|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
98-461 |
7.03e-137 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 400.68 E-value: 7.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDN-IQAMVIVPTREL 176
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPTREL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 177 ALQVSQICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDF 256
Cdd:COG0513 84 ALQVAEELRKLAKYLG-LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 257 VQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINLM-EELTLKGVTQYYAYVTERQKVHCLNTLFSRLQIN 335
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVApENATAETIEQRYYLVDKRDKLELLRRLLRDEDPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 336 QSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLA 415
Cdd:COG0513 243 RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDP 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720430166 416 ETYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEIKPIP 461
Cdd:COG0513 323 EDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEE 368
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
98-299 |
1.68e-136 |
|
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: 391.28 E-value: 1.68e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELA 177
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 178 LQVSQICIQVSKHMgGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFV 257
Cdd:cd17940 81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720430166 258 QIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEIN 299
Cdd:cd17940 160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
98-473 |
2.27e-101 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 309.45 E-value: 2.27e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELA 177
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 178 LQVSQICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFV 257
Cdd:PTZ00424 110 QQIQKVVLALGDYLK-VRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 258 QIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINL-MEELTLKGVTQYYAYV-TERQKVHCLNTLFSRLQIN 335
Cdd:PTZ00424 189 GQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVkKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETLTIT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 336 QSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLA 415
Cdd:PTZ00424 269 QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430166 416 ETYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEIKPIPsnidksLYVAEY 473
Cdd:PTZ00424 349 ENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMP------MEVADY 400
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
103-462 |
1.66e-93 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 290.93 E-value: 1.66e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 103 LKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELALQVSQ 182
Cdd:PRK11776 11 LPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 183 ICIQVSKHMGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMED 262
Cdd:PRK11776 91 EIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 263 IILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINLMEELTLKGVTQYYAYVTERQKVHCLNTLFSRLQINQSIIFCN 342
Cdd:PRK11776 171 IIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDERLPALQRLLLHHQPESCVVFCN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 343 SSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRI 422
Cdd:PRK11776 251 TKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRI 330
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1720430166 423 GRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEIK--PIPS 462
Cdd:PRK11776 331 GRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNwePLPS 372
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
107-298 |
4.79e-79 |
|
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: 244.66 E-value: 4.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 107 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLD----LKKDNIQAMVIVPTRELALQVSQ 182
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLpepkKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 183 ICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMED 262
Cdd:cd00268 81 VARKLGKGTG-LKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720430166 263 IILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEI 298
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
98-459 |
1.08e-73 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 239.07 E-value: 1.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERL-DL-KKDNIQAMVIV--PT 173
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLlDFpRRKSGPPRILIltPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 174 RELALQVSQICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLS 253
Cdd:PRK11192 83 RELAMQVADQARELAKHTH-LDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 254 QDFVQIMEDIILTLPKNRQILLYSATFPLS-VQKFMNSHLQKPYEIN----LMEEltlKGVTQ-YYAYVTERQKVHCLNT 327
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEaepsRRER---KKIHQwYYRADDLEHKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 328 LFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVI 407
Cdd:PRK11192 239 LLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1720430166 408 NFDFPKLAETYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEIKP 459
Cdd:PRK11192 319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKA 370
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
98-457 |
2.92e-72 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 235.86 E-value: 2.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDN------IQAMVIV 171
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 172 PTRELALQVSQICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKL 251
Cdd:PRK10590 83 PTRELAAQIGENVRDYSKYLN-IRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 252 LSQDFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINLMEELTL-KGVTQYYAYVTERQKVHCLNTLFS 330
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTAsEQVTQHVHFVDKKRKRELLSQMIG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 331 RLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFD 410
Cdd:PRK10590 242 KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYE 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1720430166 411 FPKLAETYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEI 457
Cdd:PRK10590 322 LPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
98-460 |
9.53e-72 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 238.98 E-value: 9.53e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELA 177
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 178 LQVSQICIQVSKHMGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFV 257
Cdd:PRK11634 88 VQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 258 QIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINLMEELTLK-GVTQYYAYVTERQKVHCLNTLFSRLQINQ 336
Cdd:PRK11634 168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRpDISQSYWTVWGMRKNEALVRFLEAEDFDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 337 SIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAE 416
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1720430166 417 TYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEIKPI 460
Cdd:PRK11634 328 SYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEV 371
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
90-476 |
4.66e-66 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 221.96 E-value: 4.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 90 VTSTKGNEFEDYCLKrellmGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIP----LLERLDLKK-DN 164
Cdd:PTZ00110 129 VVSFEYTSFPDYILK-----SLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaivhINAQPLLRYgDG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 165 IQAMVIVPTRELALQVSQICIQVSKhMGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIV 244
Cdd:PTZ00110 204 PIVLVLAPTRELAEQIREQCNKFGA-SSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 245 LDEADKLLSQDFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHL-QKPYEINLmEELTLKG---VTQYYAYVTERQ 320
Cdd:PTZ00110 283 LDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNV-GSLDLTAchnIKQEVFVVEEHE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 321 KVHCLNTLFSRLQINQS--IIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGI 398
Cdd:PTZ00110 362 KRGKLKMLLQRIMRDGDkiLIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGL 441
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720430166 399 DIQAVNVVINFDFPKLAETYLHRIGRSGRFGHLGLAINLITyDDRFNLKSIEEQLGTEIK-PIPSNIDKSLYVAEYHSE 476
Cdd:PTZ00110 442 DVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLT-PDKYRLARDLVKVLREAKqPVPPELEKLSNERSNGTE 519
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
67-458 |
2.71e-65 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 218.24 E-value: 2.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 67 KPGDDWKktlklpPKDLRIKTSDVTStkgnEFEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGK 146
Cdd:PRK01297 68 KPASLWK------LEDFVVEPQEGKT----RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 147 SGAYLIPLLERL-------DLKKDNIQAMVIVPTRELALQVSQICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDT-VHV 218
Cdd:PRK01297 138 TAAFLISIINQLlqtpppkERYMGEPRALIIAPTRELVVQIAKDAAALTKYTG-LNVMTFVGGMDFDKQLKQLEARfCDI 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 219 VIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDIILTLPK--NRQILLYSATFPLSVQKFMNSHLQKPY 296
Cdd:PRK01297 217 LVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 297 EINL-MEELTLKGVTQYYAYVTERQKVHCLNTLFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNR 375
Cdd:PRK01297 297 IVEIePENVASDTVEQHVYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 376 VFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGT 455
Cdd:PRK01297 377 TLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGR 456
|
...
