|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
381-770 |
1.71e-152 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 452.29 E-value: 1.71e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 381 KEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwittlPKIDriEDSDQGPYAII 460
Cdd:COG0513 5 ADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLL------QRLD--PSRPRAPQALI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 461 LAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADR 540
Cdd:COG0513 77 LAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 541 MIDMGFEPDVQKILEYIPVTnqkpdtddaedpekmmqnfesgkhkyRQTVMFTATMPPAVERLARSYLRRPAVVYIGSAG 620
Cdd:COG0513 157 MLDMGFIEDIERILKLLPKE--------------------------RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPEN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 621 KPHERVEQKVILMSEGEKRKKLLEVLASGFEPPIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAG 700
Cdd:COG0513 211 ATAETIEQRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNG 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 701 AKDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGKSGVAMTFLTKEDSSVFYDLKQAI 770
Cdd:COG0513 291 KIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLI 360
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
389-615 |
7.87e-143 |
|
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: 419.42 E-value: 7.87e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKIDrIEDSDQGPYAIILAPTRELA 468
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLD-EETKDDGPYALILAPTRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 469 QQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEP 548
Cdd:cd17945 80 QQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054055 549 DVQKILEYIPVTNQKPDTDDAEdpekmmQNFESGKHKYRQTVMFTATMPPAVERLARSYLRRPAVVY 615
Cdd:cd17945 160 QVTKILDAMPVSNKKPDTEEAE------KLAASGKHRYRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
352-782 |
7.95e-121 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 374.88 E-value: 7.95e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 352 MTDRDWRIFREDYSITTKGGK-IPNPIRNWKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTA 430
Cdd:PTZ00110 103 LSSKEVDEIRKEKEITIIAGEnVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 431 AFLIPLLVWITTLPKIdRIEDsdqGPYAIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVI 510
Cdd:PTZ00110 183 AFLLPAIVHINAQPLL-RYGD---GPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 511 ATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILEYIpvtnqKPDtddaedpekmmqnfesgkhkyRQTV 590
Cdd:PTZ00110 259 ACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQI-----RPD---------------------RQTL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 591 MFTATMPPAVERLARSYLRR-PAVVYIGSAG-KPHERVEQKVILMSEGEKRKKLLEVLASGFEP--PIIIFVNQKKGCDV 666
Cdd:PTZ00110 313 MWSATWPKEVQSLARDLCKEePVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADF 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 667 LAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAG 746
Cdd:PTZ00110 393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
|
410 420 430
....*....|....*....|....*....|....*...
gi 41054055 747 KSGVAMTFLTKEDSSVFYDLKQAILES--PVstcPPEL 782
Cdd:PTZ00110 473 AKGASYTFLTPDKYRLARDLVKVLREAkqPV---PPEL 507
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
352-801 |
7.98e-94 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 303.25 E-value: 7.98e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 352 MTDRDWRIFREDYSITTKGGKIPNPIRNWKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAA 431
Cdd:PLN00206 95 LSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTAS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 432 FLIPLLVWITTLpkidRIE--DSDQGPYAIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIV 509
Cdd:PLN00206 175 FLVPIISRCCTI----RSGhpSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 510 IATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILEYIPvtnqKPdtddaedpekmmqnfesgkhkyrQT 589
Cdd:PLN00206 251 VGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALS----QP-----------------------QV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 590 VMFTATMPPAVERLARSYLRRPAVVYIGSAGKPHERVEQKVILMSEGEKRKKLLEVLASG--FEPPIIIFVNQKKGCDVL 667
Cdd:PLN00206 304 LLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKqhFKPPAVVFVSSRLGADLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 668 AKSLEKM-GYNACTLHGGKGQEQREFALSNLKAGAKDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAG 746
Cdd:PLN00206 384 ANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMG 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 41054055 747 KSGVAMTFLTKEDSSVFYDLKQaILESPVSTCPPELANHPDAQHkpGTILTKKRR 801
Cdd:PLN00206 464 EKGTAIVFVNEEDRNLFPELVA-LLKSSGAAIPRELANSRYLGS--GRKRKKKRR 515
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
389-614 |
4.42e-90 |
|
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: 281.64 E-value: 4.42e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKidrieDSDQGPYAIILAPTRELA 468
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-----KKGRGPQALVLAPTRELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 469 QQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEP 548
Cdd:cd00268 76 MQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054055 549 DVQKILEYIPVTnqkpdtddaedpekmmqnfesgkhkyRQTVMFTATMPPAVERLARSYLRRPAVV 614
Cdd:cd00268 156 DVEKILSALPKD--------------------------RQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
384-792 |
1.07e-87 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 285.16 E-value: 1.07e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 384 SLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEDSDQGPYAIILAP 463
Cdd:PRK11776 10 PLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLL---------QKLDVKRFRVQALVLCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 464 TRELAQQIEEETIKFGKPL-GIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMI 542
Cdd:PRK11776 81 TRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 543 DMGFEPDVQKILEYIPvtnqkpdtddaedpekmmqnfesgkhKYRQTVMFTATMPPAVERLARSYLRRPAVVYIGSAgkp 622
Cdd:PRK11776 161 DMGFQDAIDAIIRQAP--------------------------ARRQTLLFSATYPEGIAAISQRFQRDPVEVKVEST--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 623 HE--RVEQKVILMSEGEkRKKLLEVLASGFEP-PIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKA 699
Cdd:PRK11776 212 HDlpAIEQRFYEVSPDE-RLPALQRLLLHHQPeSCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFAN 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 700 GAKDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGKSGVAMTFLTKEDSSVFYDLKQAiLESPVSTCP 779
Cdd:PRK11776 291 RSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDY-LGRKLNWEP 369
|
410
....*....|....
gi 41054055 780 -PELANHPDAQHKP 792
Cdd:PRK11776 370 lPSLSPLSGVPLLP 383
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
385-768 |
2.69e-81 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 268.21 E-value: 2.69e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 385 LPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPkidrIEDSDQGPY-AIILAP 463
Cdd:PRK10590 8 LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQ----PHAKGRRPVrALILTP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 464 TRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMID 543
Cdd:PRK10590 84 TRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 544 MGFEPDVQKILEYIPVTnqkpdtddaedpekmmqnfesgkhkyRQTVMFTATMPPAVERLARSYLRRPAVVYIGSAGKPH 623
Cdd:PRK10590 164 MGFIHDIRRVLAKLPAK--------------------------RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTAS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 624 ERVEQKVILMSEGEKRKKLLEVLASGFEPPIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKD 703
Cdd:PRK10590 218 EQVTQHVHFVDKKRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIR 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41054055 704 ILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGKSGVAMTFLTKEDSSVFYDLKQ 768
Cdd:PRK10590 298 VLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEK 362
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
385-616 |
4.41e-80 |
|
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: 256.26 E-value: 4.41e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 385 LPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKIDRIEDSD-QGPYAIILAP 463
Cdd:cd17967 7 LRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRRkAYPSALILAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 464 TRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMID 543
Cdd:cd17967 87 TRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41054055 544 MGFEPDVQKILEYipvtNQKPDTDDaedpekmmqnfesgkhkyRQTVMFTATMPPAVERLARSYLRRpavvYI 616
Cdd:cd17967 167 MGFEPQIRKIVEH----PDMPPKGE------------------RQTLMFSATFPREIQRLAADFLKN----YI 213
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
367-611 |
2.03e-79 |
|
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: 254.61 E-value: 2.03e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 367 TTKGGKIPNPIRNWKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKI 446
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 447 drieDSDQGPYAIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVL---ENR 523
Cdd:cd17953 81 ----KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 524 YLVLSRCTYVVLDEADRMIDMGFEPDVQKIleyipVTNQKPDtddaedpekmmqnfesgkhkyRQTVMFTATMPPAVERL 603
Cdd:cd17953 157 VTNLRRVTYVVLDEADRMFDMGFEPQIMKI-----VNNIRPD---------------------RQTVLFSATFPRKVEAL 210
|
....*...
