|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-402 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 607.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 1 MSFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEvnARVQALVLTP 80
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP--RAPQALILAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 81 TRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLD 160
Cdd:COG0513 80 TRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 161 MGFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIEVDQRNATASQVEQIAYEVDKHRKREITSFLIGSK 240
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 241 NWQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYVINYELP 320
Cdd:COG0513 240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 321 HNAEDYIHRIGRTGRAGETGLAISLLSADETWLLDEIHKIIDTRLMQQWLPGYEPSLEQDFA----------QKPKAGRG 390
Cdd:COG0513 320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLErlkpkikeklKGKKAGRG 399
|
410
....*....|..
gi 518451542 391 NRNKNRGRSRRR 402
Cdd:COG0513 400 GRPGPKGERKAR 411
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-402 |
1.02e-173 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 492.79 E-value: 1.02e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 1 MSFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASE-EVNAR--VQALV 77
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQpHAKGRrpVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 78 LTPTRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADR 157
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 158 MLDMGFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIEVDQRNATASQVEQIAYEVDKHRKREITSFLI 237
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 238 GSKNWQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYVINY 317
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 318 ELPHNAEDYIHRIGRTGRAGETGLAISLLSADETWLLDEIHKIIDTRLMQQWLPGYEP--SLEQDFAQKPKAGRGNRNKN 395
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEPdpSIKAEPIQNGRQQRGGGGRG 400
|
....*..
gi 518451542 396 RGRSRRR 402
Cdd:PRK10590 401 QGGGRGQ 407
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-351 |
3.71e-131 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 384.54 E-value: 3.71e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 1 MSFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASeevNARVQALVLTP 80
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVK---RFRVQALVLCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 81 TRELAQQVGKSFQQY--GAHtSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRM 158
Cdd:PRK11776 81 TRELADQVAKEIRRLarFIP-NIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 159 LDMGFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIEVDQRNAtASQVEQIAYEVDKHRKREITSFLIG 238
Cdd:PRK11776 160 LDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHD-LPAIEQRFYEVSPDERLPALQRLLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 239 SKNWQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYVINYE 318
Cdd:PRK11776 239 HHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYE 318
|
330 340 350
....*....|....*....|....*....|...
gi 518451542 319 LPHNAEDYIHRIGRTGRAGETGLAISLLSADET 351
Cdd:PRK11776 319 LARDPEVHVHRIGRTGRAGSKGLALSLVAPEEM 351
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
1-375 |
5.27e-110 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 329.60 E-value: 5.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 1 MSFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPIL-HLLEASEEVNARVQALVLT 79
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALqHLLDFPRRKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 80 PTRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRML 159
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 160 DMGFIDDIKRIlrsVPETR---QTLLFSATFD-DAIFKLSQKLLHDPALIEVDQRNATASQVEQIAYEVD-KHRKREITS 234
Cdd:PRK11192 161 DMGFAQDIETI---AAETRwrkQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADdLEHKTALLC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 235 FLIGSKNWQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYV 314
Cdd:PRK11192 238 HLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHV 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518451542 315 INYELPHNAEDYIHRIGRTGRAGETGLAISLLSADETWLLDEIHKIIDTRLMQQWLPGYEP 375
Cdd:PRK11192 318 INFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRP 378
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
3-402 |
2.20e-104 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 314.99 E-value: 2.20e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 3 FASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVNARVQ----ALVL 78
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRKVnqprALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 79 TPTRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRM 158
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 159 LDMGFIDDIKRILRSVPET--RQTLLFSATFDDAIFKLSQKLLHDPALIEVDQRNATASQV-EQIAYEVDKHRKREITSF 235
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPPAnqRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIkEELFYPSNEEKMRLLQTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 236 LigSKNW-QQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYV 314
Cdd:PRK04837 250 I--EEEWpDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 315 INYELPHNAEDYIHRIGRTGRAGETGLAISL--------LSADETWLLdeiHKIIDTRlmqqwlpgYEPS-LEQDFA--- 382
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISLaceeyalnLPAIETYIG---HSIPVSK--------YDSDaLLTDLPkpl 396
|
410 420
....*....|....*....|..
gi 518451542 383 --QKPKAGRGNRNKNRGRSRRR 402
Cdd:PRK04837 397 rlTRPRTGNGPRRSGAPRNRRR 418
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-371 |
2.62e-104 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 316.47 E-value: 2.62e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 3 FASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEAS----EEVNARVQALVL 78
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTpppkERYMGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 79 TPTRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVK-QGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADR 157
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 158 MLDMGFIDDIKRILRSVP--ETRQTLLFSATFDDAIFKLSQKLLHDPALIEVDQRNATASQVEQIAYEVDKHRKREITSF 235
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 236 LIGSKNWQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYVI 315
Cdd:PRK01297 329 LVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVI 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 518451542 316 NYELPHNAEDYIHRIGRTGRAGETGLAISLLSADETWLLDEIHKIIDTRLMQQWLP 371
Cdd:PRK01297 409 NFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPP 464
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-374 |
3.54e-104 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 321.03 E-value: 3.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 1 MSFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEAseEVNARvQALVLTP 80
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDP--ELKAP-QILVLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 81 TRELAQQVGKSFQQYGAHTSLRTVVA-YGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRML 159
Cdd:PRK11634 83 TRELAVQVAEAMTDFSKHMRGVNVVAlYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 160 DMGFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIEVDQRNATASQVEQIAYEVDKHRKREITSFLIGS 239
Cdd:PRK11634 163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 240 KNWQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYVINYEL 319
Cdd:PRK11634 243 EDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDI 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 518451542 320 PHNAEDYIHRIGRTGRAGETGLAISLLSADETWLLDEIHKIIDTRLMQQWLPGYE 374
Cdd:PRK11634 323 PMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAE 377
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
2-399 |
8.07e-103 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 314.79 E-value: 8.07e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 2 SFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALP-ILHLL-EASEEVNARVQALVLT 79
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaIVHINaQPLLRYGDGPIVLVLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 80 PTRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRML 159
Cdd:PTZ00110 211 PTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRML 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 160 DMGFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLL-HDPALIEVDQRNATASQ-VEQIAYEVDKHRKR-EITSFL 236
Cdd:PTZ00110 291 DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDLTACHnIKQEVFVVEEHEKRgKLKMLL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 237 --IGSKNwQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYV 314
Cdd:PTZ00110 371 qrIMRDG-DKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYV 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 315 INYELPHNAEDYIHRIGRTGRAGETGLAISLLSADETWLLDEIHKIIdtRLMQQWLPgyePSLEQDFAQKPKAGRGNRNK 394
Cdd:PTZ00110 450 INFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVL--REAKQPVP---PELEKLSNERSNGTERRRWG 524
|
....*
gi 518451542 395 NRGRS 399
Cdd:PTZ00110 525 GYGRF 529
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-206 |
3.86e-101 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 298.20 E-value: 3.86e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPIL-HLLEASEEVNARVQALVLTPTRELAQQVGK 90
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILeKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 91 SFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFIDDIKRI 170
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 518451542 171 LRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIE 206
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-365 |
5.05e-92 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 288.00 E-value: 5.05e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 1 MSFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVNAR----VQAL 76
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRkpedPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 77 VLTPTRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGR-QAIDLSCLSFFVLDEA 155
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 156 DRMLDMGFIDDIKRILRSVPE--TRQTLLFSATFDDAIFKLSQKLLHDPALIEVDQRNATASQVEQIAYEVDKHRKREIT 233
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 234 SFLIGSKNWQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSY 313
Cdd:PRK04537 249 LGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 518451542 314 VINYELPHNAEDYIHRIGRTGRAGETGLAISLLSADETWLLDEIHKIIDTRL 365
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKI 380
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
2-201 |
3.13e-86 |
|
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: 261.27 E-value: 3.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 2 SFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILH-LLEASEEVNARV------Q 74
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISkLLEDGPPSVGRGrrkaypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 75 ALVLTPTRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDE 154
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518451542 155 ADRMLDMGFIDDIKRILRS----VPETRQTLLFSATFDDAIFKLSQKLLHD 201
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKN 211
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
2-365 |
4.37e-84 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 262.07 E-value: 4.37e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 2 SFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASeeVNArVQALVLTPT 81
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD--LNA-CQALILAPT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 82 RELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDM 161
Cdd:PTZ00424 106 RELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 162 GFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIEVDQRNATASQVEQIAYEVDKHR-KREITSFLIGSK 240
Cdd:PTZ00424 186 GFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEwKFDTLCDLYETL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 241 NWQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYVINYELP 320
Cdd:PTZ00424 266 TITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLP 345
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 518451542 321 HNAEDYIHRIGRTGRAGETGLAISLLSADETWLLDEIHKIIDTRL 365
Cdd:PTZ00424 346 ASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQI 390
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
1-357 |
9.17e-80 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 254.71 E-value: 9.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 1 MSFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPIL------HLLEASEEVNARvq 74
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsrcctiRSGHPSEQRNPL-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 75 ALVLTPTRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDE 154
Cdd:PLN00206 199 AMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 155 ADRMLDMGFIDDIKRILRSVPeTRQTLLFSATFDDAIFKLSQKLLHDPALIEVDQRNATASQVEQIAYEVD-KHRKREIT 233
Cdd:PLN00206 279 VDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVEtKQKKQKLF 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 234 SFLIGSKNWQ-QVLIFTRTKKSADDLAKEMCK-DGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQL 311
Cdd:PLN00206 358 DILKSKQHFKpPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRV 437
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 518451542 312 SYVINYELPHNAEDYIHRIGRTGRAGETGLAISLLSADETWLLDEI 357
Cdd:PLN00206 438 RQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPEL 483
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-200 |
6.64e-75 |
|
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: 233.71 E-value: 6.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 1 MSFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPIL-----HLLEASEEVNAR-VQ 74
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLtgmmkEGLTASSFSEVQePQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 75 ALVLTPTRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDE 154
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518451542 155 ADRMLDMGFIDDIKRILRS--VP--ETRQTLLFSATFDDAIFKLSQKLLH 200
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEpgMPskEDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
12-202 |
1.18e-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: 225.60 E-value: 1.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVNARVQALVLTPTRELAQQVGKS 91
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 92 FQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLID-LLGRQAIDLSCLSFFVLDEADRMLDMGFIDDIKRI 170
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDhLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|..
