|
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: 624.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 1 MTTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTN-KDAVQGIVIAPT 79
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 80 RELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNM 159
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 160 GFIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKKKFDVLTRLLDIQS 239
Cdd:COG0513 161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 240 PELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQ 319
Cdd:COG0513 241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 320 DPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDRMEAPTLDEALEGQQRLIAEKLQSTIENDNLSYYK 399
Cdd:COG0513 321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGG 400
|
.
gi 228652232 400 R 400
Cdd:COG0513 401 R 401
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-372 |
1.41e-152 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 444.24 E-value: 1.41e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 1 MTTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTR 80
Cdd:PRK11776 3 MTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 81 ELAIQVGEELYKLGKHKR-VRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNM 159
Cdd:PRK11776 83 ELADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 160 GFIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTmPNIQQFYLEVQEKKKFDVLTRLLDIQS 239
Cdd:PRK11776 163 GFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEVSPDERLPALQRLLLHHQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 240 PELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQ 319
Cdd:PRK11776 242 PESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELAR 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 228652232 320 DPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDRMEAPTLD 372
Cdd:PRK11776 322 DPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLS 374
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
2-439 |
5.01e-151 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 446.60 E-value: 5.01e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 2 TTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTRE 81
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 82 LAIQVGEELYKLGKHKR-VRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMG 160
Cdd:PRK11634 86 LAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 161 FIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKKKFDVLTRLLDIQSP 240
Cdd:PRK11634 166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 241 ELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQD 320
Cdd:PRK11634 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 321 PESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDRMEAPTLDeaLEGQQRL--IAEKLQSTIENDNLSYY 398
Cdd:PRK11634 326 SESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAE--LLGKRRLekFAAKVQQQLESSDLDQY 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 228652232 399 KRI-----AEEMLEENDSVTVVAAALKMMTKEpdtTPIALTSEPPV 439
Cdd:PRK11634 404 RALlakiqPTAEGEELDLETLAAALLKMAQGE---RPLILPPDAPM 446
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
2-365 |
1.06e-106 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 326.13 E-value: 1.06e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 2 TTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLP----LLDKVDTNKDAVQGIVIA 77
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPalqhLLDFPRRKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 78 PTRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEML 157
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 158 NMGFIEDIEAILTDVPETHQTLLFSATMP-DPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKK-KFDVLTRLL 235
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEhKTALLCHLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 236 DIQSPELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNF 315
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 228652232 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 |
1.94e-106 |
|
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: 316.69 E-value: 1.94e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNK----DAVQGIVIAPTRELAIQVGE 88
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 89 ELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAI 168
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 228652232 169 LTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIK 204
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
3-369 |
4.38e-103 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 317.52 E-value: 4.38e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQG------IVI 76
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGrrpvraLIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 77 APTRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEM 156
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 157 LNMGFIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKKKFDVLTRLLD 236
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 237 IQSPELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFD 316
Cdd:PRK10590 242 KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 228652232 317 IPQDPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDRMEAP 369
Cdd:PRK10590 322 LPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIP 374
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
3-372 |
4.13e-102 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 313.30 E-value: 4.13e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTREL 82
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTREL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 83 AIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFI 162
Cdd:PTZ00424 109 AQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 163 EDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEV-QEKKKFDVLTRLLDIQSPE 241
Cdd:PTZ00424 189 GQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETLTIT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 242 LAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQDP 321
Cdd:PTZ00424 269 QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 228652232 322 ESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDRMEAPTLD 372
Cdd:PTZ00424 349 ENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVAD 399
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
2-343 |
1.29e-101 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 312.68 E-value: 1.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 2 TTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFgLP------LLDKVDTNKDAVQ--G 73
Cdd:PRK04837 8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF-LTatfhylLSHPAPEDRKVNQprA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 74 IVIAPTRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEA 153
Cdd:PRK04837 87 LIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 154 DEMLNMGFIEDIEAILTDVPETHQ--TLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQ--FYLEVQEKKKfd 229
Cdd:PRK04837 167 DRMFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPSNEEKMR-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 230 VLTRLLDIQSPELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGV 309
Cdd:PRK04837 245 LLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAV 324
|
330 340 350
....*....|....*....|....*....|....
