|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
158-531 |
1.96e-174 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 501.60 E-value: 1.96e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 158 MSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPgfLhLQRIRNDSRMGPTILVLS 237
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLP--L-LQRLDPSRPRAPQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 238 PTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRML 317
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 318 DMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVNIGNVDELVANksITQHIEVVAPMEKQRRLEQIL 397
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAET--IEQRYYLVDKRDKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 398 RSQEPGsKVIIFCSTKRMCDQLTRNLTRQ-FGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVKDIRAVVN 476
Cdd:COG0513 237 RDEDPE-RAIVFCNTKRGADRLAEKLQKRgISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVIN 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 18395852 477 YDFPNGVEDYVHRIGRTGRAGATGQAFTFFGDQDSKHasdLIKILEGANQRVPPQ 531
Cdd:COG0513 316 YDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRL---LRAIEKLIGQKIEEE 367
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
83-549 |
1.73e-172 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 501.61 E-value: 1.73e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 83 KYSRGSERVSRFSEGGRSG--PPYSN--GAANGVGDSAYGAAS-------------TRVPL--------PSSAPASELSP 137
Cdd:PTZ00110 29 DSSNPYGNYQANHQDNYGGfrPGYGNysGGYGGFGMNSYGSSTlgkrlqpidwksiNLVPFeknfykehPEVSALSSKEV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 138 EAYSRRHEIT-VSGGQVPPPLMSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPG 216
Cdd:PTZ00110 109 DEIRKEKEITiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 217 FLHlqrIRNDSRM----GPTILVLSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLN 292
Cdd:PTZ00110 189 IVH---INAQPLLrygdGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 293 DILEMRRISLRQISYLVLDEADRMLDMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVN-PAQVNIGNVDeL 371
Cdd:PTZ00110 266 DFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLD-L 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 372 VANKSITQHIEVVAPMEKQRRLEQIL-RSQEPGSKVIIFCSTKRMCDQLTRNLtRQFG--AAAIHGDKSQPERDNVLNQF 448
Cdd:PTZ00110 345 TACHNIKQEVFVVEEHEKRGKLKMLLqRIMRDGDKILIFVETKKGADFLTKEL-RLDGwpALCIHGDKKQEERTWVLNEF 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 449 RSGRTPVLVATDVAARGLDVKDIRAVVNYDFPNGVEDYVHRIGRTGRAGATGQAFTFFGDQDSKHASDLIKILEGANQRV 528
Cdd:PTZ00110 424 KTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPV 503
|
490 500
....*....|....*....|.
gi 18395852 529 PPQIREMATRGGGGmNKFSRW 549
Cdd:PTZ00110 504 PPELEKLSNERSNG-TERRRW 523
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
158-517 |
1.08e-120 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 365.66 E-value: 1.08e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 158 MSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKT----LGYLipgflhlQRIrNDSRMGPTI 233
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTaafgLGLL-------QKL-DVKRFRVQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 234 LVLSPTRELATQIQEEAVKFGRSSR-ISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDE 312
Cdd:PRK11776 76 LVLCPTRELADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 313 ADRMLDMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVnigNVDELVANKSITQHIEVVAPMEKQRR 392
Cdd:PRK11776 156 ADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEV---KVESTHDLPAIEQRFYEVSPDERLPA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 393 LEQILRSQEPGSkVIIFCSTKRMCDQLTRNLTRQ-FGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVKDI 471
Cdd:PRK11776 233 LQRLLLHHQPES-CVVFCNTKKECQEVADALNAQgFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 18395852 472 RAVVNYDFPNGVEDYVHRIGRTGRAGATGQAFTFFGDQDSKHASDL 517
Cdd:PRK11776 312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAI 357
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
169-364 |
1.84e-106 |
|
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: 319.31 E-value: 1.84e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 169 LLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHL---QRIRNDSrmGPTILVLSPTRELATQ 245
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHInaqPPLERGD--GPIVLVLAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 246 IQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQI 325
Cdd:cd17966 79 IQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 18395852 326 RKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVN 364
Cdd:cd17966 159 RKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
169-363 |
3.38e-101 |
|
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: 305.52 E-value: 3.38e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 169 LLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRNDSRMGPTILVLSPTRELATQIQE 248
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 249 EAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIRKI 328
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 18395852 329 VKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQV 363
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
138-366 |
1.30e-97 |
|
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: 298.08 E-value: 1.30e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 138 EAYSRRHEITVSGGQVPPPLMSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGF 217
Cdd:cd18049 4 EQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 218 LHLQRI----RNDsrmGPTILVLSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLND 293
Cdd:cd18049 84 VHINHQpfleRGD---GPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18395852 294 ILEMRRISLRQISYLVLDEADRMLDMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVNIG 366
Cdd:cd18049 161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
158-522 |
1.11e-94 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 298.26 E-value: 1.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 158 MSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHL--QRIRNDSRMGPTILV 235
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitRQPHAKGRRPVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 236 LSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADR 315
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 316 MLDMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVNIGNVDelVANKSITQHIEVVapmEKQRRLEq 395
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRN--TASEQVTQHVHFV---DKKRKRE- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 396 iLRSQEPGS----KVIIFCSTKRMCDQLTRNLTRQ-FGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVKD 470
Cdd:PRK10590 235 -LLSQMIGKgnwqQVLVFTRTKHGANHLAEQLNKDgIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEE 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 18395852 471 IRAVVNYDFPNGVEDYVHRIGRTGRAGATGQAFTFFGDQDSKHASDLIKILE 522
Cdd:PRK10590 314 LPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK 365
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
127-366 |
7.69e-93 |
|
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: 287.29 E-value: 7.69e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 127 PSSAPASELSPEAYSRRHEITVSGGQVPPPLMSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGS 206
Cdd:cd18050 31 PEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 207 GKTLGYLIPGFLHLQRI----RNDsrmGPTILVLSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGAD 282
Cdd:cd18050 111 GKTLAYLLPAIVHINHQpyleRGD---GPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 283 IVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQ 362
Cdd:cd18050 188 ICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQ 267
|
....
gi 18395852 363 VNIG 366
Cdd:cd18050 268 INIG 271
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
158-505 |
1.85e-89 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 284.14 E-value: 1.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 158 MSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRI-RNDSrmGPT-ILV 235
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFpRRKS--GPPrILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 236 LSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADR 315
Cdd:PRK11192 79 LTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 316 MLDMGFEPQIRKIVKEIPTKRQTLMYTATWP-KGVRKIAADLLVNPAQVNignvdelvAN------KSITQHIEVVAPME 388
Cdd:PRK11192 159 MLDMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVE--------AEpsrrerKKIHQWYYRADDLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 389 -KQRRLEQILRsQEPGSKVIIFCSTKRMCDQLTRNL-TRQFGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGL 466
Cdd:PRK11192 231 hKTALLCHLLK-QPEVTRSIVFVRTRERVHELAGWLrKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGI 309
|
330 340 350
....*....|....*....|....*....|....*....
gi 18395852 467 DVKDIRAVVNYDFPNGVEDYVHRIGRTGRAGATGQAFTF 505
Cdd:PRK11192 310 DIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
138-548 |
2.23e-89 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 286.68 E-value: 2.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 138 EAYSRRHEITVSGGQVPPPLMSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGF 217
Cdd:PLN00206 101 ELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPII 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 218 LHLQRIRN---DSRMGPTILVLSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDI 294
Cdd:PLN00206 181 SRCCTIRSghpSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 295 LEMRRISLRQISYLVLDEADRMLDMGFEPQIRKIVKEIPTKrQTLMYTATWPKGVRKIAADLLVNPAQVNIGNVDElvAN 374
Cdd:PLN00206 261 LSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNR--PN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 375 KSITQHIEVVAPMEKQRRLEQILRSQE---PgsKVIIFCSTKRMCDQLTRNLTRQFG--AAAIHGDKSQPERDNVLNQFR 449
Cdd:PLN00206 338 KAVKQLAIWVETKQKKQKLFDILKSKQhfkP--PAVVFVSSRLGADLLANAITVVTGlkALSIHGEKSMKERREVMKSFL 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 450 SGRTPVLVATDVAARGLDVKDIRAVVNYDFPNGVEDYVHRIGRTGRAGATGQAFTFFGDQDSKHASDLIKILEGANQRVP 529
Cdd:PLN00206 416 VGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIP 495
|
410
....*....|....*....
gi 18395852 530 PQIREMATRGGGGMNKFSR 548
Cdd:PLN00206 496 RELANSRYLGSGRKRKKKR 514
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
159-359 |
3.69e-85 |
|
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: 265.12 E-value: 3.69e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 159 SFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIP--GFLHLQRIRNDSRMG----PT 232
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPiiSKLLEDGPPSVGRGRrkayPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 233 ILVLSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDE 312
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18395852 313 ADRMLDMGFEPQIRKIVKE--IPTK--RQTLMYTATWPKGVRKIAADLLVN 359
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdMPPKgeRQTLMFSATFPREIQRLAADFLKN 211
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
160-511 |
3.99e-84 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 271.40 E-value: 3.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 160 FEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQR--IRNDSRMG-PTILVL 236
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQtpPPKERYMGePRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 237 SPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLE-RGADIVVATPGRLNDILEMRRISLRQISYLVLDEADR 315
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 316 MLDMGFEPQIRKIVKEIPTK--RQTLMYTATWPKGVRKIAADLLVNPAQVNIGnvDELVANKSITQHIEVVAPMEKQRRL 393
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIE--PENVASDTVEQHVYAVAGSDKYKLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 394 EQILRsQEPGSKVIIFCSTKRMCDQLTRNLTRQ-FGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVKDIR 472
Cdd:PRK01297 327 YNLVT-QNPWERVMVFANRKDEVRRIEERLVKDgINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGIS 405
|
330 340 350
....*....|....*....|....*....|....*....
