|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
2-393 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 611.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 2 TITFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPN-IQAIIIAPT 80
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 81 RELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNM 160
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 161 GFIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVKVKAKEMTVSNIQQFYLDIHERKKFDTLTRLLDIQS 240
Cdd:COG0513 161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 241 PELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNFDVPQ 320
Cdd:COG0513 241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515927817 321 DPESYVHRIGRTGRAGRTGMAMTFITPREKDMLRAIEQTTKRKMDRMKEPTLDEAIEGQQQVTVDRLRTIISE 393
Cdd:COG0513 321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKG 393
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-373 |
9.01e-146 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 425.37 E-value: 9.01e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 1 MTITFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPT 80
Cdd:PRK11776 2 SMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 81 RELAIQVSEELYKIGqdkRA----RVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADE 156
Cdd:PRK11776 82 RELADQVAKEIRRLA---RFipniKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 157 MLNMGFIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVKVKAKEMTvSNIQQFYLDIHERKKFDTLTRLL 236
Cdd:PRK11776 159 MLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEVSPDERLPALQRLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 237 DIQSPELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNF 316
Cdd:PRK11776 238 LHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINY 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 515927817 317 DVPQDPESYVHRIGRTGRAGRTGMAMTFITPREKDMLRAIEQTTKRKMDRMKEPTLD 373
Cdd:PRK11776 318 ELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLS 374
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
3-476 |
3.24e-133 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 399.22 E-value: 3.24e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 3 ITFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTRE 82
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 83 LAIQVSEELYKIGQDKRA-RVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMG 161
Cdd:PRK11634 86 LAVQVAEAMTDFSKHMRGvNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 162 FIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVKVKAKEMTVSNIQQFYLDIHERKKFDTLTRLLDIQSP 241
Cdd:PRK11634 166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 242 ELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNFDVPQD 321
Cdd:PRK11634 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 322 PESYVHRIGRTGRAGRTGMAMTFITPREKDMLRAIEQTTKRKMDRMKEPTLDEAIEGQQQVTVDRLRTIISENNLNFYMT 401
Cdd:PRK11634 326 SESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLEKFAAKVQQQLESSDLDQYRA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 402 AAAEL-----LEDHDSVTVVAAAIKMMTKEpdaTPVRLTDEAPMISKRNRNNRSSSKRRDGGGGGgyrgkSRSSYGDKKR 476
Cdd:PRK11634 406 LLAKIqptaeGEELDLETLAAALLKMAQGE---RPLILPPDAPMRPKREFRDRDDRGPRDRNDRG-----PRGDREDRPR 477
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
14-205 |
1.46e-107 |
|
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: 317.85 E-value: 1.46e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDP----ASPNIQAIIIAPTRELAIQVSE 89
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 90 ELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIEDIEAI 169
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 515927817 170 LSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVK 205
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
4-366 |
2.14e-103 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 316.11 E-value: 2.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 4 TFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKI------DPASPNIqaIII 77
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfprrKSGPPRI--LIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 78 APTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEM 157
Cdd:PRK11192 80 TPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 158 LNMGFIEDIEAILSNVPSEHQTLLFSATMPAP-IKRIAERFMTNPEHVKVKAKEMTVSNIQQFYL--DIHERKkFDTLTR 234
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYraDDLEHK-TALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 235 LLDIQSPELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVY 314
Cdd:PRK11192 239 LLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 515927817 315 NFDVPQDPESYVHRIGRTGRAGRTGMAMTFITPREKDMLRAIEQTTKRKMDR 366
Cdd:PRK11192 319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKA 370
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
5-358 |
1.28e-101 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 311.13 E-value: 1.28e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 5 FQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFgipLVEKID-----PASPNIQ-----A 74
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF---LTATFHyllshPAPEDRKvnqprA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 75 IIIAPTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEA 154
Cdd:PRK04837 87 LIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 155 DEMLNMGFIEDIEAILSNVPSEHQ--TLLFSATMPAPIKRIAERFMTNPEHVKVKAKEMTVSNIQQ--FYLDIHErkKFD 230
Cdd:PRK04837 167 DRMFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPSNEE--KMR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 231 TLTRLLDIQSPELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGV 310
Cdd:PRK04837 245 LLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAV 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 515927817 311 THVYNFDVPQDPESYVHRIGRTGRAGRTGMAMTFITPREKDMLRAIEQ 358
Cdd:PRK04837 325 THVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIET 372
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
3-370 |
1.63e-100 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 309.43 E-value: 1.63e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 3 ITFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPN------IQAII 76
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 77 IAPTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADE 156
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 157 MLNMGFIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVKVKAKEMTVSNIQQFYLDIHERKKFDTLTRLL 236
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 237 DIQSPELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNF 316
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 515927817 317 DVPQDPESYVHRIGRTGRAGRTGMAMTFITPREKDMLRAIEQTTKRKMDRMKEP 370
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIP 374
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
4-367 |
1.31e-98 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 302.90 E-value: 1.31e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 4 TFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTREL 83
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTREL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 84 AIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFI 163
Cdd:PTZ00424 109 AQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 164 EDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVKVKAKEMTVSNIQQFYLDIH-ERKKFDTLTRLLDIQSPE 242
Cdd:PTZ00424 189 GQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEkEEWKFDTLCDLYETLTIT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 243 LSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNFDVPQDP 322
Cdd:PTZ00424 269 QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 515927817 323 ESYVHRIGRTGRAGRTGMAMTFITPREKDMLRAIEQTTKRKMDRM 367
Cdd:PTZ00424 349 ENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEM 393
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
1-371 |
6.55e-93 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 290.66 E-value: 6.55e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 1 MTITFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQ------- 73
Cdd:PRK01297 85 GKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymgepr 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 74 AIIIAPTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKN-PHIIVGTPGRLLDHINRRTMRLQNVETVVLD 152
Cdd:PRK01297 165 ALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 153 EADEMLNMGFIEDIEAILSNVP--SEHQTLLFSATMPAPIKRIAERFMTNPEHVKVKAKEMTVSNIQQFYLDIHERKKFD 230
Cdd:PRK01297 245 EADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 231 TLTRLLDIQSPELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGV 310
Cdd:PRK01297 325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515927817 311 THVYNFDVPQDPESYVHRIGRTGRAGRTGMAMTFITPREKDMLRAIEQTTKRKMDRMKEPT 371
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPA 465
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
3-364 |
1.56e-88 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 282.22 E-value: 1.56e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 3 ITFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKI---------DPASPniQ 73
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpaladrKPEDP--R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 74 AIIIAPTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINR-RTMRLQNVETVVLD 152
Cdd:PRK04537 87 ALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 153 EADEMLNMGFIEDIEAILSNVPSE--HQTLLFSATMPAPIKRIAERFMTNPEHVKVKAKEMTVSNIQQFYLDIHERKKFD 230
Cdd:PRK04537 167 EADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 231 TLTRLLDIQSPELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGV 310
Cdd:PRK04537 247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 515927817 311 THVYNFDVPQDPESYVHRIGRTGRAGRTGMAMTFITPREKDMLRAIEQTTKRKM 364
Cdd:PRK04537 327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKI 380
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
2-347 |
4.33e-86 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 275.11 E-value: 4.33e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 2 TITFQDFqlsesLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDpASPNIQ------AI 75
Cdd:PTZ00110 134 YTSFPDY-----ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHIN-AQPLLRygdgpiVL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 76 IIAPTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEAD 155
Cdd:PTZ00110 208 VLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEAD 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 156 EMLNMGFIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTN-PEHVKVKAKEMTVS-NIQQFYLDIHERKKFDTLT 233
Cdd:PTZ00110 288 RMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAChNIKQEVFVVEEHEKRGKLK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 234 RLLD---IQSPELsIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGV 310
Cdd:PTZ00110 368 MLLQrimRDGDKI-LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDV 446
|
330 340 350
....*....|....*....|....*....|....*..