gi 228652232 310 THVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLF 343
Cdd:PRK04837 325 THVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
2-370 |
1.41e-93 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 293.74 E-value: 1.41e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 2 TTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTN---KDAVQG----I 74
Cdd:PRK01297 87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTpppKERYMGepraL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 75 VIAPTRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALK-KHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEA 153
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 154 DEMLNMGFIEDIEAILTDVP--ETHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKKKFDVL 231
Cdd:PRK01297 247 DRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 232 TRLLDIQSPELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTH 311
Cdd:PRK01297 327 YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 228652232 312 VYNFDIPQDPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKVDRMEAPT 370
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPA 465
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
3-363 |
6.82e-91 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 289.54 E-value: 6.82e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDK-------VDTNKDAVQGIV 75
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRllsrpalADRKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 76 IAPTRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINR-KTLRLQNVETVVLDEAD 154
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 155 EMLNMGFIEDIEAILTDVPE--THQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKKKFDVLT 232
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 233 RLLDIQSPELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHV 312
Cdd:PRK04537 250 GLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYV 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 228652232 313 YNFDIPQDPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKNIERTTKRKV 363
Cdd:PRK04537 330 YNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKI 380
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
1-363 |
5.74e-84 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 270.88 E-value: 5.74e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 1 MTTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQG-----IV 75
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGdgpivLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 76 IAPTRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADE 155
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 156 MLNMGFIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTE-PQHIKVKAKEVTM-PNIQQFYLEVQEKKKFDVLTR 233
Cdd:PTZ00110 289 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQEVFVVEEHEKRGKLKM 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 234 LLD--IQSPELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTH 311
Cdd:PTZ00110 369 LLQriMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKY 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 228652232 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 |
1.66e-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: 234.90 E-value: 1.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTREL 82
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 83 AIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHI-NRKTLRLQNVETVVLDEADEMLNMGF 161
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADRLLNMDF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 228652232 162 IEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIK 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 |
4.11e-71 |
|
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: 225.95 E-value: 4.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 4 FRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTRELA 83
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 84 IQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHI---NRKTLRLQNVETVVLDEADEMLNMG 160
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLrssDDTTKVLSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 228652232 161 FIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQ 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 |
7.18e-69 |
|
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: 218.65 E-value: 7.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 26 TPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTRELAIQVGEELYKLGKHKRVRILPIY 105
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 106 GGQDINRQIRALKKhPHIIVGTPGRILDHInRKTLRLQNVETVVLDEADEMLNMGFIEDIEAILTDVPETHQTLLFSATM 185
Cdd:pfam00270 81 GGDSRKEQLEKLKG-PDILVGTPGRLLDLL-QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 228652232 186 PDPIRRI 192
Cdd:pfam00270 159 PRNLEDL 165
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
4-203 |
4.45e-66 |
|
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: 212.93 E-value: 4.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 4 FRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTRELA 83
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 84 IQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIE 163
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 228652232 164 DIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
3-344 |
8.80e-66 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 221.97 E-value: 8.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLL--------DKVDTNKDAVqGI 74
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsrcctirsGHPSEQRNPL-AM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 75 VIAPTRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEAD 154
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 155 EMLNMGFIEDIEAILTDVPeTHQTLLFSATMPDPIRRIAERFMTEPqhIKVKAKEVTMPN--IQQFYLEVQEKKK----F 228
Cdd:PLN00206 281 CMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDI--ILISIGNPNRPNkaVKQLAIWVETKQKkqklF 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 229 DVLTRLLDIQSPelAIIFGRTKRRVDELSEALNL-RGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDIS 307
Cdd:PLN00206 358 DILKSKQHFKPP--AVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLL 435
|
330 340 350
....*....|....*....|....*....|....*..
gi 228652232 308 GVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLFV 344
Cdd:PLN00206 436 RVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
6-203 |
5.55e-65 |
|
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: 209.87 E-value: 5.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 6 ELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTRELAIQ 85
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 86 VGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDI 165
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 228652232 166 EAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHI 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-64 |
|
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: 210.04 E-value: 1.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAV----------Q 72
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 73 GIVIAPTRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDE 152
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 228652232 153 ADEMLNMGFIEDIEAILTD----VPETHQTLLFSATMPDPIRRIAERFM 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 |
4.04e-63 |
|
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350705 [Multi-domain] Cd Length: 196 Bit Score: 204.80 E-value: 4.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKV---DTNKDAVQGIVIAPTRELAIQVGEE 89
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 90 LYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHI-NRKTLRLQNVETVVLDEADEMLNMGFIEDIEAI 168
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 228652232 169 LTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIK 204
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
13-203 |
1.78e-61 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 201.39 E-value: 1.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVD-----TNKDAVQG---IVIAPTRELAI 84
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlpplDEETKDDGpyaLILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 85 QVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIED 164
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 228652232 165 IEAILTDVPETH--------------------QTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17945 161 VTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
215-344 |
1.69e-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: 195.80 E-value: 1.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 215 IQQFYLEVQEKKKFDVL-TRLLDIQSPELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEV 293
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 228652232 294 LVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLFV 344
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
3-204 |
1.75e-59 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 195.60 E-value: 1.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTN--KDAVQGIVIAPTR 80
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHspTVGARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 81 ELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMG 160
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 228652232 161 FIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIK 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 |
6.40e-59 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 194.20 E-value: 6.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 4 FRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTRELA 83
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 84 IQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIE 163
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 228652232 164 DIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
9-193 |
2.81e-58 |
|
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: 192.80 E-value: 2.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 9 LSESLLQSVESMGFEEATPIQAETIPHALQ-GKDIIGQAQTGTGKTAAFGLPLLDKV-----DTNKDAVQGIVIAPTREL 82
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 83 AIQVGEELYKL-GKHKRVRILPIYGGQDINRQIRALKKH-PHIIVGTPGRILDHINRKTLR--LQNVETVVLDEADEMLN 158
Cdd:cd17964 81 ALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRRGrPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEADRLLD 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 228652232 159 MGF---IEDIEAILTDVPETH-QTLLFSATMPDPIRRIA 193
Cdd:cd17964 161 MGFrpdLEQILRHLPEKNADPrQTLLFSATVPDEVQQIA 199
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
2-199 |
8.70e-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: 8.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 2 TTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTN---------KDAVQ 72
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltassfseVQEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 73 GIVIAPTRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDE 152
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 228652232 153 ADEMLNMGFIEDIEAILTD--VP--ETHQTLLFSATMPDPIRRIAERFMTE 199
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEpgMPskEDRQTLMFSATFPEEIQRLAAEFLKE 253
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
17-218 |
1.41e-57 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 190.78 E-value: 1.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 17 VESMGFEEATPIQAETIPHALQG-KDIIGQAQTGTGKTAAFGLPLLDKVDtNKDAVQGIVIAPTRELAIQVGEELYKLGK 95
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 96 HKRVRILPIYGGQDINRQIRALKK-HPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAILTDVPE 174
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESgKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 228652232 175 THQTLLFSATMPDPIRRIAERFMTEPQHIKVkaKEVTMPNIQQF 218
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
2-205 |
2.71e-57 |
|
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: 190.25 E-value: 2.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 2 TTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTRE 81
Cdd:cd17950 2 SGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 82 LAIQVGEELYKLGKH-KRVRILPIYGGQDINRQIRALK-KHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEM--- 156
Cdd:cd17950 82 LAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleq 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 228652232 157 LNMGfiEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIKV 205
Cdd:cd17950 162 LDMR--RDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
9-206 |
2.27e-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: 187.40 E-value: 2.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 9 LSESLLQSVESMGFEEATPIQAETIPHALQG--KDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTRELAIQV 86
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 87 GEELYKLGKHKRVRI-LPIYGGQ-DINRQIRAlkkhpHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNM-GFIE 163
Cdd:cd17963 81 GEVVEKMGKFTGVKVaLAVPGNDvPRGKKITA-----QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 228652232 164 DIEAILTDVPETHQTLLFSATMPDPIRRIAERFMtePQHIKVK 206
Cdd:cd17963 156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIA--PNANTIK 196
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
9-192 |
1.40e-54 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 182.78 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 9 LSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKV------DTNKDAVQGIVIAPTREL 82
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 83 AIQVGEELYKLGKH--KRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQ-NVETVVLDEADEMLNM 159
Cdd:cd17961 81 AQQVSKVLEQLTAYcrKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLsTLKYLVIDEADLVLSY 160
|
170 180 190
....*....|....*....|....*....|...