gi 41054055 604 ARSYLRRP 611
Cdd:cd17953 211 ARKVLHKP 218
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
389-755 |
4.35e-77 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 261.71 E-value: 4.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEDSDQGPYAIILAPTRELA 468
Cdd:PRK11634 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLL---------HNLDPELKAPQILVLAPTRELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 469 QQIEEETIKFGKPL-GIRTVAVIGGiSREDQGFR-LRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGF 546
Cdd:PRK11634 88 VQVAEAMTDFSKHMrGVNVVALYGG-QRYDVQLRaLRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 547 EPDVQKILEYIPVTNQkpdtddaedpekmmqnfesgkhkyrqTVMFTATMPPAVERLARSYLRRPAVVYIGSAGKPHERV 626
Cdd:PRK11634 167 IEDVETIMAQIPEGHQ--------------------------TALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 627 EQK---VILMSEGEKRKKLLEvlASGFEPPIIiFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKD 703
Cdd:PRK11634 221 SQSywtVWGMRKNEALVRFLE--AEDFDAAII-FVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLD 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 41054055 704 ILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGKSGVAMTFL 755
Cdd:PRK11634 298 ILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFV 349
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
379-782 |
3.24e-76 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 257.96 E-value: 3.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 379 NWKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKI-DRiedSDQGPY 457
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALaDR---KPEDPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 458 AIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLV-LSRCTYVVLD 536
Cdd:PRK04537 87 ALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVsLHACEICVLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 537 EADRMIDMGFEPDVQKILEYIPvtnqkpdtddaedpekmmqnfESGKhkyRQTVMFTATMPPAVERLARSYLRRPAVVYI 616
Cdd:PRK04537 167 EADRMFDLGFIKDIRFLLRRMP---------------------ERGT---RQTLLFSATLSHRVLELAYEHMNEPEKLVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 617 GSAGKPHERVEQKVILMSEGEKRKKLLEVLASGFEPPIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSN 696
Cdd:PRK04537 223 ETETITAARVRQRIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 697 LKAGAKDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGKSGVAMTFLTKEDSSVFYDLKQAILES-PV 775
Cdd:PRK04537 303 FQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKiPV 382
|
....*..
gi 41054055 776 STCPPEL 782
Cdd:PRK04537 383 EPVTAEL 389
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
389-614 |
8.38e-75 |
|
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: 241.50 E-value: 8.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKIDRiedsDQGPYAIILAPTRELA 468
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLER----GDGPIVLVLAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 469 QQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEP 548
Cdd:cd17966 77 QQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054055 549 DVQKILEYIpvtnqKPDtddaedpekmmqnfesgkhkyRQTVMFTATMPPAVERLARSYLRRPAVV 614
Cdd:cd17966 157 QIRKIVDQI-----RPD---------------------RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
357-786 |
2.27e-74 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 250.21 E-value: 2.27e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 357 WRIfrEDYSITTKGGKIpnpirNWKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPL 436
Cdd:PRK01297 73 WKL--EDFVVEPQEGKT-----RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 437 lvwITTLPKIDRIEDSDQG-PYAIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMG-CEIVIATPG 514
Cdd:PRK01297 146 ---INQLLQTPPPKERYMGePRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 515 RLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILEYIPVTNQkpdtddaedpekmmqnfesgkhkyRQTVMFTA 594
Cdd:PRK01297 223 RLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRKEE------------------------RQTLLFSA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 595 TMPPAVERLARSYLRRPAVVYIGSAGKPHERVEQKVILMSEGEKRKKLLEVLASGFEPPIIIFVNQKKGCDVLAKSLEKM 674
Cdd:PRK01297 279 TFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 675 GYNACTLHGGKGQEQREFALSNLKAGAKDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGKSGVAMTF 754
Cdd:PRK01297 359 GINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
410 420 430
....*....|....*....|....*....|..
gi 41054055 755 LTKEDSSVFYDLKQAILESPVSTCPPELANHP 786
Cdd:PRK01297 439 AGEDDAFQLPEIEELLGRKISCEMPPAELLKP 470
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
382-754 |
1.20e-71 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 241.03 E-value: 1.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 382 EYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKIDRIEDSdqGPYAIIL 461
Cdd:PRK04837 12 DFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRKVN--QPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 462 APTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRM 541
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 542 IDMGFEPDVQKILEYIPVTNQkpdtddaedpekmmqnfesgkhkyRQTVMFTATMPPAVERLARSYLRRPAVVYIGSAGK 621
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPPANQ------------------------RLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 622 PHERVEQKVILMSEGEKRKKLLEVLASGFEPPIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGA 701
Cdd:PRK04837 226 TGHRIKEELFYPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGD 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 41054055 702 KDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGKSGVAMTF 754
Cdd:PRK04837 306 LDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
378-754 |
2.16e-71 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 240.61 E-value: 2.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 378 RNWKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKidriedSDQGPY 457
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPR------RKSGPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 458 AI-ILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLD 536
Cdd:PRK11192 75 RIlILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 537 EADRMIDMGFEPDVQKIleyipvtnqkpdtddaedpekmmqnfeSGKHKYR-QTVMFTATMP-PAVERLARSYLRRPAVV 614
Cdd:PRK11192 155 EADRMLDMGFAQDIETI---------------------------AAETRWRkQTLLFSATLEgDAVQDFAERLLNDPVEV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 615 YIGSAGKPHERVEQKVILMSEGEKRKKLLEVLASGFEPP-IIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFA 693
Cdd:PRK11192 208 EAEPSRRERKKIHQWYYRADDLEHKTALLCHLLKQPEVTrSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEA 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054055 694 LSNLKAGAKDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGKSGVAMTF 754
Cdd:PRK11192 288 IKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
389-614 |
1.28e-70 |
|
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: 230.38 E-value: 1.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKIDRiedsDQGPYAIILAPTRELA 468
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEK----GEGPIAVIVAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 469 QQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEP 548
Cdd:cd17952 77 QQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054055 549 DVQKILEYIpvtnqKPDtddaedpekmmqnfesgkhkyRQTVMFTATMPPAVERLARSYLRRPAVV 614
Cdd:cd17952 157 QVRSIVGHV-----RPD---------------------RQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
370-609 |
1.32e-70 |
|
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: 232.94 E-value: 1.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 370 GGKIPNPIRNWKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwiTTLPKiDRI 449
Cdd:cd18052 35 GRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVL---TGMMK-EGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 450 EDSD----QGPYAIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYL 525
Cdd:cd18052 111 TASSfsevQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 526 VLSRCTYVVLDEADRMIDMGFEPDVQKILEyipvtnqKPDTDDAEDpekmmqnfesgkhkyRQTVMFTATMPPAVERLAR 605
Cdd:cd18052 191 SLSKLKYLILDEADRMLDMGFGPEIRKLVS-------EPGMPSKED---------------RQTLMFSATFPEEIQRLAA 248
|
....
gi 41054055 606 SYLR 609
Cdd:cd18052 249 EFLK 252
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
380-611 |
1.06e-66 |
|
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: 219.88 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 380 WKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPkidriedsdQGPYAI 459
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENP---------QRFFAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 460 ILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLEN-RYLVLSRCTYVVLDEA 538
Cdd:cd17954 73 VLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41054055 539 DRMIDMGFEPDVQKILEYIPvtnqkpdtddaedpekmmqnfesgkhKYRQTVMFTATMPPAVERLARSYLRRP 611
Cdd:cd17954 153 DRLLNMDFEPEIDKILKVIP--------------------------RERTTYLFSATMTTKVAKLQRASLKNP 199
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
360-618 |
4.00e-64 |
|
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: 214.49 E-value: 4.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 360 FREDYSITTKGGKIPNPIRNWKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVW 439
Cdd:cd18049 6 YRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 440 ITTLPKIDRiedsDQGPYAIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDV 519
Cdd:cd18049 86 INHQPFLER----GDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 520 LENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILEYIpvtnqKPDtddaedpekmmqnfesgkhkyRQTVMFTATMPPA 599
Cdd:cd18049 162 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI-----RPD---------------------RQTLMWSATWPKE 215
|
250
....*....|....*....