gi 515927817 311 THVYNFDVPQDPESYVHRIGRTGRAGRTGMAMTFITP 347
Cdd:PTZ00110 447 KYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
4-205 |
3.06e-69 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 219.88 E-value: 3.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 4 TFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTREL 83
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 84 AIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHI-NRRTMRLQNVETVVLDEADEMLNMGF 162
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADRLLNMDF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515927817 163 IEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVK 205
Cdd:cd17954 161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
5-201 |
1.71e-67 |
|
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: 215.55 E-value: 1.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 5 FQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKI--DPASpnIQAIIIAPTRE 82
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLseDPYG--IFALVLTPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 83 LAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHI---NRRTMRLQNVETVVLDEADEMLN 159
Cdd:cd17955 79 LAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLrssDDTTKVLSRVKFLVLDEADRLLT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515927817 160 MGFIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNP 201
Cdd:cd17955 159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
27-193 |
2.40e-67 |
|
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: 213.64 E-value: 2.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 27 TPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTRELAIQVSEELYKIGQDKRARVLPIY 106
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 107 GGQDIGRQIRSLKKnPHIIVGTPGRLLDHINRRTmRLQNVETVVLDEADEMLNMGFIEDIEAILSNVPSEHQTLLFSATM 186
Cdd:pfam00270 81 GGDSRKEQLEKLKG-PDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 515927817 187 PAPIKRI 193
Cdd:pfam00270 159 PRNLEDL 165
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
5-201 |
5.05e-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: 214.08 E-value: 5.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 5 FQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTRELA 84
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 85 IQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIE 164
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 515927817 165 DIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNP 201
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
4-200 |
1.22e-65 |
|
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: 211.19 E-value: 1.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 4 TFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKI--DPASPNI--------Q 73
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLleDGPPSVGrgrrkaypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 74 AIIIAPTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDE 153
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515927817 154 ADEMLNMGFIEDIEAIL--SNVPS--EHQTLLFSATMPAPIKRIAERFMTN 200
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVehPDMPPkgERQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
14-204 |
2.11e-64 |
|
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: 207.94 E-value: 2.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKID--PASPNI------QAIIIAPTRELAI 85
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlPPLDEEtkddgpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 86 QVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIED 165
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515927817 166 IEAILSNVPSEH--------------------QTLLFSATMPAPIKRIAERFMTNPEHV 204
Cdd:cd17945 161 VTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
4-205 |
1.08e-63 |
|
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: 205.62 E-value: 1.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 4 TFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASP--NIQAIIIAPTR 81
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPtvGARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 82 ELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMG 161
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515927817 162 FIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVK 205
Cdd:cd17959 162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
14-205 |
1.19e-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: 205.18 E-value: 1.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKI---DPASPNIQAIIIAPTRELAIQVSEE 90
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 91 LYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHI-NRRTMRLQNVETVVLDEADEMLNMGFIEDIEAI 169
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 515927817 170 LSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVK 205
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
7-201 |
5.38e-63 |
|
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: 203.71 E-value: 5.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 7 DFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTRELAIQ 86
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 87 VSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIEDI 166
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 515927817 167 EAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNP 201
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDP 195
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
3-361 |
2.07e-61 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 209.26 E-value: 2.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 3 ITFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVE---KIDPASPNIQ----AI 75
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTIRSGHPSEQrnplAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 76 IIAPTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEAD 155
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 156 EMLNMGFIEDIEAILSNVpSEHQTLLFSATMPAPIKRIAERFMTNPEHVKVKAKEMTVSNIQQFYLDIHERKK----FDT 231
Cdd:PLN00206 281 CMLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKkqklFDI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 232 LTRLLDIQSPelSIVFGRTKRRVDELTEALNL-RGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGV 310
Cdd:PLN00206 360 LKSKQHFKPP--AVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRV 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 515927817 311 THVYNFDVPQDPESYVHRIGRTGRAGRTGMAMTFITPREKDMLRAIEQTTK 361
Cdd:PLN00206 438 RQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLK 488
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
216-345 |
1.39e-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: 194.65 E-value: 1.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 216 IQQFYLDIHERKKFDTL-TRLLDIQSPELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDV 294
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 515927817 295 LVATDVAARGLDISGVTHVYNFDVPQDPESYVHRIGRTGRAGRTGMAMTFI 345
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
4-198 |
4.15e-60 |
|
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: 198.27 E-value: 4.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 4 TFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKI------DPASPNIQ---A 74
Cdd:cd18052 44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegltASSFSEVQepqA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 75 IIIAPTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEA 154
Cdd:cd18052 124 LIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515927817 155 DEMLNMGFIEDIEAILS--NVPS--EHQTLLFSATMPAPIKRIAERFM 198
Cdd:cd18052 204 DRMLDMGFGPEIRKLVSepGMPSkeDRQTLMFSATFPEEIQRLAAEFL 251
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
10-203 |
6.77e-60 |
|
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: 195.88 E-value: 6.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 10 LSESLMKAINRMGFEEATPIQAETIPLGLQN-KDVIGQAQTGTGKTAAFGIPLVE-----KIDPASPNIQAIIIAPTREL 83
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTgDDVLARAKTGTGKTLAFLLPAIQsllntKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 84 AIQVSEELYK-IGQDKRARVLPIYGGQDIGRQIRSLKK-NPHIIVGTPGRLLDHINRRTMR--LQNVETVVLDEADEMLN 159
Cdd:cd17964 81 ALQIAAEAKKlLQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515927817 160 MGFIEDIEAILSNVP----SEHQTLLFSATMPAPIKRIAERFMtNPEH 203
Cdd:cd17964 161 MGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTL-KKDY 207
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
18-219 |
2.66e-57 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 188.85 E-value: 2.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 18 INRMGFEEATPIQAETIPLGLQN-KDVIGQAQTGTGKTAAFGIPLVEKIDPaSPNIQAIIIAPTRELAIQVSEELYKIGQ 96
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 97 DKRARVLPIYGGQDIGRQIRSLKKN-PHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIEDIEAILSNVPS 175
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515927817 176 EHQTLLFSATMPAPIKRIAERFMTNPEHVKVkaKEMTVSNIQQF 219
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
5-201 |
1.28e-56 |
|
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: 187.27 E-value: 1.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 5 FQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTRELA 84