gi 228652232 160 GFIEDIEAILTDVPETHQTLLFSATMPDPIRRI 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 |
1.53e-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: 177.95 E-value: 1.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 1 MTTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVD-----TNKDAVQGIV 75
Cdd:cd17953 11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKdqrpvKPGEGPIGLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 76 IAPTRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHI---NRKTLRLQNVETVVLDE 152
Cdd:cd17953 91 MAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 228652232 153 ADEMLNMGFIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17953 171 ADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
4-203 |
3.14e-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: 176.50 E-value: 3.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 4 FRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTRELA 83
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 84 IQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIE 163
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 228652232 164 DIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
13-203 |
3.30e-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: 3.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLdkVDTNKDAVQG-------IVIAPTRELAIQ 85
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAI--VHINAQPPLErgdgpivLVLAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 86 VGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDI 165
Cdd:cd17966 79 IQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 228652232 166 EAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17966 159 RKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
13-203 |
1.04e-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: 174.91 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQG-----IVIAPTRELAIQVG 87
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGegpiaVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 88 EELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEA 167
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 228652232 168 ILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHI 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 |
5.57e-51 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 174.35 E-value: 5.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHAL-QGKDIIGQAQTGTGKTAAFGLP----LLDKVDTNKDA-----VQGIVIAPTREL 82
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPilerLLSQKSSNGVGgkqkpLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 83 AIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHI---NRKTLRLQNVETVVLDEADEMLNM 159
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIqegNEHLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 228652232 160 GFIEDIEAILTDVPETH-------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 |
6.37e-50 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 170.45 E-value: 6.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKV-----DTNKDAVQGIVIAPTRELAIQVG 87
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 88 EELYKLGKH--KRVRILPIYGGQDINRQIRALKKH-PHIIVGTPGRILDHINRKTLRLQ--NVETVVLDEADEMLNMGFI 162
Cdd:cd17960 81 EVLQSFLEHhlPKLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 228652232 163 EDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIK 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 |
2.00e-49 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 169.01 E-value: 2.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 6 ELGLSESllqsvesmGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNK----DAVQGIVIAPTRE 81
Cdd:cd17941 2 LKGLKEA--------GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERwtpeDGLGALIISPTRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 82 LAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALkKHPHIIVGTPGRILDHINRK-TLRLQNVETVVLDEADEMLNMG 160
Cdd:cd17941 74 LAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 228652232 161 FIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIKV 205
Cdd:cd17941 153 FKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
13-200 |
7.85e-49 |
|
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: 167.38 E-value: 7.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKV--DTNKDAVQGIVIAPTRELAIQVGEEL 90
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 91 YKLGKHKRVRILPIYGGQ-DINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAIL 169
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
|
170 180 190
....*....|....*....|....*....|..
gi 228652232 170 TDVPETH-QTLLFSATMPDPIRRIAERFMTEP 200
Cdd:cd17957 161 AACTNPNlQRSLFSATIPSEVEELARSVMKDP 192
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
13-203 |
1.07e-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: 166.87 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTN------KDAVQGIVIAPTRELAIQV 86
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQpipreqRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 87 GEELYKLgKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIE 166
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 228652232 167 AILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHI 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 |
1.43e-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: 166.67 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTRELAIQVGEELYK 92
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 93 LGKH-KRVRILPIYGGQDINRQIRALKKhPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAILTD 171
Cdd:cd17943 81 IGKKlEGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|...
gi 228652232 172 VPETHQTLLFSATMPDPIRRIAERFMTEPQHIK 204
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
13-203 |
9.84e-48 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 164.26 E-value: 9.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTRELAIQVGEELYK 92
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 93 LGK-HKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAILTD 171
Cdd:cd17962 81 LMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180 190
....*....|....*....|....*....|..
gi 228652232 172 VPETHQTLLFSATMPDPIRRIAERFMTEPQHI 203
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
1-199 |
1.95e-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: 1.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 1 MTTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTN------------- 67
Cdd:cd18051 20 IETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslpsesgyy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 68 ---KDAVQGIVIAPTRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQN 144
Cdd:cd18051 100 grrKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDY 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 228652232 145 VETVVLDEADEMLNMGFIEDIEAILT--DVPET--HQTLLFSATMPDPIRRIAERFMTE 199
Cdd:cd18051 180 CKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPTgeRQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
17-204 |
5.17e-46 |
|
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: 160.44 E-value: 5.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 17 VESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQ------GIVIAPTRELAIQVGEEL 90
Cdd:cd17949 6 KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 91 YKLGKhKRVRILP--IYGGQDINRQIRALKKHPHIIVGTPGRILDHI-NRKTLRLQNVETVVLDEADEMLNMGFIEDIEA 167
Cdd:cd17949 86 EKLLK-PFHWIVPgyLIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 228652232 168 IL-------------TDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIK 204
Cdd:cd17949 165 ILellddkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
27-197 |
1.87e-44 |
|
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: 155.78 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 27 PIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKD------AVQGIVIAPTRELAIQVGEELYKLGKhkRVR 100
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQprkrgrAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 101 ILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAILT-----DVPET 175
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvsykkDSEDN 172
|
170 180
....*....|....*....|..
