|
Name |
Accession |
Description |
Interval |
E-value |
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
228-481 |
0e+00 |
|
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: 543.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 228 SSIFSHYATGINFDKYDDILVDVSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTG 307
Cdd:cd18052 11 DEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 308 SGKTAAFLLPILQRFMTDGVAASKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKG 387
Cdd:cd18052 91 SGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 388 CNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASPGMPSKEERQTLMFSATYPEDIQRMAADF 467
Cdd:cd18052 171 CHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEF 250
|
250
....*....|....
gi 1207108023 468 LKVDYIFLAVGVVG 481
Cdd:cd18052 251 LKEDYLFLTVGRVG 264
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
259-632 |
9.19e-159 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 464.62 E-value: 9.19e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 259 IMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAAskfseiqeP 338
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--------P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 339 EAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLD 418
Cdd:COG0513 73 QALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 419 EADRMLDMGFEPEMRKLVASpgMPskEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGACSDVEQTIVQVDQYS 498
Cdd:COG0513 153 EADRMLDMGFIEDIERILKL--LP--KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 499 KRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSVAARGLDI 578
Cdd:COG0513 228 KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDI 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1207108023 579 EQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPEsDTPLARSLVKVL 632
Cdd:COG0513 308 DDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPD-ERRLLRAIEKLI 360
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
261-481 |
1.02e-144 |
|
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: 420.74 E-value: 1.02e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 261 TFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASK-FSEIQEPE 339
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGrGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 340 AIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDE 419
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207108023 420 ADRMLDMGFEPEMRKLVASPGMPSKEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVG 481
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
240-481 |
4.37e-123 |
|
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: 366.67 E-value: 4.37e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 240 FDKYDDILVDVSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIL 319
Cdd:cd18051 1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 320 QRFMTDGVAASKFSEI-------QEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLC 392
Cdd:cd18051 81 SQIYEQGPGESLPSESgyygrrkQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 393 ATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASPGMPSKEERQTLMFSATYPEDIQRMAADFLKvDY 472
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLD-NY 239
|
....*....
gi 1207108023 473 IFLAVGVVG 481
Cdd:cd18051 240 IFLAVGRVG 248
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
250-660 |
2.96e-120 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 370.26 E-value: 2.96e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 250 VSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIlqrfMTDGVAA 329
Cdd:PTZ00110 120 IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPA----IVHINAQ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 330 SKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGL 409
Cdd:PTZ00110 196 PLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 410 SKVRYLVLDEADRMLDMGFEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLKVDYIFLAVGVVG-GACSDVE 488
Cdd:PTZ00110 276 RRVTYLVLDEADRMLDMGFEPQIRKIVSQ----IRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNIK 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 489 QTIVQVDQYSKRDQLLELLRATGNE--RTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVL 566
Cdd:PTZ00110 352 QEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIM 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 567 VATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPESDTpLARSLVKVLSGAQQVVPKWLEEV 646
Cdd:PTZ00110 432 IATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYR-LARDLVKVLREAKQPVPPELEKL 510
|
410
....*....|....
gi 1207108023 647 AFSAHGTTGFNPRG 660
Cdd:PTZ00110 511 SNERSNGTERRRWG 524
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
260-619 |
1.27e-95 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 303.26 E-value: 1.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 260 MTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRfmtdgVAASKFSeIQepe 339
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK-----LDVKRFR-VQ--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 340 AIIVAPTRELINQIYLEARKFAYGT-CVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLD 418
Cdd:PRK11776 75 ALVLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 419 EADRMLDMGFEPEMRKLVASpgMPskEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGAcSDVEQTIVQVDQyS 498
Cdd:PRK11776 155 EADRMLDMGFQDAIDAIIRQ--AP--ARRQTLLFSATYPEGIAAISQRFQR-DPVEVKVESTHDL-PAIEQRFYEVSP-D 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 499 KRDQLLELLRATGN-ERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSVAARGLD 577
Cdd:PRK11776 228 ERLPALQRLLLHHQpESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLD 307
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1207108023 578 IEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPE 619
Cdd:PRK11776 308 IKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
260-614 |
1.54e-93 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 297.88 E-value: 1.54e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 260 MTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKFSEIQepe 339
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 340 AIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDE 419
Cdd:PRK10590 78 ALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 420 ADRMLDMGFEPEMRKLVASpgMPSKeeRQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGACSDVEQTIVQVDQYSK 499
Cdd:PRK10590 158 ADRMLDMGFIHDIRRVLAK--LPAK--RQNLLFSATFSDDIKALAEKLLH-NPLEIEVARRNTASEQVTQHVHFVDKKRK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 500 RdQLLELLRATGN-ERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSVAARGLDI 578
Cdd:PRK10590 233 R-ELLSQMIGKGNwQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDI 311
|
330 340 350
....*....|....*....|....*....|....*.
gi 1207108023 579 EQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVS 614
Cdd:PRK10590 312 EELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALS 347
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
248-643 |
8.00e-86 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 279.37 E-value: 8.00e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 248 VDVSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgV 327
Cdd:PLN00206 109 IHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCT--I 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 328 AASKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKI 407
Cdd:PLN00206 187 RSGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDI 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 408 GLSKVRYLVLDEADRMLDMGFEPEMRKLVASPGMPskeerQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGACSDV 487
Cdd:PLN00206 267 ELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAK-DIILISIGNPNRPNKAV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 488 EQTIVQVDQYSKRDQLLELLRATGNER--TMVFVETKRSADFIAtflcqEKISTT------SIHGDREQREREKALSDFR 559
Cdd:PLN00206 341 KQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLA-----NAITVVtglkalSIHGEKSMKERREVMKSFL 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 560 LGQCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNpESDTPLARSLVKVLSGAQQVV 639
Cdd:PLN00206 416 VGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVN-EEDRNLFPELVALLKSSGAAI 494
|
....
