|
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 ... |
211-474 |
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: 573.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 211 YVPPPPPDNEEAIFAHYQTGINFDKYDTILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG 290
Cdd:cd18052 1 YIPPPPPEDEDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 291 RDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQT 370
Cdd:cd18052 81 RDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 371 GHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFP 450
Cdd:cd18052 161 GHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFP 240
|
250 260
....*....|....*....|....
gi 1985382943 451 EEIQRLSGEFLKPEYLFVAVGQVG 474
Cdd:cd18052 241 EEIQRLAAEFLKEDYLFLTVGRVG 264
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
254-610 |
3.61e-151 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 444.98 E-value: 3.61e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGvtashfreQQEPEC 333
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR--------PRAPQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 334 IIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEA 413
Cdd:COG0513 75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 414 DRMLDMGFGPEMKKLIS-CPgmpskDRRQTLMFSATFPEEIQRLSGEFLKpEYLFVAVGQVGGACSDVQQTVLQVSQYSK 492
Cdd:COG0513 155 DRMLDMGFIEDIERILKlLP-----KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDKRDK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 493 REKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSVAARGLDIE 572
Cdd:COG0513 229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
|
330 340 350
....*....|....*....|....*....|....*...
gi 1985382943 573 KVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 610
Cdd:COG0513 309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT 346
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
254-474 |
1.26e-142 |
|
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: 415.35 E-value: 1.26e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAS-HFREQQEPE 332
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgRGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 333 CIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDE 412
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985382943 413 ADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFPEEIQRLSGEFLKpEYLFVAVGQVG 474
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
141-653 |
1.46e-117 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 362.94 E-value: 1.46e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 141 RGQQSGNVF-ISRRGGFGGPTGDNGSNRSRGFGSKGGYR-GYNEEViAGSGRSSWKSHGKTESGDNQGP----KVTYVPp 214
Cdd:PTZ00110 11 GSVSSGPSNnYNSYGPYPDSSNPYGNYQANHQDNYGGFRpGYGNYS-GGYGGFGMNSYGSSTLGKRLQPidwkSINLVP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 215 pppdNEEAIFAHYQ--TGINFDKYDTILVE-----VSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPII 287
Cdd:PTZ00110 89 ----FEKNFYKEHPevSALSSKEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 288 LAGRDLMACAQTGSGKTAAFLLPILAHmmkdgVTASH-FREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYG 366
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAIVH-----INAQPlLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 367 GTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKLIScpgmPSKDRRQTLMFS 446
Cdd:PTZ00110 240 GVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVS----QIRPDRQTLMWS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 447 ATFPEEIQRLSGEFLKPEYLFVAVGQVG-GACSDVQQTVLQVSQYSKREKLVEILQSIRDE--RTMVFVETKKKADFIAT 523
Cdd:PTZ00110 316 ATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 524 FLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSVAARGLDIEKVQHVINFDLPSTIDEYVHRIGRTGRCGNIG 603
Cdd:PTZ00110 396 ELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKG 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1985382943 604 KAISFFDSiSDSHIAQPLVKVLSDAQQEVPSWLEEIAFSAQGTGFSNPRG 653
Cdd:PTZ00110 476 ASYTFLTP-DKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWG 524
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
233-474 |
1.11e-111 |
|
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: 337.01 E-value: 1.11e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 233 FDKYDTILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPIL 312
Cdd:cd18051 1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 313 AHMMKDG-------VTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILC 385
Cdd:cd18051 81 SQIYEQGpgeslpsESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 386 ATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRRQTLMFSATFPEEIQRLSGEFLKpEY 465
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLD-NY 239
|
....*....
gi 1985382943 466 LFVAVGQVG 474
Cdd:cd18051 240 IFLAVGRVG 248
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
255-609 |
1.84e-100 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 315.59 E-value: 1.84e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 255 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHmmkdgVTASHFREQqepeCI 334
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK-----LDVKRFRVQ----AL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 335 IVAPTRELINQIFLEARKFSYGT-CIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEA 413
Cdd:PRK11776 77 VLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 414 DRMLDMGFGPEMKKLIS-CPGmpskdRRQTLMFSATFPEEIQRLSGEFLKpEYLFVAVGQVGGAcSDVQQTVLQVSQYSK 492
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRqAPA-----RRQTLLFSATYPEGIAAISQRFQR-DPVEVKVESTHDL-PAIEQRFYEVSPDER 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 493 REKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSVAARGLDIE 572
Cdd:PRK11776 230 LPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309
|
330 340 350
....*....|....*....|....*....|....*..
gi 1985382943 573 KVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 609
Cdd:PRK11776 310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLV 346
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
254-608 |
4.83e-89 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 284.91 E-value: 4.83e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashFREQQE--P 331
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLD-------FPRRKSgpP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 332 ECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLD 411
Cdd:PRK11192 75 RILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 412 EADRMLDMGFGPEMKKL-ISCPGmpskdRRQTLMFSATFP-EEIQRLSGEFLK-PEYLfvavgqvggacsdvqqtvlqVS 488
Cdd:PRK11192 155 EADRMLDMGFAQDIETIaAETRW-----RKQTLLFSATLEgDAVQDFAERLLNdPVEV--------------------EA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 489 QYSKREK-------------------LVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALW 549
Cdd:PRK11192 210 EPSRRERkkihqwyyraddlehktalLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIK 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1985382943 550 DFRSGKCPVLVATSVAARGLDIEKVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISF 608
Cdd:PRK11192 290 RLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
238-633 |
1.35e-87 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 283.99 E-value: 1.35e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 238 TILVEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMK 317
Cdd:PLN00206 106 KLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 318 dgVTASHFREQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGK 397
Cdd:PLN00206 186 --IRSGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 398 EKIGLRKVRYLVLDEADRMLDMGFGPEMKKLISCPGMPskdrrQTLMFSATFPEEIQRLSGEFLKpEYLFVAVGQVGGAC 477
Cdd:PLN00206 264 HDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAK-DIILISIGNPNRPN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 478 SDVQQTVLQVSQYSKREKLVEILQSIRDER--TMVFVETKKKADFIAtflcqEKIPTT------SIHGDREQREREEALW 549
Cdd:PLN00206 338 KAVKQLAIWVETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLA-----NAITVVtglkalSIHGEKSMKERREVMK 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 550 DFRSGKCPVLVATSVAARGLDIEKVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFDSiSDSHIAQPLVKVLSDAQ 629
Cdd:PLN00206 413 SFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNE-EDRNLFPELVALLKSSG 491
|
....
gi 1985382943 630 QEVP 633
Cdd:PLN00206 492 AAIP 495
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
253-607 |
3.01e-86 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 278.23 E-value: 3.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 253 LTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtASHFREQQEPE 332
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITR---QPHAKGRRPVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 333 CIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDE 412
Cdd:PRK10590 78 ALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 413 ADRMLDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLSGEFLK-PEYlfVAVGQVGGACSDVQQTVLQVSQYS 491
Cdd:PRK10590 158 ADRMLDMGFIHDIRRVLA--KLPAK--RQNLLFSATFSDDIKALAEKLLHnPLE--IEVARRNTASEQVTQHVHFVDKKR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 492 KREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSVAARGLDI 571
Cdd:PRK10590 232 KRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDI 311
|
330 340 350
....*....|....*....|....*....|....*.