gi 518451542 171 LRSVPETRQTLLFSATFDDAIFKLSQKLLHDP 202
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKP 192
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
2-205 |
4.13e-70 |
|
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: 219.48 E-value: 4.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 2 SFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVNArVQALVLTPT 81
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVG-ARALILSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 82 RELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDM 161
Cdd:cd17959 81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518451542 162 GFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
3-206 |
2.48e-69 |
|
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: 217.48 E-value: 2.48e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 3 FASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLeaSEEVNArVQALVLTPTR 82
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL--SEDPYG-IFALVLTPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 83 ELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLL---GRQAIDLSCLSFFVLDEADRML 159
Cdd:cd17955 78 ELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLrssDDTTKVLSRVKFLVLDEADRLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518451542 160 DMGFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIE 206
Cdd:cd17955 158 TGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
2-206 |
3.61e-68 |
|
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: 214.49 E-value: 3.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 2 SFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILH-LLEASEevnaRVQALVLTP 80
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQaLLENPQ----RFFALVLAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 81 TRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGR-QAIDLSCLSFFVLDEADRML 159
Cdd:cd17954 77 TRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEADRLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518451542 160 DMGFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIE 206
Cdd:cd17954 157 NMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
7-207 |
1.08e-64 |
|
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: 206.07 E-value: 1.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 7 GLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPIL-HLLE--ASEEVNARVqALVLTPTRE 83
Cdd:cd17953 18 GLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrHIKDqrPVKPGEGPI-GLIMAPTRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 84 LAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLL---GRQAIDLSCLSFFVLDEADRMLD 160
Cdd:cd17953 97 LALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRMFD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518451542 161 MGFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPalIEV 207
Cdd:cd17953 177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP--IEI 221
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
25-194 |
1.00e-62 |
|
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: 199.01 E-value: 1.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 25 TPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEvnaRVQALVLTPTRELAQQVGKSFQQYGAHTSLRTV 104
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN---GPQALVLAPTRELAEQIYEELKKLGKGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 105 VAYGGVSINNQLSVVKqGVDILVATPGRLIDLLgRQAIDLSCLSFFVLDEADRMLDMGFIDDIKRILRSVPETRQTLLFS 184
Cdd:pfam00270 78 SLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLL-QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLS 155
|
170
....*....|
gi 518451542 185 ATFDDAIFKL 194
Cdd:pfam00270 156 ATLPRNLEDL 165
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
8-206 |
1.12e-61 |
|
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: 197.81 E-value: 1.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 8 LNPALLQAIESKGYSQPTPIQSEAIPAIL-NRQDVMAGAQTGTGKTAAFALPIL-HLLE-ASEEVNARVQALVLTPTREL 84
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIqSLLNtKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 85 AQQVGKSFQQY-GAHTSLRTVVAYGGVSINNQL-SVVKQGVDILVATPGRLIDLLGRQ--AIDLSCLSFFVLDEADRMLD 160
Cdd:cd17964 81 ALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELnRLRRGRPDILVATPGRLIDHLENPgvAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518451542 161 MGFIDDIKRILRSVP----ETRQTLLFSATFDDAIFKLSQK-LLHDPALIE 206
Cdd:cd17964 161 MGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLtLKKDYKFID 211
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
3-202 |
6.40e-61 |
|
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: 195.62 E-value: 6.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 3 FASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLleaseevnarVQALVLTPTR 82
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI----------VVALILEPSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 83 ELAQQVGKSFQQYGAHT---SLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRML 159
Cdd:cd17938 71 ELAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518451542 160 DMGFIDDIKRILRSVP-----ETR-QTLLFSATF-DDAIFKLSQKLLHDP 202
Cdd:cd17938 151 SQGNLETINRIYNRIPkitsdGKRlQVIVCSATLhSFEVKKLADKIMHFP 200
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
217-346 |
9.36e-61 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 192.72 E-value: 9.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 217 VEQIAYEVDKHRKREIT-SFLIGSKNWQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRV 295
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 518451542 296 LVATDVASRGLDIPQLSYVINYELPHNAEDYIHRIGRTGRAGETGLAISLL 346
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
3-205 |
1.04e-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: 192.51 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 3 FASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVnarVQALVLTPTR 82
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV---IQALILVPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 83 ELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMG 162
Cdd:cd17940 78 ELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518451542 163 FIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17940 158 FQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
12-205 |
1.79e-59 |
|
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: 192.53 E-value: 1.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVNARV-----QALVLTPTRELAQ 86
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETkddgpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 87 QVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFIDD 166
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518451542 167 IKRILRSVPET--------------------RQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17945 161 VTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
12-205 |
2.48e-59 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 191.52 E-value: 2.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALP-ILHLLE--ASEEVNARVQALVLTPTRELAQQV 88
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLqpIPREQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 89 GKSFQQYgAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFIDDIK 168
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 518451542 169 RILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
2-201 |
9.34e-59 |
|
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: 191.79 E-value: 9.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 2 SFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVNARVQ------- 74
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESLPSesgyygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 75 ------ALVLTPTRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLS 148
Cdd:cd18051 102 rkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518451542 149 FFVLDEADRMLDMGFIDDIKRILR--SVPET--RQTLLFSATFDDAIFKLSQKLLHD 201
Cdd:cd18051 182 YLVLDEADRMLDMGFEPQIRRIVEqdTMPPTgeRQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
12-205 |
6.99e-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: 187.62 E-value: 6.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALP-ILHLLEASE-EVNARVQALVLTPTRELAQQVG 89
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPmLVHIMDQRElEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 90 KSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFIDDIKR 169
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 518451542 170 ILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-207 |
4.55e-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: 185.49 E-value: 4.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEvNARVQALVLTPTRELAQQVGKS 91
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRK-KKGLRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 92 FQQYGAHTSLRTVV-AYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFIDDIKRI 170
Cdd:cd17957 80 LLKLSKGTGLRIVLlSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 518451542 171 LRSVPETR-QTLLFSATFDDAIFKLSQKLLHDPALIEV 207
Cdd:cd17957 160 LAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
12-205 |
6.73e-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: 185.09 E-value: 6.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEV--NARVQALVLTPTRELAQQVG 89
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANlkKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 90 KSFQQYGAHTS--LRTVVAYGGVSINNQL-SVVKQGVDILVATPGRLIDLLGRQA--IDLSCLSFFVLDEADRMLDMGFI 164
Cdd:cd17960 81 EVLQSFLEHHLpkLKCQLLIGGTNVEEDVkKFKRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518451542 165 DDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
8-203 |
1.34e-56 |
|
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: 184.71 E-value: 1.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 8 LNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILH-LLEASEEVNAR--VQALVLTPTREL 84
