|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-382 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 592.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 1 MTFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPqvaaNSVRALVL 80
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 81 VPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRM 160
Cdd:COG0513 78 APTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 161 LDLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSIEVSPRNTAAKSVRQWLVPVDKKRKAELFCHLLQ 240
Cdd:COG0513 158 LDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 241 ANRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVVNFD 320
Cdd:COG0513 238 DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYD 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510932685 321 LPIVAEDYVHRIGRTGRAGASGQAVSLVCADEVELLAAIETLIGQTLQRREEPDFEPEHRVP 382
Cdd:COG0513 318 LPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKR 379
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-378 |
1.26e-164 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 471.60 E-value: 1.26e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 1 MTFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAANS-VRALV 79
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRpVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 80 LVPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADR 159
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 160 MLDLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSIEVSPRNTAAKSVRQWLVPVDKKRKAELFCHLL 239
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 240 QANRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVVNF 319
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 510932685 320 DLPIVAEDYVHRIGRTGRAGASGQAVSLVCADEVELLAAIETLIGQTLQRREEPDFEPE 378
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEPD 379
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
1-382 |
4.18e-128 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 377.75 E-value: 4.18e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 1 MTFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLtLEGPQVAANSVRALVL 80
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL-LDFPRRKSGPPRILIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 81 VPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRM 160
Cdd:PRK11192 80 TPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 161 LDLGFARELDELFAALPRKRQTLLFSATF-SDAIRTLARELLRDPLSIEVSPRNTAAKSVRQWLVPVD-KKRKAELFCHL 238
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLeGDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADdLEHKTALLCHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 239 LQANRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVVN 318
Cdd:PRK11192 240 LKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVIN 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510932685 319 FDLPIVAEDYVHRIGRTGRAGASGQAVSLVCADEVELLAAIETLIGQTLQRREEPDFEPEHRVP 382
Cdd:PRK11192 320 FDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRPKTKAP 383
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-386 |
9.78e-123 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 364.89 E-value: 9.78e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 1 MTFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLtlegpQVAANSVRALVL 80
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-----DVKRFRVQALVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 81 VPTRELAEQVHGSVRDYGQHLP-LRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADR 159
Cdd:PRK11776 79 CPTRELADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 160 MLDLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSIEVSPRnTAAKSVRQWLVPVDKKRKAELFCHLL 239
Cdd:PRK11776 159 MLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVEST-HDLPAIEQRFYEVSPDERLPALQRLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 240 QANRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVVNF 319
Cdd:PRK11776 238 LHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINY 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510932685 320 DLPIVAEDYVHRIGRTGRAGASGQAVSLVCADEVELLAAIETLIGQTLQRREEPDFEPEHRVPQTAP 386
Cdd:PRK11776 318 ELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPE 384
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
3-367 |
3.39e-108 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 326.54 E-value: 3.39e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 3 FASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALP----LLQRLTLEGPQVaaNSVRAL 78
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKV--NQPRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 79 VLVPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEAD 158
Cdd:PRK04837 88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 159 RMLDLGFARELDELFAALP--RKRQTLLFSATFSDAIRTLARELLRDPLSIEVSPRNTAAKSVRQWLVPVDKKRKAELFC 236
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 237 HLLQANRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLV 316
Cdd:PRK04837 248 TLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 510932685 317 VNFDLPIVAEDYVHRIGRTGRAGASGQAVSLVCADEVELLAAIETLIGQTL 367
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-376 |
1.46e-100 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 313.32 E-value: 1.46e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 1 MTFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRL--TLEGPQVaansvraL 78
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLdpELKAPQI-------L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 79 VLVPTRELAEQVHGSVRDYGQHLPLRTAVA-YGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEA 157
Cdd:PRK11634 79 VLAPTRELAVQVAEAMTDFSKHMRGVNVVAlYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 158 DRMLDLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSIEVSPRNTAAKSVRQWLVPVDKKRKAELFCH 237
Cdd:PRK11634 159 DEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 238 LLQANRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVV 317
Cdd:PRK11634 239 FLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVV 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 510932685 318 NFDLPIVAEDYVHRIGRTGRAGASGQAVSLVCADEVELLAAIETLIGQTLQRREEPDFE 376
Cdd:PRK11634 319 NYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAE 377
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-208 |
1.93e-100 |
|
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: 298.20 E-value: 1.93e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLtLEGPQVAANSVRALVLVPTRELAEQVH 91
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKL-LPEPKKKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 92 GSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELDE 171
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 510932685 172 LFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSIE 208
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
2-355 |
5.48e-96 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 299.00 E-value: 5.48e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 2 TFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLE-------GPQVaans 74
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQpllrygdGPIV---- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 75 vraLVLVPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVL 154
Cdd:PTZ00110 207 ---LVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 155 DEADRMLDLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRD-PLSIEV-SPRNTAAKSVRQWLVPVDKKRKA 232
Cdd:PTZ00110 284 DEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVgSLDLTACHNIKQEVFVVEEHEKR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 233 ELFCHLLQA--NRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDI 310
Cdd:PTZ00110 364 GKLKMLLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDV 443
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 510932685 311 EEMPLVVNFDLPIVAEDYVHRIGRTGRAGASGQAVSLVCADEVEL 355
Cdd:PTZ00110 444 KDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRL 488
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-374 |
9.54e-96 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 296.44 E-value: 9.54e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 3 FASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVA--ANSVRALVL 80
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKEryMGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 81 VPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLR-KGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADR 159
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 160 MLDLGFARELDELFAALPRK--RQTLLFSATFSDAIRTLARELLRDPLSIEVSPRNTAAKSVRQWLVPVDKKRKAELFCH 237
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 238 LLQANRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVV 317
Cdd:PRK01297 329 LVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVI 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 510932685 318 NFDLPIVAEDYVHRIGRTGRAGASGQAVSLVCADEVELLAAIETLIGQTLQRREEPD 374
Cdd:PRK01297 409 NFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPA 465
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-367 |
1.90e-88 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 280.30 E-value: 1.90e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 1 MTFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLtLEGPQVA---ANSVRA 77
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRL-LSRPALAdrkPEDPRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 78 LVLVPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQN-AVKFAQLQALVLDE 156
Cdd:PRK04537 88 LILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHkVVSLHACEICVLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 157 ADRMLDLGFARELDELFAALPRK--RQTLLFSATFSDAIRTLARELLRDPLSIEVSPRNTAAKSVRQWLVPVDKKRKAEL 234
Cdd:PRK04537 168 ADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 235 FCHLLQANRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMP 314
Cdd:PRK04537 248 LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 510932685 315 LVVNFDLPIVAEDYVHRIGRTGRAGASGQAVSLVCADEVELLAAIETLIGQTL 367
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKI 380
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
2-360 |
5.15e-82 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 258.60 E-value: 5.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 2 TFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEgpqvaANSVRALVLV 81
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD-----LNACQALILA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 82 PTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRML 161
Cdd:PTZ00424 104 PTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 162 DLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSIEVSPRNTAAKSVRQWLVPVDKKR-KAELFCHLLQ 240
Cdd:PTZ00424 184 SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEwKFDTLCDLYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 241 ANRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVVNFD 320
Cdd:PTZ00424 264 TLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYD 343
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 510932685 321 LPIVAEDYVHRIGRTGRAGASGQAVSLVCADEVELLAAIE 360
Cdd:PTZ00424 344 LPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIE 383
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
1-348 |
1.09e-79 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 255.87 E-value: 1.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 1 MTFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAANSVR--AL 78
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEQRNplAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 79 VLVPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEAD 158
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 159 RMLDLGFARELDELFAALPRKrQTLLFSATFSDAIRTLARELLRDPLSIEVSPRNTAAKSVRQWLVPVD-KKRKAELFCH 237
Cdd:PLN00206 281 CMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVEtKQKKQKLFDI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 238 LLQANRWR-QALVFAKTRKSVEELVGLLQR-QGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPL 315
Cdd:PLN00206 360 LKSKQHFKpPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQ 439
|
330 340 350
....*....|....*....|....*....|...
