|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-392 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 602.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 1 MKFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHD-SIQAIVIEPTR 79
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPrAPQALILAPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 80 ELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMG 159
Cdd:COG0513 82 ELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 160 FIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIVKIKGKELTANLIDQYFVRAKENEKFDILCRLIDVQNP 239
Cdd:COG0513 162 FIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 240 DLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIPQD 319
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489743809 320 PDSYVHRIGRTGRAGQNGMSVTFVTPNEIGYMRTIEQLTHKKMMPLKPPTDEEAFKGQLSAANKKVTELLDGD 392
Cdd:COG0513 322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGK 394
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-391 |
1.80e-139 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 408.81 E-value: 1.80e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 1 MKFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRE 80
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 81 LAIQTQEELFRLGR-DEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMG 159
Cdd:PRK11776 84 LADQVAKEIRRLARfIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 160 FIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIVKIKGKElTANLIDQYFVRAKENEKFDILCRLIDVQNP 239
Cdd:PRK11776 164 FQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH-DLPAIEQRFYEVSPDERLPALQRLLLHHQP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 240 DLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIPQD 319
Cdd:PRK11776 243 ESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARD 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489743809 320 PDSYVHRIGRTGRAGQNGMSVTFVTPNEIGYMRTIEQLTHkkmMPLKP-PTDEEAFKGQLSAANKKVTELLDG 391
Cdd:PRK11776 323 PEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLG---RKLNWePLPSLSPLSGVPLLPEMVTLCIDG 392
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-476 |
5.01e-130 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 390.75 E-value: 5.01e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 1 MKFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRE 80
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 81 LAIQTQEELFRLGRDEKArVQVV--YGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDM 158
Cdd:PRK11634 86 LAVQVAEAMTDFSKHMRG-VNVValYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 159 GFIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIVKIKGKELTANLIDQYFVRAKENEKFDILCRLIDVQN 238
Cdd:PRK11634 165 GFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 239 PDLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIPQ 318
Cdd:PRK11634 245 FDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 319 DPDSYVHRIGRTGRAGQNGMSVTFVTPNEIGYMRTIEQLTHKKMMPLKPPTDEEAFKGQLSAANKKVTELLD-GDLSKYT 397
Cdd:PRK11634 325 DSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLEKFAAKVQQQLEsSDLDQYR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 398 TEASQL-----LDDYSAVDLVAALLKNlskdAESVKVKITPEKPlPFKSKhgnsnHHFK-RNFKRGGDRNERYHRKPNAR 471
Cdd:PRK11634 405 ALLAKIqptaeGEELDLETLAAALLKM----AQGERPLILPPDA-PMRPK-----REFRdRDDRGPRDRNDRGPRGDRED 474
|
....*
gi 489743809 472 RGGRK 476
Cdd:PRK11634 475 RPRRE 479
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
2-342 |
5.77e-108 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 326.93 E-value: 5.77e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 2 KFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNL-------DKQHDSIQAIV 74
Cdd:PRK04837 9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshpapeDRKVNQPRALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 75 IEPTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADE 154
Cdd:PRK04837 89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 155 MLDMGFIQDIESILNY--ASSKHQTLLFSATMPKPILRIGEKFMHDPEIVKIKGKELTANLIDQYFVRAKENEKFDILCR 232
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRmpPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 233 LIDVQNPDLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVY 312
Cdd:PRK04837 249 LIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVF 328
|
330 340 350
....*....|....*....|....*....|
gi 489743809 313 NYDIPQDPDSYVHRIGRTGRAGQNGMSVTF 342
Cdd:PRK04837 329 NYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
1-375 |
1.36e-103 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 316.11 E-value: 1.36e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 1 MKFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLD----KQHDSIQAIVIE 76
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdfprRKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 77 PTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEML 156
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 157 DMGFIQDIESILNYASSKHQTLLFSATMP-KPILRIGEKFMHDPEIVKIKGKELTANLIDQYFVRAKENE-KFDILCRLI 234
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEhKTALLCHLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 235 DVQNPDLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNY 314
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489743809 315 DIPQDPDSYVHRIGRTGRAGQNGMSVTFVTPNEIGYMRTIEQLTHKKMMP-----LKPPTDEEAFK 375
Cdd:PRK11192 321 DMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKArvideLRPKTKAPSEK 386
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-203 |
1.41e-103 |
|
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: 307.45 E-value: 1.41e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQH----DSIQAIVIEPTRELAIQTQE 87
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 88 ELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQDIESI 167
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 489743809 168 LNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIVK 203
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-364 |
1.60e-100 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 309.05 E-value: 1.60e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 1 MKFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLD------KQHDSIQAIV 74
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLItrqphaKGRRPVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 75 IEPTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADE 154
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 155 MLDMGFIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIVKIKGKELTANLIDQYFVRAKENEKFDILCRLI 234
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 235 DVQNPDLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNY 314
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489743809 315 DIPQDPDSYVHRIGRTGRAGQNGMSVTFVTPNEIGYMRTIEQLThKKMMP 364
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL-KKEIP 369
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
2-370 |
7.06e-97 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 300.29 E-value: 7.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 2 KFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNL-------DKQHDSIQAIV 74
Cdd:PRK01297 88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtpppkERYMGEPRALI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 75 IEPTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPA-ILVGTPGRLLDHLKRGTIDISKVKTIVLDEAD 153
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARFCdILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 154 EMLDMGFIQDIESILNYASSK--HQTLLFSATMPKPILRIGEKFMHDPEIVKIKGKELTANLIDQYFVRAKENEKFDILC 231
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 232 RLIDVQNPDLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHV 311
Cdd:PRK01297 328 NLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHV 407
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 489743809 312 YNYDIPQDPDSYVHRIGRTGRAGQNGMSVTFVTPNEIGYMRTIEQLTHKKMMPLKPPTD 370
Cdd:PRK01297 408 INFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAE 466
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
3-365 |
1.94e-96 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 296.74 E-value: 1.94e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRELA 82
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 83 IQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQ 162
Cdd:PTZ00424 110 QQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 163 DIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIVKIKGKELTANLIDQYFVRA-KENEKFDILCRLIDVQNPDL 241
Cdd:PTZ00424 190 QIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETLTITQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 242 AVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIPQDPD 321
Cdd:PTZ00424 270 AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPE 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489743809 322 SYVHRIGRTGRAGQNGMSVTFVTPNEIGYMRTIEQL--THKKMMPL 365
Cdd:PTZ00424 350 NYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHynTQIEEMPM 395
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-371 |
1.76e-94 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 297.25 E-value: 1.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 1 MKFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNL-------DKQHDSIQAI 73
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 74 VIEPTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKR-GTIDISKVKTIVLDEA 152
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 153 DEMLDMGFIQDIESILNYASSK--HQTLLFSATMPKPILRIGEKFMHDPEIVKIKGKELTANLIDQYFVRAKENEKFDIL 230
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 231 CRLIDVQNPDLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSH 310
Cdd:PRK04537 249 LGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489743809 311 VYNYDIPQDPDSYVHRIGRTGRAGQNGMSVTFVTPNEIGYMRTIEQLTHKKmMPLKPPTDE 371
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQK-IPVEPVTAE 388
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
2-347 |
1.65e-91 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 288.60 E-value: 1.65e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 2 KFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQH-----DSIQAIVIE 76
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPllrygDGPIVLVLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 77 PTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEML 156
Cdd:PTZ00110 211 PTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRML 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 157 DMGFIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFM-HDPEIVKIKGKELTA-NLIDQYFVRAKENEK---FDILC 231
Cdd:PTZ00110 291 DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDLTAcHNIKQEVFVVEEHEKrgkLKMLL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 232 RLIDVQNPDLaVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHV 311
Cdd:PTZ00110 371 QRIMRDGDKI-LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYV 449
|
330 340 350
....*....|....*....|....*....|....*.