gi 18395852 473 AVVNYDFPNGVEDYVHRIGRTGRAGATGQAFTFFGDQDS 511
Cdd:PRK01297 406 HVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDA 444
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
147-363 |
3.81e-78 |
|
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: 247.29 E-value: 3.81e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 147 TVSGGQVPPPLMSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHL--QRIR 224
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIkdQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 225 NDSRmGPTILVLSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEM---RRIS 301
Cdd:cd17953 81 KPGE-GPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTAnngRVTN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18395852 302 LRQISYLVLDEADRMLDMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQV 363
Cdd:cd17953 160 LRRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
167-505 |
4.93e-78 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 253.74 E-value: 4.93e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 167 PELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHL---QRIRNDSRMGPTILVLSPTRELA 243
Cdd:PRK04837 17 PQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshPAPEDRKVNQPRALIMAPTRELA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 244 TQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEP 323
Cdd:PRK04837 97 VQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 324 QIRKIVKEIP--TKRQTLMYTATWPKGVRKIAADLLVNPAQVNIGnvDELVANKSITQhiEVVAP-MEKQRRLEQILRSQ 400
Cdd:PRK04837 177 DIRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEHMNNPEYVEVE--PEQKTGHRIKE--ELFYPsNEEKMRLLQTLIEE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 401 EPGSKVIIFCSTKRMCDQLTRNLtrqfgAAAIH------GDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVKDIRAV 474
Cdd:PRK04837 253 EWPDRAIIFANTKHRCEEIWGHL-----AADGHrvglltGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350
....*....|....*....|....*....|.
gi 18395852 475 VNYDFPNGVEDYVHRIGRTGRAGATGQAFTF 505
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
169-363 |
1.33e-77 |
|
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: 244.68 E-value: 1.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 169 LLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHL--QRIRNDSRMGPTILVLSPTRELATQI 246
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLdlQPIPREQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 247 QEEAVKFGRSSrISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIR 326
Cdd:cd17958 81 EAECSKYSYKG-LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 18395852 327 KIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQV 363
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
148-357 |
3.55e-77 |
|
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: 246.03 E-value: 3.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 148 VSGGQVPPPLMSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIP---GFLHlQRIR 224
Cdd:cd18052 33 VTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPvltGMMK-EGLT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 225 NDSRMG---PTILVLSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRIS 301
Cdd:cd18052 112 ASSFSEvqePQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKIS 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 302 LRQISYLVLDEADRMLDMGFEPQIRKIVKE--IPTK--RQTLMYTATWPKGVRKIAADLL 357
Cdd:cd18052 192 LSKLKYLILDEADRMLDMGFGPEIRKLVSEpgMPSKedRQTLMFSATFPEEIQRLAAEFL 251
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
158-505 |
1.54e-75 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 253.23 E-value: 1.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 158 MSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLqrirNDSRMGPTILVLS 237
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL----DPELKAPQILVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 238 PTRELATQIQEEAVKFGRSSR-ISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRM 316
Cdd:PRK11634 82 PTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 317 LDMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVNIGNvdELVANKSITQHIEVVAPMEKQRRLEQI 396
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS--SVTTRPDISQSYWTVWGMRKNEALVRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 397 LRSqEPGSKVIIFCSTKRMCDQLTRNLTRQ-FGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVKDIRAVV 475
Cdd:PRK11634 240 LEA-EDFDAAIIFVRTKNATLEVAEALERNgYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVV 318
|
330 340 350
....*....|....*....|....*....|
gi 18395852 476 NYDFPNGVEDYVHRIGRTGRAGATGQAFTF 505
Cdd:PRK11634 319 NYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
158-529 |
3.22e-74 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 248.33 E-value: 3.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 158 MSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIP---GFLHLQRIRNDSRMGPTIL 234
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAvmnRLLSRPALADRKPEDPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 235 VLSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRI-SLRQISYLVLDEA 313
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 314 DRMLDMGFEPQIRKIVKEIP--TKRQTLMYTATWPKGVRKIAADLLVNPAQVNIGNvdELVANKSITQHIEVVAPMEKQR 391
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPerGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVET--ETITAARVRQRIYFPADEEKQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 392 RLEQILrSQEPGSKVIIFCSTKRMCDQLTRNLTRQ-FGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVKD 470
Cdd:PRK04537 247 LLLGLL-SRSEGARTMVFVNTKAFVERVARTLERHgYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDG 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 18395852 471 IRAVVNYDFPNGVEDYVHRIGRTGRAGATGQAFTFFGDqdsKHASDLIKILEGANQRVP 529
Cdd:PRK04537 326 VKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACE---RYAMSLPDIEAYIEQKIP 381
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
169-363 |
3.11e-73 |
|
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: 233.46 E-value: 3.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 169 LLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRNDSRM-GPTILVLSPTRELATQIQ 247
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGeGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 248 EEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIRK 327
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 18395852 328 IVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQV 363
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
169-363 |
1.35e-71 |
|
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: 229.90 E-value: 1.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 169 LLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQR--IRNDSRM--GPTILVLSPTRELAT 244
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpPLDEETKddGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 245 QIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQ 324
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18395852 325 IRKIVKEIPTK--------------------RQTLMYTATWPKGVRKIAADLLVNPAQV 363
Cdd:cd17945 161 VTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
159-517 |
3.18e-70 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 232.79 E-value: 3.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 159 SFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGflhLQRIrNDSRMGPTILVLSP 238
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAA---LQLI-DYDLNACQALILAP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 239 TRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLD 318
Cdd:PTZ00424 105 TRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 319 MGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVNIGNvDELVAnKSITQHieVVAPMEKQRRLEQILR 398
Cdd:PTZ00424 185 RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKK-DELTL-EGIRQF--YVAVEKEEWKFDTLCD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 399 SQEPGS--KVIIFCSTKRMCDQLTRNLT-RQFGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVKDIRAVV 475
Cdd:PTZ00424 261 LYETLTitQAIIYCNTRRKVDYLTKKMHeRDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVI 340
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 18395852 476 NYDFPNGVEDYVHRIGRTGRAGATGQAFTFFGDQDSKHASDL 517
Cdd:PTZ00424 341 NYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
148-359 |
3.89e-67 |
|
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: 219.14 E-value: 3.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 148 VSGGQVPPPLMSFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIP----------GF 217
Cdd:cd18051 11 ATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPilsqiyeqgpGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 218 LHLQRIRNDSRMG--PTILVLSPTRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDIL 295
Cdd:cd18051 91 SLPSESGYYGRRKqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDML 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18395852 296 EMRRISLRQISYLVLDEADRMLDMGFEPQIRKIVKE--IPTK--RQTLMYTATWPKGVRKIAADLLVN 359
Cdd:cd18051 171 ERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPTgeRQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
182-352 |
8.07e-64 |
|
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: 207.48 E-value: 8.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 182 TPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRNdsrmGPTILVLSPTRELATQIQEEAVKFGRSSRISC 261
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN----GPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 262 TCLYGGAPKGPQLRDLeRGADIVVATPGRLNDILEMRRiSLRQISYLVLDEADRMLDMGFEPQIRKIVKEIPTKRQTLMY 341
Cdd:pfam00270 77 ASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
|
170
....*....|.