gi 1207108023 640 PKWL 643
Cdd:PLN00206 495 PREL 498
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
260-615 |
5.41e-84 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 271.82 E-value: 5.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 260 MTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQrFMTDgvAASKFSeiQEPE 339
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQ-HLLD--FPRRKS--GPPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 340 AIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGyTIREVLKGC-NVLCATPGRLHDLIGRGKIGLSKVRYLVLD 418
Cdd:PRK11192 76 ILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYM-NHAEVFSENqDIVVATPGRLLQYIKEENFDCRAVETLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 419 EADRMLDMGFEPEMRKLVASpgmpSKEERQTLMFSATYP-EDIQRMAADFLKvDYIFLAVgvvggACSDVEQT-IVQV-- 494
Cdd:PRK11192 155 EADRMLDMGFAQDIETIAAE----TRWRKQTLLFSATLEgDAVQDFAERLLN-DPVEVEA-----EPSRRERKkIHQWyy 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 495 ---DQYSKRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSV 571
Cdd:PRK11192 225 radDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDV 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1207108023 572 AARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSF 615
Cdd:PRK11192 305 AARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
271-475 |
2.65e-83 |
|
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: 261.61 E-value: 2.65e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 271 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKfseiqEPEAIIVAPTRELI 350
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGR-----GPQALVLAPTRELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 351 NQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEP 430
Cdd:cd00268 76 MQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1207108023 431 EMRKLVASpgMPSKeeRQTLMFSATYPEDIQRMAADFLKvDYIFL 475
Cdd:cd00268 156 DVEKILSA--LPKD--RQTLLFSATLPEEVKELAKKFLK-NPVRI 195
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
242-615 |
4.22e-80 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 262.93 E-value: 4.22e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 242 KYDDILVDvsgsnPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQR 321
Cdd:PRK01297 74 KLEDFVVE-----PQEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 322 FMTDGVAASKFseIQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREV-LKGCNVLCATPGRLHD 400
Cdd:PRK01297 149 LLQTPPPKERY--MGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 401 LIGRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgMPSKEERQTLMFSATYPEDIQRMAADFLkVDYIFLAVGVV 480
Cdd:PRK01297 227 FNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQ--TPRKEERQTLLFSATFTDDVMNLAKQWT-TDPAIVEIEPE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 481 GGACSDVEQTIVQVDQYSKRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRL 560
Cdd:PRK01297 304 NVASDTVEQHVYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFRE 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1207108023 561 GQCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSF 615
Cdd:PRK01297 384 GKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
253-615 |
1.13e-72 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 246.02 E-value: 1.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 253 SNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKF 332
Cdd:PRK04537 2 SDKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 333 SEiqEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTiREVL-KGCNVLCATPGRLHDLIGRGKI-GLS 410
Cdd:PRK04537 82 PE--DPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQ-RELLqQGVDVIIATPGRLIDYVKQHKVvSLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 411 KVRYLVLDEADRMLDMGFEPEMRKLVASpgMPSKEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGACSDVEQT 490
Cdd:PRK04537 159 ACEICVLDEADRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMN-EPEKLVVETETITAARVRQR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 491 IVQVDQYSKRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATS 570
Cdd:PRK04537 236 IYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATD 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1207108023 571 VAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSF 615
Cdd:PRK04537 316 VAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
260-615 |
1.34e-70 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 242.06 E-value: 1.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 260 MTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMtdgvaaskfSEIQEPE 339
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD---------PELKAPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 340 AIIVAPTRELINQIYLEARKFA-YGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLD 418
Cdd:PRK11634 77 ILVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 419 EADRMLDMGFEPEMRKLVASpgMPskEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGACSDVEQTIVQVDQYS 498
Cdd:PRK11634 157 EADEMLRMGFIEDVETIMAQ--IP--EGHQTALFSATMPEAIRRITRRFMK-EPQEVRIQSSVTTRPDISQSYWTVWGMR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 499 KRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSVAARGLDI 578
Cdd:PRK11634 232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311
|
330 340 350
....*....|....*....|....*....|....*..
gi 1207108023 579 EQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSF 615
Cdd:PRK11634 312 ERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
262-615 |
3.27e-70 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 235.25 E-value: 3.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 262 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDgvAASKFSEIQEPEAI 341
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSH--PAPEDRKVNQPRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 342 IVAPTRELINQIYLEARKFAYGTCVRPVVVYGGinTGYTI-REVL-KGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDE 419
Cdd:PRK04837 88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGG--DGYDKqLKVLeSGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 420 ADRMLDMGFEPEMRKLVASpgMPSKEERQTLMFSATYPEDIQRMAADFLkvdyiflavgvvggacSDVEQTIVQVDQ--- 496
Cdd:PRK04837 166 ADRMFDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHM----------------NNPEYVEVEPEQktg 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 497 --------Y-SKRDQ---LLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCP 564
Cdd:PRK04837 228 hrikeelfYpSNEEKmrlLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLD 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1207108023 565 VLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSF 615
Cdd:PRK04837 308 ILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
273-475 |
4.69e-66 |
|
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: 216.08 E-value: 4.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 273 KNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIL-----QRFMTDGvaaskfseiQEPEAIIVAPTR 347
Cdd:cd17966 3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaQPPLERG---------DGPIVLVLAPTR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 348 ELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMG 427
Cdd:cd17966 74 ELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207108023 428 FEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLKvDYIFL 475
Cdd:cd17966 154 FEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRRLAEDFLK-DYIQV 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
250-469 |
4.57e-61 |
|
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: 203.76 E-value: 4.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 250 VSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIL-----QRFMT 324
Cdd:cd17953 2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhikdQRPVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 325 DGvaaskfseiQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIG- 403
Cdd:cd17953 82 PG---------EGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTa 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207108023 404 -RGKI-GLSKVRYLVLDEADRMLDMGFEPEMRKLVaspgMPSKEERQTLMFSATYPEDIQRMAADFLK 469
Cdd:cd17953 153 nNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIV----NNIRPDRQTVLFSATFPRKVEALARKVLH 216
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
271-468 |
1.32e-60 |
|
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: 201.87 E-value: 1.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 271 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMtdgvaASKFSEIQE-PEAIIVAPTREL 349
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-----DQRELEKGEgPIAVIVAPTREL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 350 INQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFE 429
Cdd:cd17952 76 AQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFE 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207108023 430 PEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFL 468
Cdd:cd17952 156 YQVRSIVGH----VRPDRQTLLFSATFKKKIEQLARDIL 190
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
253-619 |
1.19e-58 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 203.52 E-value: 1.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 253 SNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAAskf 332
Cdd:PTZ00424 21 SNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNAC--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 333 seiqepEAIIVAPTRELINQI---------YLEARKFAygtCVrpvvvyGGINTGYTIREVLKGCNVLCATPGRLHDLIG 403
Cdd:PTZ00424 98 ------QALILAPTRELAQQIqkvvlalgdYLKVRCHA---CV------GGTVVRDDINKLKAGVHMVVGTPGRVYDMID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 404 RGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgMPSkeERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGVVGGA 483
Cdd:PTZ00424 163 KRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKK--LPP--DVQVALFSATMPNEILELTTKFMR-DPKRILVKKDELT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 484 CSDVEQTIVQVDQYS-KRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQ 562
Cdd:PTZ00424 238 LEGIRQFYVAVEKEEwKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGS 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207108023 563 CPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPE 619
Cdd:PTZ00424 318 TRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPD 374
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
487-616 |
6.46e-58 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 191.95 E-value: 6.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 487 VEQTIVQVDQYSKRDQLL-ELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPV 565
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1207108023 566 LVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFF 616
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
248-478 |
1.35e-57 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 195.23 E-value: 1.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 248 VDVSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIL-----QRF 322
Cdd:cd18049 12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIvhinhQPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 323 MTDGvaaskfseiQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLI 402
Cdd:cd18049 92 LERG---------DGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207108023 403 GRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVG 478
Cdd:cd18049 163 EAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRQLAEDFLK-DYIHINIG 233
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
275-469 |
3.41e-57 |
|
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: 193.31 E-value: 3.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 275 VSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRfMTDGVAASKFSEIQEPEAIIVAPTRELINQIY 354
Cdd:cd17945 5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVY-ISRLPPLDEETKDDGPYALILAPTRELAQQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 355 LEARKFAYGTCVRPVVVYGGIN---TGYTIRevlKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPE 431
Cdd:cd17945 84 EETQKFAKPLGIRVVSIVGGHSieeQAFSLR---NGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207108023 432 MRKLVASpgMPS------------------KEERQTLMFSATYPEDIQRMAADFLK 469
Cdd:cd17945 161 VTKILDA--MPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLR 214
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
271-478 |
5.92e-57 |
|
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: 192.03 E-value: 5.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 271 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAAskfseiqEPEAIIVAPTRELI 350
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK-------GLRALILAPTRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 351 NQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVL-KGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFE 429
Cdd:cd17957 74 SQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSiTKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207108023 430 PEMRKLVASPGMPSKeerQTLMFSATYPEDIQRMAADFLKvDYIFLAVG 478
Cdd:cd17957 154 EQTDEILAACTNPNL---QRSLFSATIPSEVEELARSVMK-DPIRIIVG 198
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
284-462 |
6.84e-57 |
|
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: 190.53 E-value: 6.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 284 TPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAaskfseiqePEAIIVAPTRELINQIYLEARKFAYG 363
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG---------PQALVLAPTRELAEQIYEELKKLGKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 364 TCVRPVVVYGGINTGYtIREVLKGCNVLCATPGRLHDLIGRGKiGLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgMPs 443
Cdd:pfam00270 72 LGLKVASLLGGDSRKE-QLEKLKGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LP- 146
|
170
....*....|....*....