gi 489743809 312 YNYDIPQDPDSYVHRIGRTGRAGQNGMSVTFVTPNE 347
Cdd:PTZ00110 450 INFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK 485
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
3-198 |
5.13e-72 |
|
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: 227.37 E-value: 5.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSI----------QA 72
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 73 IVIEPTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEA 152
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489743809 153 DEMLDMGFIQDIESILNYASS----KHQTLLFSATMPKPILRIGEKFMHD 198
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHPDMppkgERQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
5-204 |
1.11e-67 |
|
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: 215.65 E-value: 1.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 5 EMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRELAIQ 84
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 85 TQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQDI 164
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489743809 165 ESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPeiVKI 204
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDP--VRI 198
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
3-201 |
5.23e-67 |
|
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: 213.70 E-value: 5.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRELA 82
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 83 IQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQ 162
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489743809 163 DIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDP-EI 201
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPyEI 200
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
25-191 |
6.97e-66 |
|
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: 209.41 E-value: 6.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 25 TPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRELAIQTQEELFRLGRDEKARVQVVY 104
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 105 GGADIRRQIRALKqTPAILVGTPGRLLDHLKRgTIDISKVKTIVLDEADEMLDMGFIQDIESILNYASSKHQTLLFSATM 184
Cdd:pfam00270 81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 489743809 185 PKPILRI 191
Cdd:pfam00270 159 PRNLEDL 165
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
3-199 |
1.06e-64 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 207.85 E-value: 1.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRELA 82
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 83 IQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLK---RGTIDISKVKTIVLDEADEMLDMG 159
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489743809 160 FIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDP 199
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
3-205 |
1.16e-64 |
|
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: 207.94 E-value: 1.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRELA 82
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 83 IQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGT-IDISKVKTIVLDEADEMLDMGFI 161
Cdd:cd17954 82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLNMDFE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489743809 162 QDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPeiVKIK 205
Cdd:cd17954 162 PEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP--VKIE 203
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
1-343 |
5.71e-64 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 215.81 E-value: 5.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 1 MKFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPIL--------QNLDKQHDSIqA 72
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsrcctirsGHPSEQRNPL-A 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 73 IVIEPTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEA 152
Cdd:PLN00206 200 MVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 153 DEMLDMGFIQDIESILNyASSKHQTLLFSATMPKPILRIGEKFMHDPEIVKIKGKELTANLIDQY--FVRAKENEK--FD 228
Cdd:PLN00206 280 DCMLERGFRDQVMQIFQ-ALSQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLaiWVETKQKKQklFD 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 229 ILCRLIDVQNPdlAVIFGRTKRRVDELTRGLQ-ARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISG 307
Cdd:PLN00206 359 ILKSKQHFKPP--AVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
|
330 340 350
....*....|....*....|....*....|....*.
gi 489743809 308 VSHVYNYDIPQDPDSYVHRIGRTGRAGQNGMSVTFV 343
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-197 |
1.77e-63 |
|
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: 206.74 E-value: 1.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 1 MKFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDK------QHDSIQ--- 71
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKegltasSFSEVQepq 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 72 AIVIEPTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDE 151
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489743809 152 ADEMLDMGFIQDIESILNYASS----KHQTLLFSATMPKPILRIGEKFMH 197
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEPGMpskeDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
12-184 |
2.44e-63 |
|
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: 204.03 E-value: 2.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNL---DKQHDSIQAIVIEPTRELAIQTQEE 88
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 89 LFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRG-TIDISKVKTIVLDEADEMLDMGFIQDIESI 167
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170
....*....|....*..
gi 489743809 168 LNYASSKHQTLLFSATM 184
Cdd:cd17947 161 LRLCPRTRQTMLFSATM 177
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
8-191 |
4.62e-62 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 201.27 E-value: 4.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 8 LKPEILKAIKRSGFEEATPIQEKTIPLVLE-GKDVIGQAQTGTGKTAAFGLPILQNLDKQHDS-----IQAIVIEPTREL 81
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAgrrsgVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 82 AIQTQEELFRL-GRDEKARVQVVYGGADIRRQIRAL-KQTPAILVGTPGRLLDHLK--RGTIDISKVKTIVLDEADEMLD 157
Cdd:cd17964 81 ALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 489743809 158 MGFIQDIESIL----NYASSKHQTLLFSATMPKPILRI 191
Cdd:cd17964 161 MGFRPDLEQILrhlpEKNADPRQTLLFSATVPDEVQQI 198
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
3-203 |
4.68e-61 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 198.68 E-value: 4.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLdKQHDS---IQAIVIEPTR 79
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL-KAHSPtvgARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 80 ELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMG 159
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489743809 160 FIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIVK 203
Cdd:cd17959 162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
214-343 |
1.89e-60 |
|
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: 194.26 E-value: 1.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 214 IDQYFVRAKENEKFDIL-CRLIDVQNPDLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDI 292
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489743809 293 LVATDVAARGLDISGVSHVYNYDIPQDPDSYVHRIGRTGRAGQNGMSVTFV 343
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
3-199 |
3.21e-59 |
|
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: 193.43 E-value: 3.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRELA 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 83 IQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQ 162
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 489743809 163 DIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDP 199
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
3-200 |
1.05e-56 |
|
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: 187.17 E-value: 1.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRELA 82
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 83 IQTQEELFRLGRDEK-ARVQVVYGGADIRRQIRALK-QTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEM---LD 157
Cdd:cd17950 84 FQISNEYERFSKYMPnVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleqLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489743809 158 MGfiQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPE 200
Cdd:cd17950 164 MR--RDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPL 204
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
8-204 |
2.41e-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: 186.25 E-value: 2.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 8 LKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNL------DKQHDSIQAIVIEPTREL 81
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 82 AIQTQEELFRL--GRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTI-DISKVKTIVLDEADEMLDM 158
Cdd:cd17961 81 AQQVSKVLEQLtaYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489743809 159 GFIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIVKI 204
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-199 |
4.14e-56 |
|
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: 4.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDS--IQAIVIEPTRELAIQTQEEL 89
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 90 FRLGRDEKARVQVVYGG-ADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQDIESIL 168
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
|
170 180 190
....*....|....*....|....*....|..