gi 18395852 342 TATWPKGVRKI 352
Cdd:pfam00270 155 SATLPRNLEDL 165
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
167-354 |
2.01e-62 |
|
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: 205.51 E-value: 2.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 167 PELLREVLSAGFSAPTPIQAQSWPIAMQ-GRDIVAIAKTGSGKTLGYLIPGFlhlQRIRNDSRMGPT----ILVLSPTRE 241
Cdd:cd17964 3 PSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAI---QSLLNTKPAGRRsgvsALIISPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 242 LATQIQEEAVKF-GRSSRISCTCLYGGAPKGPQLRDLER-GADIVVATPGRLNDILE--MRRISLRQISYLVLDEADRML 317
Cdd:cd17964 80 LALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18395852 318 DMGFEPQIRKIVKEIPTK----RQTLMYTATWPKGVRKIAA 354
Cdd:cd17964 160 DMGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIAR 200
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
377-506 |
4.55e-62 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 201.58 E-value: 4.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 377 ITQHIEVVAPMEKQRRLEQILRSQEPGSKVIIFCSTKRMCDQLTRNLTR-QFGAAAIHGDKSQPERDNVLNQFRSGRTPV 455
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEElGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 18395852 456 LVATDVAARGLDVKDIRAVVNYDFPNGVEDYVHRIGRTGRAGATGQAFTFF 506
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
159-363 |
5.14e-61 |
|
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: 201.39 E-value: 5.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 159 SFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLqrIRNDSRMgpTILVLSP 238
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL--LENPQRF--FALVLAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 239 TRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILE-MRRISLRQISYLVLDEADRML 317
Cdd:cd17954 77 TRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEnTKGFSLKSLKFLVMDEADRLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18395852 318 DMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQV 363
Cdd:cd17954 157 NMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
159-364 |
9.86e-60 |
|
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: 198.30 E-value: 9.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 159 SFEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRirNDSRMGPTILVLSP 238
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKA--HSPTVGARALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 239 TRELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLD 318
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18395852 319 MGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVN 364
Cdd:cd17959 160 MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
169-363 |
8.62e-57 |
|
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: 190.16 E-value: 8.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 169 LLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPgflHLQRIRNDSRMGPTI--LVLSPTRELATQI 246
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLP---ILERLLYRPKKKAATrvLVLVPTRELAMQC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 247 QEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDIL-EMRRISLRQISYLVLDEADRMLDMGFEPQI 325
Cdd:cd17947 78 FSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFADEL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 18395852 326 RKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQV 363
Cdd:cd17947 158 KEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
173-380 |
6.34e-56 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 188.08 E-value: 6.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 173 VLSAGFSAPTPIQAQSWPIAMQG-RDIVAIAKTGSGKTLGYLIPGFLHLQRirndsRMGPTILVLSPTRELATQIQEEAV 251
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR-----GKGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 252 KFGRSSRISCTCLYGGAPKGPQLRDLERG-ADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIRKIVK 330
Cdd:smart00487 76 KLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18395852 331 EIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVNIGNvdelVANKSITQH 380
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF----TPLEPIEQF 201
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
169-364 |
6.61e-55 |
|
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: 185.24 E-value: 6.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 169 LLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPgfLHLQRIRNDSRM------GPTILVLSPTREL 242
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLP--LIMFALEQEKKLpfikgeGPYGLIVCPSREL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 243 ATQIQEEAVKF------GRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRM 316
Cdd:cd17951 79 ARQTHEVIEYYckalqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18395852 317 LDMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVN 364
Cdd:cd17951 159 IDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
169-366 |
1.70e-54 |
|
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: 183.94 E-value: 1.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 169 LLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRNDSrmGPTILVLSPTRELATQIQE 248
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK--GLRALILAPTRELASQIYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 249 EAVKFGRSSRISCTCLYGG-APKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIRK 327
Cdd:cd17957 79 ELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18395852 328 IVKEIPTKR-QTLMYTATWPKGVRKIAADLLVNPAQVNIG 366
Cdd:cd17957 159 ILAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
169-364 |
3.35e-52 |
|
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: 178.15 E-value: 3.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 169 LLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGF-LHLQRIRNDSRMGPTILVLSPTRELATQIQ 247
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeILLKRKANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 248 EEAVKF--GRSSRISCTCLYGGAPKGPQLRDLER-GADIVVATPGRLNDILEMR--RISLRQISYLVLDEADRMLDMGFE 322
Cdd:cd17960 81 EVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKadKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 18395852 323 PQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVN 364
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
177-360 |
5.25e-51 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 175.08 E-value: 5.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 177 GFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRI-----RNDsrmGPTILVLSPTRELATQIQEEAV 251
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLeprvdRSD---GTLALVLVPTRELALQIYEVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 252 KFGRSSR-ISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEM-RRISLRQISYLVLDEADRMLDMGFEPQIRKIV 329
Cdd:cd17949 87 KLLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITKIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18395852 330 KEI-------------PTKRQTLMYTATWPKGVRKIAADLLVNP 360
Cdd:cd17949 167 ELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDP 210
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
160-344 |
5.69e-50 |
|
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: 172.02 E-value: 5.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 160 FEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPgflHLQRIRNDSrMGPTILVLSPT 239
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP---ILQRLSEDP-YGIFALVLTPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 240 RELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILE---MRRISLRQISYLVLDEADRM 316
Cdd:cd17955 77 RELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRL 156
|
170 180
....*....|....*....|....*...
gi 18395852 317 LDMGFEPQIRKIVKEIPTKRQTLMYTAT 344
Cdd:cd17955 157 LTGSFEDDLATILSALPPKRQTLLFSAT 184
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
160-364 |
2.09e-49 |
|
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: 170.56 E-value: 2.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 160 FEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPgflHLQRIRNDSRmGPTILVLSPT 239
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIP---ILEKIDPKKD-VIQALILVPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 240 RELATQIQEEAVKFGRSSRISCTCLYGGAPkgpqLRD----LERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADR 315
Cdd:cd17940 77 RELALQTSQVCKELGKHMGVKVMVTTGGTS----LRDdimrLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18395852 316 MLDMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVN 364
Cdd:cd17940 153 LLSQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
170-365 |
4.02e-49 |
|
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: 169.78 E-value: 4.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 170 LREvlsAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRNDSRMGPTILVLSPTRELATQIQEE 249
Cdd:cd17941 5 LKE---AGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 250 AVKFGRSSRISCTCLYGGapkgpqlRDLERGAD------IVVATPGR-LNDILEMRRISLRQISYLVLDEADRMLDMGFE 322
Cdd:cd17941 82 LRKVGKYHSFSAGLIIGG-------KDVKEEKErinrmnILVCTPGRlLQHMDETPGFDTSNLQMLVLDEADRILDMGFK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18395852 323 PQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQVNI 365
Cdd:cd17941 155 ETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
169-344 |
7.49e-48 |
|
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: 167.42 E-value: 7.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 169 LLREVLSAGFSAPTPIQAQSWPIAM-QGRDIVAIAKTGSGKTLGYLIP---GFLHLQ--RIRNDSRMGPTILVLSPTREL 242
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPileRLLSQKssNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 243 ATQIQEEAVKFGRSSRISCTCLYGG--APKgpQLRDLERGADIVVATPGRLNDILEMRR---ISLRQISYLVLDEADRML 317
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGlaVQK--QERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEADRML 158
|
170 180 190
....*....|....*....|....*....|....*
gi 18395852 318 DMG-FEpQIRKIVKEIP-------TKRQTLMYTAT 344
Cdd:cd17946 159 EKGhFA-ELEKILELLNkdragkkRKRQTFVFSAT 192
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
169-363 |
5.69e-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: 163.87 E-value: 5.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 169 LLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLH-LQRIRNdsrmgPTILVLSPTRELATQIQ 247
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRcLTEHRN-----PSALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 248 EEAVKFGRSS-RISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIR 326
Cdd:cd17962 76 DQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 18395852 327 KIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQV 363
Cdd:cd17962 156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
170-353 |
2.80e-46 |
|
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: 162.14 E-value: 2.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 170 LREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRNDSRMGPTILVLSPTRELATQIQEE 249
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 250 AVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRR-ISLRQISYLVLDEADRMLDMGFEPQIRKI 328
Cdd:cd17942 82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgFLYKNLQCLIIDEADRILEIGFEEEMRQI 161
|
170 180
....*....|....*....|....*
gi 18395852 329 VKEIPTKRQTLMYTATWPKGVRKIA 353
Cdd:cd17942 162 IKLLPKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
168-365 |
3.01e-44 |
|
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: 156.33 E-value: 3.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 168 ELLREVLSAGFSAPTPIQAQS-WPIaMQGRDIVAIAKTGSGKTLGYLIpgfLHLQRIRNDSRMgPTILVLSPTRELATQI 246
Cdd:cd17939 7 DLLRGIYAYGFEKPSAIQQRAiVPI-IKGRDVIAQAQSGTGKTATFSI---GALQRIDTTVRE-TQALVLAPTRELAQQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 247 QEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIR 326
Cdd:cd17939 82 QKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIY 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 18395852 327 KIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPaqVNI 365
Cdd:cd17939 162 DIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDP--VRI 198
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
167-361 |
7.17e-41 |
|
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: 147.35 E-value: 7.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 167 PELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPgflHLQRI-----RNDSRMGPTILVLSPTRE 241
Cdd:cd17961 3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALP---IIQKIlkakaESGEEQGTRALILVPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 242 LATQIQEEAVKF--GRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILE-MRRISLRQISYLVLDEADRMLD 318
Cdd:cd17961 80 LAQQVSKVLEQLtaYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLEsGSLLLLSTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18395852 319 MGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPA 361
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
160-364 |
1.29e-40 |
|
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: 146.70 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 160 FEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPgflHLQRIRNdsrmgptiLVLSPT 239
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLP---VLQIVVA--------LILEPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 240 RELATQIQEEAVKFGR---SSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRM 316
Cdd:cd17938 70 RELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18395852 317 LDMGFEPQIRKIVKEIPT-----KR-QTLMYTATW--PKgVRKIAADLLVNPAQVN 364
Cdd:cd17938 150 LSQGNLETINRIYNRIPKitsdgKRlQVIVCSATLhsFE-VKKLADKIMHFPTWVD 204
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
183-353 |
6.61e-40 |
|
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: 144.61 E-value: 6.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 183 PIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRNDSRMG--PTILVLSPTRELATQIQEEAVKFGRssRIS 260
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGraPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 261 CTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIRKIV-----KEIPTK 335
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsykKDSEDN 172
|
170
....*....|....*...