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 85 IQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIE 164
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 515927817 165 DIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNP 201
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
14-207 |
7.08e-56 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 185.09 E-value: 7.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKI-----DPASPNIQAIIIAPTRELAIQVS 88
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 89 EELYKI--GQDKRARVLPIYGGQDIGRQIRSLKKN-PHIIVGTPGRLLDHINRRT--MRLQNVETVVLDEADEMLNMGFI 163
Cdd:cd17960 81 EVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515927817 164 EDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPehVKVK 207
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNP--VRVV 202
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
5-206 |
1.88e-54 |
|
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: 181.77 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 5 FQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTRELA 84
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 85 IQVSEELYKIGQD-KRARVLPIYGGQDIGRQIRSLKKN-PHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEM---LN 159
Cdd:cd17950 84 FQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleqLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515927817 160 MGfiEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVKV 206
Cdd:cd17950 164 MR--RDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
10-206 |
3.35e-54 |
|
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: 180.86 E-value: 3.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 10 LSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKI------DPASPNIQAIIIAPTREL 83
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 84 AIQVSEELYKIGQ--DKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQ-NVETVVLDEADEMLNM 160
Cdd:cd17961 81 AQQVSKVLEQLTAycRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLsTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515927817 161 GFIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVKV 206
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
14-204 |
8.53e-54 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350724 [Multi-domain] Cd Length: 197 Bit Score: 179.49 E-value: 8.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDpASPNIQ------AIIIAPTRELAIQV 87
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHIN-AQPPLErgdgpiVLVLAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 88 SEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIEDIE 167
Cdd:cd17966 80 QQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 515927817 168 AILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHV 204
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
14-205 |
2.79e-52 |
|
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: 175.53 E-value: 2.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTRELAIQVSEELYK 93
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 94 IGQ-DKRARVLPIYGGQDIGRQIRSLKKnPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIEDIEAILSN 172
Cdd:cd17943 81 IGKkLEGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|...
gi 515927817 173 VPSEHQTLLFSATMPAPIKRIAERFMTNPEHVK 205
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
10-201 |
8.34e-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: 174.30 E-value: 8.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 10 LSESLMKAINRMGFEEATPIQAETIPLGLQN--KDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTRELAIQV 87
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 88 SEELYKIGQDKRARV-LPIYGGQ-DIGRQIRSlkknpHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNM-GFIE 164
Cdd:cd17963 81 GEVVEKMGKFTGVKVaLAVPGNDvPRGKKITA-----QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGD 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 515927817 165 DIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNP 201
Cdd:cd17963 156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNA 192
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
14-186 |
2.02e-51 |
|
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: 174.73 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQN-KDVIGQAQTGTGKTAAFGIPLVEKI-------DPASPNI--QAIIIAPTREL 83
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRDgKDVIGAAETGSGKTLAFGIPILERLlsqkssnGVGGKQKplRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 84 AIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHI---NRRTMRLQNVETVVLDEADEMLNM 160
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIqegNEHLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 515927817 161 GFIEDIEAILSNVPSEH-------QTLLFSATM 186
Cdd:cd17946 161 GHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
10-201 |
2.39e-51 |
|
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: 174.10 E-value: 2.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 10 LSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKI---DPASPN--IQAIIIAPTRELA 84
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIkdqRPVKPGegPIGLIMAPTRELA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 85 IQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHI---NRRTMRLQNVETVVLDEADEMLNMG 161
Cdd:cd17953 99 LQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRMFDMG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515927817 162 FIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNP 201
Cdd:cd17953 179 FEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
14-204 |
4.56e-51 |
|
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: 172.21 E-value: 4.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIdPASPNIQ------AIIIAPTRELAIQV 87
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI-MDQRELEkgegpiAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 88 SEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIEDIE 167
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 515927817 168 AILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHV 204
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
16-206 |
8.19e-50 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 169.01 E-value: 8.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 16 KAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKID----PASPNIQAIIIAPTRELAIQVSEEL 91
Cdd:cd17941 3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwTPEDGLGALIISPTRELAMQIFEVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 92 YKIGQDKRARVLPIYGGQDIgrQIRSLKKNP-HIIVGTPGRLLDHINRR-TMRLQNVETVVLDEADEMLNMGFIEDIEAI 169
Cdd:cd17941 83 RKVGKYHSFSAGLIIGGKDV--KEEKERINRmNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDAI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 515927817 170 LSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVKV 206
Cdd:cd17941 161 VENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
4-200 |
1.62e-49 |
|
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: 170.22 E-value: 1.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 4 TFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKI---DPASPNIQ------- 73
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqGPGESLPSesgyygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 74 ------AIIIAPTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVE 147
Cdd:cd18051 102 rkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515927817 148 TVVLDEADEMLNMGFIEDIEAILS--NVP--SEHQTLLFSATMPAPIKRIAERFMTN 200
Cdd:cd18051 182 YLVLDEADRMLDMGFEPQIRRIVEqdTMPptGERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
19-205 |
2.13e-49 |
|
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: 168.53 E-value: 2.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 19 NRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQ------AIIIAPTRELAIQVSEELY 92
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 93 KIGQdKRARVLP--IYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHI-NRRTMRLQNVETVVLDEADEMLNMGFIEDIEAI 169
Cdd:cd17949 87 KLLK-PFHWIVPgyLIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515927817 170 LSNV-------------PSEHQTLLFSATMPAPIKRIAERFMTNPEHVK 205
Cdd:cd17949 166 LELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
5-201 |
5.38e-49 |
|
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: 167.26 E-value: 5.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 5 FQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTRELA 84
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 85 IQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIE 164
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 515927817 165 DIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNP 201
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDP 197
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
14-201 |
3.79e-47 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 161.95 E-value: 3.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTRELAIQVSEELYK 93
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 94 IGQDK-RARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIEDIEAILSN 172
Cdd:cd17962 81 LMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180
....*....|....*....|....*....