gi 228652232 176 HQTLLFSATMPDPIRRIAERFM 197
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
13-200 |
6.95e-44 |
|
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: 154.42 E-value: 6.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPL-LDKVDTNK-------DAVQGIVIAPTRELAI 84
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLiMFALEQEKklpfikgEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 85 QVGE------ELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLN 158
Cdd:cd17951 81 QTHEvieyycKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 228652232 159 MGFIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEP 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 |
8.16e-44 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 154.40 E-value: 8.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 4 FRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLdkvdtnkDAVQGIVIAPTRELA 83
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-------QIVVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 84 IQVGEELYKLGKH---KRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMG 160
Cdd:cd17938 74 EQTYNCIENFKKYldnPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 228652232 161 FIEDIEAILTDVPETH------QTLLFSATMPDP-IRRIAERFMTEPQ 201
Cdd:cd17938 154 NLETINRIYNRIPKITsdgkrlQVIVCSATLHSFeVKKLADKIMHFPT 201
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
14-184 |
5.20e-43 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 151.74 E-value: 5.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 14 LQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLP---LLDKVD-TNKDAVQGIVIAPTRELAIQVGEE 89
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKfKPRNGTGVIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 90 LYKLGKHKRVRILPIYGGqdINRQIRA--LKKHPHIIVGTPGRILDHI-NRKTLRLQNVETVVLDEADEMLNMGFIEDIE 166
Cdd:cd17942 82 AKELLKYHSQTFGIVIGG--ANRKAEAekLGKGVNILVATPGRLLDHLqNTKGFLYKNLQCLIIDEADRILEIGFEEEMR 159
|
170
....*....|....*...
gi 228652232 167 AILTDVPETHQTLLFSAT 184
Cdd:cd17942 160 QIIKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
4-207 |
5.65e-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: 153.24 E-value: 5.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 4 FRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQG-----IVIAP 78
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGdgpicLVLAP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 79 TRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLN 158
Cdd:cd18049 106 TRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 228652232 159 MGFIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIKVKA 207
Cdd:cd18049 186 MGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
3-211 |
3.45e-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: 145.55 E-value: 3.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQG--KDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTR 80
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 81 ELAIQVGEELYKLGKHKrVRILPIYGGQDiNRQIRALKKHPHIIVGTPGRILDHINR-KTLRLQNVETVVLDEADEMLNM 159
Cdd:cd18048 99 ELALQTGKVVEEMGKFC-VGIQVIYAIRG-NRPGKGTDIEAQIVIGTPGTVLDWCFKlRLIDVTNISVFVLDEADVMINV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 228652232 160 -GFIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIKVKAKEVT 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 |
2.00e-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: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 1 MTTFRELGLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQG-----IV 75
Cdd:cd18050 61 VFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 76 IAPTRELAIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADE 155
Cdd:cd18050 141 LAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADR 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 228652232 156 MLNMGFIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIKV 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 |
2.49e-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: 2.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 226 KKFDVLTRLLDIQSPELAIIFGRTKRRVDElSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLD 305
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 228652232 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 |
3.07e-30 |
|
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: 117.51 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 3 TFRELGLSESLLQSVESMGFEEATPIQAETIPHALQG--KDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQGIVIAPTR 80
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 81 ELAIQVGEELYKLGK-HKRVRILPIYGGQDINRQIRAlkkHPHIIVGTPGRILDH-INRKTLRLQNVETVVLDEADEML- 157
Cdd:cd18047 82 ELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKI---SEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIa 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 228652232 158 NMGFIEDIEAILTDVPETHQTLLFSATMPDPIRRIAERFMTEPQHIK 204
Cdd:cd18047 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
13-185 |
1.62e-29 |
|
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: 116.19 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQG---------KDIIGQAQTGTGKTAAFGLPLLDKVDTNKDA-VQGIVIAPTREL 82
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPrLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 83 AIQVGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPH--------IIVGTPGRILDHINRKT-LRLQNVETVVLDEA 153
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTPgFTLKHLRFLVIDEA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 228652232 154 DEMLNMGFIE-------------------DIEAILTDVPETH-QTLLFSATM 185
Cdd:cd17956 161 DRLLNQSFQDwletvmkalgrptapdlgsFGDANLLERSVRPlQKLLFSATL 212
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
254-335 |
1.14e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 105.76 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 254 DELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGR 333
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 228652232 334 AG 335
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
13-220 |
7.02e-26 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 105.91 E-value: 7.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 13 LLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVQ-------GIVIAPTRELAIQ 85
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEgpfnaprGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 86 VGEELYKLGKHKRVRILPIYGGQDINRQIRALKKHPHIIVGTPGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDI 165
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 166 EAILTDVP--ETH-----------QTLLFSATMPDPIRRIAERF--MTEPQHIKVKAKEVTMPNIQQFYL 220
Cdd:cd17948 161 SHFLRRFPlaSRRsentdgldpgtQLVLVSATMPSGVGEVLSKVidVDSIETVTSDKLHRLMPHVKQKFL 230
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
11-368 |
5.50e-20 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 92.90 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 11 ESLLQSVesMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLP--LLDKVdtnkdavqGIVIAPtreLaI---- 84
Cdd:COG0514 6 LEVLKRV--FGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLLPGL--------TLVVSP---L-Ialmk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 85 -QVgEELYKLG-----------KHKRVRILpiyggqdinRQIRA--LKkhphIIVGTPGRILDHINRKTLRLQNVETVVL 150
Cdd:COG0514 72 dQV-DALRAAGiraaflnsslsAEERREVL---------RALRAgeLK----LLYVAPERLLNPRFLELLRRLKISLFAI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 151 DEA--------D---EMLNMG-FIEDieaiLTDVPethqTLLFSATMPDPIRR-IAERF-MTEPQHIKVKakeVTMPNIq 216
Cdd:COG0514 138 DEAhcisqwghDfrpDYRRLGeLRER----LPNVP----VLALTATATPRVRAdIAEQLgLEDPRVFVGS---FDRPNL- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 217 qfYLEVQEKKKFDVLTRLLDI---QSPELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEV 293
Cdd:COG0514 206 --RLEVVPKPPDDKLAQLLDFlkeHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 294 LVATdVA-ARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLFVTPRESGQLKN-IERTT---------KRK 362
Cdd:COG0514 284 IVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFfIEQSPpdeerkrveRAK 362
|
....*.