gi 489743809 169 NYASSKH-QTLLFSATMPKPILRIGEKFMHDP 199
Cdd:cd17957 161 AACTNPNlQRSLFSATIPSEVEELARSVMKDP 192
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
16-217 |
5.58e-56 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 185.00 E-value: 5.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 16 IKRSGFEEATPIQEKTIPLVLEG-KDVIGQAQTGTGKTAAFGLPILQNLDKqHDSIQAIVIEPTRELAIQTQEELFRLGR 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 95 DEKARVQVVYGGADIRRQIRALKQTPA-ILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQDIESILNYASS 173
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGKTdILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489743809 174 KHQTLLFSATMPKPILRIGEKFMHDPeiVKIKGKELTANLIDQY 217
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
12-202 |
1.22e-55 |
|
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: 184.83 E-value: 1.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPIL--------QNLDKQHDSIQAIVIEPTRELAI 83
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLvyisrlppLDEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 84 QTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQD 163
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489743809 164 IESIL-----------------NYASSKH---QTLLFSATMPKPILRIGEKFMHDPEIV 202
Cdd:cd17945 161 VTKILdampvsnkkpdteeaekLAASGKHryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
12-199 |
2.55e-55 |
|
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: 183.34 E-value: 2.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPIL-----QNLDKQHDSIQAIVIEPTRELAIQTQ 86
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 87 EELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQDIES 166
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|...
gi 489743809 167 ILNYASSKHQTLLFSATMPKPILRIGEKFMHDP 199
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDY 193
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
12-202 |
2.42e-54 |
|
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: 180.56 E-value: 2.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQH----DSIQAIVIEPTRELAIQTQE 87
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERwtpeDGLGALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 88 ELFRLGRDEKARVQVVYGGADIRRQIRALKQTpAILVGTPGRLLDHLKRG-TIDISKVKTIVLDEADEMLDMGFIQDIES 166
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 489743809 167 ILNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIV 202
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
12-199 |
2.52e-54 |
|
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: 180.69 E-value: 2.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPIL------QNLDKQHDSIqAIVIEPTRELAIQT 85
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvhimdqRELEKGEGPI-AVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 86 QEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQDIE 165
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....
gi 489743809 166 SILNYASSKHQTLLFSATMPKPILRIGEKFMHDP 199
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDP 193
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
2-198 |
2.39e-52 |
|
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: 177.15 E-value: 2.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 2 KFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNL------------------ 63
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgeslpsesgyygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 64 DKQHdsIQAIVIEPTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISK 143
Cdd:cd18051 102 RKQY--PLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDY 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489743809 144 VKTIVLDEADEMLDMGFIQDIESILNY----ASSKHQTLLFSATMPKPILRIGEKFMHD 198
Cdd:cd18051 180 CKYLVLDEADRMLDMGFEPQIRRIVEQdtmpPTGERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
8-203 |
3.49e-52 |
|
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: 175.07 E-value: 3.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 8 LKPEILKAIKRSGFEEATPIQEKTIPLVLEG--KDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRELAIQT 85
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 86 QEELFRLGRDEKARVQVVYGGADIRRQIRALKQtpaILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDM-GFIQDI 164
Cdd:cd17963 81 GEVVEKMGKFTGVKVALAVPGNDVPRGKKITAQ---IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQS 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 489743809 165 ESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIVK 203
Cdd:cd17963 158 IRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
3-199 |
1.69e-51 |
|
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: 173.42 E-value: 1.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRELA 82
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 83 IQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQ 162
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 489743809 163 DIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDP 199
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDP 197
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
12-186 |
1.21e-50 |
|
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: 171.22 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDS-----IQAIVIEPTRELAIQTQ 86
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANlkkgqVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 87 EELFRL--GRDEKARVQVVYGGADIRRQIRALKQT-PAILVGTPGRLLDHLKRGTiDISKVKT---IVLDEADEMLDMGF 160
Cdd:cd17960 81 EVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSRKA-DKVKVKSlevLVLDEADRLLDLGF 159
|
170 180
....*....|....*....|....*.
gi 489743809 161 IQDIESILNYASSKHQTLLFSATMPK 186
Cdd:cd17960 160 EADLNRILSKLPKQRRTGLFSATQTD 185
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
3-202 |
4.37e-50 |
|
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: 169.81 E-value: 4.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQnldkqhdSIQAIVIEPTRELA 82
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-------IVVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 83 IQTQEELFRLGR---DEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMG 159
Cdd:cd17938 74 EQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489743809 160 FIQDIESILN------YASSKHQTLLFSATMPKP-ILRIGEKFMHDPEIV 202
Cdd:cd17938 154 NLETINRIYNripkitSDGKRLQVIVCSATLHSFeVKKLADKIMHFPTWV 203
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
2-199 |
3.03e-49 |
|
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: 168.32 E-value: 3.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 2 KFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQH-----DSIQAIVIE 76
Cdd:cd17953 13 KWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRpvkpgEGPIGLIMA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 77 PTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHL--KRGTI-DISKVKTIVLDEAD 153
Cdd:cd17953 93 PTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVtNLRRVTYVVLDEAD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489743809 154 EMLDMGFIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDP 199
Cdd:cd17953 173 RMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
12-203 |
1.49e-48 |
|
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: 165.51 E-value: 1.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRELAIQTQEELFR 91
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 92 LG-RDEKARVQVVYGGADIRRQIRALKQtPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQDIESILNY 170
Cdd:cd17943 81 IGkKLEGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|...