gi 18395852 336 RQTLMYTATWPKGVRKIA 353
Cdd:cd17944 173 PQTLLFSATCPDWVYNVA 190
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
166-363 |
1.08e-39 |
|
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: 143.87 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 166 PPELLREVLSAGFSAPTPIQAQSWPIAMQG--RDIVAIAKTGSGKTLGYLIPGflhLQRIRNDSRMgPTILVLSPTRELA 243
Cdd:cd17963 2 KPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAM---LSRVDPTLKS-PQALCLAPTRELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 244 TQIQEEAVKFGRSSRISCTClyggAPKGPQLRDLER-GADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDM-GF 321
Cdd:cd17963 78 RQIGEVVEKMGKFTGVKVAL----AVPGNDVPRGKKiTAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 18395852 322 EPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQV 363
Cdd:cd17963 154 GDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
169-347 |
1.44e-38 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 140.86 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 169 LLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGflhLQRIRNDSRmGPTILVLSPTRELATQIQE 248
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIA---LESLDLERR-HPQVLILAPTREIAVQIHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 249 EAVKFGRSSR-ISCTCLYGGAPkgpQLRDLER--GADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQI 325
Cdd:cd17943 77 VFKKIGKKLEgLKCEVFIGGTP---VKEDKKKlkGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDV 153
|
170 180
....*....|....*....|..
gi 18395852 326 RKIVKEIPTKRQTLMYTATWPK 347
Cdd:cd17943 154 NWIFSSLPKNKQVIAFSATYPK 175
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
160-363 |
4.53e-38 |
|
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: 139.52 E-value: 4.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 160 FEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGflhLQRIRNDSRmGPTILVLSPT 239
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISV---LQCLDIQVR-ETQALILSPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 240 RELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDM 319
Cdd:cd18045 77 RELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18395852 320 GFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQV 363
Cdd:cd18045 157 GFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
162-363 |
6.01e-38 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350708 [Multi-domain] Cd Length: 208 Bit Score: 139.40 E-value: 6.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 162 ATGF-----PPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGflhLQRIrNDSRMGPTILVL 236
Cdd:cd17950 1 SSGFrdfllKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLST---LQQL-EPVDGQVSVLVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 237 SPTRELATQIQEEAVKFGRS-SRISCTCLYGGAPKGPQLRDLE-RGADIVVATPGRLNDILEMRRISLRQISYLVLDEAD 314
Cdd:cd17950 77 CHTRELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18395852 315 RML-DMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQV 363
Cdd:cd17950 157 KMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
388-497 |
7.54e-38 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 135.80 E-value: 7.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 388 EKQRRLEQILRsQEPGSKVIIFCSTKRMCDQLTRNLTRQFGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLD 467
Cdd:pfam00271 1 EKLEALLELLK-KERGGKVLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 18395852 468 VKDIRAVVNYDFPNGVEDYVHRIGRTGRAG 497
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
160-363 |
3.44e-37 |
|
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: 137.19 E-value: 3.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 160 FEATGFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGflhLQRIrNDSRMGPTILVLSPT 239
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISI---LQQI-DTSLKATQALVLAPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 240 RELATQIQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDM 319
Cdd:cd18046 77 RELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18395852 320 GFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNPAQV 363
Cdd:cd18046 157 GFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
177-391 |
4.93e-36 |
|
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: 134.80 E-value: 4.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 177 GFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPgFLH--LQRIRNDSRMGPTI--LVLSPTRELATQIQEEAVK 252
Cdd:cd17948 9 GITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLP-IIQrlLRYKLLAEGPFNAPrgLVITPSRELAEQIGSVAQS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 253 FGRSSRISCTCLYGGAPKGpQLRDLERG-ADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIRKIVKE 331
Cdd:cd17948 88 LTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18395852 332 IP-------------TKRQTLMYTATWPKGVRKIAADllvnpaqvnIGNVDELvaNKSITQHIEVVAPMEKQR 391
Cdd:cd17948 167 FPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSK---------VIDVDSI--ETVTSDKLHRLMPHVKQK 228
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
168-510 |
5.18e-30 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 123.71 E-value: 5.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 168 ELLREVLsaGFSAPTPIQAQswpI---AMQGRDIVAIAKTGSGKTLGYLIPGFLhlqrirndsRMGPTILVlSPtreLat 244
Cdd:COG0514 7 EVLKRVF--GYDSFRPGQEE---IieaVLAGRDALVVMPTGGGKSLCYQLPALL---------LPGLTLVV-SP---L-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 245 qI-----QEEAVkfgRSSRISCTCLYGGAPKGPQ---LRDLERGA-DIVVATPGRLN--DILEmrRISLRQISYLVLDEA 313
Cdd:COG0514 67 -IalmkdQVDAL---RAAGIRAAFLNSSLSAEERrevLRALRAGElKLLYVAPERLLnpRFLE--LLRRLKISLFAIDEA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 314 --------DrmldmgFEP---QIRKIVKEIPtKRQTLMYTATWPKGVRK-IAADLLVNPAQVNIGNVDElvanKSITQHI 381
Cdd:COG0514 141 hcisqwghD------FRPdyrRLGELRERLP-NVPVLALTATATPRVRAdIAEQLGLEDPRVFVGSFDR----PNLRLEV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 382 EVVAPMEKQRRLEQILRSQEPGSkVIIFCSTKRMCDQLTRNLTRQ-FGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATd 460
Cdd:COG0514 210 VPKPPDDKLAQLLDFLKEHPGGS-GIVYCLSRKKVEELAEWLREAgIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT- 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 18395852 461 VA-ARGLDVKDIRAVVNYDFPNGVEDYVHRIGRTGRAGATGQAFTFFGDQD 510
Cdd:COG0514 288 IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPED 338
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
417-497 |
1.46e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 106.14 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 417 DQLTRNLT-RQFGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVKDIRAVVNYDFPNGVEDYVHRIGRTGR 495
Cdd:smart00490 1 EELAELLKeLGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 18395852 496 AG 497
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
170-352 |
3.04e-26 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 107.33 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 170 LREVLSA-GFSAPTPIQAQSWPIAMQG---------RDIVAIAKTGSGKTLGYLIPgflHLQRIRndSRMGPTI--LVLS 237
Cdd:cd17956 1 LLKNLQNnGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLP---IVQALS--KRVVPRLraLIVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 238 PTRELATQIQEEAVKFGRSSRIScTCLYGG----APKGPQLRDLERG-----ADIVVATPGRLND-ILEMRRISLRQISY 307
Cdd:cd17956 76 PTKELVQQVYKVFESLCKGTGLK-VVSLSGqksfKKEQKLLLVDTSGrylsrVDILVATPGRLVDhLNSTPGFTLKHLRF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18395852 308 LVLDEADRMLDMGFEPQIRKIVKEI-------PTKRQTLMYTATWPKGVRKI 352
Cdd:cd17956 155 LVIDEADRLLNQSFQDWLETVMKALgrptapdLGSFGDANLLERSVRPLQKL 206
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
195-475 |
1.21e-23 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 105.11 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 195 GRDIVAIAKTGSGKT-LGYLIpgflhLQRIRNDSRmgptILVLSPTRELATQIQEEAVKFGRSSRIsctclyGGAPKgpq 273
Cdd:COG1061 100 GGRGLVVAPTGTGKTvLALAL-----AAELLRGKR----VLVLVPRRELLEQWAEELRRFLGDPLA------GGGKK--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 274 lrdlERGADIVVATPGRLNDILEMRRISlRQISYLVLDEADRmldmGFEPQIRKIVKEIPTKRqTLMYTATwPK------ 347
Cdd:COG1061 162 ----DSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFPAAY-RLGLTAT-PFrsdgre 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 348 -------GVRK-------IAADLLVNPA--QVNIGNVDELVANKSITQHI-EVVAPME--KQRRLEQILRSQEPGSKVII 408
Cdd:COG1061 231 illflfdGIVYeyslkeaIEDGYLAPPEyyGIRVDLTDERAEYDALSERLrEALAADAerKDKILRELLREHPDDRKTLV 310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18395852 409 FCSTKRMCDQLTRNLTRQ-FGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVKDIRAVV 475
Cdd:COG1061 311 FCSSVDHAEALAELLNEAgIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
144-360 |
5.01e-23 |
|
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: 98.17 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 144 HEITVSGGQVPPPLMS---FEATGFPPELLREVLSAGFSAPTPIQAQSWP--IAMQGRDIVAIAKTGSGKTLGYLIPgfl 218
Cdd:cd18048 1 HRVEVLQRDPTSPLFSvksFEELHLKEELLRGIYAMGFNRPSKIQENALPmmLADPPQNLIAQSQSGTGKTAAFVLA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 219 HLQRIrNDSRMGPTILVLSPTRELATQ---IQEEAVKFGRSSRISCTCLYGGAPKGPQLRdlergADIVVATPGRLND-I 294
