|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
99-462 |
5.19e-137 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 401.06 E-value: 5.19e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDL-KKDSIQAVVIVPTREL 177
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPTREL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 178 ALQVSQICIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDF 257
Cdd:COG0513 84 ALQVAEELRKLAKYLG-LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 258 VQMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEINLM-EELTLKGVTQYYAYVTERQKVHCLNTLFSRLQIN 336
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVApENATAETIEQRYYLVDKRDKLELLRRLLRDEDPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 337 QSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLG 416
Cdd:COG0513 243 RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDP 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 68444623 417 ETYLHRIGRSGRFGHLGLAINLITYDDRFNLKGIEEQLGTEIKPIP 462
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 ... |
99-300 |
5.48e-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: 390.12 E-value: 5.48e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELA 178
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 179 LQVSQICIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFV 258
Cdd:cd17940 81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 68444623 259 QMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEIN 300
Cdd:cd17940 160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
99-474 |
3.66e-99 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 303.67 E-value: 3.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELA 178
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 179 LQVSQICIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFV 258
Cdd:PTZ00424 110 QQIQKVVLALGDYLK-VRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 259 QMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEINL-MEELTLKGVTQYYAYV-TERQKVHCLNTLFSRLQIN 336
Cdd:PTZ00424 189 GQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVkKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETLTIT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 337 QSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLG 416
Cdd:PTZ00424 269 QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 68444623 417 ETYLHRIGRSGRFGHLGLAINLITYDDRFNLKGIEEQLGTEIKPIPssidksLYVAEY 474
Cdd:PTZ00424 349 ENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMP------MEVADY 400
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
104-463 |
1.84e-92 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 288.24 E-value: 1.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 104 LKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELALQVSQ 183
Cdd:PRK11776 11 LPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 184 ICIQVSKHMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEE 263
Cdd:PRK11776 91 EIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 264 ILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEINLMEELTLKGVTQYYAYVTERQKVHCLNTLFSRLQINQSIIFCN 343
Cdd:PRK11776 171 IIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDERLPALQRLLLHHQPESCVVFCN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 344 SSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLGETYLHRI 423
Cdd:PRK11776 251 TKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRI 330
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 68444623 424 GRSGRFGHLGLAINLITYDDRFNLKGIEEQLGTEIK--PIPS 463
Cdd:PRK11776 331 GRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNwePLPS 372
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
108-299 |
1.21e-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: 246.20 E-value: 1.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 108 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERID----LKKDSIQAVVIVPTRELALQVSQ 183
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLpepkKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 184 ICIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEE 263
Cdd:cd00268 81 VARKLGKGTG-LKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 68444623 264 ILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEI 299
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
99-460 |
5.59e-75 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 242.16 E-value: 5.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLER-IDL-KKDSIQAVVIV--PT 174
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHlLDFpRRKSGPPRILIltPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 175 RELALQVSQICIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLS 254
Cdd:PRK11192 83 RELAMQVADQARELAKHTH-LDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 255 QDFVQMMEEILSSLSKQRQILLYSATFPLS-VQKFMNSHLQKPYEIN----LMEEltlKGVTQ-YYAYVTERQKVHCLNT 328
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEaepsRRER---KKIHQwYYRADDLEHKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 329 LFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVI 408
Cdd:PRK11192 239 LLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 68444623 409 NFDFPKLGETYLHRIGRSGRFGHLGLAINLITYDDRFNLKGIEEQLGTEIKP 460
Cdd:PRK11192 319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKA 370
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
99-461 |
2.24e-72 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 240.91 E-value: 2.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELA 178
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 179 LQVSQICIQVSKHMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFV 258
