|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
136-656 |
0e+00 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 577.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 136 YAQRYQKPNNGAGVAGGYQSNNYNAAALGmlskeeraeiqrekaknpgRNLVKPKW--ENLEPFLKDFYNIHPNTLAKSE 213
Cdd:PTZ00110 45 YGGFRPGYGNYSGGYGGFGMNSYGSSTLG-------------------KRLQPIDWksINLVPFEKNFYKEHPEVSALSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 214 QQVAEIRRELEIT-VSGNELPHPVVSFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYM 292
Cdd:PTZ00110 106 KEVDEIRKEKEITiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 293 LPAIVHIGNQPPIIRGEGPIALVLAPTRELAQQIQSVVRDYGHLCKpeIRHTCIFGGSSKVPQARDLDRGVEVIIATPGR 372
Cdd:PTZ00110 186 LPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSK--IRNTVAYGGVPKRGQIYALRRGVEILIACPGR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 373 LIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDY-IQINIGSMN 451
Cdd:PTZ00110 264 LIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEpVHVNVGSLD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 452 LSANHNIRQIVEICTEIEKPQRLVCLLNEIspiknsGNNGNKIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERD 531
Cdd:PTZ00110 344 LTACHNIKQEVFVVEEHEKRGKLKMLLQRI------MRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 532 SVLKDFRNGKSNILIATDVASRGLDVEDLQYVINYDYPNSSENYVHRIGRTGRCQQLGTAYTFFTPDNAKQARELISVLE 611
Cdd:PTZ00110 418 WVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLR 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 18857967 612 EAGQTPSQALLDLARSMpsSGGYRGNkRWnnnSGGDRNTGGNNGI 656
Cdd:PTZ00110 498 EAKQPVPPELEKLSNER--SNGTERR-RW---GGYGRFSNNVNNI 536
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
238-606 |
7.78e-152 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 454.61 E-value: 7.78e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 238 SFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPiirgEGPIALVLA 317
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 318 PTRELAQQIQSVVRDYGHLCKpeIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADR 397
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLG--LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 398 MLDMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQINIGSMNLSANhNIRQIVEICTEIEKPQRLVCL 477
Cdd:COG0513 157 MLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRYYLVDKRDKLELLRRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 478 LNEISPiknsgnngNKIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDV 557
Cdd:COG0513 236 LRDEDP--------ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDI 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 18857967 558 EDLQYVINYDYPNSSENYVHRIGRTGRCQQLGTAYTFFTPDNAKQAREL 606
Cdd:COG0513 308 DDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAI 356
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
248-446 |
5.65e-131 |
|
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: 392.12 E-value: 5.65e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 248 VIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRGEGPIALVLAPTRELAQQIQ 327
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 328 SVVRDYGHLCKpeIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQI 407
Cdd:cd17966 81 QEANKFGGSSR--LRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 18857967 408 RKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQIN 446
Cdd:cd17966 159 RKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
214-449 |
5.15e-127 |
|
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: 383.21 E-value: 5.15e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 214 QQVAEIRRELEITVSGNELPHPVVSFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYML 293
Cdd:cd18049 1 QEVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 294 PAIVHIGNQPPIIRGEGPIALVLAPTRELAQQIQSVVRDYGHLCKpeIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRL 373
Cdd:cd18049 81 PAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACR--LKSTCIYGGAPKGPQIRDLERGVEICIATPGRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18857967 374 IDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQINIGS 449
Cdd:cd18049 159 IDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
178-448 |
1.97e-126 |
|
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: 383.21 E-value: 1.97e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 178 KAKNPGRNLVKPKWE--NLEPFLKDFYNIHPNTLAKSEQQVAEIRRELEITVSGNELPHPVVSFEESSLPAHVIEEMKRQ 255
Cdd:cd18050 1 KFGNPGERLRKKKWDlsELPKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 256 GFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRGEGPIALVLAPTRELAQQIQSVVRDYGH 335
Cdd:cd18050 81 NFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 336 LCKpeIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKIIEQIR 415
Cdd:cd18050 161 SSR--LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR 238
|
250 260 270
....*....|....*....|....*....|...
gi 18857967 416 PDRQVVMWSATWPKEVQALAGDFLNDYIQINIG 448
Cdd:cd18050 239 PDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
248-445 |
1.81e-97 |
|
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: 304.36 E-value: 1.81e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 248 VIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIgNQPPIIRGEGPIALVLAPTRELAQQIQ 327
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKL-LPEPKKKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 328 SVVRDYGHLCKpeIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQI 407
Cdd:cd00268 80 EVARKLGKGTG--LKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDV 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 18857967 408 RKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd00268 158 EKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
238-619 |
2.98e-92 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 300.18 E-value: 2.98e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 238 SFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRgegpiALVLA 317
Cdd:PRK11776 5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQ-----ALVLC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 318 PTRELAQQIQSVVRDYGHLcKPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADR 397
Cdd:PRK11776 80 PTRELADQVAKEIRRLARF-IPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 398 MLDMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQINIGSmnLSANHNIRQIVEICTEIEKPQRLVCL 477
Cdd:PRK11776 159 MLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES--THDLPAIEQRFYEVSPDERLPALQRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 478 LNEISPiknsgnngNKIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDV 557
Cdd:PRK11776 237 LLHHQP--------ESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDI 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18857967 558 EDLQYVINYDYPNSSENYVHRIGRTGRCQQLGTAYTFFTPDNAKQARElisvLEEAGQTPSQ 619
Cdd:PRK11776 309 KALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANA----IEDYLGRKLN 366
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
226-445 |
4.83e-89 |
|
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: 283.11 E-value: 4.83e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 226 TVSGNELPHPVVSFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPI 305
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 306 IRGEGPIALVLAPTRELAQQIQSVVRDYGHLCKpeIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFL---ENRNT 382
Cdd:cd17953 81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALG--LRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18857967 383 NLQRCTYLVLDEADRMLDMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd17953 159 NLRRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
237-694 |
3.67e-88 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 289.40 E-value: 3.67e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 237 VSFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRGEGPI-ALV 315
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 316 LAPTRELAQQIQSVVRDYGHLCKpeIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEA 395
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLN--IRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 396 DRMLDMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQINIGSMNlSANHNIRQIVEICTEIEKPQRLV 475
Cdd:PRK10590 159 DRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRN-TASEQVTQHVHFVDKKRKRELLS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 476 CLLNEispiknsgNNGNKIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGL 555
Cdd:PRK10590 238 QMIGK--------GNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 556 DVEDLQYVINYDYPNSSENYVHRIGRTGRCQQLGTAYTFFTPDNAKQARELISVLEE-------AGQTP-----SQALLD 623
Cdd:PRK10590 310 DIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKeipriaiPGYEPdpsikAEPIQN 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18857967 624 LARSMPSSGGYRGNKRWNNNSGGDRNTGGNNGiYQQRNNNPLNYQAGnnyNNNRSGPPTGSSYQQYAAGGN 694
Cdd:PRK10590 390 GRQQRGGGGRGQGGGRGQQQGQPRRGEGGAKS-ASAKPAEKPSRRLG---DAKPAGEQQRRRRPRKPAAAQ 456
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
248-445 |
7.48e-88 |
|
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: 278.91 E-value: 7.48e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 248 VIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRGEGPIALVLAPTRELAQQIQ 327
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 328 SVVRDYGHLCKpeIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQI 407