gi 1207108023 444 kEERQTLMFSATYPEDIQR 462
Cdd:pfam00270 147 -KKRQILLLSATLPRNLED 164
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
269-475 |
3.32e-55 |
|
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: 187.79 E-value: 3.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 269 DSLSKNVSKSGYVKPTPVQKHGI-PIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKfSEIQepeAIIVAPTR 347
Cdd:cd17964 3 PSLLKALTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRR-SGVS---ALIISPTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 348 ELINQIYLEARKFAYG-TCVRPVVVYGGINTGYTIREVLK-GCNVLCATPGRLHDLIG--RGKIGLSKVRYLVLDEADRM 423
Cdd:cd17964 79 ELALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207108023 424 LDMGFEPEMRKLVASPGMPSKEERQTLMFSATYPEDIQRMAADFLKVDYIFL 475
Cdd:cd17964 159 LDMGFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
273-469 |
1.22e-53 |
|
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: 183.05 E-value: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 273 KNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILqrFMTDGVAASKFSEIQePEAIIVAPTRELINQ 352
Cdd:cd17958 3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF--IHLDLQPIPREQRNG-PGVLVLTPTRELALQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 353 IYLEARKFAYGTcVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEM 432
Cdd:cd17958 80 IEAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207108023 433 RKLVaspgMPSKEERQTLMFSATYPEDIQRMAADFLK 469
Cdd:cd17958 159 RKIL----LDIRPDRQTIMTSATWPDGVRRLAQSYLK 191
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
248-478 |
9.20e-53 |
|
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: 183.29 E-value: 9.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 248 VDVSGSNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPIL-----QRF 322
Cdd:cd18050 50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIvhinhQPY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 323 MTDGvaaskfseiQEPEAIIVAPTRELINQIYLEArkFAYGTCVR--PVVVYGGINTGYTIREVLKGCNVLCATPGRLHD 400
Cdd:cd18050 130 LERG---------DGPICLVLAPTRELAQQVQQVA--DDYGKSSRlkSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207108023 401 LIGRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVG 478
Cdd:cd18050 199 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRQLAEDFLR-DYVQINIG 271
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
262-469 |
1.10e-52 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 180.50 E-value: 1.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 262 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAaskfseiqePEAI 341
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYG---------IFAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 342 IVAPTRELINQIyleARKF-AYGTC--VRPVVVYGGINtgyTIREVL---KGCNVLCATPGRLHDLI---GRGKIGLSKV 412
Cdd:cd17955 72 VLTPTRELAYQI---AEQFrALGAPlgLRCCVIVGGMD---MVKQALelsKRPHIVVATPGRLADHLrssDDTTKVLSRV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207108023 413 RYLVLDEADRMLDMGFEPEMRKLVASpgMPSKeeRQTLMFSATYPEDIQRMAADFLK 469
Cdd:cd17955 146 KFLVLDEADRLLTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGN 198
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
275-489 |
1.26e-50 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 174.99 E-value: 1.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 275 VSKSGYVKPTPVQKHGIPIISAG-RDLMACAQTGSGKTAAFLLPILQRFMTDGvaaskfseiqEPEAIIVAPTRELINQI 353
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK----------GGRVLVLVPTRELAEQW 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 354 YLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGC-NVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEM 432
Cdd:smart00487 71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207108023 433 RKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLKvDYIFLAVGvvGGACSDVEQ 489
Cdd:smart00487 151 EKLLKL----LPKNVQLLLLSATPPEEIENLLELFLN-DPVFIDVG--FTPLEPIEQ 200
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
271-469 |
2.56e-50 |
|
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: 173.98 E-value: 2.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 271 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgvaasKFSEIQEPEAIIVAPTRELI 350
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY------RPKKKAATRVLVLVPTRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 351 NQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGK-IGLSKVRYLVLDEADRMLDMGFE 429
Cdd:cd17947 75 MQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1207108023 430 PEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLK 469
Cdd:cd17947 155 DELKEILRL----CPRTRQTMLFSATMTDEVKDLAKLSLN 190
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
261-455 |
3.53e-49 |
|
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: 170.96 E-value: 3.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 261 TFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDgvaASKFSeiqepeA 340
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN---PQRFF------A 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 341 IIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGK-IGLSKVRYLVLDE 419
Cdd:cd17954 72 LVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDE 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207108023 420 ADRMLDMGFEPEMRKLVASpgMPSkeERQTLMFSAT 455
Cdd:cd17954 152 ADRLLNMDFEPEIDKILKV--IPR--ERTTYLFSAT 183
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
271-475 |
3.06e-48 |
|
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: 168.92 E-value: 3.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 271 LSKN-VSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDgvaASKFSEIQEPEAIIVAPTREL 349
Cdd:cd17949 1 LVSHlKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSL---EPRVDRSDGTLALVLVPTREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 350 INQIYLEARKFaygtcVRPV--VVYGGINTGYT-------IRevlKGCNVLCATPGRLHDLIGRGK-IGLSKVRYLVLDE 419
Cdd:cd17949 78 ALQIYEVLEKL-----LKPFhwIVPGYLIGGEKrksekarLR---KGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207108023 420 ADRMLDMGFEPEMRKLV-----------ASPGMPSKeeRQTLMFSATYPEDIQRMaADFLKVDYIFL 475
Cdd:cd17949 150 ADRLLDMGFEKDITKILellddkrskagGEKSKPSR--RQTVLVSATLTDGVKRL-AGLSLKDPVYI 213
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
273-464 |
3.63e-47 |
|
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: 165.59 E-value: 3.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 273 KNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQrFMTDGVAASKFSEIQEPEAIIVAPTRELINQ 352
Cdd:cd17951 3 KGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIM-FALEQEKKLPFIKGEGPYGLIVCPSRELARQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 353 IY---------LEARKFAYgtcVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRM 423
Cdd:cd17951 82 THevieyyckaLQEGGYPQ---LRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207108023 424 LDMGFEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMA 464
Cdd:cd17951 159 IDMGFEEDIRTIFSY----FKGQRQTLLFSATMPKKIQNFA 195
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
261-470 |
4.73e-46 |
|
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: 162.47 E-value: 4.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 261 TFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDgvaaskfSEIQEPEA 340
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAH-------SPTVGARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 341 IIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEA 420
Cdd:cd17959 75 LILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207108023 421 DRMLDMGFEPEMRKLVASpgMPskEERQTLMFSATYPEdiqrMAADFLKV 470
Cdd:cd17959 155 DRLFEMGFAEQLHEILSR--LP--ENRQTLLFSATLPK----LLVEFAKA 196
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
262-469 |
4.85e-46 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 162.47 E-value: 4.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 262 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQrfMTDgvaaSKFSEIQepeAI 341
