|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-400 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 622.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 1 MTTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKE-AVQGIVIAPT 79
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPrAPQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 80 RELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNM 159
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 160 GFIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKKKFDVLTRLLDIQS 239
Cdd:COG0513 161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 240 PELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQ 319
Cdd:COG0513 241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 320 DPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDRMEAPTLDEALEGQQRLIAEKLQSTIENDNLSYYK 399
Cdd:COG0513 321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGG 400
|
.
gi 446128740 400 R 400
Cdd:COG0513 401 R 401
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
2-439 |
1.76e-152 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 450.07 E-value: 1.76e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 2 TTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTRE 81
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 82 LAIQVGEELYKIGKHKR-VRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMG 160
Cdd:PRK11634 86 LAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 161 FIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKKKFDVLTRLLDIQSP 240
Cdd:PRK11634 166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 241 ELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQD 320
Cdd:PRK11634 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 321 PESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDRMEAPTLDeaLEGQQRL--IAEKLQSTIENDNLSYY 398
Cdd:PRK11634 326 SESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAE--LLGKRRLekFAAKVQQQLESSDLDQY 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446128740 399 KRI-----AEEMLEENDSVTVVAAALKMMTKEpdtTPIALTSEPPV 439
Cdd:PRK11634 404 RALlakiqPTAEGEELDLETLAAALLKMAQGE---RPLILPPDAPM 446
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-372 |
8.62e-152 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 441.93 E-value: 8.62e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 1 MTTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTR 80
Cdd:PRK11776 3 MTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 81 ELAIQVGEELYKIGKHKR-VRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNM 159
Cdd:PRK11776 83 ELADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 160 GFIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTmPNIQQFYLEVQEKKKFDVLTRLLDIQS 239
Cdd:PRK11776 163 GFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEVSPDERLPALQRLLLHHQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 240 PELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQ 319
Cdd:PRK11776 242 PESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELAR 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446128740 320 DPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDRMEAPTLD 372
Cdd:PRK11776 322 DPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLS 374
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
2-365 |
4.98e-106 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 324.20 E-value: 4.98e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 2 TTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLP----LLDKVDTNKEAVQGIVIA 77
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPalqhLLDFPRRKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 78 PTRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEML 157
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 158 NMGFIEDIEAILTDVPDTHQTLLFSATMP-DPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKK-KFDVLTRLL 235
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEhKTALLCHLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 236 DIQSPELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNF 315
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446128740 316 DIPQDPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDR 365
Cdd:PRK11192 321 DMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKA 370
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
13-204 |
5.39e-105 |
|
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: 312.45 E-value: 5.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKE----AVQGIVIAPTRELAIQVGE 88
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKkkgrGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 89 ELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAI 168
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 446128740 169 LTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIK 204
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
3-369 |
2.24e-104 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 320.60 E-value: 2.24e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQG------IVI 76
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGrrpvraLIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 77 APTRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEM 156
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 157 LNMGFIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKKKFDVLTRLLD 236
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 237 IQSPELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFD 316
Cdd:PRK10590 242 KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446128740 317 IPQDPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDRMEAP 369
Cdd:PRK10590 322 LPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIP 374
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
2-343 |
1.24e-101 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 312.29 E-value: 1.24e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 2 TTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFgLP------LLDKVDTNKEAVQ--G 73
Cdd:PRK04837 8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF-LTatfhylLSHPAPEDRKVNQprA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 74 IVIAPTRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEA 153
Cdd:PRK04837 87 LIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 154 DEMLNMGFIEDIEAILTDVPDTHQ--TLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQ--FYLEVQEKKKfd 229
Cdd:PRK04837 167 DRMFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPSNEEKMR-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 230 VLTRLLDIQSPELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGV 309
Cdd:PRK04837 245 LLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAV 324
|
330 340 350
....*....|....*....|....*....|....
gi 446128740 310 THVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLF 343
Cdd:PRK04837 325 THVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
3-372 |
7.63e-101 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 309.83 E-value: 7.63e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTREL 82
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTREL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 83 AIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFI 162
Cdd:PTZ00424 109 AQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 163 EDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEV-QEKKKFDVLTRLLDIQSPE 241
Cdd:PTZ00424 189 GQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETLTIT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 242 LAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQDP 321
Cdd:PTZ00424 269 QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446128740 322 ESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDRMEAPTLD 372
Cdd:PTZ00424 349 ENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVAD 399
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
2-370 |
2.96e-93 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 292.59 E-value: 2.96e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 2 TTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTN---KEAVQG----I 74
Cdd:PRK01297 87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTpppKERYMGepraL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 75 VIAPTRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALK-KHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEA 153
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 154 DEMLNMGFIEDIEAILTDVP--DTHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKKKFDVL 231
Cdd:PRK01297 247 DRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 232 TRLLDIQSPELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTH 311
Cdd:PRK01297 327 YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446128740 312 VYNFDIPQDPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDRMEAPT 370
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPA 465
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
3-363 |
9.98e-92 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 291.47 E-value: 9.98e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDK-------VDTNKEAVQGIV 75
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRllsrpalADRKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 76 IAPTRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINR-KTLRLQNVETVVLDEAD 154
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 155 EMLNMGFIEDIEAILTDVPD--THQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKKKFDVLT 232
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 233 RLLDIQSPELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHV 312
Cdd:PRK04537 250 GLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYV 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446128740 313 YNFDIPQDPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKV 363
Cdd:PRK04537 330 YNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKI 380
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
1-363 |
3.35e-84 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 271.26 E-value: 3.35e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 1 MTTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQG-----IV 75
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGdgpivLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 76 IAPTRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADE 155
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 156 MLNMGFIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTE-PQHIKVKAKEVTM-PNIQQFYLEVQEKKKFDVLTR 233
Cdd:PTZ00110 289 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQEVFVVEEHEKRGKLKM 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 234 LLD--IQSPELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTH 311
Cdd:PTZ00110 369 LLQriMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKY 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446128740 312 VYNFDIPQDPESYVHRIGRTGRAGKKGIAMLFVTP---RESGQLKNIERTTKRKV 363
Cdd:PTZ00110 449 VINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPdkyRLARDLVKVLREAKQPV 503
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
3-204 |
4.54e-74 |
|
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: 233.36 E-value: 4.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTREL 82
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 83 AIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHI-NRKTLRLQNVETVVLDEADEMLNMGF 161
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADRLLNMDF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446128740 162 IEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIK 204
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 ... |
4-201 |
1.97e-70 |
|
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: 224.03 E-value: 1.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 4 FRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTRELA 83
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 84 IQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHI---NRKTLRLQNVETVVLDEADEMLNMG 160
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLrssDDTTKVLSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446128740 161 FIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQ 201
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
26-192 |
1.45e-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: 215.18 E-value: 1.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 26 TPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTRELAIQVGEELYKIGKHKRVRILPIY 105
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 106 GGQDINRQIRALKKhPHIIVGTPGRILDHInRKTLRLQNVETVVLDEADEMLNMGFIEDIEAILTDVPDTHQTLLFSATM 185
Cdd:pfam00270 81 GGDSRKEQLEKLKG-PDILVGTPGRLLDLL-QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 446128740 186 PDPIRRI 192
Cdd:pfam00270 159 PRNLEDL 165
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
3-344 |
5.83e-66 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 222.36 E-value: 5.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDT-------NKEAVQGIV 75
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTirsghpsEQRNPLAMV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 76 IAPTRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADE 155
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 156 MLNMGFIEDIEAILTDVPdTHQTLLFSATMPDPIRRIAERFMTEPqhIKVKAKEVTMPN--IQQFYLEVQEKKK----FD 229
Cdd:PLN00206 282 MLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDI--ILISIGNPNRPNkaVKQLAIWVETKQKkqklFD 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 230 VLTRLLDIQSPelAIVFGRTKRRVDELSEALNL-RGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISG 308
Cdd:PLN00206 359 ILKSKQHFKPP--AVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
|
330 340 350
....*....|....*....|....*....|....*.