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQkILKAKAESGEEqgTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 85 AQQVGKSFQQYGAHTS--LRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAI-DLSCLSFFVLDEADRMLDM 161
Cdd:cd17961 81 AQQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518451542 162 GFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPA 203
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
7-205 |
1.39e-56 |
|
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: 184.45 E-value: 1.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 7 GLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVnarVQALVLTPTRELAQ 86
Cdd:cd17939 3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRE---TQALVLAPTRELAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 87 QVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFIDD 166
Cdd:cd17939 80 QIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 518451542 167 IKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17939 160 IYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
16-220 |
2.65e-55 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 181.15 E-value: 2.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 16 IESKGYSQPTPIQSEAIPAIL-NRQDVMAGAQTGTGKTAAFALPILHLLEAseevNARVQALVLTPTRELAQQVGKSFQQ 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLsGLRDVILAAPTGSGKTLAALLPALEALKR----GKGGRVLVLVPTRELAEQWAEELKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 95 YGAHTSLRTVVAYGGVSINNQLSVVKQGV-DILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFIDDIKRILRS 173
Cdd:smart00487 77 LGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518451542 174 VPETRQTLLFSATFDDAIFKLSQKLLHDPalIEVDQRNATASQVEQI 220
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
12-231 |
8.11e-55 |
|
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: 180.90 E-value: 8.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIP-AILNRQDVMAGAQTGTGKTAAFALPILH-LLEASE-----EVNARVQALVLTPTREL 84
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILErLLSQKSsngvgGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 85 AQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLG---RQAIDLSCLSFFVLDEADRMLDM 161
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQegnEHLANLKSLRFLVLDEADRMLEK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518451542 162 GFIDDIKRILRSVPET-------RQTLLFSATFDdaifklsqKLLHDPALIEVDQRNATASQVEQIAYEVDKHRKRE 231
Cdd:cd17946 161 GHFAELEKILELLNKDragkkrkRQTFVFSATLT--------LDHQLPLKLNSKKKKKKKEKKQKLELLIEKVGFRK 229
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
12-205 |
1.05e-54 |
|
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: 179.49 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALP-ILHLLeaseeVNARVQ------ALVLTPTREL 84
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPaIVHIN-----AQPPLErgdgpiVLVLAPTREL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 85 AQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFI 164
Cdd:cd17966 76 AQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518451542 165 DDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17966 156 PQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
2-207 |
2.23e-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: 171.37 E-value: 2.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 2 SFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLeasEEVNARVQALVLTPT 81
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL---EPVDGQVSVLVICHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 82 RELAQQVGKSFQQYGAH-TSLRTVVAYGGVSINNQLSVVKQGV-DILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRM- 158
Cdd:cd17950 80 RELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMl 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518451542 159 --LDMGfiDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIEV 207
Cdd:cd17950 160 eqLDMR--RDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
8-205 |
7.45e-50 |
|
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: 166.60 E-value: 7.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 8 LNPALLQAIESKGYSQPTPIQSEAIPAILN--RQDVMAGAQTGTGKTAAFALPILhlleasEEVNARV---QALVLTPTR 82
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSdpPENLIAQSQSGTGKTAAFVLAML------SRVDPTLkspQALCLAPTR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 83 ELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQgvdILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDM- 161
Cdd:cd17963 75 ELARQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKITAQ---IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTq 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518451542 162 GFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17963 152 GHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
12-205 |
7.46e-50 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 166.57 E-value: 7.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILhlLEASEEVNARVqALVLTPTRELAQQVGKS 91
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVI--IRCLTEHRNPS-ALILTPTRELAVQIEDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 92 FQQYG-AHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFIDDIKRI 170
Cdd:cd17962 78 AKELMkGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDI 157
|
170 180 190
....*....|....*....|....*....|....*
gi 518451542 171 LRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17962 158 LENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
12-205 |
3.60e-49 |
|
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: 165.20 E-value: 3.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALP-ILHLLEASEEVNARVQ----ALVLTPTRELAQ 86
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEKKLPFIKGegpyGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 87 QVGKSFQQY------GAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLD 160
Cdd:cd17951 81 QTHEVIEYYckalqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518451542 161 MGFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
3-205 |
1.04e-48 |
|
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: 164.16 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 3 FASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASeeVNArVQALVLTPTR 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTS--LKA-TQALVLAPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 83 ELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMG 162
Cdd:cd18046 78 ELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518451542 163 FIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd18046 158 FKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
12-205 |
7.13e-47 |
|
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: 159.67 E-value: 7.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESK-GYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEevnARVQ------ALVLTPTREL 84
Cdd:cd17949 1 LVSHLKSKmGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLE---PRVDrsdgtlALVLVPTREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 85 AQQVGKSFQQYGaHTSLRTVVAY--GGVSINNQLSVVKQGVDILVATPGRLID-LLGRQAIDLSCLSFFVLDEADRMLDM 161
Cdd:cd17949 78 ALQIYEVLEKLL-KPFHWIVPGYliGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDM 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518451542 162 GFIDDIKRILRSV-------------PETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17949 157 GFEKDITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
13-207 |
3.76e-46 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 157.07 E-value: 3.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 13 LQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLL--EASEEVNArVQALVLTPTRELAQQVGK 90
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyrERWTPEDG-LGALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 91 SFQQYGAHTSLRTVVAYGGVSINNQLSVVKQgVDILVATPGRLIDLLgRQAIDLSC--LSFFVLDEADRMLDMGFIDDIK 168
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHM-DETPGFDTsnLQMLVLDEADRILDMGFKETLD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 518451542 169 RILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIEV 207
Cdd:cd17941 159 AIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
4-207 |
1.03e-44 |
|
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: 154.78 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 4 ASFGLNpaLLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALP-ILHLLEAS--EEVNARVqALVLTP 80
Cdd:cd18049 29 ANFPAN--VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPaIVHINHQPflERGDGPI-CLVLAP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 81 TRELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLD 160
Cdd:cd18049 106 TRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518451542 161 MGFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIEV 207
Cdd:cd18049 186 MGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
3-205 |
4.69e-43 |
|
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: 149.15 E-value: 4.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 3 FASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEvnaRVQALVLTPTR 82
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVR---ETQALILSPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 83 ELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMG 162
Cdd:cd18045 78 ELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518451542 163 FIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd18045 158 FKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
12-207 |
1.75e-42 |
|
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: 150.16 E-value: 1.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALP-ILHLLEAS--EEVNARVqALVLTPTRELAQQV 88
Cdd:cd18050 73 VMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPaIVHINHQPylERGDGPI-CLVLAPTRELAQQV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 89 GKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFIDDIK 168
Cdd:cd18050 152 QQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIR 231
|
170 180 190
....*....|....*....|....*....|....*....