gi 515927817 173 VPSEHQTLLFSATMPAPIKRIAERFMTNP 201
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNP 189
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
14-201 |
4.40e-47 |
|
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: 161.99 E-value: 4.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKI--DPASPNIQAIIIAPTRELAIQVSEEL 91
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 92 YKIGQDKRARVLPIYGGQ-DIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIEDIEAIL 170
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
|
170 180 190
....*....|....*....|....*....|..
gi 515927817 171 SNVPSEH-QTLLFSATMPAPIKRIAERFMTNP 201
Cdd:cd17957 161 AACTNPNlQRSLFSATIPSEVEELARSVMKDP 192
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
14-204 |
4.01e-46 |
|
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: 159.55 E-value: 4.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIP--------LVEKIDPASPNIqaIIIAPTRELAI 85
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgfihldlqPIPREQRNGPGV--LVLTPTRELAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 86 QVSEELYKIGQdKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIED 165
Cdd:cd17958 79 QIEAECSKYSY-KGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQ 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 515927817 166 IEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHV 204
Cdd:cd17958 158 IRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
14-201 |
3.05e-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: 157.50 E-value: 3.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLV------EKIDPASPNIQ--AIIIAPTRELAI 85
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqEKKLPFIKGEGpyGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 86 QVSE------ELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLN 159
Cdd:cd17951 81 QTHEvieyycKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515927817 160 MGFIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNP 201
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKP 202
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
5-204 |
1.53e-44 |
|
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: 155.56 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 5 FQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKidpaspnIQAIIIAPTRELA 84
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------VVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 85 IQVSEELYKIGQ---DKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMG 161
Cdd:cd17938 74 EQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515927817 162 FIEDIEAILSNVPSEH------QTLLFSATMPAP-IKRIAERFMTNPEHV 204
Cdd:cd17938 154 NLETINRIYNRIPKITsdgkrlQVIVCSATLHSFeVKKLADKIMHFPTWV 203
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
3-208 |
3.08e-44 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 155.55 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 3 ITFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDpASPNIQ------AII 76
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHIN-HQPFLErgdgpiCLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 77 IAPTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADE 156
Cdd:cd18049 103 LAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADR 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515927817 157 MLNMGFIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVKVKA 208
Cdd:cd18049 183 MLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
15-194 |
3.29e-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: 151.74 E-value: 3.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 15 MKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVE-----KIDPASpNIQAIIIAPTRELAIQ--- 86
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyklKFKPRN-GTGVIIISPTRELALQiyg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 87 VSEELYKIGQDKRARVLpiyGGQDIGRQIRSLKKNPHIIVGTPGRLLDHI-NRRTMRLQNVETVVLDEADEMLNMGFIED 165
Cdd:cd17942 81 VAKELLKYHSQTFGIVI---GGANRKAEAEKLGKGVNILVATPGRLLDHLqNTKGFLYKNLQCLIIDEADRILEIGFEEE 157
|
170 180
....*....|....*....|....*....
gi 515927817 166 IEAILSNVPSEHQTLLFSATMPAPIKRIA 194
Cdd:cd17942 158 MRQIIKLLPKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
28-198 |
1.30e-41 |
|
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: 147.69 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 28 PIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPASPNI------QAIIIAPTRELAIQVSEELYKIgqDKRAR 101
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQVTKDFKDI--TRKLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 102 VLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIEDIEAILS-----NVPSE 176
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvsykkDSEDN 172
|
170 180
....*....|....*....|..