gi 41054055 600 VERLARSYLRRPAVVYIGS 618
Cdd:cd18049 216 VRQLAEDFLKDYIHINIGA 234
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
389-759 |
9.81e-63 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 216.23 E-value: 9.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIpllvwiTTLPKIDRIEDSDQgpyAIILAPTRELA 468
Cdd:PTZ00424 39 LLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVI------AALQLIDYDLNACQ---ALILAPTRELA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 469 QQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEP 548
Cdd:PTZ00424 110 QQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 549 DVQKILEYIPvtnqkPDTddaedpekmmqnfesgkhkyrQTVMFTATMPPAVERLARSYLRRPAVVYIGSAGKPHERVEQ 628
Cdd:PTZ00424 190 QIYDVFKKLP-----PDV---------------------QVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 629 KVILMsegEKRKKLLEVLASGFEP----PIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKDI 704
Cdd:PTZ00424 244 FYVAV---EKEEWKFDTLCDLYETltitQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 41054055 705 LVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGKSGVAMTFLTKED 759
Cdd:PTZ00424 321 LITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDD 375
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
336-617 |
1.57e-60 |
|
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: 206.01 E-value: 1.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 336 KQRWD---------DRHWSQKKLDEMTDRDWRIFREDYSITTKGGKIPNPIRNWKEYSLPPHILEVIEKCGYKDPTPIQR 406
Cdd:cd18050 11 KKKWDlselpkfekNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQC 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 407 QAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKIDRiedsDQGPYAIILAPTRELAQQIEEETIKFGKPLGIRT 486
Cdd:cd18050 91 QGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLER----GDGPICLVLAPTRELAQQVQQVADDYGKSSRLKS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 487 VAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILEYIpvtnqKPDt 566
Cdd:cd18050 167 TCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI-----RPD- 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 41054055 567 ddaedpekmmqnfesgkhkyRQTVMFTATMPPAVERLARSYLRRPAVVYIG 617
Cdd:cd18050 241 --------------------RQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
402-603 |
5.35e-60 |
|
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: 200.55 E-value: 5.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 402 TPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEDSDQGPYAIILAPTRELAQQIEEETIKFGKP 481
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPAL---------EALDKLDNGPQALVLAPTRELAEQIYEELKKLGKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 482 LGIRTVAVIGGISREDQGFRLRmGCEIVIATPGRLIDVLENRYLvLSRCTYVVLDEADRMIDMGFEPDVQKILEYIPvtn 561
Cdd:pfam00270 72 LGLKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLP--- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 41054055 562 qkpdtddaedpekmmqnfesgkhKYRQTVMFTATMPPAVERL 603
Cdd:pfam00270 147 -----------------------KKRQILLLSATLPRNLEDL 165
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
379-614 |
1.06e-59 |
|
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: 201.38 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 379 NWKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLlvwittlpkIDRIEDSDQ--GP 456
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPM---------IEKLKAHSPtvGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 457 YAIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQgFRLRMGC-EIVIATPGRLIDVLENRYLVLSRCTYVVL 535
Cdd:cd17959 73 RALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQ-FEALASNpDIIIATPGRLLHLLVEMNLKLSSVEYVVF 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054055 536 DEADRMIDMGFEPDVQKILEYIPVTnqkpdtddaedpekmmqnfesgkhkyRQTVMFTATMPPAVERLARSYLRRPAVV 614
Cdd:cd17959 152 DEADRLFEMGFAEQLHEILSRLPEN--------------------------RQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
389-615 |
7.06e-59 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 198.84 E-value: 7.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWI--TTLPKIDRIedsdqGPYAIILAPTRE 466
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLdlQPIPREQRN-----GPGVLVLTPTRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 467 LAQQIEEETIKFgKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGF 546
Cdd:cd17958 76 LALQIEAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054055 547 EPDVQKILEYIpvtnqKPDtddaedpekmmqnfesgkhkyRQTVMFTATMPPAVERLARSYLRRPAVVY 615
Cdd:cd17958 155 EPQIRKILLDI-----RPD---------------------RQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
389-617 |
1.85e-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: 194.73 E-value: 1.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKidriedsDQGPYAIILAPTRELA 468
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRK-------KKGLRALILAPTRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 469 QQIEEETIKFGKPLGIRTVAVIGGIS-REDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFE 547
Cdd:cd17957 74 SQIYRELLKLSKGTGLRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 548 pdvqkileyipvtnqkpdtddaedpEKMMQNFESGKHKYRQTVMFTATMPPAVERLARSYLRRPAVVYIG 617
Cdd:cd17957 154 -------------------------EQTDEILAACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
362-608 |
2.23e-57 |
|
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: 196.41 E-value: 2.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 362 EDYSITTKGGKIPNPIRNWKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWIT 441
Cdd:cd18051 5 EDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 442 TL-PKIDRIEDSDQG------PYAIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPG 514
Cdd:cd18051 85 EQgPGESLPSESGYYgrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 515 RLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILEyipvtnqkpdtDDAEDPekmmqnfeSGKhkyRQTVMFTA 594
Cdd:cd18051 165 RLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVE-----------QDTMPP--------TGE---RQTLMFSA 222
|
250
....*....|....