gi 446128740 309 VTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLFV 344
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
4-203 |
2.05e-64 |
|
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: 208.31 E-value: 2.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 4 FRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTRELA 83
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 84 IQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIE 163
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446128740 164 DIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
6-203 |
4.91e-64 |
|
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: 207.18 E-value: 4.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 6 ELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTRELAIQ 85
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 86 VGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDI 165
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 446128740 166 EAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
3-197 |
1.03e-63 |
|
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: 206.95 E-value: 1.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAV----------Q 72
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 73 GIVIAPTRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDE 152
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446128740 153 ADEMLNMGFIEDIEAILTD----VPDTHQTLLFSATMPDPIRRIAERFM 197
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFL 209
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
13-204 |
7.76e-62 |
|
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: 201.33 E-value: 7.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKV---DTNKEAVQGIVIAPTRELAIQVGEE 89
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 90 LYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHI-NRKTLRLQNVETVVLDEADEMLNMGFIEDIEAI 168
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 446128740 169 LTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIK 204
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
215-344 |
1.47e-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: 195.42 E-value: 1.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 215 IQQFYLEVQEKKKFDVL-TRLLDIQSPELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEV 293
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446128740 294 LVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLFV 344
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
13-203 |
4.12e-60 |
|
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: 197.54 E-value: 4.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVD-----TNKEAVQG---IVIAPTRELAI 84
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlpplDEETKDDGpyaLILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 85 QVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIED 164
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446128740 165 IEAILTDVPDTH--------------------QTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17945 161 VTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
3-204 |
1.07e-58 |
|
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: 193.68 E-value: 1.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTN--KEAVQGIVIAPTR 80
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHspTVGARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 81 ELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMG 160
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446128740 161 FIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIK 204
Cdd:cd17959 162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
4-203 |
4.94e-58 |
|
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: 191.51 E-value: 4.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 4 FRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTRELA 83
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 84 IQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIE 163
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446128740 164 DIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
2-199 |
7.12e-58 |
|
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: 193.26 E-value: 7.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 2 TTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTN---------KEAVQ 72
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltassfseVQEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 73 GIVIAPTRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDE 152
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446128740 153 ADEMLNMGFIEDIEAILTD--VPDT--HQTLLFSATMPDPIRRIAERFMTE 199
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEpgMPSKedRQTLMFSATFPEEIQRLAAEFLKE 253
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
9-193 |
2.24e-57 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 190.10 E-value: 2.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 9 LSESLLQSVESMGFEEATPIQAETIPHALQ-GKDIIGQAQTGTGKTAAFGLPLLDKV-----DTNKEAVQGIVIAPTREL 82
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 83 AIQVGEELYK-IGKHKRVRILPIYGGQDINRQIRALKKH-PHIIVGTPGRILDHINRKTLR--LQNVETVVLDEADEMLN 158
Cdd:cd17964 81 ALQIAAEAKKlLQGLRKLRVQSAVGGTSRRAELNRLRRGrPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLD 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 446128740 159 MGFIEDIEAILTDVPDTH----QTLLFSATMPDPIRRIA 193
Cdd:cd17964 161 MGFRPDLEQILRHLPEKNadprQTLLFSATVPDEVQQIA 199
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
17-218 |
1.68e-56 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 187.70 E-value: 1.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 17 VESMGFEEATPIQAETIPHALQG-KDIIGQAQTGTGKTAAFGLPLLDKVDTNKeAVQGIVIAPTRELAIQVGEELYKIGK 95
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 96 HKRVRILPIYGGQDINRQIRALKK-HPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAILTDVPD 174
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESgKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446128740 175 THQTLLFSATMPDPIRRIAERFMTEPQHIKVkaKEVTMPNIQQF 218
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
9-206 |
2.01e-56 |
|
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: 187.01 E-value: 2.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 9 LSESLLQSVESMGFEEATPIQAETIPHALQG--KDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTRELAIQV 86
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 87 GEELYKIGKHKRVRI-LPIYGGQ-DINRQIRAlkkhpHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNM-GFIE 163
Cdd:cd17963 81 GEVVEKMGKFTGVKVaLAVPGNDvPRGKKITA-----QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446128740 164 DIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMtePQHIKVK 206
Cdd:cd17963 156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIA--PNANTIK 196
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
2-205 |
4.70e-56 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350708 [Multi-domain] Cd Length: 208 Bit Score: 186.78 E-value: 4.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 2 TTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTRE 81
Cdd:cd17950 2 SGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 82 LAIQVGEELYKIGKH-KRVRILPIYGGQDINRQIRALK-KHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEM--- 156
Cdd:cd17950 82 LAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleq 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446128740 157 LNMGfiEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIKV 205
Cdd:cd17950 162 LDMR--RDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
9-192 |
4.50e-53 |
|
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: 178.55 E-value: 4.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 9 LSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKE------AVQGIVIAPTREL 82
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAesgeeqGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 83 AIQVGEELYKIGKH--KRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQ-NVETVVLDEADEMLNM 159
Cdd:cd17961 81 AQQVSKVLEQLTAYcrKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLsTLKYLVIDEADLVLSY 160
|
170 180 190
....*....|....*....|....*....|...