Cdd:cd17952 81 LEAKKFGKAYN--LRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQV 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 18857967 408 RKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd17952 159 RSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
238-448 |
2.16e-83 |
|
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: 267.82 E-value: 2.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 238 SFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRGEG-----PI 312
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 313 ALVLAPTRELAQQIQSVVRDYGHlcKPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVL 392
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSY--RSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 393 DEADRMLDMGFEPQIRKIIEQ----IRPDRQVVMWSATWPKEVQALAGDFLNDYIQINIG 448
Cdd:cd17967 159 DEADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
239-591 |
5.03e-79 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 263.73 E-value: 5.03e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 239 FEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPiiRGEGPI-ALVLA 317
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPR--RKSGPPrILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 318 PTRELAQQiqsVVRDYGHLCKpeirHT-----CIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVL 392
Cdd:PRK11192 81 PTRELAMQ---VADQARELAK----HThldiaTITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 393 DEADRMLDMGFEPQIRKIIEQIRPDRQVVMWSATWPKE-VQALAGDFLNDYIQINIGSmNLSANHNIRQIVEICTEIEKP 471
Cdd:PRK11192 154 DEADRMLDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEP-SRRERKKIHQWYYRADDLEHK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 472 QRLVC-LLNEISPiknsgnngNKIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDV 550
Cdd:PRK11192 233 TALLChLLKQPEV--------TRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDV 304
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 18857967 551 ASRGLDVEDLQYVINYDYPNSSENYVHRIGRTGRCQQLGTA 591
Cdd:PRK11192 305 AARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTA 345
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
248-445 |
5.89e-78 |
|
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: 252.39 E-value: 5.89e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 248 VIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQP-PIIRGEGPIALVLAPTRELAQQI 326
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPiPREQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 327 QSVVRDYGHlckPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQ 406
Cdd:cd17958 81 EAECSKYSY---KGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQ 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 18857967 407 IRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd17958 158 IRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
207-639 |
1.04e-75 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 257.41 E-value: 1.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 207 NTLAKSEQQVAEIRRELEITVSGNELPHPVVSFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSG 286
Cdd:PLN00206 91 STSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 287 KTLAYMLPAI-----VHIGNQPpiiRGEGPIALVLAPTRELAQQI--QSVVRDYGHLCKPEIrhtcIFGGSSKVPQARDL 359
Cdd:PLN00206 171 KTASFLVPIIsrcctIRSGHPS---EQRNPLAMVLTPTRELCVQVedQAKVLGKGLPFKTAL----VVGGDAMPQQLYRI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 360 DRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKIIeQIRPDRQVVMWSATWPKEVQALAGDFL 439
Cdd:PLN00206 244 QQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPEVEKFASSLA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 440 NDYIQINIGSMNlSANHNIRQIVEICTEIEKPQRLVCLLNEISPIKNSGnngnkiIVFVETKIKVEDILQIIR-AEGYNA 518
Cdd:PLN00206 323 KDIILISIGNPN-RPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKPPA------VVFVSSRLGADLLANAITvVTGLKA 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 519 TSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDVEDLQYVINYDYPNSSENYVHRIGRTGRCQQLGTAYTFFTPD 598
Cdd:PLN00206 396 LSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE 475
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 18857967 599 NAKQARELISVLEEAGQTPSQallDLARSMPSSGGYRGNKR 639
Cdd:PLN00206 476 DRNLFPELVALLKSSGAAIPR---ELANSRYLGSGRKRKKK 513
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
236-606 |
2.81e-74 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 249.74 E-value: 2.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 236 VVSFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIgnQPPIIRGEgpiALV 315
Cdd:PTZ00424 27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI--DYDLNACQ---ALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 316 LAPTRELAQQIQSVVRDYGHLCKpeIR-HTCIfGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDE 394
Cdd:PTZ00424 102 LAPTRELAQQIQKVVLALGDYLK--VRcHACV-GGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 395 ADRMLDMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQINIGSMNLSAnHNIRQIVEICTEIEKPQRL 474
Cdd:PTZ00424 179 ADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTL-EGIRQFYVAVEKEEWKFDT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 475 VCLLNEISPIKNSgnngnkiIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRG 554
Cdd:PTZ00424 258 LCDLYETLTITQA-------IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARG 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 18857967 555 LDVEDLQYVINYDYPNSSENYVHRIGRTGRCQQLGTAYTFFTPDNAKQAREL 606
Cdd:PTZ00424 331 IDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
235-594 |
1.03e-73 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 253.72 E-value: 1.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 235 PVVSFEESSLPAH--VIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPII--RGEG 310
Cdd:PRK04537 5 PLTDLTFSSFDLHpaLLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALAdrKPED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 311 PIALVLAPTRELAQQIQSVVRDYGhlCKPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFL-ENRNTNLQRCTY 389
Cdd:PRK04537 85 PRALILAPTRELAIQIHKDAVKFG--ADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVkQHKVVSLHACEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 390 LVLDEADRMLDMGFEPQIRKIIEQI--RPDRQVVMWSATWPKEVQALAGDFLNDYIQINIGSMNLSANHnIRQIVEICTE 467
Cdd:PRK04537 163 CVLDEADRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR-VRQRIYFPAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 468 IEKPQRLVCLLneispiknSGNNGNKIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIA 547
Cdd:PRK04537 242 EEKQTLLLGLL--------SRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVA 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 18857967 548 TDVASRGLDVEDLQYVINYDYPNSSENYVHRIGRTGRCQQLGTAYTF 594
Cdd:PRK04537 314 TDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
247-602 |
1.85e-72 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 247.13 E-value: 1.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 247 HVIEEMkrqGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPI---IRGEgPIALVLAPTRELA 323
Cdd:PRK01297 100 HAIHDL---GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPkerYMGE-PRALIIAPTRELV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 324 QQIQSvvrDYGHLCKPEIRHTCIF-GGSSKVPQARDLD-RGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDM 401
Cdd:PRK01297 176 VQIAK---DAAALTKYTGLNVMTFvGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDM 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 402 GFEPQIRKIIEQIRP--DRQVVMWSATWPKEVQALAGDFLNDYIQINIGSMNLsANHNIRQIVEICTEIEKPQRLVCLLN 479
Cdd:PRK01297 253 GFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENV-ASDTVEQHVYAVAGSDKYKLLYNLVT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 480 EispiknsgNNGNKIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDVED 559
Cdd:PRK01297 332 Q--------NPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 18857967 560 LQYVINYDYPNSSENYVHRIGRTGRCQQLGTAYTFFTPDNAKQ 602
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQ 446
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
248-440 |
5.21e-72 |
|
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: 236.83 E-value: 5.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 248 VIEEMkrqGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPI---IRGEGPIALVLAPTRELAQ 324
Cdd:cd17945 4 VIRKL---GYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLdeeTKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 325 QIQSVVRDYGHlcKPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFE 404
Cdd:cd17945 81 QIEEETQKFAK--PLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18857967 405 PQIRKIIEQI-----RPD---------------RQVVMWSATWPKEVQALAGDFLN 440
Cdd:cd17945 159 PQVTKILDAMpvsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLR 214
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
222-448 |
1.81e-71 |
|
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: 237.17 E-value: 1.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 222 ELEITVSGNELPHPVVSFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGN 301
Cdd:cd18052 28 EIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 302 Q----PPIIRGEGPIALVLAPTRELAQQIQSVVRDYGHlckpeirHTCI-----FGGSSKVPQARDLDRGVEVIIATPGR 372
Cdd:cd18052 108 EgltaSSFSEVQEPQALIVAPTRELANQIFLEARKFSY-------GTCIrpvvvYGGVSVGHQIRQIEKGCHILVATPGR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 373 LIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKIIEQI----RPDRQVVMWSATWPKEVQALAGDFLN-DYIQINI 447
Cdd:cd18052 181 LLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKeDYLFLTV 260
|
.