gi 489743809 171 ASSKHQTLLFSATMPKPILRIGEKFMHDPEIVK 203
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
16-199 |
2.61e-48 |
|
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: 164.64 E-value: 2.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 16 IKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRELAIQTQEELFRLGRD 95
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 96 E-KARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQDIESILNYASSK 174
Cdd:cd17962 85 LpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHD 164
|
170 180
....*....|....*....|....*
gi 489743809 175 HQTLLFSATMPKPILRIGEKFMHDP 199
Cdd:cd17962 165 HQTILVSATIPRGIEQLAGQLLQNP 189
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
17-203 |
1.54e-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: 163.53 E-value: 1.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 17 KRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQ------AIVIEPTRELAIQTQEELF 90
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 91 RLGR-----------------DEKARvqvvyggadIRRQIralkqtpAILVGTPGRLLDHLKRGT-IDISKVKTIVLDEA 152
Cdd:cd17949 87 KLLKpfhwivpgyliggekrkSEKAR---------LRKGV-------NILIATPGRLLDHLKNTQsFDVSNLRWLVLDEA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489743809 153 DEMLDMGFIQDIESILNY-------------ASSKHQTLLFSATMPKPILRIGEKFMHDPEIVK 203
Cdd:cd17949 151 DRLLDMGFEKDITKILELlddkrskaggeksKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
1-198 |
8.78e-47 |
|
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: 162.10 E-value: 8.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 1 MKFSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQ-----HDSIQAIVI 75
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQpflerGDGPICLVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 76 EPTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEM 155
Cdd:cd18049 104 APTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489743809 156 LDMGFIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHD 198
Cdd:cd18049 184 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
12-184 |
3.40e-46 |
|
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: 160.48 E-value: 3.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPL-VLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDS---------IQAIVIEPTREL 81
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSngvggkqkpLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 82 AIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLD-------HLKRgtidISKVKTIVLDEADE 154
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWEliqegneHLAN----LKSLRFLVLDEADR 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 489743809 155 MLDMGFIQDIESILN-------YASSKHQTLLFSATM 184
Cdd:cd17946 157 MLEKGHFAELEKILEllnkdraGKKRKRQTFVFSATL 193
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
13-196 |
2.33e-45 |
|
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: 157.32 E-value: 2.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 13 LKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSI------QAIVIEPTRELAIQTQ 86
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 87 EELFRLGRdeKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQDIES 166
Cdd:cd17944 82 KDFKDITR--KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 489743809 167 ILNYASSKH-----QTLLFSATMPKPILRIGEKFM 196
Cdd:cd17944 160 ILSVSYKKDsednpQTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
12-202 |
7.83e-45 |
|
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: 155.70 E-value: 7.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQ------HDSIQAIVIEPTRELAIQT 85
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQpipreqRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 86 QEELFRLGRdEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQDIE 165
Cdd:cd17958 81 EAECSKYSY-KGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 489743809 166 SILNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIV 202
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
12-202 |
8.41e-45 |
|
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: 155.96 E-value: 8.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLP-ILQNLDK-------QHDSIQAIVIEPTRELAI 83
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQekklpfiKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 84 QTQE------ELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLD 157
Cdd:cd17951 81 QTHEvieyycKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489743809 158 MGFIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIV 202
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
3-198 |
2.98e-43 |
|
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: 154.01 E-value: 2.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQ-----HDSIQAIVIEP 77
Cdd:cd18050 64 FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQpylerGDGPICLVLAP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 78 TRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLD 157
Cdd:cd18050 144 TRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLD 223
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489743809 158 MGFIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHD 198
Cdd:cd18050 224 MGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
12-183 |
7.65e-43 |
|
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: 150.59 E-value: 7.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDK----QHDSIQAIVIEPTRELAIQTQE 87
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKlkfkPRNGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 88 ELFRLGRDEKARVQVVYGGADIRRQIRALKQTPAILVGTPGRLLDHLKRGTIDISK-VKTIVLDEADEMLDMGFIQDIES 166
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGFEEEMRQ 160
|
170
....*....|....*..
gi 489743809 167 ILNYASSKHQTLLFSAT 183
Cdd:cd17942 161 IIKLLPKRRQTMLFSAT 177
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
225-334 |
9.70e-37 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 131.18 E-value: 9.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 225 EKFDILCRLIDVQNPDLAVIFGRTKRRVDE--LtrgLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARG 302
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAelL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 489743809 303 LDISGVSHVYNYDIPQDPDSYVHRIGRTGRAG 334
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
3-210 |
4.18e-36 |
|
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: 133.61 E-value: 4.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEG--KDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRE 80
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 81 LAIQTQEELFRLGRdEKARVQVVYGgadIR--RQIRALKQTPAILVGTPGRLLDH-LKRGTIDISKVKTIVLDEADEMLD 157
Cdd:cd18048 100 LALQTGKVVEEMGK-FCVGIQVIYA---IRgnRPGKGTDIEAQIVIGTPGTVLDWcFKLRLIDVTNISVFVLDEADVMIN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489743809 158 M-GFIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMHDPEIVKIKGKELT 210
Cdd:cd18048 176 VqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
3-203 |
3.62e-31 |
|
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: 119.44 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAIKRSGFEEATPIQEKTIPLVLEG--KDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIVIEPTRE 80
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 81 LAIQTQEELFRLGRdEKARVQVVYG--GADIRRQIRALKQtpaILVGTPGRLLDH-LKRGTIDISKVKTIVLDEADEMLD 157
Cdd:cd18047 83 LALQTGKVIEQMGK-FYPELKLAYAvrGNKLERGQKISEQ---IVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489743809 158 MGFIQD----IESILNYASskhQTLLFSATMPKPILRIGEKFMHDPEIVK 203
Cdd:cd18047 159 TQGHQDqsirIQRMLPRNC---QMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
253-334 |
8.11e-31 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 114.23 E-value: 8.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 253 DELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIPQDPDSYVHRIGRTGR 332
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 489743809 333 AG 334
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
12-184 |
1.03e-30 |
|
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: 118.89 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEG---------KDVIGQAQTGTGKTAAFGLPILQNL-DKQHDSIQAIVIEPTREL 81
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 82 AIQTQEELFRLGRDEKARVQVVYGGADIRRQIRALKQTPA--------ILVGTPGRLLDHLKRGT-IDISKVKTIVLDEA 152
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTPgFTLKHLRFLVIDEA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489743809 153 DEMLDMGFiQDIESILNYA--------------------SSKH-QTLLFSATM 184
Cdd:cd17956 161 DRLLNQSF-QDWLETVMKAlgrptapdlgsfgdanllerSVRPlQKLLFSATL 212
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
12-220 |
2.18e-28 |
|
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: 112.46 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 12 ILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNL-------DKQHDSIQAIVIEPTRELAIQ 84
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 85 TQEELFRLGRDEKARVQVVYGGaDIRRQIRALKQ-TPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQD 163
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGG-RTKRQIRNPHFeEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489743809 164 IESILNYA-------------SSKHQTLLFSATMPKPILRIGEKFMHDPEIVKIKGKELTANL--IDQYFVR 220
Cdd:cd17948 160 LSHFLRRFplasrrsentdglDPGTQLVLVSATMPSGVGEVLSKVIDVDSIETVTSDKLHRLMphVKQKFLR 231
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
38-183 |
5.43e-22 |
|
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: 92.08 E-value: 5.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 38 GKDVIGQAQTGTGKTAAFGLPILQNLDKQHDsiQAIVIEPTRELAIQTQEELFRLgRDEKARVQVVYGGADIRRQIRALK 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGK--KVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489743809 118 QTPAILVGTPGRLLDHLKR-GTIDISKVKTIVLDEADEMLDMGF--IQDIESILNYASSKHQTLLFSAT 183
Cdd:cd00046 78 GDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRgaLILDLAVRKAGLKNAQVILLSAT 146
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
20-373 |
9.11e-19 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 88.66 E-value: 9.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 20 GFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLP--ILQNLdkqhdsiqAIVIEPTreLA-IQTQ-EELFRLG-- 93
Cdd:COG0514 14 GYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLLPGL--------TLVVSPL--IAlMKDQvDALRAAGir 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 94 ---------RDEKARVQvvyggADIRR-QIRALkqtpaiLVgTPGRL-----LDHLKRGTIDIskvktIVLDEA------ 152
Cdd:COG0514 84 aaflnsslsAEERREVL-----RALRAgELKLL------YV-APERLlnprfLELLRRLKISL-----FAIDEAhcisqw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 153 --D---EMLDMG-FIQDIESIlnyasskhQTLLFSATMPKPILR-IGEKF-MHDPEIVKikgkelT----ANLidQYFVR 220
Cdd:COG0514 147 ghDfrpDYRRLGeLRERLPNV--------PVLALTATATPRVRAdIAEQLgLEDPRVFV------GsfdrPNL--RLEVV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 221 AK-ENEKFDILCRLIDVQNPDLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATdVA 299
Cdd:COG0514 211 PKpPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IA 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489743809 300 -ARGLDISGVSHVYNYDIPQDPDSYVHRIGRTGRAGQNGMSVTFVTPNEIGymrtieqlTHKKMMPLKPPTDEEA 373
Cdd:COG0514 290 fGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVA--------IQRFFIEQSPPDEERK 356
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
3-204 |
1.01e-17 |
|
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: 82.42 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 3 FSEMNLKPEILKAI---------KRSGFEEATPIQEKTIPLVL----------EGKDVIGQ------AQTGTGKTAAFGL 57
Cdd:cd17965 1 FDQLKLLPSVREAIikeilkgsnKTDEEIKPSPIQTLAIKKLLktlmrkvtkqTSNEEPKLevfllaAETGSGKTLAYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 58 PILQNLDKQ-----------------HDSIQAIVIEPTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRQ--IRALKQ 118
Cdd:cd17965 81 PLLDYLKRQeqepfeeaeeeyesakdTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQrlQLAFKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 119 TPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEMLDMGFIQDIESILNYASSKHQTLLFSATMPKPILRIGEKFMhd 198
Cdd:cd17965 161 RIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLF-- 238
|
....*.