gi 228652232 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 |
2.58e-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: 84.74 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 3 TFRELGLSESLLQSVESMGFEEATPIQAETIP---------HALQGKDIIGQ-------AQTGTGKTAAFGLPLLDKVD- 65
Cdd:cd17965 9 SVREAIIKEILKGSNKTDEEIKPSPIQTLAIKkllktlmrkVTKQTSNEEPKlevfllaAETGSGKTLAYLAPLLDYLKr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 66 ----------------TNKDAVQGIVIAPTRELAIQVGEELYKLGKHKRVRILPIYG--GQDINRQIRALKKHPHIIVGT 127
Cdd:cd17965 89 qeqepfeeaeeeyesaKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSgfGPSYQRLQLAFKGRIDILVTT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 228652232 128 PGRILDHINRKTLRLQNVETVVLDEADEMLNMGFIEDIEAILTDVPETHQTLLFSATMP 186
Cdd:cd17965 169 PGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
213-368 |
6.68e-17 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 83.99 E-value: 6.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 213 PNIQqfYLEVQEKKKFDVLTRLLDIQSPELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIE 292
Cdd:PRK11057 211 PNIR--YTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQ 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 293 VLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLFVTP------------RESGQLKNIERttk 360
Cdd:PRK11057 289 IVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPadmawlrrcleeKPAGQQQDIER--- 365
|
....*...
gi 228652232 361 RKVDRMEA 368
Cdd:PRK11057 366 HKLNAMGA 373
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
213-343 |
6.79e-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: 77.25 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 213 PNIqqfYLEVQEKKKFDVLTRLLDIQSP----ELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKE 288
Cdd:cd18794 2 PNL---FYSVRPKDKKDEKLDLLKRIKVehlgGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 228652232 289 GAIEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLF 343
Cdd:cd18794 79 DKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
39-184 |
9.50e-17 |
|
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: 77.06 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 39 GKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAVqgIVIAPTRELAIQVGEELYKLGKHKrVRILPIYGGQDINRQIRALK 118
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKV--LVLVPTKALALQTAERLRELFGPG-IRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 228652232 119 KHPHIIVGTPGRILDHINR-KTLRLQNVETVVLDEADEML------NMGFIEDIEAILTDVpethQTLLFSAT 184
Cdd:cd00046 78 GDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLidsrgaLILDLAVRKAGLKNA----QVILLSAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
48-330 |
1.45e-14 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 76.22 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 48 TGTGKT--AAFglpLLDKVDTNKDAvqgIVIAPTRELAIQVGEELyklgkhKRVRILPIYGGQDINRqiralkkHPHIIV 125
Cdd:COG1061 109 TGTGKTvlALA---LAAELLRGKRV---LVLVPRRELLEQWAEEL------RRFLGDPLAGGGKKDS-------DAPITV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 126 GTPGRILDHINRKTLRlQNVETVVLDEADEMLNMGFiediEAILTDVPETHqTLLFSATmpdPIRR-------------- 191
Cdd:COG1061 170 ATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTAT---PFRSdgreillflfdgiv 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 192 --------IAERFMTEPQHIKVkakEVTMPNIQQFY----------LEVQEKKKFDVLTRLLD-IQSPELAIIFGRTKRR 252
Cdd:COG1061 241 yeyslkeaIEDGYLAPPEYYGI---RVDLTDERAEYdalserlreaLAADAERKDKILRELLReHPDDRKTLVFCSSVDH 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228652232 253 VDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGR 330
Cdd:COG1061 318 AEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGR 395
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
8-342 |
3.51e-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: 72.18 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 8 GLSESLLQSVESMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAvQGIVIAPTRELAI-QV 86
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA-TALYLYPTKALARdQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 87 gEELYKLGKHKRVRILP-IYGGqDINRQIR-ALKKHPHIIVGTPgrilDHINRKTLR--------LQNVETVVLDEADem 156
Cdd:COG1205 119 -RRLRELAEALGLGVRVaTYDG-DTPPEERrWIREHPDIVLTNP----DMLHYGLLPhhtrwarfFRNLRYVVIDEAH-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 157 lnmgfiedieaILTDVPETHQTLLFsatmpDPIRRIAERFMTEPQHIKVKAkevTMPNIQQF--------YLEVQE---- 224
Cdd:COG1205 191 -----------TYRGVFGSHVANVL-----RRLRRICRHYGSDPQFILASA---TIGNPAEHaerltgrpVTVVDEdgsp 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 225 --KKKF---------------------DVLTRLL--DIQSpelaIIFGR-----------TKRRVDELSEALNLRGYaae 268
Cdd:COG1205 252 rgERTFvlwnpplvddgirrsalaeaaRLLADLVreGLRT----LVFTRsrrgaellaryARRALREPDLADRVAAY--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 269 giHGDLTQAKRMSVLRKFKEGAIEVLVAT-------DVAarGLD---ISGvthvynfdIPQDPESYVHRIGRTGRAGKKG 338
Cdd:COG1205 325 --RAGYLPEERREIERGLRSGELLGVVSTnalelgiDIG--GLDavvLAG--------YPGTRASFWQQAGRAGRRGQDS 392
|
....