gi 510932685 316 VVNFDLPIVAEDYVHRIGRTGRAGASGQAVSLV 348
Cdd:PLN00206 440 VIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
2-209 |
1.85e-73 |
|
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: 230.07 E-value: 1.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 2 TFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLtLEGPQVAANSVR----- 76
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKL-LEDGPPSVGRGRrkayp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 77 -ALVLVPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLD 155
Cdd:cd17967 80 sALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510932685 156 EADRMLDLGFARELDELFAA--LPRK--RQTLLFSATFSDAIRTLARELLRDPLSIEV 209
Cdd:cd17967 160 EADRMLDMGFEPQIRKIVEHpdMPPKgeRQTLMFSATFPREIQRLAADFLKNYIFLTV 217
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
12-207 |
9.04e-72 |
|
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: 224.83 E-value: 9.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAAnsVRALVLVPTRELAEQVH 91
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAA--TRVLVLVPTRELAMQCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 92 GSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQN-AVKFAQLQALVLDEADRMLDLGFARELD 170
Cdd:cd17947 79 SVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELK 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 510932685 171 ELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17947 159 EILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
2-208 |
1.14e-69 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 219.50 E-value: 1.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 2 TFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLtLEGPQvaanSVRALVLV 81
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL-LENPQ----RFFALVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 82 PTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLD-LYRQNAVKFAQLQALVLDEADRM 160
Cdd:cd17954 76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510932685 161 LDLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSIE 208
Cdd:cd17954 156 LNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-202 |
3.40e-66 |
|
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: 212.91 E-value: 3.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 1 MTFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLT---LEGPQVA-ANSVR 76
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkegLTASSFSeVQEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 77 ALVLVPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDE 156
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510932685 157 ADRMLDLGFARELDEL--FAALPRK--RQTLLFSATFSDAIRTLARELLR 202
Cdd:cd18052 203 ADRMLDMGFGPEIRKLvsEPGMPSKedRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
3-208 |
3.84e-64 |
|
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: 205.54 E-value: 3.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 3 FASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTlEGPQvaanSVRALVLVP 82
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLS-EDPY----GIFALVLTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 83 TRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQN---AVKFAQLQALVLDEADR 159
Cdd:cd17955 76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSddtTKVLSRVKFLVLDEADR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510932685 160 MLDLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSIE 208
Cdd:cd17955 156 LLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
12-207 |
3.07e-61 |
|
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: 198.70 E-value: 3.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAANSV---RALVLVPTRELAE 88
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKDdgpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 89 QVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARE 168
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510932685 169 LDELFAALP--------------------RKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17945 161 VTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
2-207 |
1.04e-60 |
|
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: 197.21 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 2 TFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAANSVRALVLV 81
Cdd:cd17953 13 KWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEGPIGLIMA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 82 PTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQA---LVLDEAD 158
Cdd:cd17953 93 PTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNLRRvtyVVLDEAD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510932685 159 RMLDLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17953 173 RMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
2-204 |
3.55e-60 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 195.22 E-value: 3.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 2 TFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAansVRALVLV 81
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVG---ARALILS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 82 PTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRML 161
Cdd:cd17959 79 PTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 510932685 162 DLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDP 204
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEP 201
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
25-196 |
2.45e-59 |
|
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: 191.69 E-value: 2.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 25 TPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGpqvaaNSVRALVLVPTRELAEQVHGSVRDYGQHLPLR 104
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 105 TAVAYGGVSINPQMMKLrKGVDILVATPGRLLDLYrQNAVKFAQLQALVLDEADRMLDLGFARELDELFAALPRKRQTLL 184
Cdd:pfam00270 76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLL-QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 510932685 185 FSATFSDAIRTL 196
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
3-207 |
2.45e-59 |
|
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: 192.90 E-value: 2.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 3 FASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLtlegpQVAANSVRALVLVP 82
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-----DPKKDVIQALILVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 83 TRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLD 162
Cdd:cd17940 76 TRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510932685 163 LGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17940 156 QDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
12-207 |
5.17e-58 |
|
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: 189.50 E-value: 5.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAANSVRALVLVPTRELAEQVH 91
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 92 GSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELDE 171
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 510932685 172 LFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
219-348 |
7.93e-58 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 186.56 E-value: 7.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 219 VRQWLVPVDKKRKAE-LFCHLLQANRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDL 297
Cdd:cd18787 1 IKQLYVVVEEEEKKLlLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 510932685 298 LVATDVAARGLDIEEMPLVVNFDLPIVAEDYVHRIGRTGRAGASGQAVSLV 348
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
12-207 |
9.81e-58 |
|
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: 188.78 E-value: 9.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAANSVRALVLVPTRELAEQVH 91
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 92 GSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELDE 171
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 510932685 172 LFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
12-207 |
1.11e-57 |
|
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: 188.55 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAANSVRALVLVPTRELAEQVH 91
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 92 GSVRDY--GQHLPLRTAVAYGGVSINPQMMKL-RKGVDILVATPGRLLDLYR--QNAVKFAQLQALVLDEADRMLDLGFA 166
Cdd:cd17960 81 EVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 510932685 167 RELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
9-202 |
4.20e-57 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 187.41 E-value: 4.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 9 LDP-LLKALEGLGHGTPTPIQAQAIPPAL-KGRDLLAAAQTGTGKTAGFALPLLQRLtLEGPQVAANS-VRALVLVPTRE 85
Cdd:cd17964 1 LDPsLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSL-LNTKPAGRRSgVSALIISPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 86 LAEQVHGSVRDYGQHLP-LRTAVAYGGVSINPQMMKLRK-GVDILVATPGRLLDLYRQNAVK--FAQLQALVLDEADRML 161
Cdd:cd17964 80 LALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510932685 162 DLGFARELDELFAALP----RKRQTLLFSATFSDAIRTLARELLR 202
Cdd:cd17964 160 DMGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-209 |
4.65e-57 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 187.03 E-value: 4.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLtleGPQVAANSVRALVLVPTRELAEQVH 91
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKL---GKPRKKKGLRALILAPTRELASQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 92 GSVRDYGQHLPLRTAV-AYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELD 170
Cdd:cd17957 78 RELLKLSKGTGLRIVLlSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 510932685 171 ELFAALPRKR-QTLLFSATFSDAIRTLARELLRDPLSIEV 209
Cdd:cd17957 158 EILAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
13-209 |
1.89e-56 |
|
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: 185.19 E-value: 1.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 13 LKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGpQVAANSVRALVLVPTRELAEQVHG 92