Cdd:PRK11634 88 VQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 259 QMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEINLMEELTLK-GVTQYYAYVTERQKVHCLNTLFSRLQINQ 337
Cdd:PRK11634 168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRpDISQSYWTVWGMRKNEALVRFLEAEDFDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 338 SIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLGE 417
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 68444623 418 TYLHRIGRSGRFGHLGLAINLITYDDRFNLKGIEEQLGTEIKPI 461
Cdd:PRK11634 328 SYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEV 371
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
99-458 |
2.32e-71 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 233.55 E-value: 2.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLK------KDSIQAVVIV 172
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqphakgRRPVRALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 173 PTRELALQVSQICIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKL 252
Cdd:PRK10590 83 PTRELAAQIGENVRDYSKYLN-IRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 253 LSQDFVQMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEINLMEELTL-KGVTQYYAYVTERQKVHCLNTLFS 331
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTAsEQVTQHVHFVDKKRKRELLSQMIG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 332 RLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFD 411
Cdd:PRK10590 242 KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYE 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 68444623 412 FPKLGETYLHRIGRSGRFGHLGLAINLITYDDRFNLKGIEEQLGTEI 458
Cdd:PRK10590 322 LPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
99-442 |
1.42e-67 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 226.19 E-value: 1.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKrellmGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERID----LKK-DSIQAVVIVP 173
Cdd:PTZ00110 137 FPDYILK-----SLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINaqplLRYgDGPIVLVLAP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 174 TRELALQVSQICIQVSKhMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLL 253
Cdd:PTZ00110 212 TRELAEQIREQCNKFGA-SSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRML 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 254 SQDFVQMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHL-QKPYEINLmEELTLKG---VTQYYAYVTERQKVHCLNTL 329
Cdd:PTZ00110 291 DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNV-GSLDLTAchnIKQEVFVVEEHEKRGKLKML 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 330 FSRLQINQS--IIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVV 407
Cdd:PTZ00110 370 LQRIMRDGDkiLIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYV 449
|
330 340 350
....*....|....*....|....*....|....*
gi 68444623 408 INFDFPKLGETYLHRIGRSGRFGHLGLAINLITYD 442
Cdd:PTZ00110 450 INFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPD 484
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
11-459 |
1.21e-66 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 221.71 E-value: 1.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 11 ILGLSNQNGQMRGSVKPAGGPGGGGGGSQTTQPAQVKASSTVNNGNSQPV---PTANTIIKPGDDWK-KNLKLPPKDlrM 86
Cdd:PRK01297 8 IFGKGEAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEKPKkdkPRRERKPKPASLWKlEDFVVEPQE--G 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 87 KTsdvtatkgnEFEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLEriDLKKDSI 166
Cdd:PRK01297 86 KT---------RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIIN--QLLQTPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 167 Q---------AVVIVPTRELALQVSQICIQVSKHMGgVKVMATTGGTNLRDDIMRLDET-VHVVIATPGRILDLIKKGVA 236
Cdd:PRK01297 155 PkerymgeprALIIAPTRELVVQIAKDAAALTKYTG-LNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 237 KVGQVQMIVLDEADKLLSQDFVQMMEEIL--SSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEINL-MEELTLKGVTQY 313
Cdd:PRK01297 234 HLDMVEVMVLDEADRMLDMGFIPQVRQIIrqTPRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIePENVASDTVEQH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 314 YAYVTERQKVHCLNTLFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTD 393
Cdd:PRK01297 314 VYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68444623 394 LFTRGIDIQAVNVVINFDFPKLGETYLHRIGRSGRFGHLGLAINLITYDDRFNLKGIEEQLGTEIK 459
Cdd:PRK01297 394 VAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIS 459
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
101-299 |
1.07e-55 |
|
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: 184.45 E-value: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 101 DYCLKRELLMGIFEMGWEKPSPIQEESI-PIaLSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELAL 179
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIvPI-IKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 180 QVSQICIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQ 259
Cdd:cd17939 80 QIQKVVKALGDYM-GVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 68444623 260 MMEEILSSLSKQRQILLYSATFPLSV----QKFMNshlqKPYEI 299
Cdd:cd17939 159 QIYDIFQFLPPETQVVLFSATMPHEVlevtKKFMR----DPVRI 198
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
121-288 |
6.28e-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: 6.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 121 SPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELALQVSQICIQVSKHMgGVKVMAT 200
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 201 TGGTNLRDDIMRLdETVHVVIATPGRILDLIKKGVaKVGQVQMIVLDEADKLLSQDFVQMMEEILSSLSKQRQILLYSAT 280
Cdd:pfam00270 80 LGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157
|
....*...