gi 18857967 448 G 448
Cdd:cd18052 261 G 261
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
227-448 |
1.31e-70 |
|
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: 234.16 E-value: 1.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 227 VSGNELPHPVVSFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLP---AIVHIGNQP 303
Cdd:cd18051 11 ATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPilsQIYEQGPGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 304 PIIRGEG--------PIALVLAPTRELAQQIQSVVRDYGHlcKPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLID 375
Cdd:cd18051 91 SLPSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAY--RSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18857967 376 FLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKIIEQI----RPDRQVVMWSATWPKEVQALAGDFLNDYIQINIG 448
Cdd:cd18051 169 MLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
242-594 |
3.70e-69 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 236.41 E-value: 3.70e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 242 SSLPAH--VIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYmLPAIVHIGNQPPIIRGE---GPIALVL 316
Cdd:PRK04837 11 SDFALHpqVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF-LTATFHYLLSHPAPEDRkvnQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 317 APTRELAQQIQsvvrdygHLCKPEIRHT-----CIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLV 391
Cdd:PRK04837 90 APTRELAVQIH-------ADAEPLAQATglklgLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 392 LDEADRMLDMGFEPQIRKIIEQIRP--DRQVVMWSATWPKEVQALAGDFLND--YIQInigSMNLSANHNIRQIVEICTE 467
Cdd:PRK04837 163 LDEADRMFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNpeYVEV---EPEQKTGHRIKEELFYPSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 468 IEKPQRLVCLLNEISPiknsgnngNKIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIA 547
Cdd:PRK04837 240 EEKMRLLQTLIEEEWP--------DRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVA 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 18857967 548 TDVASRGLDVEDLQYVINYDYPNSSENYVHRIGRTGRCQQLGTAYTF 594
Cdd:PRK04837 312 TDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
237-594 |
7.34e-69 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 241.68 E-value: 7.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 237 VSFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPaIVHigNQPPIIRGegPIALVL 316
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP-LLH--NLDPELKA--PQILVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 317 APTRELAQQIQSVVRDYG-HLckPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEA 395
Cdd:PRK11634 81 APTRELAVQVAEAMTDFSkHM--RGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 396 DRMLDMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQINIGSmNLSANHNIRQIVEICTEIEKPQRLV 475
Cdd:PRK11634 159 DEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS-SVTTRPDISQSYWTVWGMRKNEALV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 476 CLLneispiknSGNNGNKIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGL 555
Cdd:PRK11634 238 RFL--------EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGL 309
|
330 340 350
....*....|....*....|....*....|....*....
gi 18857967 556 DVEDLQYVINYDYPNSSENYVHRIGRTGRCQQLGTAYTF 594
Cdd:PRK11634 310 DVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
248-446 |
6.33e-64 |
|
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: 214.13 E-value: 6.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 248 VIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQP---PIIRGEGPIALVLAPTRELAQ 324
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEkklPFIKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 325 QIQSVVRDYGHLCK----PEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLD 400
Cdd:cd17951 81 QTHEVIEYYCKALQeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18857967 401 MGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQIN 446
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
261-434 |
2.17e-61 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 205.55 E-value: 2.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 261 TAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPiirgeGPIALVLAPTRELAQQIQSVVRDYGHLCKpe 340
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN-----GPQALVLAPTRELAEQIYEELKKLGKGLG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 341 IRHTCIFGGSSKVPQARDLdRGVEVIIATPGRLIDFLENRNTnLQRCTYLVLDEADRMLDMGFEPQIRKIIEQIRPDRQV 420
Cdd:pfam00270 74 LKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQI 151
|
170
....*....|....
gi 18857967 421 VMWSATWPKEVQAL 434
Cdd:pfam00270 152 LLLSATLPRNLEDL 165
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
252-445 |
1.51e-58 |
|
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: 199.73 E-value: 1.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 252 MKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPII-RGEGPIALVLAPTRELAQQIQSVV 330
Cdd:cd17949 6 KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVdRSDGTLALVLVPTRELALQIYEVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 331 RDYGHLCkPEIRHTCIFGGSSKVPQ-ARdLDRGVEVIIATPGRLIDFLEN-RNTNLQRCTYLVLDEADRMLDMGFEPQIR 408
Cdd:cd17949 86 EKLLKPF-HWIVPGYLIGGEKRKSEkAR-LRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDIT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18857967 409 KIIEQIR-------------PDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd17949 164 KILELLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
238-445 |
1.73e-56 |
|
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: 193.69 E-value: 1.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 238 SFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIrgegpIALVLA 317
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRF-----FALVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 318 PTRELAQQIQSVVRDYGHLckPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNT-NLQRCTYLVLDEAD 396
Cdd:cd17954 76 PTRELAQQISEQFEALGSS--IGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGfSLKSLKFLVMDEAD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18857967 397 RMLDMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd17954 154 RLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
458-595 |
1.09e-55 |
|
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: 188.49 E-value: 1.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 458 IRQIVEICTEIEKPQRLVCLLNEIspiknsgNNGNKIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDF 537
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEK-------LKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKF 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 18857967 538 RNGKSNILIATDVASRGLDVEDLQYVINYDYPNSSENYVHRIGRTGRCQQLGTAYTFF 595
Cdd:cd18787 74 RSGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
253-461 |
4.61e-55 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 189.63 E-value: 4.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 253 KRQGFTKPTAIQSQGWPIALSG-RDLVGIAQTGSGKTLAYMLPAIVHIgnqppiIRGEGPIALVLAPTRELAQQIQSVVR 331
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL------KRGKGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 332 DYGHlcKPEIRHTCIFGGSSKVPQARDLDRGV-EVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKI 410
Cdd:smart00487 76 KLGP--SLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18857967 411 IEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQINIGSmnlSANHNIRQI 461
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF---TPLEPIEQF 201
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
238-446 |
2.49e-53 |
|
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: 184.82 E-value: 2.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 238 SFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIrgeGPIALVLA 317
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTV---GARALILS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 318 PTRELAQQIQSVVRDYGhlCKPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADR 397
Cdd:cd17959 79 PTRELALQTLKVTKELG--KFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18857967 398 MLDMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQIN 446
Cdd:cd17959 157 LFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
239-441 |
4.57e-53 |
|
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: 183.96 E-value: 4.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 239 FEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPaIVHIGNQPPIirgeGPIALVLAP 318
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP-ILQRLSEDPY----GIFALVLTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 319 TRELAQQIQSVVRDYGhlcKP-EIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNT---NLQRCTYLVLDE 394
Cdd:cd17955 76 TRELAYQIAEQFRALG---APlGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttkVLSRVKFLVLDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18857967 395 ADRMLDMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLND 441
Cdd:cd17955 153 ADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNK 199
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
255-445 |
2.66e-52 |
|
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: 181.30 E-value: 2.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 255 QGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRGEGpiALVLAPTRELAQQIQSVVRDYG 334
Cdd:cd17947 8 LGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATR--VLVLVPTRELAMQCFSVLQQLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 335 HLCkpEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLEN-RNTNLQRCTYLVLDEADRMLDMGFEPQIRKIIEQ 413
Cdd:cd17947 86 QFT--DITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFADELKEILRL 163
|
170 180 190
....*....|....*....|....*....|..
gi 18857967 414 IRPDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd17947 164 CPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
253-435 |
8.45e-51 |
|
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: 177.78 E-value: 8.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 253 KRQGFTKPTAIQSQGWPIALS-GRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRGEGPIALVLAPTRELAQQIQSVVR 331
Cdd:cd17964 10 TRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTRELALQIAAEAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 332 DYGHlCKPEIRHTCIFGGSSKVPQARDLDR-GVEVIIATPGRLIDFLEN--RNTNLQRCTYLVLDEADRMLDMGFEPQIR 408
Cdd:cd17964 90 KLLQ-GLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENpgVAKAFTDLDYLVLDEADRLLDMGFRPDLE 168
|
170 180 190
....*....|....*....|....*....|.