gi 41054055 595 TMPPAVERLARSYL 608
Cdd:cd18051 223 TFPKEIQMLARDFL 236
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
394-617 |
2.52e-57 |
|
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: 195.11 E-value: 2.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 394 EKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTL-PKIDRiedsDQGPYAIILAPTRELAQQIE 472
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLePRVDR----SDGTLALVLVPTRELALQIY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 473 EETIKFGKP-LGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLEN-RYLVLSRCTYVVLDEADRMIDMGFEPDV 550
Cdd:cd17949 83 EVLEKLLKPfHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054055 551 QKILEYIpvtnqkpdtddaeDPEKMMQNFESGKHKYRQTVMFTATMPPAVERLARSYLRRPavVYIG 617
Cdd:cd17949 163 TKILELL-------------DDKRSKAGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDP--VYID 214
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
389-614 |
3.25e-56 |
|
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: 191.78 E-value: 3.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWI----TTLPKIDRiedsdQGPYAIILAPT 464
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFAleqeKKLPFIKG-----EGPYGLIVCPS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 465 RELAQQIEEETIKFGKPL------GIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEA 538
Cdd:cd17951 76 RELARQTHEVIEYYCKALqeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054055 539 DRMIDMGFEPDVQKILEYIpvTNQkpdtddaedpekmmqnfesgkhkyRQTVMFTATMPPAVERLARSYLRRPAVV 614
Cdd:cd17951 156 DRMIDMGFEEDIRTIFSYF--KGQ------------------------RQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
385-611 |
1.01e-55 |
|
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: 190.13 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 385 LPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEDSDQGPYAIILAPT 464
Cdd:cd17955 6 LSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL---------QRLSEDPYGIFALVLTPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 465 RELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYL---VLSRCTYVVLDEADRM 541
Cdd:cd17955 77 RELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttkVLSRVKFLVLDEADRL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 542 IDMGFEPDVQKILEYIPvtnqkpdtddaedpekmmqnfesgkhKYRQTVMFTATMPPAVERLARSYLRRP 611
Cdd:cd17955 157 LTGSFEDDLATILSALP--------------------------PKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
389-611 |
1.46e-55 |
|
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: 189.39 E-value: 1.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKidriedsdQGPY--AIILAPTRE 466
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPK--------KKAAtrVLVLVPTRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 467 LAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLV-LSRCTYVVLDEADRMIDMG 545
Cdd:cd17947 73 LAMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFdLDSIEILVLDEADRMLEEG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054055 546 FEPDVQKILEYIPvtnqkpdtddaedpekmmqnfesgkhKYRQTVMFTATMPPAVERLARSYLRRP 611
Cdd:cd17947 153 FADELKEILRLCP--------------------------RTRQTMLFSATMTDEVKDLAKLSLNKP 192
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
626-755 |
1.25e-54 |
|
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: 184.63 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 626 VEQKVILMSEGEKRKKLL-EVLASGFEPPIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKDI 704
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 41054055 705 LVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGKSGVAMTFL 755
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
385-609 |
2.93e-53 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 183.94 E-value: 2.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 385 LPPHILEVIEKCGYKDPTPIQRQAIPIGLQNR-DIIGVAETGSGKTAAFLIPLL-VWITTLPKIDRiedSDQGpyAIILA 462
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTGdDVLARAKTGTGKTLAFLLPAIqSLLNTKPAGRR---SGVS--ALIIS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 463 PTRELAQQIEEETIKFGKPL-GIRTVAVIGGISREDQGFRL-RMGCEIVIATPGRLIDVLENRYL--VLSRCTYVVLDEA 538
Cdd:cd17964 76 PTRELALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054055 539 DRMIDMGFEPDVQKILEYIPVTNQKPdtddaedpekmmqnfesgkhkyRQTVMFTATMPPAVERLARSYLR 609
Cdd:cd17964 156 DRLLDMGFRPDLEQILRHLPEKNADP----------------------RQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
389-614 |
1.58e-51 |
|
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: 178.54 E-value: 1.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwiTTLPKiDRIEDSDQGPYAIILAPTRELA 468
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVL---EILLK-RKANLKKGQVGALIISPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 469 QQIEEETIKFGKPLG--IRTVAVIGG--ISREDQGFRlRMGCEIVIATPGRLIDVLENRYLV--LSRCTYVVLDEADRMI 542
Cdd:cd17960 77 TQIYEVLQSFLEHHLpkLKCQLLIGGtnVEEDVKKFK-RNGPNILVGTPGRLEELLSRKADKvkVKSLEVLVLDEADRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054055 543 DMGFEPDVQKILEYIPvtnqkpdtddaedpekmmqnfesgkhKYRQTVMFTATMPPAVERLARSYLRRPAVV 614
Cdd:cd17960 156 DLGFEADLNRILSKLP--------------------------KQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
393-629 |
1.75e-51 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 178.45 E-value: 1.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 393 IEKCGYKDPTPIQRQAIPIGLQN-RDIIGVAETGSGKTAAFLIPLLvwittlpkidRIEDSDQGPYAIILAPTRELAQQI 471
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPAL----------EALKRGKGGRVLVLVPTRELAEQW 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 472 EEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGC-EIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDV 550
Cdd:smart00487 71 AEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054055 551 QKILEYIPvtnqkpdtddaedpekmmqnfesgkhKYRQTVMFTATMPPAVERLARSYLRRPAVVYIGSagKPHERVEQK 629
Cdd:smart00487 151 EKLLKLLP--------------------------KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
389-596 |
1.72e-50 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 177.05 E-value: 1.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNR-DIIGVAETGSGKTAAFLIPLLVWITTLPKIDRIEDSDQGPYAIILAPTREL 467
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRDGkDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 468 AQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLE--NRYLV-LSRCTYVVLDEADRMIDM 544
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQegNEHLAnLKSLRFLVLDEADRMLEK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 41054055 545 G-FEpDVQKILEYIPVTNQkpdtddaedpekmmqnfesGKHKYRQTVMFTATM 596
Cdd:cd17946 161 GhFA-ELEKILELLNKDRA-------------------GKKRKRQTFVFSATL 193
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
380-611 |
5.64e-50 |
|
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: 174.41 E-value: 5.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 380 WKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPllvwitTLPKIDRIEDSDQgpyAI 459
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIP------ILEKIDPKKDVIQ---AL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 460 ILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEAD 539
Cdd:cd17940 72 ILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEAD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054055 540 RMIDMGFEPDVQKILEYIPvtnqkpdtddaedpekmmqnfesgkhKYRQTVMFTATMPPAVERLARSYLRRP 611
Cdd:cd17940 152 KLLSQDFQPIIEKILNFLP--------------------------KERQILLFSATFPLTVKNFMDRHMHNP 197
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
393-614 |
2.74e-47 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 166.57 E-value: 2.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 393 IEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLlvwittlpkIDRIEDSDQGPYAIILAPTRELAQQIE 472
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPV---------IIRCLTEHRNPSALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 473 EETIKFGKPL-GIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQ 551
Cdd:cd17962 76 DQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41054055 552 KILEYIPvtnqkpdtddaEDPekmmqnfesgkhkyrQTVMFTATMPPAVERLARSYLRRPAVV 614
Cdd:cd17962 156 DILENIS-----------HDH---------------QTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
397-617 |
3.65e-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: 163.61 E-value: 3.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 397 GYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLlvwittLPKIDRIE-DSDQGPYAIILAPTRELAQQIEEET 475
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPL------LEKLYRERwTPEDGLGALIISPTRELAMQIFEVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 476 IKFGKPLGIRTVAVIGGISREDQgfRLRMG-CEIVIATPGRLIDVL-ENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKI 553
Cdd:cd17941 83 RKVGKYHSFSAGLIIGGKDVKEE--KERINrMNILVCTPGRLLQHMdETPGFDTSNLQMLVLDEADRILDMGFKETLDAI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054055 554 LEYIPvtnqkpdtddaedpekmmqnfesgkhKYRQTVMFTATMPPAVERLARSYLRRPavVYIG 617
Cdd:cd17941 161 VENLP--------------------------KSRQTLLFSATQTKSVKDLARLSLKNP--EYIS 196
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
385-614 |
8.44e-46 |
|
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: 162.75 E-value: 8.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 385 LPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKIDRIEdsdQGPYAIILAPT 464
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEE---QGTRALILVPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 465 RELAQQ----IEEETIKFGKPlgIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLE-NRYLVLSRCTYVVLDEAD 539
Cdd:cd17961 78 RELAQQvskvLEQLTAYCRKD--VRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLEsGSLLLLSTLKYLVIDEAD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41054055 540 RMIDMGFEPDVQKILEYIPvtnqkpdtddaedpekmmqnfesgkhKYRQTVMFTATMPPAVERLARSYLRRPAVV 614
Cdd:cd17961 156 LVLSYGYEEDLKSLLSYLP--------------------------KNYQTFLMSATLSEDVEALKKLVLHNPAIL 204
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
389-617 |
1.90e-42 |
|
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: 153.28 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKIDRiedsdQGPYAIILAPTRELA 468
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPR-----NGTGVIIISPTRELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 469 QQIE---EETIKFG-KPLGIrtvaVIGGISREDQGFRLRMGCEIVIATPGRLIDVLEN-RYLVLSRCTYVVLDEADRMID 543