gi 228652232 339 IAML 342
Cdd:COG1205 393 LVVL 396
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
227-329 |
2.56e-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: 61.34 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 227 KFDVLTRLLD--IQSPELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKE--GAIEVLVATDVAAR 302
Cdd:cd18793 12 KLEALLELLEelREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 228652232 303 GLDISGVTHVYNFDIPQDP------ESYVHRIG 329
Cdd:cd18793 92 GLNLTAANRVILYDPWWNPaveeqaIDRAHRIG 124
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
230-342 |
1.10e-10 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 64.37 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 230 VLTRLLDIQSPELAIIFGRTKRRVDELSEALNLRGYAAE------GIHGD--LTQAKRMSVLRKFKEGAIEVLVATDVAA 301
Cdd:COG1111 343 ILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAE 422
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 228652232 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 |
5.80e-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: 57.60 E-value: 5.80e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 273 DLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAML 342
Cdd:cd18802 73 LMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSKYILMV 142
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
45-337 |
9.53e-09 |
|
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: 57.46 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 45 QAQTGTGKTAAFGLPLLDKVDTNKdAVQGIVIAPTRELAIQVGEELYKLGKHKRVRILPIYGGQDIN--------RQIRA 116
Cdd:TIGR01587 5 EAPTGYGKTEAALLWALHSIKSQK-ADRVIIALPTRATINAMYRRAKELFGSELVGLHHSSSFSRIKemgdseefEHLFP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 117 LKKHPH-------IIVGTP-------GRILDHINRKTLRLQNvETVVLDEAD--EMLNMGFIEDIEAILTDVPETHqtLL 180
Cdd:TIGR01587 84 LYIHSNdklfldpITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHfyDEYTLALILAVLEVLKDNDVPI--LL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 181 FSATMPDPIRRIAERFMTEPQHIKVKAKEVTMPNIQQFYLEVQEKK-KFDVLTRLLD-IQSPELAIIFGRTKRRVDELSE 258
Cdd:TIGR01587 161 MSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVgEISSLERLLEfIKKGGSIAIIVNTVDRAQEFYQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 259 ALNLRGYAAEGI--HGDLTQAKR-----MSVLRKFKEGAIEVLVATDVAARGLDISgvthvynFDI----PQDPESYVHR 327
Cdd:TIGR01587 241 QLKEKAPEEEIIlyHSRFTEKDRakkeaELLREMKKSNEKFVIVATQVIEASLDIS-------ADVmiteLAPIDSLIQR 313
|
330
....*....|
gi 228652232 328 IGRTGRAGKK 337
Cdd:TIGR01587 314 LGRLHRYGRK 323
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
29-153 |
1.04e-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: 54.90 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 29 QAETIPHALQGKDIIGQAQTGTGKTAAFGLPLLDKV--DTNkdaVQGIVIAPTRELAIQVGEELYKL--GKHKRVRILPI 104
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALlrDPG---SRALYLYPTKALAQDQLRSLRELleQLGLGIRVATY 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 228652232 105 YGGQDINRQIRALKKHPHIIVGTPGR----ILDHINRKTLRLQNVETVVLDEA 153
Cdd:cd17923 82 DGDTPREERRAIIRNPPRILLTNPDMlhyaLLPHHDRWARFLRNLRYVVLDEA 134
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
227-440 |
1.15e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.96 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 227 KFDVLTRL----LDIQSPELAIIFGRTKRRVDELSEALNLRGYAAEGIHGD--------LTQAKRMSVLRKFKEGAIEVL 294
Cdd:PRK13766 348 KLEKLREIvkeqLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 295 VATDVAARGLDISGVTHVYNFD-IPQDPESyVHRIGRTGRaGKKGIAMLFVT--PRESGQLknieRTTKRKVDRMEaptl 371
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEGRVVVLIAkgTRDEAYY----WSSRRKEKKMK---- 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 228652232 372 dEALEGQQRLIAEKLQSTIENDNLSYYKRIAEEMLEENDSVTVVAAALKMMTKEPDTTPIALTSEPPVV 440
Cdd:PRK13766 498 -EELKNLKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKDKETEEDEPEGPKI 565
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
227-331 |
1.22e-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: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 227 KFDVLTRLLD--IQSPELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEG--AIEVLVATDVAAR 302
Cdd:COG0553 534 KLEALLELLEelLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAGGE 613
|
90 100 110
....*....|....*....|....*....|....*
gi 228652232 303 GLDISGVTHVYNFDIPQDPESY------VHRIGRT 331
Cdd:COG0553 614 GLNLTAADHVIHYDLWWNPAVEeqaidrAHRIGQT 648
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
291-344 |
2.08e-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: 2.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 228652232 291 IEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKK-GIAMLFV 344
Cdd:cd18785 23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDeGEVILFV 77
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
266-343 |
2.83e-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: 52.74 E-value: 2.83e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228652232 266 AAEGIHGdLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRIGRTGRAGKKGIAMLF 343
Cdd:cd18801 67 SGKSSKG-MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQGRVVVLL 143
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
227-338 |
4.41e-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: 52.64 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 227 KFDVLTRLLDIQSP-ELAIIFGRTKRRVDELSEALNlrgyaAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLD 305
Cdd:cd18789 35 KLRALEELLKRHEQgDKIIVFTDNVEALYRYAKRLL-----KPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGID 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 228652232 306 IsgvthvynfdipqdPES---------------YVHRIGRTGRAGKKG 338