gi 518451542 169 RILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIEV 207
Cdd:cd18050 232 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
13-199 |
8.40e-42 |
|
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: 146.15 E-value: 8.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 13 LQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVNARVQA---LVLTPTRELAQQVG 89
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRApkvLVLAPTRELANQVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 90 KSFQQYGahTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFIDDIKR 169
Cdd:cd17944 82 KDFKDIT--RKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 518451542 170 ILR-----SVPETRQTLLFSATFDDAIFKLSQKLL 199
Cdd:cd17944 160 ILSvsykkDSEDNPQTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
13-186 |
1.67e-41 |
|
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: 145.20 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 13 LQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVNAR-VQALVLTPTRELAQQ---V 88
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNgTGVIIISPTRELALQiygV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 89 GKSFQQYGAHTSLrtvVAYGGVSINNQLSVVKQGVDILVATPGRLIDLL----GRQAIDLSCLsffVLDEADRMLDMGFI 164
Cdd:cd17942 82 AKELLKYHSQTFG---IVIGGANRKAEAEKLGKGVNILVATPGRLLDHLqntkGFLYKNLQCL---IIDEADRILEIGFE 155
|
170 180
....*....|....*....|..
gi 518451542 165 DDIKRILRSVPETRQTLLFSAT 186
Cdd:cd17942 156 EEMRQIIKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
12-206 |
4.12e-41 |
|
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: 143.94 E-value: 4.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASeevNARVQALVLTPTRELAQQVGKS 91
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE---RRHPQVLILAPTREIAVQIHDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 92 FQQYGAH-TSLRTVVAYGGVSINNQLSVVKqGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFIDDIKRI 170
Cdd:cd17943 78 FKKIGKKlEGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWI 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 518451542 171 LRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIE 206
Cdd:cd17943 157 FSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
12-205 |
2.47e-39 |
|
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: 140.46 E-value: 2.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQ---------DVMAGAQTGTGKTAAFALPILHLLeaSEEVNARVQALVLTPTR 82
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPIVQAL--SKRVVPRLRALIVVPTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 83 ELAQQVGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQG--------VDILVATPGRLID-LLGRQAIDLSCLSFFVLD 153
Cdd:cd17956 79 ELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDhLNSTPGFTLKHLRFLVID 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518451542 154 EADRMLDMGFID---------------------DIKRILRSVPETrQTLLFSATFDDAIFKLSQKLLHDPALI 205
Cdd:cd17956 159 EADRLLNQSFQDwletvmkalgrptapdlgsfgDANLLERSVRPL-QKLLFSATLTRDPEKLSSLKLHRPRLF 230
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
2-213 |
1.36e-38 |
|
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: 138.62 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 2 SFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNR--QDVMAGAQTGTGKTAAFALPILHLLEASEEVNarvQALVLT 79
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYP---QCLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 80 PTRELAQQVGKSFQQYGAH-TSLRTVVAYGGVSINNQLSVVKQgvdILVATPGRLIDLLGR-QAIDLSCLSFFVLDEADR 157
Cdd:cd18048 96 PTFELALQTGKVVEEMGKFcVGIQVIYAIRGNRPGKGTDIEAQ---IVIGTPGTVLDWCFKlRLIDVTNISVFVLDEADV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518451542 158 MLDM-GFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIEVDQRNAT 213
Cdd:cd18048 173 MINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
12-197 |
3.85e-38 |
|
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: 137.11 E-value: 3.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 12 LLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVNAR----VQALVLTPTRELAQQ 87
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfnaPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 88 VGKSFQQYGAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADRMLDMGFIDDI 167
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190
....*....|....*....|....*....|
gi 518451542 168 KRILRSVPetrqtllFSATFDDAIFKLSQK 197
Cdd:cd17948 161 SHFLRRFP-------LASRRSENTDGLDPG 183
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
229-337 |
1.27e-35 |
|
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: 126.56 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 229 KREITSFLIGSKNWQQVLIFTRTKKSADdlAKEMC-KDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLD 307
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLE--AELLLeKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 518451542 308 IPQLSYVINYELPHNAEDYIHRIGRTGRAG 337
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
2-206 |
6.28e-32 |
|
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: 120.21 E-value: 6.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 2 SFASFGLNPALLQAIESKGYSQPTPIQSEAIPAILNR--QDVMAGAQTGTGKTAAFALPILHLLEASEEVNarvQALVLT 79
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYP---QCLCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 80 PTRELAQQVGKSFQQYGAHTSlRTVVAYG--------GVSINNQlsvvkqgvdILVATPGRLID-LLGRQAIDLSCLSFF 150
Cdd:cd18047 79 PTYELALQTGKVIEQMGKFYP-ELKLAYAvrgnklerGQKISEQ---------IVIGTPGTVLDwCSKLKFIDPKKIKVF 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518451542 151 VLDEADRML-DMGFIDDIKRILRSVPETRQTLLFSATFDDAIFKLSQKLLHDPALIE 206
Cdd:cd18047 149 VLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
256-337 |
3.02e-29 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 108.84 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 256 DDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYVINYELPHNAEDYIHRIGRTGR 335
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 518451542 336 AG 337
Cdd:smart00490 81 AG 82
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
11-186 |
1.65e-26 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 106.69 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 11 ALLQAIESKGYSQPTPIQSEAIPAIL---------------NRQDV-MAGAQTGTGKTAAFALPILHLL---------EA 65
Cdd:cd17965 18 ILKGSNKTDEEIKPSPIQTLAIKKLLktlmrkvtkqtsneePKLEVfLLAAETGSGKTLAYLAPLLDYLkrqeqepfeEA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 66 SEEVN-----ARVQALVLTPTRELAQQVG---KSFQQYgAHTSLRTVVAYGGVSINNQLSVVKQGVDILVATPGRLIDLL 137
Cdd:cd17965 98 EEEYEsakdtGRPRSVILVPTHELVEQVYsvlKKLSHT-VKLGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518451542 138 GRQAIDLSCLSFFVLDEADRMLDMGFIDDIKRILRSVPETRQTLLFSAT 186
Cdd:cd17965 177 KSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSAT 225
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
23-315 |
4.53e-24 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 103.95 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 23 QPTPIQSEAIPAILNRQD--------VMAgaqTGTGKTAAFAlpilhllEASEEVNARVQALVLTPTRELAQQVGKSFQQ 94
Cdd:COG1061 80 ELRPYQQEALEALLAALErgggrglvVAP---TGTGKTVLAL-------ALAAELLRGKRVLVLVPRRELLEQWAEELRR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 95 YgahtsLRTVVAYGGVSinnqlsvvKQGVDILVATpgrlIDLLGRQAIDLSCLSFF---VLDEADRMLDMGFiddiKRIL 171
Cdd:COG1061 150 F-----LGDPLAGGGKK--------DSDAPITVAT----YQSLARRAHLDELGDRFglvIIDEAHHAGAPSY----RRIL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 172 RSVPETRqTLLFSAT-------------FDDAIFKLS------QKLLHDPALIEV-----DQRNATASQVEQIAYEVDKH 227
Cdd:COG1061 209 EAFPAAY-RLGLTATpfrsdgreillflFDGIVYEYSlkeaieDGYLAPPEYYGIrvdltDERAEYDALSERLREALAAD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 228 --RKREI-TSFLIGSKNWQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASR 304
Cdd:COG1061 288 aeRKDKIlRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNE 367
|
330
....*....|.