gi 18857967 409 KIIEQIRP----DRQVVMWSATWPKEVQALA 435
Cdd:cd17964 169 QILRHLPEknadPRQTLLFSATVPDEVQQIA 199
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
248-448 |
1.15e-50 |
|
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: 177.01 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 248 VIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPpiiRGEGPIALVLAPTRELAQQIQ 327
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPR---KKKGLRALILAPTRELASQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 328 SVVRdygHLCKPEIRHTCIFGGSS--KVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEP 405
Cdd:cd17957 78 RELL---KLSKGTGLRIVLLSKSLeaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFRE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18857967 406 QIRKIIEQIR-PDRQVVMWSATWPKEVQALAGDFLNDYIQINIG 448
Cdd:cd17957 155 QTDEILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
249-435 |
3.10e-49 |
|
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: 172.93 E-value: 3.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 249 IEEMkrqGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAI---VHIGNQPPiiRGEGpiALVLAPTRELAQQ 325
Cdd:cd17942 5 IEEM---GFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIellYKLKFKPR--NGTG--VIIISPTRELALQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 326 IQSVVRDyghLCK-PEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRN----TNLQrctYLVLDEADRMLD 400
Cdd:cd17942 78 IYGVAKE---LLKyHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQ---CLIIDEADRILE 151
|
170 180 190
....*....|....*....|....*....|....*
gi 18857967 401 MGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALA 435
Cdd:cd17942 152 IGFEEEMRQIIKLLPKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
248-426 |
5.85e-47 |
|
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: 167.80 E-value: 5.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 248 VIEEMKRQGFTKPTAIQSQGWPIALS-GRDLVGIAQTGSGKTLAYMLPAIVHIGNQ----PPIIRGEGPIALVLAPTREL 322
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQkssnGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 323 AQQIQSvvrdygHL---CK-PEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNT---NLQRCTYLVLDEA 395
Cdd:cd17946 81 AVQVKD------HLkaiAKyTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEA 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 18857967 396 DRMLDMG-FEpQIRKIIEQI-------RPDRQVVMWSAT 426
Cdd:cd17946 155 DRMLEKGhFA-ELEKILELLnkdragkKRKRQTFVFSAT 192
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
248-435 |
6.11e-47 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 166.60 E-value: 6.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 248 VIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRGEGPIALVLAPTRELAQQIQ 327
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 328 SVVRDYGHLCKPEIRHTCIFGGSSKVPQARDLDR-GVEVIIATPGRLIDFLENRNT--NLQRCTYLVLDEADRMLDMGFE 404
Cdd:cd17960 81 EVLQSFLEHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADkvKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190
....*....|....*....|....*....|.
gi 18857967 405 PQIRKIIEQIRPDRQVVMWSATWPKEVQALA 435
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELI 191
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
252-445 |
8.46e-46 |
|
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: 163.10 E-value: 8.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 252 MKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIgnqppIIRGEGPIALVLAPTRELAQQIQSVVR 331
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRC-----LTEHRNPSALILTPTRELAVQIEDQAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 332 DYGHlCKPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKII 411
Cdd:cd17962 80 ELMK-GLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
|
170 180 190
....*....|....*....|....*....|....
gi 18857967 412 EQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd17962 159 ENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
256-446 |
1.09e-44 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 160.16 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 256 GFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRgegpiALVLAPTRELAQQIQSVVRDYGH 335
Cdd:cd17940 18 GFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQ-----ALILVPTRELALQTSQVCKELGK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 336 LCKpeIRHTCIFGGSSkvpqARD----LDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKII 411
Cdd:cd17940 93 HMG--VKVMVTTGGTS----LRDdimrLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKIL 166
|
170 180 190
....*....|....*....|....*....|....*
gi 18857967 412 EQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQIN 446
Cdd:cd17940 167 NFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
253-441 |
1.30e-44 |
|
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: 160.06 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 253 KRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRGE-GPIALVLAPTRELAQQIQSVVR 331
Cdd:cd17961 10 AKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqGTRALILVPTRELAQQVSKVLE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 332 DYGHLCKPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNT-NLQRCTYLVLDEADRMLDMGFEPQIRKI 410
Cdd:cd17961 90 QLTAYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGYEEDLKSL 169
|
170 180 190
....*....|....*....|....*....|.
gi 18857967 411 IEQIRPDRQVVMWSATWPKEVQALAGDFLND 441
Cdd:cd17961 170 LSYLPKNYQTFLMSATLSEDVEALKKLVLHN 200
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
256-445 |
2.30e-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: 159.03 E-value: 2.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 256 GFTKPTAIQSQG-WPIaLSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRgegpiALVLAPTRELAQQIQSVVRDYG 334
Cdd:cd17939 16 GFEKPSAIQQRAiVPI-IKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQ-----ALVLAPTRELAQQIQKVVKALG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 335 HLCKPEIrHTCIfGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKIIEQI 414
Cdd:cd17939 90 DYMGVKV-HACI-GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFL 167
|
170 180 190
....*....|....*....|....*....|.
gi 18857967 415 RPDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd17939 168 PPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
252-447 |
4.89e-43 |
|
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: 155.14 E-value: 4.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 252 MKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIgNQPPIIRGEGPIALVLAPTRELAQQIQSVVR 331
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL-YRERWTPEDGLGALIISPTRELAMQIFEVLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 332 DYGhlcKPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFL-ENRN---TNLQrctYLVLDEADRMLDMGFEPQI 407
Cdd:cd17941 84 KVG---KYHSFSAGLIIGGKDVKEEKERINRMNILVCTPGRLLQHMdETPGfdtSNLQ---MLVLDEADRILDMGFKETL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18857967 408 RKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQINI 447
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
256-445 |
7.30e-41 |
|
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: 149.13 E-value: 7.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 256 GFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPiirgeGPIALVLAPTRELAQQIQSVVRDYGH 335
Cdd:cd18046 18 GFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLK-----ATQALVLAPTRELAQQIQKVVMALGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 336 LCKPEIrHTCIfGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKIIEQIR 415
Cdd:cd18046 93 YMGIKC-HACI-GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLP 170
|
170 180 190
....*....|....*....|....*....|
gi 18857967 416 PDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd18046 171 PDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
248-445 |
8.36e-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: 140.09 E-value: 8.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 248 VIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIvhignQPPIIRGEGPIALVLAPTRELAQQIQ 327
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL-----ESLDLERRHPQVLILAPTREIAVQIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 328 SVVRDYGHLCkPEIrHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQI 407
Cdd:cd17943 76 DVFKKIGKKL-EGL-KCEVFIGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDV 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 18857967 408 RKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd17943 154 NWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
239-445 |
1.72e-37 |
|
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: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 239 FEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIgnqPPIIRGegPIALVLAP 318
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL---DIQVRE--TQALILSP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 319 TRELAQQIQSVVRDYGHLCKPEIrHTCIfGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRM 398
Cdd:cd18045 76 TRELAVQIQKVLLALGDYMNVQC-HACI-GGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18857967 399 LDMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd18045 154 LNKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
469-584 |
4.74e-37 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 134.65 E-value: 4.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 469 EKPQRLVCLLNEispiknsgNNGNKIIVFVETKIKVEDILqIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIAT 548
Cdd:pfam00271 1 EKLEALLELLKK--------ERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVAT 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 18857967 549 DVASRGLDVEDLQYVINYDYPNSSENYVHRIGRTGR 584
Cdd:pfam00271 72 DVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
239-426 |
1.31e-36 |
|
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: 137.07 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 239 FEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIvhignqpPIIRgegpiALVLAP 318
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-------QIVV-----ALILEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 319 TRELAQQIQSVVRDYG-HLCKPEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADR 397
Cdd:cd17938 69 SRELAEQTYNCIENFKkYLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADR 148
|
170 180 190
....*....|....*....|....*....|....*
gi 18857967 398 MLDMGFEPQIRKIIEQI-----RPDR-QVVMWSAT 426
Cdd:cd17938 149 LLSQGNLETINRIYNRIpkitsDGKRlQVIVCSAT 183
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
244-445 |
3.81e-36 |
|
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: 135.40 E-value: 3.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 244 LPAHVIEEMKRQGFTKPTAIQSQGWPIALSG--RDLVGIAQTGSGKTLAY---ML----PAIVHignqppiirgegPIAL 314
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFvlaMLsrvdPTLKS------------PQAL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 315 VLAPTRELAQQIQSVVRDYGHlcKPEIRHTCIFGGSSkvpqaRDLDRGVE--VIIATPGRLIDFLENRNTNLQRCTYLVL 392
Cdd:cd17963 69 CLAPTRELARQIGEVVEKMGK--FTGVKVALAVPGND-----VPRGKKITaqIVIGTPGTVLDWLKKRQLDLKKIKILVL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 18857967 393 DEADRMLDM-GFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd17963 142 DEADVMLDTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
249-446 |
1.16e-34 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 131.51 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 249 IEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHI-GNQPPIIRGEGPIALVLAPTRELAQQIQ 327
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLqEDQQPRKRGRAPKVLVLAPTRELANQVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 328 SVVRDYGHlckpEIRHTCIFGGSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQI 407
Cdd:cd17944 82 KDFKDITR----KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18857967 408 RKII-EQIRPDR----QVVMWSATWPKEVQALAGDFL-NDYIQIN 446
Cdd:cd17944 158 EEILsVSYKKDSednpQTLLFSATCPDWVYNVAKKYMkSQYEQVD 202
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
248-443 |
3.49e-33 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 128.25 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 248 VIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRGE--GPIALVLAPTRELAQQ 325
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfnAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 326 IQSVVRDyghLCKP-EIRHTCIFGGSSKvPQARDLDRG-VEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGF 403
Cdd:cd17948 81 IGSVAQS---LTEGlGLKVKVITGGRTK-RQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18857967 404 EPQIRKIIEQIR-------------PDRQVVMWSATWPKEVqalaGDFLNDYI 443
Cdd:cd17948 157 NEKLSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGV----GEVLSKVI 205
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
505-584 |
1.54e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 109.22 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 505 EDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDVEDLQYVINYDYPNSSENYVHRIGRTGR 584
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
256-445 |
7.30e-28 |
|
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: 112.05 E-value: 7.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 256 GFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIIRgegpiALVLAPTRELAQQIQsvvRDYGH 335
Cdd:cd17950 21 GFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVS-----VLVICHTRELAFQIS---NEYER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 336 LCK--PEIRHTCIFGGsskVPQARDLDR----GVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRML-DMGFEPQIR 408
Cdd:cd17950 93 FSKymPNVKTAVFFGG---VPIKKDIEVlknkCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDMRRDVQ 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 18857967 409 KIIEQIRPDRQVVMWSATWPKEVQALAGDFLNDYIQI 445
Cdd:cd17950 170 EIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
248-404 |
1.38e-25 |
|
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: 106.18 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 248 VIEEMKRQGFTK---------PTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQP-PIIRgegpiALVLA 317
Cdd:cd17956 1 LLKNLQNNGITSafpvqaaviPWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVvPRLR-----ALIVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 318 PTRELAQQIQSVvrdYGHLCKPEIRHTCIFGGSSKVPQ---------ARDLDRGVEVIIATPGRLIDFL-ENRNTNLQRC 387
Cdd:cd17956 76 PTKELVQQVYKV---FESLCKGTGLKVVSLSGQKSFKKeqklllvdtSGRYLSRVDILVATPGRLVDHLnSTPGFTLKHL 152
|
170
....*....|....*..