gi 446128740 160 GFIEDIEAILTDVPDTHQTLLFSATMPDPIRRI 192
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEAL 193
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
1-203 |
2.54e-52 |
|
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: 177.18 E-value: 2.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 1 MTTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVD-----TNKEAVQGIV 75
Cdd:cd17953 11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKdqrpvKPGEGPIGLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 76 IAPTRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHI---NRKTLRLQNVETVVLDE 152
Cdd:cd17953 91 MAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446128740 153 ADEMLNMGFIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17953 171 ADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
13-203 |
2.56e-52 |
|
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: 176.41 E-value: 2.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLdkVDTNKEAVQG-------IVIAPTRELAIQ 85
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAI--VHINAQPPLErgdgpivLVLAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 86 VGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDI 165
Cdd:cd17966 79 IQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 446128740 166 EAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17966 159 RKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
4-203 |
6.95e-52 |
|
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: 175.35 E-value: 6.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 4 FRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTRELA 83
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 84 IQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIE 163
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446128740 164 DIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
13-203 |
2.39e-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: 173.76 E-value: 2.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQG-----IVIAPTRELAIQVG 87
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGegpiaVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 88 EELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEA 167
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 446128740 168 ILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
13-185 |
1.97e-50 |
|
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: 172.81 E-value: 1.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHAL-QGKDIIGQAQTGTGKTAAFGLP----LLDKVDTNKEA-----VQGIVIAPTREL 82
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPilerLLSQKSSNGVGgkqkpLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 83 AIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHI---NRKTLRLQNVETVVLDEADEMLNM 159
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIqegNEHLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 446128740 160 GFIEDIEAILTDVPDTH-------QTLLFSATM 185
Cdd:cd17946 161 GHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
13-204 |
7.70e-49 |
|
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: 167.37 E-value: 7.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKV-----DTNKEAVQGIVIAPTRELAIQVG 87
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 88 EELYKIGKH--KRVRILPIYGGQDINRQIRALKKH-PHIIVGTPGRILDHINRKTLRLQ--NVETVVLDEADEMLNMGFI 162
Cdd:cd17960 81 EVLQSFLEHhlPKLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446128740 163 EDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIK 204
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
6-205 |
1.38e-48 |
|
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: 166.70 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 6 ELGLSESllqsvesmGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNK----EAVQGIVIAPTRE 81
Cdd:cd17941 2 LKGLKEA--------GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERwtpeDGLGALIISPTRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 82 LAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALkKHPHIIVGTPGRILDHINRK-TLRLQNVETVVLDEADEMLNMG 160
Cdd:cd17941 74 LAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446128740 161 FIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIKV 205
Cdd:cd17941 153 FKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
13-203 |
1.45e-48 |
|
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: 166.49 E-value: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVD---TNKEAVQG---IVIAPTRELAIQV 86
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDlqpIPREQRNGpgvLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 87 GEELYKIgKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIE 166
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 446128740 167 AILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
13-204 |
3.36e-48 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 165.51 E-value: 3.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTRELAIQVGEELYK 92
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 93 IGKH-KRVRILPIYGGQDINRQIRALKKhPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAILTD 171
Cdd:cd17943 81 IGKKlEGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|...
gi 446128740 172 VPDTHQTLLFSATMPDPIRRIAERFMTEPQHIK 204
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
13-200 |
1.52e-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: 163.91 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKV--DTNKEAVQGIVIAPTRELAIQVGEEL 90
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 91 YKIGKHKRVRILPIYGGQ-DINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAIL 169
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
|
170 180 190
....*....|....*....|....*....|..
gi 446128740 170 TDVPDTH-QTLLFSATMPDPIRRIAERFMTEP 200
Cdd:cd17957 161 AACTNPNlQRSLFSATIPSEVEELARSVMKDP 192
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
1-199 |
1.34e-46 |
|
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: 162.90 E-value: 1.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 1 MTTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTN------------- 67
Cdd:cd18051 20 IETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslpsesgyy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 68 ---KEAVQGIVIAPTRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQN 144
Cdd:cd18051 100 grrKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDY 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446128740 145 VETVVLDEADEMLNMGFIEDIEAILT--DVPDT--HQTLLFSATMPDPIRRIAERFMTE 199
Cdd:cd18051 180 CKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPTgeRQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
13-203 |
1.84e-46 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 160.79 E-value: 1.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTRELAIQVGEELYK 92
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 93 IGK-HKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAILTD 171
Cdd:cd17962 81 LMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180 190
....*....|....*....|....*....|..
gi 446128740 172 VPDTHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
27-197 |
1.23e-45 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 158.86 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 27 PIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKE------AVQGIVIAPTRELAIQVGEELYKIGKhkRVR 100
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQprkrgrAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 101 ILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAILT-----DVPDT 175
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvsykkDSEDN 172
|
170 180
....*....|....*....|..
