|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
336-705 |
2.16e-161 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 473.48 E-value: 2.16e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 336 MRKWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYItrlppisEENEAEGPY 415
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-------DPSRPRAPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 416 AVVMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDE 495
Cdd:COG0513 74 ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 496 ADRMIDMGFEPQVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVVTIGTAGKATDLI 575
Cdd:COG0513 154 ADRMLDMGFIEDIERILKLLPKE-----------------RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 576 TQNVIMVKESEKMPRLQKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLV 655
Cdd:COG0513 217 EQRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLV 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 670360632 656 ATDVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSFLT 705
Cdd:COG0513 297 ATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT 346
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
348-564 |
6.94e-145 |
|
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: 423.27 E-value: 6.94e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPISEENEAEGPYAVVMAPTRELAQ 427
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 428 QIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQ 507
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 508 VVGVLDAMPSSNLKPENED---EELDEKRIYRTTYMFSATMPPAVERLARKYLRNPVVVT 564
Cdd:cd17945 161 VTKILDAMPVSNKKPDTEEaekLAASGKHRYRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
329-730 |
7.01e-111 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 347.53 E-value: 7.01e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 329 GSRIPRPMRKWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPIsee 408
Cdd:PTZ00110 122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLL--- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 409 NEAEGPYAVVMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQC 488
Cdd:PTZ00110 199 RYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 489 NYVVLDEADRMIDMGFEPQVVGVLdampsSNLKPEnedeeldekriyRTTYMFSATMPPAVERLARKYLRN-PVVVTIGT 567
Cdd:PTZ00110 279 TYLVLDEADRMLDMGFEPQIRKIV-----SQIRPD------------RQTLMWSATWPKEVQSLARDLCKEePVHVNVGS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 568 AG-KATDLITQNVIMVKESEKMPRLQKILTDLGDKTA--IVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLD 644
Cdd:PTZ00110 342 LDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGDkiLIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLN 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 645 GFRNRRFNVLVATDVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSFLTLENTDIFFDLKQMLIQSNS 724
Cdd:PTZ00110 422 EFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQ 501
|
....*.
gi 670360632 725 PVPPEL 730
Cdd:PTZ00110 502 PVPPEL 507
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
335-703 |
9.81e-100 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 315.59 E-value: 9.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 335 PMRKWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYI--TRLppiseeneae 412
Cdd:PRK11776 2 SMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLdvKRF---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 413 GPYAVVMAPTRELAQQIEEETVKFATYL-GIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYV 491
Cdd:PRK11776 72 RVQALVLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 492 VLDEADRMIDMGFEPQVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVVTIGTAGKA 571
Cdd:PRK11776 152 VLDEADRMLDMGFQDAIDAIIRQAPAR-----------------RQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 572 TDlITQNVIMVKESEKMPRLQKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRF 651
Cdd:PRK11776 215 PA-IEQRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSC 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 670360632 652 NVLVATDVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSF 703
Cdd:PRK11776 294 SVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSL 345
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
348-564 |
3.12e-88 |
|
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: 275.86 E-value: 3.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRlppiSEENEAEGPYAVVMAPTRELAQ 427
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLP----EPKKKGRGPQALVLAPTRELAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 428 QIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQ 507
Cdd:cd00268 77 QIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEED 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 670360632 508 VVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVVT 564
Cdd:cd00268 157 VEKILSALPKD-----------------RQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
311-752 |
2.50e-86 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 282.45 E-value: 2.50e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 311 MTERDWRIFREDFNISYKGSRIPRPMRKWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAA 390
Cdd:PLN00206 95 LSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTAS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 391 FVLPMLSYITRLPPiSEENEAEGPYAVVMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIAT 470
Cdd:PLN00206 175 FLVPIISRCCTIRS-GHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 471 PGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQVVGVLDAMPSSNLkpenedeeldekriyrttYMFSATMPPAVE 550
Cdd:PLN00206 254 PGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQPQV------------------LLFSATVSPEVE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 551 RLARKYLRNPVVVTIGTAGKATDLITQNVIMVKESEKMPRLQKILTDLGDKT--AIVFCNTKKTADMRAKDLDK-SGFRV 627
Cdd:PLN00206 316 KFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLANAITVvTGLKA 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 628 TTLHGGKSQDQREISLDGFRNRRFNVLVATDVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSFLTLE 707
Cdd:PLN00206 396 LSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 670360632 708 NTDIFFDLKQMLIQSNSPVPPELARHEASkfkpGSIPDRPPRRND 752
Cdd:PLN00206 476 DRNLFPELVALLKSSGAAIPRELANSRYL----GSGRKRKKKRRY 516
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
339-703 |
2.53e-85 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 276.82 E-value: 2.53e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 339 WSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPpiseeNEAEGPYAV- 417
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFP-----RRKSGPPRIl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 418 VMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQG--FKIRQgcEIVIATPGRLLDCLERRYAVLNQCNYVVLDE 495
Cdd:PRK11192 78 ILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAevFSENQ--DIVVATPGRLLQYIKEENFDCRAVETLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 496 ADRMIDMGFEpQVVGVLDAmpssnlkpenedeeldEKRIYRTTYMFSATMP-PAVERLARKYLRNPVVVTIGTAGKATDL 574
Cdd:PRK11192 156 ADRMLDMGFA-QDIETIAA----------------ETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 575 ITQNVIMVKESE-KMPRLQKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNV 653
Cdd:PRK11192 219 IHQWYYRADDLEhKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNV 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 670360632 654 LVATDVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSF 703
Cdd:PRK11192 299 LVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
316-704 |
3.32e-84 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 275.25 E-value: 3.32e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 316 WRIfrEDFNISykgsriPRPMR-KWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLP 394
Cdd:PRK01297 73 WKL--EDFVVE------PQEGKtRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLIS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 395 MLSYITRLPPISEENEAEgPYAVVMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIR-QGCEIVIATPGR 473
Cdd:PRK01297 145 IINQLLQTPPPKERYMGE-PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGR 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 474 LLDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQVVGVLDAMPssnlkPENEdeeldekriyRTTYMFSATMPPAVERLA 553
Cdd:PRK01297 224 LLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTP-----RKEE----------RQTLLFSATFTDDVMNLA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 554 RKYLRNPVVVTIGTAGKATDLITQNVIMVKESEKMPRLQKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGG 633
Cdd:PRK01297 289 KQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGD 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 670360632 634 KSQDQREISLDGFRNRRFNVLVATDVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSFL 704
Cdd:PRK01297 369 VPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFA 439
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
344-719 |
1.46e-83 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 272.84 E-value: 1.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 344 LGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPiseenEAEG--PY-AVVMA 420
Cdd:PRK10590 8 LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQP-----HAKGrrPVrALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 421 PTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDcLERRYAV-LNQCNYVVLDEADRM 499
Cdd:PRK10590 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVkLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 500 IDMGFEPQVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVVTIGTAGKATDLITQNV 579
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAK-----------------RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 580 IMVKESEKMPRLQKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVATDV 659
Cdd:PRK10590 225 HFVDKKRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDI 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 660 AGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSFLTLENTDIFFDLKQML 719
Cdd:PRK10590 305 AARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL 364
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
328-564 |
1.35e-81 |
|
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: 259.62 E-value: 1.35e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 328 KGSRIPRPMRKWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPISE 407
Cdd:cd17953 3 RGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 408 EneaEGPYAVVMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCL---ERRYAV 484
Cdd:cd17953 83 G---EGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 485 LNQCNYVVLDEADRMIDMGFEPQVVGVLDampssNLKPEnedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVVT 564
Cdd:cd17953 160 LRRVTYVVLDEADRMFDMGFEPQIMKIVN-----NIRPD------------RQTVLFSATFPRKVEALARKVLHKPIEIT 222
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
340-569 |
6.34e-79 |
|
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: 252.41 E-value: 6.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 340 SESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPISE---ENEAEgPYA 416
Cdd:cd17967 3 EEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgrgRRKAY-PSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 417 VVMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEA 496
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 670360632 497 DRMIDMGFEPQVVGVLDAMPSsnlkPENEDeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVVTIGTAG 569