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILE--KID----PKKDVIQ---AL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 342 IVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEAD 421
Cdd:cd17940 72 ILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEAD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207108023 422 RMLDMGFEPEMRKLVASpgmpSKEERQTLMFSATYPEDIQRMAADFLK 469
Cdd:cd17940 152 KLLSQDFQPIIEKILNF----LPKERQILLFSATFPLTVKNFMDRHMH 195
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
262-465 |
1.99e-44 |
|
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: 158.25 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 262 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMtdgvaaskfseiqepeAI 341
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV----------------AL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 342 IVAPTRELINQIYLEARKFAY---GTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLD 418
Cdd:cd17938 65 ILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207108023 419 EADRMLDMGFEPEMRKLVAS-PGMPSKEER-QTLMFSAT-YPEDIQRMAA 465
Cdd:cd17938 145 EADRLLSQGNLETINRIYNRiPKITSDGKRlQVIVCSATlHSFEVKKLAD 194
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
275-464 |
4.24e-43 |
|
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: 154.27 E-value: 4.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 275 VSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRfMTDGVAASKFSEIQepeAIIVAPTRELINQIY 354
Cdd:cd17960 5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEI-LLKRKANLKKGQVG---ALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 355 LEARKFA--YGTCVRPVVVYGGINTGYTIREVL-KGCNVLCATPGRLHDLIGR--GKIGLSKVRYLVLDEADRMLDMGFE 429
Cdd:cd17960 81 EVLQSFLehHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1207108023 430 PEMRKLVASpgMPskEERQTLMFSATYPEDIQRMA 464
Cdd:cd17960 161 ADLNRILSK--LP--KQRRTGLFSATQTDAVEELI 191
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
273-477 |
3.83e-42 |
|
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: 151.67 E-value: 3.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 273 KNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFM------TDGVAaskfseiqepeAIIVAPT 346
Cdd:cd17941 3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwtpEDGLG-----------ALIISPT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 347 RELINQIYLEARKFAYGTCVRPVVVYGGINTGYTiREVLKGCNVLCATPGR-LHDLIGRGKIGLSKVRYLVLDEADRMLD 425
Cdd:cd17941 72 RELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEE-KERINRMNILVCTPGRlLQHMDETPGFDTSNLQMLVLDEADRILD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207108023 426 MGFEPEMRKLVASpgMPSKeeRQTLMFSATYPEDIQRMAADFLKvDYIFLAV 477
Cdd:cd17941 151 MGFKETLDAIVEN--LPKS--RQTLLFSATQTKSVKDLARLSLK-NPEYISV 197
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
271-469 |
2.66e-41 |
|
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: 149.24 E-value: 2.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 271 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgvaaskfsEIQEPEAIIVAPTRELI 350
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT---------EHRNPSALILTPTRELA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 351 NQIYLEARKFAYGTC-VRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFE 429
Cdd:cd17962 72 VQIEDQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207108023 430 PE-MRKLVASPGMPskeerQTLMFSATYPEDIQRMAADFLK 469
Cdd:cd17962 152 QQvLDILENISHDH-----QTILVSATIPRGIEQLAGQLLQ 187
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
271-461 |
1.18e-39 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 145.84 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 271 LSKNVSKSGYVKPTPVQKHGIP-IISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKFSEIQEPEAIIVAPTREL 349
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 350 INQI--YLEArkFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLS---KVRYLVLDEADRML 424
Cdd:cd17946 81 AVQVkdHLKA--IAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLAnlkSLRFLVLDEADRML 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207108023 425 DMG-FEpEMRKL---VASPGMPSKEERQTLMFSATYPEDIQ 461
Cdd:cd17946 159 EKGhFA-ELEKIlelLNKDRAGKKRKRQTFVFSATLTLDHQ 198
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
271-469 |
1.13e-38 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 141.95 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 271 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgvAASKFSEIQEPEAIIVAPTRELI 350
Cdd:cd17961 5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILK---AKAESGEEQGTRALILVPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 351 NQIYLEARKFAYGTC--VRPVVVYGGINTGyTIREVLKGC-NVLCATPGRLHDLIGRGKIGL-SKVRYLVLDEADRMLDM 426
Cdd:cd17961 82 QQVSKVLEQLTAYCRkdVRVVNLSASSSDS-VQRALLAEKpDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207108023 427 GFEPEMRKLVAS-PGMPskeerQTLMFSATYPEDIQRMAADFLK 469
Cdd:cd17961 161 GYEEDLKSLLSYlPKNY-----QTFLMSATLSEDVEALKKLVLH 199
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
273-475 |
2.60e-38 |
|
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: 140.96 E-value: 2.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 273 KNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRfmtdgVAASKFSEIQEPEAIIVAPTRELINQ 352
Cdd:cd17942 3 KAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEL-----LYKLKFKPRNGTGVIIISPTRELALQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 353 IYLEARKF-AYGTCVRPVVVyGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSK-VRYLVLDEADRMLDMGFEP 430
Cdd:cd17942 78 IYGVAKELlKYHSQTFGIVI-GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGFEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1207108023 431 EMRKLVASpgMPSkeERQTLMFSATYPEDIQRMAADFLKVDYIFL 475
Cdd:cd17942 157 EMRQIIKL--LPK--RRQTMLFSATQTRKVEDLARISLKKKPLYV 197
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
498-607 |
3.92e-38 |
|
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: 136.96 E-value: 3.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 498 SKRDQLLELLRATGNERTMVFVETKRSADfIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSVAARGLD 577
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 1207108023 578 IEQVQHVVNFDMPSSIDEYVHRIGRTGRCG 607
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
273-469 |
1.43e-36 |
|
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: 135.85 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 273 KNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMtdgvaaskfSEIQEPEAIIVAPTRELINQ 352
Cdd:cd17943 3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD---------LERRHPQVLILAPTREIAVQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 353 IYlearkfaygTCVRPVVVY-GGINTGYTI--------REVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRM 423
Cdd:cd17943 74 IH---------DVFKKIGKKlEGLKCEVFIggtpvkedKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207108023 424 LDMGFEPEMRKLVASpgMPSKeeRQTLMFSATYPEDIQRMAADFLK 469
Cdd:cd17943 145 MEGSFQKDVNWIFSS--LPKN--KQVIAFSATYPKNLDNLLARYMR 186
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
262-469 |
5.86e-35 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350708 [Multi-domain] Cd Length: 208 Bit Score: 131.70 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 262 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGvaaskfseiQEPEAI 341
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD---------GQVSVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 342 IVAPTRELINQIYLEARKFA-YGTCVRPVVVYGGINTGYTIrEVLK--GCNVLCATPGRLHDLIGRGKIGLSKVRYLVLD 418
Cdd:cd17950 75 VICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDI-EVLKnkCPHIVVGTPGRILALVREKKLKLSHVKHFVLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207108023 419 EADRMLDmgfEPEMRKLVASPGMPSKEERQTLMFSATYPEDIQRMAADFLK 469
Cdd:cd17950 154 ECDKMLE---QLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQ 201
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
264-468 |
1.08e-33 |
|