gi 489743809 199 PEIVKI 204
Cdd:cd17965 239 PDVVRI 244
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
217-335 |
6.91e-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: 74.17 E-value: 6.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 217 YFVRAKENEKFDILCRLIDVQNP--DLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILV 294
Cdd:cd18794 6 YSVRPKDKKDEKLDLLKRIKVEHlgGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIV 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489743809 295 ATDVAARGLDISGVSHVYNYDIPQDPDSYVHRIGRTGRAGQ 335
Cdd:cd18794 86 ATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGL 126
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
7-341 |
1.38e-15 |
|
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: 79.49 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 7 NLKPEILKAIKRSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLdKQHDSIQAIVIEPTRELAiQTQ 86
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPTKALA-RDQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 87 -EELFRLGRDEKARVQV-VYGG---ADIRRQIRAlkqTPAILVGTP-----GRLLDHLKRGTIdISKVKTIVLDEADE-- 154
Cdd:COG1205 118 lRRLRELAEALGLGVRVaTYDGdtpPEERRWIRE---HPDIVLTNPdmlhyGLLPHHTRWARF-FRNLRYVVIDEAHTyr 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 155 --------MLdmgfIQDIESILNYASSKHQTLLFSATMPKPilrigekfmhdpeivkikgKELTANLIDQYFV------- 219
Cdd:COG1205 194 gvfgshvaNV----LRRLRRICRHYGSDPQFILASATIGNP-------------------AEHAERLTGRPVTvvdedgs 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 220 --------------------RAKENEKFDILCRLI--DVQnpdlAVIFGRTKRRVDELTRGLQAR------GYNAAGIHG 271
Cdd:COG1205 251 prgertfvlwnpplvddgirRSALAEAARLLADLVreGLR----TLVFTRSRRGAELLARYARRAlrepdlADRVAAYRA 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 272 DLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIPQDPDSYVHRIGRTGRAGQNGMSVT 341
Cdd:COG1205 327 GYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
223-435 |
9.51e-14 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 73.61 E-value: 9.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 223 ENEKFDILCRLIDVQ---NPD-LAVIFGRTKRRVDELTRGLQARGYNA------AGIHGD--LSQAKRMSVLKRFRKGKL 290
Cdd:COG1111 333 EHPKLSKLREILKEQlgtNPDsRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEF 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 291 DILVATDVAARGLDISGVSHVYNYD-IPqdpdS---YVHRIGRTGRAGQnGMSVTFVTPN---EIGYMRTI--EQLTHKK 361
Cdd:COG1111 413 NVLVATSVAEEGLDIPEVDLVIFYEpVP----SeirSIQRKGRTGRKRE-GRVVVLIAKGtrdEAYYWSSRrkEKKMKSI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489743809 362 MMPLKPPTDEEAFKGQLSAANKKVTELLDGDLSKYTTEASQLLDDYSAVDLVAALLKNLSKDAESVKVKITPEK 435
Cdd:COG1111 488 LKKLKKLLDKQEKEKLKESAQATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVIVSTLAESL 561
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
47-343 |
2.89e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 71.98 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 47 TGTGKTAAFGLPILQNLDKQHdsiqAIVIEPTRELAIQTQEELfrlgrdekARVQVVYGGADIRRQIRAlkqtpAILVGT 126
Cdd:COG1061 109 TGTGKTVLALALAAELLRGKR----VLVLVPRRELLEQWAEEL--------RRFLGDPLAGGGKKDSDA-----PITVAT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 127 PGRLLDHLKRGTIDiSKVKTIVLDEADEMLDMGFIQdiesILNYASSKHqTLLFSAT------MPKPILR---------- 190
Cdd:COG1061 172 YQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRR----ILEAFPAAY-RLGLTATpfrsdgREILLFLfdgivyeysl 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 191 ---IGEKFMHDPEIVKIKG---------KELTANLIDQYfvRAKENEKFDILCRLIDvQNPDL--AVIFGRTKRRVDELT 256
Cdd:COG1061 246 keaIEDGYLAPPEYYGIRVdltderaeyDALSERLREAL--AADAERKDKILRELLR-EHPDDrkTLVFCSSVDHAEALA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 257 RGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIPQDPDSYVHRIGRTGRAGQN 336
Cdd:COG1061 323 ELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPG 402
|
....*..
gi 489743809 337 GMSVTFV 343
Cdd:COG1061 403 KEDALVY 409
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
225-352 |
4.34e-13 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 71.28 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 225 EKF---DILCRLIDVQNPDLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAAR 301
Cdd:PRK11057 219 EKFkplDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGM 298
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489743809 302 GLDISGVSHVYNYDIPQDPDSYVHRIGRTGRAGQNGMSVTFVTPNEIGYMR 352
Cdd:PRK11057 299 GINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLR 349
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
226-328 |
5.05e-11 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 60.18 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 226 KFDILCRLID--VQNPDLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGK--LDILVATDVAAR 301
Cdd:cd18793 12 KLEALLELLEelREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|....
