 260
Cdd:cd18034 21 VVLPTGSGKT---LIAVMlikEMGELNRKEKNPKKR-----------AVFLVPTVPLVAQQAEAIRSHTDLK-VGEYSGE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
1705_300A 261 GGSPIGNQLR--EIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEA 308
Cdd:cd18034 86 MGVDKWTKERwkEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
429-499 |
3.45e-04 |
|
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: 41.18 E-value: 3.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1705_300A 429 IHGDRTQSERERALAAFRSGAATLLVATAVAARGLDIPNV-THVINydlpsDVDDY----VHRI-GRTGRAGNTGLA 499
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNAnTIIIE-----RADKFglaqLYQLrGRVGRSKERAYA 128
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
381-490 |
6.89e-04 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 42.87 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 381 VENQDKKsALLDLLSA---STDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAF-RSGAATLLVAT 456
Cdd:PLN03142 467 VENSGKM-VLLDKLLPklkERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFnKPGSEKFVFLL 545
|
90 100 110 120
....*....|....*....|....*....|....*....|....
1705_300A 457 AVAARGLDIPNVTH--VINYDlpSD----VD----DYVHRIGRT 490
Cdd:PLN03142 546 STRAGGLGINLATAdiVILYD--SDwnpqVDlqaqDRAHRIGQK 587
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
161-193 |
1.61e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 41.41 E-value: 1.61e-03
10 20 30
....*....|....*....|....*....|...
1705_300A 161 RFTKPTPVQKYSVPIVANGRDLKACAQTGSGKT 193
Cdd:PRK13767 29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKT 61
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
164-311 |
1.92e-03 |
|
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: 39.71 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 164 KPTPVQKYSVPIVANG------RDLKACAQTGSGKTGGFLFPvlsesfktgpspqpesqgSFYQRKAYPTAVIMAPTREL 237
Cdd:cd17918 15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGA------------------ALLAYKNGKQVAILVPTEIL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1705_300A 238 ATQIFDEAKKFTyrSWVKACVVYGGSPignqlREIERGCDLLVATPGRLNdLLERGKislaNVKYLVLDEADRM 311
Cdd:cd17918 77 AHQHYEEARKFL--PFINVELVTGGTK-----AQILSGISLLVGTHALLH-LDVKFK----NLDLVIVDEQHRF 138
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
229-310 |
5.44e-03 |
|
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: 38.26 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1705_300A 229 VIMAPTRELATQIFDEAKKFTyrSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRL-NDLLErGKISLANVKYLVLDE 307
Cdd:cd18035 49 LILAPSRPLVEQHAENLKRVL--NIPDKITSLTGEVKPEERAERWDASKIIVATPQVIeNDLLA-GRITLDDVSLLIFDE 125
|
...
1705_300A 308 ADR 310
Cdd:cd18035 126 AHH 128
|
|
| |