gi 1985382943 572 EKVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAIS 607
Cdd:PRK10590 312 EELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALS 347
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
264-462 |
4.27e-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: 260.84 E-value: 4.27e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 264 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVtashfREQQEPECIIVAPTRELI 343
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-----KKGRGPQALVLAPTRELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 344 NQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGP 423
Cdd:cd00268 76 MQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1985382943 424 EMKKLIS-CPgmpskDRRQTLMFSATFPEEIQRLSGEFLK 462
Cdd:cd00268 156 DVEKILSaLP-----KDRQTLLFSATLPEEVKELAKKFLK 190
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
246-608 |
3.87e-79 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 260.23 E-value: 3.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 246 LDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHF 325
Cdd:PRK01297 80 VEPQEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 326 ReqQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQI-MQGCNILCATPGRLMDIIGKEKIGLRK 404
Cdd:PRK01297 160 M--GEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHLDM 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 405 VRYLVLDEADRMLDMGFGPEMKKLIScpGMPSKDRRQTLMFSATFPEEIQRLSGEFL-KPEYLFVAVGQVggACSDVQQT 483
Cdd:PRK01297 238 VEVMVLDEADRMLDMGFIPQVRQIIR--QTPRKEERQTLLFSATFTDDVMNLAKQWTtDPAIVEIEPENV--ASDTVEQH 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 484 VLQVSQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATS 563
Cdd:PRK01297 314 VYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATD 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1985382943 564 VAARGLDIEKVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISF 608
Cdd:PRK01297 394 VAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
247-608 |
2.72e-75 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 252.95 E-value: 2.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 247 DPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAShfR 326
Cdd:PRK04537 3 DKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALAD--R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 327 EQQEPECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKI-GLRKV 405
Cdd:PRK04537 81 KPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 406 RYLVLDEADRMLDMGFGPEMKKLIScpGMPSKDRRQTLMFSATFPEEIQRLSGEFL-KPEYLFVAVGQVGGAcsDVQQTV 484
Cdd:PRK04537 161 EICVLDEADRMFDLGFIKDIRFLLR--RMPERGTRQTLLFSATLSHRVLELAYEHMnEPEKLVVETETITAA--RVRQRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 485 LQVSQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSV 564
Cdd:PRK04537 237 YFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDV 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1985382943 565 AARGLDIEKVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISF 608
Cdd:PRK04537 317 AARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
268-608 |
1.37e-70 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 236.02 E-value: 1.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 268 IAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvTASHFREQQEPECIIVAPTRELINQIF 347
Cdd:PRK04837 23 LEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSH--PAPEDRKVNQPRALIMAPTRELAVQIH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 348 LEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKK 427
Cdd:PRK04837 101 ADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRW 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 428 LIScpGMPSKDRRQTLMFSATFPEEIQRLSGEFL-KPEYLFVAVGQVGGacSDVQQTVLQVSQYSKREKLVEILQSIRDE 506
Cdd:PRK04837 181 LFR--RMPPANQRLNMLFSATLSYRVRELAFEHMnNPEYVEVEPEQKTG--HRIKEELFYPSNEEKMRLLQTLIEEEWPD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 507 RTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSVAARGLDIEKVQHVINFDLPSTI 586
Cdd:PRK04837 257 RAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDC 336
|
330 340
....*....|....*....|..
gi 1985382943 587 DEYVHRIGRTGRCGNIGKAISF 608
Cdd:PRK04837 337 EDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
254-611 |
9.17e-66 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 228.58 E-value: 9.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILaHMMKDGVTAshfreqqePEC 333
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLL-HNLDPELKA--------PQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 334 IIVAPTRELINQIFLEARKFS-YGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDE 412
Cdd:PRK11634 78 LVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 413 ADRMLDMGFGPEMKKLIScpGMPskDRRQTLMFSATFPEEIQRLSGEFLK-PEYlfVAVGQVGGACSDVQQTVLQVSQYS 491
Cdd:PRK11634 158 ADEMLRMGFIEDVETIMA--QIP--EGHQTALFSATMPEAIRRITRRFMKePQE--VRIQSSVTTRPDISQSYWTVWGMR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 492 KREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSVAARGLDI 571
Cdd:PRK11634 232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1985382943 572 EKVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFDS 611
Cdd:PRK11634 312 ERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVEN 351
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
266-468 |
1.43e-65 |
|
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: 214.93 E-value: 1.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtaSHFREQQEPECIIVAPTRELINQ 345
Cdd:cd17966 3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQ----PPLERGDGPIVLVLAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 346 IFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEM 425
Cdd:cd17966 79 IQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1985382943 426 KKLIScpgmPSKDRRQTLMFSATFPEEIQRLSGEFLKpEYLFV 468
Cdd:cd17966 159 RKIVD----QIRPDRQTLMWSATWPKEVRRLAEDFLK-DYIQV 196
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
277-456 |
7.07e-61 |
|
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: 200.93 E-value: 7.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 277 TPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfrEQQEPECIIVAPTRELINQIFLEARKFSYG 356
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDK---------LDNGPQALVLAPTRELAEQIYEELKKLGKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 357 TCIRPVVIYGGTQTGHSIRQImQGCNILCATPGRLMDIIGKEKiGLRKVRYLVLDEADRMLDMGFGPEMKKLISCpgMPS 436
Cdd:pfam00270 72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR--LPK 147
|
170 180
....*....|....*....|
gi 1985382943 437 KdrRQTLMFSATFPEEIQRL 456
Cdd:pfam00270 148 K--RQILLLSATLPRNLEDL 165
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
264-461 |
2.15e-59 |
|
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: 198.41 E-value: 2.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 264 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtaSHFREQQEPECIIVAPTRELI 343
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ----RELEKGEGPIAVIVAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 344 NQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGP 423
Cdd:cd17952 77 QQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEY 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1985382943 424 EMKKLIScpgmPSKDRRQTLMFSATFPEEIQRLSGEFL 461
Cdd:cd17952 157 QVRSIVG----HVRPDRQTLLFSATFKKKIEQLARDIL 190
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
266-468 |
3.11e-59 |
|
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: 198.58 E-value: 3.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 266 KNIAKAGYLKLTPVQKYSIPIILA-GRDLMACAQTGSGKTAAFLLPILAHMMKDgvtasHFREQQEP-ECIIVAPTRELI 343
Cdd:cd17964 7 KALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNT-----KPAGRRSGvSALIISPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 344 NQIFLEARKF-SYGTCIRPVVIYGGTQTGHSIRQIM-QGCNILCATPGRLMDIIGKEKIG--LRKVRYLVLDEADRMLDM 419
Cdd:cd17964 82 LQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLDM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1985382943 420 GFGPEMKKLISCPGMPSKDRRQTLMFSATFPEEIQRLSGEFLKPEYLFV 468
Cdd:cd17964 162 GFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
480-609 |
4.14e-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: 192.34 E-value: 4.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 480 VQQTVLQVSQYSKREKL-VEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPV 558
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1985382943 559 LVATSVAARGLDIEKVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 609
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
243-462 |
1.08e-57 |
|
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: 194.52 E-value: 1.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 243 VSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMkdgvtA 322
Cdd:cd17953 2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIK-----D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 323 SHFREQQE-PECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDII---GKE 398
Cdd:cd17953 77 QRPVKPGEgPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985382943 399 KIGLRKVRYLVLDEADRMLDMGFGPEMKKLIscpgMPSKDRRQTLMFSATFPEEIQRLSGEFLK 462
Cdd:cd17953 157 VTNLRRVTYVVLDEADRMFDMGFEPQIMKIV----NNIRPDRQTVLFSATFPRKVEALARKVLH 216
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
264-471 |
6.37e-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: 191.65 E-value: 6.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 264 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtashfREQQEPECIIVAPTRELI 343
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP-------RKKKGLRALILAPTRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 344 NQIFLEARKFSYGTCIRPVVIYGGTQTG-HSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFG 422
Cdd:cd17957 74 SQIYRELLKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1985382943 423 PEMKKLI-SCPGmPSKdrrQTLMFSATFPEEIQRLSGEFLKPeYLFVAVG 471
Cdd:cd17957 154 EQTDEILaACTN-PNL---QRSLFSATIPSEVEELARSVMKD-PIRIIVG 198
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
241-471 |
2.32e-56 |
|
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: 191.76 E-value: 2.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 241 VEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHmmkdgV 320
Cdd:cd18049 12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH-----I 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 321 TASHFREQQE-PECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEK 399
Cdd:cd18049 87 NHQPFLERGDgPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985382943 400 IGLRKVRYLVLDEADRMLDMGFGPEMKKLIScpgmPSKDRRQTLMFSATFPEEIQRLSGEFLKpEYLFVAVG 471
Cdd:cd18049 167 TNLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLK-DYIHINIG 233
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
268-462 |
3.84e-56 |
|
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: 190.61 E-value: 3.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 268 IAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMK----DGVTashfrEQQEPECIIVAPTRELI 343
Cdd:cd17945 5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpplDEET-----KDDGPYALILAPTRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 344 NQIFLEARKFSYGTCIRPVVIYGGtqtgHSIR----QIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDM 419
Cdd:cd17945 80 QQIEEETQKFAKPLGIRVVSIVGG----HSIEeqafSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985382943 420 GFGPEMKKLIScpGMPS------------------KDRRQTLMFSATFPEEIQRLSGEFLK 462
Cdd:cd17945 156 GFEPQVTKILD--AMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLR 214
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
254-608 |
6.47e-55 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 193.12 E-value: 6.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAshfreqqepEC 333
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNAC---------QA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 334 IIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEA 413
Cdd:PTZ00424 100 LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 414 DRMLDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLSGEFLK-PEYLFVAVGQVggACSDVQQTVLQVSQYS- 491
Cdd:PTZ00424 180 DEMLSRGFKGQIYDVFK--KLPPD--VQVALFSATMPNEILELTTKFMRdPKRILVKKDEL--TLEGIRQFYVAVEKEEw 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 492 KREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSVAARGLDI 571
Cdd:PTZ00424 254 KFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDV 333
|
330 340 350
....*....|....*....|....*....|....*..