gi 489743809 302 GLDISGVSHVYNYDIPQDPdSY-------VHRIG 328
Cdd:cd18793 92 GLNLTAANRVILYDPWWNP-AVeeqaidrAHRIG 124
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1-304 |
6.06e-11 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 64.91 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 1 MKFSEMNLKPEiLKAIKRSGFEEATPIQEKTIPL-VLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQAIViePTR 79
Cdd:COG1202 188 VPVDDLDLPPE-LKDLLEGRGEELLPVQSLAVENgLLEGKDQLVVSATATGKTLIGELAGIKNALEGKGKMLFLV--PLV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 80 ELAIQTQEElFRLGRDEKARVQVVYGGADIRrqIRALKQTP--AILVGT-PGrlLDHLKRGTIDISKVKTIVLDEAdEML 156
Cdd:COG1202 265 ALANQKYED-FKDRYGDGLDVSIRVGASRIR--DDGTRFDPnaDIIVGTyEG--IDHALRTGRDLGDIGTVVIDEV-HML 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 157 DM--------GFIqdieSILNYASSKHQTLLFSATmpkpilrIGekfmhDPEIVkikGKELTANL---------IDQYFV 219
Cdd:COG1202 339 EDperghrldGLI----ARLKYYCPGAQWIYLSAT-------VG-----NPEEL---AKKLGAKLveyeerpvpLERHLT 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 220 RAKENEKFDILCRLIDV------------QnpdlAVIFGRTKRRVDELTRGLqarGYNAAGIHGDLSQAKRMSVLKRFRK 287
Cdd:COG1202 400 FADGREKIRIINKLVKRefdtksskgyrgQ----TIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFAD 472
|
330
....*....|....*..
gi 489743809 288 GKLDILVATDVAARGLD 304
Cdd:COG1202 473 QELAAVVTTAALAAGVD 489
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
272-343 |
2.51e-10 |
|
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: 58.37 E-value: 2.51e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489743809 272 DLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIPQDPDSYVHRIGRtGRAgQNGMSVTFV 343
Cdd:cd18802 73 LMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA-PNSKYILMV 142
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
38-157 |
3.69e-10 |
|
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: 58.75 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 38 GKDVIGQAQTGTGKTAAFGLPILQNLDKQH-DSIQAIVIEPTRELAIQTQEELFRLGRDEKA--RVQVVYGGADIRRQIR 114
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPeKGVQVLYISPLKALINDQERRLEEPLDEIDLeiPVAVRHGDTSQSEKAK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489743809 115 ALKQTPAILVGTP---GRLLDHlKRGTIDISKVKTIVLDEADEMLD 157
Cdd:cd17922 81 QLKNPPGILITTPeslELLLVN-KKLRELFAGLRYVVVDEIHALLG 125
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
226-335 |
3.88e-10 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 62.16 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 226 KFDILCRLID--VQNPDLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGK--LDILVATDVAAR 301
Cdd:COG0553 534 KLEALLELLEelLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGE 613
|
90 100 110
....*....|....*....|....*....|....
gi 489743809 302 GLDISGVSHVYNYDIPQDPDSYVHRIGRTGRAGQ 335
Cdd:COG0553 614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQ 647
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-152 |
4.96e-10 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 58.75 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 28 QEKTIPLVLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSiQAIVIEPTRELAiQTQEELFR---LGRDEKARVQVVY 104
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGS-RALYLYPTKALA-QDQLRSLRellEQLGLGIRVATYD 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489743809 105 GGADIRRQIRALKQTPAILVGTPgRLLDH--LKRGTIDI---SKVKTIVLDEA 152
Cdd:cd17923 83 GDTPREERRAIIRNPPRILLTNP-DMLHYalLPHHDRWArflRNLRYVVLDEA 134
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
260-332 |
9.92e-10 |
|
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: 56.98 E-value: 9.92e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489743809 260 QARGYNAAGihgdLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIPQDPDSYVHRIGRTGR 332
Cdd:cd18801 65 QASGKSSKG----MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
25-187 |
2.45e-09 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 56.50 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 25 TPIQEKTI-PLVLEGKDVIGQAQTGTGKTAAFGLPILQNLdKQHDSIqAIVIEPTRELAIQTQEELFRLGRDEKARVQVV 103
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRAL-ATSGGK-AVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 104 YGGADIRRQiraLKQTPAILVGTPGRLLDHLKRGTID-ISKVKTIVLDEAdEMLDMG----FIQDIESILNYASSKHQTL 178
Cdd:cd17921 81 TGDPSVNKL---LLAEADILVATPEKLDLLLRNGGERlIQDVRLVVVDEA-HLIGDGergvVLELLLSRLLRINKNARFV 156
|
....*....
gi 489743809 179 LFSATMPKP 187
Cdd:cd17921 157 GLSATLPNA 165
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
18-331 |
3.45e-08 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 56.05 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 18 RSGFEEATPIQEKTIPLVLEGKDVIGQAQTGTGKT-AAFgLPILQNL------DKQHDSIQAIVIEPTRELA-------I 83
Cdd:PRK13767 27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF-LAIIDELfrlgreGELEDKVYCLYVSPLRALNndihrnlE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 84 QTQEELFRLGRDEKARVQvvyggaDIRRQIRA-----------LKQTPAILVGTPGRLLDHL------KRgtidISKVKT 146
Cdd:PRK13767 106 EPLTEIREIAKERGEELP------EIRVAIRTgdtssyekqkmLKKPPHILITTPESLAILLnspkfrEK----LRTVKW 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 147 IVLDEADEMldmgfiqdiesilnyASSK---HQTL---LFSATMPKPILRIGEKFMHDP--EIVKI------KGKELTAN 212
Cdd:PRK13767 176 VIVDEIHSL---------------AENKrgvHLSLsleRLEELAGGEFVRIGLSATIEPleEVAKFlvgyedDGEPRDCE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 213 LIDQYFVRakeneKFDI--LCRLIDVQNPDLAVIFGRTKRRVDEL------------TRG--------LQAR---GYNAA 267
Cdd:PRK13767 241 IVDARFVK-----PFDIkvISPVDDLIHTPAEEISEALYETLHELikehrttliftnTRSgaervlynLRKRfpeEYDED 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489743809 268 GI---HGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIPQDPDSYVHRIGRTG 331
Cdd:PRK13767 316 NIgahHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
219-332 |
1.84e-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: 51.09 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 219 VRAKENEKFDILCRLID-VQNPDLAVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATD 297
Cdd:cd18790 6 VRPTEGQVDDLLGEIRKrVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGIN 85
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489743809 298 VAARGLDISGVSHVYNYD-----IPQDPDSYVHRIGRTGR 332
Cdd:cd18790 86 LLREGLDLPEVSLVAILDadkegFLRSETSLIQTIGRAAR 125
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
289-344 |
2.54e-07 |
|
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: 48.08 E-value: 2.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 489743809 289 KLDILVATDVAARGLDISGVSHVYNYDIPQDPDSYVHRIGRTGRAGQNGMSVTFVT 344
Cdd:cd18785 22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
223-334 |
3.83e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 52.57 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 223 ENEKFDILCRLIDVQ---NPDLAVI-FGRTKRRVDELTRGLQARGYNA------AGIHGD--LSQAKRMSVLKRFRKGKL 290
Cdd:PRK13766 345 EHPKLEKLREIVKEQlgkNPDSRIIvFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDkgMSQKEQIEILDKFRAGEF 424
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489743809 291 DILVATDVAARGLDISGVSHVYNYD-IPQDPDSyVHRIGRTGRAG 334
Cdd:PRK13766 425 NVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGRQE 468
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
226-337 |
4.79e-07 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 49.17 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 226 KFDILCRLIDV-QNPDLAVIFGRTkrrVDELTRglQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLD 304
Cdd:cd18789 35 KLRALEELLKRhEQGDKIIVFTDN---VEALYR--YAKRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGID 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489743809 305 IsgvshvynydipqdPDS---------------YVHRIGRTGRAGQNG 337
Cdd:cd18789 110 L--------------PEAnvaiqisghggsrrqEAQRLGRILRPKKGG 143
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
45-329 |
2.29e-06 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 50.08 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 45 AQTGTGKTAAFGLPILQNLDK-QHDSIqaIVIEPTRELAIQTQEELFRLGRDE------KARVQVVYGGADIRRQIRALK 117
Cdd:COG1203 154 APTGGGKTEAALLFALRLAAKhGGRRI--IYALPFTSIINQTYDRLRDLFGEDvllhhsLADLDLLEEEEEYESEARWLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 118 ------QTPaILVGTPGRLLDHL-KRGTIDISKV-----KTIVLDEADeMLDMGFIQDIESILNYASSKHQTLLF-SATM 184
Cdd:COG1203 232 llkelwDAP-VVVTTIDQLFESLfSNRKGQERRLhnlanSVIILDEVQ-AYPPYMLALLLRLLEWLKNLGGSVILmTATL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 185 PKPILRIGEKFmhdPEIV---KIKGKELTANLIDQ-YFVRAKENEKFDILCRLIDV--QNPDLAVIFGrTKRRVDELTRG 258
Cdd:COG1203 310 PPLLREELLEA---YELIpdePEELPEYFRAFVRKrVELKEGPLSDEELAELILEAlhKGKSVLVIVN-TVKDAQELYEA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 259 LQARGyNAAGI---HGDLSQAKRMSVLK----RFRKGKLDILVATDVAARGLDISgvshvynYDI----PQDPDSYVHRI 327
Cdd:COG1203 386 LKEKL-PDEEVyllHSRFCPADRSEIEKeikeRLERGKPCILVSTQVVEAGVDID-------FDVvirdLAPLDSLIQRA 457
|
..