gi 18857967 388 TYLVLDEADRMLDMGFE 404
Cdd:cd17956 153 RFLVIDEADRLLNQSFQ 169
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
281-454 |
3.75e-25 |
|
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: 105.54 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 281 AQTGSGKTLAYMLPAIVHIGNQP------------PIIRGEGPIALVLAPTRELAQQIQSVVRDYGHLCKPEIRHTCIFG 348
Cdd:cd17965 68 AETGSGKTLAYLAPLLDYLKRQEqepfeeaeeeyeSAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 349 GSSKVPQARDLDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKIIEQIRPDRQVVMWSATWP 428
Cdd:cd17965 148 GPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227
|
170 180
....*....|....*....|....*.
gi 18857967 429 KEVQALAGDFLNDyiQINIGSMNLSA 454
Cdd:cd17965 228 KEFDKTLRKLFPD--VVRIATPRLHA 251
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
283-581 |
5.72e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 95.09 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 283 TGSGKTLAyMLPAIVHIGNQPPIirgegpiaLVLAPTRELAQQIQSVVRDYghlckpeiRHTCIFGGSSKvpqardlDRG 362
Cdd:COG1061 109 TGTGKTVL-ALALAAELLRGKRV--------LVLVPRRELLEQWAEELRRF--------LGDPLAGGGKK-------DSD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 363 VEVIIATPGRLIDFLENRNTNlQRCTYLVLDEADRmldmGFEPQIRKIIEQIRPDRQVVMwSAT-------WPKEV---- 431
Cdd:COG1061 165 APITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFPAAYRLGL-TATpfrsdgrEILLFlfdg 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 432 --------QALAGDFLNDYIQINIGSMNLSANHNIRQIVEICTE--IEKPQRLVCLLNEIspIKNSGNNGnKIIVFVETK 501
Cdd:COG1061 239 ivyeyslkEAIEDGYLAPPEYYGIRVDLTDERAEYDALSERLREalAADAERKDKILREL--LREHPDDR-KTLVFCSSV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 502 IKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDVEDLQYVInYDYPNSSEN-YVHRIG 580
Cdd:COG1061 316 DHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPTGSPReFIQRLG 394
|
.
gi 18857967 581 R 581
Cdd:COG1061 395 R 395
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
271-627 |
2.46e-19 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 92.51 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 271 ALSGRDLVGIAQTGSGKTLAYMLPAIVhignqppiirGEGPiALVLAPTRELAQ-QIQSVvRDYGhlckpeIRHTCIfgG 349
Cdd:COG0514 29 VLAGRDALVVMPTGGGKSLCYQLPALL----------LPGL-TLVVSPLIALMKdQVDAL-RAAG------IRAAFL--N 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 350 SSKVPQAR-----DLDRG-VEVIIATPGRL-----IDFLENRNTNLqrctyLVLDEA--------DrmldmgFEP---QI 407
Cdd:COG0514 89 SSLSAEERrevlrALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 408 RKIIEQIrPDRQVVMWSATWPKEVQA-----LAgdfLNDyIQINIGSMNlsaNHNIRQIVEICTEIEKPQRLVCLLNEIS 482
Cdd:COG0514 158 GELRERL-PNVPVLALTATATPRVRAdiaeqLG---LED-PRVFVGSFD---RPNLRLEVVPKPPDDKLAQLLDFLKEHP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 483 PikNSGnngnkiIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATdVA-SRGLDVEDLQ 561
Cdd:COG0514 230 G--GSG------IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVR 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18857967 562 YVINYDYPNSSENYVHRIGRTGRCQQLGTAYTFFTPDNAKQARELIsvleeAGQTPSQALLDLARS 627
Cdd:COG0514 301 FVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFI-----EQSPPDEERKRVERA 361
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
446-584 |
2.98e-19 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 93.26 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 446 NIGSMNLSANHNIRQIVEICTEIE----KPQRLVCLLNEISpiknSGNNGNKIIVFVETKIKVEDILQIIRAEGYNAT-- 519
Cdd:COG1111 308 SKASKRLVSDPRFRKAMRLAEEADiehpKLSKLREILKEQL----GTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrf 383
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18857967 520 ----SIHGDK--TQNERDSVLKDFRNGKSNILIATDVASRGLDVEDLQYVINYDyPNSSE-NYVHRIGRTGR 584
Cdd:COG1111 384 vgqaSKEGDKglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PVPSEiRSIQRKGRTGR 454
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
236-441 |
3.38e-19 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 87.77 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 236 VVSFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSG--RDLVGIAQTGSGKTLAYMLPAIVHIGNQPPIirgegPIA 313
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY-----PQC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 314 LVLAPTRELAQQIQSVVRDYGHLCKPEIRHTCIFGgsSKVPQARDLDRgvEVIIATPGRLIDF-LENRNTNLQRCTYLVL 392
Cdd:cd18048 92 LCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRG--NRPGKGTDIEA--QIVIGTPGTVLDWcFKLRLIDVTNISVFVL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18857967 393 DEADRMLDM-GFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLND 441
Cdd:cd18048 168 DEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPD 217
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
241-593 |
1.42e-17 |
|
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: 87.97 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 241 ESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHignqppIIRGEGPIALVLAPTR 320
Cdd:COG1205 38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEA------LLEDPGATALYLYPTK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 321 ELAQ-QIQSvVRDYGHLCKPEIRHTCIFGGSSkvPQARD--LDRGvEVIIATP-----------GRLIDFLENrntnlqr 386
Cdd:COG1205 112 ALARdQLRR-LRELAEALGLGVRVATYDGDTP--PEERRwiREHP-DIVLTNPdmlhygllphhTRWARFFRN------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 387 CTYLVLDEA---------------DRMldmgfepqiRKIIEQIRPDRQVVMWSATW--PKE-VQALAGdflndyiqinig 448
Cdd:COG1205 181 LRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRHYGSDPQFILASATIgnPAEhAERLTG------------ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 449 smnlsanhniRQIVEIcTEIEKPQ--RLVCLLNeiSPIKNSG-----------------NNGNKIIVFVETKIKVEDILQ 509
Cdd:COG1205 240 ----------RPVTVV-DEDGSPRgeRTFVLWN--PPLVDDGirrsalaeaarlladlvREGLRTLVFTRSRRGAELLAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 510 IIR---AEGYNATSI---HGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDVEDLQYVINYDYPNSSENYVHRIGRTG 583
Cdd:COG1205 307 YARralREPDLADRVaayRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAG 386
|
410
....*....|
gi 18857967 584 RCQQLGTAYT 593
Cdd:COG1205 387 RRGQDSLVVL 396
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
281-426 |
1.45e-15 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 74.75 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 281 AQTGSGKTLAYMLPAIVHIGNQppiirgeGPIALVLAPTRELAQQIQSVVRDYGhlcKPEIRHTCIFGGSSKVPQARDLD 360
Cdd:cd00046 8 APTGSGKTLAALLAALLLLLKK-------GKKVLVLVPTKALALQTAERLRELF---GPGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18857967 361 RGVEVIIATPGRLidfLENRNTNLQRC----TYLVLDEADRMLDMGFEPQIRKIIEQ--IRPDRQVVMWSAT 426
Cdd:cd00046 78 GDADIIIATPDML---LNLLLREDRLFlkdlKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
238-441 |
1.05e-14 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 73.99 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 238 SFEESSLPAHVIEEMKRQGFTKPTAIQSQGWPIALSG--RDLVGIAQTGSGKTLAYMLPAIVHIgnQPPIIRGEgpiALV 315