gi 1985382943 572 EKVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISF 608
Cdd:PTZ00424 334 QQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINF 370
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
266-462 |
1.58e-51 |
|
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: 177.27 E-value: 1.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMmkdgVTASHFREQQE-PECIIVAPTRELIN 344
Cdd:cd17958 3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHL----DLQPIPREQRNgPGVLVLTPTRELAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 345 QIFLEARKFSYGTcIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPE 424
Cdd:cd17958 79 QIEAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQ 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1985382943 425 MKKLIscpgMPSKDRRQTLMFSATFPEEIQRLSGEFLK 462
Cdd:cd17958 158 IRKIL----LDIRPDRQTIMTSATWPDGVRRLAQSYLK 191
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
268-468 |
1.67e-51 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 177.30 E-value: 1.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 268 IAKAGYLKLTPVQKYSIPIILAG-RDLMACAQTGSGKTAAFLLPILAHmmkdgvtashFREQQEPECIIVAPTRELINQI 346
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA----------LKRGKGGRVLVLVPTRELAEQW 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 347 FLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGC-NILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEM 425
Cdd:smart00487 71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1985382943 426 KKLIScpgmPSKDRRQTLMFSATFPEEIQRLSGEFLKPEYLFV 468
Cdd:smart00487 151 EKLLK----LLPKNVQLLLLSATPPEEIENLLELFLNDPVFID 189
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
255-468 |
4.03e-51 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 176.26 E-value: 4.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 255 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVtaSHFreqqepeCI 334
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPY--GIF-------AL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 335 IVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQtghSIRQ---IMQGCNILCATPGRLMDII---GKEKIGLRKVRYL 408
Cdd:cd17955 72 VLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMD---MVKQaleLSKRPHIVVATPGRLADHLrssDDTTKVLSRVKFL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 409 VLDEADRMLDMGFGPEMKKLISCpgMPSKdrRQTLMFSATFPEEIQRLSGEFLKPEYLFV 468
Cdd:cd17955 149 VLDEADRLLTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
241-471 |
7.37e-51 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350808 [Multi-domain] Cd Length: 271 Bit Score: 177.90 E-value: 7.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 241 VEVSGLDPPPAILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgv 320
Cdd:cd18050 50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQ-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 321 taSHFREQQEPECIIVAPTRELINQIflEARKFSYGTC--IRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKE 398
Cdd:cd18050 128 --PYLERGDGPICLVLAPTRELAQQV--QQVADDYGKSsrLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAG 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985382943 399 KIGLRKVRYLVLDEADRMLDMGFGPEMKKLIScpgmPSKDRRQTLMFSATFPEEIQRLSGEFLKpEYLFVAVG 471
Cdd:cd18050 204 KTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD----QIRPDRQTLMWSATWPKEVRQLAEDFLR-DYVQINIG 271
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
270-466 |
2.39e-49 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 172.00 E-value: 2.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 270 KAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtASHFREQQEPECIIVAPTRELINQIFLE 349
Cdd:cd17949 8 KMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSL---EPRVDRSDGTLALVLVPTRELALQIYEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 350 ARKF-SYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEK-IGLRKVRYLVLDEADRMLDMGFGPEMKK 427
Cdd:cd17949 85 LEKLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEKDITK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1985382943 428 LIS--------CPGMPSKD-RRQTLMFSATFPEEIQRLSGEFLK-PEYL 466
Cdd:cd17949 165 ILEllddkrskAGGEKSKPsRRQTVLVSATLTDGVKRLAGLSLKdPVYI 213
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
254-451 |
1.65e-48 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 169.41 E-value: 1.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPIL----AHMMKDGVTAshfreqq 329
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIeklkAHSPTVGARA------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 330 epecIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLV 409
Cdd:cd17959 75 ----LILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1985382943 410 LDEADRMLDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPE 451
Cdd:cd17959 151 FDEADRLFEMGFAEQLHEILS--RLPEN--RQTLLFSATLPK 188
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
266-462 |
2.77e-48 |
|
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: 168.20 E-value: 2.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMkdgvtashFREQQEPEC--IIVAPTRELI 343
Cdd:cd17947 3 RALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLL--------YRPKKKAATrvLVLVPTRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 344 NQIFLEARKFSYGTCIRPVVIYGGTqtghSIRQ----IMQGCNILCATPGRLMDIIGKEK-IGLRKVRYLVLDEADRMLD 418
Cdd:cd17947 75 MQCFSVLQQLAQFTDITFALAVGGL----SLKAqeaaLRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1985382943 419 MGFGPEMKKLI-SCPGmpskdRRQTLMFSATFPEEIQRLSGEFLK 462
Cdd:cd17947 151 EGFADELKEILrLCPR-----TRQTMLFSATMTDEVKDLAKLSLN 190
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
254-456 |
3.71e-48 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 168.26 E-value: 3.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtashfreQQEPEC 333
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN---------PQRFFA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 334 IIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEK-IGLRKVRYLVLDE 412
Cdd:cd17954 72 LVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1985382943 413 ADRMLDMGFGPEMKKLISCpgMPSkdRRQTLMFSATFPEEIQRL 456
Cdd:cd17954 152 ADRLLNMDFEPEIDKILKV--IPR--ERTTYLFSATMTTKVAKL 191
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
268-456 |
7.57e-47 |
|
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: 164.67 E-value: 7.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 268 IAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfREQQEPE----CIIVAPTRELI 343
Cdd:cd17960 5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLK--------RKANLKKgqvgALIISPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 344 NQIFLEARKF--SYGTCIRPVVIYGGTQTGHSIRQIM-QGCNILCATPGRLMDIIGKEKiGLRKVR---YLVLDEADRML 417
Cdd:cd17960 77 TQIYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRKA-DKVKVKsleVLVLDEADRLL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1985382943 418 DMGFGPEMKKLISCpgMPsKDRRqTLMFSATFPEEIQRL 456
Cdd:cd17960 156 DLGFEADLNRILSK--LP-KQRR-TGLFSATQTDAVEEL 190
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
266-468 |
2.77e-46 |
|
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: 162.84 E-value: 2.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMmkdgvtashFREQQEPE----CIIVAPTRE 341
Cdd:cd17941 3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL---------YRERWTPEdglgALIISPTRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 342 LINQIFLEARKFSYGTCIRPVVIYGGTQTGHSiRQIMQGCNILCATPGRL---MDiigkEKIGL--RKVRYLVLDEADRM 416
Cdd:cd17941 74 LAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEE-KERINRMNILVCTPGRLlqhMD----ETPGFdtSNLQMLVLDEADRI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1985382943 417 LDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLSGEFLK-PEYLFV 468
Cdd:cd17941 149 LDMGFKETLDAIVE--NLPKS--RQTLLFSATQTKSVKDLARLSLKnPEYISV 197
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
266-468 |
6.52e-45 |
|
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: 159.06 E-value: 6.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmmkDGVTASHFREQQEPECIIVAPTRELINQ 345
Cdd:cd17942 3 KAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI-----ELLYKLKFKPRNGTGVIIISPTRELALQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 346 IFLEARKF------SYGTCIrpvviyGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRK-VRYLVLDEADRMLD 418
Cdd:cd17942 78 IYGVAKELlkyhsqTFGIVI------GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1985382943 419 MGFGPEMKKLISCpgMPSkdRRQTLMFSATFPEEIQRLSGEFLKPEYLFV 468
Cdd:cd17942 152 IGFEEEMRQIIKL--LPK--RRQTMLFSATQTRKVEDLARISLKKKPLYV 197
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
255-465 |
1.05e-44 |
|
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: 158.62 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 255 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPIL--AHMMKDGVTAshfreqqepe 332
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILekIDPKKDVIQA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 333 cIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDE 412
Cdd:cd17940 71 -LILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1985382943 413 ADRMLDMGFGPEMKKLIS-CPgmpskDRRQTLMFSATFPEEIQRLSGEFLKPEY 465
Cdd:cd17940 150 ADKLLSQDFQPIIEKILNfLP-----KERQILLFSATFPLTVKNFMDRHMHNPY 198
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
255-448 |
5.03e-43 |
|
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: 154.02 E-value: 5.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 255 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmmkdgvtashfreqQEPECI 334
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------------QIVVAL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 335 IVAPTRELINQIFLEARKFSY---GTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLD 411
Cdd:cd17938 65 ILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1985382943 412 EADRMLDMGFGPEMKKLIS-CPGMPSKDRR-QTLMFSAT 448
Cdd:cd17938 145 EADRLLSQGNLETINRIYNrIPKITSDGKRlQVIVCSAT 183
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
266-454 |
1.72e-42 |
|
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: 152.88 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAShFREQQEPECIIVAPTRELINQ 345
Cdd:cd17951 3 KGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLP-FIKGEGPYGLIVCPSRELARQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 346 IF---------LEARKFSYgtcIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRM 416
Cdd:cd17951 82 THevieyyckaLQEGGYPQ---LRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1985382943 417 LDMGFGPEMKKLISCpgmpSKDRRQTLMFSATFPEEIQ 454
Cdd:cd17951 159 IDMGFEEDIRTIFSY----FKGQRQTLLFSATMPKKIQ 192
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
264-462 |
1.23e-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: 150.01 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 264 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfrEQQEPECIIVAPTRELI 343
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT---------EHRNPSALILTPTRELA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 344 NQIFLEARKFSYGTC-IRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFG 422
Cdd:cd17962 72 VQIEDQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1985382943 423 PE-MKKLISCPGMPskdrrQTLMFSATFPEEIQRLSGEFLK 462
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 ... |
266-449 |
4.69e-41 |
|
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: 149.70 E-value: 4.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 266 KNIAKAGYLKLTPVQKYSIP-IILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHFREQQEPECIIVAPTRELIN 344
Cdd:cd17946 3 RALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALILTPTRELAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 345 QI---FLEARKFsygTCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGK--EKIG-LRKVRYLVLDEADRMLD 418
Cdd:cd17946 83 QVkdhLKAIAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEgnEHLAnLKSLRFLVLDEADRMLE 159
|
170 180 190
....*....|....*....|....*....|....