Cdd:cd18789 110 L--------------PEAnvaiqisghggsrrqEAQRLGRILRPKKGG 143
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
45-345 |
5.95e-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: 54.74 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 45 QAQTGTGKTAAfGLPLLDKVDTNKDAVQGIVIAPTRELAIQVGEELYKLGKHKRVRILPI-------YGGQDINRQIRAL 117
Cdd:cd09639 5 EAPTGYGKTEA-ALLWALHSLKSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSIlssrikeMGDSEEFEHLFPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 118 KKHPH-------IIVGTP-------GRILDHINRKTLRLQNvETVVLDEAD--EMLNMGFIEDIEAILTDVPETHqtLLF 181
Cdd:cd09639 84 YIHSNdtlfldpITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHfyDEYTLALILAVLEVLKDNDVPI--LLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 182 SATMPdpirriaERFMTEPQHIKVKAKEVTMPNI----QQFYLEVQEKK-KFDVLTRLLD-IQSPELAIIFGRTKRRVDE 255
Cdd:cd09639 161 SATLP-------KFLKEYAEKIGYVEENEPLDLKpnerAPFIKIESDKVgEISSLERLLEfIKKGGSVAIIVNTVDRAQE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 256 LSEALNLRGYAAEG--IHGDLTQA----KRMSVLRKFKEGAIEVLVATDVAARGLDISgvthvynFDI----PQDPESYV 325
Cdd:cd09639 234 FYQQLKEKGPEEEImlIHSRFTEKdrakKEAELLLEFKKSEKFVIVATQVIEASLDIS-------VDVmiteLAPIDSLI 306
|
330 340
....*....|....*....|
gi 228652232 326 HRIGRTGRAGKKGIAMLFVT 345
Cdd:cd09639 307 QRLGRLHRYGEKNGEEVYII 326
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
39-157 |
1.18e-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: 48.73 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 39 GKDIIGQAQTGTGKTAAFGLPLLDKV-DTNKDAVQGIVIAPTRELAIQVGEELYKLGKHKR--VRILPIYGgqDINRQIR 115
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPLDEIDleIPVAVRHG--DTSQSEK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 228652232 116 A--LKKHPHIIVGTPGRILDHINRKTLR--LQNVETVVLDEADEML 157
Cdd:cd17922 79 AkqLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDEIHALL 124
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
22-156 |
3.23e-06 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 49.88 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 22 FEEATPIQAETIPHALQGKDIIGQAQTGTGKT-AAF-----GLPLLDKVDTNKDAVQGIVIAPTRELA--IQVG-----E 88
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFlaiidELFRLGREGELEDKVYCLYVSPLRALNndIHRNleeplT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 89 ELYKLGKHKRVRILPI-----YGGQDINRQIRALKKHPHIIVGTPgrildhinrKTL-----------RLQNVETVVLDE 152
Cdd:PRK13767 110 EIREIAKERGEELPEIrvairTGDTSSYEKQKMLKKPPHILITTP---------ESLaillnspkfreKLRTVKWVIVDE 180
|
....
gi 228652232 153 ADEM 156
Cdd:PRK13767 181 IHSL 184
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
11-204 |
3.47e-06 |
|
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: 47.91 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 11 ESLLQSVesMGFEEATPIQAETIPHALQGKDIIGQAQTGTGKTAAFGLP--LLDKVdtnkdavqGIVIAPTreLAI---Q 85
Cdd:cd17920 1 EQILKEV--FGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV--------TLVVSPL--ISLmqdQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 86 VgEELYKLGkhkrVRILPIYGGQDIN--RQIRALKKHP--HIIVGTP-----GRILDHINRKTLRLQnVETVVLDEA--- 153
Cdd:cd17920 69 V-DRLQQLG----IRAAALNSTLSPEekREVLLRIKNGqyKLLYVTPerllsPDFLELLQRLPERKR-LALIVVDEAhcv 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228652232 154 --------DEMLNMGfieDIEAILTDVPethqTLLFSATMPDPIRR-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 |
2.12e-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: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 249 TKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFD-----IPQDPES 323
Cdd:cd18790 36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSETS 115
|
90
....*....|
gi 228652232 324 YVHRIGRTGR 333
Cdd:cd18790 116 LIQTIGRAAR 125
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
46-411 |
7.64e-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: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 46 AQTGTGKT---AAFGLPLLDKVDTNKdavqGIVIAPTRELAIQVGEELYKLGK------HKRVRILPIYGGQDINRQIRA 116
Cdd:COG1203 154 APTGGGKTeaaLLFALRLAAKHGGRR----IIYALPFTSIINQTYDRLRDLFGedvllhHSLADLDLLEEEEEYESEARW 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 117 LKKH------PhIIVGTPGRILD-------HINRKTLRLQN-VetVVLDEAD----EMLNMgfiedIEAILTDVPETHQT 178
Cdd:COG1203 230 LKLLkelwdaP-VVVTTIDQLFEslfsnrkGQERRLHNLANsV--IILDEVQayppYMLAL-----LLRLLEWLKNLGGS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 179 LLF-SATMPDPIRriaeRFMTEPQHIKVKAKEVTMPNIQQFY---LEVQEKKKF--DVLTRLLDIQSPE--LAIIFGrTK 250
Cdd:COG1203 302 VILmTATLPPLLR----EELLEAYELIPDEPEELPEYFRAFVrkrVELKEGPLSdeELAELILEALHKGksVLVIVN-TV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 251 RRVDELSEALNLRGyAAEGI---HGDLTQAKRMSVLRK----FKEGAIEVLVATDVAARGLDISgvthvynFDI----PQ 319
Cdd:COG1203 377 KDAQELYEALKEKL-PDEEVyllHSRFCPADRSEIEKEikerLERGKPCILVSTQVVEAGVDID-------FDVvirdLA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 320 DPESYVHRIGRT---GRAGKKGIAMLFVTPRESGQL----KNIERTtkrkvdrmeaptlDEALEGQQRLIAEKLQSTIEn 392
Cdd:COG1203 449 PLDSLIQRAGRCnrhGRKEEEGNVYVFDPEDEGGGYvydkPLLERT-------------RELLREHDEILPEDKRELIE- 514
|
410
....*....|....*....
gi 228652232 393 dnlSYYKRIAEEMLEENDS 411
Cdd:COG1203 515 ---EYYRELYELLPDELDS 530
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
241-343 |
2.16e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 44.12 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 241 ELAIIFGRTKRRVDELSEALNLRGYAAEGIHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQD 320
Cdd:PLN03137 681 ECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKS 760
|
90 100
....*....|....*....|...