Cdd:cd18048 78 MLSRV-DALKLYPQCLCLSPTFELALQtgkVVEEMGKFCVGIQVIYAIRGNRPGKGTDIE-----AQIVIGTPGTVLDwC 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18395852 295 LEMRRISLRQISYLVLDEADRMLDM-GFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNP 360
Cdd:cd18048 152 FKLRLIDVTNISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
181-347 |
2.02e-19 |
|
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: 88.20 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 181 PTPIQ---------------AQSWPIAMQGRDIVAIA-KTGSGKTLGYLIPGFLHLQR---------------IRNDSRM 229
Cdd:cd17965 31 PSPIQtlaikkllktlmrkvTKQTSNEEPKLEVFLLAaETGSGKTLAYLAPLLDYLKRqeqepfeeaeeeyesAKDTGRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 230 GPTILVlsPTRELATQIQEEAvkfgrsSRISCTCLYGGAP----KGPQLRDLER----GADIVVATPGRLNDILEMRRIS 301
Cdd:cd17965 111 RSVILV--PTHELVEQVYSVL------KKLSHTVKLGIKTfssgFGPSYQRLQLafkgRIDILVTTPGKLASLAKSRPKI 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18395852 302 LRQISYLVLDEADRMLDMGFEPQIRKIVKEIPTKRQTLMYTATWPK 347
Cdd:cd17965 183 LSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPK 228
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
195-344 |
5.60e-19 |
|
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: 83.99 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 195 GRDIVAIAKTGSGKTLGYLIPGFLHLqrirnDSRmGPTILVLSPTRELATQiQEEAVKFGRSSRISCTCLYGGAPKGPQL 274
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLL-----LKK-GKKVLVLVPTKALALQ-TAERLRELFGPGIRVAVLVGGSSAEERE 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18395852 275 RDLERGADIVVATPGRL-NDILEMRRISLRQISYLVLDEADRMLDMGFEPQIRK--IVKEIPTKRQTLMYTAT 344
Cdd:cd00046 74 KNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
380-506 |
8.87e-18 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 79.95 E-value: 8.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 380 HIEV--VAPMEKQRRLEQILRSQEPGSKVIIFCSTKRMCDQLTRNL-TRQFGAAAIHGDKSQPERDNVLNQFRSGRTPVL 456
Cdd:cd18794 5 FYSVrpKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLqSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 18395852 457 VATDVAARGLDVKDIRAVVNYDFPNGVEDYVHRIGRTGRAGATGQAFTFF 506
Cdd:cd18794 85 VATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
159-360 |
1.22e-16 |
|
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: 78.99 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 159 SFEATGFPPELLREVLSAGFSAPTPIQAQSWP--IAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRNDSRmgptILVL 236
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPlmLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ----CLCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 237 SPTRELATQ---IQEEAVKFGRSSRISCTCLYGGAPKGPQLRDlergaDIVVATPGRLND-ILEMRRISLRQISYLVLDE 312
Cdd:cd18047 78 SPTYELALQtgkVIEQMGKFYPELKLAYAVRGNKLERGQKISE-----QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18395852 313 ADRML-DMGFEPQIRKIVKEIPTKRQTLMYTATWPKGVRKIAADLLVNP 360
Cdd:cd18047 153 ADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
164-504 |
3.06e-16 |
|
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: 82.58 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 164 GFPPELLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGflhLQRIRNDSRmgPTILVLSPTRELA 243
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPV---LEALLEDPG--ATALYLYPTKALA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 244 ----TQIQEEAVKFGRssRISCTCLYGGAPKG--PQLRDlerGADIVVATPgrlnDILEM---------RRIsLRQISYL 308
Cdd:COG1205 115 rdqlRRLRELAEALGL--GVRVATYDGDTPPEerRWIRE---HPDIVLTNP----DMLHYgllphhtrwARF-FRNLRYV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 309 VLDEA---------------DRML----DMGFEPQIrkivkeiptkrqtLMYTATW-----------------------P 346
Cdd:COG1205 185 VIDEAhtyrgvfgshvanvlRRLRricrHYGSDPQF-------------ILASATIgnpaehaerltgrpvtvvdedgsP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 347 KGVRKIAadlLVNPAQVNIGnvdelVANKSITQHIEVVApmekqrrleQILRSqepGSKVIIFCSTKRMCDQLTRNLTRQ 426
Cdd:COG1205 252 RGERTFV---LWNPPLVDDG-----IRRSALAEAARLLA---------DLVRE---GLRTLVFTRSRRGAELLARYARRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 427 FgAAAIHGDKSQP--------ERDNVLNQFRSGRTPVLVAT-------DVAarGLDvkdirAVVNYDFPNGVEDYVHRIG 491
Cdd:COG1205 312 L-REPDLADRVAAyragylpeERREIERGLRSGELLGVVSTnalelgiDIG--GLD-----AVVLAGYPGTRASFWQQAG 383
|
410
....*....|...
gi 18395852 492 RTGRAGATGQAFT 504
Cdd:COG1205 384 RAGRRGQDSLVVL 396
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
389-498 |
3.13e-16 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 82.47 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 389 KQRRLEQILRSQ---EPGSKVIIFCSTKRMCDQLTRNLTRQ-------FGAAAIHGDK--SQPERDNVLNQFRSGRTPVL 456
Cdd:COG1111 336 KLSKLREILKEQlgtNPDSRIIVFTQYRDTAEMIVEFLSEPgikagrfVGQASKEGDKglTQKEQIEILERFRAGEFNVL 415
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 18395852 457 VATDVAARGLDVKDIRAVVNYD-FPNGVEdYVHRIGRTGRAGA 498
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEpVPSEIR-SIQRKGRTGRKRE 457
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
166-510 |
1.49e-13 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 73.59 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 166 PPELLREVLsaGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLhlqrirndsRMGPTiLVLSPTRELatq 245
Cdd:PRK11057 13 AKQVLQETF--GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALV---------LDGLT-LVVSPLISL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 246 iQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLER----GADIVVATPGRL--NDILEmrRISLRQISYLVLDEADRMLDM 319
Cdd:PRK11057 78 -MKDQVDQLLANGVAAACLNSTQTREQQLEVMAGcrtgQIKLLYIAPERLmmDNFLE--HLAHWNPALLAVDEAHCISQW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 320 G--FEP------QIRKIVKEIPTkrqtLMYTATWPKGVRK-IAADLLVNPAQVNIGNVDElvANKSITQhievvapMEKQ 390
Cdd:PRK11057 155 GhdFRPeyaalgQLRQRFPTLPF----MALTATADDTTRQdIVRLLGLNDPLIQISSFDR--PNIRYTL-------VEKF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 391 RRLEQILR--SQEPGSKVIIFCSTKRMCDQLTRNL-TRQFGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLD 467
Cdd:PRK11057 222 KPLDQLMRyvQEQRGKSGIIYCNSRAKVEDTAARLqSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGIN 301
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 18395852 468 VKDIRAVVNYDFPNGVEDYVHRIGRTGRAGATGQAFTFFGDQD 510
Cdd:PRK11057 302 KPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPAD 344
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
166-497 |
8.52e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 71.08 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 166 PPELLREVLSA-GFSAPTPIQAQSWP-IAMQGRDIVAIAKTGSGKTL-GYLipgflhlqRIRNDSRMGPTILVLSPTREL 242
Cdd:COG1204 7 PLEKVIEFLKErGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLiAEL--------AILKALLNGGKALYIVPLRAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 243 ATQIQEEAVKFGRSSRISCTCLYGGAPKGPqlRDLERgADIVVATPGRLnDILeMRRIS--LRQISYLVLDEAdRMLDmg 320
Cdd:COG1204 79 ASEKYREFKRDFEELGIKVGVSTGDYDSDD--EWLGR-YDILVATPEKL-DSL-LRNGPswLRDVDLVVVDEA-HLID-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 321 fEPQiRKIVKEIptkrqtlmytatwpkgvrkIAADLL-VNP-AQV-----NIGNVDElVAN-----------KSITQHIE 382
Cdd:COG1204 151 -DES-RGPTLEV-------------------LLARLRrLNPeAQIvalsaTIGNAEE-IAEwldaelvksdwRPVPLNEG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 383 VVAP-----MEKQRRLEQ-----ILRSQEPGSKVIIFCSTKRMC--------DQLTRNLTRQ------------------ 426
Cdd:COG1204 209 VLYDgvlrfDDGSRRSKDptlalALDLLEEGGQVLVFVSSRRDAeslakklaDELKRRLTPEereeleelaeellevsee 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 427 ------------FGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATD-------VAARGLDVKDIRAVVNYDFPngVEDYV 487
Cdd:COG1204 289 thtnekladcleKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIP--VLEFK 366
|
410
....*....|
gi 18395852 488 HRIGRTGRAG 497
Cdd:COG1204 367 QMAGRAGRPG 376
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
389-506 |
2.68e-12 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 64.96 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 389 KQRRLEQILRSQEPGSKVIIFCSTKrmcDQLTRnLTRQFGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDV 468
Cdd:cd18789 35 KLRALEELLKRHEQGDKIIVFTDNV---EALYR-YAKRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDL 110
|
90 100 110
....*....|....*....|....*....|....*....
gi 18395852 469 KDIRAVVNYDFPNGVE-DYVHRIGRTGRAGATGQAFTFF 506
Cdd:cd18789 111 PEANVAIQISGHGGSRrQEAQRLGRILRPKKGGGKNAFF 149
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
386-499 |
6.02e-12 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 63.38 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 386 PMEKQRRLEQILRSQ---EPGSKVIIFCSTKRMCDQLTR----------NLTRQF--GAAAIHGDK----SQPERDNVLN 446
Cdd:cd18802 5 VIPKLQKLIEILREYfpkTPDFRGIIFVERRATAVVLSRllkehpstlaFIRCGFliGRGNSSQRKrslmTQRKQKETLD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 18395852 447 QFRSGRTPVLVATDVAARGLDVKDIRAVVNYDFPNGVEDYVHRIGRTGRAGAT 499
Cdd:cd18802 85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSK 137
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
405-505 |
2.79e-11 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 59.64 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 405 KVIIFCSTKRMCDQLTRNLTrqfgaaaihgdksqperdnvlnqfrsgrtpVLVATDVAARGLDVKDIRAVVNYDFPNGVE 484
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSAA 54
|
90 100
....*....|....*....|..