gi 446128740 176 HQTLLFSATMPDPIRRIAERFM 197
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
17-204 |
2.02e-45 |
|
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: 158.52 E-value: 2.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 17 VESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQ------GIVIAPTRELAIQVGEEL 90
Cdd:cd17949 6 KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 91 YKIGKhKRVRILP--IYGGQDINRQIRALKKHPHIIVGTPGRILDHI-NRKTLRLQNVETVVLDEADEMLNMGFIEDIEA 167
Cdd:cd17949 86 EKLLK-PFHWIVPgyLIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446128740 168 IL-----------TDVPDTH--QTLLFSATMPDPIRRIAERFMTEPQHIK 204
Cdd:cd17949 165 ILellddkrskagGEKSKPSrrQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
13-200 |
7.97e-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: 156.73 E-value: 7.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPL-LDKVDTNK-------EAVQGIVIAPTRELAI 84
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLiMFALEQEKklpfikgEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 85 QVGE------ELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLN 158
Cdd:cd17951 81 QTHEvieyycKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446128740 159 MGFIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEP 200
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 ... |
4-201 |
1.10e-43 |
|
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: 153.63 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 4 FRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLdkvdtnkEAVQGIVIAPTRELA 83
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-------QIVVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 84 IQVGEELYKIGKH---KRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMG 160
Cdd:cd17938 74 EQTYNCIENFKKYldnPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446128740 161 FIEDIEAILTDVP------DTHQTLLFSATMPDP-IRRIAERFMTEPQ 201
Cdd:cd17938 154 NLETINRIYNRIPkitsdgKRLQVIVCSATLHSFeVKKLADKIMHFPT 201
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
4-207 |
8.83e-43 |
|
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: 152.47 E-value: 8.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 4 FRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQG-----IVIAP 78
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGdgpicLVLAP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 79 TRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLN 158
Cdd:cd18049 106 TRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446128740 159 MGFIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIKVKA 207
Cdd:cd18049 186 MGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
14-184 |
1.21e-41 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 147.89 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 14 LQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLP---LLDKVD-TNKEAVQGIVIAPTRELAIQVGEE 89
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKfKPRNGTGVIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 90 LYKIGKHKRVRILPIYGGqdINRQIRA--LKKHPHIIVGTPGRILDHI-NRKTLRLQNVETVVLDEADEMLNMGFIEDIE 166
Cdd:cd17942 82 AKELLKYHSQTFGIVIGG--ANRKAEAekLGKGVNILVATPGRLLDHLqNTKGFLYKNLQCLIIDEADRILEIGFEEEMR 159
|
170
....*....|....*...
gi 446128740 167 AILTDVPDTHQTLLFSAT 184
Cdd:cd17942 160 QIIKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
3-211 |
6.41e-40 |
|
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: 144.39 E-value: 6.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQG--KDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTR 80
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 81 ELAIQVGEELYKIGKHKrVRILPIYGGQDiNRQIRALKKHPHIIVGTPGRILDHINR-KTLRLQNVETVVLDEADEMLNM 159
Cdd:cd18048 99 ELALQTGKVVEEMGKFC-VGIQVIYAIRG-NRPGKGTDIEAQIVIGTPGTVLDWCFKlRLIDVTNISVFVLDEADVMINV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446128740 160 -GFIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVT 211
Cdd:cd18048 177 qGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
1-205 |
1.69e-39 |
|
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: 144.77 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 1 MTTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQG-----IV 75
Cdd:cd18050 61 VFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 76 IAPTRELAIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADE 155
Cdd:cd18050 141 LAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADR 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446128740 156 MLNMGFIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIKV 205
Cdd:cd18050 221 MLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
226-335 |
2.28e-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: 125.40 E-value: 2.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 226 KKFDVLTRLLDIQSPELAIVFGRTKRRVDElSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLD 305
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 446128740 306 ISGVTHVYNFDIPQDPESYVHRIGRTGRAG 335
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
3-204 |
1.28e-29 |
|
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: 115.59 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQG--KDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQGIVIAPTR 80
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 81 ELAIQVGEELYKIGK-HKRVRILPIYGGQDINRQIRAlkkHPHIIVGTPGRILDH-INRKTLRLQNVETVVLDEADEML- 157
Cdd:cd18047 82 ELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKI---SEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIa 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446128740 158 NMGFIEDIEAILTDVPDTHQTLLFSATMPDPIRRIAERFMTEPQHIK 204
Cdd:cd18047 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
254-335 |
7.15e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 106.53 E-value: 7.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 254 DELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGR 333
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 446128740 334 AG 335
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
13-185 |
1.19e-27 |
|
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: 110.80 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQG---------KDIIGQAQTGTGKTAAFGLPLLDKVDTNKEA-VQGIVIAPTREL 82
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPrLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 83 AIQVGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPH--------IIVGTPGRILDHINRKT-LRLQNVETVVLDEA 153
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTPgFTLKHLRFLVIDEA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446128740 154 DEMLNMGFIE-------------------DIEAILTDVPDTH-QTLLFSATM 185
Cdd:cd17956 161 DRLLNQSFQDwletvmkalgrptapdlgsFGDANLLERSVRPlQKLLFSATL 212
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
13-220 |
1.18e-25 |
|
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: 105.14 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVQ-------GIVIAPTRELAIQ 85
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEgpfnaprGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 86 VGEELYKIGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDI 165
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 166 EAILTDVP-------DTH------QTLLFSATMPDPIRRIAERF--MTEPQHIKVKAKEVTMPNIQQFYL 220
Cdd:cd17948 161 SHFLRRFPlasrrseNTDgldpgtQLVLVSATMPSGVGEVLSKVidVDSIETVTSDKLHRLMPHVKQKFL 230
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
11-368 |
1.25e-19 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 91.74 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 11 ESLLQSVesMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLP--LLDKVdtnkeavqGIVIAPtreLaI---- 84
Cdd:COG0514 6 LEVLKRV--FGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLLPGL--------TLVVSP---L-Ialmk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 85 -QVgEELYKIG-----------KHKRVRILpiyggqdinRQIRA--LKkhphIIVGTPGRILDHINRKTLRLQNVETVVL 150
Cdd:COG0514 72 dQV-DALRAAGiraaflnsslsAEERREVL---------RALRAgeLK----LLYVAPERLLNPRFLELLRRLKISLFAI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 151 DEA--------D---EMLNMG-FIEDieaiLTDVPdthqTLLFSATMPDPIRR-IAERF-MTEPQHIKVKakeVTMPNIq 216
Cdd:COG0514 138 DEAhcisqwghDfrpDYRRLGeLRER----LPNVP----VLALTATATPRVRAdIAEQLgLEDPRVFVGS---FDRPNL- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 217 qfYLEVQEKKKFDVLTRLLDI---QSPELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEV 293
Cdd:COG0514 206 --RLEVVPKPPDDKLAQLLDFlkeHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 294 LVATdVA-ARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKN-IERTT---------KRK 362
Cdd:COG0514 284 IVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFfIEQSPpdeerkrveRAK 362
|
....*.