Cdd:cd17942 76 LQIYgvaKELLKYHsQTFGI----VIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNtKGFLYKNLQCLIIDEADRILE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054055 544 MGFEPDVQKILEYIPvtnqkpdtddaedpekmmqnfesgkhKYRQTVMFTATMPPAVERLARSYLRRPAvVYIG 617
Cdd:cd17942 152 IGFEEEMRQIIKLLP--------------------------KRRQTMLFSATQTRKVEDLARISLKKKP-LYVG 198
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
397-611 |
9.65e-42 |
|
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: 151.32 E-value: 9.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 397 GYKDPTPIQRQAI-PIgLQNRDIIGVAETGSGKTAAFLIpllvwiTTLPKIDRIEDSDQgpyAIILAPTRELAQQIEEET 475
Cdd:cd17939 16 GFEKPSAIQQRAIvPI-IKGRDVIAQAQSGTGKTATFSI------GALQRIDTTVRETQ---ALVLAPTRELAQQIQKVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 476 IKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILE 555
Cdd:cd17939 86 KALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 41054055 556 YIPvtnqkPDTddaedpekmmqnfesgkhkyrQTVMFTATMPPAVERLARSYLRRP 611
Cdd:cd17939 166 FLP-----PET---------------------QVVLFSATMPHEVLEVTKKFMRDP 195
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
382-614 |
5.27e-39 |
|
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: 143.62 E-value: 5.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 382 EYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwittlpkidriedsdQGPYAIIL 461
Cdd:cd17938 3 ELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------------QIVVALIL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 462 APTRELAQQIEEETIKFGKPL---GIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEA 538
Cdd:cd17938 67 EPSRELAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054055 539 DRMIDMGFEPDVQKILEYIPvtnqkpdtddaedpekmmQNFESGKHkyRQTVMFTATM-PPAVERLARSYLRRPAVV 614
Cdd:cd17938 147 DRLLSQGNLETINRIYNRIP------------------KITSDGKR--LQVIVCSATLhSFEVKKLADKIMHFPTWV 203
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
381-616 |
7.42e-39 |
|
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: 143.25 E-value: 7.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 381 KEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEDSDQGPYAII 460
Cdd:cd17950 5 RDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL---------QQLEPVDGQVSVLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 461 LAPTRELAQQIEEETIKFGKPL-GIRTVAVIGGIS-REDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEA 538
Cdd:cd17950 76 ICHTRELAFQISNEYERFSKYMpNVKTAVFFGGVPiKKDIEVLKNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDEC 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054055 539 DRMI-DMGFEPDVQKIleyipvtnqkpdtddaedpekmmqnFESGKHKyRQTVMFTATMPPAVERLARSYLRRPAVVYI 616
Cdd:cd17950 156 DKMLeQLDMRRDVQEI-------------------------FRATPHD-KQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
385-611 |
2.43e-38 |
|
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: 141.43 E-value: 2.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 385 LPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEDSDQGPYAIILAPT 464
Cdd:cd18046 6 LKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISIL---------QQIDTSLKATQALVLAPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 465 RELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDM 544
Cdd:cd18046 77 RELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054055 545 GFEPDVQKILEYIPvtnqkPDTddaedpekmmqnfesgkhkyrQTVMFTATMPPAVERLARSYLRRP 611
Cdd:cd18046 157 GFKDQIYDIFQKLP-----PDT---------------------QVVLLSATMPNDVLEVTTKFMRDP 197
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
389-614 |
1.70e-37 |
|
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: 138.94 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEDSDQGPYAIILAPTRELA 468
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL---------ESLDLERRHPQVLILAPTREIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 469 QQIEEETIKFGKPL-GIRTVAVIGGISREDQGFRLRmGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFE 547
Cdd:cd17943 72 VQIHDVFKKIGKKLeGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41054055 548 PDVQKILEYIPvtnqkpdtddaedpekmmqnfesgkhKYRQTVMFTATMPPAV-ERLARsYLRRPAVV 614
Cdd:cd17943 151 KDVNWIFSSLP--------------------------KNKQVIAFSATYPKNLdNLLAR-YMRKPVLV 191
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
385-607 |
1.31e-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: 130.77 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 385 LPPHILEVIEKCGYKDPTPIQRQAIPIGLQN--RDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEDSDQGPYAIILA 462
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAML---------SRVDPTLKSPQALCLA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 463 PTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDqgfRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMI 542
Cdd:cd17963 72 PTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPR---GKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVML 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054055 543 DM-GFEPDVQKILEYIPvtnqkpdtddaedpekmmQNFesgkhkyrQTVMFTATMPPAVERLARSY 607
Cdd:cd17963 149 DTqGHGDQSIRIKRMLP------------------RNC--------QILLFSATFPDSVRKFAEKI 188
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
389-603 |
1.03e-33 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 129.41 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKIDriEDSDQGPYAIILAPTRELA 468
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLA--EGPFNAPRGLVITPSRELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 469 QQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEP 548
Cdd:cd17948 79 EQIGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 41054055 549 DVQKILEYIPVTNQKPDTDDAEDPEKmmqnfesgkhkyrQTVMFTATMPPAVERL 603
Cdd:cd17948 159 KLSHFLRRFPLASRRSENTDGLDPGT-------------QLVLVSATMPSGVGEV 200
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
637-746 |
4.01e-33 |
|
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: 123.09 E-value: 4.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 637 EKRKKLLEVLASGFEPPIIIFVNQKKGCDvLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKDILVATDVAGRGID 716
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 41054055 717 IQDVSMVLNYDMAKNIEDYIHRIGRTGRAG 746
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
384-562 |
4.31e-30 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350803 [Multi-domain] Cd Length: 201 Bit Score: 117.95 E-value: 4.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 384 SLPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEDSDQGPYAIILAP 463
Cdd:cd18045 5 GLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL---------QCLDIQVRETQALILSP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 464 TRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMID 543
Cdd:cd18045 76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155
|
170
....*....|....*....
gi 41054055 544 MGFEPDVQKILEYIPVTNQ 562
Cdd:cd18045 156 KGFKEQIYDVYRYLPPATQ 174
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
403-609 |
9.93e-29 |
|
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: 114.17 E-value: 9.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 403 PIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLlvwITTLPKIDRIEDSDQGPYAIILAPTRELAQQIEEETIKFGKPL 482
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPL---IEKLQEDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 483 GIrtVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILEyipvTNQ 562
Cdd:cd17944 92 SV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILS----VSY 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 41054055 563 KPDTDDaeDPekmmqnfesgkhkyrQTVMFTATMPPAVERLARSYLR 609
Cdd:cd17944 166 KKDSED--NP---------------QTLLFSATCPDWVYNVAKKYMK 195
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
665-746 |
6.70e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 107.30 E-value: 6.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 665 DVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGR 744
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 41054055 745 AG 746
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
389-611 |
1.05e-27 |
|
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: 111.96 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 389 ILEVIEKCGYKDPTPIQRQAIP---------IGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPkIDRIEdsdqgpyAI 459
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPwllpsskstPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRV-VPRLR-------AL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 460 ILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGIS--------REDQGFRLRMGCEIVIATPGRLIDVL-ENRYLVLSRC 530
Cdd:cd17956 73 IVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSfkkeqkllLVDTSGRYLSRVDILVATPGRLVDHLnSTPGFTLKHL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 531 TYVVLDEADRMIDMGFEpdvqkilEYIPVTNQKPDTDDAEDPekmmQNFESGKHKYR-----QTVMFTATMPPAVERLAR 605
Cdd:cd17956 153 RFLVIDEADRLLNQSFQ-------DWLETVMKALGRPTAPDL----GSFGDANLLERsvrplQKLLFSATLTRDPEKLSS 221
|
....*.
gi 41054055 606 SYLRRP 611
Cdd:cd17956 222 LKLHRP 227
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
385-562 |
7.01e-26 |
|
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: 107.46 E-value: 7.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 385 LPP---HILEVIEKCGYKD-----PTPIQRQAIPIGLQNRDIIG----------------VAETGSGKTAAFLIPLLVWI 440
Cdd:cd17965 7 LPSvreAIIKEILKGSNKTdeeikPSPIQTLAIKKLLKTLMRKVtkqtsneepklevfllAAETGSGKTLAYLAPLLDYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 441 ttlpKIDRIEDSDQG------------PYAIILAPTRELAQQIEEETIKFGKP--LGIRTVAVIGGISREDQGFRLRMGC 506
Cdd:cd17965 87 ----KRQEQEPFEEAeeeyesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTvkLGIKTFSSGFGPSYQRLQLAFKGRI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 41054055 507 EIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILEYIPVTNQ 562
Cdd:cd17965 163 DILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKH 218
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
592-759 |
5.72e-20 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 94.05 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 592 FTATMPPAV-----ERLArsyLRRPAVvYIGSAGKP--HERVEQKVilmsEGEKRKKLLEVLASGFEPPIIIFVNQKKGC 664
Cdd:COG0514 172 LTATATPRVradiaEQLG---LEDPRV-FVGSFDRPnlRLEVVPKP----PDDKLAQLLDFLKEHPGGSGIVYCLSRKKV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 665 DVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKDILVATdVA-GRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTG 743
Cdd:COG0514 244 EELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAG 322
|
170
....*....|....*.