gi 18395852 485 DYVHRIGRTGRAGAT-GQAFTF 505
Cdd:cd18785 55 SYIQRVGRAGRGGKDeGEVILF 76
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
380-491 |
3.54e-11 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 60.95 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 380 HIEVVAPmeKQRRLEQILRS-QEPGSKVIIFCSTKRMCDQLTRNLT-RQFGAAAIHGDKSQPERDNVLNQFRSGRTP--V 455
Cdd:cd18793 5 IEEVVSG--KLEALLELLEElREPGEKVLIFSQFTDTLDILEEALReRGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 18395852 456 LVATDVAARGLDVkdIRA--VVNYDFP-N-GVE----DYVHRIG 491
Cdd:cd18793 83 LLSTKAGGVGLNL--TAAnrVILYDPWwNpAVEeqaiDRAHRIG 124
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
168-369 |
3.63e-11 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 62.66 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 168 ELLREVLsaGFSAPTPiqAQSWPIA--MQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRndsrmGPTiLVLSPTRELaTQ 245
Cdd:cd18018 2 KLLRRVF--GHPSFRP--GQEEAIArlLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGP-----GLT-LVVSPLIAL-MK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 246 IQEEAVKfgrsSRISCTCLYGGAPKGPQLRDLER----GADIVVATPGRLN--DILEMRRiSLRQISYLVLDEADRMLDM 319
Cdd:cd18018 71 DQVDALP----RAIKAAALNSSLTREERRRILEKlragEVKILYVSPERLVneSFRELLR-QTPPISLLVVDEAHCISEW 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18395852 320 G--FEP---QIRKIVKEIPTKRQTLMYTATWPKGVRK-IAADLLVNPAQVNIGNVD 369
Cdd:cd18018 146 ShnFRPdylRLCRVLRELLGAPPVLALTATATKRVVEdIASHLGIPESGVVRGPLY 201
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
389-493 |
2.46e-10 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 63.32 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 389 KQRRLEQILRS-QEPGSKVIIFCSTKRMCDQLTRNLTRQ-FGAAAIHGDKSQPERDNVLNQFRSGRTP--VLVATDVAAR 464
Cdd:COG0553 534 KLEALLELLEElLAEGEKVLVFSQFTDTLDLLEERLEERgIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGE 613
|
90 100 110
....*....|....*....|....*....|....*
gi 18395852 465 GLDVKDIRAVVNYDFP-N-GVE----DYVHRIGRT 493
Cdd:COG0553 614 GLNLTAADHVIHYDLWwNpAVEeqaiDRAHRIGQT 648
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
168-363 |
3.36e-10 |
|
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: 59.86 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 168 ELLREVlsAGFSAPTPIQAQSwpI--AMQGRDIVAIAKTGSGKTLGYLIPGFLhlqrirndsRMGPTIlVLSPTRELatq 245
Cdd:cd17920 2 QILKEV--FGYDEFRPGQLEA--InaVLAGRDVLVVMPTGGGKSLCYQLPALL---------LDGVTL-VVSPLISL--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 246 iQEEAVKFGRSSRISCTCLYGGAPKGPQLRDLER----GADIVVATPGRLNDILEMRRI----SLRQISYLVLDEADRML 317
Cdd:cd17920 65 -MQDQVDRLQQLGIRAAALNSTLSPEEKREVLLRikngQYKLLYVTPERLLSPDFLELLqrlpERKRLALIVVDEAHCVS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18395852 318 DMG--FEP---QIRKIVKEIPtKRQTLMYTATWPKGVRK-IAADL-LVNPAQV 363
Cdd:cd17920 144 QWGhdFRPdylRLGRLRRALP-GVPILALTATATPEVREdILKRLgLRNPVIF 195
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
182-313 |
4.99e-10 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 58.81 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 182 TPIQAQSWPIAMQGRDIVAI-AKTGSGKTlgyLIPGFLHLQRIRndsRMGPTILVLSPTRELATQIQEEAVKFGRSSRIS 260
Cdd:cd17921 3 NPIQREALRALYLSGDSVLVsAPTSSGKT---LIAELAILRALA---TSGGKAVYIAPTRALVNQKEADLRERFGPLGKN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 18395852 261 CTCLYGGAPKGPQlrdLERGADIVVATPGRLNDILemRRIS---LRQISYLVLDEA 313
Cdd:cd17921 77 VGLLTGDPSVNKL---LLAEADILVATPEKLDLLL--RNGGerlIQDVRLVVVDEA 127
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
185-313 |
6.99e-10 |
|
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: 58.75 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 185 QAQSWPIAMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRndsrmGPTILVLSPTRELAtQIQEEAV-KFGRS--SRISC 261
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP-----GSRALYLYPTKALA-QDQLRSLrELLEQlgLGIRV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 18395852 262 TCLYGGAPKGPQLRDLERGADIVVATPGRLNDIL----EMRRISLRQISYLVLDEA 313
Cdd:cd17923 79 ATYDGDTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
389-498 |
2.16e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 60.66 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 389 KQRRLEQILRSQ---EPGSKVIIFCSTKRMCDQLTRNLTRQ-------FGAAAIHGDK--SQPERDNVLNQFRSGRTPVL 456
Cdd:PRK13766 348 KLEKLREIVKEQlgkNPDSRIIVFTQYRDTAEKIVDLLEKEgikavrfVGQASKDGDKgmSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 18395852 457 VATDVAARGLDVKDIRAVVNYD-FPNGVEdYVHRIGRTGRAGA 498
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEIR-SIQRKGRTGRQEE 469
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
381-495 |
6.10e-09 |
|
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: 55.05 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 381 IEVVAPmeKQRRLEQILRSQ------EPGSKVIIFCSTKRMCDQLTRNLTRQF---------GAAAIHGDK--SQPERDN 443
Cdd:cd18801 4 VEKIHP--KLEKLEEIVKEHfkkkqeGSDTRVIIFSEFRDSAEEIVNFLSKIRpgiratrfiGQASGKSSKgmSQKEQKE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 18395852 444 VLNQFRSGRTPVLVATDVAARGLDVKDIRAVVNYDFPNGVEDYVHRIGRTGR 495
Cdd:cd18801 82 VIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
158-518 |
6.65e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 55.88 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 158 MSFEA--TGFPPeLLREVLSAGFSAPTPIQAQSWPIAMQGRDIVAIAKTGSGKTLGylipGFLH-LQRIRNDSRMGPT-- 232
Cdd:COG1201 1 MSAEDvlSLLHP-AVRAWFAARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLA----AFLPaLDELARRPRPGELpd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 233 ---ILVLSPTRELATQIQeeavkfgRSSRISCTCLYGGAPKGPQL----------------RDLERGADIVVATPgrlnd 293
Cdd:COG1201 76 glrVLYISPLKALANDIE-------RNLRAPLEEIGEAAGLPLPEirvgvrtgdtpaserqRQRRRPPHILITTP----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 294 ilEmrriSLrqisYLVL--DEADRMLdmgfepqiRK----IVKEI----PTKRQTLM------YTATWPKGVRKI----- 352
Cdd:COG1201 144 --E----SL----ALLLtsPDARELL--------RGvrtvIVDEIhalaGSKRGVHLalslerLRALAPRPLQRIglsat 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 353 ------AADLLV---NPAQVNIGNVDelvANKSItqHIEVVAPMEK------------QRRLEQILRSQEPGSKVIIFCS 411
Cdd:COG1201 206 vgpleeVARFLVgyeDPRPVTIVDAG---AGKKP--DLEVLVPVEDlierfpwaghlwPHLYPRVLDLIEAHRTTLVFTN 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 412 TKRMCDQLTRNLTRQFG-----AAAIHG--DKSQpeRDNVLNQFRSGRTPVLVAT---DVaarGLDVKDIRAVVNYDFPN 481
Cdd:COG1201 281 TRSQAERLFQRLNELNPedalpIAAHHGslSREQ--RLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGSPK 355
|
410 420 430
....*....|....*....|....*....|....*...
gi 18395852 482 GVEDYVHRIGRTG-RAGATGQAfTFFgdqdSKHASDLI 518
Cdd:COG1201 356 SVARLLQRIGRAGhRVGEVSKG-RLV----PTHRDELV 388
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
393-497 |
7.84e-08 |
|
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: 51.78 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 393 LEQILRSQEPGSKVIIFCSTKRMCDQLTRNLTrqfGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLD----- 467
Cdd:cd18795 33 VLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpart 109
|
90 100 110
....*....|....*....|....*....|...