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRER-WTPEDGLGALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 93 SVRDYGQHLPLRTAVAYGGVSINPQMMKLrKGVDILVATPGRLLDLYRQNA-VKFAQLQALVLDEADRMLDLGFARELDE 171
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETPgFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 510932685 172 LFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSIEV 209
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
16-222 |
1.57e-54 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 180.38 E-value: 1.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 16 LEGLGHGTPTPIQAQAIPPALKG-RDLLAAAQTGTGKTAGFALPLLQRLTLEGPQvaansvRALVLVPTRELAEQVHGSV 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG------RVLVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 95 RDYGQHLPLRTAVAYGGVSINPQMMKLRKGV-DILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELDELF 173
Cdd:smart00487 75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510932685 174 AALPRKRQTLLFSATFSDAIRTLARELLRDPlsIEVSPRNTAAKSVRQW 222
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
2-203 |
2.86e-54 |
|
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: 181.39 E-value: 2.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 2 TFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAANSVR----- 76
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESLPSESgyygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 77 ------ALVLVPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQ 150
Cdd:cd18051 102 rkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 510932685 151 ALVLDEADRMLDLGFA---RELDELFAALPR-KRQTLLFSATFSDAIRTLARELLRD 203
Cdd:cd18051 182 YLVLDEADRMLDMGFEpqiRRIVEQDTMPPTgERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
3-204 |
5.09e-54 |
|
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: 179.05 E-value: 5.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 3 FASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQrltlegpqvaanSVRALVLVP 82
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ------------IVVALILEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 83 TRELAEQVHGSVRDYGQHL---PLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADR 159
Cdd:cd17938 69 SRELAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510932685 160 MLDLGFARELDELFAALPR-----KR-QTLLFSATF-SDAIRTLARELLRDP 204
Cdd:cd17938 149 LLSQGNLETINRIYNRIPKitsdgKRlQVIVCSATLhSFEVKKLADKIMHFP 200
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
6-207 |
7.65e-54 |
|
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: 178.67 E-value: 7.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 6 LGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEgpqvaANSVRALVLVPTRE 85
Cdd:cd17939 2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTT-----VRETQALVLAPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 86 LAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGF 165
Cdd:cd17939 77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510932685 166 ARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
13-207 |
6.49e-52 |
|
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: 173.32 E-value: 6.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 13 LKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEG--PQvaaNSVRALVLVPTRELAEQV 90
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKfkPR---NGTGVIIISPTRELALQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 91 HGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDlYRQNAVKF--AQLQALVLDEADRMLDLGFARE 168
Cdd:cd17942 79 YGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLD-HLQNTKGFlyKNLQCLIIDEADRILEIGFEEE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 510932685 169 LDELFAALPRKRQTLLFSATFSDAIRTLAR-ELLRDPLSI 207
Cdd:cd17942 158 MRQIIKLLPKRRQTMLFSATQTRKVEDLARiSLKKKPLYV 197
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
3-209 |
1.61e-51 |
|
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: 172.91 E-value: 1.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 3 FASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAansvrALVLVP 82
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVS-----VLVICH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 83 TRELAEQVHGSVRDYGQHLP-LRTAVAYGGVSINPQMMKLRKGV-DILVATPGRLLDLYRQNAVKFAQLQALVLDEADRM 160
Cdd:cd17950 79 TRELAFQISNEYERFSKYMPnVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510932685 161 L-DLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSIEV 209
Cdd:cd17950 159 LeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
12-207 |
1.97e-51 |
|
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: 172.52 E-value: 1.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLL-----QRLTL-----EGPQvaansvrALVLV 81
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleQEKKLpfikgEGPY-------GLIVC 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 82 PTRELAEQVHGSVRDYGQHL------PLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLD 155
Cdd:cd17951 74 PSRELARQTHEVIEYYCKALqeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510932685 156 EADRMLDLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17951 154 EADRMIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
12-207 |
3.83e-51 |
|
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: 171.19 E-value: 3.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEgpqvaANSVRALVLVPTRELAEQVH 91
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTE-----HRNPSALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 92 GSVRDYGQHLP-LRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELD 170
Cdd:cd17962 76 DQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 510932685 171 ELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17962 156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
12-207 |
1.15e-50 |
|
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: 170.34 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLE-GPQVAANSVRALVLVPTRELAEQV 90
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQpIPREQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 91 HGSVRDYgQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELD 170
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 510932685 171 ELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
12-190 |
3.29e-49 |
|
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: 3.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALK-GRDLLAAAQTGTGKTAGFALPLLQRL----TLEGPQVAANSVRALVLVPTREL 86
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlsqkSSNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 87 AEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQN---AVKFAQLQALVLDEADRMLDL 163
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....
gi 510932685 164 GFARELDELFAALP-------RKRQTLLFSATFS 190
Cdd:cd17946 161 GHFAELEKILELLNkdragkkRKRQTFVFSATLT 194
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
12-207 |
1.17e-48 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 165.45 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEG-LGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAANS-VRALVLVPTRELAEQ 89
Cdd:cd17949 1 LVSHLKSkMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDgTLALVLVPTRELALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 90 VHGSVRDYGQHLP-LRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLD-LYRQNAVKFAQLQALVLDEADRMLDLGFAR 167
Cdd:cd17949 81 IYEVLEKLLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510932685 168 ELDELFAAL-------------PRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17949 161 DITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
9-204 |
9.11e-48 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 162.75 E-value: 9.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 9 LDP-LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLtLEGPQVAANS--VRALVLVPTRE 85
Cdd:cd17961 1 LDPrLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKI-LKAKAESGEEqgTRALILVPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 86 LAEQVHGSVRDYGQHLP--LRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKF-AQLQALVLDEADRMLD 162
Cdd:cd17961 80 LAQQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510932685 163 LGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDP 204
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
12-204 |
2.01e-46 |
|
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: 158.97 E-value: 2.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEgpqvaANSVRALVLVPTRELAEQVH 91
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE-----RRHPQVLILAPTREIAVQIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 92 GSVRDYGQHLP-LRTAVAYGGVSINPQMMKLrKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELD 170
Cdd:cd17943 76 DVFKKIGKKLEgLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154
|
170 180 190
....*....|....*....|....*....|....
gi 510932685 171 ELFAALPRKRQTLLFSATFSDAIRTLARELLRDP 204
Cdd:cd17943 155 WIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKP 188
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
3-207 |
7.08e-46 |
|
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: 157.99 E-value: 7.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 3 FASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEgpqvaANSVRALVLVP 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTS-----LKATQALVLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 83 TRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLD 162
Cdd:cd18046 76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510932685 163 LGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
24-209 |
1.00e-45 |
|
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: 158.63 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 24 PTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAANSVRALVLVPTRELAEQVHGSVRDYGQHLPL 103
Cdd:cd18049 47 PTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 104 RTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELDELFAALPRKRQTL 183
Cdd:cd18049 127 KSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTL 206
|
170 180
....*....|....*....|....*.