gi 41054055 744 RAGKSGVAMTFLTKED 759
Cdd:COG0514 323 RDGLPAEALLLYGPED 338
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
377-562 |
8.25e-18 |
|
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: 83.15 E-value: 8.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 377 IRNWKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQN--RDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEDSDQ 454
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML---------SRVDALKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 455 GPYAIILAPTRELAQQ---IEEETIKFGkpLGIRTVAVIGGiSREDQGFRLRMgcEIVIATPGRLID-VLENRYLVLSRC 530
Cdd:cd18048 88 YPQCLCLSPTFELALQtgkVVEEMGKFC--VGIQVIYAIRG-NRPGKGTDIEA--QIVIGTPGTVLDwCFKLRLIDVTNI 162
|
170 180 190
....*....|....*....|....*....|...
gi 41054055 531 TYVVLDEADRMIDM-GFEPDVQKILEYIPVTNQ 562
Cdd:cd18048 163 SVFVLDEADVMINVqGHSDHSVRVKRSMPKECQ 195
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
403-741 |
4.46e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 85.46 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 403 PIQRQAI-----PIGLQNRDIIGVAETGSGKT--AAFLIpllvwiTTLPKIDRIedsdqgpyaIILAPTRELAQQIEEET 475
Cdd:COG1061 83 PYQQEALeallaALERGGGRGLVVAPTGTGKTvlALALA------AELLRGKRV---------LVLVPRRELLEQWAEEL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 476 IKFgkplgiRTVAVIGGISREDqgfrlrmGCEIVIATPGRLIDVLENRYLVlSRCTYVVLDEADRMIDMGFepdvQKILE 555
Cdd:COG1061 148 RRF------LGDPLAGGGKKDS-------DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 556 YIPV--------TnqkPDTDDAEDPEkmMQNFESGKHKYrqtvmftatmpPAVERLARSYLRRPAVVYI-------GSAG 620
Cdd:COG1061 210 AFPAayrlgltaT---PFRSDGREIL--LFLFDGIVYEY-----------SLKEAIEDGYLAPPEYYGIrvdltdeRAEY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 621 KPHERVEQKVILMSEGEKRKKLLEVLAS-GFEPPIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKA 699
Cdd:COG1061 274 DALSERLREALAADAERKDKILRELLREhPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRD 353
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 41054055 700 GAKDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGR 741
Cdd:COG1061 354 GELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGR 395
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
633-754 |
1.40e-15 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 74.17 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 633 MSEGEKRKKLLEVLASGFEP--PIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKDILVATDV 710
Cdd:cd18794 10 PKDKKDEKLDLLKRIKVEHLggSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVA 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 41054055 711 AGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGKSGVAMTF 754
Cdd:cd18794 90 FGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
385-538 |
6.23e-14 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 75.32 E-value: 6.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 385 LPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGV-AETGSGKTaafLIPLLVWITTLpkidriedsDQGPYAIILAP 463
Cdd:COG1204 7 PLEKVIEFLKERGIEELYPPQAEALEAGLLEGKNLVVsAPTASGKT---LIAELAILKAL---------LNGGKALYIVP 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41054055 464 TRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRlrmGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEA 538
Cdd:COG1204 75 LRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWLG---RYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA 146
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
653-756 |
5.07e-13 |
|
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: 65.03 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 653 PIIIFVNQKKGCDVLAKSLEkmgynactlhggkgqeqrefalsnlkagakdILVATDVAGRGIDIQDVSMVLNYDMAKNI 732
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90 100
....*....|....*....|....
gi 41054055 733 EDYIHRIGRTGRAGKSGVAMTFLT 756
Cdd:cd18785 54 ASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
624-768 |
7.50e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 72.07 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 624 ERVEQKVILMSE--GE--KRKKLLEVLAS--GFEPP--IIIFVNQKKGCDVLAKSLEKMGYNACTL------HGGKG--Q 687
Cdd:COG1111 318 PRFRKAMRLAEEadIEhpKLSKLREILKEqlGTNPDsrIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskEGDKGltQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 688 EQREFALSNLKAGAKDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGR--AGKSGVAMTFLTKeDSSVFYD 765
Cdd:COG1111 398 KEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRkrEGRVVVLIAKGTR-DEAYYWS 476
|
...
gi 41054055 766 LKQ 768
Cdd:COG1111 477 SRR 479
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
378-542 |
3.38e-12 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 66.28 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 378 RNWKEYSLPPHILEVIEKCGYKDPTPIQRQAIPIGLQN--RDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEDSDQG 455
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAML---------SQVEPANKY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 456 PYAIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMgcEIVIATPGRLID-VLENRYLVLSRCTYVV 534
Cdd:cd18047 72 PQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDwCSKLKFIDPKKIKVFV 149
|
....*...
gi 41054055 535 LDEADRMI 542
Cdd:cd18047 150 LDEADVMI 157
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
637-748 |
1.89e-11 |
|
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: 62.61 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 637 EKRKKLLEVLASGFEPPI----IIFVNQKKGCDVLAKSLEKMG-----YNACTLHGG-------------KGQEQrefAL 694
Cdd:cd18802 7 PKLQKLIEILREYFPKTPdfrgIIFVERRATAVVLSRLLKEHPstlafIRCGFLIGRgnssqrkrslmtqRKQKE---TL 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 41054055 695 SNLKAGAKDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRtGRAGKS 748
Cdd:cd18802 84 DKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNS 136
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
421-556 |
8.70e-11 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 60.88 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 421 VAETGSGKTAAFLIPLLvwittlpkiDRIEDsdQGPYAIILAPTRELAQQIEEETIKFGKPlGIRTVAVIGGISREDQGF 500
Cdd:cd00046 7 TAPTGSGKTLAALLAAL---------LLLLK--KGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREK 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 41054055 501 RLRMGCEIVIATPGRLI-DVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILEY 556
Cdd:cd00046 75 NKLGDADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVR 131
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
402-538 |
1.08e-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: 61.51 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 402 TPIQRQAI-PIGLQNRDIIGVAETGSGKTaafLIPLLVWITTLPKidriedsdQGPYAIILAPTRELAQQIEEETIKFGK 480
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKT---LIAELAILRALAT--------SGGKAVYIAPTRALVNQKEADLRERFG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 481 PLGIRTVAVIGGISREDQGFRlrmGCEIVIATPGRLiDVLENR--YLVLSRCTYVVLDEA 538
Cdd:cd17921 72 PLGKNVGLLTGDPSVNKLLLA---EADILVATPEKL-DLLLRNggERLIQDVRLVVVDEA 127
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
385-538 |
2.32e-10 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 64.09 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 385 LPPHILEVIEKCGYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEDsDQGPYAIILAPT 464
Cdd:COG1205 41 LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVL---------EALLE-DPGATALYLYPT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 465 RELAQQIEEETIKFGKPLGIR-TVAVI-GGISREDqgfR--LRMGCEIVIATPgrliDVLENRYL--------VLSRCTY 532
Cdd:COG1205 111 KALARDQLRRLRELAEALGLGvRVATYdGDTPPEE---RrwIREHPDIVLTNP----DMLHYGLLphhtrwarFFRNLRY 183
|
....*.