gi 18395852 468 --VKDIRAVVNYDFPN-GVEDYVHRIGRTGRAG 497
Cdd:cd18795 110 viIKGTQRYDGKGYRElSPLEYLQMIGRAGRPG 142
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
193-497 |
8.13e-08 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 55.67 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 193 MQGRDIVAIAKTGSGKTLGYLIPGFLhlqrirndsrmGPTI-LVLSPtreLATQIQEEAVKFGRSSrISCTCLYGGAPKG 271
Cdd:PLN03137 473 MSGYDVFVLMPTGGGKSLTYQLPALI-----------CPGItLVISP---LVSLIQDQIMNLLQAN-IPAASLSAGMEWA 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 272 PQLRDL-ERGAD-----IVVATPGRL--NDILeMRRI----SLRQISYLVLDEADRMLDMG--FEPQIRK--IVKEIPTK 335
Cdd:PLN03137 538 EQLEILqELSSEyskykLLYVTPEKVakSDSL-LRHLenlnSRGLLARFVIDEAHCVSQWGhdFRPDYQGlgILKQKFPN 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 336 RQTLMYTATWPKGVRKIAADLLvnpaqvniGNVDELVANKSITQHIEVVAPMEKQRR-LEQI---LRSQEPGSKVIIFCS 411
Cdd:PLN03137 617 IPVLALTATATASVKEDVVQAL--------GLVNCVVFRQSFNRPNLWYSVVPKTKKcLEDIdkfIKENHFDECGIIYCL 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 412 TKRMCDQLTRNLtRQFG--AAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVKDIRAVVNYDFPNGVEDYVHR 489
Cdd:PLN03137 689 SRMDCEKVAERL-QEFGhkAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQE 767
|
....*...
gi 18395852 490 IGRTGRAG 497
Cdd:PLN03137 768 CGRAGRDG 775
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
181-313 |
2.57e-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: 51.50 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 181 PTPIQAQSWPIAMQgRDIVAIAKTGSGKTL--GYLIPGFLHLqrIRNDSRMGPTILVLSPTRELATQiQEEAVKfgrssr 258
Cdd:cd18034 3 PRSYQLELFEAALK-RNTIVVLPTGSGKTLiaVMLIKEMGEL--NRKEKNPKKRAVFLVPTVPLVAQ-QAEAIR------ 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18395852 259 iSCTCLYGGAPKGPQLRDLERGA---------DIVVATPGRLNDILEMRRISLRQISYLVLDEA 313
Cdd:cd18034 73 -SHTDLKVGEYSGEMGVDKWTKErwkeelekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
204-344 |
4.48e-07 |
|
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: 49.61 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 204 TGSGKTLgylipgfLHLQRIRNdsRMGPTILVLSPTRELATQIQEEAVKFGRSSRIsctCLYGGAPKgpqlrDLERGADI 283
Cdd:cd17926 27 TGSGKTL-------TALALIAY--LKELRTLIVVPTDALLDQWKERFEDFLGDSSI---GLIGGGKK-----KDFDDANV 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395852 284 VVATPGRLNDILEMRRISLRQISYLVLDEADRmldmGFEPQIRKIVKEIPTKRQtLMYTAT 344
Cdd:cd17926 90 VVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFSEILKELNAKYR-LGLTAT 145
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
378-495 |
2.30e-06 |
|
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: 47.64 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 378 TQHIEVVAPMEKQ-------RRLEQILRSQEPGSKVIIFCSTKRMCDQLTRNLTRQFGAAAI-------HGDKSQPERDN 443
Cdd:cd18796 6 IKVILPVAPEIFPwagesgaDAYAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRVPpdfialhHGSLSRELREE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 18395852 444 VLNQFRSGRTPVLVATDVAARGLDVKDIRAVVNYDFPNGVEDYVHRIGRTGR 495
Cdd:cd18796 86 VEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
403-497 |
2.73e-06 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 47.25 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 403 GSKVIIFCSTKRMCDQLTRNLTRQFGAAAIHGDKSQP--------ERDNVLNQFRSGRTPVLVATDVAARGLDVKDIRAV 474
Cdd:cd18797 35 GVKTIVFCRSRKLAELLLRYLKARLVEEGPLASKVASyragylaeDRREIEAELFNGELLGVVATNALELGIDIGGLDAV 114
|
90 100
....*....|....*....|...
gi 18395852 475 VNYDFPNGVEDYVHRIGRTGRAG 497
Cdd:cd18797 115 VLAGYPGSLASLWQQAGRAGRRG 137
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
202-512 |
2.86e-06 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 50.26 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 202 AKTGSGKT--LGYLIPGFLhlqrirndsRMGPTILVLSP----TRELATQIQEEavkFgrsSRISCTCLYGGAPkgpqlr 275
Cdd:COG4098 136 AVCGAGKTemLFPAIAEAL---------KQGGRVCIATPrvdvVLELAPRLQQA---F---PGVDIAALYGGSE------ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 276 DLERGADIVVATPGRLndilemrrisLRqisY------LVLDEADrmldmGF----EPQIRKIVKEIPTKRQTLMY-TAT 344
Cdd:COG4098 195 EKYRYAQLVIATTHQL----------LR---FyqafdlLIIDEVD-----AFpysgDPMLQYAVKRARKPDGKLIYlTAT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 345 WPK-----------GVRKIAA----DLLVNPAQVNIGNVDELVANKSItqhIEVVapmekqrrLEQILRSQEPGSKVIIF 409
Cdd:COG4098 257 PSKalqrqvkrgklKVVKLPAryhgHPLPVPKFKWLGNWKKRLRRGKL---PRKL--------LKWLKKRLKEGRQLLIF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 410 CSTKRMCDQLTRNLTRQFGAAAIHGDKSQ-PERDNVLNQFRSGRTPVLVATDVAARGLDVKDIR-AVVNYDfpngvedyv 487
Cdd:COG4098 326 VPTIELLEQLVALLQKLFPEERIAGVHAEdPERKEKVQAFRDGEIPILVTTTILERGVTFPNVDvAVLGAD--------- 396
|
330 340 350
....*....|....*....|....*....|....*..
gi 18395852 488 HRI----------GRTGRAGA--TGQaFTFFGDQDSK 512
Cdd:COG4098 397 HPVfteaalvqiaGRVGRSADypTGE-VIFFHHGKTR 432
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
192-315 |
5.47e-06 |
|
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: 47.43 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 192 AMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRndSRMGPTILVLSPTRELATQiQEEAVK--FGRSSrISCTCLYGGAP 269
Cdd:cd17927 14 ALKGKNTIICLPTGSGKTFVAVLICEHHLKKFP--AGRKGKVVFLANKVPLVEQ-QKEVFRkhFERPG-YKVTGLSGDTS 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 18395852 270 KGPQLRDLERGADIVVATPGRL-NDILEMRRISLRQISYLVLDEADR 315
Cdd:cd17927 90 ENVSVEQIVESSDVIIVTPQILvNDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
415-523 |
6.63e-06 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 46.57 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 415 MCDQLTRNLTRQFGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDVkdiravvnydfPNG----VED----- 485
Cdd:cd18811 50 MYEYLKERFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDV-----------PNAtvmvIEDaerfg 118
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 18395852 486 --YVHRI-GRTGRAGATGQAFTFFGDQDSKHASDLIKILEG 523
Cdd:cd18811 119 lsQLHQLrGRVGRGDHQSYCLLVYKDPLTETAKQRLRVMTE 159
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
19-49 |
1.37e-05 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 42.11 E-value: 1.37e-05
10 20 30
....*....|....*....|....*....|.
gi 18395852 19 LPKPWKGLIDDrTGYLYFWNPETNVTQYEKP 49
Cdd:pfam00397 1 LPPGWEERWDP-DGRVYYYNHETGETQWEKP 30
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
201-315 |
2.24e-05 |
|
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: 45.58 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 201 IAKTGSGKTLGYLIPGFLHLQRirndsrMGPTILVLSPTRELATQiQEEAVKFGRSSRISCTCLYGgaPKGPQLR-DLER 279
Cdd:cd18035 22 VLPTGLGKTIIAILVAADRLTK------KGGKVLILAPSRPLVEQ-HAENLKRVLNIPDKITSLTG--EVKPEERaERWD 92
|
90 100 110
....*....|....*....|....*....|....*..
gi 18395852 280 GADIVVATPGRL-NDILEmRRISLRQISYLVLDEADR 315
Cdd:cd18035 93 ASKIIVATPQVIeNDLLA-GRITLDDVSLLIFDEAHH 128
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
405-475 |
2.27e-05 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 44.09 E-value: 2.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18395852 405 KVIIFCSTKRMCDQLTRNLTRQFG-AAAIHGDKSQPER-DNVLNQFRSGRT--PVLVATDVAARGLDVKDIRAVV 475
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIdAVALNSDYSDRERgDEALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV 82
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
197-468 |
3.68e-05 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 46.27 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 197 DIVAIAKTGSGKT-LGYLIPGFLHLQRIRNDSrmgptILVLsPTRELATQIQEEAVK-FG---------RSSRISctcLY 265
Cdd:cd09639 1 LLVIEAPTGYGKTeAALLWALHSLKSQKADRV-----IIAL-PTRATINAMYRRAKEaFGetglyhssiLSSRIK---EM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 266 GGAPKGPQLRDL-ERGADIVVATPGRLNDI----------LEMRRISLRQISY--LVLDEADRMLD--MGFEPQIRKIVK 330
Cdd:cd09639 72 GDSEEFEHLFPLyIHSNDTLFLDPITVCTIdqvlksvfgeFGHYEFTLASIANslLIFDEVHFYDEytLALILAVLEVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 331 EIPTKrqTLMYTATWPKgvrkiaadLLVNPAQvNIGNVDE-----LVANKSITQHIEVVAPMEKQRRLEQILRSQEPGSK 405
Cdd:cd09639 152 DNDVP--ILLMSATLPK--------FLKEYAE-KIGYVEEnepldLKPNERAPFIKIESDKVGEISSLERLLEFIKKGGS 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 406 VIIFCST---KRMCDQLTRNLTRQFGAAAIHGDKSQPERDN----VLNQFRSGRTPVLVATDVAARGLDV 468
Cdd:cd09639 221 VAIIVNTvdrAQEFYQQLKEKGPEEEIMLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLDI 290
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
18-51 |
4.82e-05 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 40.66 E-value: 4.82e-05
10 20 30
....*....|....*....|....*....|....