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHPDM----PPKGE---------RQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
338-703 |
2.43e-77 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 255.28 E-value: 2.43e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 338 KWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRlPPISEENEAEGPYAV 417
Cdd:PRK04837 9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLS-HPAPEDRKVNQPRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 418 VMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEAD 497
Cdd:PRK04837 88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 498 RMIDMGFEPQVVGVLDAMPSSNlkpenedeeldekriYRTTYMFSATMPPAVERLARKYLRNPVVVTIGTAGKATDLITQ 577
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMPPAN---------------QRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 578 NVIMVKESEKMPRLQKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVAT 657
Cdd:PRK04837 233 ELFYPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVAT 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 670360632 658 DVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSF 703
Cdd:PRK04837 313 DVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
344-704 |
4.80e-74 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 252.46 E-value: 4.80e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 344 LGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYItrlppiseENEAEGPYAVVMAPTR 423
Cdd:PRK11634 13 LKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--------DPELKAPQILVLAPTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 424 ELAQQIEEETVKFATYL-GIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDM 502
Cdd:PRK11634 85 ELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 503 GFEPQVVGVLDAMPSSNlkpenedeeldekriyrTTYMFSATMPPAVERLARKYLRNPVVVTIGTAGKATDLITQNVIMV 582
Cdd:PRK11634 165 GFIEDVETIMAQIPEGH-----------------QTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 583 KESEKMPRLQKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVATDVAGR 662
Cdd:PRK11634 228 WGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAAR 307
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 670360632 663 GIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSFL 704
Cdd:PRK11634 308 GLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFV 349
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
343-710 |
2.95e-73 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 243.97 E-value: 2.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 343 KLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYItrlppiseENEAEGPYAVVMAPT 422
Cdd:PTZ00424 34 KLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI--------DYDLNACQALILAPT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 423 RELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDM 502
Cdd:PTZ00424 106 RELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 503 GFEPQVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVVTIGTAGKATDLITQNVIMV 582
Cdd:PTZ00424 186 GFKGQIYDVFKKLPPD-----------------VQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 583 -KESEKMPRLQKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVATDVAG 661
Cdd:PTZ00424 249 eKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLA 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 670360632 662 RGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSFLTLENTD 710
Cdd:PTZ00424 329 RGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIE 377
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
339-703 |
2.30e-71 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 243.70 E-value: 2.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 339 WSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPISEENeAEGPYAVV 418
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRK-PEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 419 MAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAV-LNQCNYVVLDEAD 497
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVsLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 498 RMIDMGFEPQVVGVLDAMPssnlkpenedeeldeKRIYRTTYMFSATMPPAVERLARKYLRNPVVVTIGTAGKATDLITQ 577
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMP---------------ERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 578 NVIMVKESEKMPRLQKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVAT 657
Cdd:PRK04537 235 RIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVAT 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 670360632 658 DVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSF 703
Cdd:PRK04537 315 DVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
348-564 |
9.68e-71 |
|
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: 229.99 E-value: 9.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPISEEneaEGPYAVVMAPTRELAQ 427
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKG---EGPIAVIVAPTRELAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 428 QIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQ 507
Cdd:cd17952 78 QIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 670360632 508 VVGVLDampssNLKPEnedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVVT 564
Cdd:cd17952 158 VRSIVG-----HVRPD------------RQTLLFSATFKKKIEQLARDILSDPIRVV 197
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
329-569 |
9.78e-69 |
|
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: 227.16 E-value: 9.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 329 GSRIPRPMRKWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSY-ITRLPPISE 407
Cdd:cd18052 35 GRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGmMKEGLTASS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 408 ENEAEGPYAVVMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQ 487
Cdd:cd18052 115 FSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 488 CNYVVLDEADRMIDMGFEPQVVGVLDA--MPSSNlkpenedeeldekriYRTTYMFSATMPPAVERLARKYLR-NPVVVT 564
Cdd:cd18052 195 LKYLILDEADRMLDMGFGPEIRKLVSEpgMPSKE---------------DRQTLMFSATFPEEIQRLAAEFLKeDYLFLT 259
|
....*
gi 670360632 565 IGTAG 569
Cdd:cd18052 260 VGRVG 264
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
339-563 |
2.25e-65 |
|
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: 215.64 E-value: 2.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 339 WSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPiseeneaeGPYAVV 418
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ--------RFFALV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 419 MAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAV-LNQCNYVVLDEAD 497
Cdd:cd17954 74 LAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFsLKSLKFLVMDEAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670360632 498 RMIDMGFEPQVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVV 563
Cdd:cd17954 154 RLLNMDFEPEIDKILKVIPRE-----------------RTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
348-564 |
1.22e-64 |
|
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: 213.38 E-value: 1.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPISEeneAEGPYAVVMAPTRELAQ 427
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLER---GDGPIVLVLAPTRELAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 428 QIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQ 507
Cdd:cd17966 78 QIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 670360632 508 VVGVLDampssNLKPEnedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVVT 564
Cdd:cd17966 158 IRKIVD-----QIRPD------------RQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
321-569 |
1.38e-61 |
|
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: 207.20 E-value: 1.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 321 EDFNISYKGSRIPRPMRKWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYI- 399
Cdd:cd18051 5 EDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 400 TRLPPISEENEAEG-------PYAVVMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPG 472
Cdd:cd18051 85 EQGPGESLPSESGYygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 473 RLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQVVGVL--DAMPSSNLkpenedeeldekriyRTTYMFSATMPPAVE 550
Cdd:cd18051 165 RLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPTGE---------------RQTLMFSATFPKEIQ 229
|
250
....*....|....*....
gi 670360632 551 RLARKYLRNPVVVTIGTAG 569
Cdd:cd18051 230 MLARDFLDNYIFLAVGRVG 248
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
348-566 |
2.49e-59 |
|
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: 199.35 E-value: 2.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLppiseeNEAEGPYAVVMAPTRELAQ 427
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP------RKKKGLRALILAPTRELAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 428 QIEEETVKFATYLGIKVVSIVGGQS-IEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEP 506
Cdd:cd17957 75 QIYRELLKLSKGTGLRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFRE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 507 QVVGVLDAMPSSNLkpenedeeldekriyrTTYMFSATMPPAVERLARKYLRNPVVVTIG 566
Cdd:cd17957 155 QTDEILAACTNPNL----------------QRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
575-704 |
9.73e-59 |
|
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: 195.03 E-value: 9.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 575 ITQNVIMVKESEKMPRL-QKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNV 653
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 670360632 654 LVATDVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSFL 704
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
344-563 |
2.73e-57 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 194.06 E-value: 2.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 344 LGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPISeeneaeGPYAVVMAPTR 423
Cdd:cd17959 8 LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTV------GARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 424 ELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMG 503
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 504 FEPQVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVV 563
Cdd:cd17959 162 FAEQLHEILSRLPEN-----------------RQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
348-564 |
7.01e-57 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 192.68 E-value: 7.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITrLPPISEENEaEGPYAVVMAPTRELAQ 427
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLD-LQPIPREQR-NGPGVLVLTPTRELAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 428 QIEEETVKFaTYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQ 507
Cdd:cd17958 79 QIEAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 670360632 508 VVGVLdampsSNLKPEnedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVVT 564
Cdd:cd17958 158 IRKIL-----LDIRPD------------RQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
361-552 |
1.39e-55 |
|
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: 187.83 E-value: 1.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 361 SPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPiseeneaeGPYAVVMAPTRELAQQIEEETVKFATYL 440
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN--------GPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 441 GIKVVSIVGGQSIEEQGFKIRqGCEIVIATPGRLLDCLERRyAVLNQCNYVVLDEADRMIDMGFEPQVVGVLDAMPSSnl 520
Cdd:pfam00270 73 GLKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKK-- 148
|
170 180 190
....*....|....*....|....*....|..