gi 1720430166 456 EIK 458
Cdd:PRK01297 457 KIS 459
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
100-298 |
8.94e-58 |
|
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: 189.84 E-value: 8.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 100 DYCLKRELLMGIFEMGWEKPSPIQEESI-PIaLSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELAL 178
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIvPI-IKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 179 QVSQICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQ 258
Cdd:cd17939 80 QIQKVVKALGDYMG-VKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720430166 259 IMEDIILTLPKNRQILLYSATFPLSV----QKFMNshlqKPYEI 298
Cdd:cd17939 159 QIYDIFQFLPPETQVVLFSATMPHEVlevtKKFMR----DPVRI 198
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
98-481 |
2.71e-56 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 196.71 E-value: 2.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERL-------DLKKDNIQAMVI 170
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 171 VPTRELALQVSQICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKK-GVAKVDHVQMIVLDEAD 249
Cdd:PRK04537 91 APTRELAIQIHKDAVKFGADLG-LRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 250 KLLSQDFVQIMEDIILTLPK--NRQILLYSATFPLSVQKFMNSHLQKPYEINL-MEELTLKGVTQYYAYVTERQKVHCLN 326
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVeTETITAARVRQRIYFPADEEKQTLLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 327 TLFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVV 406
Cdd:PRK04537 250 GLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYV 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720430166 407 INFDFPKLAETYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEI--KPIPSNIDKSLYVAEYHSEPAEDE 481
Cdd:PRK04537 330 YNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIpvEPVTAELLTPLPRPPRVPVEGEEA 406
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
107-290 |
8.10e-56 |
|
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: 184.39 E-value: 8.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 107 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELALQVSQICIQ 186
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 187 VSKHMGGAKVMATTGGTNLRDDIMRLDDTvHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDIILT 266
Cdd:cd17943 81 IGKKLEGLKCEVFIGGTPVKEDKKKLKGC-HIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180
....*....|....*....|....*...
gi 1720430166 267 LPKNRQILLYSATFPLS----VQKFMNS 290
Cdd:cd17943 160 LPKNKQVIAFSATYPKNldnlLARYMRK 187
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
98-288 |
1.06e-55 |
|
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: 184.19 E-value: 1.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELA 177
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 178 LQVSQICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFV 257
Cdd:cd18046 81 QQIQKVVMALGDYMG-IKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1720430166 258 QIMEDIILTLPKNRQILLYSATFPLSV----QKFM 288
Cdd:cd18046 160 DQIYDIFQKLPPDTQVVLLSATMPNDVlevtTKFM 194
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
309-438 |
3.90e-55 |
|
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: 180.40 E-value: 3.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 309 VTQYYAYVTERQKVHCLN-TLFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRN 387
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720430166 388 LVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRIGRSGRFGHLGLAINLI 438
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
120-287 |
7.92e-55 |
|
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: 180.90 E-value: 7.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 120 SPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELALQVSQICIQVSKHMgGAKVMAT 199
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 200 TGGTNLRDDIMRLdDTVHVVIATPGRILDLIKKGVaKVDHVQMIVLDEADKLLSQDFVQIMEDIILTLPKNRQILLYSAT 279
Cdd:pfam00270 80 LGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157
|
....*...
gi 1720430166 280 FPLSVQKF 287
Cdd:pfam00270 158 LPRNLEDL 165
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
107-298 |
7.54e-54 |
|
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: 179.37 E-value: 7.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 107 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERL---DLKKDNIQAMVIVPTRELALQVSQI 183
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 184 CIQVSKHmGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVA-KVDHVQMIVLDEADKLLSQDFVQIMED 262
Cdd:cd17947 81 LQQLAQF-TDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADELKE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720430166 263 IILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEI 298
Cdd:cd17947 160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
86-467 |
1.42e-53 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 185.56 E-value: 1.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 86 KTSDVTSTKgneFEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERL------- 158
Cdd:PRK04837 1 SKTHLTEQK---FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshpape 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 159 DLKKDNIQAMVIVPTRELALQVSQICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVD 238
Cdd:PRK04837 78 DRKVNQPRALIMAPTRELAVQIHADAEPLAQATG-LKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 239 HVQMIVLDEADKLLSQDFVQimeDIILTL-----PKNRQILLYSATFPLSVQKFMNSHLQKPYEINLM-EELTLKGVTQY 312
Cdd:PRK04837 157 AIQVVVLDEADRMFDLGFIK---DIRWLFrrmppANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEpEQKTGHRIKEE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 313 YAYVTERQKVHCLNTLFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTD 392
Cdd:PRK04837 234 LFYPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATD 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720430166 393 LFTRGIDIQAVNVVINFDFPKLAETYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGteiKPIP-SNIDKS 467
Cdd:PRK04837 314 VAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIG---HSIPvSKYDSD 386
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
98-471 |
2.37e-53 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 187.30 E-value: 2.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDL-------KKDNIQAMVI 170
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTirsghpsEQRNPLAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 171 VPTRELalqvsqiCIQVSKHmggAKVMA---------TTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQ 241
Cdd:PLN00206 203 TPTREL-------CVQVEDQ---AKVLGkglpfktalVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 242 MIVLDEADKLLSQDFV-QIMEdIILTLPKNrQILLYSATFPLSVQKFMNSHLQKPYEINL-MEELTLKGVTQYYAYVTER 319
Cdd:PLN00206 273 VLVLDEVDCMLERGFRdQVMQ-IFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIgNPNRPNKAVKQLAIWVETK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 320 QKVHclnTLFSRLQINQ-----SIIFCNSSQRVELLAKKISQL-GYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDL 393
Cdd:PLN00206 351 QKKQ---KLFDILKSKQhfkppAVVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGV 427
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430166 394 FTRGIDIQAVNVVINFDFPKLAETYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEIKPIPSNIDKSLYVA 471
Cdd:PLN00206 428 LGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELANSRYLG 505
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
98-298 |
1.34e-51 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350803 [Multi-domain] Cd Length: 201 Bit Score: 173.81 E-value: 1.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELA 177
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 178 LQVSQICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFV 257
Cdd:cd18045 81 VQIQKVLLALGDYMN-VQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720430166 258 QIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEI 298
Cdd:cd18045 160 EQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
98-298 |
1.06e-50 |
|
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: 171.35 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELA 177
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 178 LQVSqiciQVSKHMG---GAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIK--KGVaKVDHVQMIVLDEADKLL 252
Cdd:cd17954 82 QQIS----EQFEALGssiGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEntKGF-SLKSLKFLVMDEADRLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720430166 253 SQDFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEI 298
Cdd:cd17954 157 NMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
98-298 |
2.81e-50 |
|
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: 170.22 E-value: 2.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELA 177
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 178 LQVSQICIQVSKHMGGAKVMATTGGTNLRDDIMRL-DDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQ-D 255
Cdd:cd17950 84 FQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQlD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720430166 256 FVQIMEDIILTLPKNRQILLYSATFPLSVQ----KFMnshlQKPYEI 298
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRpvckKFM----QDPLEI 206
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
98-295 |
2.49e-49 |
|
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: 167.87 E-value: 2.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLD--LKKDNIQAMVIVPTRE 175
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKahSPTVGARALILSPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 176 LALQVSQICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQD 255
Cdd:cd17959 83 LALQTLKVTKELGKFTD-LRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720430166 256 FVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKP 295
Cdd:cd17959 162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEP 201
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
106-297 |
3.69e-49 |
|
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: 167.37 E-value: 3.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 106 ELLMGIFEMGWEKPSPIQEESIPIALS-GRDILARAKNGTGKSGAYLIPLLERL-----DLKKDNIQAMVIVPTRELALQ 179
Cdd:cd17964 4 SLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTRELALQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 180 VSQICIQVSKHMGGAKVMATTGGTNLRDDIMRL-DDTVHVVIATPGRILDLIKK-GVAKV-DHVQMIVLDEADKLLSQDF 256
Cdd:cd17964 84 IAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENpGVAKAfTDLDYLVLDEADRLLDMGF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720430166 257 VQIMEDIILTLPKN----RQILLYSATFPLSVQKFMNSHLQKPYE 297
Cdd:cd17964 164 RPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTLKKDYK 208
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
103-286 |
6.15e-47 |
|
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: 161.60 E-value: 6.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 103 LKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLER-LDLKKDN-----IQAMVIVPTREL 176
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKiLKAKAESgeeqgTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 177 ALQVSQICIQVSKHMGGA-KVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKV-DHVQMIVLDEADKLLSQ 254
Cdd:cd17961 81 AQQVSKVLEQLTAYCRKDvRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160
|
170 180 190
....*....|....*....|....*....|..