gi 510932685 184 LFSATFSDAIRTLARELLRDPLSIEV 209
Cdd:cd18049 207 MWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
24-209 |
1.77e-45 |
|
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: 159.02 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 24 PTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVAANSVRALVLVPTRELAEQVHGSVRDYGQHLPL 103
Cdd:cd18050 85 PTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 104 RTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELDELFAALPRKRQTL 183
Cdd:cd18050 165 KSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTL 244
|
170 180
....*....|....*....|....*.
gi 510932685 184 LFSATFSDAIRTLARELLRDPLSIEV 209
Cdd:cd18050 245 MWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
3-207 |
2.69e-44 |
|
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: 153.78 E-value: 2.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 3 FASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQ--RLTLEGPQVaansvraLVL 80
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQclDIQVRETQA-------LIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 81 VPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRM 160
Cdd:cd18045 74 SPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510932685 161 LDLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd18045 154 LNKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
13-202 |
7.44e-43 |
|
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: 150.00 E-value: 7.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 13 LKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVA-ANSVRALVLVPTRELAEQVH 91
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKrGRAPKVLVLAPTRELANQVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 92 GSVRDYGQHLplRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELDE 171
Cdd:cd17944 82 KDFKDITRKL--SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 510932685 172 LFAALPRKR-----QTLLFSATFSDAIRTLARELLR 202
Cdd:cd17944 160 ILSVSYKKDsednpQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
9-207 |
2.96e-41 |
|
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: 145.41 E-value: 2.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 9 LDP-LLKALEGLGHGTPTPIQAQAIPPALKG--RDLLAAAQTGTGKTAGFALPLLQR--LTLEGPQvaansvrALVLVPT 83
Cdd:cd17963 1 LKPeLLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRvdPTLKSPQ-------ALCLAPT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 84 RELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPqmmklRKGVD--ILVATPGRLLDLYRQNAVKFAQLQALVLDEADRML 161
Cdd:cd17963 74 RELARQIGEVVEKMGKFTGVKVALAVPGNDVPR-----GKKITaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVML 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510932685 162 DL-GFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSI 207
Cdd:cd17963 149 DTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
12-189 |
6.52e-39 |
|
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: 140.19 E-value: 6.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRL--TLEGPQVAANSVRALVLVPTRELAEQ 89
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrYKLLAEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 90 VHGSVRDYGQHLPLRTAVAYGGVSINpQMMKLRKG-VDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARE 168
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190
....*....|....*....|....*....|....
gi 510932685 169 L-------------DELFAALPRKRQTLLFSATF 189
Cdd:cd17948 160 LshflrrfplasrrSENTDGLDPGTQLVLVSATM 193
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
12-190 |
7.78e-34 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 126.59 E-value: 7.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 12 LLKALEGLGHGTPTPIQAQAIPPALKG---------RDLLAAAQTGTGKTAGFALPLLQRLTlegpQVAANSVRALVLVP 82
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALS----KRVVPRLRALIVVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 83 TRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQMMKLRKG--------VDILVATPGRLLD-LYRQNAVKFAQLQALV 153
Cdd:cd17956 77 TKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDhLNSTPGFTLKHLRFLV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 510932685 154 LDEADRMLDLGFARELDELFAAL--------------------PRKRQTLLFSATFS 190
Cdd:cd17956 157 IDEADRLLNQSFQDWLETVMKALgrptapdlgsfgdanllersVRPLQKLLFSATLT 213
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
231-339 |
8.36e-34 |
|
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: 122.70 E-value: 8.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 231 KAELFCHLLQANRWRQALVFAKTRKSVEELVgLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDI 310
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 510932685 311 EEMPLVVNFDLPIVAEDYVHRIGRTGRAG 339
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
258-339 |
1.32e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 99.59 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 258 EELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVVNFDLPIVAEDYVHRIGRTGR 337
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 510932685 338 AG 339
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
2-204 |
5.60e-25 |
|
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: 102.41 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 2 TFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKG--RDLLAAAQTGTGKTAGFALPLLQRltlegpqVAANSV--RA 77
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR-------VDALKLypQC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 78 LVLVPTRELAEQVHGSVRDYGQH-LPLRTAVAYGGVSInPQMMKLRKgvDILVATPGRLLD-LYRQNAVKFAQLQALVLD 155
Cdd:cd18048 92 LCLSPTFELALQTGKVVEEMGKFcVGIQVIYAIRGNRP-GKGTDIEA--QIVIGTPGTVLDwCFKLRLIDVTNISVFVLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510932685 156 EADRMLDL-GFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDP 204
Cdd:cd18048 169 EADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
24-212 |
3.84e-22 |
|
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: 95.14 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 24 PTPIQAQAIPPALKGR----------------DLLAAAQTGTGKTAGFALPLLQRL--------TLEGPQVA----ANSV 75
Cdd:cd17965 31 PSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLkrqeqepfEEAEEEYEsakdTGRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 76 RALVLVPTRELAEQVHGSVRDYGQHLPLRTAV--AYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALV 153
Cdd:cd17965 111 RSVILVPTHELVEQVYSVLKKLSHTVKLGIKTfsSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLV 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510932685 154 LDEADRMLDLGFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDPLSIeVSPR 212
Cdd:cd17965 191 VDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRI-ATPR 248
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
37-310 |
4.36e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 92.78 E-value: 4.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 37 KGRDLLAAAQTGTGKTaGFALPLLQRLtlegpqvaANSVRALVLVPTRELAEQVHGSVRDYgqhlpLRTAVAYGGvsinp 116
Cdd:COG1061 99 GGGRGLVVAPTGTGKT-VLALALAAEL--------LRGKRVLVLVPRRELLEQWAEELRRF-----LGDPLAGGG----- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 117 qmmKLRKGVDILVATPGRLldlyrQNAVKFAQLQA----LVLDEADRmldlGFARELDELFAALPRKRqTLLFSAT--FS 190
Cdd:COG1061 160 ---KKDSDAPITVATYQSL-----ARRAHLDELGDrfglVIIDEAHH----AGAPSYRRILEAFPAAY-RLGLTATpfRS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 191 D------------AIRTLARELLR-------------DPLSIEVSPRNTAAKSVRQWLVPvDKKRKAELFCHLLQAN-RW 244
Cdd:COG1061 227 DgreillflfdgiVYEYSLKEAIEdgylappeyygirVDLTDERAEYDALSERLREALAA-DAERKDKILRELLREHpDD 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510932685 245 RQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDI 310
Cdd:COG1061 306 RKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
38-188 |
1.48e-19 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 84.76 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 38 GRDLLAAAQTGTGKTAGFALPLLQRLTLEGPQVaansvraLVLVPTRELAEQVHGSVRDYGQHlPLRTAVAYGGVSINPQ 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKV-------LVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEER 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510932685 118 MMKLRKGVDILVATPGRLLDLYRQNA-VKFAQLQALVLDEADRMLDLGF-ARELDELFAALPRKR-QTLLFSAT 188
Cdd:cd00046 73 EKNKLGDADIIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHALLIDSRgALILDLAVRKAGLKNaQVILLSAT 146
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
2-204 |
2.38e-19 |
|
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: 85.93 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 2 TFASLGLLDPLLKALEGLGHGTPTPIQAQAIPPALKG--RDLLAAAQTGTGKTAGFALPLLQRLtlegpQVAANSVRALV 79
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-----EPANKYPQCLC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 80 LVPTRELAEQVHGSVRDYGQHLPlRTAVAYGgvsinPQMMKLRKGV----DILVATPGRLLD-LYRQNAVKFAQLQALVL 154
Cdd:cd18047 77 LSPTYELALQTGKVIEQMGKFYP-ELKLAYA-----VRGNKLERGQkiseQIVIGTPGTVLDwCSKLKFIDPKKIKVFVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510932685 155 DEADRMLDL-GFARELDELFAALPRKRQTLLFSATFSDAIRTLARELLRDP 204
Cdd:cd18047 151 DEADVMIATqGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
239-348 |
3.82e-17 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 84.01 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 239 LQANRWRQALVFAKTRKSVEELVGLLQRQGIAAD------SIHGDK--PQPARLRALQRFKAGEVDLLVATDVAARGLDI 310
Cdd:COG1111 348 LGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGEFNVLVATSVAEEGLDI 427
|
90 100 110
....*....|....*....|....*....|....*...