gi 18395852 18 TLPKPWKGLIDdRTGYLYFWNPETNVTQYEKPTP 51
Cdd:smart00456 1 PLPPGWEERKD-PDGRPYYYNHETKETQWEKPRE 33
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
195-312 |
1.17e-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: 42.96 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 195 GRDIVAIAKTGSGKTLGYLIPGflhLQRIRNDSRMGPTILVLSPTRELATQIQeeavkfgRSSRISCTCLY--------- 265
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPA---LSSLADEPEKGVQVLYISPLKALINDQE-------RRLEEPLDEIDleipvavrh 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 18395852 266 GGAPKGPQLRDLERGADIVVATPGRLNDILEMRRIS--LRQISYLVLDE 312
Cdd:cd17922 71 GDTSQSEKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
20-51 |
1.95e-04 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 38.66 E-value: 1.95e-04
10 20 30
....*....|....*....|....*....|..
gi 18395852 20 PKPWKGLIDdRTGYLYFWNPETNVTQYEKPTP 51
Cdd:cd00201 1 PPGWEERWD-PDGRVYYYNHNTKETQWEDPRE 31
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
204-344 |
9.96e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 40.35 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 204 TGSGKTLGY--LIPGFLHLQRIRNdsrmgptILVLSPTRELATQIQEEAVKFGRSSRISCTCLYGgapkgpQLRDLERG- 280
Cdd:pfam04851 32 TGSGKTLTAakLIARLFKKGPIKK-------VLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISG------DKKDESVDd 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18395852 281 ADIVVATPGRLNDILEMRRISLR--QISYLVLDEADRmldmGFEPQIRKIVKEIPTKRQtLMYTAT 344
Cdd:pfam04851 99 NKIVVTTIQSLYKALELASLELLpdFFDVIIIDEAHR----SGASSYRNILEYFKPAFL-LGLTAT 159
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
384-495 |
1.15e-03 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 40.31 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 384 VAPMEKQRR--LEQILRSQEPGSKVIIFCSTKRMCDQLTRNLTRQ-FGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATD 460
Cdd:cd18790 6 VRPTEGQVDdlLGEIRKRVARGERVLVTTLTKRMAEDLTEYLQELgVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGIN 85
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 18395852 461 VAARGLDVKDIRAVVNYD-----FPNGVEDYVHRIGRTGR 495
Cdd:cd18790 86 LLREGLDLPEVSLVAILDadkegFLRSETSLIQTIGRAAR 125
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
192-312 |
1.53e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 40.15 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 192 AMQGRDIVAIAKTGSGKTLGYLIPGFLHLQRIRNDSRMGpTILVLSPTRELatqIQEEAVKFGRSSR--ISCTCLYGGAP 269
Cdd:cd18036 14 ALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKG-RVVVLVNKVPL---VEQQLEKFFKYFRkgYKVTGLSGDSS 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 18395852 270 KGPQLRDLERGADIVVATP----GRLNDILEMRRISLRQISYLVLDE 312
Cdd:cd18036 90 HKVSFGQIVKASDVIICTPqiliNNLLSGREEERVYLSDFSLLIFDE 136
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
194-497 |
1.77e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 41.41 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 194 QGRDIVAIAKTGSGKTL-GYlipgflhlQRIRNDSRMGPTILVLSPTRELATQIQEEAVKFgRSSRISCTCLYGGAPKGP 272
Cdd:PRK01172 36 KGENVIVSVPTAAGKTLiAY--------SAIYETFLAGLKSIYIVPLRSLAMEKYEELSRL-RSLGMRVKISIGDYDDPP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 273 qlrDLERGADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIrkivkeiptkrQTLMYTAtwpkgvRKI 352
Cdd:PRK01172 107 ---DFIKRYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTL-----------ETVLSSA------RYV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 353 AADLLVNPAQVNIGNVDELVA--NKSITQHIEVVAPME------KQRRLEQILRSQ-----------EPGSKVIIFCSTK 413
Cdd:PRK01172 167 NPDARILALSATVSNANELAQwlNASLIKSNFRPVPLKlgilyrKRLILDGYERSQvdinsliketvNDGGQVLVFVSSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 414 RMCDQLTRNLTRQF--------------------------GAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLD 467
Cdd:PRK01172 247 KNAEDYAEMLIQHFpefndfkvssennnvyddslnemlphGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVN 326
|
330 340 350
....*....|....*....|....*....|....*....
gi 18395852 468 VKdIRAVVNYDFPNGVEDYV---------HRIGRTGRAG 497
Cdd:PRK01172 327 LP-ARLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPG 364
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
205-313 |
2.01e-03 |
|
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 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: 350770 [Multi-domain] Cd Length: 218 Bit Score: 39.86 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 205 GSGKTLGYLIpgflHLQRIRNDSRMGPTiLVLSPTrELATQIQEEAVKFgrSSRISCTCLYGGAPKGPQLRDLErGADIV 284
Cdd:cd18012 33 GLGKTLQTLA----LLLSRKEEGRKGPS-LVVAPT-SLIYNWEEEAAKF--APELKVLVIHGTKRKREKLRALE-DYDLV 103
|
90 100 110
....*....|....*....|....*....|
gi 18395852 285 VATPGRL-NDIlemRRISLRQISYLVLDEA 313
Cdd:cd18012 104 ITSYGLLrRDI---ELLKEVKFHYLVLDEA 130
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
195-371 |
2.41e-03 |
|
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: 39.24 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 195 GRDIVAIAKTGSGKTLGYLIPGFLHLQRirndsrmGPTILVLSPTRELATQiqeeavKFGRSSRISCTCLYGGAPKGPQL 274
Cdd:cd18028 17 GENLLISIPTASGKTLIAEMAMVNTLLE-------GGKALYLVPLRALASE------KYEEFKKLEEIGLKVGISTGDYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 275 RDLER--GADIVVATPGRLNDILEMRRISLRQISYLVLDEADRMLDMGFEPQIRKIV---KEIPTKRQTLMYTATwpkgv 349
Cdd:cd18028 84 EDDEWlgDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVarlRRLNPNTQIIGLSAT----- 158
|
170 180
....*....|....*....|..
gi 18395852 350 rkiaadllvnpaqvnIGNVDEL 371
Cdd:cd18028 159 ---------------IGNPDEL 165
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
181-253 |
4.56e-03 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 38.55 E-value: 4.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18395852 181 PTPIQAQS-WPIAM-----QGRDIVAIAKTGSGKTLGYLIPGFLHLQRirndsrmGPTILVLSPTRELATQIQEEAVKF 253
Cdd:cd17918 16 LTKDQAQAiKDIEKdlhspEPMDRLLSGDVGSGKTLVALGAALLAYKN-------GKQVAILVPTEILAHQHYEEARKF 87
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
414-468 |
4.61e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 38.02 E-value: 4.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 18395852 414 RMCDQLtRNLTRQFGAAAIHGDKSQPERDNVLNQFRSGRTPVLVATDVAARGLDV 468
Cdd:cd18792 49 ALAEEL-KELVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDV 102
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
194-253 |
5.67e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 39.52 E-value: 5.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 194 QGRDIVAIAKTGSGKTLGYLIPGFLHLQriRNDSRmgptILVLSPTRELATQIQEEAVKF 253
Cdd:COG1199 32 EGRHLLIEAGTGTGKTLAYLVPALLAAR--ETGKK----VVISTATKALQEQLVEKDLPL 85
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
392-503 |
9.36e-03 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 37.99 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395852 392 RLEQILRSQEPGSKVIifcstkRMCDQLTRNltrqfgaaaihgdksQPERDNVLNQFRSGRTPVLVATDVAARGLDVKDI 471
Cdd:cd18804 105 RVEEELKTLFPEARIA------RIDRDTTRK---------------KGALEKLLDQFERGEIDILIGTQMIAKGLDFPNV 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 18395852 472 R--AVVNYDFPNGVEDY---------VHRI-GRTGRAGATGQAF 503
Cdd:cd18804 164 TlvGILNADSGLNSPDFraserafqlLTQVsGRAGRGDKPGKVI 207
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
201-255 |
9.63e-03 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 38.81 E-value: 9.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 18395852 201 IAKTGSGKTLGYLIPGFLHLQRirndsrmGPTILVLSPTRELATQIQEEAVKFGR 255
Cdd:COG3505 5 IGPTGSGKTVGLVIPNLTQLAR-------GESVVVTDPKGDLAELTAGFRRRAGY 52
|
|
| |