gi 518451542 305 GLDIPQLSYVI 315
Cdd:COG1061 368 GVDVPRLDVAI 378
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
7-349 |
1.73e-23 |
|
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: 102.61 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 7 GLNPALLQAIESKGYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEAseevNARVQALVLTPTRELAQ 86
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE----DPGATALYLYPTKALAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 87 -QVGKsFQQYGAHTSLR-TVVAYGGVSINNQLSVVKQGVDILVATPgrliDLLgRQAID---------LSCLSFFVLDEA 155
Cdd:COG1205 116 dQLRR-LRELAEALGLGvRVATYDGDTPPEERRWIREHPDIVLTNP----DML-HYGLLphhtrwarfFRNLRYVVIDEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 156 ---------------DRMldmgfiddiKRILRSVPETRQTLLFSATFDDAIfKLSQKLLHDPALiEVDQRNATASQVEQI 220
Cdd:COG1205 190 htyrgvfgshvanvlRRL---------RRICRHYGSDPQFILASATIGNPA-EHAERLTGRPVT-VVDEDGSPRGERTFV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 221 AYE---VDKHRKR-------EITSFLIGSKnwQQVLIFTRTKKSADDLAKeMCKDGLKtEAIHGDKSQG------ARER- 283
Cdd:COG1205 259 LWNpplVDDGIRRsalaeaaRLLADLVREG--LRTLVFTRSRRGAELLAR-YARRALR-EPDLADRVAAyragylPEERr 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518451542 284 ALE-GFKDGSIRVLVATDVASRGLDIPQLSYVINYELPHNAEDYIHRIGRTGRAGETGLAISLLSAD 349
Cdd:COG1205 335 EIErGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVAGDD 401
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
20-349 |
2.74e-19 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 89.43 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 20 GYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPilhlleaseevnARVQ---ALVLTPTRELAQ-QVgKSFQQY 95
Cdd:COG0514 14 GYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLP------------ALLLpglTLVVSPLIALMKdQV-DALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 96 GAHtslrtvVAYggvsINNQLSV---------VKQG-VDILVATPGRL-----IDLLGRQAIdlsclSFFVLDEA----- 155
Cdd:COG0514 81 GIR------AAF----LNSSLSAeerrevlraLRAGeLKLLYVAPERLlnprfLELLRRLKI-----SLFAIDEAhcisq 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 156 ---DrmldmgF------IDDIKRILRSVPetrqTLLFSATFDDAIFK-LSQKL-LHDPALIE--VDQRNatasqveqIAY 222
Cdd:COG0514 146 wghD------FrpdyrrLGELRERLPNVP----VLALTATATPRVRAdIAEQLgLEDPRVFVgsFDRPN--------LRL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 223 EV----DKHRKREITSFLIGSKNwQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVA 298
Cdd:COG0514 208 EVvpkpPDDKLAQLLDFLKEHPG-GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 518451542 299 TdVA-SRGLDIPQLSYVINYELPHNAEDYIHRIGRTGRAGETGLAISLLSAD 349
Cdd:COG0514 287 T-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
193-399 |
4.05e-19 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 89.40 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 193 KLSQKLLHDPALIEVdQRNATASQVEqiayevdkHRK----REITSFLIGSKNWQQVLIFTRTKKSADDLAKEMCKDGLK 268
Cdd:COG1111 309 KASKRLVSDPRFRKA-MRLAEEADIE--------HPKlsklREILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 269 TE------AIHGDK--SQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYVINYELPHNAEDYIHRIGRTGRAGEtG 340
Cdd:COG1111 380 AGrfvgqaSKEGDKglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKRE-G 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518451542 341 LAISLL---SADET--W-----------LLDEIHKIIDTRLMQQWLPGYEPSLEQDFAQKPKAGRGNRNKNRGRS 399
Cdd:COG1111 459 RVVVLIakgTRDEAyyWssrrkekkmksILKKLKKLLDKQEKEKLKESAQATLDEFESIKELAEDEINEKDLDEI 533
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
45-186 |
1.95e-18 |
|
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: 81.30 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 45 AQTGTGKTAAFALPILHLLEAseevnARVQALVLTPTRELAQQVGKSFQQYGAHtSLRTVVAYGGVSINNQLSVVKQGVD 124
Cdd:cd00046 8 APTGSGKTLAALLAALLLLLK-----KGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKNKLGDAD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518451542 125 ILVATPGRLIDLLGRQA-IDLSCLSFFVLDEADRMLDMGFIDDIK--RILRSVPETRQTLLFSAT 186
Cdd:cd00046 82 IIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHALLIDSRGALILdlAVRKAGLKNAQVILLSAT 146
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
10-337 |
2.37e-16 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 80.71 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 10 PALLQAIESKGYSQPTPIQSEAIPA-ILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEvnarvqALVLTPTRELAQQV 88
Cdd:COG1204 9 EKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK------ALYIVPLRALASEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 89 ----GKSFQQYGahtsLRTVVAYGGVSINNQLSVVKqgvDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADrmldmgFI 164
Cdd:COG1204 83 yrefKRDFEELG----IKVGVSTGDYDSDDEWLGRY---DILVATPEKLDSLLRNGPSWLRDVDLVVVDEAH------LI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 165 DD----------IKRILRSVPETrQTLLFSATFDDAifklsQKLLH--DPALIEVDQRnaTASQVEQIAYE-----VDKH 227
Cdd:COG1204 150 DDesrgptlevlLARLRRLNPEA-QIVALSATIGNA-----EEIAEwlDAELVKSDWR--PVPLNEGVLYDgvlrfDDGS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 228 RKREITSFLIGSK---NWQQVLIFTRTKKSADDLAKEM-------------------------CKDGLKT-----EAI-- 272
Cdd:COG1204 222 RRSKDPTLALALDlleEGGQVLVFVSSRRDAESLAKKLadelkrrltpeereeleelaeelleVSEETHTneklaDCLek 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518451542 273 -----HGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPqLSYVI------NYELPHNAEDYIHRIGRTGRAG 337
Cdd:COG1204 302 gvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIirdtkrGGMVPIPVLEFKQMAGRAGRPG 376
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
218-346 |
9.32e-16 |
|
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: 73.40 E-value: 9.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 218 EQIAYEV---DKHRKREITSFLIGSKNWQQ-VLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSI 293
Cdd:cd18794 2 PNLFYSVrpkDKKDEKLDLLKRIKVEHLGGsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 518451542 294 RVLVATDVASRGLDIPQLSYVINYELPHNAEDYIHRIGRTGRAGEtgLAISLL 346
Cdd:cd18794 82 QVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGL--PSECIL 132
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
193-351 |
8.05e-14 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 73.37 E-value: 8.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 193 KLSQKLLHDPALIEVdQRNATASQVEqiayevdkHRK----REITSFLIGSKNWQQVLIFTRTKKSADDLAKEMCKDGLK 268
Cdd:PRK13766 321 KASKRLVEDPRFRKA-VRKAKELDIE--------HPKleklREIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 269 TEAIHG----DKSQGARER----ALEGFKDGSIRVLVATDVASRGLDIPQLSYVINYELPHNAEDYIHRIGRTGRaGETG 340
Cdd:PRK13766 392 AVRFVGqaskDGDKGMSQKeqieILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGR-QEEG 470
|
170
....*....|....
gi 518451542 341 LAISLLS---ADET 351
Cdd:PRK13766 471 RVVVLIAkgtRDEA 484
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
25-190 |
1.07e-13 |
|
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: 68.83 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 25 TPIQSEAIPAILNRQD-VMAGAQTGTGKTAAFALPILHLLEASEEVnarvqALVLTPTRELAQQVGKSFQQYGAHTSLRT 103
Cdd:cd17921 3 NPIQREALRALYLSGDsVLVSAPTSSGKTLIAELAILRALATSGGK-----AVYIAPTRALVNQKEADLRERFGPLGKNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 104 VVAYGGVSINNQLsvvKQGVDILVATPGRLiDLLGRQAIDLSC--LSFFVLDEADrmldmgFIDD----------IKRIL 171
Cdd:cd17921 78 GLLTGDPSVNKLL---LAEADILVATPEKL-DLLLRNGGERLIqdVRLVVVDEAH------LIGDgergvvlellLSRLL 147
|
170
....*....|....*....