gi 41054055 533 VVLDEA 538
Cdd:COG1205 184 VVIDEA 189
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
638-740 |
7.99e-09 |
|
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: 54.79 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 638 KRKKLLEVLASGFEPP--IIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKD--ILVATDVAGR 713
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 41054055 714 GIDIQDVSMVLNYDMAKNI------EDYIHRIG 740
Cdd:cd18793 92 GLNLTAANRVILYDPWWNPaveeqaIDRAHRIG 124
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
403-538 |
8.04e-09 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 55.00 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 403 PIQRQAIPIGLQN----RDIIgVAETGSGKTA-AFLIPLLVWITTLpkidriedsdqgpyaIILAPTRELAQQIEEEtik 477
Cdd:cd17926 3 PYQEEALEAWLAHknnrRGIL-VLPTGSGKTLtALALIAYLKELRT---------------LIVVPTDALLDQWKER--- 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054055 478 FGKPLGIRTVAVIGGISREDQGfrlrmGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEA 538
Cdd:cd17926 64 FEDFLGDSSIGLIGGGKKKDFD-----DANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
655-748 |
9.54e-09 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 54.96 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 655 IIFVNQKKGCDVLAKSLEKMGYNACT-----LHGGK-GQEQREFALSNLKAGAKDILVATDVAGRGIDIQDVSMVLNYDM 728
Cdd:cd18796 42 LVFTNTRSQAERLAQRLRELCPDRVPpdfiaLHHGSlSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90 100
....*....|....*....|
gi 41054055 729 AKNIEDYIHRIGRTGRAGKS 748
Cdd:cd18796 122 PKSVARLLQRLGRSGHRPGA 141
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
405-538 |
1.95e-08 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 54.90 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 405 QRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLvwittlpkiDRIEdSDQGPYAIILAPTRELAQQIEEETIKFGKPLGI 484
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPIL---------EALL-RDPGSRALYLYPTKALAQDQLRSLRELLEQLGL 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054055 485 R-TVAVIGG-ISREDQGFRLRMGCEIVIATPgrliDVLEnrYLVL----------SRCTYVVLDEA 538
Cdd:cd17923 75 GiRVATYDGdTPREERRAIIRNPPRILLTNP----DMLH--YALLphhdrwarflRNLRYVVLDEA 134
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
416-538 |
1.05e-07 |
|
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: 53.04 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 416 RDIIGVAETGSGKTaafLIPLLVwITTLPKIDRiEDSDQGPYAIILAPTRELAQQiEEETIKFGKPLgirTVAVIGGISR 495
Cdd:cd18034 17 RNTIVVLPTGSGKT---LIAVML-IKEMGELNR-KEKNPKKRAVFLVPTVPLVAQ-QAEAIRSHTDL---KVGEYSGEMG 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 41054055 496 EDQGFRLRMGCE-----IVIATPGRLIDVLENRYLVLSRCTYVVLDEA 538
Cdd:cd18034 88 VDKWTKERWKEElekydVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
608-754 |
1.12e-07 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 55.49 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 608 LRRPaVVYIGSAGKPHER---VEQ-----KVILMSEGEKRKkllevlaSGfeppiIIFVNQKKGCDVLAKSLEKMGYNAC 679
Cdd:PRK11057 198 LNDP-LIQISSFDRPNIRytlVEKfkpldQLMRYVQEQRGK-------SG-----IIYCNSRAKVEDTAARLQSRGISAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 680 TLHGG-----KGQEQREFALSNLKagakdILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGKSGVAMTF 754
Cdd:PRK11057 265 AYHAGldndvRADVQEAFQRDDLQ-----IVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
638-742 |
1.46e-07 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 55.23 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 638 KRKKLLEVLASGFEP--PIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAG--AKDILVATDVAGR 713
Cdd:COG0553 534 KLEALLELLEELLAEgeKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAGGE 613
|
90 100 110
....*....|....*....|....*....|....*.
gi 41054055 714 GIDIQDVSMVLNYDM----AKnIE---DYIHRIGRT 742
Cdd:COG0553 614 GLNLTAADHVIHYDLwwnpAV-EEqaiDRAHRIGQT 648
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
638-744 |
2.90e-07 |
|
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: 50.43 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 638 KRKKLLEVLASGFE-------PPIIIFVNQKKGCDVLAKSLEKMGYN--ACTLHG------GKGQEQRE--FALSNLKAG 700
Cdd:cd18801 10 KLEKLEEIVKEHFKkkqegsdTRVIIFSEFRDSAEEIVNFLSKIRPGirATRFIGqasgksSKGMSQKEqkEVIEQFRKG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 41054055 701 AKDILVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGR 744
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
638-747 |
8.35e-07 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 52.98 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 638 KRKKLLE-----VLASGFEPPIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKDILVATDVAG 712
Cdd:PLN03137 662 KTKKCLEdidkfIKENHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFG 741
|
90 100 110
....*....|....*....|....*....|....*
gi 41054055 713 RGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGK 747
Cdd:PLN03137 742 MGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQ 776
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
638-747 |
9.89e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 52.57 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 638 KRKKLLEVLASGFE----PPIIIFVNQKKGCDVLAKSLEKMGYNA------CTLHGGKG---QEQREfALSNLKAGAKDI 704
Cdd:PRK13766 348 KLEKLREIVKEQLGknpdSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKGmsqKEQIE-ILDKFRAGEFNV 426
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 41054055 705 LVATDVAGRGIDIQDVSMVLNYDMAKNIEDYIHRIGRTGRAGK 747
Cdd:PRK13766 427 LVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGRQEE 469
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
399-558 |
3.70e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 47.67 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 399 KDPTPIQRQAI-----PIGLQNRDIIGVAETGSGKT--AAFLIPLLvwiTTLPKIDRIedsdqgpyaIILAPTRELAQQI 471
Cdd:pfam04851 2 LELRPYQIEAIenlleSIKNGQKRGLIVMATGSGKTltAAKLIARL---FKKGPIKKV---------LFLVPRKDLLEQA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 472 EEETIKFGKplgirTVAVIGGISREDQGFRLRMGCEIVIATPGRL--IDVLENRYLVLSRCTYVVLDEADRMIDMGFepd 549
Cdd:pfam04851 70 LEEFKKFLP-----NYVEIGEIISGDKKDESVDDNKIVVTTIQSLykALELASLELLPDFFDVIIIDEAHRSGASSY--- 141
|
....*....
gi 41054055 550 vQKILEYIP 558
Cdd:pfam04851 142 -RNILEYFK 149
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
397-618 |
1.33e-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: 46.76 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 397 GYKDPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVwittLPKIdriedsdqgpyAIILAPTRELAQ-QIEEEt 475
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL----LDGV-----------TLVVSPLISLMQdQVDRL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 476 ikfgKPLGIRTVAVIGGISREDQ---GFRLRMG-CEIVIATPGRL-----IDVLENRYLvLSRCTYVVLDEA-------- 538
Cdd:cd17920 73 ----QQLGIRAAALNSTLSPEEKrevLLRIKNGqYKLLYVTPERLlspdfLELLQRLPE-RKRLALIVVDEAhcvsqwgh 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 539 DrmidmgFEPDVQKILEYIpvtNQKPDTddaedpekmmqnfesgkhkyrQTVMFTATMPPAVERLARSYLR-RPAVVYIG 617
Cdd:cd17920 148 D------FRPDYLRLGRLR---RALPGV---------------------PILALTATATPEVREDILKRLGlRNPVIFRA 197
|
.