gi 515927817 177 HQTLLFSATMPAPIKRIAERFM 198
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
5-206 |
1.72e-40 |
|
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: 146.69 E-value: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 5 FQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDpASPNIQ------AIIIA 78
Cdd:cd18050 64 FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHIN-HQPYLErgdgpiCLVLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 79 PTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEML 158
Cdd:cd18050 143 PTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515927817 159 NMGFIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVKV 206
Cdd:cd18050 223 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
4-212 |
6.71e-35 |
|
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: 130.53 E-value: 6.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 4 TFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQN--KDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTR 81
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 82 ELAIQ---VSEELYKIGQDkrARVLPIYGGQDIGRQIRSLKKnphIIVGTPGRLLDHINR-RTMRLQNVETVVLDEADEM 157
Cdd:cd18048 99 ELALQtgkVVEEMGKFCVG--IQVIYAIRGNRPGKGTDIEAQ---IVIGTPGTVLDWCFKlRLIDVTNISVFVLDEADVM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515927817 158 LNM-GFIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVKVKAKEMT 212
Cdd:cd18048 174 INVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
227-336 |
1.88e-34 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 125.02 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 227 KKFDTLTRLLDIQSPELSIVFGRTKRRVDElTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLD 306
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 515927817 307 ISGVTHVYNFDVPQDPESYVHRIGRTGRAG 336
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
14-186 |
7.29e-32 |
|
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: 121.97 E-value: 7.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQN---------KDVIGQAQTGTGKTAAFGIPLVEKI-DPASPNIQAIIIAPTREL 83
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 84 AIQVSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPH--------IIVGTPGRLLDHINR-RTMRLQNVETVVLDEA 154
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNStPGFTLKHLRFLVIDEA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515927817 155 DEMLNMGFIE-------------------DIEAILSNVPSEH-QTLLFSATM 186
Cdd:cd17956 161 DRLLNQSFQDwletvmkalgrptapdlgsFGDANLLERSVRPlQKLLFSATL 212
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
255-336 |
1.05e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 108.45 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 255 DELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNFDVPQDPESYVHRIGRTGR 334
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 515927817 335 AG 336
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
4-205 |
3.97e-27 |
|
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: 108.27 E-value: 3.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 4 TFQDFQLSESLMKAINRMGFEEATPIQAETIPLGLQN--KDVIGQAQTGTGKTAAFGIPLVEKIDPASPNIQAIIIAPTR 81
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 82 ELAIQVSEELYKIGQdKRARVLPIYGGQDiGRQIRSLKKNPHIIVGTPGRLLDH-INRRTMRLQNVETVVLDEADEML-N 159
Cdd:cd18047 82 ELALQTGKVIEQMGK-FYPELKLAYAVRG-NKLERGQKISEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIaT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515927817 160 MGFIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTNPEHVK 205
Cdd:cd18047 160 QGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
14-229 |
5.52e-26 |
|
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: 105.91 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 14 LMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKI-------DPASPNIQAIIIAPTRELAIQ 86
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 87 VSEELYKIGQDKRARVLPIYGGQDIGRQIRSLKKNPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEADEMLNMGFIEDI 166
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515927817 167 EAILSNVP-------------SEHQTLLFSATMPAPIKRIAERfMTNPEHVKvkakemTVSNIQQFYLDIHERKKF 229
Cdd:cd17948 161 SHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSK-VIDVDSIE------TVTSDKLHRLMPHVKQKF 229
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
12-200 |
3.45e-16 |
|
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: 78.19 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 12 ESLMKAI-----NRMGFEEATPIQAETIP------LGLQNKDVIGQ----------AQTGTGKTAAFGIPLVEKI---DP 67
Cdd:cd17965 12 EAIIKEIlkgsnKTDEEIKPSPIQTLAIKkllktlMRKVTKQTSNEepklevfllaAETGSGKTLAYLAPLLDYLkrqEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 68 ASPN--------------IQAIIIAPTRELAIQVSEELYKIGQDKRARVLPIYGGQDIGRQ--IRSLKKNPHIIVGTPGR 131
Cdd:cd17965 92 EPFEeaeeeyesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQrlQLAFKGRIDILVTTPGK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515927817 132 LLDHINRRTMRLQNVETVVLDEADEMLNMGFIEDIEAILSNVPSEHQTLLFSATMPAPIKRIAERFMTN 200
Cdd:cd17965 172 LASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPD 240
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
128-354 |
1.71e-15 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 78.64 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 128 TPGRLLDHINRRTMRLQNVETVVLDEA--------D---EMLNMG-FIEDieaiLSNVPsehqTLLFSATMPAPIKR-IA 194
Cdd:COG0514 114 APERLLNPRFLELLRRLKISLFAIDEAhcisqwghDfrpDYRRLGeLRER----LPNVP----VLALTATATPRVRAdIA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 195 ERF-MTNPEHVkvkakemtVS-----NIqqfYLDIHERKKFDTLTRLLDI---QSPELSIVFGRTKRRVDELTEALNLRG 265
Cdd:COG0514 186 EQLgLEDPRVF--------VGsfdrpNL---RLEVVPKPPDDKLAQLLDFlkeHPGGSGIVYCLSRKKVEELAEWLREAG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 266 YTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATdVA-ARGLDISGVTHVYNFDVPQDPESYVHRIGRTGRAGRTGMAMTF 344
Cdd:COG0514 255 IRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
|
250
....*....|
gi 515927817 345 ITPREKDMLR 354
Cdd:COG0514 334 YGPEDVAIQR 343
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
49-411 |
3.77e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 77.76 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 49 TGTGKT--AAFgipLVEKIDPASPniqAIIIAPTRELAIQVSEELykigqdkrARVLPIYGGQDIGRQIRSlkknpHIIV 126
Cdd:COG1061 109 TGTGKTvlALA---LAAELLRGKR---VLVLVPRRELLEQWAEEL--------RRFLGDPLAGGGKKDSDA-----PITV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 127 GTPGRLLDHINRRTMRlQNVETVVLDEADEMLNMGFiediEAILSNVPSEHqTLLFSAT------MPAPIKR-------- 192
Cdd:COG1061 170 ATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTATpfrsdgREILLFLfdgivyey 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 193 -----IAERFMTNPEHVKVK----AKEMTVSNIQQFY---LDIHERKKFDTLTRLLD-IQSPELSIVFGRTKRRVDELTE 259
Cdd:COG1061 244 slkeaIEDGYLAPPEYYGIRvdltDERAEYDALSERLreaLAADAERKDKILRELLReHPDDRKTLVFCSSVDHAEALAE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 260 ALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNFDVPQDPESYVHRIGRTGRAGRTG 339
Cdd:COG1061 324 LLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGK 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515927817 340 MAMTFIT--PREKDMLRAIeqTTKRKMDRMKEPTLDEAIEGQQQVTVDRLRTIISENNLNFYMTAAAELLEDHD 411
Cdd:COG1061 404 EDALVYDfvGNDVPVLEEL--AKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDA 475
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
40-185 |
3.42e-14 |
|
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: 69.74 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 40 NKDVIGQAQTGTGKTAAFGIPLVEKIDPASPniQAIIIAPTRELAIQVSEELYKIGQDKrARVLPIYGGQDIGRQIRSLK 119
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGK--KVLVLVPTKALALQTAERLRELFGPG-IRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515927817 120 KNPHIIVGTPGRLLDHINR-RTMRLQNVETVVLDEADEML------NMGFIEDIEAILSNVpsehQTLLFSAT 185
Cdd:cd00046 78 GDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLidsrgaLILDLAVRKAGLKNA----QVILLSAT 146
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
215-405 |
7.09e-13 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 70.90 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 215 NIQqfYLDIHERKKFDTLTRLLDIQSPELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDV 294
Cdd:PRK11057 212 NIR--YTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQI 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 295 LVATDVAARGLDISGVTHVYNFDVPQDPESYVHRIGRTGRAGRTGMAMTFITPREKDMLRaieqttkrkmdRMkeptLDE 374
Cdd:PRK11057 290 VVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLR-----------RC----LEE 354
|
170 180 190
....*....|....*....|....*....|.