gi 670360632 521 kpenedeeldekriyRTTYMFSATMPPAVERL 552
Cdd:pfam00270 149 ---------------RQILLLSATLPRNLEDL 165
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
348-564 |
2.06e-54 |
|
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: 185.86 E-value: 2.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLppiSEENEAEGPYAVVMAPTRELAQ 427
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKR---KANLKKGQVGALIISPTRELAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 428 QIEEETVKFATYLGIKVVS--IVGGQSIEEQGFKI-RQGCEIVIATPGRLLDCLERRYAVLN--QCNYVVLDEADRMIDM 502
Cdd:cd17960 78 QIYEVLQSFLEHHLPKLKCqlLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 670360632 503 GFEPQVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVVT 564
Cdd:cd17960 158 GFEADLNRILSKLPKQ-----------------RRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
348-563 |
2.94e-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: 185.54 E-value: 2.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPiseeneaEGPY--AVVMAPTREL 425
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPK-------KKAAtrVLVLVPTREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 426 AQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAV-LNQCNYVVLDEADRMIDMGF 504
Cdd:cd17947 74 AMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFdLDSIEILVLDEADRMLEEGF 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 670360632 505 EPQVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVV 563
Cdd:cd17947 154 ADELKEILRLCPRT-----------------RQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
348-563 |
5.59e-54 |
|
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: 184.85 E-value: 5.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYI----TRLPPIseenEAEGPYAVVMAPTR 423
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFAleqeKKLPFI----KGEGPYGLIVCPSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 424 ELAQQIEEETVKFATYL------GIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEAD 497
Cdd:cd17951 77 ELARQTHEVIEYYCKALqeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEAD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670360632 498 RMIDMGFEPQVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVV 563
Cdd:cd17951 157 RMIDMGFEEDIRTIFSYFKGQ-----------------RQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
319-566 |
6.73e-54 |
|
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: 185.98 E-value: 6.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 319 FREDFNISYKGSRIPRPMRKWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSY 398
Cdd:cd18049 6 YRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 399 ITRLPPISEeneAEGPYAVVMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCL 478
Cdd:cd18049 86 INHQPFLER---GDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 479 ERRYAVLNQCNYVVLDEADRMIDMGFEPQVVGVLDampssNLKPEnedeeldekriyRTTYMFSATMPPAVERLARKYLR 558
Cdd:cd18049 163 EAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD-----QIRPD------------RQTLMWSATWPKEVRQLAEDFLK 225
|
....*...
gi 670360632 559 NPVVVTIG 566
Cdd:cd18049 226 DYIHINIG 233
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
339-563 |
3.50e-52 |
|
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: 179.80 E-value: 3.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 339 WSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYI-TRLPPISeeneaegpyAV 417
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIdPKKDVIQ---------AL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 418 VMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEAD 497
Cdd:cd17940 72 ILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEAD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670360632 498 RMIDMGFEPQVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVV 563
Cdd:cd17940 152 KLLSQDFQPIIEKILNFLPKE-----------------RQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
344-558 |
7.29e-52 |
|
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: 179.32 E-value: 7.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 344 LGTELLRAIDKAGYEKPSPIQMAAIPLGLQQR-DVIGIAETGSGKTAAFVLPML-SYITRLPPISEENEAegpyAVVMAP 421
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTGdDVLARAKTGTGKTLAFLLPAIqSLLNTKPAGRRSGVS----ALIISP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 422 TRELAQQIEEETVKFATYL-GIKVVSIVGGQSIEEQGFKI-RQGCEIVIATPGRLLDCLERRYA--VLNQCNYVVLDEAD 497
Cdd:cd17964 77 TRELALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEAD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 670360632 498 RMIDMGFEPQVVGVLDAMPSSNLKPenedeeldekriyRTTYMFSATMPPAVERLARKYLR 558
Cdd:cd17964 157 RLLDMGFRPDLEQILRHLPEKNADP-------------RQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
354-564 |
1.16e-51 |
|
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: 178.93 E-value: 1.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 354 KAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPP-ISEEneaEGPYAVVMAPTRELAQQIEEE 432
Cdd:cd17949 8 KMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPrVDRS---DGTLALVLVPTRELALQIYEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 433 T---VKFATYLgikVV-SIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYA-VLNQCNYVVLDEADRMIDMGFEPQ 507
Cdd:cd17949 85 LeklLKPFHWI---VPgYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADRLLDMGFEKD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 670360632 508 VVGVLDAMPSSNLKPENEDEELdekrIYRTTYMFSATMPPAVERLARKYLRNPVVVT 564
Cdd:cd17949 162 ITKILELLDDKRSKAGGEKSKP----SRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
348-562 |
2.65e-51 |
|
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: 177.80 E-value: 2.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLsyiTRLppiSEEneAEGPYAVVMAPTRELAQ 427
Cdd:cd17955 10 LVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL---QRL---SED--PYGIFALVLTPTRELAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 428 QIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLE---RRYAVLNQCNYVVLDEADRMIDMGF 504
Cdd:cd17955 82 QIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGSF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 670360632 505 EPQVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVV 562
Cdd:cd17955 162 EDDLATILSALPPK-----------------RQTLLFSATLTDALKALKELFGNKPFF 202
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
311-566 |
7.53e-51 |
|
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: 178.67 E-value: 7.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 311 MTERDWRIFREDFNISYKGSRIPRPMRKWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAA 390
Cdd:cd18050 36 MTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 391 FVLPMLSYITRLPPISEeneAEGPYAVVMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIAT 470
Cdd:cd18050 116 YLLPAIVHINHQPYLER---GDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIAT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 471 PGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQVVGVLDampssNLKPEnedeeldekriyRTTYMFSATMPPAVE 550
Cdd:cd18050 193 PGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD-----QIRPD------------RQTLMWSATWPKEVR 255
|
250
....*....|....*.