gi 1985382943 419 MGFGPEMKKLISC---PGMPSKDRRQTLMFSATF 449
Cdd:cd17946 160 KGHFAELEKILELlnkDRAGKKRKRQTFVFSATL 193
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
491-600 |
2.75e-39 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 140.42 E-value: 2.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 491 SKREKLVEILQSIRDERTMVFVETKKKADfIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSVAARGLD 570
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 1985382943 571 IEKVQHVINFDLPSTIDEYVHRIGRTGRCG 600
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
264-462 |
3.66e-36 |
|
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: 135.02 E-value: 3.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 264 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAshfREQQEPECIIVAPTRELI 343
Cdd:cd17961 5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAES---GEEQGTRALILVPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 344 NQIFLEARKFSYGTC--IRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDII-GKEKIGLRKVRYLVLDEADRMLDMG 420
Cdd:cd17961 82 QQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLeSGSLLLLSTLKYLVIDEADLVLSYG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1985382943 421 FGPEMKKLIScpGMPSkdRRQTLMFSATFPEEIQRLSGEFLK 462
Cdd:cd17961 162 YEEDLKSLLS--YLPK--NYQTFLMSATLSEDVEALKKLVLH 199
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
264-463 |
7.26e-34 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350721 [Multi-domain] Cd Length: 196 Bit Score: 128.08 E-value: 7.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 264 LNKNIAKAGYLKLTPVQKYSIPIILAG--RDLMACAQTGSGKTAAFLLPILAHMmkDgvtashfREQQEPECIIVAPTRE 341
Cdd:cd17963 5 LLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV--D-------PTLKSPQALCLAPTRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 342 LINQIFLEARKFSYGT------CIRPVVIYGGTQ-TGHsirqimqgcnILCATPGRLMDIIGKEKIGLRKVRYLVLDEAD 414
Cdd:cd17963 76 LARQIGEVVEKMGKFTgvkvalAVPGNDVPRGKKiTAQ----------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEAD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1985382943 415 RMLDM-GFGPE---MKKLIscpgmpsKDRRQTLMFSATFPEEIQRLSGEFLKP 463
Cdd:cd17963 146 VMLDTqGHGDQsirIKRML-------PRNCQILLFSATFPDSVRKFAEKIAPN 191
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
266-465 |
9.95e-34 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 128.04 E-value: 9.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDgvtASHFREQQEPECIIVAPTRELINQ 345
Cdd:cd17944 3 KLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQED---QQPRKRGRAPKVLVLAPTRELANQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 346 IFLE----ARKFSYgTCIrpvviYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGF 421
Cdd:cd17944 80 VTKDfkdiTRKLSV-ACF-----YGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGF 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1985382943 422 GPEMKKLISCP-GMPSKDRRQTLMFSATFPEEIQRLSGEFLKPEY 465
Cdd:cd17944 154 AEQVEEILSVSyKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQY 198
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
264-456 |
4.39e-33 |
|
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: 126.98 E-value: 4.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 264 LNKNIAKAGYLKLTPVQKYSIPIILAG---------RDLMACAQTGSGKTAAFLLPILAhMMKDGVtASHFReqqepeCI 334
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQ-ALSKRV-VPRLR------AL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 335 IVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGHSIRQIMQGC--------NILCATPGRLMD-IIGKEKIGLRKV 405
Cdd:cd17956 73 IVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDhLNSTPGFTLKHL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 406 RYLVLDEADRMLDMGFGPEMKKLISCPGMPSKDRR----------------QTLMFSATF---PEEIQRL 456
Cdd:cd17956 153 RFLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLgsfgdanllersvrplQKLLFSATLtrdPEKLSSL 222
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
264-468 |
1.36e-30 |
|
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: 119.37 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 264 LNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILaHMMKDgvtashfrEQQEPECIIVAPTRELI 343
Cdd:cd17950 13 LLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL-QQLEP--------VDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 344 NQIFLEARKFS-YGTCIRPVVIYGGTQTGHSIRQIMQGC-NILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDmgf 421
Cdd:cd17950 84 FQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE--- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1985382943 422 GPEMKKLI-----SCPgmpsKDrRQTLMFSATFPEEIQRLSGEFLK-PEYLFV 468
Cdd:cd17950 161 QLDMRRDVqeifrATP----HD-KQVMMFSATLSKEIRPVCKKFMQdPLEIFV 208
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
267-451 |
1.58e-29 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 117.08 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 267 NIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGVTAShfREQQEPECIIVAPTRELINQI 346
Cdd:cd17948 4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAE--GPFNAPRGLVITPSRELAEQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 347 FLEARKFSYGTCIRPVVIYGgtqtGHSIRQIM----QGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFG 422
Cdd:cd17948 82 GSVAQSLTEGLGLKVKVITG----GRTKRQIRnphfEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1985382943 423 PEMKKLIS-CP--GMPSKDRR------QTLMFSATFPE 451
Cdd:cd17948 158 EKLSHFLRrFPlaSRRSENTDgldpgtQLVLVSATMPS 195
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
257-461 |
3.50e-29 |
|
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: 115.11 E-value: 3.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 257 EANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMkdgvtashfREQQEPECIIV 336
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRID---------TTVRETQALVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 337 APTRELINQI---------FLEARKFsygTCIrpvviyGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRY 407
Cdd:cd17939 72 APTRELAQQIqkvvkalgdYMGVKVH---ACI------GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKM 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1985382943 408 LVLDEADRMLDMGFGPEMKKLISCpgMPSKdrRQTLMFSATFPEEIQRLSGEFL 461
Cdd:cd17939 143 FVLDEADEMLSRGFKDQIYDIFQF--LPPE--TQVVLFSATMPHEVLEVTKKFM 192
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
266-451 |
3.71e-29 |
|
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: 114.67 E-value: 3.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 266 KNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLlpILAHMMKDgvtashfREQQEPECIIVAPTRELINQ 345
Cdd:cd17943 3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFV--VIALESLD-------LERRHPQVLILAPTREIAVQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 346 IFLEARKF-SYGTCIRPVVIYGGTQTGHSiRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPE 424
Cdd:cd17943 74 IHDVFKKIgKKLEGLKCEVFIGGTPVKED-KKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKD 152
|
170 180
....*....|....*....|....*..