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYPQ---CLC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 316 LAPTRELAQQIQSVVRDYGHLcKPEIRHTCIFGGSSkvpqardLDRGV----EVIIATPGRLIDF-LENRNTNLQRCTYL 390
Cdd:cd18047 77 LSPTYELALQTGKVIEQMGKF-YPELKLAYAVRGNK-------LERGQkiseQIVIGTPGTVLDWcSKLKFIDPKKIKVF 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18857967 391 VLDEADRML-DMGFEPQIRKIIEQIRPDRQVVMWSATWPKEVQALAGDFLND 441
Cdd:cd18047 149 VLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 200
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
468-581 |
4.54e-13 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 67.23 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 468 IEKPQRLVCLLNEISPiknsGNNGNKIIVFVETKIKVEDILQIIRAEG-----YNATSIHG----------DKTQNERDS 532
Cdd:cd18802 6 IPKLQKLIEILREYFP----KTPDFRGIIFVERRATAVVLSRLLKEHPstlafIRCGFLIGrgnssqrkrsLMTQRKQKE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 18857967 533 VLKDFRNGKSNILIATDVASRGLDVEDLQYVINYDYPNSSENYVHRIGR 581
Cdd:cd18802 82 TLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
459-584 |
8.82e-13 |
|
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: 66.61 E-value: 8.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 459 RQIVEICTEIEKPQRLVCllnEISPIKNSGNNgNKIIVFVETKIKVEDILQI-------IRAEGY----NATSIHGdKTQ 527
Cdd:cd18801 2 RKVEKIHPKLEKLEEIVK---EHFKKKQEGSD-TRVIIFSEFRDSAEEIVNFlskirpgIRATRFigqaSGKSSKG-MSQ 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 18857967 528 NERDSVLKDFRNGKSNILIATDVASRGLDVEDLQYVINYDyPNSSE-NYVHRIGRTGR 584
Cdd:cd18801 77 KEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYD-ASPSPiRMIQRMGRTGR 133
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
489-595 |
1.02e-12 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 66.08 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 489 NNGNKIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDVEDLQYVINYDY 568
Cdd:cd18794 28 HLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSL 107
|
90 100
....*....|....*....|....*..
gi 18857967 569 PNSSENYVHRIGRTGRCQQLGTAYTFF 595
Cdd:cd18794 108 PKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
449-584 |
1.86e-12 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 71.44 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 449 SMNLSANHNIRQIVEICTEIE----KPQRLVCLLNEISPIknsgNNGNKIIVFVETKIKVEDILQIIRAEGYNA------ 518
Cdd:PRK13766 323 SKRLVEDPRFRKAVRKAKELDiehpKLEKLREIVKEQLGK----NPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgq 398
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18857967 519 TSIHGDK--TQNERDSVLKDFRNGKSNILIATDVASRGLDVEDLQYVINYDyPNSSE-NYVHRIGRTGR 584
Cdd:PRK13766 399 ASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYE-PVPSEiRSIQRKGRTGR 466
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
264-395 |
6.50e-12 |
|
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: 65.30 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 264 QSQGWPIALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPpiirgeGPIALVLAPTRELAQQIQSVVRDYGHLCKPEIRH 343
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQDQLRSLRELLEQLGLGIRV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18857967 344 TCIFGGSSKVPQARDLDRGVEVIIATP-----------GRLIDFLEnrntNLQrctYLVLDEA 395
Cdd:cd17923 79 ATYDGDTPREERRAIIRNPPRILLTNPdmlhyallphhDRWARFLR----NLR---YVVLDEA 134
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
493-584 |
4.47e-10 |
|
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: 56.56 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 493 KIIVFVETKIKVEDILQIIraegynatsihgdktqnerdsvlkdfrngksNILIATDVASRGLDVEDLQYVINYDYPNSS 572
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSL-------------------------------EILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90
....*....|..
gi 18857967 573 ENYVHRIGRTGR 584
Cdd:cd18785 54 ASYIQRVGRAGR 65
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
484-580 |
4.89e-10 |
|
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: 58.26 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 484 IKNSGNNGNKIIVFVETKiKVEDIL-QIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSN--ILIATDVASRGLdveDL 560
Cdd:cd18793 20 LEELREPGEKVLIFSQFT-DTLDILeEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGL---NL 95
|
90 100
....*....|....*....|....*....
gi 18857967 561 Q---YVINYDYP-NSS-----ENYVHRIG 580
Cdd:cd18793 96 TaanRVILYDPWwNPAveeqaIDRAHRIG 124
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
470-598 |
5.45e-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: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 470 KPQRLVCLLNEIspiknsGNNGNKIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSN--ILIA 547
Cdd:COG0553 534 KLEALLELLEEL------LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLIS 607
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 548 TDVASRGLdveDLQ---YVINYDYP-N-SSENY----VHRIGRTGRCQqlgtAYTFFTPD 598
Cdd:COG0553 608 LKAGGEGL---NLTaadHVIHYDLWwNpAVEEQaidrAHRIGQTRDVQ----VYKLVAEG 660
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
271-619 |
2.45e-09 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 60.88 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 271 ALSGRDLVGIAQTGSGKTLAYMLPAIVHIGnqppiirgegpIALVLAPTRELAQQIQSVVRDYGhlckpeIRHTCIFGGS 350
Cdd:PRK11057 37 VLSGRDCLVVMPTGGGKSLCYQIPALVLDG-----------LTLVVSPLISLMKDQVDQLLANG------VAAACLNSTQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 351 SKVPQARDLDR----GVEVIIATPGRLI--DFLEnRNTNLQRCTyLVLDEADRMLDMG--FEPQIRKI--IEQIRPDRQV 420
Cdd:PRK11057 100 TREQQLEVMAGcrtgQIKLLYIAPERLMmdNFLE-HLAHWNPAL-LAVDEAHCISQWGhdFRPEYAALgqLRQRFPTLPF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 421 VMWSATWP----KEVQALAGdfLNDYIqINIGSMNlsaNHNIRQiveicTEIEKPQRLVCLLNEISpiknsGNNGNKIIV 496
Cdd:PRK11057 178 MALTATADdttrQDIVRLLG--LNDPL-IQISSFD---RPNIRY-----TLVEKFKPLDQLMRYVQ-----EQRGKSGII 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 497 FVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDVEDLQYVINYDYPNSSENYV 576
Cdd:PRK11057 242 YCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYY 321
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 18857967 577 HRIGRTGRCQQLGTAYTFFTPDNAKQARELisvLEEAGQTPSQ 619
Cdd:PRK11057 322 QETGRAGRDGLPAEAMLFYDPADMAWLRRC---LEEKPAGQQQ 361
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
263-447 |
5.88e-09 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 56.50 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 263 IQSQGW-PIALSGRDLVGIAQTGSGKTLAYMLpAIVHIgnqppiIRGEGPIALVLAPTRELAQQI-QSVVRDYGHLCKPE 340
Cdd:cd17921 5 IQREALrALYLSGDSVLVSAPTSSGKTLIAEL-AILRA------LATSGGKAVYIAPTRALVNQKeADLRERFGPLGKNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 341 IRHTcifgGSSKVPQARDLDRgvEVIIATPGRLiDFLENR--NTNLQRCTYLVLDEAdRMLDMG-----FEPQIRKIIeQ 413
Cdd:cd17921 78 GLLT----GDPSVNKLLLAEA--DILVATPEKL-DLLLRNggERLIQDVRLVVVDEA-HLIGDGergvvLELLLSRLL-R 148
|
170 180 190
....*....|....*....|....*....|....