gi 670360632 551 RLARKYLRNPVVVTIG 566
Cdd:cd18050 256 QLAEDFLRDYVQINIG 271
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
352-577 |
1.96e-50 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 174.99 E-value: 1.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 352 IDKAGYEKPSPIQMAAIPLGLQ-QRDVIGIAETGSGKTAAFVLPMLSYITRLPpiseeneaeGPYAVVMAPTRELAQQIE 430
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEALKRGK---------GGRVLVLVPTRELAEQWA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 431 EETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGC-EIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQVV 509
Cdd:smart00487 72 EELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 670360632 510 GVLDAMPSSNlkpenedeeldeKRIyrttyMFSATMPPAVERLARKYLRNPVVVTIGTagKATDLITQ 577
Cdd:smart00487 152 KLLKLLPKNV------------QLL-----LLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQ 200
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
348-545 |
2.12e-50 |
|
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: 176.28 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQR-DVIGIAETGSGKTAAFVLPML-SYITRLPPISEENEAEGPYAVVMAPTREL 425
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRDGkDVIGAAETGSGKTLAFGIPILeRLLSQKSSNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 426 AQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQ---CNYVVLDEADRMIDM 502
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANlksLRFLVLDEADRMLEK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 670360632 503 G-FEpQVVGVLDAMPSSNlkpenedeelDEKRIYRTTYMFSATM 545
Cdd:cd17946 161 GhFA-ELEKILELLNKDR----------AGKKRKRQTFVFSATL 193
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
348-565 |
3.29e-49 |
|
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: 172.00 E-value: 3.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPpiSEENEAEGPYAVVMAPTRELAQ 427
Cdd:cd17961 5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAK--AESGEEQGTRALILVPTRELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 428 QIEEETVKFATYLG--IKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLER-RYAVLNQCNYVVLDEADRMIDMGF 504
Cdd:cd17961 83 QVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESgSLLLLSTLKYLVIDEADLVLSYGY 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 670360632 505 EPQVVGVLDAMPssnlkpenedeeldekRIYRTTYMfSATMPPAVERLARKYLRNPVVVTI 565
Cdd:cd17961 163 EEDLKSLLSYLP----------------KNYQTFLM-SATLSEDVEALKKLVLHNPAILKL 206
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
348-564 |
7.22e-48 |
|
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: 167.73 E-value: 7.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITrlppiseeNEAEGPYAVVMAPTRELAQ 427
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL--------TEHRNPSALILTPTRELAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 428 QIEEETVKFAT-YLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEP 506
Cdd:cd17962 73 QIEDQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 670360632 507 QVVGVLDAMPSSNlkpenedeeldekriyrTTYMFSATMPPAVERLARKYLRNPVVVT 564
Cdd:cd17962 153 QVLDILENISHDH-----------------QTILVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
344-561 |
2.20e-45 |
|
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: 160.95 E-value: 2.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 344 LGTELLRAIDKAGYEKPSPIQMAAI-PLgLQQRDVIGIAETGSGKTAAFVLPMLSYItrlppiseENEAEGPYAVVMAPT 422
Cdd:cd17939 4 LSEDLLRGIYAYGFEKPSAIQQRAIvPI-IKGRDVIAQAQSGTGKTATFSIGALQRI--------DTTVRETQALVLAPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 423 RELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDM 502
Cdd:cd17939 75 RELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 670360632 503 GFEPQVVGVLDAMPSSNlkpenedeeldekriyrTTYMFSATMPPAVERLARKYLRNPV 561
Cdd:cd17939 155 GFKDQIYDIFQFLPPET-----------------QVVLFSATMPHEVLEVTKKFMRDPV 196
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
349-563 |
6.87e-45 |
|
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: 159.76 E-value: 6.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 349 LRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLppisEENEAEGPYAVVMAPTRELAQQ 428
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRE----RWTPEDGLGALIISPTRELAMQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 429 IEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQgCEIVIATPGRLLDCL-ERRYAVLNQCNYVVLDEADRMIDMGFEPQ 507
Cdd:cd17941 78 IFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMdETPGFDTSNLQMLVLDEADRILDMGFKET 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 670360632 508 VVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVV 563
Cdd:cd17941 157 LDAIVENLPKS-----------------RQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
347-564 |
1.66e-44 |
|
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: 158.51 E-value: 1.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 347 ELLRAIDKAGYEKPSPIQMAAIPLGLQQ--RDVIGIAETGSGKTAAFVLPMLSYItrlppisEENEAEgPYAVVMAPTRE 424
Cdd:cd17963 4 ELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-------DPTLKS-PQALCLAPTRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 425 LAQQIEEETVKFATYLGIKVVSIV------GGQSIEEQgfkirqgceIVIATPGRLLDCLERRYAVLNQCNYVVLDEADR 498
Cdd:cd17963 76 LARQIGEVVEKMGKFTGVKVALAVpgndvpRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 670360632 499 MIDM-GFEPQVVGVLDAMPsSNLKpenedeeldekriyrtTYMFSATMPPAVERLARKYLRNPVVVT 564
Cdd:cd17963 147 MLDTqGHGDQSIRIKRMLP-RNCQ----------------ILLFSATFPDSVRKFAEKIAPNANTIK 196
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
344-561 |
4.06e-43 |
|
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: 154.91 E-value: 4.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 344 LGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYItrlppiseENEAEGPYAVVMAPTR 423
Cdd:cd18046 6 LKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI--------DTSLKATQALVLAPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 424 ELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMG 503
Cdd:cd18046 78 ELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 670360632 504 FEPQVVGVLDAMPSSNlkpenedeeldekriyrTTYMFSATMPPAVERLARKYLRNPV 561
Cdd:cd18046 158 FKDQIYDIFQKLPPDT-----------------QVVLLSATMPNDVLEVTTKFMRDPI 198
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
347-563 |
4.92e-41 |
|
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: 149.01 E-value: 4.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 347 ELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSyITRlppiseeneaegpyAVVMAPTRELA 426
Cdd:cd17938 9 ELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-IVV--------------ALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 427 QQIEEETVKFATYL---GIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMG 503
Cdd:cd17938 74 EQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 670360632 504 FEPQVVGVLDAMPSSNlkpenedeeLDEKRIyrTTYMFSATM-PPAVERLARKYLRNPVVV 563
Cdd:cd17938 154 NLETINRIYNRIPKIT---------SDGKRL--QVIVCSATLhSFEVKKLADKIMHFPTWV 203
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
348-563 |
1.95e-38 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 141.25 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRlppiseenEAEGPYAVVMAPTRELAQ 427
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDL--------ERRHPQVLILAPTREIAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 428 QIEEETVKFATYL-GIKVVSIVGGQSIEEQGFKIRqGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEP 506
Cdd:cd17943 73 QIHDVFKKIGKKLeGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 670360632 507 QVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNPVVV 563
Cdd:cd17943 152 DVNWIFSSLPKN-----------------KQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
344-565 |
2.66e-38 |
|
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: 141.33 E-value: 2.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 344 LGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPISEeneaegpyAVVMAPTR 423
Cdd:cd17950 9 LKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVS--------VLVICHTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 424 ELAQQIEEETVKFATYL-GIKVVSIVGGQSIEEQGFKIRQGC-EIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMId 501
Cdd:cd17950 81 ELAFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKML- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 670360632 502 mgfepqvvgvldampssnlkpenedEELDEKR----IYRTT------YMFSATMPPAVERLARKYLRNPVVVTI 565
Cdd:cd17950 160 -------------------------EQLDMRRdvqeIFRATphdkqvMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
586-695 |
9.99e-37 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 133.49 E-value: 9.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 586 EKMPRLQKILTDLGDKTAIVFCNTKKTADMRAKdLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVATDVAGRGID 665
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 670360632 666 IPDVAHVINYEMPSSVDTYTHRIGRTGRAG 695
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
343-563 |
1.64e-35 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350803 [Multi-domain] Cd Length: 201 Bit Score: 133.36 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 343 KLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYItrlppiseENEAEGPYAVVMAPT 422
Cdd:cd18045 5 GLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL--------DIQVRETQALILSPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 423 RELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDM 502
Cdd:cd18045 77 RELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 670360632 503 GFEPQVVGVLDAMPSsnlKPENedeeldekriyrttYMFSATMPPAVERLARKYLRNPVVV 563
Cdd:cd18045 157 GFKEQIYDVYRYLPP---ATQV--------------VLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
349-560 |
5.76e-35 |
|
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: 131.71 E-value: 5.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 349 LRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLppisEENEAEGPYAVVMAPTRELAQQ 428
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKL----KFKPRNGTGVIIISPTRELALQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 429 IEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLE--RRYAVLN-QCnyVVLDEADRMIDMGFE 505
Cdd:cd17942 78 IYGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQntKGFLYKNlQC--LIIDEADRILEIGFE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 670360632 506 PQVVGVLDAMPSSnlkpenedeeldekriyRTTYMFSATMPPAVERLARKYLRNP 560
Cdd:cd17942 156 EEMRQIIKLLPKR-----------------RQTMLFSATQTRKVEDLARISLKKK 193
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
348-564 |
3.13e-32 |
|
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: 125.05 E-value: 3.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQ---------RDVIGIAETGSGKTAAFVLP---MLSY--ITRLppiseeneaeg 413
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPivqALSKrvVPRL----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 414 pYAVVMAPTRELAQQIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCE--------IVIATPGRLLDCLER-RYAV 484
Cdd:cd17956 70 -RALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNStPGFT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 485 LNQCNYVVLDEADRMIDMGFE---PQVVGVLDAMPSSNLKPENEDEELDEKRIYRTTYMFSATMPPAVERLARKYLRNPV 561
Cdd:cd17956 149 LKHLRFLVIDEADRLLNQSFQdwlETVMKALGRPTAPDLGSFGDANLLERSVRPLQKLLFSATLTRDPEKLSSLKLHRPR 228
|
...