gi 68444623 281 FPLSVQKF 288
Cdd:pfam00270 158 LPRNLEDL 165
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
310-439 |
2.03e-54 |
|
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: 178.47 E-value: 2.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 310 VTQYYAYVTERQKVHCLN-TLFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRN 388
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 68444623 389 LVCTDLFTRGIDIQAVNVVINFDFPKLGETYLHRIGRSGRFGHLGLAINLI 439
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
99-481 |
2.09e-54 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 191.70 E-value: 2.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI-------DLKKDSIQAVVI 171
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 172 VPTRELALQVSQICIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKK-GVAKVGQVQMIVLDEAD 250
Cdd:PRK04537 91 APTRELAIQIHKDAVKFGADLG-LRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 251 KLLSQDFVQMMEEILSSLSKQ--RQILLYSATFPLSVQKFMNSHLQKPYEINL-MEELTLKGVTQYYAYVTERQKVHCLN 327
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVeTETITAARVRQRIYFPADEEKQTLLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 328 TLFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVV 407
Cdd:PRK04537 250 GLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYV 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68444623 408 INFDFPKLGETYLHRIGRSGRFGHLGLAINLITYDDRFNLKGIEEQLGTEI--KPIPSSIDKSLYVAEYHSESGEE 481
Cdd:PRK04537 330 YNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIpvEPVTAELLTPLPRPPRVPVEGEE 405
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
108-291 |
2.20e-54 |
|
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: 180.54 E-value: 2.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 108 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELALQVSQICIQ 187
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 188 VSKHMGGVKVMATTGGTNLRDDIMRLDETvHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEEILSS 267
Cdd:cd17943 81 IGKKLEGLKCEVFIGGTPVKEDKKKLKGC-HIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180
....*....|....*....|....*...
gi 68444623 268 LSKQRQILLYSATFPLS----VQKFMNS 291
Cdd:cd17943 160 LPKNKQVIAFSATYPKNldnlLARYMRK 187
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
108-299 |
2.70e-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: 180.53 E-value: 2.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 108 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI---DLKKDSIQAVVIVPTRELALQVSQI 184
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 185 CIQVSKHmGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVA-KVGQVQMIVLDEADKLLSQDFVQMMEE 263
Cdd:cd17947 81 LQQLAQF-TDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADELKE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 68444623 264 ILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEI 299
Cdd:cd17947 160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
99-289 |
5.68e-54 |
|
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: 179.95 E-value: 5.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELA 178
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 179 LQVSQICIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFV 258
Cdd:cd18046 81 QQIQKVVMALGDYM-GIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
|
170 180 190
....*....|....*....|....*....|....*
gi 68444623 259 QMMEEILSSLSKQRQILLYSATFPLSV----QKFM 289
Cdd:cd18046 160 DQIYDIFQKLPPDTQVVLLSATMPNDVlevtTKFM 194
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
99-478 |
8.39e-52 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 180.94 E-value: 8.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI-------DLKKDSIQAVVI 171
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshpapeDRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 172 VPTRELALQVSQICIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADK 251
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATG-LKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 252 LLSQDFVQMMEEILSSL--SKQRQILLYSATFPLSVQKFMNSHLQKPYEINLM-EELTLKGVTQYYAYVTERQKVHCLNT 328
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMppANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEpEQKTGHRIKEELFYPSNEEKMRLLQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 329 LFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVI 408
Cdd:PRK04837 249 LIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVF 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 409 NFDFPKLGETYLHRIGRSGRFGHLGLAINLITYDDRFNLKGIEEQLGteiKPIPssidkslyVAEYHSES 478
Cdd:PRK04837 329 NYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIG---HSIP--------VSKYDSDA 387
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
99-299 |
2.49e-51 |
|
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: 172.89 E-value: 2.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELA 178