gi 1720430166 255 DFVQIMEDIILTLPKNRQILLYSATFPLSVQK 286
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEA 192
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
98-279 |
9.89e-47 |
|
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: 160.95 E-value: 9.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERldlkkdnIQAMVIVPTRELA 177
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------VVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 178 LQVSQICIQVSKHMGGAKV--MATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQD 255
Cdd:cd17938 74 EQTYNCIENFKKYLDNPKLrvALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190
....*....|....*....|....*....|
gi 1720430166 256 FVQIMEDIILTLPK------NRQILLYSAT 279
Cdd:cd17938 154 NLETINRIYNRIPKitsdgkRLQVIVCSAT 183
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
111-312 |
1.20e-46 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 160.74 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 111 IFEMGWEKPSPIQEESIPIALSG-RDILARAKNGTGKSGAYLIPLLERLdLKKDNIQAMVIVPTRELALQVSQICIQVSK 189
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 190 HMGGaKVMATTGGTNLRDDIMRL-DDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDIILTLP 268
Cdd:smart00487 80 SLGL-KVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720430166 269 KNRQILLYSATFPLSVQKFMNSHLQKPYEINLmEELTLKGVTQY 312
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDV-GFTPLEPIEQF 201
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
108-300 |
6.53e-46 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 158.61 E-value: 6.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 108 LMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKK----DNIQAMVIVPTRELALQVSQI 183
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERwtpeDGLGALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 184 CIQVSKH--MGGAKVMattGGTNLRDDIMRLdDTVHVVIATPGRILDLIKKGVA-KVDHVQMIVLDEADKLLSQDFVQIM 260
Cdd:cd17941 82 LRKVGKYhsFSAGLII---GGKDVKEEKERI-NRMNILVCTPGRLLQHMDETPGfDTSNLQMLVLDEADRILDMGFKETL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720430166 261 EDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINL 300
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
103-298 |
2.83e-44 |
|
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: 154.27 E-value: 2.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 103 LKRELLMGIFEMGWEKPSPIQEESIPIALSG--RDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELALQV 180
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 181 SQICIQVSKHMgGAKVMATTGGTNLRddiMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQD--FVQ 258
Cdd:cd17963 81 GEVVEKMGKFT-GVKVALAVPGNDVP---RGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTQghGDQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720430166 259 IMEdIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEI 298
Cdd:cd17963 157 SIR-IKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
107-298 |
3.55e-44 |
|
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: 153.86 E-value: 3.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 107 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELALQVSQiciQ 186
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIED---Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 187 VSKHMGGAKVMATT---GGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDI 263
Cdd:cd17962 78 AKELMKGLPPMKTAllvGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDI 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1720430166 264 ILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEI 298
Cdd:cd17962 158 LENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
98-298 |
1.12e-43 |
|
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: 152.76 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELA 177
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 178 LQVSQICIQVSKHMgGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIK---KGVAKVDHVQMIVLDEADKLLSQ 254
Cdd:cd17955 81 YQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720430166 255 DFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEI 298
Cdd:cd17955 160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFW 203
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
98-292 |
2.46e-43 |
|
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: 152.26 E-value: 2.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNI----------QA 167
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 168 MVIVPTRELAlqvSQICIQVSK--HMGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVL 245
Cdd:cd17967 82 LILAPTRELA---IQIYEEARKfsYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720430166 246 DEADKLLSQDFV----QIMEDIILTLPKNRQILLYSATFPLSVQK----FMNSHL 292
Cdd:cd17967 159 DEADRMLDMGFEpqirKIVEHPDMPPKGERQTLMFSATFPREIQRlaadFLKNYI 213
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
107-299 |
1.29e-42 |
|
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: 150.03 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 107 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERL-----DLKKDNIQAMVIVPTRELALQVS 181
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 182 QICIQVSKHMGG-AKVMATTGGTN-LRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVD--HVQMIVLDEADKLLSQDFV 257
Cdd:cd17960 81 EVLQSFLEHHLPkLKCQLLIGGTNvEEDVKKFKRNGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720430166 258 QIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEIN 299
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
107-295 |
2.14e-42 |
|
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: 149.78 E-value: 2.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 107 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERL-------DLKKDNI-QAMVIVPTRELAL 178
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsrlppldEETKDDGpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 179 QVSQICIQVSKHMgGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQ 258
Cdd:cd17945 81 QIEEETQKFAKPL-GIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720430166 259 IMEDIILTLP--------------------KNRQILLYSATFPLSVQKFMNSHLQKP 295
Cdd:cd17945 160 QVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRP 216
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
107-298 |
6.04e-42 |
|
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: 147.95 E-value: 6.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 107 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLL-----ERLDLKKDNIQAMVIVPTRELALQVS 181
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvhimdQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 182 QICIQVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIME 261
Cdd:cd17952 81 LEAKKFGKAYN-LRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720430166 262 DIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEI 298