gi 18857967 414 IRPDRQVVMWSATWPkEVQALAgDFLNDYIQINI 447
Cdd:cd17921 149 INKNARFVGLSATLP-NAEDLA-EWLGVEDLIRF 180
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
490-595 |
1.04e-07 |
|
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: 52.25 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 490 NGNKIIVFVETKIKVEDIlqiirAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDVED--LQYVINYD 567
Cdd:cd18789 48 QGDKIIVFTDNVEALYRY-----AKRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEanVAIQISGH 122
|
90 100
....*....|....*....|....*...
gi 18857967 568 YpNSSENYVHRIGRTGRCQQLGTAYTFF 595
Cdd:cd18789 123 G-GSRRQEAQRLGRILRPKKGGGKNAFF 149
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
271-433 |
1.40e-07 |
|
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: 52.92 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 271 ALSGRDLVGIAQTGSGKTLAYMLPAIVhignqppiirgEGPIALVLAPTRELAQ-QIQsvvrdygHLCKPEIRHTCIFGG 349
Cdd:cd17920 24 VLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVD-------RLQQLGIRAAALNST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 350 SSKVPQARDLDR----GVEVIIATPGRL-----IDFLENRNtNLQRCTYLVLDEADRMLDMG--FEPQIRKIIEQIR--P 416
Cdd:cd17920 86 LSPEEKREVLLRikngQYKLLYVTPERLlspdfLELLQRLP-ERKRLALIVVDEAHCVSQWGhdFRPDYLRLGRLRRalP 164
|
170
....*....|....*..
gi 18857967 417 DRQVVMWSATWPKEVQA 433
Cdd:cd17920 165 GVPILALTATATPEVRE 181
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
257-327 |
2.78e-07 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 54.72 E-value: 2.78e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18857967 257 FTKPTAIQSQGWPIALSGRD-LVgIAQTGSGKTLAYMLPAIVHIGNQPPIIRGEGPI-ALVLAPTRELAQQIQ 327
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGEStLL-IAPTGSGKTLAAFLPALDELARRPRPGELPDGLrVLYISPLKALANDIE 93
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
244-426 |
3.28e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 54.13 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 244 LPAHVIEEMKRQGFTKPTAIQSQGWP-IALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNqppiirgeGPIALVLAPTREL 322
Cdd:COG1204 7 PLEKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLN--------GGKALYIVPLRAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 323 AQQI-QSVVRDYGHLckpEIRhtciFGGSSkvpqaRDLDRGVE------VIIATPGRLIDFLENRNTNLQRCTYLVLDEA 395
Cdd:COG1204 79 ASEKyREFKRDFEEL---GIK----VGVST-----GDYDSDDEwlgrydILVATPEKLDSLLRNGPSWLRDVDLVVVDEA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18857967 396 ------DRmldmGfePQIRKIIEQIR---PDRQVVMWSAT 426
Cdd:COG1204 147 hliddeSR----G--PTLEVLLARLRrlnPEAQIVALSAT 180
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
283-395 |
1.14e-06 |
|
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: 48.84 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 283 TGSGKTLAyMLPAIVHIGNQPpiirgegpiALVLAPTRELAQQIQSVVRDYGHlckpeIRHTCIFGGSSKvpqarDLDRG 362
Cdd:cd17926 27 TGSGKTLT-ALALIAYLKELR---------TLIVVPTDALLDQWKERFEDFLG-----DSSIGLIGGGKK-----KDFDD 86
|
90 100 110
....*....|....*....|....*....|...
gi 18857967 363 VEVIIATPGRLIDFLENRNTNLQRCTYLVLDEA 395
Cdd:cd17926 87 ANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
266-431 |
1.24e-06 |
|
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: 49.95 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 266 QGWPIA--LSGRDLVGIAQTGSGKTLAYMLPAIvhignqppIIRGEGP-IALVLAPTrelaqqiQSVVRDYGHLCKPEIR 342
Cdd:cd18018 17 QEEAIArlLSGRSTLVVLPTGAGKSLCYQLPAL--------LLRRRGPgLTLVVSPL-------IALMKDQVDALPRAIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 343 HTCIFGGSSKVPQARDLDR----GVEVIIATPGRLI--DFLEnrntNLQRCT---YLVLDEADRMLDMG--FEP---QIR 408
Cdd:cd18018 82 AAALNSSLTREERRRILEKlragEVKILYVSPERLVneSFRE----LLRQTPpisLLVVDEAHCISEWShnFRPdylRLC 157
|
170 180
....*....|....*....|...
gi 18857967 409 KIIEQIRPDRQVVMWSATWPKEV 431
Cdd:cd18018 158 RVLRELLGAPPVLALTATATKRV 180
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
274-394 |
2.54e-06 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 48.35 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 274 GRDLVGIAQTGSGKTLAYMLPAIVHIgnqppIIRGEGPIALV-LAPTRELAQQIQSVVRDYGHLCKPEIRHTCIFGGSSK 352
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSL-----ADEPEKGVQVLyISPLKALINDQERRLEEPLDEIDLEIPVAVRHGDTSQ 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 18857967 353 VPQARDLDRGVEVIIATPGRLIDFLENRNTN--LQRCTYLVLDE 394
Cdd:cd17922 76 SEKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
272-584 |
4.38e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 50.66 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 272 LSGRDLVGIAQTGSGKTLAYMLPAIVHIGnqppiirgegpIALVLAPTRELAQ-QIQsvvrdygHLCKPEIRHTCIFGGS 350
Cdd:PLN03137 473 MSGYDVFVLMPTGGGKSLTYQLPALICPG-----------ITLVISPLVSLIQdQIM-------NLLQANIPAASLSAGM 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 351 SKVPQA---RDLDRG---VEVIIATPGR------LIDFLENRNTN--LQRctyLVLDEADRMLDMG--FEPQIRK--IIE 412
Cdd:PLN03137 535 EWAEQLeilQELSSEyskYKLLYVTPEKvaksdsLLRHLENLNSRglLAR---FVIDEAHCVSQWGhdFRPDYQGlgILK 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 413 QIRPDRQVVMWSATWP---KE--VQALAgdflndyiQINIGSMNLSANH-NIRQIVeicteieKPQRLVCLLNEISPIKN 486
Cdd:PLN03137 612 QKFPNIPVLALTATATasvKEdvVQALG--------LVNCVVFRQSFNRpNLWYSV-------VPKTKKCLEDIDKFIKE 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 487 sgNNGNKI-IVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDVEDLQYVIN 565
Cdd:PLN03137 677 --NHFDECgIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIH 754
|
330
....*....|....*....