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: 127.83 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 264 EAGLCDSLSKNVSKSGYVKPTPVQKHGI-PIISaGRDLMACAQTGSGKTAAFLLPILQRFmtdgvaASKFSEIQepeAII 342
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIvPIIK-GRDVIAQAQSGTGKTATFSIGALQRI------DTTVRETQ---ALV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 343 VAPTRELINQI---------YLEARKFAygtCVrpvvvyGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVR 413
Cdd:cd17939 71 LAPTRELAQQIqkvvkalgdYMGVKVHA---CI------GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIK 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207108023 414 YLVLDEADRMLDMGFEPEMRKLVASpgMPSkeERQTLMFSATYPEDIQRMAADFL 468
Cdd:cd17939 142 MFVLDEADEMLSRGFKDQIYDIFQF--LPP--ETQVVLFSATMPHEVLEVTKKFM 192
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
271-473 |
6.47e-33 |
|
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: 126.71 E-value: 6.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 271 LSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKfsEIQEPEAIIVAPTRELI 350
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEG--PFNAPRGLVITPSRELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 351 NQIYLEARKFAYGTCVRPVVVYGGiNTGYTIRE-VLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFE 429
Cdd:cd17948 79 EQIGSVAQSLTEGLGLKVKVITGG-RTKRQIRNpHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207108023 430 PEMRKL-----VASPGMPSKEER----QTLMFSATYPEDIQRMAADFLKVDYI 473
Cdd:cd17948 158 EKLSHFlrrfpLASRRSENTDGLdpgtQLVLVSATMPSGVGEVLSKVIDVDSI 210
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
262-469 |
1.67e-32 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 124.48 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 262 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgvaaskfsEIQEPEAI 341
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDT---------SLKATQAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 342 IVAPTRELINQI---------YLEARKFAygtCVrpvvvyGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKV 412
Cdd:cd18046 72 VLAPTRELAQQIqkvvmalgdYMGIKCHA---CI------GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207108023 413 RYLVLDEADRMLDMGFEPEMRKLVASpgMPskEERQTLMFSATYPEDIQRMAADFLK 469
Cdd:cd18046 143 KMFVLDEADEMLSRGFKDQIYDIFQK--LP--PDTQVVLLSATMPNDVLEVTTKFMR 195
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
270-469 |
3.00e-32 |
|
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: 123.45 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 270 SLSKNVSKSGYVKPTPVQKHGIPIISAG--RDLMACAQTGSGKTAAFLLPILQRFMTDgvaaskfseIQEPEAIIVAPTR 347
Cdd:cd17963 4 ELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPT---------LKSPQALCLAPTR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 348 ELINQIYLEARKFAYgtcvrpvvvYGGINTGYTIREVLKGCN------VLCATPGRLHDLIGRGKIGLSKVRYLVLDEAD 421
Cdd:cd17963 75 ELARQIGEVVEKMGK---------FTGVKVALAVPGNDVPRGkkitaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEAD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207108023 422 RMLDM-GFEPEMRKLVASPGMPSkeerQTLMFSATYPEDIQRMAADFLK 469
Cdd:cd17963 146 VMLDTqGHGDQSIRIKRMLPRNC----QILLFSATFPDSVRKFAEKIAP 190
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
285-473 |
6.66e-32 |
|
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: 123.03 E-value: 6.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 285 PVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDgvaASKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGT 364
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQED---QQPRKRGRAPKVLVLAPTRELANQVTKDFKDITRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 365 CVrpVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADRMLDMGFEPEMRKLV-ASPGMPS 443
Cdd:cd17944 92 SV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsVSYKKDS 169
|
170 180 190
....*....|....*....|....*....|
gi 1207108023 444 KEERQTLMFSATYPEDIQRMAADFLKVDYI 473
Cdd:cd17944 170 EDNPQTLLFSATCPDWVYNVAKKYMKSQYE 199
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
262-468 |
3.38e-30 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350803 [Multi-domain] Cd Length: 201 Bit Score: 117.95 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 262 FEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgvaaskfsEIQEPEAI 341
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDI---------QVRETQAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 342 IVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEAD 421
Cdd:cd18045 72 ILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEAD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207108023 422 RMLDMGFEPEM----RKLVASPgmpskeerQTLMFSATYPEDIQRMAADFL 468
Cdd:cd18045 152 EMLNKGFKEQIydvyRYLPPAT--------QVVLVSATLPQDILEMTNKFM 194
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
271-475 |
1.36e-28 |
|
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: 114.27 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 271 LSKNVSKSGYVKPTPVQKHGIPIISAG---------RDLMACAQTGSGKTAAFLLPILQRFMTDGVAaskfsEIQepeAI 341
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVP-----RLR---AL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 342 IVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYTIREVLKGC--------NVLCATPGRLHDLIgRGKIG--LSK 411
Cdd:cd17956 73 IVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDHL-NSTPGftLKH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 412 VRYLVLDEADRMLDMGFEPEMRKLVASPGMPSKEER----------------QTLMFSATYPEDIQRMAAdfLKVDYIFL 475
Cdd:cd17956 152 LRFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLgsfgdanllersvrplQKLLFSATLTRDPEKLSS--LKLHRPRL 229
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
526-607 |
3.65e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 108.07 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 526 DFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGR 605
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1207108023 606 CG 607
Cdd:smart00490 81 AG 82
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
271-467 |
2.72e-21 |
|
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: 93.60 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 271 LSKNVSKSGYVKPTPVQKHGIPIISAGR----------------DLMACAQTGSGKTAAFLLPILQRFMTDGVAASKFSE 334
Cdd:cd17965 19 LKGSNKTDEEIKPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPFEEAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 335 IQE--------PEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVYGGINTGYtIREVL---KGCNVLCATPGRLHDLIG 403
Cdd:cd17965 99 EEYesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSY-QRLQLafkGRIDILVTTPGKLASLAK 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207108023 404 -RGKIgLSKVRYLVLDEADRMLDMGFEPEMRKLVASpgMPSKeeRQTLMFSATYPEDIQRMAADF 467
Cdd:cd17965 178 sRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APKL--KHLILCSATIPKEFDKTLRKL 237
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
295-617 |
1.63e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 95.86 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 295 SAGRDLMACAQTGSGKTAAFLLpILQRFMTDGVAaskfseiqepeaIIVAPTRELINQIYLEARKFaygtcvrpvvvYGG 374
Cdd:COG1061 98 RGGGRGLVVAPTGTGKTVLALA-LAAELLRGKRV------------LVLVPRRELLEQWAEELRRF-----------LGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 375 INTGYTIREVlkGCNVLCATPGRLHDLIGRGKIGlSKVRYLVLDEA--------DRMLDMgFEPemRKLV---ASPG-MP 442
Cdd:COG1061 154 PLAGGGKKDS--DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAhhagapsyRRILEA-FPA--AYRLgltATPFrSD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 443 SKEERQTLMFSATYPEDIQRMAADFLKVDYIFLAVGV-------VGGACSDVEQTIVQVDQYSKRDQLLELLRATGN-ER 514
Cdd:COG1061 228 GREILLFLFDGIVYEYSLKEAIEDGYLAPPEYYGIRVdltderaEYDALSERLREALAADAERKDKILRELLREHPDdRK 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 515 TMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSVAARGLDIEQVQHVVNFDMPSSID 594
Cdd:COG1061 308 TLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPR 387
|
330 340
....*....|....*....|...