gi 489743809 328 GR 329
Cdd:COG1203 458 GR 459
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
243-342 |
4.59e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 49.51 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 243 VIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIPQDPDS 322
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90 100
....*....|....*....|
gi 489743809 323 YVHRIGRTGRAGQNGMSVTF 342
Cdd:PLN03137 764 YHQECGRAGRDGQRSSCVLY 783
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
40-334 |
6.65e-06 |
|
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: 48.19 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 40 DVIGQAQTGTGKTAAfGLPILQNLDKQHDSIQAIVIEPTRELA-------IQTQEELFRLGRDEKARVQVVYGGADIRRQ 112
Cdd:cd09639 1 LLVIEAPTGYGKTEA-ALLWALHSLKSQKADRVIIALPTRATInamyrraKEAFGETGLYHSSILSSRIKEMGDSEEFEH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 113 IRALKQTpailvGTPGRLLDHLKRGTID---ISKVKT---------------IVLDEADEMLD--MGFIQDIESILNYAS 172
Cdd:cd09639 80 LFPLYIH-----SNDTLFLDPITVCTIDqvlKSVFGEfghyeftlasianslLIFDEVHFYDEytLALILAVLEVLKDND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 173 SKHqtLLFSATMPKPILRIGEKFmhdpEIVKIKGKELTANLIDQYFVR--AKENEKFDILCRLIDVQNPDLAV-IFGRTK 249
Cdd:cd09639 155 VPI--LLMSATLPKFLKEYAEKI----GYVEENEPLDLKPNERAPFIKieSDKVGEISSLERLLEFIKKGGSVaIIVNTV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 250 RRVDELTRGLQARG--YNAAGIHGDLSQA----KRMSVLKRFRKGKLDILVATDVAARGLDISgvshvynYDI----PQD 319
Cdd:cd09639 229 DRAQEFYQQLKEKGpeEEIMLIHSRFTEKdrakKEAELLLEFKKSEKFVIVATQVIEASLDIS-------VDVmiteLAP 301
|
330
....*....|....*
gi 489743809 320 PDSYVHRIGRTGRAG 334
Cdd:cd09639 302 IDSLIQRLGRLHRYG 316
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
254-335 |
9.93e-06 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 45.80 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 254 ELTRGLQARgYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVynydIPQDPD----SYVHRI-G 328
Cdd:cd18811 53 YLKERFRPE-LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVM----VIEDAErfglSQLHQLrG 127
|
....*..
gi 489743809 329 RTGRAGQ 335
Cdd:cd18811 128 RVGRGDH 134
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
244-343 |
2.56e-05 |
|
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: 44.18 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 244 IFGRTKRRVDELTRGL-QARGYNAAGI-----HGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIP 317
Cdd:cd18796 43 VFTNTRSQAERLAQRLrELCPDRVPPDfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
|
90 100
....*....|....*....|....*.
gi 489743809 318 QDPDSYVHRIGRTGRAGQNGMSVTFV 343
Cdd:cd18796 123 KSVARLLQRLGRSGHRPGAASKGRLV 148
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
264-348 |
4.34e-05 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 43.79 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 264 YNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVshvyNYDIPQDPD----SYVHRI-GRTGRAGQNGM 338
Cdd:cd18792 61 ARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA----NTMIIEDADrfglSQLHQLrGRVGRGKHQSY 136
|
90
....*....|
gi 489743809 339 SVtFVTPNEI 348
Cdd:cd18792 137 CY-LLYPDPK 145
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
44-190 |
4.62e-05 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 43.94 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 44 QAQTGTGKTAAFGLPILQNLDKQHdsiQAIVIEPTRELAIQTQEELFRLGRDekARVQVVYGGAdiRRQIralKQTPAIL 123
Cdd:cd17918 42 SGDVGSGKTLVALGAALLAYKNGK---QVAILVPTEILAHQHYEEARKFLPF--INVELVTGGT--KAQI---LSGISLL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489743809 124 VGTPGRLldHLKRgtidisKVKTIVLDEADEMLDMGFIQDiESIlnYASSKHQTLLFSATmpkPILR 190
Cdd:cd17918 112 VGTHALL--HLDV------KFKNLDLVIVDEQHRFGVAQR-EAL--YNLGATHFLEATAT---PIPR 164
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
40-335 |
6.19e-05 |
|
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: 45.14 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 40 DVIGQAQTGTGKTAAfGLPILQNLDKQHDSIQAIVIEPTRELA---IQTQEELFRLGrdekarvQVVYGGADIRRQIRAL 116
Cdd:TIGR01587 1 LLVIEAPTGYGKTEA-ALLWALHSIKSQKADRVIIALPTRATInamYRRAKELFGSE-------LVGLHHSSSFSRIKEM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 117 KQTPAIL-------VGTPGRLLDHLKRGTID---ISKVKT---------------IVLDEADEMLD--MGFIQDIESILN 169
Cdd:TIGR01587 73 GDSEEFEhlfplyiHSNDKLFLDPITVCTIDqvlKSVFGEfghyeftlasianslLIFDEVHFYDEytLALILAVLEVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 170 YASSKHqtLLFSATMPKPILRIGEKFMHDPEIVKIKGKELTANLIDQYFVRAKE-NEKFDILCRLIDVQNPDLAV-IFGR 247
Cdd:TIGR01587 153 DNDVPI--LLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDkVGEISSLERLLEFIKKGGSIaIIVN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 248 TKRRVDELTRGLQARGYNAAGI--HGDLSQA----KRMSVLKRFRK-GKLDILVATDVAARGLDISgvshvynYDI---- 316
Cdd:TIGR01587 231 TVDRAQEFYQQLKEKAPEEEIIlyHSRFTEKdrakKEAELLREMKKsNEKFVIVATQVIEASLDIS-------ADVmite 303
|
330
....*....|....*....