gi 446128740 363 VDRMEA 368
Cdd:COG0514 363 LDAMLA 368
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
3-186 |
1.18e-18 |
|
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: 85.51 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 3 TFRELGLSESLLQSVESMGFEEATPIQAETIP---------HALQGKDIIGQ-------AQTGTGKTAAFGLPLLDKVD- 65
Cdd:cd17965 9 SVREAIIKEILKGSNKTDEEIKPSPIQTLAIKkllktlmrkVTKQTSNEEPKlevfllaAETGSGKTLAYLAPLLDYLKr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 66 ----------------TNKEAVQGIVIAPTRELAIQVGEELYKIGKHKRVRILPIYG--GQDINRQIRALKKHPHIIVGT 127
Cdd:cd17965 89 qeqepfeeaeeeyesaKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSgfGPSYQRLQLAFKGRIDILVTT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446128740 128 PGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAILTDVPDTHQTLLFSATMP 186
Cdd:cd17965 169 PGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
213-343 |
9.63e-17 |
|
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: 76.86 E-value: 9.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 213 PNIqqfYLEVQEKKKFDVLTRLLDIQSP----ELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKE 288
Cdd:cd18794 2 PNL---FYSVRPKDKKDEKLDLLKRIKVehlgGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446128740 289 GAIEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLF 343
Cdd:cd18794 79 DKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
213-368 |
1.55e-16 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 82.45 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 213 PNIQqfYLEVQEKKKFDVLTRLLDIQSPELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIE 292
Cdd:PRK11057 211 PNIR--YTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQ 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 293 VLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLFVTP------------RESGQLKNIERttk 360
Cdd:PRK11057 289 IVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPadmawlrrcleeKPAGQQQDIER--- 365
|
....*...
gi 446128740 361 RKVDRMEA 368
Cdd:PRK11057 366 HKLNAMGA 373
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
39-184 |
4.06e-16 |
|
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: 75.52 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 39 GKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAVqgIVIAPTRELAIQVGEELYKIGKHKrVRILPIYGGQDINRQIRALK 118
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKV--LVLVPTKALALQTAERLRELFGPG-IRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446128740 119 KHPHIIVGTPGRILDHINR-KTLRLQNVETVVLDEADEML------NMGFIEDIEAILTDVpdthQTLLFSAT 184
Cdd:cd00046 78 GDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLidsrgaLILDLAVRKAGLKNA----QVILLSAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
48-330 |
4.21e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.14 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 48 TGTGKT--AAFglpLLDKVDTNKEAvqgIVIAPTRELAIQVGEELykigkhKRVRILPIYGGQDINRqiralkkHPHIIV 125
Cdd:COG1061 109 TGTGKTvlALA---LAAELLRGKRV---LVLVPRRELLEQWAEEL------RRFLGDPLAGGGKKDS-------DAPITV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 126 GTPGRILDHINRKTLRlQNVETVVLDEADEMLNMGFiediEAILTDVPDTHqTLLFSATmpdPIRR-------------- 191
Cdd:COG1061 170 ATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTAT---PFRSdgreillflfdgiv 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 192 --------IAERFMTEPQHIKVkakEVTMPNIQQFY----------LEVQEKKKFDVLTRLLD-IQSPELAIVFGRTKRR 252
Cdd:COG1061 241 yeyslkeaIEDGYLAPPEYYGI---RVDLTDERAEYdalserlreaLAADAERKDKILRELLReHPDDRKTLVFCSSVDH 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446128740 253 VDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGR 330
Cdd:COG1061 318 AEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGR 395
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
8-342 |
2.44e-13 |
|
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: 72.56 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 8 GLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAvQGIVIAPTRELAI-QV 86
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA-TALYLYPTKALARdQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 87 GE--ELYKIGKhKRVRILPIYGgqDINRQIR-ALKKHPHIIVGTPgrilDHINRKTLR--------LQNVETVVLDEADe 155
Cdd:COG1205 119 RRlrELAEALG-LGVRVATYDG--DTPPEERrWIREHPDIVLTNP----DMLHYGLLPhhtrwarfFRNLRYVVIDEAH- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 156 mlnmgfiedieaILTDVPDTHQTLLFsatmpDPIRRIAERFMTEPQHIKVKAkevTMPNIQQF--------YLEVQE--- 224
Cdd:COG1205 191 ------------TYRGVFGSHVANVL-----RRLRRICRHYGSDPQFILASA---TIGNPAEHaerltgrpVTVVDEdgs 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 225 ---KKKF---------------------DVLTRLL--DIQSpelaIVFGR-----------TKRRVDELSEALNLRGYaa 267
Cdd:COG1205 251 prgERTFvlwnpplvddgirrsalaeaaRLLADLVreGLRT----LVFTRsrrgaellaryARRALREPDLADRVAAY-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 268 egiHGDLTQAKRMSVLRKFKEGAIEVLVAT-------DVAarGLD---ISGvthvynfdIPQDPESYVHRIGRTGRAGKK 337
Cdd:COG1205 325 ---RAGYLPEERREIERGLRSGELLGVVSTnalelgiDIG--GLDavvLAG--------YPGTRASFWQQAGRAGRRGQD 391
|
....*
gi 446128740 338 GIAML 342
Cdd:COG1205 392 SLVVL 396
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
227-329 |
3.77e-11 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 60.95 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 227 KFDVLTRLLD--IQSPELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKE--GAIEVLVATDVAAR 302
Cdd:cd18793 12 KLEALLELLEelREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 446128740 303 GLDISGVTHVYNFDIPQDP------ESYVHRIG 329
Cdd:cd18793 92 GLNLTAANRVILYDPWWNPaveeqaIDRAHRIG 124
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
230-342 |
9.18e-11 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 64.37 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 230 VLTRLLDIQSPELAIVFGRTKRRVDELSEALNLRGYAAE------GIHGD--LTQAKRMSVLRKFKEGAIEVLVATDVAA 301
Cdd:COG1111 343 ILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAE 422
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446128740 302 RGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAML 342
Cdd:COG1111 423 EGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGRVVVL 463
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
273-342 |
6.98e-10 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 57.22 E-value: 6.98e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 273 DLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAML 342