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
103-298 |
1.36e-39 |
|
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: 142.52 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 103 LKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLER-LDLKK----DNIQAMVIVPTRELA 177
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHiKDQRPvkpgEGPIGLIMAPTRELA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 178 LQVSQICIQVSKHMgGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDH---VQMIVLDEADKLLSQ 254
Cdd:cd17953 99 LQIYVECKKFSKAL-GLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNlrrVTYVVLDEADRMFDM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720430166 255 DF-VQIMEdIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEI 298
Cdd:cd17953 178 GFePQIMK-IVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
107-295 |
2.27e-39 |
|
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: 141.06 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 107 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDL------KKDNIQAMVIVPTRELALQV 180
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLqpipreQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 181 SQICIQVSKHmgGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDF-VQI 259
Cdd:cd17958 81 EAECSKYSYK--GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFePQI 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720430166 260 MEdIILTLPKNRQILLYSATFPLSVQKFMNSHLQKP 295
Cdd:cd17958 159 RK-ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDP 193
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
107-295 |
3.59e-39 |
|
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: 140.42 E-value: 3.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 107 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERL--DLKKDNIQAMVIVPTRELAlqvSQIC 184
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELA---SQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 185 IQVSKHMGG----AKVMATTGGTNLRDDImRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIM 260
Cdd:cd17957 78 RELLKLSKGtglrIVLLSKSLEAKAKDGP-KSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720430166 261 EDIILTLP-KNRQILLYSATFPLSVQKFMNSHLQKP 295
Cdd:cd17957 157 DEILAACTnPNLQRSLFSATIPSEVEELARSVMKDP 192
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
96-296 |
7.70e-39 |
|
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: 141.64 E-value: 7.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 96 NEFEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERL------DLKKDNIQ--- 166
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegltASSFSEVQepq 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 167 AMVIVPTRELALqvsQICIQVSKHMGGAKVMATT--GGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIV 244
Cdd:cd18052 123 ALIVAPTRELAN---QIFLEARKFSYGTCIRPVVvyGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720430166 245 LDEADKLLSQDFV----QIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPY 296
Cdd:cd18052 200 LDEADRMLDMGFGpeirKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFLKEDY 255
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
111-299 |
7.89e-39 |
|
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: 139.81 E-value: 7.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 111 IFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIP---------LLERldlkKDNIQAMVIVPTRELALQVS 181
Cdd:cd17966 5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPaivhinaqpPLER----GDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 182 QICIQVSkHMGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIME 261
Cdd:cd17966 81 QEANKFG-GSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720430166 262 DIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEIN 299
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
108-279 |
7.37e-37 |
|
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: 134.41 E-value: 7.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 108 LMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLE---RLDLKKDN-IQAMVIVPTRELALQVSQI 183
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyKLKFKPRNgTGVIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 184 CIQVSKHmGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILD-LIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMED 262
Cdd:cd17942 82 AKELLKY-HSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
|
170
....*....|....*..
gi 1720430166 263 IILTLPKNRQILLYSAT 279
Cdd:cd17942 161 IIKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
114-295 |
8.88e-36 |
|
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: 131.94 E-value: 8.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 114 MGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQ------AMVIVPTRELALQVSQICIQV 187
Cdd:cd17949 9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 188 SKHMGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVA-KVDHVQMIVLDEADKLLSQDFVQIMEDII-- 264
Cdd:cd17949 89 LKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADRLLDMGFEKDITKILel 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720430166 265 -----------LTLPKNRQILLYSATFPLSVQKFMNSHLQKP 295
Cdd:cd17949 169 lddkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDP 210
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
84-305 |
2.11e-35 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 131.68 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 84 RIKTSDVTSTKgnEFEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSG--RDILARAKNGTGKSGAYLIPLLERLDLK 161
Cdd:cd18048 8 RDPTSPLFSVK--SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 162 KDNIQAMVIVPTRELALQVSQICIQVSKHMGGAKVMATTGGTNLRDDImrlDDTVHVVIATPGRILD-LIKKGVAKVDHV 240
Cdd:cd18048 86 KLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGT---DIEAQIVIGTPGTVLDwCFKLRLIDVTNI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720430166 241 QMIVLDEADKLLS-QDFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINL-MEELT 305
Cdd:cd18048 163 SVFVLDEADVMINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLkKEELT 229
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
107-280 |
7.96e-35 |
|
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: 130.05 E-value: 7.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 107 LLMGIFEMGWEKPSPIQEESIPIALS-GRDILARAKNGTGKSGAYLIPLLER-LDLKKDNI--------QAMVIVPTREL 176
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERlLSQKSSNGvggkqkplRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 177 ALQVSQICIQVSKHmGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKG---VAKVDHVQMIVLDEADKLLS 253
Cdd:cd17946 81 AVQVKDHLKAIAKY-TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLE 159
|
170 180 190
....*....|....*....|....*....|....