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 179 LQVSqiciQVSKHMG---GVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIK--KGVaKVGQVQMIVLDEADKLL 253
Cdd:cd17954 82 QQIS----EQFEALGssiGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEntKGF-SLKSLKFLVMDEADRLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 68444623 254 SQDFVQMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEI 299
Cdd:cd17954 157 NMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
99-472 |
3.54e-51 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 181.52 E-value: 3.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLER---IDLKKDSIQ----AVVI 171
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcctIRSGHPSEQrnplAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 172 VPTRELALQVSQICIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADK 251
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 252 LLSQDFVQMMEEILSSLSkQRQILLYSATFPLSVQKFMNSHLQKPYEINLME-ELTLKGVTQYYAYVTERQKVHclnTLF 330
Cdd:PLN00206 282 MLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNpNRPNKAVKQLAIWVETKQKKQ---KLF 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 331 SRLQINQ-----SIIFCNSSQRVELLAKKISQL-GYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAV 404
Cdd:PLN00206 358 DILKSKQhfkppAVVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRV 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68444623 405 NVVINFDFPKLGETYLHRIGRSGRFGHLGLAINLITYDDRFNLKGIEEQLGTEIKPIPSSIDKSLYVA 472
Cdd:PLN00206 438 RQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELANSRYLG 505
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
99-296 |
9.89e-51 |
|
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: 171.33 E-value: 9.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERidLKKDS----IQAVVIVPT 174
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEK--LKAHSptvgARALILSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 175 RELALQVSQICIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLS 254
Cdd:cd17959 81 RELALQTLKVTKELGKFTD-LRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 68444623 255 QDFVQMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKP 296
Cdd:cd17959 160 MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEP 201
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
99-299 |
6.94e-50 |
|
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: 169.19 E-value: 6.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELA 178
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 179 LQVSQICIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFV 258
Cdd:cd18045 81 VQIQKVLLALGDYM-NVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 68444623 259 QMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEI 299
Cdd:cd18045 160 EQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
99-299 |
1.58e-49 |
|
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: 168.29 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELA 178
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 179 LQVSQICIQVSKHMGGVKVMATTGGTNLRDDIMRL-DETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQ-D 256
Cdd:cd17950 84 FQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQlD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 68444623 257 FVQMMEEILSSLSKQRQILLYSATFPLSVQ----KFMnshlQKPYEI 299
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRpvckKFM----QDPLEI 206
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
107-298 |
2.95e-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: 167.76 E-value: 2.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 107 ELLMGIFEMGWEKPSPIQEESIPIALS-GRDILARAKNGTGKSGAYLIPLLERI-----DLKKDSIQAVVIVPTRELALQ 180
Cdd:cd17964 4 SLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTRELALQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 181 VSQICIQVSKHMGGVKVMATTGGTNLRDDIMRL-DETVHVVIATPGRILDLIKK-GVAKV-GQVQMIVLDEADKLLSQDF 257
Cdd:cd17964 84 IAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENpGVAKAfTDLDYLVLDEADRLLDMGF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68444623 258 VQMMEEILSSL----SKQRQILLYSATFPLSVQKFMNSHLQKPYE 298
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 ... |
104-287 |
1.19e-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: 163.52 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 104 LKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI-DLKKDS-----IQAVVIVPTREL 177
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlKAKAESgeeqgTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 178 ALQVSQICIQVSKHMGG-VKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKV-GQVQMIVLDEADKLLSQ 255
Cdd:cd17961 81 AQQVSKVLEQLTAYCRKdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160
|
170 180 190
....*....|....*....|....*....|..