gi 1985382943 425 MKKLIScpGMPSkdRRQTLMFSATFPE 451
Cdd:cd17943 153 VNWIFS--SLPK--NKQVIAFSATYPK 175
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
519-600 |
1.69e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 108.84 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 519 DFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSVAARGLDIEKVQHVINFDLPSTIDEYVHRIGRTGR 598
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1985382943 599 CG 600
Cdd:smart00490 81 AG 82
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
255-461 |
4.09e-27 |
|
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: 109.09 E-value: 4.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 255 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILaHMMKDGVtashfreqQEPECI 334
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDIQV--------RETQAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 335 IVAPTRELINQI---FLEARKF---SYGTCIrpvviyGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYL 408
Cdd:cd18045 72 ILSPTRELAVQIqkvLLALGDYmnvQCHACI------GGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKML 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1985382943 409 VLDEADRMLDMGFgpemKKLISCPGMPSKDRRQTLMFSATFPEEIQRLSGEFL 461
Cdd:cd18045 146 VLDEADEMLNKGF----KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFM 194
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
255-462 |
4.41e-26 |
|
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: 105.99 E-value: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 255 FEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashfrEQQEPECI 334
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDT---------SLKATQAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 335 IVAPTRELINQI---------FLEARKFSygtCIrpvviyGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKV 405
Cdd:cd18046 72 VLAPTRELAQQIqkvvmalgdYMGIKCHA---CI------GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1985382943 406 RYLVLDEADRMLDMGFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEIQRLSGEFLK 462
Cdd:cd18046 143 KMFVLDEADEMLSRGFKDQIYDIFQ--KLPPD--TQVVLLSATMPNDVLEVTTKFMR 195
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
241-453 |
1.62e-21 |
|
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: 93.93 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 241 VEVSGLDPPP---AILTFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG--RDLMACAQTGSGKTAAFLLPILAHm 315
Cdd:cd18048 3 VEVLQRDPTSplfSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 316 mkdgVTAshfrEQQEPECIIVAPTRELINQ---IFLEARKFsygtCIRPVVIYG--GTQTGHSIRQIMQgcnILCATPGR 390
Cdd:cd18048 82 ----VDA----LKLYPQCLCLSPTFELALQtgkVVEEMGKF----CVGIQVIYAirGNRPGKGTDIEAQ---IVIGTPGT 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985382943 391 LMDIIGKEK-IGLRKVRYLVLDEADRMLDM-GFGPEMKKLIScpGMPSKdrRQTLMFSATFPEEI 453
Cdd:cd18048 147 VLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKR--SMPKE--CQMLLFSATFEDSV 207
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
266-460 |
2.61e-20 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 90.90 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 266 KNIAKAGYLKL------TPVQKYSIPIILAGR----------------DLMACAQTGSGKTAAFLLPILAHMMKDGVTAS 323
Cdd:cd17965 15 IKEILKGSNKTdeeikpSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 324 HFREQQE--------PECIIVAPTRELINQIFLEARKFSYGTCIRPVVIYGGTQTGH--SIRQIMQGCNILCATPGRLMD 393
Cdd:cd17965 95 EEAEEEYesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYqrLQLAFKGRIDILVTTPGKLAS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985382943 394 IIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKLIScPGMPSKDrrqtLMF-SATFPEEIQRLSGEF 460
Cdd:cd17965 175 LAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIK-RAPKLKH----LILcSATIPKEFDKTLRKL 237
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
489-606 |
4.98e-20 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 94.80 E-value: 4.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 489 QYSKREKLVEILQSIR----DERTMVFVETKKKADFIATFLCQEKIPTTSIHG--DRE------QREREEALWDFRSGKC 556
Cdd:COG1111 333 EHPKLSKLREILKEQLgtnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGEF 412
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1985382943 557 PVLVATSVAARGLDIEKVQHVINFDL-PSTIdEYVHRIGRTGRcGNIGKAI 606
Cdd:COG1111 413 NVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVV 461
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
289-615 |
2.51e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 92.01 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 289 AGRDLMACAQTGSGKTAAFLLpILAHMMKDGVTashfreqqepecIIVAPTRELINQIFLEARKFsygtcirpvviYGGT 368
Cdd:COG1061 99 GGGRGLVVAPTGTGKTVLALA-LAAELLRGKRV------------LVLVPRRELLEQWAEELRRF-----------LGDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 369 QTGHSIRQImqGCNILCATPGRLMDIIGKEKIGlRKVRYLVLDEADRmldmGFGPEMKKLIScpGMPSKDRrqtLMFSAT 448
Cdd:COG1061 155 LAGGGKKDS--DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILE--AFPAAYR---LGLTAT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 449 ------FPEEIQRLSG-------------EFLKP-EYLFVAVG-----QVGGACSDVQQTVLQVSQYSKREKLVEILQSI 503
Cdd:COG1061 223 pfrsdgREILLFLFDGivyeyslkeaiedGYLAPpEYYGIRVDltderAEYDALSERLREALAADAERKDKILRELLREH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 504 RD-ERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSVAARGLDIEKVQHVINFDL 582
Cdd:COG1061 303 PDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRP 382
|
330 340 350
....*....|....*....|....*....|...
gi 1985382943 583 PSTIDEYVHRIGRTGRCGNIGKAISFFDSISDS 615
Cdd:COG1061 383 TGSPREFIQRLGRGLRPAPGKEDALVYDFVGND 415
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
287-610 |
2.12e-18 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 88.66 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 287 ILAGRDLMACAQTGSGKTAAFLLPILahmMKDGVTashfreqqepecIIVAPtreLI----NQI-FLEARKfsygtcIRP 361
Cdd:COG0514 29 VLAGRDALVVMPTGGGKSLCYQLPAL---LLPGLT------------LVVSP---LIalmkDQVdALRAAG------IRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 362 VVIYGgTQTGHSIRQIMQGCN-----ILCATPGRLM-----DIIGKEKIGLrkvryLVLDEA--------DrmldmgFGP 423
Cdd:COG0514 85 AFLNS-SLSAEERREVLRALRagelkLLYVAPERLLnprflELLRRLKISL-----FAIDEAhcisqwghD------FRP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 424 E---MKKLI-SCPGMPskdrrqTLMFSATFPEE-----IQRLSgefLKPEYLFVAvgqvggacS-D---VQQTVLQVSQY 490
Cdd:COG0514 153 DyrrLGELReRLPNVP------VLALTATATPRvradiAEQLG---LEDPRVFVG--------SfDrpnLRLEVVPKPPD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 491 SKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSvaARGLD 570
Cdd:COG0514 216 DKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AFGMG 293
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1985382943 571 IEK--VQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 610
Cdd:COG0514 294 IDKpdVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYG 335
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
490-595 |
2.62e-16 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 76.09 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 490 YSKREKLVEILQSIRDE----RTMVFVETKKKADFIATFLCQEKIPTTSIHGD---------------REQREREEALWD 550
Cdd:cd18802 6 IPKLQKLIEILREYFPKtpdfRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDK 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1985382943 551 FRSGKCPVLVATSVAARGLDIEKVQHVINFDLPSTIDEYVHRIGR 595
Cdd:cd18802 86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
492-606 |
5.41e-15 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 78.76 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 492 KREKLVEILQSI----RDERTMVFVETKKKADFIATFLCQEKIPTTSIHG--DRE------QREREEALWDFRSGKCPVL 559
Cdd:PRK13766 348 KLEKLREIVKEQlgknPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaSKDgdkgmsQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1985382943 560 VATSVAARGLDIEKVQHVINFD-LPSTIdEYVHRIGRTGRcGNIGKAI 606
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVV 473
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