gi 518451542 172 RSVPETRQTLLfSATFDDA 190
Cdd:cd17921 148 RINKNARFVGL-SATLPNA 165
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
245-331 |
1.50e-13 |
|
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: 67.12 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 245 VLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGF-KDGSIRV-LVATDVASRGLDIPQLSYVINYELPHN 322
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnEDPDIRVfLLSTKAGGVGLNLTAANRVILYDPWWN 109
|
90
....*....|....*
gi 518451542 323 ------AEDYIHRIG 331
Cdd:cd18793 110 paveeqAIDRAHRIG 124
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
213-335 |
1.92e-12 |
|
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: 64.59 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 213 TASQVEQIAYEVDKHRKreitsfligsknwqqVLIFTRTKKSADDLA---KEMCKD---GLKTEAIHGDKSQGARERALE 286
Cdd:cd18796 24 GADAYAEVIFLLERHKS---------------TLVFTNTRSQAERLAqrlRELCPDrvpPDFIALHHGSLSRELREEVEA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 518451542 287 GFKDGSIRVLVATDVASRGLDIPQLSYVINYELPHNAEDYIHRIGRTGR 335
Cdd:cd18796 89 ALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
20-356 |
1.09e-11 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 66.28 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 20 GYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILhLLEAseevnarvQALVLTPTRELAQQVGKSFQQYG-AH 98
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL-VLDG--------LTLVVSPLISLMKDQVDQLLANGvAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 99 TSLRTVVayggvSINNQLSV---VKQG-VDILVATPGRLI--DLLGRQAiDLScLSFFVLDEA--------DRMLDMGFI 164
Cdd:PRK11057 93 ACLNSTQ-----TREQQLEVmagCRTGqIKLLYIAPERLMmdNFLEHLA-HWN-PALLAVDEAhcisqwghDFRPEYAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 165 DDIKRILRSVPetrqTLLFSATFDDA----IFKLSQklLHDPaLIEV---DQRNatasqveqIAYE-VDKHRKRE-ITSF 235
Cdd:PRK11057 166 GQLRQRFPTLP----FMALTATADDTtrqdIVRLLG--LNDP-LIQIssfDRPN--------IRYTlVEKFKPLDqLMRY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 236 LIGSKNwQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYVI 315
Cdd:PRK11057 231 VQEQRG-KSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 518451542 316 NYELPHNAEDYIHRIGRTGRAGETGLAISLLS-ADETWL---LDE 356
Cdd:PRK11057 310 HFDIPRNIESYYQETGRAGRDGLPAEAMLFYDpADMAWLrrcLEE 354
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
243-335 |
1.15e-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: 61.99 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 243 QQVLIFTRTKKSADDLAKEMCKDGLKTEAI----HGDK------SQGARERALEGFKDGSIRVLVATDVASRGLDIPQLS 312
Cdd:cd18801 31 TRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGksskgmSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVD 110
|
90 100
....*....|....*....|...
gi 518451542 313 YVINYELPHNAEDYIHRIGRTGR 335
Cdd:cd18801 111 LIICYDASPSPIRMIQRMGRTGR 133
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
203-336 |
1.41e-11 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 61.84 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 203 ALIEVDQRnATASQVEQIAYEVDKHRKREITSFLIGSKNWQQVliftrtkksaddlakemckdglkTEAIHGDKSQgarE 282
Cdd:cd18802 28 GIIFVERR-ATAVVLSRLLKEHPSTLAFIRCGFLIGRGNSSQR-----------------------KRSLMTQRKQ---K 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 518451542 283 RALEGFKDGSIRVLVATDVASRGLDIPQLSYVINYELPHNAEDYIHRIGRtGRA 336
Cdd:cd18802 81 ETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
228-338 |
1.42e-10 |
|
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: 59.19 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 228 RKREITSFLIGS-KNWQQVLIFTRTKKSADDLAKEMCKdglktEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGL 306
Cdd:cd18789 34 NKLRALEELLKRhEQGDKIIVFTDNVEALYRYAKRLLK-----PFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGI 108
|
90 100 110
....*....|....*....|....*....|....*...
gi 518451542 307 DIP------QLSYVINyelphNAEDYIHRIGRTGRAGE 338
Cdd:cd18789 109 DLPeanvaiQISGHGG-----SRRQEAQRLGRILRPKK 141
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
47-155 |
1.67e-10 |
|
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: 59.97 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 47 TGTGKT--AAFALPILHLLEASEEVNARVqALVLTPTRELAQQVGKSFQQygaHTSLRTVVAYGGVSINNQLSVVKQGV- 123
Cdd:cd18034 25 TGSGKTliAVMLIKEMGELNRKEKNPKKR-AVFLVPTVPLVAQQAEAIRS---HTDLKVGEYSGEMGVDKWTKERWKEEl 100
|
90 100 110
....*....|....*....|....*....|....*
gi 518451542 124 ---DILVATPGRLIDLLGRQAIDLSCLSFFVLDEA 155
Cdd:cd18034 101 ekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
245-333 |
4.11e-10 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 61.39 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 245 VLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERALEGFKDGS--IRVLVATDVASRGLDIPQLSYVINYELPHN 322
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLWWN 631
|
90
....*....|....*..
gi 518451542 323 ------AEDYIHRIGRT 333
Cdd:COG0553 632 paveeqAIDRAHRIGQT 648
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-155 |
6.37e-10 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 57.98 E-value: 6.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 28 QSEAIPAILNRQDVMAGAQTGTGKTAAFALPIL-HLLEASeevnaRVQALVLTPTRELAQQVGKSFQQYGAHTSLRTVVA 106
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeALLRDP-----GSRALYLYPTKALAQDQLRSLRELLEQLGLGIRVA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 518451542 107 -YGG-VSINNQLSVVKQGVDILVATPgrliDLL--------GRQAIDLSCLSFFVLDEA 155
Cdd:cd17923 80 tYDGdTPREERRAIIRNPPRILLTNP----DMLhyallphhDRWARFLRNLRYVVLDEA 134
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
242-340 |
8.27e-10 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 55.02 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 242 WQQVLIFTRTKKSADDLAKemckdglkteaihgdksqgareralegfkdgSIRVLVATDVASRGLDIPQLSYVINYELPH 321
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIAS-------------------------------SLEILVATNVLGEGIDVPSLDTVIFFDPPS 51
|
90
....*....|....*....
gi 518451542 322 NAEDYIHRIGRTGRAGETG 340
Cdd:cd18785 52 SAASYIQRVGRAGRGGKDE 70
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
21-339 |
2.34e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 56.26 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 21 YSQPTPIQSEAIPAILNRQDVMAGAQTGTGKT-AAFaLPIL-HLLEASEEVNA--RVQALVLTPTRELAQQVgksfqqyg 96
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALdELARRPRPGELpdGLRVLYISPLKALANDI-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 97 aHTSLRTVVAYGGVSINNQLSVVKQGV------------------DILVATPGRLIDLL----GRQAidLSCLSFFVLDE 154
Cdd:COG1201 93 -ERNLRAPLEEIGEAAGLPLPEIRVGVrtgdtpaserqrqrrrppHILITTPESLALLLtspdAREL--LRGVRTVIVDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 155 A-------------------DRMLDMGF-----------IDDIKRILRSVPETRQTLL----FSATFDDAIfklsqkLLH 200
Cdd:COG1201 170 IhalagskrgvhlalslerlRALAPRPLqriglsatvgpLEEVARFLVGYEDPRPVTIvdagAGKKPDLEV------LVP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 201 DPALIEVDQ-RNATASQV-EQIAYEVDKHRkreiTSfligsknwqqvLIFTRTKKSAD----DLAKEMCKDGLKTEAIHG 274
Cdd:COG1201 244 VEDLIERFPwAGHLWPHLyPRVLDLIEAHR----TT-----------LVFTNTRSQAErlfqRLNELNPEDALPIAAHHG 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518451542 275 DKSQGARERALEGFKDGSIRVLVATdvAS--RGLDIPQLSYVINYELPHNAEDYIHRIGRTG-RAGET 339
Cdd:COG1201 309 SLSREQRLEVEEALKAGELRAVVAT--SSleLGIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEV 374
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
27-154 |
6.65e-08 |
|
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: 52.74 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 27 IQSEAIPAIL-NRQDVMAGAQTGTGKTAAFALPILHLLEASEEVN-ARVQALVLTPTRELAQQVGKSFQQYGAHTSLRTV 104
Cdd:cd18023 5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPwGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCA 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 518451542 105 VAYGGVSINNQLSVvkQGVDILVATPGRLiDLLGRQAIDLSCLS----FFVLDE 154
Cdd:cd18023 85 ELTGDTEMDDTFEI--QDADIILTTPEKW-DSMTRRWRDNGNLVqlvaLVLIDE 135
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
221-350 |
1.93e-07 |
|
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: 50.77 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 221 AYEVDKHRKREITSFL--IGSKnwqqVLIFTRT---KKSADDLAKEMCKDGLKTEAIHGDksqgaRERALEGFKDGSIRV 295
Cdd:cd18798 5 VYIEDSDSLEKLLELVkkLGDG----GLIFVSIdygKEYAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEIDV 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518451542 296 LVAT----DVASRGLDIPQ-LSYVINYELPhnAEDYIHRIGRTGR--AGE--TGLAISLLSADE 350
Cdd:cd18798 76 LIGVasyyGVLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPE 137
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
244-343 |
5.69e-07 |
|
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: 48.79 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 244 QVLIFTRTKKSADDLAKEMcKDGLKTEAIHGDKSQGAR-------ERALE-GFKDGSIRVLVATDVASRGLDIPQLSYVI 315
Cdd:cd18797 37 KTIVFCRSRKLAELLLRYL-KARLVEEGPLASKVASYRagylaedRREIEaELFNGELLGVVATNALELGIDIGGLDAVV 115
|
90 100
....*....|....*....|....*...