gi 670360632 562 VVT 564
Cdd:cd17956 229 LFT 231
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
348-552 |
1.65e-30 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 120.16 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 348 LLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRlPPISEENEAEGPYAVVMAPTRELAQ 427
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLR-YKLLAEGPFNAPRGLVITPSRELAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 428 QIEEETVKFATYLGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQ 507
Cdd:cd17948 80 QIGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 670360632 508 VVGVLDAMPSSNLKPENEDEEldekriYRTTYMF--SATMPPAVERL 552
Cdd:cd17948 160 LSHFLRRFPLASRRSENTDGL------DPGTQLVlvSATMPSGVGEV 200
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
362-558 |
1.15e-28 |
|
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: 113.79 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 362 PIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMlsyITRLPPISEE-NEAEGPYAVVMAPTRELAQQIEEETVKFATYL 440
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPL---IEKLQEDQQPrKRGRAPKVLVLAPTRELANQVTKDFKDITRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 441 giKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADRMIDMGFEPQVVGVLdampSSNL 520
Cdd:cd17944 92 --SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIL----SVSY 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 670360632 521 KPENEDEEldekriyrTTYMFSATMPPAVERLARKYLR 558
Cdd:cd17944 166 KKDSEDNP--------QTLLFSATCPDWVYNVAKKYMK 195
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
617-695 |
2.15e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 108.84 E-value: 2.15e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 670360632 617 AKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVATDVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAG 695
Cdd:smart00490 4 AELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
336-565 |
1.94e-25 |
|
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: 105.49 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 336 MRKWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQ--RDVIGIAETGSGKTAAFVLPMLSYITRLPPIseeneaeg 413
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 414 PYAVVMAPTRELAQQ---IEEETVKFATylGIKVVSIVGGQSIeEQGFKIRQgcEIVIATPGRLLD-CLERRYAVLNQCN 489
Cdd:cd18048 89 PQCLCLSPTFELALQtgkVVEEMGKFCV--GIQVIYAIRGNRP-GKGTDIEA--QIVIGTPGTVLDwCFKLRLIDVTNIS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 670360632 490 YVVLDEADRMIDM-GFEPQVVGVLDAMPSSNlkpenedeeldekriyrTTYMFSATMPPAVERLARKYLRNPVVVTI 565
Cdd:cd18048 164 VFVLDEADVMINVqGHSDHSVRVKRSMPKEC-----------------QMLLFSATFEDSVWAFAERIVPDPNIIKL 223
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
356-564 |
4.38e-24 |
|
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: 102.07 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 356 GYEKPSPIQMAAIPLGLQQR---------------DVIGIA-ETGSGKTAAFVLPMLSYITRL---PPISEENEAEG--- 413
Cdd:cd17965 27 EEIKPSPIQTLAIKKLLKTLmrkvtkqtsneepklEVFLLAaETGSGKTLAYLAPLLDYLKRQeqePFEEAEEEYESakd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 414 ---PYAVVMAPTRELAQQIEEETVKFATY--LGIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAVLNQC 488
Cdd:cd17965 107 tgrPRSVILVPTHELVEQVYSVLKKLSHTvkLGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRV 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670360632 489 NYVVLDEADRMIDMGFEPQVVGVLDAMPSSNlkpenedeeldeKRIyrttyMFSATMPPAVERLARKYLRNPVVVT 564
Cdd:cd17965 187 THLVVDEADTLFDRSFLQDTTSIIKRAPKLK------------HLI-----LCSATIPKEFDKTLRKLFPDVVRIA 245
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
579-737 |
8.58e-22 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 99.44 E-value: 8.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 579 VIMVKESEKMPRLQKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVATd 658
Cdd:COG0514 209 VVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 659 VA-GRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVATSFLTLENTDIffdLKQMLiqSNSPVPPELARHEASK 737
Cdd:COG0514 288 IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAI---QRFFI--EQSPPDEERKRVERAK 362
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
293-701 |
2.66e-21 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 98.56 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 293 DAFDMRVDRHWSEKALEEMTERDWRIFREDFNISYKGSRIPRPMRKWSESKLGT-------ELLRAIDKAGYEKPS--PI 363
Cdd:COG1061 5 GIAERGADKLRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTerelaeaEALEAGDEASGTSFElrPY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 364 QMAAI-----PLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPpiseeneaegpyAVVMAPTRELAQQIEEEtvkFAT 438
Cdd:COG1061 85 QQEALeallaALERGGGRGLVVAPTGTGKTVLALALAAELLRGKR------------VLVLVPRRELLEQWAEE---LRR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 439 YLGIKVVSivggqsieeqGFKIRQGCEIVIATPGRLLDCLERRYaVLNQCNYVVLDEADRMIDMGFEpqvvGVLDAMPSS 518
Cdd:COG1061 150 FLGDPLAG----------GGKKDSDAPITVATYQSLARRAHLDE-LGDRFGLVIIDEAHHAGAPSYR----RILEAFPAA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 519 NL-----KPENEDE-ELDEKR----IYRTTYmfsatmppaVERLARKYLRNPVVVTIGT----AGKATDLITQNV---IM 581
Cdd:COG1061 215 YRlgltaTPFRSDGrEILLFLfdgiVYEYSL---------KEAIEDGYLAPPEYYGIRVdltdERAEYDALSERLreaLA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 582 VKESEKMPRLQKILTDLGD-KTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVATDVA 660
Cdd:COG1061 286 ADAERKDKILRELLREHPDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVL 365
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 670360632 661 GRGIDIPDVAHVInYEMP-SSVDTYTHRIGRTGRAGK-KGVAT 701
Cdd:COG1061 366 NEGVDVPRLDVAI-LLRPtGSPREFIQRLGRGLRPAPgKEDAL 407
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
584-709 |
1.45e-17 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 87.09 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 584 ESEKMPRL----QKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHG--------GKSQDQREISLDGFRNRRF 651
Cdd:COG1111 333 EHPKLSKLreilKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEF 412
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 670360632 652 NVLVATDVAGRGIDIPDVAHVINYE-MPSSVdTYTHRIGRTGRAGKKGVATsfLTLENT 709
Cdd:COG1111 413 NVLVATSVAEEGLDIPEVDLVIFYEpVPSEI-RSIQRKGRTGRKREGRVVV--LIAKGT 468
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
337-563 |
1.52e-17 |
|
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: 81.69 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 337 RKWSESKLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQ--RDVIGIAETGSGKTAAFVLPMLSYITRLPPISEeneaegp 414
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 415 yAVVMAPTRELAQQ---IEEETVKFatYLGIKVVSIVGGQSIeEQGFKIRQgcEIVIATPGRLLD-CLERRYAVLNQCNY 490
Cdd:cd18047 74 -CLCLSPTYELALQtgkVIEQMGKF--YPELKLAYAVRGNKL-ERGQKISE--QIVIGTPGTVLDwCSKLKFIDPKKIKV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 670360632 491 VVLDEADRMI-DMGFEPQVVGVLDAMPSSNlkpenedeeldekriyrTTYMFSATMPPAVERLARKYLRNPVVV 563
Cdd:cd18047 148 FVLDEADVMIaTQGHQDQSIRIQRMLPRNC-----------------QMLLFSATFEDSVWKFAQKVVPDPNVI 204
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
579-696 |
2.14e-17 |
|
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: 79.17 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 579 VIMV-KESEKMPRLQKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVAT 657
Cdd:cd18794 8 VRPKdKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 670360632 658 DVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGK 696
Cdd:cd18794 88 VAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGL 126
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