gi 510932685 311 EEMPLVVNFDLPIVAEDYVHRIGRTGRAGAsGQAVSLV 348
Cdd:COG1111 428 PEVDLVIFYEPVPSEIRSIQRKGRTGRKRE-GRVVVLI 464
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
28-356 |
8.54e-17 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 82.50 E-value: 8.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 28 QAQAIPPALKGRDLLAAAQTGTGKTAGFALP-LLqrltLEGP-------------QVAA---NSVRALVLVPTRELAEqv 90
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPaLL----LPGLtlvvsplialmkdQVDAlraAGIRAAFLNSSLSAEE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 91 hgsvrdygqhlplRTAVayggvsinpqMMKLRKG-VDILVATPGRLLDLYRQNAVKFAQLQALVLDEA--------Drml 161
Cdd:COG0514 96 -------------RREV----------LRALRAGeLKLLYVAPERLLNPRFLELLRRLKISLFAIDEAhcisqwghD--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 162 dlgFA---RELDELFAALPRkRQTLLFSATFSDAIRT-LAREL-LRDP-----------LSIEVSPRNTAAKsvRQWLVp 225
Cdd:COG0514 150 ---FRpdyRRLGELRERLPN-VPVLALTATATPRVRAdIAEQLgLEDPrvfvgsfdrpnLRLEVVPKPPDDK--LAQLL- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 226 vdkkrkaelfcHLLQANRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVAT---- 301
Cdd:COG0514 223 -----------DFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATiafg 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510932685 302 ------DVaaRgldieempLVVNFDLPIVAEDYVHRIGRTGRAGASGQAVSLVCADEVELL 356
Cdd:COG0514 292 mgidkpDV--R--------FVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQ 342
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
9-345 |
2.41e-16 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 81.42 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 9 LDPLLK-ALEGLGHGTPTPIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLtLEGPqvaanSVRALVLVPTRELA 87
Cdd:COG1205 41 LPPELRaALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDP-----GATALYLYPTKALA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 88 -EQVhGSVRDYGQHLPLRTAVA-YGGVSINPQMMKLRKGVDILVATP-----GrLLDLYRQNAVKFAQLQALVLDEA--- 157
Cdd:COG1205 115 rDQL-RRLRELAEALGLGVRVAtYDGDTPPEERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARFFRNLRYVVIDEAhty 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 158 ------------DRMldlgfaRELDELFAALPrkrQTLLFSATFSDAiRTLARELLRDPLSiEVSpRNTAAKSVRQWLV- 224
Cdd:COG1205 193 rgvfgshvanvlRRL------RRICRHYGSDP---QFILASATIGNP-AEHAERLTGRPVT-VVD-EDGSPRGERTFVLw 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 225 --PVDKKRK--------AELFCHLLQANrwRQALVFAKTRKSVEELVGLLQRQgiAADSIHGDKPQPAR---L----RAL 287
Cdd:COG1205 261 npPLVDDGIrrsalaeaARLLADLVREG--LRTLVFTRSRRGAELLARYARRA--LREPDLADRVAAYRagyLpeerREI 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510932685 288 -QRFKAGEVDLLVAT-------DVAarGLDieempLVVNFDLP--IVAedYVHRIGRTGRAGASGQAV 345
Cdd:COG1205 337 eRGLRSGELLGVVSTnalelgiDIG--GLD-----AVVLAGYPgtRAS--FWQQAGRAGRRGQDSLVV 395
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
23-192 |
1.41e-14 |
|
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: 71.52 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 23 TPTPIQAQAIPPA-LKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPqvaansvRALVLVPTRELAEQVHGSVRDYGQHL 101
Cdd:cd17921 1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSGG-------KAVYIAPTRALVNQKEADLRERFGPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 102 PLRTAVAYGGVSINPQMMKLRkgvDILVATPGRLLDLYRQNAVKFAQ-LQALVLDEAdRMLDLGfARE--LDELFAALPR 178
Cdd:cd17921 74 GKNVGLLTGDPSVNKLLLAEA---DILVATPEKLDLLLRNGGERLIQdVRLVVVDEA-HLIGDG-ERGvvLELLLSRLLR 148
|
170
....*....|....*..