gi 68444623 256 DFVQMMEEILSSLSKQRQILLYSATFPLSVQK 287
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 ... |
99-280 |
1.26e-46 |
|
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: 160.56 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLEridlkkdSIQAVVIVPTRELA 178
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-------IVVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 179 LQVSQICIQVSKHMGGVKV--MATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQD 256
Cdd:cd17938 74 EQTYNCIENFKKYLDNPKLrvALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190
....*....|....*....|....*....|
gi 68444623 257 FVQMMEEILSSLSK-----QR-QILLYSAT 280
Cdd:cd17938 154 NLETINRIYNRIPKitsdgKRlQVIVCSAT 183
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
112-313 |
3.00e-46 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 159.58 E-value: 3.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 112 IFEMGWEKPSPIQEESIPIALSG-RDILARAKNGTGKSGAYLIPLLERIdLKKDSIQAVVIVPTRELALQVSQICIQVSK 190
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 191 HMGGvKVMATTGGTNLRDDIMRL-DETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEEILSSLS 269
Cdd:smart00487 80 SLGL-KVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 68444623 270 KQRQILLYSATFPLSVQKFMNSHLQKPYEINLmEELTLKGVTQY 313
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDV-GFTPLEPIEQF 201
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
108-296 |
3.52e-46 |
|
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: 160.18 E-value: 3.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 108 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERID--------LKKDSIQAVVIVPTRELAL 179
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlppldeeTKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 180 QVSQICIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQ 259
Cdd:cd17945 81 QIEEETQKFAKPL-GIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 68444623 260 MMEEILSSL--------------------SKQRQILLYSATFPLSVQKFMNSHLQKP 296
Cdd:cd17945 160 QVTKILDAMpvsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRRP 216
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
99-299 |
6.28e-45 |
|
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: 156.23 E-value: 6.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERidLKKD--SIQAVVIVPTRE 176
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQR--LSEDpyGIFALVLTPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 177 LALQVSQICIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVG---QVQMIVLDEADKLL 253
Cdd:cd17955 79 LAYQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTKvlsRVKFLVLDEADRLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 68444623 254 SQDFVQMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEI 299
Cdd:cd17955 158 TGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFW 203
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
109-301 |
7.80e-45 |
|
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: 155.53 E-value: 7.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 109 LMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKK----DSIQAVVIVPTRELALQVSQI 184
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERwtpeDGLGALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 185 CIQVSKHmggvKVMAT---TGGTNLRDDIMRLDeTVHVVIATPGRILDLIKKGVA-KVGQVQMIVLDEADKLLSQDFVQM 260
Cdd:cd17941 82 LRKVGKY----HSFSAgliIGGKDVKEEKERIN-RMNILVCTPGRLLQHMDETPGfDTSNLQMLVLDEADRILDMGFKET 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 68444623 261 MEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEINL 301
Cdd:cd17941 157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
108-299 |
1.65e-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: 154.63 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 108 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELALQVSQiciQ 187
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIED---Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 188 VSKHMGGVKVMATT---GGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEEI 264
Cdd:cd17962 78 AKELMKGLPPMKTAllvGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDI 157
|
170 180 190
....*....|....*....|....*....|....*
gi 68444623 265 LSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEI 299
Cdd:cd17962 158 LENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
99-293 |
1.84e-44 |
|
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: 155.34 E-value: 1.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSI----------QA 168
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 169 VVIVPTRELAlqvSQICIQVSK--HMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVL 246
Cdd:cd17967 82 LILAPTRELA---IQIYEEARKfsYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 68444623 247 DEADKLLSQDFVQMMEEILSSLS----KQRQILLYSATFPLSVQK----FMNSHL 293
Cdd:cd17967 159 DEADRMLDMGFEPQIRKIVEHPDmppkGERQTLMFSATFPREIQRlaadFLKNYI 213
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
108-299 |
2.51e-44 |
|
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: 154.50 E-value: 2.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 108 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI----DLKK-DSIQAVVIVPTRELALQVS 182
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImdqrELEKgEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 183 QICIQVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMME 262
Cdd:cd17952 81 LEAKKFGKAYN-LRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 68444623 263 EILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEI 299
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
104-299 |
3.82e-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: 153.89 E-value: 3.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 104 LKRELLMGIFEMGWEKPSPIQEESIPIALSG--RDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRELALQV 181
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 182 SQICIQVSKHMgGVKVMATtggtnLRDDIMRLDETV--HVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQdfvQ 259
Cdd:cd17963 81 GEVVEKMGKFT-GVKVALA-----VPGNDVPRGKKItaQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDT---Q 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 68444623 260 MMEE----ILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEI 299
Cdd:cd17963 152 GHGDqsirIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
108-300 |
5.12e-44 |
|
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: 153.50 E-value: 5.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 108 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI-----DLKKDSIQAVVIVPTRELALQVS 182
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 183 QICIQVSKHMGG-VKVMATTGGTN-LRDDIMRLDETVHVVIATPGRILDLI--KKGVAKVGQVQMIVLDEADKLLSQDFV 258
Cdd:cd17960 81 EVLQSFLEHHLPkLKCQLLIGGTNvEEDVKKFKRNGPNILVGTPGRLEELLsrKADKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 68444623 259 QMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEIN 300
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
108-296 |
2.07e-43 |
|
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: 151.97 E-value: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 108 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI--DLKKDSIQAVVIVPTRELAlqvSQIC 185
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELA---SQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 186 IQVSKHMGG----VKVMATTGGTNLRDDImRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMM 261
Cdd:cd17957 78 RELLKLSKGtglrIVLLSKSLEAKAKDGP-KSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 68444623 262 EEILSSL-SKQRQILLYSATFPLSVQKFMNSHLQKP 296
Cdd:cd17957 157 DEILAACtNPNLQRSLFSATIPSEVEELARSVMKDP 192
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
112-300 |
1.26e-42 |
|
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: 149.83 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 112 IFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKK-----DSIQAVVIVPTRELALQVSQICI 186
Cdd:cd17966 5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPplergDGPIVLVLAPTRELAQQIQQEAN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 187 QVSkHMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEEILS 266
Cdd:cd17966 85 KFG-GSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVD 163
|
170 180 190
....*....|....*....|....*....|....