376-499 |
6.83e-15 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 72.44 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 376 DVIGIAETGSGKTAAFVLPMLSYItrlppiseenEAEGPYAVVMAPTRELAQQIEEEtVKFATYLGIKVVSIVGGQSIEE 455
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLL----------LKKGKKVLVLVPTKALALQTAER-LRELFGPGIRVAVLVGGSSAEE 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 670360632 456 QGFKIRQGCEIVIATPGRLLDCLERRYA-VLNQCNYVVLDEADRM 499
Cdd:cd00046 72 REKNKLGDADIIIATPDMLLNLLLREDRlFLKDLKLIIVDEAHAL 116
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
344-724 |
7.37e-15 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 78.01 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 344 LGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRD-VIGIAETGSGKTAAFVLPMLSYItrlppiseeneAEGPYAVVMAPT 422
Cdd:COG1204 7 PLEKVIEFLKERGIEELYPPQAEALEAGLLEGKnLVVSAPTASGKTLIAELAILKAL-----------LNGGKALYIVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 423 RELAQQIEEETVKFATYLGIKVVSIVGGqsIEEQGFKIRQgCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEA------ 496
Cdd:COG1204 76 RALASEKYREFKRDFEELGIKVGVSTGD--YDSDDEWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhlidde 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 497 ----------DRMIDMGFEPQVVGVldampssnlkpenedeeldekriyrttymfSATMpPAVERLARkYLRNPVVvtiG 566
Cdd:COG1204 153 srgptlevllARLRRLNPEAQIVAL------------------------------SATI-GNAEEIAE-WLDAELV---K 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 567 TAGKATDL----ITQNVIMVKESEKmpRLQKILTDLGDKT------AIVFCNTKKTADMRAK----------------DL 620
Cdd:COG1204 198 SDWRPVPLnegvLYDGVLRFDDGSR--RSKDPTLALALDLleeggqVLVFVSSRRDAESLAKkladelkrrltpeereEL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 621 DKSGFRVTTL---------------------HGGKSQDQREISLDGFRNRRFNVLVATDVAGRGIDIPdVAHVI------ 673
Cdd:COG1204 276 EELAEELLEVseethtnekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIirdtkr 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 670360632 674 NYEMPSSVDTYTHRIGRTGRAGKKGVATSFLTLENTDIFFDLKQMLIQSNS 724
Cdd:COG1204 355 GGMVPIPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDEADELFERYILGEP 405
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
587-696 |
1.89e-13 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 74.14 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 587 KMPRL----QKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHG--------GKSQ-DQREIsLDGFRNRRFNV 653
Cdd:PRK13766 348 KLEKLreivKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaskdgdkGMSQkEQIEI-LDKFRAGEFNV 426
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 670360632 654 LVATDVAGRGIDIPDVAHVINYE-MPSSVDTyTHRIGRTGRAGK 696
Cdd:PRK13766 427 LVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGRQEE 469
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
335-700 |
3.15e-13 |
|
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: 73.33 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 335 PMRKWseskLGTELLRAIDKAGYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPpiseeneaeGP 414
Cdd:COG1205 36 PWPDW----LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP---------GA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 415 YAVVMAPTRELAQQIEEETVKFATYLGIKV-VSIVGGQSIEEQGFKIRQGCEIVIATP--------------GRLLDCLE 479
Cdd:COG1205 103 TALYLYPTKALARDQLRRLRELAEALGLGVrVATYDGDTPPEERRWIREHPDIVLTNPdmlhygllphhtrwARFFRNLR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 480 rryavlnqcnYVVLDEAD--RmidmgfepqvvGVLDA-MpsSNLkpenedeeldekrIYRttymfsatmppaVERLARKY 556
Cdd:COG1205 183 ----------YVVIDEAHtyR-----------GVFGShV--ANV-------------LRR------------LRRICRHY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 557 LRNPVVV----TIGTA--------GKATDLITQN--------VIMVKESEKMPRLQK--------ILTDL---GDKTaIV 605
Cdd:COG1205 215 GSDPQFIlasaTIGNPaehaerltGRPVTVVDEDgsprgertFVLWNPPLVDDGIRRsalaeaarLLADLvreGLRT-LV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 606 FCNTKKTAD---MRAKD-LDKSGF--RVTTLHGG-KSQDQREISlDGFRNRRFNVLVATDVAGRGIDIPDVAHVINYEMP 678
Cdd:COG1205 294 FTRSRRGAEllaRYARRaLREPDLadRVAAYRAGyLPEERREIE-RGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYP 372
|
410 420
....*....|....*....|..
gi 670360632 679 SSVDTYTHRIGRTGRAGKKGVA 700
Cdd:COG1205 373 GTRASFWQQAGRAGRRGQDSLV 394
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
587-678 |
9.47e-13 |
|
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: 65.96 E-value: 9.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 587 KMPRLQKILTDL---GDKtAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRN----RRFnvLVATDV 659
Cdd:cd18793 12 KLEALLELLEELrepGEK-VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpdiRVF--LLSTKA 88
|
90
....*....|....*....
gi 670360632 660 AGRGIDIPDVAHVINYEMP 678
Cdd:cd18793 89 GGVGLNLTAANRVILYDPW 107
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
585-694 |
1.32e-12 |
|
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: 65.69 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 585 SEKMPRLQKIL----TDLGDKTAIVFCNTKKTADMRAKDLDK-----SGFRVTTLHGGKSQDQREIS----------LDG 645
Cdd:cd18802 6 IPKLQKLIEILreyfPKTPDFRGIIFVERRATAVVLSRLLKEhpstlAFIRCGFLIGRGNSSQRKRSlmtqrkqketLDK 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 670360632 646 FRNRRFNVLVATDVAGRGIDIPDVAHVINYEMPSSVDTYthrIGRTGRA 694
Cdd:cd18802 86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSY---IQSRGRA 131
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
649-699 |
2.12e-11 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 60.03 E-value: 2.12e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 670360632 649 RRFNVLVATDVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGV 699
Cdd:cd18785 21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEG 71
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
587-693 |
2.90e-11 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 61.99 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 587 KMPRLQKILTD-------LGDKTAIVFCNTKKTADMRAKDLDK--SGFRVTTLHG--------GKSQDQREISLDGFRNR 649
Cdd:cd18801 10 KLEKLEEIVKEhfkkkqeGSDTRVIIFSEFRDSAEEIVNFLSKirPGIRATRFIGqasgksskGMSQKEQKEVIEQFRKG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 670360632 650 RFNVLVATDVAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGR 693
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
601-695 |
1.15e-10 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 64.73 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 601 KTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVATDVAGRGIDIPDVAHVINYEMPSS 680
Cdd:PRK11057 237 KSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRN 316
|
90
....*....|....*
gi 670360632 681 VDTYTHRIGRTGRAG 695
Cdd:PRK11057 317 IESYYQETGRAGRDG 331
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
374-496 |
1.06e-09 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 58.82 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 374 QRDVIGIAETGSGKT--AAFVLPMLSYITRLPPISeeneaeGPYAVVMAPTRELA-QQIEEetvkFATYLGIKVVSIVGG 450
Cdd:cd18034 16 KRNTIVVLPTGSGKTliAVMLIKEMGELNRKEKNP------KKRAVFLVPTVPLVaQQAEA----IRSHTDLKVGEYSGE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 670360632 451 QSIEEQGFKIRQGC----EIVIATPGRLLDCLERRYAVLNQCNYVVLDEA 496
Cdd:cd18034 86 MGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
600-696 |
2.08e-09 |
|
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: 56.89 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 600 DKTAIVFCNTKKTADMRAKDL------DKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVATDVAGRGIDIPDVAHVI 673
Cdd:cd18796 38 HKSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVI 117
|
90 100
....*....|....*....|...