gi 515927817 375 AIEGQQQVtvdrlrtiISENNLNfYMTAAAE 405
Cdd:PRK11057 355 KPAGQQQD--------IERHKLN-AMGAFAE 376
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
10-341 |
5.70e-12 |
|
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: 68.32 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 10 LSESLMKAINRMGFEEATPIQAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDpASPNIQAIIIAPTRELAI-QVS 88
Cdd:COG1205 41 LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL-EDPGATALYLYPTKALARdQLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 89 E--ELYKIGqDKRARVLPIYGgqDIGRQIRS-LKKNPHIIVGTP-----GRLLDHinRRTMR-LQNVETVVLDEADE--- 156
Cdd:COG1205 120 RlrELAEAL-GLGVRVATYDG--DTPPEERRwIREHPDIVLTNPdmlhyGLLPHH--TRWARfFRNLRYVVIDEAHTyrg 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 157 -----MLNMgfIEDIEAILSNVPSEHQTLLFSATMPAPiKRIAERFmTNPEHVKVKaKEMTVSNIQQFYL------DIHE 225
Cdd:COG1205 195 vfgshVANV--LRRLRRICRHYGSDPQFILASATIGNP-AEHAERL-TGRPVTVVD-EDGSPRGERTFVLwnpplvDDGI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 226 RKKFDTLTRLL-------DIQspelSIVFGRTKRRVdELTeALNLRGYTAEGIHGDLTQA---------KRMVAlRKFKE 289
Cdd:COG1205 270 RRSALAEAARLladlvreGLR----TLVFTRSRRGA-ELL-ARYARRALREPDLADRVAAyragylpeeRREIE-RGLRS 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515927817 290 GSIDVLVAT-------DVAarGLD---ISGvthvynfdVPQDPESYVHRIGRTGRAGRTGMA 341
Cdd:COG1205 343 GELLGVVSTnalelgiDIG--GLDavvLAG--------YPGTRASFWQQAGRAGRRGQDSLV 394
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
218-344 |
9.38e-12 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 62.23 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 218 QFYLDIHE----RKKFDTLTRLLDIQSPELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSID 293
Cdd:cd18794 3 NLFYSVRPkdkkDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQ 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 515927817 294 VLVATDVAARGLDISGVTHVYNFDVPQDPESYVHRIGRTGRAGRTGMAMTF 344
Cdd:cd18794 83 VIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
232-379 |
3.36e-11 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 65.52 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 232 LTRLLDIQSPELSIVFGRTKRRVDELTEALNLRGYTAE------GIHGD--LTQAKRMVALRKFKEGSIDVLVATDVAAR 303
Cdd:COG1111 344 LKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 304 GLDISGVTHVYNFD-VPqdpeS---YVHRIGRTGRaGRTGMAMTFITP-------------REKDMLRAIeQTTKRKMDR 366
Cdd:COG1111 424 GLDIPEVDLVIFYEpVP----SeirSIQRKGRTGR-KREGRVVVLIAKgtrdeayywssrrKEKKMKSIL-KKLKKLLDK 497
|
170
....*....|...
gi 515927817 367 MKEPTLDEAIEGQ 379
Cdd:COG1111 498 QEKEKLKESAQAT 510
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
228-330 |
1.59e-10 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 59.03 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 228 KFDTLTRLLD--IQSPELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGS--IDVLVATDVAAR 303
Cdd:cd18793 12 KLEALLELLEelREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 515927817 304 GLDISGVTHVYNFDVPQDP------ESYVHRIG 330
Cdd:cd18793 92 GLNLTAANRVILYDPWWNPaveeqaIDRAHRIG 124
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
30-154 |
6.99e-09 |
|
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: 55.28 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 30 QAETIPLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIDPAsPNIQAIIIAPTRELAIQVSEELYKIGQDKRARVLP-IYGG 108
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD-PGSRALYLYPTKALAQDQLRSLRELLEQLGLGIRVaTYDG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 515927817 109 Q-DIGRQIRSLKKNPHIIVGTPGRL----LDHINRRTMRLQNVETVVLDEA 154
Cdd:cd17923 84 DtPREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
274-335 |
1.23e-08 |
|
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: 53.75 E-value: 1.23e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515927817 274 DLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNFDVPQDPESYVHRIGRtGRA 335
Cdd:cd18802 73 LMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
228-427 |
1.33e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.58 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 228 KFDTLTRL----LDIQSPELSIVFGRTKRRVDELTEALNLRGYTAEGIHGD--------LTQAKRMVALRKFKEGSIDVL 295
Cdd:PRK13766 348 KLEKLREIvkeqLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 296 VATDVAARGLDISGVTHVYNFD-VPQDPESyVHRIGRTGRaGRTGMAMTFITP-------------REKDMLRAIeqttk 361
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEGRVVVLIAKgtrdeayywssrrKEKKMKEEL----- 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515927817 362 RKMDRMKEPTLDEAIEGQQQVTVDRLRTiisENNLNFYMTAAAELLEDHDSVTVVAAAIKMMTKEP 427
Cdd:PRK13766 501 KNLKGILNKKLQELDEEQKGEEEEKDEQ---LSLDDFVKSKGKEEEEEEEKEEKDKETEEDEPEGP 563
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
250-363 |
1.34e-08 |
|
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: 54.17 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 250 TKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNFDV-----PQDPES 324
Cdd:cd18790 36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDAdkegfLRSETS 115
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 515927817 325 YVHRIGRTGR--AGRTGMAMTFITpreKDMLRAIEQTTKRK 363
Cdd:cd18790 116 LIQTIGRAARnvNGKVILYADKIT---DSMQKAIEETERRR 153
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
27-189 |
4.15e-08 |
|
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: 53.03 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 27 TPIQAETI-PLGLQNKDVIGQAQTGTGKTAAFGIPLVEKIdpASPNIQAIIIAPTRELAIQVSEELYKIGQDKRARVLPI 105
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRAL--ATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 106 YGGQDIGRQirsLKKNPHIIVGTPGRLLDHINR-RTMRLQNVETVVLDEAdEMLNMG----FIEDIEAILSNVPSEHQTL 180
Cdd:cd17921 81 TGDPSVNKL---LLAEADILVATPEKLDLLLRNgGERLIQDVRLVVVDEA-HLIGDGergvVLELLLSRLLRINKNARFV 156
|
....*....