gi 18857967 566 YDYPNSSENYVHRIGRTGR 584
Cdd:PLN03137 755 HSLPKSIEGYHQECGRAGR 773
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
490-587 |
8.27e-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: 46.48 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 490 NGNKIIVFVETKIKVEDILQIIRA----EGYNATSIHGDK---TQNERDSVLKDFRNGKSNILIATDVASRGLDVEDLQY 562
Cdd:cd18797 34 AGVKTIVFCRSRKLAELLLRYLKArlveEGPLASKVASYRagyLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDA 113
|
90 100
....*....|....*....|....*
gi 18857967 563 VINYDYPNSSENYVHRIGRTGRCQQ 587
Cdd:cd18797 114 VVLAGYPGSLASLWQQAGRAGRRGK 138
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
271-397 |
2.78e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 46.27 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 271 ALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPiirGEGPIALVLAPTRELAQQIQSVVRDygHLCKPEIRHTCIFGGS 350
Cdd:cd17927 14 ALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPA---GRKGKVVFLANKVPLVEQQKEVFRK--HFERPGYKVTGLSGDT 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 18857967 351 SKVPQARDLDRGVEVIIATPGRLIDFLEN-RNTNLQRCTYLVLDEADR 397
Cdd:cd17927 89 SENVSVEQIVESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
272-426 |
5.59e-05 |
|
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: 44.63 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 272 LSGRDLVGIAQTGSGKTLAYMLPAIVHIgnqppiirGEGPIALVLAPTRELAQQiqsVVRDYGHLCKPEIRHTCIFGgss 351
Cdd:cd18028 15 LKGENLLISIPTASGKTLIAEMAMVNTL--------LEGGKALYLVPLRALASE---KYEEFKKLEEIGLKVGISTG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 352 kvpqarDLDRGVE------VIIATPGRLIDFLENRNTNLQRCTYLVLDEADRMLDMGFEPQIRKIIEQIR---PDRQVVM 422
Cdd:cd18028 81 ------DYDEDDEwlgdydIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnPNTQIIG 154
|
....
gi 18857967 423 WSAT 426
Cdd:cd18028 155 LSAT 158
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
521-612 |
6.64e-05 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 43.87 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 521 IHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDVEDLQYVI--NYDYPNSSENYVHRiGRTGRCQQLGTAYtFFTPD 598
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQLR-GRVGRSKERAYAY-FLYPD 134
|
90
....*....|....*..
gi 18857967 599 NAK---QARELISVLEE 612
Cdd:cd18810 135 QKKlteDALKRLEAIQE 151
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
283-395 |
7.96e-05 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 44.56 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 283 TGSGKTL-AYMLpaIVHIGNQPPIIRGEGPIALVLAPTRELAQQIQSVVRDY-GHLCKPeirhtcIFGGSSKVPQARD-- 358
Cdd:cd18034 25 TGSGKTLiAVML--IKEMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHtDLKVGE------YSGEMGVDKWTKErw 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 18857967 359 --LDRGVEVIIATPGRLIDFLENRNTNLQRCTYLVLDEA 395
Cdd:cd18034 97 keELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
271-394 |
1.14e-04 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 44.39 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 271 ALSGRDLVGIAQTGSGKTLAYMLPAIVHIGNQPPiiRGEGPIALVLAPTRELAQQIQSVVRDYghlCKPEIRHTCIFGGS 350
Cdd:cd18036 14 ALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRS--AGEKGRVVVLVNKVPLVEQQLEKFFKY---FRKGYKVTGLSGDS 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 18857967 351 SKVPQARDLDRGVEVIIATPGRLIDFL----ENRNTNLQRCTYLVLDE 394
Cdd:cd18036 89 SHKVSFGQIVKASDVIICTPQILINNLlsgrEEERVYLSDFSLLIFDE 136
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
493-557 |
1.61e-04 |
|
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: 42.16 E-value: 1.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18857967 493 KIIVFVETKIKVEDILQIIRAEGYNATSIHGDKTQNER-DSVLKDFRNGKS--NILIATDVASRGLDV 557
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELkpPILVTVDLLTTGVDI 75
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
510-584 |
3.49e-04 |
|
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: 41.95 E-value: 3.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18857967 510 IIRAEgYNATSIHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDVEDLQYVINYDYPNSSENYVHRI-GRTGR 584
Cdd:cd18811 57 RFRPE-LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGR 131
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
270-395 |
5.84e-04 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) 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.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 42.35 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 270 IALSGRDLVGIAQTGSGKTLAYMLPAIVHIGnqppiirgegpIALVLAPTRELAQQIQSVVRDYGhlckpeIRHTCIFGG 349
Cdd:cd18015 29 ATMAGRDVFLVMPTGGGKSLCYQLPALCSDG-----------FTLVVSPLISLMEDQLMALKKLG------ISATMLNAS 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 18857967 350 SSK-----VPQA-RDLDRGVEVIIATP------GRLIDFLENRNtNLQRCTYLVLDEA 395
Cdd:cd18015 92 SSKehvkwVHAAlTDKNSELKLLYVTPekiaksKRFMSKLEKAY-NAGRLARIAIDEV 148
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
521-557 |
8.83e-04 |
|
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: 41.10 E-value: 8.83e-04
10 20 30
....*....|....*....|....*....|....*..
gi 18857967 521 IHGDKTQNERDSVLKDFRNGKSNILIATDVASRGLDV 557
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDV 102
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
280-429 |
9.65e-04 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 41.12 E-value: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 280 IAQTGSGKTLAYMLPAIVHignqppIIRGEGPIALVLAPTRELAQQIQSVVRDYGHLCKPEIRHTCIFGGSSKVPQARDL 359
Cdd:cd17930 7 EAPTGSGKTEAALLWALKL------AARGGKRRIIYALPTRATINQMYERIREILGRLDDEDKVLLLHSKAALELLESDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 360 DRGV------------------EVIIATPGRLIDFLENRNTNLQRC-----TYLVLDEAdRMLDMGFEPQIRKIIEQI-- 414
Cdd:cd17930 81 EPDDdpveavdwalllkrswlaPIVVTTIDQLLESLLKYKHFERRLhglanSVVVLDEV-QAYDPEYMALLLKALLELlg 159
|
170
....*....|....*
gi 18857967 415 RPDRQVVMWSATWPK 429
Cdd:cd17930 160 ELGGPVVLMTATLPA 174
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
275-369 |
1.17e-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: 40.86 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 275 RDLVGIAQTGSGKTLAYMLPAIVHIGNqppiirgeGPIALVLAPTRELAQQIQSVVRDYghlcKPEIRHTCIFGGSskvp 354
Cdd:cd17918 37 MDRLLSGDVGSGKTLVALGAALLAYKN--------GKQVAILVPTEILAHQHYEEARKF----LPFINVELVTGGT---- 100
|
90
....*....|....*
gi 18857967 355 QARDLDrGVEVIIAT 369
Cdd:cd17918 101 KAQILS-GISLLVGT 114
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
271-397 |
3.93e-03 |
|
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: 39.42 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 271 ALSGRDLVgIAQTGSGKTLAYMLPAIVhignqppIIRGEGPIALVLAPTRELAQQIQSVVRdygHLCKPEIRHTCIFGGS 350
Cdd:cd18035 14 ALNGNTLI-VLPTGLGKTIIAILVAAD-------RLTKKGGKVLILAPSRPLVEQHAENLK---RVLNIPDKITSLTGEV 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 18857967 351 SKVPQARDLDRGvEVIIATPGRLIDFLENRNTNLQRCTYLVLDEADR 397
Cdd:cd18035 83 KPEERAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
271-440 |
4.90e-03 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) 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 in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 39.42 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 271 ALSGRDLVGIAQTGSGKTLAYMLPAIVHIGnqppiirgegpIALVLAPTREL-AQQIQSvvrdyghLCKPEIRHTCIFGG 349
Cdd:cd18016 29 ALLGEDCFVLMPTGGGKSLCYQLPACVSPG-----------VTVVISPLRSLiVDQVQK-------LTSLDIPATYLTGD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18857967 350 SSKVPQAR---DLDRG---VEVIIATP------GRLIDFLENRNTN--LQRctyLVLDEADRMLDMG--FEPQIRKI--I 411
Cdd:cd18016 91 KTDAEATKiylQLSKKdpiIKLLYVTPekisasNRLISTLENLYERklLAR---FVIDEAHCVSQWGhdFRPDYKRLnmL 167
|
170 180
....*....|....*....|....*....
gi 18857967 412 EQIRPDRQVVMWSATWPKEVQALAGDFLN 440
Cdd:cd18016 168 RQKFPSVPMMALTATATPRVQKDILNQLK 196
|
|
| |