254-457 |
1.16e-14 |
|
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: 73.22 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 254 TFEEANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAG--RDLMACAQTGSGKTAAFLLPILAHMmkDGVTashfreqQEP 331
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPAN-------KYP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 332 ECIIVAPTRELINQ---IFLEARKFSygtcirPVVIYGGTQTGHSI-RQIMQGCNILCATPGRLMDIIGKEK-IGLRKVR 406
Cdd:cd18047 73 QCLCLSPTYELALQtgkVIEQMGKFY------PELKLAYAVRGNKLeRGQKISEQIVIGTPGTVLDWCSKLKfIDPKKIK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1985382943 407 YLVLDEADRMLDMGfGPEMKKLISCPGMPSKdrRQTLMFSATFPEEIQRLS 457
Cdd:cd18047 147 VFVLDEADVMIATQ-GHQDQSIRIQRMLPRN--CQMLLFSATFEDSVWKFA 194
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
257-606 |
9.13e-14 |
|
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: 74.87 E-value: 9.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 257 EANLCQTLNKNIAKAGYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKD-GVTAshfreqqepecII 335
Cdd:COG1205 38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDpGATA-----------LY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 336 VAPTRELIN-QifLEA-RKF--SYGTCIRPVVIYGGTqTGHSIRQIMQGCNILCATPgrlmDII------GKEKIG--LR 403
Cdd:COG1205 107 LYPTKALARdQ--LRRlRELaeALGLGVRVATYDGDT-PPEERRWIREHPDIVLTNP----DMLhygllpHHTRWArfFR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 404 KVRYLVLDEAD--RmldmG-FGPEMKKLIscpgmpskdRR------------QTLMFSATF--PEEI-QRLSGEflkPey 465
Cdd:COG1205 180 NLRYVVIDEAHtyR----GvFGSHVANVL---------RRlrricrhygsdpQFILASATIgnPAEHaERLTGR---P-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 466 lFVAVGQVGGAC---------SDVQQTVLQVSQYSKREKLVEILqSIRDERTMVFVETKKKADFIATFL---CQEKIPTT 533
Cdd:COG1205 242 -VTVVDEDGSPRgertfvlwnPPLVDDGIRRSALAEAARLLADL-VREGLRTLVFTRSRRGAELLARYArraLREPDLAD 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985382943 534 SIHGDR------EQREREEALwdfRSGKCPVLVATSVAARGLDIEKVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAI 606
Cdd:COG1205 320 RVAAYRagylpeERREIERGL---RSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
492-598 |
9.63e-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: 68.92 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 492 KREKLVEIL-------QSIRDERTMVFVETKKKADFIATFLCQEKI---PTTSI-HGDRE------QREREEALWDFRSG 554
Cdd:cd18801 10 KLEKLEEIVkehfkkkQEGSDTRVIIFSEFRDSAEEIVNFLSKIRPgirATRFIgQASGKsskgmsQKEQKEVIEQFRKG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1985382943 555 KCPVLVATSVAARGLDIEKVQHVINFD-LPSTIdEYVHRIGRTGR 598
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
268-563 |
4.79e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 72.24 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 268 IAKAGYLKLTPVQKYSIP-IILAGRDLMACAQTGSGKTAAFLLPILAHMMKDGvtashfreqqepECIIVAPTRELINQI 346
Cdd:COG1204 15 LKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------KALYIVPLRALASEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 347 FLEARKF--SYGtcIRPVVIYGGTQtghSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEAdRML-DMGFGP 423
Cdd:COG1204 83 YREFKRDfeELG--IKVGVSTGDYD---SDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLIdDESRGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 424 --EM---KKLISCPGMpskdrrQTLMFSATF--PEEIQR-LSGEFLKPEYlfVAVGQVGGACSDVQQTVLQVSQYSKREK 495
Cdd:COG1204 157 tlEVllaRLRRLNPEA------QIVALSATIgnAEEIAEwLDAELVKSDW--RPVPLNEGVLYDGVLRFDDGSRRSKDPT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 496 LVEILQSIRDE-RTMVFVETKKKA-----------------------DFIATFLCQEKIPTTSI--------------HG 537
Cdd:COG1204 229 LALALDLLEEGgQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELLEVSEETHTNekladclekgvafhHA 308
|
330 340
....*....|....*....|....*...
gi 1985382943 538 D--REQREREEALwdFRSGKCPVLVATS 563
Cdd:COG1204 309 GlpSELRRLVEDA--FREGLIKVLVATP 334
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
496-609 |
2.25e-12 |
|
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: 64.54 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 496 LVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSvaARGLDIEK-- 573
Cdd:cd18794 21 LKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATV--AFGMGIDKpd 98
|
90 100 110
....*....|....*....|....*....|....*.
gi 1985382943 574 VQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFF 609
Cdd:cd18794 99 VRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
491-594 |
4.68e-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: 63.65 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 491 SKREKLVEILQSIRD--ERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSG-KCPV-LVATSVAA 566
Cdd:cd18793 11 GKLEALLELLEELREpgEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKAGG 90
|
90 100 110
....*....|....*....|....*....|....
gi 1985382943 567 RGLDIEKVQHVINFDLP--STIDEY----VHRIG 594
Cdd:cd18793 91 VGLNLTAANRVILYDPWwnPAVEEQaidrAHRIG 124
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
476-596 |
5.79e-12 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 69.10 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 476 ACSDVQQTVLQVSQY----SKREKLVEILQSI--RDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALW 549
Cdd:COG0553 514 ICSHPALLLEEGAELsgrsAKLEALLELLEELlaEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVD 593
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1985382943 550 DFRSGK-CPV-LVATSVAARGLDIEKVQHVINFDLP-------STIDEyVHRIGRT 596
Cdd:COG0553 594 RFQEGPeAPVfLISLKAGGEGLNLTAADHVIHYDLWwnpaveeQAIDR-AHRIGQT 648
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
504-615 |
5.49e-10 |
|
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: 58.80 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 504 RDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSVAARGLDIEKVQHVINFD-- 581
Cdd:cd18790 26 RGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDad 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 1985382943 582 ----LPSTiDEYVHRIGRTGRCGNiGKAISFFDSISDS 615
Cdd:cd18790 106 kegfLRSE-TSLIQTIGRAARNVN-GKVILYADKITDS 141
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
276-413 |
8.34e-10 |
|
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: 58.43 E-value: 8.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 276 LTPVQKYSI-PIILAGRDLMACAQTGSGKTAAFLLPILAHmmkdgvtashfREQQEPECIIVAPTRELINQIFLEARKFS 354
Cdd:cd17921 2 LNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRA-----------LATSGGKAVYIAPTRALVNQKEADLRERF 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 355 YGTCIRPVVIYGGTQTGhsiRQIMQGCNILCATPGRLMDIIGKEKI-GLRKVRYLVLDEA 413
Cdd:cd17921 71 GPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
272-610 |
1.20e-09 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 61.27 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 272 GYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmMKDGVTashfreqqepecIIVAPTREL----INQif 347
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL---VLDGLT------------LVVSPLISLmkdqVDQ-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 348 LEARKFSyGTCIrpvviyGGTQTGHSIRQIMQGCN-----ILCATPGRLM--DIIgkEKIGLRKVRYLVLDEADRMLDMG 420
Cdd:PRK11057 85 LLANGVA-AACL------NSTQTREQQLEVMAGCRtgqikLLYIAPERLMmdNFL--EHLAHWNPALLAVDEAHCISQWG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 421 --FGPEMKKL----ISCPGMP--------SKDRRQTLMFSATFPEEIQRLSgEFLKPeylfvavgqvggacsDVQQTVlq 486
Cdd:PRK11057 156 hdFRPEYAALgqlrQRFPTLPfmaltataDDTTRQDIVRLLGLNDPLIQIS-SFDRP---------------NIRYTL-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 487 VSQYSKREKLVEILQSIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATsvAA 566
Cdd:PRK11057 218 VEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVAT--VA 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1985382943 567 RGLDIEK--VQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 610
Cdd:PRK11057 296 FGMGINKpnVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
280-413 |