gi 518451542 316 NYELPHNAEDYIHRIGRTGRAGETGLAI 343
Cdd:cd18797 116 LAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
201-335 |
9.40e-07 |
|
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: 48.40 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 201 DPaLIEVdqrNATASQVEQIAYEVDKHRKREitsfligsknwQQVLIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGA 280
Cdd:cd18790 1 DP-EIEV---RPTEGQVDDLLGEIRKRVARG-----------ERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLE 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 281 RERALEGFKDGSIRVLVATDVASRGLDIPQLSYVINYE-----LPHNAEDYIHRIGRTGR 335
Cdd:cd18790 66 RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSETSLIQTIGRAAR 125
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
20-186 |
2.03e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 45.22 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 20 GYSQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLleaseevnARVqALVLTPTRELAQ-QVgKSFQQYGah 98
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLL--------DGV-TLVVSPLISLMQdQV-DRLQQLG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 99 tsLRTVVAYGGVSINNQLSV----VKQGVDILVATPGRL-----IDLLGRQAiDLSCLSFFVLDEA--------DRMLDM 161
Cdd:cd17920 77 --IRAAALNSTLSPEEKREVllriKNGQYKLLYVTPERLlspdfLELLQRLP-ERKRLALIVVDEAhcvsqwghDFRPDY 153
|
170 180
....*....|....*....|....*
gi 518451542 162 GFIDDIKRILRSVPetrqTLLFSAT 186
Cdd:cd17920 154 LRLGRLRRALPGVP----ILALTAT 174
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
39-154 |
6.99e-05 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 42.96 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 39 QDVMAGAQTGTGKTAAFALPILHLLEASEEvnARVQALVLTPTRELAQQVGKSFQQYGAHTSL--RTVVAYGGVSINNQL 116
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALSSLADEPE--KGVQVLYISPLKALINDQERRLEEPLDEIDLeiPVAVRHGDTSQSEKA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 518451542 117 SVVKQGVDILVATPGRLIDLLGRQAID--LSCLSFFVLDE 154
Cdd:cd17922 80 KQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
22-157 |
7.01e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 43.58 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 22 SQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVN-ARVqaLVLTPTRELAQQVGKSFQQYGAHTS 100
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRkGKV--VFLANKVPLVEQQKEVFRKHFERPG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 518451542 101 LRTVVAYGGVSINNQLSVVKQGVDILVATPGRLI-DLLGRQAIDLSCLSFFVLDEADR 157
Cdd:cd17927 79 YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
23-189 |
8.42e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 42.66 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 23 QPTPIQSEAIPAILNRQD--------VMAgaqTGTGKTAAFALPILHLLEASEEVNarvqALVLTPTRELAQQVGKSFQQ 94
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKngqkrgliVMA---TGSGKTLTAAKLIARLFKKGPIKK----VLFLVPRKDLLEQALEEFKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 95 YGAHTSLRTVVAYGgvsiNNQLSVVKQGvDILVATPGRLIDLLGRQAIDLSCLSFFVL--DEADRmldmGFIDDIKRILR 172
Cdd:pfam04851 76 FLPNYVEIGEIISG----DKKDESVDDN-KIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHR----SGASSYRNILE 146
|
170
....*....|....*..
gi 518451542 173 SVPETRQtLLFSATFDD 189
Cdd:pfam04851 147 YFKPAFL-LGLTATPER 162
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
26-187 |
2.33e-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: 41.14 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 26 PIQSEAIPAIL--NRQD----VMAgaqTGTGKTA-AFALpILHLLEASeevnarvqALVLTPTRELAQQVGKSFQQYGAH 98
Cdd:cd17926 3 PYQEEALEAWLahKNNRrgilVLP---TGSGKTLtALAL-IAYLKELR--------TLIVVPTDALLDQWKERFEDFLGD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 99 TSLRTVvayGGVSINnqlsvVKQGVDILVATpgrlIDLLGRQAIDLSCL----SFFVLDEADRMLDMGFiddiKRILRSV 174
Cdd:cd17926 71 SSIGLI---GGGKKK-----DFDDANVVVAT----YQSLSNLAEEEKDLfdqfGLLIVDEAHHLPAKTF----SEILKEL 134
|
170
....*....|...
gi 518451542 175 PETRQtLLFSATF 187
Cdd:cd17926 135 NAKYR-LGLTATP 146
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
243-343 |
3.42e-04 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 40.61 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 243 QQVLIFTRTKKSADDLAKEMckdgLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIP-------QLSYVI 315
Cdd:cd18795 44 KPVLVFCSSRKECEKTAKDL----AGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPartviikGTQRYD 119
|
90 100 110
....*....|....*....|....*....|.
gi 518451542 316 NYEL-PHNAEDYIHRIGRTGRAG--ETGLAI 343
Cdd:cd18795 120 GKGYrELSPLEYLQMIGRAGRPGfdTRGEAI 150
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
24-158 |
5.00e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 40.86 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 24 PTPIQSEAIPAILN------RQDVMAGAQTGTGKTAAFALPILHLLEASEevnarvQALVLTPTRELAQQVGKSFQQYGA 97
Cdd:cd17918 16 LTKDQAQAIKDIEKdlhspePMDRLLSGDVGSGKTLVALGAALLAYKNGK------QVAILVPTEILAHQHYEEARKFLP 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518451542 98 HTSLRTVVAYGGVSInnqlsvvKQGVDILVATPGRLIDLLGRQAIDLSclsffVLDEADRM 158
Cdd:cd17918 90 FINVELVTGGTKAQI-------LSGISLLVGTHALLHLDVKFKNLDLV-----IVDEQHRF 138
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
141-338 |
5.78e-04 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 41.65 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 141 AIDLSCLsffVLDEADRMLD--MGFIDDIKRILRsvpETRQT-LLFSATFDDAIFKLSQKLLHDPALIEVDqRNATASQV 217
Cdd:cd09639 121 SIANSLL---IFDEVHFYDEytLALILAVLEVLK---DNDVPiLLMSATLPKFLKEYAEKIGYVEENEPLD-LKPNERAP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 218 EQIAYEVDKHRKREITSFLIGSKNWQQVLIFTRTKKSADDLAKEMCKDGLKTEA--IHGDKSQGARERA----LEGFKDG 291
Cdd:cd09639 194 FIKIESDKVGEISSLERLLEFIKKGGSVAIIVNTVDRAQEFYQQLKEKGPEEEImlIHSRFTEKDRAKKeaelLLEFKKS 273
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518451542 292 SIRVLVATDVASRGLDIpqlSYVINYELPHNAEDYIHRIGRTGRAGE 338
Cdd:cd09639 274 EKFVIVATQVIEASLDI---SVDVMITELAPIDSLIQRLGRLHRYGE 317
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
26-155 |
5.91e-04 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 40.70 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 26 PIQSEAIPAILNRQD-VMAGAQTGTGKTAAFALPILHLLeaSEEVNARvqALVLTPTRELAQQVGKSFQQYGAHTSLRTV 104
Cdd:cd18021 6 PIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAELALLRHW--RQNPKGR--AVYIAPMQELVDARYKDWRAKFGPLLGKKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 518451542 105 VAYGGvSINNQLSVVKQGvDILVATPGRLiDLLGR---QAIDLSCLSFFVLDEA 155
Cdd:cd18021 82 VKLTG-ETSTDLKLLAKS-DVILATPEQW-DVLSRrwkQRKNVQSVELFIADEL 132
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
21-85 |
7.46e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 41.80 E-value: 7.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518451542 21 YSQPTPIQSEAIPAILNRQDVMAGAQTGTGKT-AAFALPI--LHLLEASEEVNARVQALVLTPTRELA 85
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAIIdeLFRLGREGELEDKVYCLYVSPLRALN 97
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
45-173 |
1.70e-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: 39.23 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 45 AQTGTGKTAaFALpILHLLEASeeVNARVqaLVLTPTRELAQQVGKSFQQYG--AHTSLRTVVAYGGVSINNQLSVVKQ- 121
Cdd:cd17924 39 APTGVGKTT-FGL-ATSLYLAS--KGKRS--YLIFPTKSLVKQAYERLSKYAekAGVEVKILVYHSRLKKKEKEELLEKi 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 518451542 122 ---GVDILVATpgrlIDLLGRQAIDLSCLSFfvldeadrmlDMGFIDDIKRILRS 173
Cdd:cd17924 113 ekgDFDILVTT----NQFLSKNFDLLSNKKF----------DFVFVDDVDAVLKS 153
|
|
| secA |
PRK12898 |
preprotein translocase subunit SecA; Reviewed |
245-350 |
3.44e-03 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237253 [Multi-domain] Cd Length: 656 Bit Score: 39.61 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 245 VLIFTRTKKSADDLAKEMCKDGLKTEAIHGdkSQGARERALEGFKDGSIRVLVATDVASRGLDI---PQLS-----YVIN 316
Cdd:PRK12898 476 VLVGTRSVAASERLSALLREAGLPHQVLNA--KQDAEEAAIVARAGQRGRITVATNMAGRGTDIklePGVAargglHVIL 553
|
90 100 110
....*....|....*....|....*....|....*.