gi 1207108023 595 EYVHRIGRTGRCGNTGRAVSFFN 617
Cdd:COG1061 388 EFIQRLGRGLRPAPGKEDALVYD 410
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
253-464 |
3.50e-19 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 87.00 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 253 SNPPKAIMTFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAG--RDLMACAQTGSGKTAAFLLPILQRfmtdgVAAS 330
Cdd:cd18048 11 TSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR-----VDAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 331 KfseiQEPEAIIVAPTRELINQ---IYLEARKFaygtCVrpvvvygGINTGYTIR--EVLKGCN----VLCATPGRLHDL 401
Cdd:cd18048 86 K----LYPQCLCLSPTFELALQtgkVVEEMGKF----CV-------GIQVIYAIRgnRPGKGTDieaqIVIGTPGTVLDW 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207108023 402 IGRGK-IGLSKVRYLVLDEADRMLDM-GFEPEMRKLVASpgMPSkeERQTLMFSATYPEDIQRMA 464
Cdd:cd18048 151 CFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKRS--MPK--ECQMLLFSATFEDSVWAFA 211
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
294-619 |
1.87e-18 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 89.04 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 294 ISAGRDLMACAQTGSGKTAAFLLPILqrfMTDGVAaskfseiqepeaIIVAPtreLI----NQI-YLEARKFAygtcvrp 368
Cdd:COG0514 29 VLAGRDALVVMPTGGGKSLCYQLPAL---LLPGLT------------LVVSP---LIalmkDQVdALRAAGIR------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 369 vVVYggIN---TGYTIREVLKGCN-----VLCATPGRL-----HDLIGRGKIGLskvryLVLDEA--------Drmldmg 427
Cdd:COG0514 84 -AAF--LNsslSAEERREVLRALRagelkLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 428 FEPEMRKLV----ASPGMPskeerqTLMFSATYP----EDIQRM--AADFLKVDY------IFLAVgvvggacsdveqti 491
Cdd:COG0514 150 FRPDYRRLGelreRLPNVP------VLALTATATprvrADIAEQlgLEDPRVFVGsfdrpnLRLEV-------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 492 VQVDQYSKRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSv 571
Cdd:COG0514 210 VPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI- 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1207108023 572 aARGL--DIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPE 619
Cdd:COG0514 289 -AFGMgiDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
495-613 |
9.17e-18 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 87.48 E-value: 9.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 495 DQYSKRDQLLELLRAT----GNERTMVFVETKRSADFIATFLCQEKISTTSIHG--DRE------QREREKALSDFRLGQ 562
Cdd:COG1111 332 IEHPKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGE 411
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207108023 563 CPVLVATSVAARGLDIEQVQHVVNFD-MPSSIdEYVHRIGRTGRcGNTGRAV 613
Cdd:COG1111 412 FNVLVATSVAEEGLDIPEVDLVIFYEpVPSEI-RSIQRKGRTGR-KREGRVV 461
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
499-613 |
1.58e-14 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 77.22 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 499 KRDQLLELLRAT----GNERTMVFVETKRSADFIATFLCQEKIST------TSIHGDR--EQREREKALSDFRLGQCPVL 566
Cdd:PRK13766 348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1207108023 567 VATSVAARGLDIEQVQHVVNFD-MPSSIdEYVHRIGRTGRcGNTGRAV 613
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
499-613 |
4.25e-14 |
|
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: 70.08 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 499 KRDQLLELLR-------ATGNERTMVFVETKRSADFIATFLCQEK--------ISTTSIHGDR--EQREREKALSDFRLG 561
Cdd:cd18801 10 KLEKLEEIVKehfkkkqEGSDTRVIIFSEFRDSAEEIVNFLSKIRpgiratrfIGQASGKSSKgmSQKEQKEVIEQFRKG 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207108023 562 QCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRcGNTGRAV 613
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVV 140
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
497-602 |
3.71e-13 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 67.23 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 497 YSKRDQLLELLRA----TGNERTMVFVETKRSADFIATFLCQEKISTTSIHGD---------------REQREREKALSD 557
Cdd:cd18802 6 IPKLQKLIEILREyfpkTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDK 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1207108023 558 FRLGQCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGR 602
Cdd:cd18802 86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
264-613 |
2.08e-12 |
|
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: 70.63 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 264 EAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGVAAskfseiqepeAIIV 343
Cdd:COG1205 38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGAT----------ALYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 344 APTRELINQIYLEARKFA--YGTCVRPVVVYGGinTGYTIR-EVLKGCNVLCATPGRLHDLI--GRGKIG--LSKVRYLV 416
Cdd:COG1205 108 YPTKALARDQLRRLRELAeaLGLGVRVATYDGD--TPPEERrWIREHPDIVLTNPDMLHYGLlpHHTRWArfFRNLRYVV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 417 LDEA---------------DRMLDMgfepeMRKLVASPgmpskeerQTLMFSATY--PEDiqrMAADFLKVDyiFLAVGV 479
Cdd:COG1205 186 IDEAhtyrgvfgshvanvlRRLRRI-----CRHYGSDP--------QFILASATIgnPAE---HAERLTGRP--VTVVDE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 480 VGGACSdvEQTIV-----QVDQYSKRDQLLE----LLRATGNE-RTMVFVETKRSADFIATFL---CQEKISTTSIHGDR 546
Cdd:COG1205 248 DGSPRG--ERTFVlwnppLVDDGIRRSALAEaarlLADLVREGlRTLVFTRSRRGAELLARYArraLREPDLADRVAAYR 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207108023 547 ------EQREREKALSDfrlGQCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAV 613
Cdd:COG1205 326 agylpeERREIERGLRS---GELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
275-605 |
4.84e-12 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 68.77 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 275 VSKSGYVKPTPVQKHGIP-IISAGRDLMACAQTGSGKTAAFLLPILQRFMTDGvaaskfseiqepEAIIVAPTRELINQI 353
Cdd:COG1204 15 LKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------KALYIVPLRALASEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 354 YLEARKF--AYGtcVRPVVVYGGINTGytiREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEA----------- 420
Cdd:COG1204 83 YREFKRDfeELG--IKVGVSTGDYDSD---DEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddesrgpt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 421 -----DRMLDMGfePEMRKLVASPGMPSkeerqtlmfsatyPEDIQR-MAADFLKVDY--IFLAVGVVggacsdVEQTIV 492
Cdd:COG1204 158 levllARLRRLN--PEAQIVALSATIGN-------------AEEIAEwLDAELVKSDWrpVPLNEGVL------YDGVLR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 493 QVDQYSK-RDQLLELLRAT--GNERTMVFVETKRSA-----------------------DFIATFL--CQEKISTTSI-- 542
Cdd:COG1204 217 FDDGSRRsKDPTLALALDLleEGGQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELleVSEETHTNEKla 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 543 ----------HGD--REQRER-EKAlsdFRLGQCPVLVATSVAARGL----------DIEQvqhvvNFDMPSSIDEYVHR 599
Cdd:COG1204 297 dclekgvafhHAGlpSELRRLvEDA---FREGLIKVLVATPTLAAGVnlparrviirDTKR-----GGMVPIPVLEFKQM 368
|
....*.