gi 515927817 181 LFSATMPAP 189
Cdd:cd17921 157 GLSATLPNA 165
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
40-158 |
1.73e-07 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 51.04 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 40 NKDVIGQAQTGTGKT-AAFGIPLVEKIDPASPNIQAIIIAPTRELAIQVSEELYKIGQDKRA--RVLPIYGgqDIGRQIR 116
Cdd:cd17922 1 GRNVLIAAPTGSGKTeAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLeiPVAVRHG--DTSQSEK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 515927817 117 S--LKKNPHIIVGTPGRLLDHINRRTMR--LQNVETVVLDEADEML 158
Cdd:cd17922 79 AkqLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDEIHALL 124
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
267-334 |
2.90e-07 |
|
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: 49.66 E-value: 2.90e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515927817 267 TAEGIHGdLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNFDVPQDPESYVHRIGRTGR 334
Cdd:cd18801 67 SGKSSKG-MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
291-336 |
6.10e-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: 46.93 E-value: 6.10e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 515927817 291 SIDVLVATDVAARGLDISGVTHVYNFDVPQDPESYVHRIGRTGRAG 336
Cdd:cd18785 22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
226-307 |
1.08e-06 |
|
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: 48.40 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 226 RKKFDTLTRLLDIQSP-ELSIVFGRTKRRVDELTEALNlrgytAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARG 304
Cdd:cd18789 33 PNKLRALEELLKRHEQgDKIIVFTDNVEALYRYAKRLL-----KPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEG 107
|
...
gi 515927817 305 LDI 307
Cdd:cd18789 108 IDL 110
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
228-332 |
2.02e-06 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 50.22 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 228 KFDTLTRLLD--IQSPELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGS--IDVLVATDVAAR 303
Cdd:COG0553 534 KLEALLELLEelLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGE 613
|
90 100 110
....*....|....*....|....*....|....*
gi 515927817 304 GLDISGVTHVYNFDVPQDPESY------VHRIGRT 332
Cdd:COG0553 614 GLNLTAADHVIHYDLWWNPAVEeqaidrAHRIGQT 648
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
149-337 |
1.59e-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: 47.06 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 149 VVLDEAD--EMLNMGFIEDIEAILSNVPSEHqtLLFSATMPAPIKRIAERFMTNPEHVKVKAKEMTVSNIQQFYLdIHER 226
Cdd:TIGR01587 128 LIFDEVHfyDEYTLALILAVLEVLKDNDVPI--LLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFIL-IESD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 227 KKFD--TLTRLLDIQSPELSI-VFGRTKRRVDELTEALNLRGYTAEGI--HGDLTQAKR-----MVALRKFKEGSIDVLV 296
Cdd:TIGR01587 205 KVGEisSLERLLEFIKKGGSIaIIVNTVDRAQEFYQQLKEKAPEEEIIlyHSRFTEKDRakkeaELLREMKKSNEKFVIV 284
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515927817 297 ATDVAARGLDISgvthvynFDV----PQDPESYVHRIGRTGRAGR 337
Cdd:TIGR01587 285 ATQVIEASLDIS-------ADVmiteLAPIDSLIQRLGRLHRYGR 322
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
149-337 |
2.15e-05 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 46.65 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 149 VVLDEAD--EMLNMGFIEDIEAILSNVPSEHqtLLFSATMPAPIKRIAErfmtNPEHVKVKAKEMTVSNIQQFYLDIHER 226
Cdd:cd09639 127 LIFDEVHfyDEYTLALILAVLEVLKDNDVPI--LLMSATLPKFLKEYAE----KIGYVEENEPLDLKPNERAPFIKIESD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 227 KKFD--TLTRLLDIQSPELSI-VFGRTKRRVDELTEALNLRGYTAEG--IHGDLTQA----KRMVALRKFKEGSIDVLVA 297
Cdd:cd09639 201 KVGEisSLERLLEFIKKGGSVaIIVNTVDRAQEFYQQLKEKGPEEEImlIHSRFTEKdrakKEAELLLEFKKSEKFVIVA 280
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515927817 298 TDVAARGLDISgvthvynFDV----PQDPESYVHRIGRTGRAGR 337
Cdd:cd09639 281 TQVIEASLDIS-------VDVmiteLAPIDSLIQRLGRLHRYGE 317
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
23-333 |
3.86e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 46.42 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 23 FEEATPIQAETIPLGLQNKDVIGQAQTGTGKT-AAFGIPLVEKIDPASPN-----IQAIIIAPTRELA-------IQVSE 89
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAIIDELFRLGREGeledkVYCLYVSPLRALNndihrnlEEPLT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 90 ELYKIGQDKRARVLPIYGGQDIG------RQiRSLKKNPHIIVGTPGRLLDHIN--RRTMRLQNVETVVLDEADEMLN-- 159
Cdd:PRK13767 110 EIREIAKERGEELPEIRVAIRTGdtssyeKQ-KMLKKPPHILITTPESLAILLNspKFREKLRTVKWVIVDEIHSLAEnk 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 160 -----MGFIEDIEAIlsnVPSEHQTLLFSATMpAPIKRIAE-----RFMTNPEHVKVK----AKEMT------VSNIqqf 219
Cdd:PRK13767 189 rgvhlSLSLERLEEL---AGGEFVRIGLSATI-EPLEEVAKflvgyEDDGEPRDCEIVdarfVKPFDikvispVDDL--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 220 yldIHE------RKKFDTLTRLldIQSPELSIVFGRTK---RRVdelteALNLR-----GYTAEGI---HGDLTQAKRMV 282
Cdd:PRK13767 262 ---IHTpaeeisEALYETLHEL--IKEHRTTLIFTNTRsgaERV-----LYNLRkrfpeEYDEDNIgahHSSLSREVRLE 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 515927817 283 ALRKFKEGSIDVLVATDVAARGLDISGVTHVYNFDVPQDPESYVHRIGRTG 333
Cdd:PRK13767 332 VEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
29-219 |
5.89e-05 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 44.27 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 29 IQAETIPLGLQ-NKDVIGQAQTGTGKTAAFGIPLV----EKIDPASPNIQAIIIAPTRELaiqVSEELykigQDKRARVL 103
Cdd:cd18023 5 IQSEVFPDLLYsDKNFVVSAPTGSGKTVLFELAILrllkERNPLPWGNRKVVYIAPIKAL---CSEKY----DDWKEKFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 104 P-------IYGGQDIGRqIRSLkKNPHIIVGTPGRlLDHINRRTMRLQN-VETVVLDEADEMLNMGFIED--IEAILSNV 173
Cdd:cd18023 78 PlglscaeLTGDTEMDD-TFEI-QDADIILTTPEK-WDSMTRRWRDNGNlVQLVALVLIDEVHIIKENRGatLEVVVSRM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515927817 174 PSEHqtlLFSATMPAPIKRIaeRFmtnpehVKVKAkemTVSNIQQF 219
Cdd:cd18023 155 KTLS---SSSELRGSTVRPM--RF------VAVSA---TIPNIEDL 186
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
244-334 |
7.81e-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: 43.02 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 244 SIVFGRTKRRVDELTEALN-LRGYTAEGI-----HGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNFD 317
Cdd:cd18796 41 TLVFTNTRSQAERLAQRLReLCPDRVPPDfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
90
....*....|....*..