gi 518451542 317 YElPHNAEDyIHR--IGRTGRAGETGLAISLLSADE 350
Cdd:PRK12898 554 TE-RHDSAR-IDRqlAGRCGRQGDPGSYEAILSLED 587
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
27-157 |
3.81e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 38.26 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 27 IQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEaseEVNARVqaLVLTPTRELAQQVGKSFQQYgaHTSLRTVVA 106
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLT---KKGGKV--LILAPSRPLVEQHAENLKRV--LNIPDKITS 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 518451542 107 YGGVSINNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADR 157
Cdd:cd18035 78 LTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
40-338 |
4.68e-03 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 38.97 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 40 DVMAGAQTGTGKTAAFALPILHLLEASEEvNARVQALvltPTRELAQQVGKSFQqygAHTSLRTVVAYGGVSI------- 112
Cdd:TIGR01587 1 LLVIEAPTGYGKTEAALLWALHSIKSQKA-DRVIIAL---PTRATINAMYRRAK---ELFGSELVGLHHSSSFsrikemg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 113 ----------NNQLSVVKQGVDIL-VATPGRLIDLLGRQ---------AIDLSCLsffVLDEADRMLD--MGFIDDIKRI 170
Cdd:TIGR01587 74 dseefehlfpLYIHSNDKLFLDPItVCTIDQVLKSVFGEfghyeftlaSIANSLL---IFDEVHFYDEytLALILAVLEV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 171 LRsvpETRQT-LLFSATFDDAIFKLSQKLLHDPALIEVDQRNATASQVEQIAYEVDKHRKRE--ITSFLIGSKNWQQVLI 247
Cdd:TIGR01587 151 LK---DNDVPiLLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVGEIssLERLLEFIKKGGSIAI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 248 FTRTKKSADDLAKEMCKDGLKTEAI--HGDKSQGARERA-----LEGFKDGSIRVLVATDVASRGLDIpqlSYVINYELP 320
Cdd:TIGR01587 228 IVNTVDRAQEFYQQLKEKAPEEEIIlyHSRFTEKDRAKKeaellREMKKSNEKFVIVATQVIEASLDI---SADVMITEL 304
|
330
....*....|....*...
gi 518451542 321 HNAEDYIHRIGRTGRAGE 338
Cdd:TIGR01587 305 APIDSLIQRLGRLHRYGR 322
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
266-398 |
4.91e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 39.11 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 266 GLKTEAIHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYVINYELPHNAEDYIHRIGRTGRAGETGLAISL 345
Cdd:PLN03137 704 GHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLY 783
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 518451542 346 LSADetwllDEI---HKIIDTRLMQ-QWLPGYepsleqdfaqkpkagrgNRNKNRGR 398
Cdd:PLN03137 784 YSYS-----DYIrvkHMISQGGVEQsPMAMGY-----------------NRMASSGR 818
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
22-154 |
5.40e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 37.84 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 22 SQPTPIQSEAIPAILNRQDVMAGAQTGTGKTAAFALPILHLLEASEEVNARVQALVLTPTRELAQQVGKSFQQY------ 95
Cdd:cd18036 1 LELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQQLEKFFKYfrkgyk 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518451542 96 --GAHTSLRTVVAYGGVSINNqlsvvkqgvDILVATPGRLIDLL--GRQ--AIDLSCLSFFVLDE 154
Cdd:cd18036 81 vtGLSGDSSHKVSFGQIVKAS---------DVIICTPQILINNLlsGREeeRVYLSDFSLLIFDE 136
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
24-157 |
5.54e-03 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain] Cd Length: 163 Bit Score: 37.16 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 24 PTPIQSEAIPAILNRQD--------VMAgaqTGTGKTAAFALPILHLLEASEevNARVqaLVLTPTRELAQQVGKSFQQY 95
Cdd:cd18032 1 PRYYQQEAIEALEEAREkgqrrallVMA---TGTGKTYTAAFLIKRLLEANR--KKRI--LFLAHREELLEQAERSFKEV 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518451542 96 GAHTSLRTVvayggvsinNQLSVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEADR 157
Cdd:cd18032 74 LPDGSFGNL---------KGGKKKPDDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHH 126
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
246-309 |
6.56e-03 |
|
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: 36.38 E-value: 6.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518451542 246 LIFTRTKKSADDLAKEMCKDGLKTEAIHGDKSQGARERA---LEGFKDGSIRVLVATDVASRGLDIP 309
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIP 76
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
253-337 |
8.35e-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: 36.94 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 253 KSADDLAkEMCKDGLKTEA----IHGDKSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYVINYelphNAEDY-- 326
Cdd:cd18811 45 KAAVAMY-EYLKERFRPELnvglLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIE----DAERFgl 119
|
90
....*....|....
gi 518451542 327 --IHRI-GRTGRAG 337
Cdd:cd18811 120 sqLHQLrGRVGRGD 133
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
276-343 |
8.80e-03 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 37.61 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 276 KSQGARERALEGFKDGSIRVLVATDVASRGLDIPQLSYV--INYELPHNAEDY---------IHRI-GRTGRAGETGLAI 343
Cdd:cd18804 128 RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADSGLNSPDFraserafqlLTQVsGRAGRGDKPGKVI 207
|
|
| CMS1 |
pfam14617 |
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant ... |
77-182 |
8.88e-03 |
|
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant CMS1-like proteins. The family has similarity to the DEAD-box helicases.
Pssm-ID: 373164 Cd Length: 250 Bit Score: 37.54 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518451542 77 VLTPTRELAQQVGKSFQQYGAHTSLRTVVAYggvsinnqlsVVKQGVDILVATPGRLIDLLGRQAIDLSCLSFFVLDEAd 156
Cdd:pfam14617 140 VLRPLKKLQTKGFKVAKLFAKHIKLEEHITY----------CKASRIGIGVGTPGRIADLLENESLSVDNLKYIILDAS- 208
|
90 100
....*....|....*....|....*.
gi 518451542 157 rmldmgFIDDIKRILRSVPETRQTLL 182
Cdd:pfam14617 209 ------FRDIKNRGILDIRETRKAVI 228
|
|
| |