gi 1720430166 254 QDFVQIMEDIILTLPKN-------RQILLYSATF 280
Cdd:cd17946 160 KGHFAELEKILELLNKDragkkrkRQTFVFSATL 193
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
107-299 |
1.14e-34 |
|
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: 128.61 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 107 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLL-------ERLD-LKKDNIQAMVIVPTRELAL 178
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqeKKLPfIKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 179 QVSQICIQVSKHMGGA-----KVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLS 253
Cdd:cd17951 81 QTHEVIEYYCKALQEGgypqlRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720430166 254 QDFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEIN 299
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
96-285 |
3.78e-34 |
|
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: 128.62 E-value: 3.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 96 NEFEDYCLKrELLMGIFEMG-WEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERL---------------- 158
Cdd:cd18051 21 ETFSDLDLG-EIIRNNIELArYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgeslpsesgyy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 159 DLKKDNIQAMVIVPTRELAlqvSQICIQVSK--HMGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAK 236
Cdd:cd18051 100 GRRKQYPLALVLAPTRELA---SQIYDEARKfaYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720430166 237 VDHVQMIVLDEADKLLSQDFVQIMEDIIL--TLPK--NRQILLYSATFPLSVQ 285
Cdd:cd18051 177 LDYCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPtgERQTLMFSATFPKEIQ 229
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
320-429 |
2.00e-31 |
|
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: 116.54 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 320 QKVHCLNTLFSRLQINQSIIFCNSSQRVEllAKKI-SQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGI 398
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLlEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 1720430166 399 DIQAVNVVINFDFPKLAETYLHRIGRSGRFG 429
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
97-300 |
7.87e-31 |
|
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: 119.34 E-value: 7.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 97 EFEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKK-----DNIQAMVIV 171
Cdd:cd18049 25 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflergDGPICLVLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 172 PTRELALQVSQICIQVSKhmgGAKVMATT--GGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEAD 249
Cdd:cd18049 105 PTRELAQQVQQVAAEYGR---ACRLKSTCiyGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEAD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720430166 250 KLLSQDFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINL 300
Cdd:cd18049 182 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
111-300 |
1.56e-30 |
|
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: 119.35 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 111 IFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDL-----KKDNIQAMVIVPTRELALQVSQICI 185
Cdd:cd18050 77 LLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHqpyleRGDGPICLVLAPTRELAQQVQQVAD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 186 QVSKHmGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDIIL 265
Cdd:cd18050 157 DYGKS-SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD 235
|
170 180 190
....*....|....*....|....*....|....*
gi 1720430166 266 TLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINL 300
Cdd:cd18050 236 QIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
113-289 |
6.32e-30 |
|
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: 116.70 E-value: 6.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 113 EMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDN-------IQAMVIVPTRELALQVSQICI 185
Cdd:cd17948 7 RQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLaegpfnaPRGLVITPSRELAEQIGSVAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 186 QVSKHMGgAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDII- 264
Cdd:cd17948 87 SLTEGLG-LKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLr 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720430166 265 ----------LTLPKNR--QILLYSATFPLSVQKFMN 289
Cdd:cd17948 166 rfplasrrseNTDGLDPgtQLVLVSATMPSGVGEVLS 202
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
98-295 |
8.18e-28 |
|
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: 110.19 E-value: 8.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 98 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSG--RDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRE 175
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 176 LALQVSQICIQVSKHMGGAKVMATTGGTNLRDDImRLDDtvHVVIATPGRILD-LIKKGVAKVDHVQMIVLDEADKLLSQ 254
Cdd:cd18047 83 LALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQ-KISE--QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIAT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720430166 255 DFVQIME-DIILTLPKNRQILLYSATFPLSVQKFMNSHLQKP 295
Cdd:cd18047 160 QGHQDQSiRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
121-297 |
1.79e-27 |
|
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: 109.17 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 121 PIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNI------QAMVIVPTRELALQVSQICIQVSKHMgga 194
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQVTKDFKDITRKL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 195 KVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDIILTLPK----- 269
Cdd:cd17944 92 SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSYKkdsed 171
|
170 180
....*....|....*....|....*...
gi 1720430166 270 NRQILLYSATFPLSVQKFMNSHLQKPYE 297
Cdd:cd17944 172 NPQTLLFSATCPDWVYNVAKKYMKSQYE 199
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
113-294 |
4.74e-27 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 108.49 E-value: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 113 EMGWEKPSPIQEESIPIALSG---------RDILARAKNGTGKSGAYLIPLLERL-DLKKDNIQAMVIVPTRELALQVSQ 182
Cdd:cd17956 7 NNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKELVQQVYK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 183 ICIQVSKHMgGAKVMATTGGTNLRDDIM--------RLDDTVHVVIATPGRILDLIKKGVA-KVDHVQMIVLDEADKLLS 253
Cdd:cd17956 87 VFESLCKGT-GLKVVSLSGQKSFKKEQKlllvdtsgRYLSRVDILVATPGRLVDHLNSTPGfTLKHLRFLVIDEADRLLN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720430166 254 QDFvQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQK 294
Cdd:cd17956 166 QSF-QDWLETVMKALGRPTAPDLGSFGDANLLERSVRPLQK 205
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
348-429 |
2.63e-26 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 101.52 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 348 ELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRIGRSGR 427
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1720430166 428 FG 429
Cdd:smart00490 81 AG 82
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
118-301 |
1.10e-19 |
|
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: 88.20 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 118 KPSPIQEESIPIALSGRDILAR----------------AKNGTGKSGAYLIPLLERL---------------DLKKDN-- 164
Cdd:cd17965 30 KPSPIQTLAIKKLLKTLMRKVTkqtsneepklevfllaAETGSGKTLAYLAPLLDYLkrqeqepfeeaeeeyESAKDTgr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 165 IQAMVIVPTRELALQVSQICIQVSKHMG-GAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIK---KGVAKVDHV 240
Cdd:cd17965 110 PRSVILVPTHELVEQVYSVLKKLSHTVKlGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKsrpKILSRVTHL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720430166 241 qmiVLDEADKLLSQDFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNShlQKPYEINLM 301
Cdd:cd17965 190 ---VVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRK--LFPDVVRIA 245
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
133-279 |
2.64e-15 |
|
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: 72.82 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 133 GRDILARAKNGTGKSGAYLIPLLERLDLKKDniQAMVIVPTRELALQVSQICIQVSKHmgGAKVMATTGGTNLRDDIMRL 212
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGK--KVLVLVPTKALALQTAERLRELFGP--GIRVAVLVGGSSAEEREKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 213 DDTVHVVIATPGRILDLIKKGVA-KVDHVQMIVLDEADKLL--SQDFVQIMEDIILTLPKNRQILLYSAT 279
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLREDRlFLKDLKLIIVDEAHALLidSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
143-407 |
9.57e-14 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 73.52 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 143 GTGKS--GAYLIpllERLDLKKdniQAMVIVPTRELALQVSQiciQVSKHMGGAKVmatTGGtnlrddimRLDDTVHVVI 220
Cdd:COG1061 110 GTGKTvlALALA---AELLRGK---RVLVLVPRRELLEQWAE---ELRRFLGDPLA---GGG--------KKDSDAPITV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 221 ATpgrILDLIKKGVAK--VDHVQMIVLDEADKLLSQDFVQIMEDIiltlpKNRQILLYSAT------------------F 280
Cdd:COG1061 170 AT---YQSLARRAHLDelGDRFGLVIIDEAHHAGAPSYRRILEAF-----PAAYRLGLTATpfrsdgreillflfdgivY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 281 PLSVQKFMNSHLQKPYEI-----------NLMEELTlKGVTQYYAYVTERqKVHCLNTLFSRL-QINQSIIFCNSSQRVE 348
Cdd:COG1061 242 EYSLKEAIEDGYLAPPEYygirvdltderAEYDALS-ERLREALAADAER-KDKILRELLREHpDDRKTLVFCSSVDHAE 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720430166 349 LLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVI 407
Cdd:COG1061 320 ALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
338-429 |
1.39e-13 |
|
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: 67.62 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 338 IIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAET 417
Cdd:cd18794 34 IIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMES 113
|
90
....*....|..