gi 228652232 321 PESYVHRIGRTGRAGKKGIAMLF 343
Cdd:PLN03137 761 IEGYHQECGRAGRDGQRSSCVLY 783
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
270-349 |
2.58e-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: 41.56 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 270 IHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVynfdIPQDPE----SYVHRI-GRTGRAGKKGIAMLFV 344
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVM----VIEDAErfglSQLHQLrGRVGRGDHQSYCLLVY 142
|
....*
gi 228652232 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 |
3.31e-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: 41.48 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 270 IHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVynfdIPQDPE----SYVHRI-GRTGRAGKKGIAMLFV 344
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTM----IIEDADrfglSQLHQLrGRVGRGKHQSYCYLLY 141
|
90 100
....*....|....*....|....
gi 228652232 345 TPRESgqlknierTTKRKVDRMEA 368
Cdd:cd18792 142 PDPKK--------LTETAKKRLRA 157
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
45-175 |
4.41e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 41.25 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 45 QAQTGTGKTAAFGLPLLDKVDTNKdavQGIVIAPTRELAIQVGEELYKLgkHKRVRILPIYGG--QDINRQIralkkhpH 122
Cdd:cd17918 42 SGDVGSGKTLVALGAALLAYKNGK---QVAILVPTEILAHQHYEEARKF--LPFINVELVTGGtkAQILSGI-------S 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228652232 123 IIVGTPGRIldHINRKTLrlqNVETVVLDEA--------DEMLNMGFIEDIEAILTDVPET 175
Cdd:cd17918 110 LLVGTHALL--HLDVKFK---NLDLVIVDEQhrfgvaqrEALYNLGATHFLEATATPIPRT 165
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
28-218 |
4.89e-04 |
|
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: 41.57 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 28 IQAETIPHALQG-KDIIGQAQTGTGKTAAFGLPLL----DKVDTNKDAVQGIVIAPTRELAiqvgEELYKLGKHK----R 98
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILrllkERNPLPWGNRKVVYIAPIKALC----SEKYDDWKEKfgplG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 99 VRILPIYGGQDINRQIRAlkKHPHIIVGTPGRiLDHINRKTLRLQN-VETVVLDEADEMLNMGFIED--IEAILTDVPET 175
Cdd:cd18023 81 LSCAELTGDTEMDDTFEI--QDADIILTTPEK-WDSMTRRWRDNGNlVQLVALVLIDEVHIIKENRGatLEVVVSRMKTL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 228652232 176 HqtlLFSATMPDPIRRIaeRFmtepqhIKVKAkevTMPNIQQF 218
Cdd:cd18023 158 S---SSSELRGSTVRPM--RF------VAVSA---TIPNIEDL 186
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
270-368 |
5.65e-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: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 270 IHGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDIPQDPESYVHRI-GRTGRAGKKGIAMLFVTPRE 348
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYAYFLYPDQK 136
|
90 100
....*....|....*....|
gi 228652232 349 SgqlknierTTKRKVDRMEA 368
Cdd:cd18810 137 K--------LTEDALKRLEA 148
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
219-345 |
6.73e-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: 40.23 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 219 YLEVQEKKKF--DVLTRLLDIQSPEL--AIIFGRTKRRVDELseALNLRGYAAegIHGDLTQAKRMSVLRKFKEGAIEVL 294
Cdd:cd18795 18 KLRVDVMNKFdsDIIVLLKIETVSEGkpVLVFCSSRKECEKT--AKDLAGIAF--HHAGLTREDRELVEELFREGLIKVL 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 228652232 295 VATDVAARGLD-------ISGVTHvYNFDIPQD-PESYVHR-IGRTGRAGK--KGIAMLFVT 345
Cdd:cd18795 94 VATSTLAAGVNlpartviIKGTQR-YDGKGYRElSPLEYLQmIGRAGRPGFdtRGEAIIMTK 154
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
244-336 |
2.16e-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: 38.78 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 244 IIFGRTKRRVDELSEALN-LRGYAAEGI-----HGDLTQAKRMSVLRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDI 317
Cdd:cd18796 42 LVFTNTRSQAERLAQRLReLCPDRVPPDfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90
....*....|....*....
gi 228652232 318 PQDPESYVHRIGRTGRAGK 336
Cdd:cd18796 122 PKSVARLLQRLGRSGHRPG 140
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
244-349 |
3.64e-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: 38.44 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 244 IIFGRT---KRRVDELSEALNLRGYAAEGIHgdltqAKRMSVLRKFKEGAIEVLVAT----DVAARGLDISG-VTHVYNF 315
Cdd:cd18798 28 LIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLPErIKYAIFY 102
|
90 100 110
....*....|....*....|....*....|....*...
gi 228652232 316 DIPqdPESYVHRIGRTGR--AG--KKGIAMLFVTPRES 349
Cdd:cd18798 103 GVP--VTTYIQASGRTSRlyAGglTKGLSVVLVDDPEL 138
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
27-194 |
4.87e-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: 38.08 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 27 PIQAETIPHAL-QGKDIIGQAQTGTGKTAAFGLPLLDKVDTNKDAvqgIVIAPTRELAIQVGEE---LYKLGkhkrVRIL 102
Cdd:cd18028 4 PPQAEAVRAGLlKGENLLISIPTASGKTLIAEMAMVNTLLEGGKA---LYLVPLRALASEKYEEfkkLEEIG----LKVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228652232 103 PIYGgqDINRQIRALKKHpHIIVGTPGRiLDHINR-KTLRLQNVETVVLDE---ADEMLNMGFIEDIEA-ILTDVPEThQ 177
Cdd:cd18028 77 ISTG--DYDEDDEWLGDY-DIIVATYEK-FDSLLRhSPSWLRDVGVVVVDEihlISDEERGPTLESIVArLRRLNPNT-Q 151
|
170
....*....|....*..
gi 228652232 178 TLLFSATMPDPiRRIAE 194
Cdd:cd18028 152 IIGLSATIGNP-DELAE 167
|
|
| |