gi 510932685 179 ---KRQTLLFSATFSDA 192
Cdd:cd17921 149 inkNARFVGLSATLPNA 165
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
248-348 |
3.30e-12 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 68.75 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 248 LVFAKTRKSVEELVGLLQRQGIAA------DSIHGDK--PQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVVnF 319
Cdd:PRK13766 369 IVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-F 447
|
90 100 110
....*....|....*....|....*....|
gi 510932685 320 DLPIVAE-DYVHRIGRTGRaGASGQAVSLV 348
Cdd:PRK13766 448 YEPVPSEiRSIQRKGRTGR-QEEGRVVVLI 476
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
228-341 |
5.55e-12 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 62.99 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 228 KKRKAELFCHLLQANRWR----QALVFAKTRKSVEELVGLLQRQGIAADSI-------HGDKPQPARL--------RALQ 288
Cdd:cd18802 5 VIPKLQKLIEILREYFPKtpdfRGIIFVERRATAVVLSRLLKEHPSTLAFIrcgfligRGNSSQRKRSlmtqrkqkETLD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 510932685 289 RFKAGEVDLLVATDVAARGLDIEEMPLVVNFDLPIVAEDYVHRIGRtGRAGAS 341
Cdd:cd18802 85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNS 136
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-373 |
7.41e-12 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 67.23 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 1 MTFASLGLLDpLLKALEGLGHGTPTPIQAQAIPPAL-KGRDLLAAAQTGTGKTAGFALPLLQRLtlegpqvaANSVRALV 79
Cdd:COG1204 1 MKVAELPLEK-VIEFLKERGIEELYPPQAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKAL--------LNGGKALY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 80 LVPTRELAEQVHGSVRDYGQHLPLRTAVAYGGVSINPQmmKLRKgVDILVATPGRLLDLYRQNAVKFAQLQALVLDEA-- 157
Cdd:COG1204 72 IVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDE--WLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 158 ----DRMLDLgfareldEL----FAALPRKRQTLLFSATFSDAiRTLAR----ELLRD-----PLSIEV---SPRNTAAK 217
Cdd:COG1204 149 iddeSRGPTL-------EVllarLRRLNPEAQIVALSATIGNA-EEIAEwldaELVKSdwrpvPLNEGVlydGVLRFDDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 218 SVRQwlvpvdKKRKAELFCHLLQANrwRQALVFAKTRKSVE----ELVGLLQRQGIA----------------------- 270
Cdd:COG1204 221 SRRS------KDPTLALALDLLEEG--GQVLVFVSSRRDAEslakKLADELKRRLTPeereeleelaeellevseethtn 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 271 ---ADSI-------HGDKPQPARLRALQRFKAGEVDLLVATDVAARGL----------DIEEMPLVvnfdlPIVAEDYVH 330
Cdd:COG1204 293 eklADCLekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVnlparrviirDTKRGGMV-----PIPVLEFKQ 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 510932685 331 RIGRTGRAGA--SGQAVsLVCADEVELlaaiETLIGQTLQRREEP 373
Cdd:COG1204 368 MAGRAGRPGYdpYGEAI-LVAKSSDEA----DELFERYILGEPEP 407
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
247-339 |
1.58e-11 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 61.46 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 247 ALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATdVA-ARGLDIEEMPLVVNFDLPIVA 325
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-VAfGMGIDKPDVRFVIHYSLPKSM 111
|
90
....*....|....
gi 510932685 326 EDYVHRIGRTGRAG 339
Cdd:cd18794 112 ESYYQESGRAGRDG 125
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
26-347 |
2.85e-11 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 65.50 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 26 PIQAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQR--LTL-----------EGPQVAANSVRALVLVPTRELAEQVhg 92
Cdd:PRK11057 28 PGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLdgLTLvvsplislmkdQVDQLLANGVAAACLNSTQTREQQL-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 93 svrdygqhlplrtAVayggvsinpqMMKLRKG-VDILVATPGRLL-DLYRQNAVKFaQLQALVLDEADRMLDLG--FARE 168
Cdd:PRK11057 106 -------------EV----------MAGCRTGqIKLLYIAPERLMmDNFLEHLAHW-NPALLAVDEAHCISQWGhdFRPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 169 ldelFAALPRKRQ------TLLFSATFSDAIRT-LAREL-LRDPLsIEVSPRNTAakSVRQWLVpvDKKRKAELFCHLLQ 240
Cdd:PRK11057 162 ----YAALGQLRQrfptlpFMALTATADDTTRQdIVRLLgLNDPL-IQISSFDRP--NIRYTLV--EKFKPLDQLMRYVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 241 ANRWRQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVVNFD 320
Cdd:PRK11057 233 EQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFD 312
|
330 340
....*....|....*....|....*..
gi 510932685 321 LPIVAEDYVHRIGRTGRAGASGQAVSL 347
Cdd:PRK11057 313 IPRNIESYYQETGRAGRDGLPAEAMLF 339
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
247-337 |
5.40e-11 |
|
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: 60.45 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 247 ALVFAKTRKSVEELVGLLQRQG--------IAADSIHGDK--PQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLV 316
Cdd:cd18801 33 VIIFSEFRDSAEEIVNFLSKIRpgiratrfIGQASGKSSKgmSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112
|
90 100
....*....|....*....|.
gi 510932685 317 VNFDLPIVAEDYVHRIGRTGR 337
Cdd:cd18801 113 ICYDASPSPIRMIQRMGRTGR 133
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
47-157 |
1.17e-09 |
|
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: 57.66 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 47 TGTGKTAgFALPLLQRLTLEGPQVAANSVRALVLVPTRELAEQVHGSVRdygQHLPLRTAVAYG--GVSINPQMMKLR-- 122
Cdd:cd18034 25 TGSGKTL-IAVMLIKEMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIR---SHTDLKVGEYSGemGVDKWTKERWKEel 100
|
90 100 110
....*....|....*....|....*....|....*
gi 510932685 123 KGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEA 157
Cdd:cd18034 101 EKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
22-301 |
1.35e-09 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 60.50 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 22 GTPTPIQAQAIPPALKGRDLLAAAQTGTGKT-AGFaLPLLQRLTLEG-PQVAANSVRALVLVPTRELAEQVH-------- 91
Cdd:COG1201 23 GAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPrPGELPDGLRVLYISPLKALANDIErnlraple 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 92 GSVRDYGQHLP-LRTAVAYGGVSINP-QMMkLRKGVDILVATPGRL--LDLYRQNAVKFAQLQALVLDE----AD--R-- 159
Cdd:COG1201 102 EIGEAAGLPLPeIRVGVRTGDTPASErQRQ-RRRPPHILITTPESLalLLTSPDARELLRGVRTVIVDEihalAGskRgv 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 160 MLDLGFAReLDELfaaLPRKRQTLLFSATFSDaIRTLARELLRDPlsievSPRNTA---AKSVRQW----LVPVDKkrKA 232
Cdd:COG1201 181 HLALSLER-LRAL---APRPLQRIGLSATVGP-LEEVARFLVGYE-----DPRPVTivdAGAGKKPdlevLVPVED--LI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 233 ELFCH--------------LLQANrwRQALVFAKTRKSVEELVG-LLQRQGIAADSI---HG--DKPQpaRLRALQRFKA 292
Cdd:COG1201 249 ERFPWaghlwphlyprvldLIEAH--RTTLVFTNTRSQAERLFQrLNELNPEDALPIaahHGslSREQ--RLEVEEALKA 324
|
....*....