gi 1720430166 418 YLHRIGRSGRFG 429
Cdd:cd18794 114 YYQESGRAGRDG 125
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
89-482 |
5.30e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 71.08 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 89 DVTSTKGNEFEDYCLKRellmGIFEMgwekpSPIQEESIP-IALSGRDILARAKNGTGKSgayLI---PLLERLDLKKDn 164
Cdd:COG1204 2 KVAELPLEKVIEFLKER----GIEEL-----YPPQAEALEaGLLEGKNLVVSAPTASGKT---LIaelAILKALLNGGK- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 165 iqAMVIVPTRELAlqvSQICIQVSKHMG--GAKVMATTGGTNLRDDIMRLDDtvhVVIATPGRILDLIKKGVAKVDHVQM 242
Cdd:COG1204 69 --ALYIVPLRALA---SEKYREFKRDFEelGIKVGVSTGDYDSDDEWLGRYD---ILVATPEKLDSLLRNGPSWLRDVDL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 243 IVLDEADKLLSQDFVQIMEDII---LTLPKNRQILLYSATFPlSVQKF---MNSHL----QKPyeINLMEELTLKGVTqY 312
Cdd:COG1204 141 VVVDEAHLIDDESRGPTLEVLLarlRRLNPEAQIVALSATIG-NAEEIaewLDAELvksdWRP--VPLNEGVLYDGVL-R 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 313 YAYVTERQKVHCLNTLFSRLQIN-QSIIFCNSSQRVELLAKKISQ-LGYSCFYI-------------------------- 364
Cdd:COG1204 217 FDDGSRRSKDPTLALALDLLEEGgQVLVFVSSRRDAESLAKKLADeLKRRLTPEereeleelaeellevseethtnekla 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 365 ----------HAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVI-------NFDFPKLaeTYLHRIGRSGR 427
Cdd:COG1204 297 dclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIrdtkrggMVPIPVL--EFKQMAGRAGR 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720430166 428 FGH--LGLAInLITYDDRFNLKSIEEQLGTEIKPIPSNI--DKSLY---VAEYHSEPAEDEK 482
Cdd:COG1204 375 PGYdpYGEAI-LVAKSSDEADELFERYILGEPEPIRSKLanESALRthlLALIASGFANSRE 435
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
115-429 |
3.08e-11 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 65.50 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 115 GWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLER----------LDLKKDN--------IQAMVIVPT--R 174
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLdgltlvvsplISLMKDQvdqllangVAAACLNSTqtR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 175 ELALQVSQICiqvskHMGGAKVMATTGGTNLRDDIM-RLDDTVHVVIATPG---------------RILDLIKKgvaKVD 238
Cdd:PRK11057 102 EQQLEVMAGC-----RTGQIKLLYIAPERLMMDNFLeHLAHWNPALLAVDEahcisqwghdfrpeyAALGQLRQ---RFP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 239 HVQMIVLDE-ADKLLSQDFVQIMEdiiLTLPknrqiLLYSATFPLSVQKFMnshlqkpyeinLMEELtlKGVTQYYAYVT 317
Cdd:PRK11057 174 TLPFMALTAtADDTTRQDIVRLLG---LNDP-----LIQISSFDRPNIRYT-----------LVEKF--KPLDQLMRYVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 318 ErQKVHClntlfsrlqinqSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRG 397
Cdd:PRK11057 233 E-QRGKS------------GIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMG 299
|
330 340 350
....*....|....*....|....*....|..
gi 1720430166 398 IDIQAVNVVINFDFPKLAETYLHRIGRSGRFG 429
Cdd:PRK11057 300 INKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
338-456 |
9.88e-11 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 63.62 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 338 IIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAET 417
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1720430166 418 YLHRIGRSGRFGHLGLAINLITYDDRFNLKS-IEEQLGTE 456
Cdd:COG0514 314 YYQEIGRAGRDGLPAEALLLYGPEDVAIQRFfIEQSPPDE 353
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
123-442 |
1.18e-08 |
|
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: 57.54 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 123 QEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLdLKKDNIQAMVIVPTRELAL-QVSQIcIQVSKHMG-GAKVMATT 200
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPTKALARdQLRRL-RELAEALGlGVRVATYD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 201 GGT--NLRDDIMrldDTVHVVIATPgrilDLIkkgvakvdHVQM----------------IVLDE--------------- 247
Cdd:COG1205 139 GDTppEERRWIR---EHPDIVLTNP----DML--------HYGLlphhtrwarffrnlryVVIDEahtyrgvfgshvanv 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 248 ------------------------------ADKLLSQDFVQIMEDiilTLPK-NRQILLYSAtfPLSVQKFMNSHLQkpy 296
Cdd:COG1205 204 lrrlrricrhygsdpqfilasatignpaehAERLTGRPVTVVDED---GSPRgERTFVLWNP--PLVDDGIRRSALA--- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 297 E-INLMEELTLKGVtqyyayvterqkvhclntlfsrlqinQSIIFCNSSQRVELLAKKISQL-----------GYscfyi 364
Cdd:COG1205 276 EaARLLADLVREGL--------------------------RTLVFTRSRRGAELLARYARRAlrepdladrvaAY----- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 365 HAKMRQEHRNRVFHDFRNGLCRNLVCT---DLftrGIDIQAVNVVINFDFPKLAETYLHRIGRSGRFGHLGLAInLITYD 441
Cdd:COG1205 325 RAGYLPEERREIERGLRSGELLGVVSTnalEL---GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGD 400
|
.
gi 1720430166 442 D 442
Cdd:COG1205 401 D 401
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
113-442 |
1.53e-08 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 57.13 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 113 EMGWEKPSPIQEESIPI-ALSGRDILARAKNGTGKSGAYLIPLLERLdlKKDNIQAMVIVPTRELALQVSQICIQVSKHm 191
Cdd:PRK00254 18 ERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKL--LREGGKAVYLVPLKALAEEKYREFKDWEKL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 192 gGAKVMATTGGTNLRDDIMRLDDtvhVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDIILTLPKNR 271
Cdd:PRK00254 95 -GLRVAMTTGDYDSTDEWLGKYD---IIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 272 QILLYSATF--PLSVQKFMNSHL----QKPYEINlmeeltlKGVTqYYAYVT-ERQKVHCLNTLFSRLQIN------QSI 338
Cdd:PRK00254 171 QILGLSATVgnAEELAEWLNAELvvsdWRPVKLR-------KGVF-YQGFLFwEDGKIERFPNSWESLVYDavkkgkGAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 339 IFCNSSQRVE----LLAKKISQL------------------------------GYSCFYiHAKMRQEHRNRVFHDFRNGL 384
Cdd:PRK00254 243 VFVNTRRSAEkealELAKKIKRFltkpelralkeladsleenptneklkkalrGGVAFH-HAGLGRTERVLIEDAFREGL 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720430166 385 CRNLVCTDLFTRGIDIQAVNVVINfDFPKLAETYLHRI---------GRSGR--FGHLGLAINLITYDD 442
Cdd:PRK00254 322 IKVITATPTLSAGINLPAFRVIIR-DTKRYSNFGWEDIpvleiqqmmGRAGRpkYDEVGEAIIVATTEE 389
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
121-281 |
3.51e-08 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 53.03 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 121 PIQEESI-PIALSGRDILARAKNGTGKSgayLIPLLERLD-LKKDNIQAMVIVPTRELALQVSQICIQVSKHMGGAKVMA 198
Cdd:cd17921 4 PIQREALrALYLSGDSVLVSAPTSSGKT---LIAELAILRaLATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 199 TTGGTnlrDDIMRLDDTvHVVIATPgRILD--LIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDIILTLP---KNRQI 273
Cdd:cd17921 81 TGDPS---VNKLLLAEA-DILVATP-EKLDllLRNGGERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrinKNARF 155
|
....*...