Cdd:cd18802 73 LMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSKYILMV 142
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
227-440 |
5.35e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 58.73 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 227 KFDVLTRL----LDIQSPELAIVFGRTKRRVDELSEALNLRGYAAEGIHGD--------LTQAKRMSVLRKFKEGAIEVL 294
Cdd:PRK13766 348 KLEKLREIvkeqLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 295 VATDVAARGLDISGVTHVYNFD-IPQDPESyVHRIGRTGRaGKKGIAMLFVT--PRESGQLknieRTTKRKVDRMEaptl 371
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEGRVVVLIAkgTRDEAYY----WSSRRKEKKMK---- 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446128740 372 dEALEGQQRLIAEKLQSTIENDNLSYYKRIAEEMLEENDSVTVVAAALKMMTKEPDTTPIALTSEPPVV 440
Cdd:PRK13766 498 -EELKNLKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKDKETEEDEPEGPKI 565
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
29-153 |
1.27e-08 |
|
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: 54.51 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 29 QAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAvQGIVIAPTRELAIQVGEELYKI--GKHKRVRILPIYG 106
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGS-RALYLYPTKALAQDQLRSLRELleQLGLGIRVATYDG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446128740 107 GQDINRQIRALKKHPHIIVGTPGR----ILDHINRKTLRLQNVETVVLDEA 153
Cdd:cd17923 84 DTPREERRAIIRNPPRILLTNPDMlhyaLLPHHDRWARFLRNLRYVVLDEA 134
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
227-331 |
1.34e-08 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 57.54 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 227 KFDVLTRLLD--IQSPELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEG--AIEVLVATDVAAR 302
Cdd:COG0553 534 KLEALLELLEelLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAGGE 613
|
90 100 110
....*....|....*....|....*....|....*
gi 446128740 303 GLDISGVTHVYNFDIPQDPESY------VHRIGRT 331
Cdd:COG0553 614 GLNLTAADHVIHYDLWWNPAVEeqaidrAHRIGQT 648
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
45-337 |
1.67e-08 |
|
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: 56.31 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 45 QAQTGTGKTAAFGLPLLDKVDtNKEAVQGIVIAPTRELAIQVGEELYKIGKHKRVRILPIYGGQDIN--------RQIRA 116
Cdd:TIGR01587 5 EAPTGYGKTEAALLWALHSIK-SQKADRVIIALPTRATINAMYRRAKELFGSELVGLHHSSSFSRIKemgdseefEHLFP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 117 LKKHPH-------IIVGTP-------GRILDHINRKTLRLQNvETVVLDEAD--EMLNMGFIEDIEAILTDVPDTHqtLL 180
Cdd:TIGR01587 84 LYIHSNdklfldpITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHfyDEYTLALILAVLEVLKDNDVPI--LL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 181 FSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKK-KFDVLTRLLD-IQSPELAIVFGRTKRRVDELSE 258
Cdd:TIGR01587 161 MSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVgEISSLERLLEfIKKGGSIAIIVNTVDRAQEFYQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 259 ALNLRGYAAEGI--HGDLTQAKR-----MSVLRKFKEGAIEVLVATDVAARGLDISgvthvynFDI----PQDPESYVHR 327
Cdd:TIGR01587 241 QLKEKAPEEEIIlyHSRFTEKDRakkeaELLREMKKSNEKFVIVATQVIEASLDIS-------ADVmiteLAPIDSLIQR 313
|
330
....*....|
gi 446128740 328 IGRTGRAGKK 337
Cdd:TIGR01587 314 LGRLHRYGRK 323
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
291-344 |
2.13e-08 |
|
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: 51.17 E-value: 2.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446128740 291 IEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKK-GIAMLFV 344
Cdd:cd18785 23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDeGEVILFV 77
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
227-338 |
2.49e-08 |
|
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: 53.02 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 227 KFDVLTRLLDIQSP-ELAIVFGRTKRRVDELSEALNlrgyaAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLD 305
Cdd:cd18789 35 KLRALEELLKRHEQgDKIIVFTDNVEALYRYAKRLL-----KPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGID 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446128740 306 IsgvthvynfdipqdPES---------------YVHRIGRTGRAGKKG 338
Cdd:cd18789 110 L--------------PEAnvaiqisghggsrrqEAQRLGRILRPKKGG 143
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
266-343 |
3.40e-08 |
|
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: 52.36 E-value: 3.40e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446128740 266 AAEGIHGdLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLF 343
Cdd:cd18801 67 SGKSSKG-MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQGRVVVLL 143
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
45-345 |
6.89e-08 |
|
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: 54.36 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 45 QAQTGTGKTAAfGLPLLDKVDTNKEAVQGIVIAPTRELAIQVGEELYKIGKHKRVRILPI-------YGGQDINRQIRAL 117
Cdd:cd09639 5 EAPTGYGKTEA-ALLWALHSLKSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSIlssrikeMGDSEEFEHLFPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 118 KKHPH-------IIVGTP-------GRILDHINRKTLRLQNvETVVLDEAD--EMLNMGFIEDIEAILTDVPDTHqtLLF 181
Cdd:cd09639 84 YIHSNdtlfldpITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHfyDEYTLALILAVLEVLKDNDVPI--LLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 182 SATMPdpirriaERFMTEPQHIKVKAKEVTMPNI----QQFYLEVQEKK-KFDVLTRLLD-IQSPELAIVFGRTKRRVDE 255
Cdd:cd09639 161 SATLP-------KFLKEYAEKIGYVEENEPLDLKpnerAPFIKIESDKVgEISSLERLLEfIKKGGSVAIIVNTVDRAQE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 256 LSEALNLRGYAAEG--IHGDLTQA----KRMSVLRKFKEGAIEVLVATDVAARGLDISgvthvynFDI----PQDPESYV 325
Cdd:cd09639 234 FYQQLKEKGPEEEImlIHSRFTEKdrakKEAELLLEFKKSEKFVIVATQVIEASLDIS-------VDVmiteLAPIDSLI 306
|
330 340
....*....|....*....|
gi 446128740 326 HRIGRTGRAGKKGIAMLFVT 345
Cdd:cd09639 307 QRLGRLHRYGEKNGEEVYII 326
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
22-156 |
4.57e-06 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 49.50 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 22 FEEATPIQAETIPHALQGKDIIGQAQTGTGKT-AAF-----GLPLLDKVDTNKEAVQGIVIAPTRELA--IQVG-----E 88
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFlaiidELFRLGREGELEDKVYCLYVSPLRALNndIHRNleeplT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 89 ELYKIGKHKRVRILPI-----YGGQDINRQIRALKKHPHIIVGTPgrildhinrKTL-----------RLQNVETVVLDE 152
Cdd:PRK13767 110 EIREIAKERGEELPEIrvairTGDTSSYEKQKMLKKPPHILITTP---------ESLaillnspkfreKLRTVKWVIVDE 180
|
....