gi 510932685 293 GEVDLLVAT 301
Cdd:COG1201 325 GELRAVVAT 333
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
231-333 |
3.85e-09 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 54.79 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 231 KAELFCHLLQANRWRQ--ALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKA--GEVDLLVATDVAAR 306
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 510932685 307 GLDIEEMPLVVNFDL---PIV---AEDYVHRIG 333
Cdd:cd18793 92 GLNLTAANRVILYDPwwnPAVeeqAIDRAHRIG 124
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
23-159 |
8.03e-08 |
|
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: 52.43 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 23 TPTPIQAQAIPPALKGRDLLAAAQTGTGKTagFALPLLQRLTLEGPQvAANSVRALVLVPTRELAEQVHGSVRDYGQHLP 102
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKT--FVAVLICEHHLKKFP-AGRKGKVVFLANKVPLVEQQKEVFRKHFERPG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 510932685 103 LRTAVAYGGVSINPQMMKLRKGVDILVATPGRLL-DLYRQNAVKFAQLQALVLDEADR 159
Cdd:cd17927 79 YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
38-156 |
4.49e-07 |
|
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: 49.50 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 38 GRDLLAAAQTGTGKTAGFALPLLQRLTLEGPqvaaNSVRALVLVPTRELAEQVHGSVRDYGQH--LPLRTAVAYGGVSIN 115
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPE----KGVQVLYISPLKALINDQERRLEEPLDEidLEIPVAVRHGDTSQS 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 510932685 116 PQMMKLRKGVDILVATPGRL--LDLYRQNAVKFAQLQALVLDE 156
Cdd:cd17922 77 EKAKQLKNPPGILITTPESLelLLVNKKLRELFAGLRYVVVDE 119
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
26-287 |
8.81e-07 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 51.36 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 26 PIQAQAIPP-ALKGRDLLAAAQTGTGKTAGFALPLLQRLTLEGPqvaansvRALVLVPTRELAEQVHGSVRDYgQHLPLR 104
Cdd:PRK00254 26 PPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGG-------KAVYLVPLKALAEEKYREFKDW-EKLGLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 105 TAVAYGGVSINPQMMklrKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELDELFAALPRKRQTLL 184
Cdd:PRK00254 98 VAMTTGDYDSTDEWL---GKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQILG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 185 FSATFSDAirtlarELLRDPLSievsprntaAKSVRQWLVPVDKKR----KAELFCHLLQANRW---------------R 245
Cdd:PRK00254 175 LSATVGNA------EELAEWLN---------AELVVSDWRPVKLRKgvfyQGFLFWEDGKIERFpnsweslvydavkkgK 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 510932685 246 QALVFAKTRKSVE----ELVGLLQRqgiaadsiHGDKPQPARLRAL 287
Cdd:PRK00254 240 GALVFVNTRRSAEkealELAKKIKR--------FLTKPELRALKEL 277
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-157 |
1.73e-06 |
|
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: 47.96 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 28 QAQAIPPALKGRDLLAAAQTGTGKTAGFALPLLQRLtlegpqVAANSVRALVLVPTRELA-EQVHgSVRDYGQHLPLRTA 106
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL------LRDPGSRALYLYPTKALAqDQLR-SLRELLEQLGLGIR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 510932685 107 VA-YGG-VSINPQMMKLRKGVDILVATPGRL---LDLYRQNAVKFAQ-LQALVLDEA 157
Cdd:cd17923 78 VAtYDGdTPREERRAIIRNPPRILLTNPDMLhyaLLPHHDRWARFLRnLRYVVLDEA 134
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
297-339 |
2.41e-06 |
|
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: 45.00 E-value: 2.41e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 510932685 297 LLVATDVAARGLDIEEMPLVVNFDLPIVAEDYVHRIGRTGRAG 339
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
247-384 |
3.90e-06 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 46.85 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 247 ALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVVNFD-----L 321
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegF 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510932685 322 PIVAEDYVHRIGRTGRaGASGQAVslVCADEVEllAAIETLIGQTLQRRE-EPDFEPEHR-VPQT 384
Cdd:cd18790 110 LRSETSLIQTIGRAAR-NVNGKVI--LYADKIT--DSMQKAIEETERRREiQMEYNEEHGiTPKT 169
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
166-335 |
5.04e-06 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 49.07 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 166 ARELDELFAALPRKRQTLLFSAtfsdaiRTLARELLRDPLSIEVSPRNTAAKSVR-QWLVpvdkkrkaELFCHLLQANRw 244
Cdd:COG0553 486 EYLRRELEGAEGIRRRGLILAA------LTRLRQICSHPALLLEEGAELSGRSAKlEALL--------ELLEELLAEGE- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 245 rQALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPARLRALQRFKAGE--VDLLVATDVAARGLDIEEMPLVVNFDL- 321
Cdd:COG0553 551 -KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLw 629
|
170
....*....|....*....
gi 510932685 322 --PIV---AEDYVHRIGRT 335
Cdd:COG0553 630 wnPAVeeqAIDRAHRIGQT 648
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
248-361 |
7.17e-06 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain] Cd Length: 174 Bit Score: 46.14 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 248 LVFAKTRKSVE---ELVGLLQRQGIAADSIHGDKPQParlraLQRFKAGEVDLLVAT----DVAARGLDieeMPLVVNF- 319
Cdd:cd18798 28 LIFVSIDYGKEyaeELKEFLERHGIKAELALSSTEKN-----LEKFEEGEIDVLIGVasyyGVLVRGID---LPERIKYa 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 510932685 320 ---DLPIVAedYVHRIGRTGR--AGASGQAVSLVCADEVELLAAIET 361
Cdd:cd18798 100 ifyGVPVTT--YIQASGRTSRlyAGGLTKGLSVVLVDDPELFEALKK 144
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
247-323 |
1.17e-05 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 44.47 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 247 ALVFAKTRKSVEELVGLLQRQGIAADSIHGDKPQPAR-LRALQRFKAGEVDL--LVATDVAARGLDIEEMPLVVnFDLPI 323
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELKPpiLVTVDLLTTGVDIPEVDNVV-FLRPT 87
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
23-197 |
1.21e-05 |
|
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: 45.48 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 23 TPTPIQAQAIPPALKG------RDLLAAAQTGTGKTAGFALPLLQrltlegpqVAANSVRALVLVPTRELAEQVHGSVRD 96
Cdd:cd17918 15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL--------AYKNGKQVAILVPTEILAHQHYEEARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 97 YGQHLPLRTAVAYGGVSINPqmmklrkGVDILVATPGRLldlyrQNAVKFAQLQALVLDEADRMldlGFAREldelfAAL 176
Cdd:cd17918 87 FLPFINVELVTGGTKAQILS-------GISLLVGTHALL-----HLDVKFKNLDLVIVDEQHRF---GVAQR-----EAL 146
|
170 180
....*....|....*....|....