2.38e-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: 57.21 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 280 QKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMKD-GVTAshfreqqepecIIVAPTRELINQIFLEARKF--SYG 356
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDpGSRA-----------LYLYPTKALAQDQLRSLRELleQLG 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985382943 357 TCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDII----GKEKIGLRKVRYLVLDEA 413
Cdd:cd17923 74 LGIRVATYDGDTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
290-448 |
3.78e-09 |
|
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: 55.87 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 290 GRDLMACAQTGSGKTAAFLLPILAHMmkdgvtashfrEQQEPECIIVAPTRELINQIFLEARKFsYGTCIRPVVIYGGTQ 369
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLL-----------LKKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 370 TGHSIRQIMQGCNILCATPGRL-MDIIGKEKIGLRKVRYLVLDEADRMLDMGFGPEMKKLISCPGMPsKDRRQTLMfSAT 448
Cdd:cd00046 69 AEEREKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGL-KNAQVILL-SAT 146
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
275-448 |
5.10e-08 |
|
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: 53.19 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 275 KLTPVQKYSIPIILAG------RDLMACAQTGSGKTAAFLLPILAhmmkdgVTASHFReqqepeCIIVAPTRELINQIFL 348
Cdd:cd17918 15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL------AYKNGKQ------VAILVPTEILAHQHYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 349 EARKFSygTCIRPVVIYGGTQTghsirQIMQGCNILCATPGRLMDIIGKEKIGLrkvryLVLDEADRmldmgFGPEMKKL 428
Cdd:cd17918 83 EARKFL--PFINVELVTGGTKA-----QILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHR-----FGVAQREA 145
|
170 180
....*....|....*....|
gi 1985382943 429 ISCPGMPSkdrrqTLMFSAT 448
Cdd:cd17918 146 LYNLGATH-----FLEATAT 160
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
276-597 |
7.28e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 55.88 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 276 LTPVQKYSIPIILAGRDLMACAQTGSGKT-AAFlLPILAHMMKDGVTASHfreQQEPECIIVAPTRELINQI------FL 348
Cdd:COG1201 25 PTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGEL---PDGLRVLYISPLKALANDIernlraPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 349 EARKFSYGTCIRPVVIygGTQTG---HSIRQIM--QGCNILCATPGRLMDII----GKEKigLRKVRYLVLDEA------ 413
Cdd:COG1201 101 EEIGEAAGLPLPEIRV--GVRTGdtpASERQRQrrRPPHILITTPESLALLLtspdAREL--LRGVRTVIVDEIhalags 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 414 -------------DRMLDMGFgpemkkliscpgmpskdRRQTLmfSATF--PEEIQR-LSGEFLKPEYLFVAVGqvGGAC 477
Cdd:COG1201 177 krgvhlalslerlRALAPRPL-----------------QRIGL--SATVgpLEEVARfLVGYEDPRPVTIVDAG--AGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 478 SDVqQTVLQVSQYSKR--------EKLVE-ILQSIRDER-TMVFVETKKKADFIATFLCqEKIPTTSI-----HG--DRE 540
Cdd:COG1201 236 PDL-EVLVPVEDLIERfpwaghlwPHLYPrVLDLIEAHRtTLVFTNTRSQAERLFQRLN-ELNPEDALpiaahHGslSRE 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1985382943 541 QRER-EEALwdfRSGKCPVLVATSVAARGLDIEKVQHVINFDLPSTIDEYVHRIGRTG 597
Cdd:COG1201 314 QRLEvEEAL---KAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
292-600 |
1.81e-07 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 53.61 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 292 DLMACAQTGSGKTAAFLLpILAHMMKdgvtashfrEQQEPECIIVAPTRELINQIFLEARK-FSYGTcirpvviyGGTQT 370
Cdd:TIGR01587 1 LLVIEAPTGYGKTEAALL-WALHSIK---------SQKADRVIIALPTRATINAMYRRAKElFGSEL--------VGLHH 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 371 GHSIRQIM----------------QGCNILCATPGRL--MDIIGKEKIGLRKVRY----------LVLDEADRMLdmgfg 422
Cdd:TIGR01587 63 SSSFSRIKemgdseefehlfplyiHSNDKLFLDPITVctIDQVLKSVFGEFGHYEftlasianslLIFDEVHFYD----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 423 PEMKKLISCPGMPSKDRRQTLM-FSATFPEEIQRlsgEFLKPEYLFVAVGQV--GGACSDVQQTVLQVSQY-SKREKLVE 498
Cdd:TIGR01587 138 EYTLALILAVLEVLKDNDVPILlMSATLPKFLKE---YAEKIGYVEFNEPLDlkEERRFENHRFILIESDKvGEISSLER 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 499 ILQSIRDE-RTMVFVETKKKADFIATFLcQEKIPTTSI---HG-----DREQREREEALWDFRSGKCPVLVATSVAARGL 569
Cdd:TIGR01587 215 LLEFIKKGgSIAIIVNTVDRAQEFYQQL-KEKAPEEEIilyHSrftekDRAKKEAELLREMKKSNEKFVIVATQVIEASL 293
|
330 340 350
....*....|....*....|....*....|....*
gi 1985382943 570 DiekvqhvINFDL----PSTIDEYVHRIGRTGRCG 600
Cdd:TIGR01587 294 D-------ISADVmiteLAPIDSLIQRLGRLHRYG 321
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
297-595 |
2.00e-07 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 54.32 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 297 AQTGSGKTAAFLLPILAHMmkdgvtashfREQQEPECIIVAPTRELINQIFLEARKFSYGTcirpVVIYGGTQTGHSIRQ 376
Cdd:COG1203 154 APTGGGKTEAALLFALRLA----------AKHGGRRIIYALPFTSIINQTYDRLRDLFGED----VLLHHSLADLDLLEE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 377 IMQGCN---------------ILCATPGRLMDII-----GKEKIGLR---KVryLVLDEADrMLDmgfgPEMKKLIscpg 433
Cdd:COG1203 220 EEEYESearwlkllkelwdapVVVTTIDQLFESLfsnrkGQERRLHNlanSV--IILDEVQ-AYP----PYMLALL---- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 434 mpskdrRQTLMF-----------SATFPEEIQrlsgEFLKPEYLFVavgqvggaCSDVQQTVLQVSQYSKR--------- 493
Cdd:COG1203 289 ------LRLLEWlknlggsvilmTATLPPLLR----EELLEAYELI--------PDEPEELPEYFRAFVRKrvelkegpl 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 494 ------EKLVEILQSirDERTMVFVETKKKAdfIATF-LCQEKIPTTSIH--------GDREQRErEEALWDFRSGKCPV 558
Cdd:COG1203 351 sdeelaELILEALHK--GKSVLVIVNTVKDA--QELYeALKEKLPDEEVYllhsrfcpADRSEIE-KEIKERLERGKPCI 425
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1985382943 559 LVATSVAARGLDiekvqhvINFDL----PSTIDEYVHRIGR 595
Cdd:COG1203 426 LVSTQVVEAGVD-------IDFDVvirdLAPLDSLIQRAGR 459
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
498-598 |
2.78e-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: 50.34 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 498 EILQSIRDERTM-VFVETKKKADFIAT---FLCQEKIPTTSI---HG--DREQREREEAlwDFRSGKCPVLVATSVAARG 568
Cdd:cd18796 30 EVIFLLERHKSTlVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEVEA--ALKRGDLKVVVATSSLELG 107
|
90 100 110
....*....|....*....|....*....|
gi 1985382943 569 LDIEKVQHVINFDLPSTIDEYVHRIGRTGR 598
Cdd:cd18796 108 IDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
558-610 |
3.21e-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: 48.08 E-value: 3.21e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1985382943 558 VLVATSVAARGLDIEKVQHVINFDLPSTIDEYVHRIGRTGRCGNIGKAISFFD 610
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
273-412 |
5.37e-07 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 52.97 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 273 YLKLTPVQKYSIPIILAGRDLMACAQTGSGKT-AAFLlpilahmmkdGVTASHFREQQEPE------CIIVAPTRELINQ 345
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL----------AIIDELFRLGREGEledkvyCLYVSPLRALNND 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 346 IF--LE---------ARKFSYG-TCIRPVVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIG----KEKigLRKVRYLV 409
Cdd:PRK13767 100 IHrnLEeplteireiAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLNspkfREK--LRTVKWVI 177
|
...
gi 1985382943 410 LDE 412
Cdd:PRK13767 178 VDE 180
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
290-412 |
3.55e-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: 47.58 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 290 GRDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHfreqqepeCIIVAPTRELINQIF--LEArkfsYGTCI---RPVVI 364
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ--------VLYISPLKALINDQErrLEE----PLDEIdleIPVAV 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1985382943 365 YGGtQTGHSIRQIM--QGCNILCATPGRLMDIIGKEKIG--LRKVRYLVLDE 412
Cdd:cd17922 69 RHG-DTSQSEKAKQlkNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
502-595 |
3.76e-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: 46.40 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 502 SIRDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQRERE-EALWDFRSG--KCPVLVATSVAARGLDIEKVQHVI 578
Cdd:cd18799 3 KYVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV 82
|
90
....*....|....*....