gi 446128740 153 ADEM 156
Cdd:PRK13767 181 IHSL 184
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
39-157 |
5.34e-06 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 46.81 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 39 GKDIIGQAQTGTGKTAAFGLPLLDKV-DTNKEAVQGIVIAPTRELAIQVGEELYKIGKHKR--VRILPIYGgqDINRQIR 115
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPLDEIDleIPVAVRHG--DTSQSEK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446128740 116 A--LKKHPHIIVGTPGRILDHINRKTLR--LQNVETVVLDEADEML 157
Cdd:cd17922 79 AkqLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDEIHALL 124
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
11-204 |
1.26e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 45.99 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 11 ESLLQSVesMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLP--LLDKVdtnkeavqGIVIAPTreLAI---Q 85
Cdd:cd17920 1 EQILKEV--FGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV--------TLVVSPL--ISLmqdQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 86 VgEELykigKHKRVRILPIYGGQDIN--RQIRALKKHP--HIIVGTP-----GRILDHINRKTLRLQnVETVVLDEA--- 153
Cdd:cd17920 69 V-DRL----QQLGIRAAALNSTLSPEekREVLLRIKNGqyKLLYVTPerllsPDFLELLQRLPERKR-LALIVVDEAhcv 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446128740 154 --------DEMLNMGfieDIEAILTDVPdthqTLLFSATMPDPIRR-IAER-FMTEPQHIK 204
Cdd:cd17920 143 sqwghdfrPDYLRLG---RLRRALPGVP----ILALTATATPEVREdILKRlGLRNPVIFR 196
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
249-333 |
2.08e-05 |
|
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: 44.93 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 249 TKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFD-----IPQDPES 323
Cdd:cd18790 36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSETS 115
|
90
....*....|
gi 446128740 324 YVHRIGRTGR 333
Cdd:cd18790 116 LIQTIGRAAR 125
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
46-411 |
7.29e-05 |
|
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: 45.46 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 46 AQTGTGKT---AAFGLPLLDKVDTNKeavqGIVIAPTRELAIQVGEELYKIGK------HKRVRILPIYGGQDINRQIRA 116
Cdd:COG1203 154 APTGGGKTeaaLLFALRLAAKHGGRR----IIYALPFTSIINQTYDRLRDLFGedvllhHSLADLDLLEEEEEYESEARW 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 117 LKKH------PhIIVGTPGRILD-------HINRKTLRLQN-VetVVLDEAD----EMLNMgfiedIEAILTDVPDTHQT 178
Cdd:COG1203 230 LKLLkelwdaP-VVVTTIDQLFEslfsnrkGQERRLHNLANsV--IILDEVQayppYMLAL-----LLRLLEWLKNLGGS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 179 LLF-SATMPDPIRriaeRFMTEPQHIKVKAKEVTMPNIQQFY---LEVQEKKKF--DVLTRLLDIQSPE---LAIVfgRT 249
Cdd:COG1203 302 VILmTATLPPLLR----EELLEAYELIPDEPEELPEYFRAFVrkrVELKEGPLSdeELAELILEALHKGksvLVIV--NT 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 250 KRRVDELSEALNLRGyAAEGI---HGDLTQAKRMSVLRK----FKEGAIEVLVATDVAARGLDISgvthvynFDI----P 318
Cdd:COG1203 376 VKDAQELYEALKEKL-PDEEVyllHSRFCPADRSEIEKEikerLERGKPCILVSTQVVEAGVDID-------FDVvirdL 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 319 QDPESYVHRIGRT---GRAGKKGIAMLFVTPRESGQL----KNIERTtkrkvdrmeaptlDEALEGQQRLIAEKLQSTIE 391
Cdd:COG1203 448 APLDSLIQRAGRCnrhGRKEEEGNVYVFDPEDEGGGYvydkPLLERT-------------RELLREHDEILPEDKRELIE 514
|
410 420
....*....|....*....|
gi 446128740 392 ndnlSYYKRIAEEMLEENDS 411
Cdd:COG1203 515 ----EYYRELYELLPDELDS 530
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
270-349 |
3.30e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 41.18 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 270 IHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVynfdIPQDPE----SYVHRI-GRTGRAGKKGIAMLFV 344
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVM----VIEDAErfglSQLHQLrGRVGRGDHQSYCLLVY 142
|
....*
gi 446128740 345 TPRES 349
Cdd:cd18811 143 KDPLT 147
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
270-368 |
4.44e-04 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 41.10 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 270 IHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVynfdIPQDPE----SYVHRI-GRTGRAGKKGIAMLFV 344
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTM----IIEDADrfglSQLHQLrGRVGRGKHQSYCYLLY 141
|
90 100
....*....|....*....|....
gi 446128740 345 TPRESgqlknierTTKRKVDRMEA 368
Cdd:cd18792 142 PDPKK--------LTETAKKRLRA 157
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
219-345 |
5.07e-04 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 40.61 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 219 YLEVQEKKKF--DVLTRLLDIQSPEL--AIVFGRTKRRVDELseALNLRGYAAegIHGDLTQAKRMSVLRKFKEGAIEVL 294
Cdd:cd18795 18 KLRVDVMNKFdsDIIVLLKIETVSEGkpVLVFCSSRKECEKT--AKDLAGIAF--HHAGLTREDRELVEELFREGLIKVL 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446128740 295 VATDVAARGLD-------ISGVTHvYNFDIPQD-PESYVHR-IGRTGRAGK--KGIAMLFVT 345
Cdd:cd18795 94 VATSTLAAGVNlpartviIKGTQR-YDGKGYRElSPLEYLQmIGRAGRPGFdtRGEAIIMTK 154
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
241-343 |
5.32e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 42.96 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 241 ELAIVFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQD 320
Cdd:PLN03137 681 ECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKS 760
|
90 100
....*....|....*....|...
gi 446128740 321 PESYVHRIGRTGRAGKKGIAMLF 343
Cdd:PLN03137 761 IEGYHQECGRAGRDGQRSSCVLY 783
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
270-368 |
6.05e-04 |
|
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: 40.40 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 270 IHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRI-GRTGRAGKKGIAMLFVTPRE 348
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYAYFLYPDQK 136
|
90 100
....*....|....*....|
gi 446128740 349 SgqlknierTTKRKVDRMEA 368
Cdd:cd18810 137 K--------LTEDALKRLEA 148
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
28-218 |
1.66e-03 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 40.03 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 28 IQAETIPHALQG-KDIIGQAQTGTGKTAAFGLPLL----DKVDTNKEAVQGIVIAPTRELAiqvgEELYKIGKHK----R 98
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILrllkERNPLPWGNRKVVYIAPIKALC----SEKYDDWKEKfgplG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 99 VRILPIYGGQDINRQIRAlkKHPHIIVGTPGRiLDHINRKTLRLQN-VETVVLDEADEMLNMGFIED--IEAILTDVPDT 175
Cdd:cd18023 81 LSCAELTGDTEMDDTFEI--QDADIILTTPEK-WDSMTRRWRDNGNlVQLVALVLIDEVHIIKENRGatLEVVVSRMKTL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446128740 176 HqtlLFSATMPDPIRRIaeRFmtepqhIKVKAkevTMPNIQQF 218
Cdd:cd18023 158 S---SSSELRGSTVRPM--RF------VAVSA---TIPNIEDL 186
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
244-336 |
1.75e-03 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 39.17 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 244 IVFGRTKRRVDELSEALN-LRGYAAEGI-----HGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDI 317
Cdd:cd18796 42 LVFTNTRSQAERLAQRLReLCPDRVPPDfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90
....*....|....*....