gi 1720430166 274 LLYSATFP 281
Cdd:cd17921 156 VGLSATLP 163
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
388-429 |
4.99e-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: 50.01 E-value: 4.99e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1720430166 388 LVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRIGRSGRFG 429
Cdd:cd18785 26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
321-424 |
6.18e-08 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 51.44 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 321 KVHCL-NTL---FSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAK-------------MRQEHRN--RVFHDFR 381
Cdd:cd18802 8 KLQKLiEILreyFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrSLMTQRKqkETLDKFR 87
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1720430166 382 NGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRIGR 424
Cdd:cd18802 88 DGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
336-435 |
1.04e-07 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 51.10 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 336 QSIIFCNSSQRVEL--------------LAKKIS--QLGYscfyihakmRQEHRNRVFHDFRNGLCRNLVCTDLFTRGID 399
Cdd:cd18797 37 KTIVFCRSRKLAELllrylkarlveegpLASKVAsyRAGY---------LAEDRREIEAELFNGELLGVVATNALELGID 107
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720430166 400 IQAVNVVINFDFPKLAETYLHRIGRSGRFGHLGLAI 435
Cdd:cd18797 108 IGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
328-427 |
1.27e-07 |
|
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: 50.73 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 328 LFSRLQINQSIIFCNSSQRVELLAKKISQLGYSC-----FYIH-AKMRQEHRNRVFHDFRNGLCRNLVCT---DLftrGI 398
Cdd:cd18796 32 IFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRvppdfIALHhGSLSRELREEVEAALKRGDLKVVVATsslEL---GI 108
|
90 100
....*....|....*....|....*....
gi 1720430166 399 DIQAVNVVINFDFPKLAETYLHRIGRSGR 427
Cdd:cd18796 109 DIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
123-248 |
3.90e-07 |
|
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: 50.28 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 123 QEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLdLKKDNIQAMVIVPTRELAL-QVSQICIQVSKHMGGAKVMATTG 201
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAQdQLRSLRELLEQLGLGIRVATYDG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1720430166 202 GTNLRDDIMRLDDTVHVVIATPgRILD--LIKKGVAKVDHVQM---IVLDEA 248
Cdd:cd17923 84 DTPREERRAIIRNPPRILLTNP-DMLHyaLLPHHDRWARFLRNlryVVLDEA 134
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
338-429 |
8.93e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 51.65 E-value: 8.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 338 IIFCNSSQRVELLAKKISQLGYSC--FYIHAK------MRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINF 409
Cdd:COG1111 357 IVFTQYRDTAEMIVEFLSEPGIKAgrFVGQASkegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFY 436
|
90 100
....*....|....*....|.
gi 1720430166 410 DfPKLAET-YLHRIGRSGRFG 429
Cdd:COG1111 437 E-PVPSEIrSIQRKGRTGRKR 456
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
347-430 |
1.09e-06 |
|
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: 48.11 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 347 VELLAKKISQL--GYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLH---- 420
Cdd:cd18810 38 IEKLATQLRQLvpEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYqlrg 117
|
90
....*....|
gi 1720430166 421 RIGRSGRFGH 430
Cdd:cd18810 118 RVGRSKERAY 127
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
337-423 |
2.17e-06 |
|
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: 47.09 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 337 SIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGL--CRNLVCTDLFTRGIDIQAVNVVINFDFP-- 412
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPWwn 109
|
90
....*....|....*
gi 1720430166 413 --KL--AETYLHRIG 423
Cdd:cd18793 110 paVEeqAIDRAHRIG 124
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
345-451 |
5.99e-06 |
|
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: 46.11 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 345 QRVELLAKKISQL--GYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLH-- 420
Cdd:cd18792 45 KSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHql 124
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720430166 421 --RIGRSGRFGHLGLAIN---LITYDDRFNLKSIEE 451
Cdd:cd18792 125 rgRVGRGKHQSYCYLLYPdpkKLTETAKKRLRAIAE 160
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
335-427 |
6.64e-06 |
|
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: 46.01 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 335 NQSIIFCNSSQRVELLAKKISQLGyscfYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVIN------ 408
Cdd:cd18795 44 KPVLVFCSSRKECEKTAKDLAGIA----FHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKgtqryd 119
|
90 100
....*....|....*....|..
gi 1720430166 409 ---FDFPKLAEtYLHRIGRSGR 427
Cdd:cd18795 120 gkgYRELSPLE-YLQMIGRAGR 140
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
347-450 |
8.96e-06 |
|
transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273152 [Multi-domain] Cd Length: 926 Bit Score: 48.51 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 347 VELLAKKISQL--GYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRI-G 423
Cdd:TIGR00580 673 IEKLATQLRELvpEARIAIAHGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIERADKFGLAQLYQLrG 752
|
90 100
....*....|....*....|....*..