gi 489743809 317 PQDPDSYVHRIGRTGRAGQ 335
Cdd:TIGR01587 304 LAPIDSLIQRLGRLHRYGR 322
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1-187 |
8.41e-05 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 45.19 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 1 MKFSEMNLKPEILKAIKRSGFEEATPIQEKTIPL-VLEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDsiQAIVIEPTR 79
Cdd:PRK00254 1 MKVDELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGG--KAVYLVPLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 80 ELAiqtqEELFRLGRD-EKARVQVVYGGADIRRQIRALKQTPaILVGTPGRLLDHLKRGTIDISKVKTIVLDEADEM--L 156
Cdd:PRK00254 79 ALA----EEKYREFKDwEKLGLRVAMTTGDYDSTDEWLGKYD-IIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIgsY 153
|
170 180 190
....*....|....*....|....*....|.
gi 489743809 157 DMGfiQDIESILNYASSKHQTLLFSATMPKP 187
Cdd:PRK00254 154 DRG--ATLEMILTHMLGRAQILGLSATVGNA 182
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
21-152 |
3.16e-04 |
|
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: 41.87 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 21 FEEAtpIQEKTIpLVLEgkdvigqaqTGTGKT--AAFGLPI---LQNLDKQHDSIqAIVIEPTRELAIQtQEELFRlgRD 95
Cdd:cd18034 11 FEAA--LKRNTI-VVLP---------TGSGKTliAVMLIKEmgeLNRKEKNPKKR-AVFLVPTVPLVAQ-QAEAIR--SH 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489743809 96 EKARVQVVYGGADIRRQIRALKQ----TPAILVGTPGRLLDHLKRGTIDISKVKTIVLDEA 152
Cdd:cd18034 75 TDLKVGEYSGEMGVDKWTKERWKeeleKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
212-348 |
4.20e-04 |
|
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: 41.14 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 212 NLIDQYFVRAKENEKFDILCRLIDvqnpDLAVIFGRT---KRRVDELTRGLQARGYNAAGIHgdlsqAKRMSVLKRFRKG 288
Cdd:cd18798 1 NIVDVYIEDSDSLEKLLELVKKLG----DGGLIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489743809 289 KLDILVAT----DVAARGLDISG-VSHVYNYDIPqdPDSYVHRIGRTGRAGQNGM----SVTFVTPNEI 348
Cdd:cd18798 72 EIDVLIGVasyyGVLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSRLYAGGLtkglSVVLVDDPEL 138
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
27-93 |
1.01e-03 |
|
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: 40.42 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489743809 27 IQEKTIPLVLEG-KDVIGQAQTGTGKTAAFGLPILQNLDKQHDS----IQAIVIEPTRELAIQT----QEELFRLG 93
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPLpwgnRKVVYIAPIKALCSEKyddwKEKFGPLG 80
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
242-305 |
1.19e-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: 38.69 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489743809 242 AVIFGRTKRRVDELTRGLQARGYNAAGIHGDLSQAKR-MSVLKRFRKGKL--DILVATDVAARGLDI 305
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELkpPILVTVDLLTTGVDI 75
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
245-335 |
1.51e-03 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 39.16 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 245 FGRTKRRVDELTRGLQAR-------GYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDVAARGLDISGVSHVYNYDIP 317
Cdd:cd18797 41 FCRSRKLAELLLRYLKARlveegplASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYP 120
|
90
....*....|....*...
gi 489743809 318 QDPDSYVHRIGRTGRAGQ 335
Cdd:cd18797 121 GSLASLWQQAGRAGRRGK 138
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
45-95 |
1.53e-03 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 40.74 E-value: 1.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489743809 45 AQTGTGKTAAFGLPILQNLDKqHDSiqAIVIEPTRELAIQTQEELFRLGRD 95
Cdd:COG3505 6 GPTGSGKTVGLVIPNLTQLAR-GES--VVVTDPKGDLAELTAGFRRRAGYD 53
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
47-183 |
2.05e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.81 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 47 TGTGKT--AAFglpILQNLDKQHDSIQAIVIEPTRELAIQTQEELFRLGRDEKARVQVVYGGADIRRqiralKQTPAILV 124
Cdd:pfam04851 32 TGSGKTltAAK---LIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDES-----VDDNKIVV 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489743809 125 GTPGRLLDHLKRGTIDISKVKTIVL--DEADEMLDMGFiqdiESILNYasSKHQTLL-FSAT 183
Cdd:pfam04851 104 TTIQSLYKALELASLELLPDFFDVIiiDEAHRSGASSY----RNILEY--FKPAFLLgLTAT 159
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
36-152 |
2.55e-03 |
|
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: 39.34 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 36 LEGKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIQA--IVIEPTRELAIQTQEELFRLGRDEKARVQVVYGgaDIRRQI 113
Cdd:cd17927 15 LKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGkvVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSG--DTSENV 92
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489743809 114 RALK--QTPAILVGTPGRLLDHLKRGTI-DISKVKTIVLDEA 152
Cdd:cd17927 93 SVEQivESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDEC 134
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
38-194 |
3.76e-03 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 38.43 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 38 GKDVIGQAQTGTGKTAAFGLPILQNLDKQHDSIqAIVIEPTRELAIQTQEE----LFRLGRDEKarVQVVYGGADIRRQI 113
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWALKLAARGGKRR-IIYALPTRATINQMYERireiLGRLDDEDK--VLLLHSKAALELLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743809 114 RALKQTPAILVGTpgRLLDHLKR--------GTID------------------ISKvKTIVLDEA----DEMLDMgFIQD 163
Cdd:cd17930 78 SDEEPDDDPVEAV--DWALLLKRswlapivvTTIDqllesllkykhferrlhgLAN-SVVVLDEVqaydPEYMAL-LLKA 153
|
170 180 190
....*....|....*....|....*....|.
gi 489743809 164 IESILNYASSKHqtLLFSATMPKPILRIGEK 194
Cdd:cd17930 154 LLELLGELGGPV--VLMTATLPALLRDELLE 182
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
263-298 |
9.70e-03 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 38.49 E-value: 9.70e-03
10 20 30
....*....|....*....|....*....|....*.
gi 489743809 263 GYNAAGIHGDLSQAKRMSVLKRFRKGKLDILVATDV 298
Cdd:COG1200 503 GLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV 538
|
|
| |