gi 446128740 318 PQDPESYVHRIGRTGRAGK 336
Cdd:cd18796 122 PKSVARLLQRLGRSGHRPG 140
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
45-175 |
2.32e-03 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 39.32 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 45 QAQTGTGKTAAFGLPLLDKVDTNKeavQGIVIAPTRELAIQVGEELYKigKHKRVRILPIYGG--QDINRQIralkkhpH 122
Cdd:cd17918 42 SGDVGSGKTLVALGAALLAYKNGK---QVAILVPTEILAHQHYEEARK--FLPFINVELVTGGtkAQILSGI-------S 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446128740 123 IIVGTPGRIldHINRKTLrlqNVETVVLDEA--------DEMLNMGFIEDIEAILTDVPDT 175
Cdd:cd17918 110 LLVGTHALL--HLDVKFK---NLDLVIVDEQhrfgvaqrEALYNLGATHFLEATATPIPRT 165
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
27-194 |
3.14e-03 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 38.85 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 27 PIQAETIPHAL-QGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKEAvqgIVIAPTRELAIQVGEE---LYKIGkhkrVRIL 102
Cdd:cd18028 4 PPQAEAVRAGLlKGENLLISIPTASGKTLIAEMAMVNTLLEGGKA---LYLVPLRALASEKYEEfkkLEEIG----LKVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 103 PIYGgqDINRQIRALKKHpHIIVGTPGRiLDHINR-KTLRLQNVETVVLDE---ADEMLNMGFIEDIEAILTDVPDTHQT 178
Cdd:cd18028 77 ISTG--DYDEDDEWLGDY-DIIVATYEK-FDSLLRhSPSWLRDVGVVVVDEihlISDEERGPTLESIVARLRRLNPNTQI 152
|
170
....*....|....*.
gi 446128740 179 LLFSATMPDPiRRIAE 194
Cdd:cd18028 153 IGLSATIGNP-DELAE 167
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
244-342 |
4.55e-03 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 37.62 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 244 IVFGRTKRRVD----ELSEALNLRGYAAEGI---HGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFD 316
Cdd:cd18797 39 IVFCRSRKLAElllrYLKARLVEEGPLASKVasyRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*.
gi 446128740 317 IPQDPESYVHRIGRTGRAGKKGIAML 342
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
250-349 |
5.09e-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: 38.05 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 250 KRRVDELSEALNLRGYAAEGIHgdltqAKRMSVLRKFKEGAIEVLVAT----DVAARGLDISG-VTHVYNFDIPqdPESY 324
Cdd:cd18798 37 KEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLPErIKYAIFYGVP--VTTY 109
|
90 100
....*....|....*....|....*....
gi 446128740 325 VHRIGRTGR--AG--KKGIAMLFVTPRES 349
Cdd:cd18798 110 IQASGRTSRlyAGglTKGLSVVLVDDPEL 138
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
6-408 |
5.76e-03 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 39.42 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 6 ELGLSESLLQSVESMGFEEATPIQAETIPH-ALQGKDIIGQAQTGTGKTAAFGLPLLDKVdtNKEAVQGIVIAPTRELAi 84
Cdd:PRK00254 5 ELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKL--LREGGKAVYLVPLKALA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 85 qvgEELYKIGKH-KRVRILPIYGGQDINRQIRALKKHpHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIE 163
Cdd:PRK00254 82 ---EEKYREFKDwEKLGLRVAMTTGDYDSTDEWLGKY-DIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 164 DIEAILTDVPDTHQTLLFSATMPDPIRRI----AERFMTEPQHIKVK--------------AKEVTMPNIQQFYLEVQEK 225
Cdd:PRK00254 158 TLEMILTHMLGRAQILGLSATVGNAEELAewlnAELVVSDWRPVKLRkgvfyqgflfwedgKIERFPNSWESLVYDAVKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 226 KK----FDVLTRLLDIQSPELAIVFGR-----TKRRVDELSEALN-----------LRGYAAEGiHGDLTQAKRMSVLRK 285
Cdd:PRK00254 238 GKgalvFVNTRRSAEKEALELAKKIKRfltkpELRALKELADSLEenptneklkkaLRGGVAFH-HAGLGRTERVLIEDA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446128740 286 FKEGAIEVLVATDVAARGLD-------ISGVTHVYNFDIPQDPESYVHR-IGRTGRA--GKKGIAMLFVTPRESGQLknI 355
Cdd:PRK00254 317 FREGLIKVITATPTLSAGINlpafrviIRDTKRYSNFGWEDIPVLEIQQmMGRAGRPkyDEVGEAIIVATTEEPSKL--M 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446128740 356 ERTTKRKVDRMEAPTLDE-ALEGQ-QRLIA-------EKLQSTIENdNLSYYKRIAEEMLEE 408
Cdd:PRK00254 395 ERYIFGKPEKLFSMLSNEsAFRSQvLALITnfgvsnfKELVNFLER-TFYAHQRKDLYSLEE 455
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
29-153 |
7.32e-03 |
|
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: 38.02 E-value: 7.32e-03
10 20 30 40 50 60 70 80
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gi 446128740 29 QAETIPHALQgKDIIGQAQTGTGKT--AAFGL-PLLDKVDTNKEAVQGIV-IAPTRELAIQVGEElykIGKHKRVRILPI 104
Cdd:cd18034 7 QLELFEAALK-RNTIVVLPTGSGKTliAVMLIkEMGELNRKEKNPKKRAVfLVPTVPLVAQQAEA---IRSHTDLKVGEY 82
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90 100 110 120 130
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gi 446128740 105 YGGQDINRQIR-----ALKKHpHIIVGTPGRILDHINRKTLRLQNVETVVLDEA 153
Cdd:cd18034 83 SGEMGVDKWTKerwkeELEKY-DVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
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