gi 670360632 674 NYEMPSSVDTYTHRIGRTGRAGK 696
Cdd:cd18796 118 QIGSPKSVARLLQRLGRSGHRPG 140
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
584-709 |
6.89e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 59.08 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 584 ESEKMPRLQKILTDL---GDKtAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRR-FNV-LVATD 658
Cdd:COG0553 531 RSAKLEALLELLEELlaeGEK-VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVfLISLK 609
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 670360632 659 VAGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAG-KKGVATSFLTLENT 709
Cdd:COG0553 610 AGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGqTRDVQVYKLVAEGT 661
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
363-483 |
9.35e-09 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 56.21 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 363 IQMAAIPLGLQ-QRDVIGIAETGSGKTAAFVLPMLSYITRLPPISEENeaegPYAVVMAPTRELAQQIEEE-TVKFATyL 440
Cdd:cd18023 5 IQSEVFPDLLYsDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN----RKVVYIAPIKALCSEKYDDwKEKFGP-L 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 670360632 441 GIKVVSIVGGQSIEEQgFKIrQGCEIVIATPGRlLDCLERRYA 483
Cdd:cd18023 80 GLSCAELTGDTEMDDT-FEI-QDADIILTTPEK-WDSMTRRWR 119
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
362-496 |
9.94e-09 |
|
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: 55.35 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 362 PIQMAAIPLGLQQRD--VIGiAETGSGKTAAFVLPMLSYITRlppiseeneaEGPYAVVMAPTRELAQQIEEETVKFATY 439
Cdd:cd17921 4 PIQREALRALYLSGDsvLVS-APTSSGKTLIAELAILRALAT----------SGGKAVYIAPTRALVNQKEADLRERFGP 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 670360632 440 LGIKVVSIVGgqSIEEQGFKIRQgCEIVIATPGRLLDCLER-RYAVLNQCNYVVLDEA 496
Cdd:cd17921 73 LGKNVGLLTG--DPSVNKLLLAE-ADILVATPEKLDLLLRNgGERLIQDVRLVVVDEA 127
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
364-496 |
1.38e-08 |
|
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: 55.28 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 364 QMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRlppiseeneAEGPYAVVMAPTRELAQQIEEETVKFATYL--G 441
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLR---------DPGSRALYLYPTKALAQDQLRSLRELLEQLglG 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 670360632 442 IKVVSIVGGQSIEEQGFKIRQGCEIVIATPgrllDCLE--------RRYAVLNQCNYVVLDEA 496
Cdd:cd17923 76 IRVATYDGDTPREERRAIIRNPPRILLTNP----DMLHyallphhdRWARFLRNLRYVVLDEA 134
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
589-701 |
1.59e-08 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 54.19 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 589 PRLQKILTDLGDKTaIVFCNTKKTADMRAKDLdKSGFRVTTLHGGK---------SQDQREISlDGFRNRRFNVLVATDV 659
Cdd:cd18797 25 ARLFADLVRAGVKT-IVFCRSRKLAELLLRYL-KARLVEEGPLASKvasyragylAEDRREIE-AELFNGELLGVVATNA 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 670360632 660 AGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKGVAT 701
Cdd:cd18797 102 LELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
603-673 |
1.70e-08 |
|
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: 52.95 E-value: 1.70e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 670360632 603 AIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQRE---ISLDGFRNRRFNVLVATDVAGRGIDIPDVAHVI 673
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdeaLILLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
599-704 |
2.75e-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: 53.41 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 599 GDKTaIVFCNTKKTADMRAKDLDKSGfrvttLHGGKSQDQREISLDGFRNRRFNVLVATDVAGRGIDIPD--VAHVINYE 676
Cdd:cd18789 49 GDKI-IVFTDNVEALYRYAKRLLKPF-----ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEanVAIQISGH 122
|
90 100
....*....|....*....|....*...
gi 670360632 677 MPSSVDtYTHRIGRTGRAGKKGVATSFL 704
Cdd:cd18789 123 GGSRRQ-EAQRLGRILRPKKGGGKNAFF 149
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
588-721 |
5.91e-08 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 56.44 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 588 MPRLQKILTDLG--------DKTAIVFCNTKKTADMRAKDLDKSGFRVTTLHGGKSQDQREISLDGFRNRRFNVLVATDV 659
Cdd:PLN03137 660 VPKTKKCLEDIDkfikenhfDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVA 739
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 670360632 660 AGRGIDIPDVAHVINYEMPSSVDTYTHRIGRTGRAGKKgvATSFLTLENTDiFFDLKQMLIQ 721
Cdd:PLN03137 740 FGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQR--SSCVLYYSYSD-YIRVKHMISQ 798
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
383-496 |
6.39e-08 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 52.31 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 383 TGSGKTA-AFVLPMLSYITRLppiseeneaegpyaVVMAPTRELAQQIEEEtvkFATYLGIKVVSIVGGQSIEEQGfkir 461
Cdd:cd17926 27 TGSGKTLtALALIAYLKELRT--------------LIVVPTDALLDQWKER---FEDFLGDSSIGLIGGGKKKDFD---- 85
|
90 100 110
....*....|....*....|....*....|....*
gi 670360632 462 qGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEA 496
Cdd:cd17926 86 -DANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
359-498 |
4.79e-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: 50.89 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 359 KPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPpiseenEAEGPYAVVMAPTRELAQQIEEetvKFAT 438
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFP------AGRKGKVVFLANKVPLVEQQKE---VFRK 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 670360632 439 YLGI---KVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCLERRYAV-LNQCNYVVLDEADR 498
Cdd:cd17927 73 HFERpgyKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVsLSDFSLLVFDECHN 136
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
581-695 |
2.98e-06 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 47.55 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 581 MVKESEKMPRLQKILTDLGDKTAIVFCNTKKTADMRAKDLDKSGFrvttLHGGKSQDQREISLDGFRNRRFNVLVATDVA 660
Cdd:cd18795 24 MNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRELVEELFREGLIKVLVATSTL 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 670360632 661 GRGIDIPdvAH-VI---------NYEMPSSVDTYTHRIGRTGRAG 695
Cdd:cd18795 100 AAGVNLP--ARtVIikgtqrydgKGYRELSPLEYLQMIGRAGRPG 142
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
356-496 |
3.37e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 45.60 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 356 GYEKPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLsyitrlppiseeneAEGPYAVVMAPTRELAQ-QIEEetv 434
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL--------------LLDGVTLVVSPLISLMQdQVDR--- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 670360632 435 kfATYLGIKVVSIVGGQSIEEQ---GFKIRQG-CEIVIATPGRL-----LDCLERRYAvLNQCNYVVLDEA 496
Cdd:cd17920 72 --LQQLGIRAAALNSTLSPEEKrevLLRIKNGqYKLLYVTPERLlspdfLELLQRLPE-RKRLALIVVDEA 139
|
|
| secA |
PRK12898 |
preprotein translocase subunit SecA; Reviewed |
636-707 |
3.45e-05 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237253 [Multi-domain] Cd Length: 656 Bit Score: 47.31 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 636 QDQREISLDGFRNRRFNVLVATDVAGRGIDI---PDVA-----HVINYEMPSSVDTYTHRIGRTGRAGKKGVATSFLTLE 707
Cdd:PRK12898 507 QDAEEAAIVARAGQRGRITVATNMAGRGTDIklePGVAargglHVILTERHDSARIDRQLAGRCGRQGDPGSYEAILSLE 586
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
357-447 |
1.56e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 45.26 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 357 YEKPSPIQMAAIPLGLQQRDVIGIAETGSGKT-AAFvlpmLSYITRLPPISEENEAE-GPYAVVMAPTRELAQQIE---- 430
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF----LAIIDELFRLGREGELEdKVYCLYVSPLRALNNDIHrnle 105
|
90 100
....*....|....*....|
gi 670360632 431 ---EETVKFATYLGIKVVSI 447
Cdd:PRK13767 106 eplTEIREIAKERGEELPEI 125
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
381-499 |
1.72e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 43.17 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 381 AETGSGKTAAFVLPMLSYITRlppiseeneaeGPYAVVMAPTRELAQQIEEETVKFatYLGIKVVSIVGGQSIeeqgfKI 460
Cdd:cd17918 43 GDVGSGKTLVALGAALLAYKN-----------GKQVAILVPTEILAHQHYEEARKF--LPFINVELVTGGTKA-----QI 104
|
90 100 110
....*....|....*....|....*....|....*....