gi 510932685 177 PRKRQT--LLFSATfsdAI-RTLA 197
Cdd:cd17918 147 YNLGAThfLEATAT---PIpRTLA 167
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
27-156 |
1.58e-05 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 45.81 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 27 IQAQAIPPALKG-RDLLAAAQTGTGKTAGFALPLLqRLTLEGPQVAANSVRALVLVPTRELAEQvhgSVRDYGQHLPlRT 105
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAIL-RLLKERNPLPWGNRKVVYIAPIKALCSE---KYDDWKEKFG-PL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 510932685 106 AVAYGGVSINPQMMKLR--KGVDILVATPGR--LLDLYRQNAVKFAQLQALVL-DE 156
Cdd:cd18023 80 GLSCAELTGDTEMDDTFeiQDADIILTTPEKwdSMTRRWRDNGNLVQLVALVLiDE 135
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
26-156 |
5.35e-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: 43.86 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 26 PIQAQAIPPAL-KGRDLLAAAQTGTGKTAGFALPLLQRLtLEGPqvaansvRALVLVPTRELAEQVHGSVRDYgQHLPLR 104
Cdd:cd18028 4 PPQAEAVRAGLlKGENLLISIPTASGKTLIAEMAMVNTL-LEGG-------KALYLVPLRALASEKYEEFKKL-EEIGLK 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 510932685 105 TAVAYGGVSINPQMMklrKGVDILVATPGRLLDLYRQNAVKFAQLQALVLDE 156
Cdd:cd18028 75 VGISTGDYDEDDEWL---GDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE 123
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
47-189 |
1.75e-04 |
|
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: 41.52 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 47 TGTGKTA-GFALPLLQRltlegpqvaanSVRALVLVPTRELAEQVHGSVRDYGQHLPLrtavayGGVSINPQmmKLRKGV 125
Cdd:cd17926 27 TGSGKTLtALALIAYLK-----------ELRTLIVVPTDALLDQWKERFEDFLGDSSI------GLIGGGKK--KDFDDA 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510932685 126 DILVATPGRLLDLYRQNAVKFAQLQALVLDEADRMLDLGFARELDELFAALprkrqTLLFSATF 189
Cdd:cd17926 88 NVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSEILKELNAKY-----RLGLTATP 146
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1-156 |
1.94e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 43.79 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 1 MTFASLGLLDPLLKALEGLGHGTPTPIQAQAIPP-ALKGRDLLAAAQTGTGKTAGFALPLLQRltlegpqvAANSVRALV 79
Cdd:PRK02362 1 MKIAELPLPEGVIEFYEAEGIEELYPPQAEAVEAgLLDGKNLLAAIPTASGKTLIAELAMLKA--------IARGGKALY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 80 LVPTRELAEQVHGSVRDYGQhLPLRTAVAYG-------GVSINpqmmklrkgvDILVATPGRLLDLYRQNAVKFAQLQAL 152
Cdd:PRK02362 73 IVPLRALASEKFEEFERFEE-LGVRVGISTGdydsrdeWLGDN----------DIIVATSEKVDSLLRNGAPWLDDITCV 141
|
....
gi 510932685 153 VLDE 156
Cdd:PRK02362 142 VVDE 145
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
22-156 |
3.18e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 43.34 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 22 GTPTPIQAQAIPPALKGRDLLAAAQTGTGKT-AGFA------LPLLQRLTLEgpqvaaNSVRALVLVPTRELAEQVH--- 91
Cdd:PRK13767 31 GTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLaiidelFRLGREGELE------DKVYCLYVSPLRALNNDIHrnl 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510932685 92 --------GSVRDYGQHLP-LRTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYrqNAVKFAQ----LQALVLDE 156
Cdd:PRK13767 105 eeplteirEIAKERGEELPeIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILL--NSPKFREklrtVKWVIVDE 180
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
23-189 |
4.48e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 40.73 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 23 TPTPIQAQAIPPALKGRD------LLAAAqTGTGKTAgFALPLLQRLTLEGPqvaanSVRALVLVPTRELAEQvhgSVRD 96
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKngqkrgLIVMA-TGSGKTL-TAAKLIARLFKKGP-----IKKVLFLVPRKDLLEQ---ALEE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 97 YGQHLPlrTAVAYGGVSINPQMMKLRKGVDILVATPGRLLDLYRQNAVKFAQLQALVL--DEADRMLDLGFaRELDELFa 174
Cdd:pfam04851 73 FKKFLP--NYVEIGEIISGDKKDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHRSGASSY-RNILEYF- 148
|
170
....*....|....*.
gi 510932685 175 alprKRQTLL-FSATF 189
Cdd:pfam04851 149 ----KPAFLLgLTATP 160
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
246-339 |
5.82e-04 |
|
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: 40.31 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 246 QALVFAKtrkSVEELVGLLQRQGIAAdsIHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVVnfdlpIVA 325
Cdd:cd18789 51 KIIVFTD---NVEALYRYAKRLLKPF--ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAI-----QIS 120
|
90 100
....*....|....*....|
gi 510932685 326 ------EDYVHRIGRTGRAG 339
Cdd:cd18789 121 ghggsrRQEAQRLGRILRPK 140
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
232-339 |
6.44e-04 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 39.93 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 232 AELFCHLLQANRwrQALVFAKTRKSVEELVGLLQrqgiaaDSIHGDKPQPARLRAL-------------QRFKAGEVDLL 298
Cdd:cd18797 25 ARLFADLVRAGV--KTIVFCRSRKLAELLLRYLK------ARLVEEGPLASKVASYragylaedrreieAELFNGELLGV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 510932685 299 VATDVAARGLDIEEMPLVVNFDLPIVAEDYVHRIGRTGRAG 339
Cdd:cd18797 97 VATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRG 137
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
23-89 |
9.85e-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: 40.15 E-value: 9.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510932685 23 TPTPIQAQAIPPALKGRDLLAAAQTGTGKTagFALPLLQRLTLEGPQVAANSVRALVLVPTRELAEQ 89
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKT--RVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQ 66
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
237-337 |
1.09e-03 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 39.55 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 237 HLLQANRWRQALVFAKTRKSVEEL-VGLLQRQGIAADSI-----HGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDI 310
Cdd:cd18796 31 VIFLLERHKSTLVFTNTRSQAERLaQRLRELCPDRVPPDfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDI 110
|
90 100
....*....|....*....|....*..
gi 510932685 311 EEMPLVVNFDLPIVAEDYVHRIGRTGR 337
Cdd:cd18796 111 GDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
36-131 |
1.22e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain] Cd Length: 189 Bit Score: 40.00 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 36 LKGRDLLAAAQTGTGKTA-GFALPLLqrltlegpqVAANSVRALVLVPTRELAEQVHGSVRDYGQHL--PLRTAVAYGGV 112
Cdd:cd17924 30 LRGKSFAIIAPTGVGKTTfGLATSLY---------LASKGKRSYLIFPTKSLVKQAYERLSKYAEKAgvEVKILVYHSRL 100
|
90 100
....*....|....*....|...
gi 510932685 113 SINPQ---MMKLRKG-VDILVAT 131
Cdd:cd17924 101 KKKEKeelLEKIEKGdFDILVTT 123
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
274-339 |
1.60e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 39.25 E-value: 1.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510932685 274 IHGDKPQPARLRALQRFKAGEVDLLVATDVAARGLDIEEMPLVVNFDlpivAEDY----VHRI-GRTGRAG 339
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED----AERFglsqLHQLrGRVGRGD 133
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
23-159 |
6.44e-03 |
|
DEXH/Q-box 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 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: 350749 [Multi-domain] Cd Length: 193 Bit Score: 37.55 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510932685 23 TPTPIQAQAIPPALK----GR--DLLAAAQTGTGKTAgFALPLLQRLTLEGPQVAansvralVLVPTRELAEQVHGSVRD 96
Cdd:cd17991 15 EETPDQLKAIEEILKdmesGKpmDRLICGDVGFGKTE-VAMRAAFKAVLSGKQVA-------VLVPTTLLAQQHYETFKE 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510932685 97 YGQHLPLRTAVAYGGVSINPQ---MMKLRKG-VDILVATpGRLLdlyrQNAVKFAQLQALVLDEADR 159
Cdd:cd17991 87 RFANFPVNVELLSRFTTAAEQreiLEGLKEGkVDIVIGT-HRLL----SKDVEFKNLGLLIIDEEQR 148
|
|
| |