gi 1985382943 579 nFDLP--STIdEYVHRIGR 595
Cdd:cd18799 83 -FLRPteSRT-LFLQMLGR 99
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
272-455 |
1.58e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 46.37 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 272 GYLKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILahmMKDGVTashfreqqepecIIVAPTRELIN--QIFLE 349
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL---LLDGVT------------LVVSPLISLMQdqVDRLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 350 ARkfsygtCIRPVVIyGGTQTGHSIRQIMQGC-----NILCATPGRLMDIIGKEKIG----LRKVRYLVLDEADRMLDMG 420
Cdd:cd17920 74 QL------GIRAAAL-NSTLSPEEKREVLLRIkngqyKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAHCVSQWG 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1985382943 421 --FGPEMKKLIS----CPGMPskdrrqTLMFSATFPEEIQR 455
Cdd:cd17920 147 hdFRPDYLRLGRlrraLPGVP------ILALTATATPEVRE 181
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
491-612 |
3.12e-05 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 44.55 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 491 SKREKLVEILQSIRD-ERTMVFVETKKKADFIATFLcqeKIPttSIHGDREQREREEALWDFRSGKCPVLVATSVAARGL 569
Cdd:cd18789 34 NKLRALEELLKRHEQgDKIIVFTDNVEALYRYAKRL---LKP--FITGETPQSEREEILQNFREGEYNTLVVSKVGDEGI 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1985382943 570 DI--EKVQHVINFDLPSTiDEYVHRIGRTGRCGNIGKAISFFDSI 612
Cdd:cd18789 109 DLpeANVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFFYSL 152
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
291-412 |
8.10e-05 |
|
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: 44.27 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 291 RDLMACAQTGSGKTAAFLLPILAHMMKDGVTASHfreqqEPECIIVAPTRELINQIFLEAR-KFSyGTCIRPVVIYGGTQ 369
Cdd:cd18023 18 KNFVVSAPTGSGKTVLFELAILRLLKERNPLPWG-----NRKVVYIAPIKALCSEKYDDWKeKFG-PLGLSCAELTGDTE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1985382943 370 TGhSIRQImQGCNILCATPGR--LMDIIGKEKIGL-RKVRYLVLDE 412
Cdd:cd18023 92 MD-DTFEI-QDADIILTTPEKwdSMTRRWRDNGNLvQLVALVLIDE 135
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
291-413 |
1.13e-04 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 43.79 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 291 RDLMACAQTGSGKT--AAFLLPILAHMmkdgvtashFREQQEPECIIV--APTRELINQIFLEARKFSYGTCIrpvVIYG 366
Cdd:cd18034 17 RNTIVVLPTGSGKTliAVMLIKEMGEL---------NRKEKNPKKRAVflVPTVPLVAQQAEAIRSHTDLKVG---EYSG 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1985382943 367 GTQTGHSIRQIMQGC----NILCATPGRLMDIIGKEKIGLRKVRYLVLDEA 413
Cdd:cd18034 85 EMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
286-415 |
3.48e-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: 42.12 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 286 IILAGRDL----MACAQTGSGKTAAFLLPILAHMMKDGvtashfreqqePECIIVAPTRELINQIFLEARKFSygTCIRP 361
Cdd:cd18035 8 VLIAAVALngntLIVLPTGLGKTIIAILVAADRLTKKG-----------GKVLILAPSRPLVEQHAENLKRVL--NIPDK 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1985382943 362 VVIYGGTQTGHSIRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVLDEADR 415
Cdd:cd18035 75 ITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
296-430 |
8.37e-04 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 41.09 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 296 CAQTGSGKTAAFLLPILAhmmkdgvtasHFREQQEPECIIVAPTRELINQIFLE-ARKFSYGTCIRPVVIYGGTQTghSI 374
Cdd:cd18021 25 GAPTGSGKTVCAELALLR----------HWRQNPKGRAVYIAPMQELVDARYKDwRAKFGPLLGKKVVKLTGETST--DL 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1985382943 375 RQIMQGcNILCATPGRLmDIIG---KEKIGLRKVRYLVLDEAdRMLDMGFGPEMKKLIS 430
Cdd:cd18021 93 KLLAKS-DVILATPEQW-DVLSrrwKQRKNVQSVELFIADEL-HLIGGENGPVYEVVVS 148
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
507-601 |
1.35e-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: 39.55 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 507 RTMVFVETKKKADFIATFLCQEKIPT----TSIHGDR-----EQREREEAlwDFRSGKCPVLVATSVAARGLDIEKVQHV 577
Cdd:cd18797 37 KTIVFCRSRKLAELLLRYLKARLVEEgplaSKVASYRagylaEDRREIEA--ELFNGELLGVVATNALELGIDIGGLDAV 114
|
90 100
....*....|....*....|....
gi 1985382943 578 INFDLPSTIDEYVHRIGRTGRCGN 601
Cdd:cd18797 115 VLAGYPGSLASLWQQAGRAGRRGK 138
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
272-412 |
1.48e-03 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350777 [Multi-domain] Cd Length: 214 Bit Score: 40.43 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 272 GYLKLTPVQKYSIPIILAGRD-LMACAQTGSGKTAAFLLPILAHMMKD-----GVTASHFReqqepeCIIVAPTRELINQ 345
Cdd:cd18019 14 GFKSLNRIQSKLFPAAFETDEnLLLCAPTGAGKTNVALLTILREIGKHrnpdgTINLDAFK------IVYIAPMKALVQE 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985382943 346 IF--LEARKFSYGTCIRPVviyggtqTG-HSI--RQIMQgCNILCATPGRlMDII---GKEKIGLRKVRYLVLDE 412
Cdd:cd18019 88 MVgnFSKRLAPYGITVAEL-------TGdQQLtkEQISE-TQIIVTTPEK-WDIItrkSGDRTYTQLVRLIIIDE 153
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
290-353 |
1.58e-03 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 39.97 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985382943 290 GRDLMACAQTGSGKTAAFLLPILahmmkdgvtaSHFREQQEPECIIVAPTRELINQIFLEARKF 353
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWAL----------KLAARGGKRRIIYALPTRATINQMYERIREI 54
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
535-571 |
3.06e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 38.79 E-value: 3.06e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1985382943 535 IHGDREQREREEALWDFRSGKCPVLVATSVAARGLDI 571
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDV 102
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
274-451 |
3.40e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.81 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 274 LKLTPVQKYSIPIILAGRDL--------MAcaqTGSGKTAafllpILAHMMkdgvtASHFREQQEPECIIVAPTRELINQ 345
Cdd:pfam04851 2 LELRPYQIEAIENLLESIKNgqkrglivMA---TGSGKTL-----TAAKLI-----ARLFKKGPIKKVLFLVPRKDLLEQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 346 IFLEARKFSYGTCIRPVVIYGGTQtghsiRQIMQGCNILCATPGRLMDIIGKEKIGLRKVRYLVL--DEADRmldmGFGP 423
Cdd:pfam04851 69 ALEEFKKFLPNYVEIGEIISGDKK-----DESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHR----SGAS 139
|
170 180
....*....|....*....|....*...
gi 1985382943 424 EMKKLISCpgmpSKDRRQtLMFSATFPE 451
Cdd:pfam04851 140 SYRNILEY----FKPAFL-LGLTATPER 162
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
535-595 |
3.69e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 38.48 E-value: 3.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985382943 535 IHGDREQREREEALWDFRSGKCPVLVATSVAARGLDIEK-----VQHVINFDLpSTIDEYVHRIGR 595
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGL-SQLHQLRGRVGR 131
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
288-415 |
3.92e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 39.34 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 288 LAGRDLMACAQTGSGKTAAFLLPILAHMMKdgvtashFREQQEPECIIVAPTRELINQiflEARKFSYGTCIRP---VVI 364
Cdd:cd17927 15 LKGKNTIICLPTGSGKTFVAVLICEHHLKK-------FPAGRKGKVVFLANKVPLVEQ---QKEVFRKHFERPGykvTGL 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1985382943 365 YGGTQTGHSIRQIMQGCNILCATPGRLM-DIIGKEKIGLRKVRYLVLDEADR 415
Cdd:cd17927 85 SGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
496-615 |
9.08e-03 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 39.26 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985382943 496 LVEILQSI-RDERTMVFVETKKKADFIATFLCQEKIPTTSIHGDREQREREEALWDFRSGKCPVLVATSVAARGLDIEKV 574
Cdd:PRK05298 436 LSEIRKRVaKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEV 515
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1985382943 575 QHVINFD------LPSTideyvhR-----IGRTGRcgNI-GKAISFFDSISDS 615
Cdd:PRK05298 516 SLVAILDadkegfLRSE------RsliqtIGRAAR--NVnGKVILYADKITDS 560
|
|
| |