gi 670360632 461 RQGCEIVIATPGrLLDCLERRYAVlnqcNYVVLDEADRM 499
Cdd:cd17918 105 LSGISLLVGTHA-LLHLDVKFKNL----DLVIVDEQHRF 138
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
362-510 |
3.19e-04 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 42.32 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 362 PIQMAAIPLGLQQ-RDVIGIAETGSGKTAAFVLPMLSYItrlppiseeneAEGPYAVVMAPTRELAqqiEEETVKFATY- 439
Cdd:cd18028 4 PPQAEAVRAGLLKgENLLISIPTASGKTLIAEMAMVNTL-----------LEGGKALYLVPLRALA---SEKYEEFKKLe 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 440 -LGIKVVSIVGGQSIEEQGFKIrqgCEIVIATPGRLLDCLERRYAVLNQCNYVVLDE----------------ADRMIDM 502
Cdd:cd18028 70 eIGLKVGISTGDYDEDDEWLGD---YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEihlisdeergptlesiVARLRRL 146
|
....*...
gi 670360632 503 GFEPQVVG 510
Cdd:cd18028 147 NPNTQIIG 154
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
626-700 |
5.15e-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: 5.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 670360632 626 RVTTLHGGKSQDQREISLDGFRNRRFNVLVATDVAGRGIDIPDVAHVI--NYEMPSSVDTYTHRiGRTGRAGKKGVA 700
Cdd:cd18810 53 RIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQLR-GRVGRSKERAYA 128
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
330-430 |
1.17e-03 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 42.40 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 330 SRIPRPMRKWSESKLGTellraidkagyekPSPIQMAAIPLGLQQRDVIGIAETGSGKT-AAFvLPMLSYITRLPPisEE 408
Cdd:COG1201 8 SLLHPAVRAWFAARFGA-------------PTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPR--PG 71
|
90 100
....*....|....*....|..
gi 670360632 409 NEAEGPYAVVMAPTRELAQQIE 430
Cdd:COG1201 72 ELPDGLRVLYISPLKALANDIE 93
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
359-528 |
1.33e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 40.92 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 359 KPSPIQMAAIPLGLQQRDVIGIAETGSGKTAAFVLPMLSYITRLPPISEENEaegpyAVVMAPTRELAQQieeETVKFAT 438
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGR-----VVVLVNKVPLVEQ---QLEKFFK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 439 YL--GIKVVSIVGGQSIEEQGFKIRQGCEIVIATPGRLLDCL------ERRY------------------AVLNQCNYVV 492
Cdd:cd18036 74 YFrkGYKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLlsgreeERVYlsdfsllifdechhtqkeHPYNKIMRMY 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 670360632 493 LDEadRMIDMGFEPQVVGVLDAMPSSNLKPENEDEE 528
Cdd:cd18036 154 LDK--KLSSQGPLPQILGLTASPGVGGARSFEEALE 187
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
625-700 |
3.70e-03 |
|
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: 38.79 E-value: 3.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 670360632 625 FRVTTLHGGKSQDQREISLDGFRNRRFNVLVATDVAGRGIDIPDVAHVI--NYEMPSSVDTYTHRiGRTGRAGKKGVA 700
Cdd:cd18792 61 ARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIieDADRFGLSQLHQLR-GRVGRGKHQSYC 137
|
|
| PRK09200 |
PRK09200 |
preprotein translocase subunit SecA; Reviewed |
641-707 |
3.84e-03 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 236408 [Multi-domain] Cd Length: 790 Bit Score: 40.69 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 641 ISLDGFRNRrfnVLVATDVAGRGIDI---PDVA-----HVINYEMPSSvdtytHRI-----GRTGRAGKKGVATSFLTLE 707
Cdd:PRK09200 470 IAEAGQKGA---VTVATNMAGRGTDIklgEGVHelgglAVIGTERMES-----RRVdlqlrGRSGRQGDPGSSQFFISLE 541
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
382-499 |
4.22e-03 |
|
SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.
Pssm-ID: 425504 [Multi-domain] Cd Length: 289 Bit Score: 39.97 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 382 ETGSGKTaafvLPMLSYITRLppISEENEAEGPYAVVmAPTrELAQQIEEETVKFATYLGIKVVSIVG---GQSIEEQGF 458
Cdd:pfam00176 25 EMGLGKT----LQTISLLLYL--KHVDKNWGGPTLIV-VPL-SLLHNWMNEFERWVSPPALRVVVLHGnkrPQERWKNDP 96
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 670360632 459 KIRQGCEIVIATpgrlLDCLERRYAVLNQCN--YVVLDEADRM 499
Cdd:pfam00176 97 NFLADFDVVITT----YETLRKHKELLKKVHwhRIVLDEGHRL 135
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
375-495 |
5.88e-03 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 38.33 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 375 RDVIGIAETGSGKTAAFVLPMLSYITRLPPiseeneaEGPYAVVMAPTRELAQQIEE--ETVKFATYLGIKVVSIVGGQS 452
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALSSLADEPE-------KGVQVLYISPLKALINDQERrlEEPLDEIDLEIPVAVRHGDTS 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 670360632 453 IEEQGFKIRQGCEIVIATPGRLLDCL--ERRYAVLNQCNYVVLDE 495
Cdd:cd17922 75 QSEKAKQLKNPPGILITTPESLELLLvnKKLRELFAGLRYVVVDE 119
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
377-496 |
6.03e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438707 [Multi-domain] Cd Length: 159 Bit Score: 38.21 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 377 VIGIAETGSGKTaafvlpmlsyiTRLPP-ISEENEAEGPYA--VVMAPTR----ELAQQIEEEtvkfatyLGIKVvsivg 449
Cdd:cd17917 4 VVIVGETGSGKT-----------TQVPQfLLEDGLAKGGKGriVCTQPRRiaaiSVAERVAEE-------RGEKL----- 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 670360632 450 GQSIeeqGFKIRQ------GCEIVIATPGRLLdcleRRYAV---LNQCNYVVLDEA 496
Cdd:cd17917 61 GEEV---GYQIRFesktssKTRIKFCTDGILL----RELLSdplLSGYSHVILDEA 109
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
383-498 |
6.13e-03 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 38.46 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 383 TGSGKT--AAFVlpMLSYItRLPPISeeneaegpYAVVMAPTREL-AQQIEeetvkfATYlgiKVVSIVGGQSIEEQG-- 457
Cdd:cd18033 25 TGLGKTfiAAVV--MLNYY-RWFPKG--------KIVFMAPTKPLvSQQIE------ACY---KITGIPSSQTAELTGsv 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 670360632 458 -----FKIRQGCEIVIATPGRLLDCLERRYAVLNQCNYVVLDEADR 498
Cdd:cd18033 85 pptkrAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHR 130
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
381-482 |
9.16e-03 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 38.01 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670360632 381 AETGSGKTAAFVLPMLSYITRLPPISeeneaegpyAVVMAPTRELAQQIEEETV-KFATYLGIKVVSIVGGQSieeQGFK 459
Cdd:cd18021 26 APTGSGKTVCAELALLRHWRQNPKGR---------AVYIAPMQELVDARYKDWRaKFGPLLGKKVVKLTGETS---TDLK 93
|
90 100
....*....|....*....|...
gi 670360632 460 IRQGCEIVIATPGRlLDCLERRY 482
Cdd:cd18021 94 LLAKSDVILATPEQ-WDVLSRRW 115
|
|
| |