gi 41054055 618 S 618
Cdd:cd17920 198 S 198
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
404-513 |
1.57e-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: 46.58 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 404 IQRQAIPIGLQ-NRDIIGVAETGSGKTAAF---LIPLLVWITTLPKIDRIedsdqgpyAIILAPTRELAQQIEEE-TIKF 478
Cdd:cd18023 5 IQSEVFPDLLYsDKNFVVSAPTGSGKTVLFelaILRLLKERNPLPWGNRK--------VVYIAPIKALCSEKYDDwKEKF 76
|
90 100 110
....*....|....*....|....*....|....*
gi 41054055 479 GkPLGIRTVAVIGGISREDqgFRLRMGCEIVIATP 513
Cdd:cd18023 77 G-PLGLSCAELTGDTEMDD--TFEIQDADIILTTP 108
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
398-493 |
1.99e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 48.34 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 398 YKDPTPIQRQAIPIGLQNRDIIGVAETGSGKT-AAFLIPllvwITTLPKIDRIEDSDQGPYAIILAPTRELAQQIE---E 473
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAI----IDELFRLGREGELEDKVYCLYVSPLRALNNDIHrnlE 105
|
90 100
....*....|....*....|.
gi 41054055 474 EtikfgkPL-GIRTVAVIGGI 493
Cdd:PRK13767 106 E------PLtEIREIAKERGE 120
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
413-540 |
3.18e-05 |
|
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: 45.50 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 413 LQNRDIIGVAETGSGKTaafLIPLLVWITTLPKIdrieDSDQGPYAIILAPTREL-AQQIEEETIKFGKPlGIRTVAVIG 491
Cdd:cd17927 15 LKGKNTIICLPTGSGKT---FVAVLICEHHLKKF----PAGRKGKVVFLANKVPLvEQQKEVFRKHFERP-GYKVTGLSG 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 41054055 492 GISREDQGFRLRMGCEIVIATPGRLIDVLENRYLV-LSRCTYVVLDEADR 540
Cdd:cd17927 87 DTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVsLSDFSLLVFDECHN 136
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
401-537 |
8.54e-05 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 44.39 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 401 PTPIQRQAIPIGLQNRDIIGVAETGSGKT-AAFLIpllvwitTLPKIDRIEDSDQGPYAIILAPTRELAQQieeETIKFG 479
Cdd:cd18036 3 LRNYQLELVLPALRGKNTIICAPTGSGKTrVAVYI-------CRHHLEKRRSAGEKGRVVVLVNKVPLVEQ---QLEKFF 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054055 480 KPL-GIRTVAVIGGISREDQGFR-LRMGCEIVIATPGRLIDVL----ENRYLVLSRCTYVVLDE 537
Cdd:cd18036 73 KYFrKGYKVTGLSGDSSHKVSFGqIVKASDVIICTPQILINNLlsgrEEERVYLSDFSLLIFDE 136
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
415-537 |
1.40e-04 |
|
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: 43.34 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 415 NRDIIGVAETGSGKT-AAFlipllvwittLPKIDRIEDSDQGPYAII-LAPTRELAQQIEE------ETIKFGKPLGIRT 486
Cdd:cd17922 1 GRNVLIAAPTGSGKTeAAF----------LPALSSLADEPEKGVQVLyISPLKALINDQERrleeplDEIDLEIPVAVRH 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 41054055 487 vaviGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYL--VLSRCTYVVLDE 537
Cdd:cd17922 71 ----GDTSQSEKAKQLKNPPGILITTPESLELLLVNKKLreLFAGLRYVVVDE 119
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
398-537 |
2.17e-04 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 44.71 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 398 YKDPTPIQRQAIPIGLQNRDIIGVAETGSGKT-AAFLIPLLVWITTLPKIDRiedsDQGPYAIILAPTRELAQQIE---- 472
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDELARRPRPGEL----PDGLRVLYISPLKALANDIErnlr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 473 ---EE-TIKFGKPLGIRTVAVIGG--ISREDQGFRLRMgCEIVIATPgrlidvlENRYLVLSR---------CTYVVLDE 537
Cdd:COG1201 98 aplEEiGEAAGLPLPEIRVGVRTGdtPASERQRQRRRP-PHILITTP-------ESLALLLTSpdarellrgVRTVIVDE 169
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
403-537 |
5.57e-04 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 41.55 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 403 PIQRQAIPIGL-QNRDIIGVAETGSGKTaaflipLLVWITTLPKIDRiedsdqGPYAIILAPTRELAQQIEEETIKFgKP 481
Cdd:cd18028 4 PPQAEAVRAGLlKGENLLISIPTASGKT------LIAEMAMVNTLLE------GGKALYLVPLRALASEKYEEFKKL-EE 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 41054055 482 LGIRTVAVIGGISREDQGFRlrmGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDE 537
Cdd:cd18028 71 IGLKVGISTGDYDEDDEWLG---DYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE 123
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
401-492 |
8.01e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 41.25 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 401 PTPIQRQAIpiglqnRDIIG------------VAETGSGKTAAFLIPLLVWIttlpkidriedsDQGPYAIILAPTRELA 468
Cdd:cd17918 16 LTKDQAQAI------KDIEKdlhspepmdrllSGDVGSGKTLVALGAALLAY------------KNGKQVAILVPTEILA 77
|
90 100
....*....|....*....|....
gi 41054055 469 QQIEEETIKFGKPlgIRTVAVIGG 492
Cdd:cd17918 78 HQHYEEARKFLPF--INVELVTGG 99
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
404-540 |
9.47e-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: 40.96 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 404 IQRQAIPIGLQNRDIIGVAETGSGKTaafLIPLLVWITTLPKidriedsdQGPYAIILAPTRELAQQiEEETIKFGKPLG 483
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKT---IIAILVAADRLTK--------KGGKVLILAPSRPLVEQ-HAENLKRVLNIP 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 41054055 484 IRTVAVIGGISREDQGFRLRmGCEIVIATPGRL-IDVLENRYlVLSRCTYVVLDEADR 540
Cdd:cd18035 73 DKITSLTGEVKPEERAERWD-ASKIIVATPQVIeNDLLAGRI-TLDDVSLLIFDEAHH 128
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
614-751 |
2.61e-03 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 39.07 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 614 VYIGSAGKPHERVEQKVILMSEgekRKKLLEVLASGFEPPIIIFVNQKKGCDVLAKSLEKMGYnactLHGGKGQEQRE-- 691
Cdd:cd18795 9 VLGFNGLGIKLRVDVMNKFDSD---IIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRElv 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41054055 692 ---FALSNLKagakdILVATD--VAG-----RGIDIQDVSMVLNYDMAK-NIEDYIHRIGRTGRAG--KSGVA 751
Cdd:cd18795 82 eelFREGLIK-----VLVATStlAAGvnlpaRTVIIKGTQRYDGKGYRElSPLEYLQMIGRAGRPGfdTRGEA 149
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
400-537 |
4.20e-03 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 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: 350783 [Multi-domain] Cd Length: 192 Bit Score: 39.27 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 400 DPTPIQRQAIPIGLQNRDIIGVAETGSGKTaafliplLVWITTLPKIDRieDSDQGpYAIILAPTRELAQQIEEETI-KF 478
Cdd:cd18025 1 NPDAWQRELLDIVDRRESALIVAPTSSGKT-------FISYYCMEKVLR--ESDDG-VVVYVAPTKALVNQVVAEVYaRF 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054055 479 GKPLGIRTVAVIGGISREdqgFRLR--MGCEIVIATPgrliDVLEnrYLVLS--------RCTYVVLDE 537
Cdd:cd18025 71 SKKYPPSGKSLWGVFTRD---YRHNnpMNCQVLITVP----ECLE--ILLLSphnaswvpRIKYVIFDE 130
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
421-540 |
5.34e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 40.24 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054055 421 VAETGSGKTAaflIPLLVWITTLPKIdriedsdqGPYAIILAPTRELAQQIEEetiKFGKPLGIRT---VAVIGGISRED 497
Cdd:PRK13766 35 VLPTGLGKTA---IALLVIAERLHKK--------GGKVLILAPTKPLVEQHAE---FFRKFLNIPEekiVVFTGEVSPEK 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 41054055 498 QGfRLRMGCEIVIATPgRLI--DVLENRYlVLSRCTYVVLDEADR 540
Cdd:PRK13766 101 RA-ELWEKAKVIVATP-QVIenDLIAGRI-SLEDVSLLIFDEAHR 142
|
|
|