gi 515927817 318 VPQDPESYVHRIGRTGR 334
Cdd:cd18796 121 SPKSVARLLQRLGRSGH 137
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
49-154 |
2.14e-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: 42.25 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 49 TGTGKT--AAFGIP--LVEKIDPASPNIQAIIIAPTRELAIQVSEElykIGQDKRARVLPIYGGQDIGRQIRSLKK---- 120
Cdd:cd18034 25 TGSGKTliAVMLIKemGELNRKEKNPKKRAVFLVPTVPLVAQQAEA---IRSHTDLKVGEYSGEMGVDKWTKERWKeele 101
|
90 100 110
....*....|....*....|....*....|....
gi 515927817 121 NPHIIVGTPGRLLDHINRRTMRLQNVETVVLDEA 154
Cdd:cd18034 102 KYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
47-318 |
2.98e-04 |
|
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: 43.15 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 47 AQTGTGKT-AAFGIPLVEKIDPASPNIqaIIIAPTRELAIQVSEELYKIGQDK------RARVLPIYGGQDIGRQIRSLK 119
Cdd:COG1203 154 APTGGGKTeAALLFALRLAAKHGGRRI--IYALPFTSIINQTYDRLRDLFGEDvllhhsLADLDLLEEEEEYESEARWLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 120 KN------PhIIVGTPGRLLDHI----NRRTMRLQNVET--VVLDEAD----EMLNM--GFIEDIEAILSNVpsehqtLL 181
Cdd:COG1203 232 LLkelwdaP-VVVTTIDQLFESLfsnrKGQERRLHNLANsvIILDEVQayppYMLALllRLLEWLKNLGGSV------IL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 182 FSATMPAPIKRI---AERFMTNPEH-------------VKVKAKEMTVSNIQQFYLDIHERKKfdtltRLLdiqspelsI 245
Cdd:COG1203 305 MTATLPPLLREElleAYELIPDEPEelpeyfrafvrkrVELKEGPLSDEELAELILEALHKGK-----SVL--------V 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 246 VFGrTKRRVDELTEALNLRGyTAEGI---HGDLTQAKRMVALRK----FKEGSIDVLVATDVAARGLDISgvthvynFDV 318
Cdd:COG1203 372 IVN-TVKDAQELYEALKEKL-PDEEVyllHSRFCPADRSEIEKEikerLERGKPCILVSTQVVEAGVDID-------FDV 442
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
271-336 |
7.57e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 40.02 E-value: 7.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515927817 271 IHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVynfdVPQDPE----SYVHRI-GRTGRAG 336
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVM----VIEDAErfglSQLHQLrGRVGRGD 133
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
243-363 |
2.35e-03 |
|
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: 38.82 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 243 LSIVFGRTKrrVDELTEALNLRGYTAEGIHgdltqAKRMVALRKFKEGSIDVLVAT----DVAARGLDISG-VTHVYNFD 317
Cdd:cd18798 31 VSIDYGKEY--AEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLPErIKYAIFYG 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 515927817 318 VPqdPESYVHRIGRTGR--AGR--TGMAMTFITPRE-----KDMLRAIEQTTKRK 363
Cdd:cd18798 104 VP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPElfealKKRLKLILDEFIFK 156
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
271-358 |
2.78e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 38.40 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 271 IHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVynfdVPQDPE----SYVHRI-GRTGRAGRTGMAMtFI 345
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTM----IIEDADrfglSQLHQLrGRVGRGKHQSYCY-LL 140
|
90 100
....*....|....*....|
gi 515927817 346 TPREKDM-------LRAIEQ 358
Cdd:cd18792 141 YPDPKKLtetakkrLRAIAE 160
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
242-337 |
4.48e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 39.88 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 242 ELSIVFGRTKRRVDELTEALNLRGYTAEGIHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNFDVPQD 321
Cdd:PLN03137 681 ECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKS 760
|
90
....*....|....*.
gi 515927817 322 PESYVHRIGRTGRAGR 337
Cdd:PLN03137 761 IEGYHQECGRAGRDGQ 776
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
271-358 |
5.28e-03 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 37.71 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927817 271 IHGDLTQAKRMVALRKFKEGSIDVLVATDVAARGLDISGVTHVYNFDVPQDPESYVHRI-GRTGRAGRTGMAMtFITPRE 349
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYAY-FLYPDQ 135
|
90
....*....|....*.
gi 515927817 350 KDM-------LRAIEQ 358
Cdd:cd18810 136 KKLtedalkrLEAIQE 151
|
|
| |