gi 1720430166 424 RSGRFGHLGLAINLITYDDRFNLKSIE 450
Cdd:TIGR00580 753 RVGRSKKKAYAYLLYPHQKALTEDAQK 779
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
123-466 |
1.47e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 47.57 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 123 QEESIPIALSGRDILARAKNGTGKSgayLIPLLERLDLKKDNIQAMVIVPTRELALQVSQICIQVSKHmgGAKVMATTGG 202
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKT---LIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELSRLRSL--GMRVKISIGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 203 TNLRDDIMRLDDtvhVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDIILTL----PKNRqILLYSA 278
Cdd:PRK01172 102 YDDPPDFIKRYD---VVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSAryvnPDAR-ILALSA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 279 TFP--LSVQKFMNSHLQK------PYEINLM--EELTLKGvtqyyayvTERQKVHCLNTLFSRLQIN-QSIIFCNSSQRV 347
Cdd:PRK01172 178 TVSnaNELAQWLNASLIKsnfrpvPLKLGILyrKRLILDG--------YERSQVDINSLIKETVNDGgQVLVFVSSRKNA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 348 ELLAKKISQ-------------------------LGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQA 402
Cdd:PRK01172 250 EDYAEMLIQhfpefndfkvssennnvyddslnemLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPA 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720430166 403 VNVVIN--FDFPKLAETYL------HRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEIKPIPSNIDK 466
Cdd:PRK01172 330 RLVIVRdiTRYGNGGIRYLsnmeikQMIGRAGRPGYDQYGIGYIYAASPASYDAAKKYLSGEPEPVISYMGS 401
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
118-248 |
2.40e-05 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 45.34 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 118 KPSPIQEESIPIALSgRDILARAKNGTGKS--GAYLIPLLERLDLKKDNIQAMVI--VPTRELalqVSQICIQVSKHMGg 193
Cdd:cd18034 2 TPRSYQLELFEAALK-RNTIVVLPTGSGKTliAVMLIKEMGELNRKEKNPKKRAVflVPTVPL---VAQQAEAIRSHTD- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720430166 194 AKVMATTGGTNL----RDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEA 248
Cdd:cd18034 77 LKVGEYSGEMGVdkwtKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
338-427 |
2.52e-05 |
|
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: 44.27 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 338 IIFCNSSQRVELLAKKISQLGY----SCFYIHAK------MRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVI 407
Cdd:cd18801 34 IIFSEFRDSAEEIVNFLSKIRPgiraTRFIGQASgksskgMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLII 113
|
90 100
....*....|....*....|
gi 1720430166 408 NFDFPKLAETYLHRIGRSGR 427
Cdd:cd18801 114 CYDASPSPIRMIQRMGRTGR 133
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
338-407 |
5.72e-05 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 42.55 E-value: 5.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720430166 338 IIFCNSSQRVELLAKKISQLGYSCFYIHAK--MRQEHRNRVFHDFRNGLCRN-LVCTDLFTRGIDIQAVNVVI 407
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFFGELKPPiLVTVDLLTTGVDIPEVDNVV 82
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
337-426 |
8.51e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 45.09 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 337 SIIFCNS-SQrVELLAKKISQLGYSCFYI----HAKMRQEHRNRVFHDFRNGLCRNLVCT---DLftrGIDIQAVNVVIN 408
Cdd:COG1201 275 TLVFTNTrSQ-AERLFQRLNELNPEDALPiaahHGSLSREQRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQ 350
|
90
....*....|....*...
gi 1720430166 409 FDFPKLAETYLHRIGRSG 426
Cdd:COG1201 351 VGSPKSVARLLQRIGRAG 368
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
338-459 |
1.17e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 44.89 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 338 IIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCrNLVC-TDLFTRGIDIQAVNVVINFDFPKLAE 416
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEI-NIICaTVAFGMGINKPDVRFVIHHSLPKSIE 762
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1720430166 417 TYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEIKP 459
Cdd:PLN03137 763 GYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSP 805
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
338-429 |
1.44e-04 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 44.45 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 338 IIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRN--LVCTDLFTRGIDIQAVNVVINFDFP--- 412
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPvfLISLKAGGEGLNLTAADHVIHYDLWwnp 632
|
90
....*....|....*...
gi 1720430166 413 -KLAEtylhRIGRSGRFG 429
Cdd:COG0553 633 aVEEQ----AIDRAHRIG 646
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
120-295 |
1.99e-04 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 42.63 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 120 SPIQEESIPIALSGRDILARAKNGTGKSGAYLIP-LLerLDLKKDNIqAMVIVPTreLAL---QVSqiciQVSKHMGGAK 195
Cdd:cd18018 14 RPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPaLL--LRRRGPGL-TLVVSPL--IALmkdQVD----ALPRAIKAAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 196 VMATTGGTNLRDDIMRLD-DTVHVVIATPGRILDL-IKKGVAKVDHVQMIVLDEADKL--LSQDF---VQIMEDIILTLP 268
Cdd:cd18018 85 LNSSLTREERRRILEKLRaGEVKILYVSPERLVNEsFRELLRQTPPISLLVVDEAHCIseWSHNFrpdYLRLCRVLRELL 164
|
170 180
....*....|....*....|....*..
gi 1720430166 269 KNRQILLYSATFPLSVQKFMNSHLQKP 295
Cdd:cd18018 165 GAPPVLALTATATKRVVEDIASHLGIP 191
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
364-430 |
2.16e-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: 2.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430166 364 IHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRI-GRSGRFGH 430
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGRGDH 134
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
114-248 |
2.31e-04 |
|
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: 42.14 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 114 MGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIP--LLERLdlkkdniqAMVIVPTreLAL---QVSQiCIQVs 188
Cdd:cd17920 8 FGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV--------TLVVSPL--ISLmqdQVDR-LQQL- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720430166 189 khmgGAKVMATTGGT----NLRDDIMRLDDTVHVVIATP-----GRILDLIKKgVAKVDHVQMIVLDEA 248
Cdd:cd17920 76 ----GIRAAALNSTLspeeKREVLLRIKNGQYKLLYVTPerllsPDFLELLQR-LPERKRLALIVVDEA 139
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
121-281 |
2.71e-04 |
|
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: 41.55 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 121 PIQEESIPIAL-SGRDILARAKNGTGKSgayLIPLLERLDLKKDNIQAMVIVPTRELAlqvSQICIQVSKHMG-GAKVMA 198
Cdd:cd18028 4 PPQAEAVRAGLlKGENLLISIPTASGKT---LIAEMAMVNTLLEGGKALYLVPLRALA---SEKYEEFKKLEEiGLKVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430166 199 TTGGTNLRDDimRLDDTvHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDII---LTLPKNRQILL 275
Cdd:cd18028 78 STGDYDEDDE--WLGDY-DIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVarlRRLNPNTQIIG 154
|
....*.
gi 1720430166 276 YSATFP 281
Cdd:cd18028 155 LSATIG 160
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
365-434 |
7.28e-04 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 42.42 E-value: 7.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720430166 365 HAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVI--NFDFPKLAEtyLHRI-GRSGRFGHLGLA 434
Cdd:PRK10689 842 HGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIieRADHFGLAQ--LHQLrGRVGRSHHQAYA 912
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
365-426 |
2.10e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 40.68 E-value: 2.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720430166 365 HAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRIGRSG 426
Cdd:PRK09751 308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| CMS1 |
pfam14617 |
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant ... |
216-293 |
6.52e-03 |
|
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant CMS1-like proteins. The family has similarity to the DEAD-box helicases.
Pssm-ID: 373164 Cd Length: 250 Bit Score: 38.31 E-value: 6.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430166 216 VHVVIATPGRILDLIKKGVAKVDHVQMIVLDEAdkllsqdFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQ 293
Cdd:pfam14617 176 IGIGVGTPGRIADLLENESLSVDNLKYIILDAS-------FRDIKNRGILDIRETRKAVIKFLTSKTVLERMAEGKVK 246
|
|
| |