gi 1207108023 600 IGRTGR 605
Cdd:COG1204 369 AGRAGR 374
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
498-601 |
6.05e-12 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 63.26 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 498 SKRDQLLELLRA--TGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDF-RLGQCPV-LVATSVAA 573
Cdd:cd18793 11 GKLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnEDPDIRVfLLSTKAGG 90
|
90 100 110
....*....|....*....|....*....|....
gi 1207108023 574 RGLDIEQVQHVVNFDMP--SSIDEY----VHRIG 601
Cdd:cd18793 91 VGLNLTAANRVILYDPWwnPAVEEQaidrAHRIG 124
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
261-464 |
8.36e-12 |
|
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: 65.13 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 261 TFEEAGLCDSLSKNVSKSGYVKPTPVQKHGIPIISAG--RDLMACAQTGSGKTAAFLLPILQRFMtdgvAASKFSeiqep 338
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE----PANKYP----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 339 EAIIVAPTRELINQ---IYLEARKFAYGTCVRPVVVYGGINTGYTIREvlkgcNVLCATPGRLHDLIGRGK-IGLSKVRY 414
Cdd:cd18047 73 QCLCLSPTYELALQtgkVIEQMGKFYPELKLAYAVRGNKLERGQKISE-----QIVIGTPGTVLDWCSKLKfIDPKKIKV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207108023 415 LVLDEADRMldmgfepemrklVASPGMPSKEER---------QTLMFSATYPEDIQRMA 464
Cdd:cd18047 148 FVLDEADVM------------IATQGHQDQSIRiqrmlprncQMLLFSATFEDSVWKFA 194
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
495-616 |
1.16e-11 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 62.61 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 495 DQYSKRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSVAAR 574
Cdd:cd18794 13 KKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGM 92
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207108023 575 GLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFF 616
Cdd:cd18794 93 GIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
293-420 |
2.06e-11 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 63.05 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 293 IISAGRDLMACAQTGSGKTAAFLLPILQRFMTdgvaaskfseiQEPEAIIVAPTRELINQIYLEARKFAYGTCVRPVVVY 372
Cdd:cd17921 13 LYLSGDSVLVSAPTSSGKTLIAELAILRALAT-----------SGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLT 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1207108023 373 GGINTGytiREVLKGCNVLCATPGRLHDLIGRGKI-GLSKVRYLVLDEA 420
Cdd:cd17921 82 GDPSVN---KLLLAEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
297-435 |
2.69e-10 |
|
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: 58.95 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 297 GRDLMACAQTGSGKTAAFLLPILQRFmtdgvaaskfsEIQEPEAIIVAPTRELINQIYLEARKFAygtcvRPVVVYGGIN 376
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLL-----------LKKGKKVLVLVPTKALALQTAERLRELF-----GPGIRVAVLV 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207108023 377 TGYTIREVLKGCN----VLCATPGRLHDLIGR-GKIGLSKVRYLVLDEADRMLDMGFEPEMRKL 435
Cdd:cd00046 65 GGSSAEEREKNKLgdadIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDL 128
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
498-603 |
9.87e-10 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 61.78 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 498 SKRDQLLELLR--ATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQ-CPV-LVATSVAA 573
Cdd:COG0553 533 AKLEALLELLEelLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVfLISLKAGG 612
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207108023 574 RGLDIEQVQHVVNFDMP-------SSIDEyVHRIGRT 603
Cdd:COG0553 613 EGLNLTAADHVIHYDLWwnpaveeQAIDR-AHRIGQT 648
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
283-613 |
1.76e-09 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 61.27 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 283 PTPVQKHGIPIISAGRDLMACAQTGSGKT-AAFlLPILQRFMTDGVAASKFSEIQepeAIIVAPTRELINQIY------L 355
Cdd:COG1201 25 PTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGLR---VLYISPLKALANDIErnlrapL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 356 EARKFAYGTCVRPVVVygGINTGYT-----IREVLKGCNVLCATPGRLHDLIG--RGKIGLSKVRYLVLDE----AD--R 422
Cdd:COG1201 101 EEIGEAAGLPLPEIRV--GVRTGDTpaserQRQRRRPPHILITTPESLALLLTspDARELLRGVRTVIVDEihalAGskR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 423 --MLDMGFEpEMRKLVASP----GMpskeerqtlmfSATY--PEDiqrmAADFLkvdyiflavgvvGGACSDVEQTIVQV 494
Cdd:COG1201 179 gvHLALSLE-RLRALAPRPlqriGL-----------SATVgpLEE----VARFL------------VGYEDPRPVTIVDA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 495 DqYSKR---------------------------DQLLELLRATGNerTMVFVETKRSADFIATFLCQEKISTTSI----H 543
Cdd:COG1201 231 G-AGKKpdlevlvpvedlierfpwaghlwphlyPRVLDLIEAHRT--TLVFTNTRSQAERLFQRLNELNPEDALPiaahH 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207108023 544 G--DREQRER-EKALSDfrlGQCPVLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTG-RCGNTGRAV 613
Cdd:COG1201 308 GslSREQRLEvEEALKA---GELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEVSKGR 378
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
294-420 |
4.49e-09 |
|
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: 56.44 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 294 ISAGRDLMACAQTGSGKTAAFLLPILQRFMTDgvaaskfseiQEPEAIIVAPTRELINQIYLEARKFAYGtCVRPVVV-- 371
Cdd:cd17923 12 ARAGRSVVVTTGTASGKSLCYQLPILEALLRD----------PGSRALYLYPTKALAQDQLRSLRELLEQ-LGLGIRVat 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1207108023 372 YGGiNTGYTIREVL--KGCNVLCATPGRLHDLIGRGKIG----LSKVRYLVLDEA 420
Cdd:cd17923 81 YDG-DTPREERRAIirNPPRILLTNPDMLHYALLPHHDRwarfLRNLRYVVLDEA 134
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
494-639 |
5.78e-09 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 59.34 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 494 VDQYSKRDQLLELLRATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSVAA 573
Cdd:PRK11057 218 VEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFG 297
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207108023 574 RGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFNPESDTPLARSLVKVLSGAQQVV 639
Cdd:PRK11057 298 MGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDI 363
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
565-617 |
1.28e-07 |
|
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: 49.24 E-value: 1.28e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1207108023 565 VLVATSVAARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGRCGNTGRAVSFFN 617
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
498-613 |
3.53e-07 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 50.71 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 498 SKRDQLLELL-----RATGNERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSVA 572
Cdd:cd18790 8 PTEGQVDDLLgeirkRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLL 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1207108023 573 ARGLDIEQVQHVVNFD-----MPSSIDEYVHRIGRTGRCGNtGRAV 613
Cdd:cd18790 88 REGLDLPEVSLVAILDadkegFLRSETSLIQTIGRAARNVN-GKVI 132
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
501-605 |
4.78e-07 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 49.96 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 501 DQLLELLRATGNerTMVFVETKRSADFIAT---FLCQEKISTTSI---HG--DREQRER-EKALSDFRLgqcPVLVATSV 571
Cdd:cd18796 29 AEVIFLLERHKS--TLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAALKRGDL---KVVVATSS 103
|
90 100 110
....*....|....*....|....*....|....
gi 1207108023 572 AARGLDIEQVQHVVNFDMPSSIDEYVHRIGRTGR 605
Cdd:cd18796 104 LELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
282-455 |
4.79e-07 |
|
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: 50.49 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 282 KPTPVQKHGI-PIISA-----GRDLMACAQTGSGKTAAFLLPILqrfmtDGVAASKfseiqepEAIIVAPTRELINQIYL 355
Cdd:cd17918 15 SLTKDQAQAIkDIEKDlhspePMDRLLSGDVGSGKTLVALGAAL-----LAYKNGK-------QVAILVPTEILAHQHYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 356 EARKFaygtcvrpvvvYGGIN----TGYTIREVLKGCNVLCATPGRLHDLIGRGKIGLskvryLVLDEADRmldmgFEPE 431
Cdd:cd17918 83 EARKF-----------LPFINvelvTGGTKAQILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHR-----FGVA 141
|
170 180
....*....|....*....|....
gi 1207108023 432 MRKLVASPGMPSkeerqTLMFSAT 455
Cdd:cd17918 142 QREALYNLGATH-----FLEATAT 160
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
513-602 |
6.50e-06 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 45.63 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 513 ERTMVFVETKRSADFIATFLCQEKISTTSIHGDREQREREKA---LSDFRLGQCPVLVATSVAARGLDIEQVQHVVnFDM 589
Cdd:cd18799 7 IKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV-FLR 85
|
90
....*....|....*
gi 1207108023 590 P--SSIdEYVHRIGR 602
Cdd:cd18799 86 PteSRT-LFLQMLGR 99
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
297-419 |
8.00e-06 |
|
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: 46.42 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 297 GRDLMACAQTGSGKTAAFLLPILQRFMTDGVAASKfseiqepeAIIVAPTRELINQIYLEARKFAYGTCV-RPVVVYGGI 375
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ--------VLYISPLKALINDQERRLEEPLDEIDLeIPVAVRHGD 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207108023 376 NTGYTIREVLKGC-NVLCATPGRLHDLIGRGKIG--LSKVRYLVLDE 419
Cdd:cd17922 73 TSQSEKAKQLKNPpGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
298-420 |
4.97e-05 |
|
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: 44.95 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 298 RDLMACAQTGSGKT--AAFLLPILqrfmtdgvaASKFSEIQEPEAIIV--APTRELINQIYLEARKFaygTCVRPVVVYG 373
Cdd:cd18034 17 RNTIVVLPTGSGKTliAVMLIKEM---------GELNRKEKNPKKRAVflVPTVPLVAQQAEAIRSH---TDLKVGEYSG 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1207108023 374 GINTGYTIREVLKGC----NVLCATPGRLHDLIGRGKIGLSKVRYLVLDEA 420
Cdd:cd18034 85 EMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
277-354 |
7.31e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 46.03 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 277 KSGYVKPTPVQKHGIPIISAGRDLMACAQTGSGKT-AAFLLPI---LQRFMTDGVAASKFseiqepeAIIVAPTRELINQ 352
Cdd:PRK13767 27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAIIdelFRLGREGELEDKVY-------CLYVSPLRALNND 99
|
..
gi 1207108023 353 IY 354
Cdd:PRK13767 100 IH 101
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
301-440 |
5.90e-04 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 41.35 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 301 MACAQTGSGKTAAFLLPILQRFMTDGvaaskfseiqePEAIIVAPTRELINQIYLEARKFAygTCVRPVVVYGGINTGYT 380
Cdd:cd18035 20 LIVLPTGLGKTIIAILVAADRLTKKG-----------GKVLILAPSRPLVEQHAENLKRVL--NIPDKITSLTGEVKPEE 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207108023 381 IREVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDEADR--------MLDMGFEPEMRK-----LVASPG 440
Cdd:cd18035 87 RAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHHavgnyayvYIAHRYKREANNplilgLTASPG 159
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
297-419 |
5.91e-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: 41.17 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 297 GRDLMACAQTGSGKTAAFLLPILQRFMTDGvaaskfseiqepEAIIVAPTRELINQIYLEARKFaygtcvRPVVVYGGIN 376
Cdd:cd18028 17 GENLLISIPTASGKTLIAEMAMVNTLLEGG------------KALYLVPLRALASEKYEEFKKL------EEIGLKVGIS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1207108023 377 TG-YTIR-EVLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVLDE 419
Cdd:cd18028 79 TGdYDEDdEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE 123
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
298-470 |
7.80e-04 |
|
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: 41.19 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 298 RDLMACAQTGSGKTAAFLLPILQRFMTDGVAASkfseiQEPEAIIVAPTRELINQIYLEAR-KFA-YGTCVRPVVvygGI 375
Cdd:cd18023 18 KNFVVSAPTGSGKTVLFELAILRLLKERNPLPW-----GNRKVVYIAPIKALCSEKYDDWKeKFGpLGLSCAELT---GD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 376 NTGYTIREvLKGCNVLCATPGRLHDLIGRGKIG---LSKVRYLVLDE---------------ADRMLDMGFEPEMRKLVA 437
Cdd:cd18023 90 TEMDDTFE-IQDADIILTTPEKWDSMTRRWRDNgnlVQLVALVLIDEvhiikenrgatlevvVSRMKTLSSSSELRGSTV 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1207108023 438 SPgmpskeeRQTLMFSATYP--EDIqrmaADFLKV 470
Cdd:cd18023 169 RP-------MRFVAVSATIPniEDL----AEWLGD 192
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
511-616 |
1.83e-03 |
|
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: 39.54 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 511 GNERTMVFVETKRSADFIAtflcqEKISTTSIHGDREQREREKALSDFRLGQCPVLVATSVAARGLDIEQ----VQHVVN 586
Cdd:cd18789 48 QGDKIIVFTDNVEALYRYA-----KRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEanvaIQISGH 122
|
90 100 110
....*....|....*....|....*....|
gi 1207108023 587 FdmpSSIDEYVHRIGRTGRCGNTGRAVSFF 616
Cdd:cd18789 123 G---GSRRQEAQRLGRILRPKKGGGKNAFF 149
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
514-608 |
2.04e-03 |
|
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: 39.16 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 514 RTMVFVETKRSADFIATFLCQEKIST----TSIHGDR---EQREREKALSDFRLGQCPVLVATSVAARGLDIEQVQHVVN 586
Cdd:cd18797 37 KTIVFCRSRKLAELLLRYLKARLVEEgplaSKVASYRagyLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
|
90 100
....*....|....*....|..
gi 1207108023 587 FDMPSSIDEYVHRIGRTGRCGN 608
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGK 138
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
306-422 |
3.36e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.81 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207108023 306 TGSGKT--AAFLlpilqrfmtdgvAASKFSEIQEPEAIIVAPTRELINQIYLEARKFAYGTcvrpvVVYGGINTGYTIRE 383
Cdd:pfam04851 32 TGSGKTltAAKL------------IARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNY-----VEIGEIISGDKKDE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207108023 384 VLKGCNVLCATPGRLHDLIGRGKIGLSKVRYLVL--DEADR 422
Cdd:pfam04851 95 SVDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHR 135
|
|
| |