gi 68444623 267 SLSKQRQILLYSATFPLSVQKFMNSHLQKPYEIN 300
Cdd:cd17966 164 QIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
97-297 |
3.19e-41 |
|
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: 148.19 E-value: 3.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 97 NEFEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERidLKKDSI---------- 166
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTG--MMKEGLtassfsevqe 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 167 -QAVVIVPTRELALQVSQICIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIV 245
Cdd:cd18052 121 pQALIVAPTRELANQIFLEARKFSYGT-CIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 68444623 246 LDEADKLLSQDFVQMMEEILSSLS----KQRQILLYSATFPLSVQKFMNSHLQKPY 297
Cdd:cd18052 200 LDEADRMLDMGFGPEIRKLVSEPGmpskEDRQTLMFSATFPEEIQRLAAEFLKEDY 255
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
104-299 |
6.62e-41 |
|
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: 145.98 E-value: 6.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 104 LKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIdLKKDSIQ------AVVIVPTREL 177
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHI-KDQRPVKpgegpiGLIMAPTREL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 178 ALQVSQICIQVSKHMgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVG---QVQMIVLDEADKLLS 254
Cdd:cd17953 98 ALQIYVECKKFSKAL-GLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTnlrRVTYVVLDEADRMFD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68444623 255 QDFVQMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEI 299
Cdd:cd17953 177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
108-296 |
6.84e-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: 139.91 E-value: 6.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 108 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDL------KKDSIQAVVIVPTRELALQV 181
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLqpipreQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 182 SQICIQVSKHmgGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMM 261
Cdd:cd17958 81 EAECSKYSYK--GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*
gi 68444623 262 EEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKP 296
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDP 193
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
108-300 |
1.22e-38 |
|
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: 139.40 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 108 LLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLL-----ERIDL---KKDSIQAVVIVPTRELAL 179
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleQEKKLpfiKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 180 QVSQICIQVSKH-----MGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLS 254
Cdd:cd17951 81 QTHEVIEYYCKAlqeggYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 68444623 255 QDFVQMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEIN 300
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
115-296 |
2.09e-38 |
|
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: 139.26 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 115 MGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQ------AVVIVPTRELALQVSQICIQV 188
Cdd:cd17949 9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 189 SKHMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVA-KVGQVQMIVLDEADKLLSQDFVQMMEEILS- 266
Cdd:cd17949 89 LKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADRLLDMGFEKDITKILEl 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 68444623 267 ------------SLSKQRQILLYSATFPLSVQKFMNSHLQKP 296
Cdd:cd17949 169 lddkrskaggekSKPSRRQTVLVSATLTDGVKRLAGLSLKDP 210
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
109-280 |
2.70e-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: 135.57 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 109 LMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERID----LKKDSIQAVVIVPTRELALQVSQI 184
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYklkfKPRNGTGVIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 185 CIQVSKHmGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILD-LIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEE 263
Cdd:cd17942 82 AKELLKY-HSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
|
170
....*....|....*..
gi 68444623 264 ILSSLSKQRQILLYSAT 280
Cdd:cd17942 161 IIKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
99-306 |
2.40e-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: 131.30 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSG--RDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRE 176
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 177 LALQVSQICIQVSKHMGGVKVMATTGGTNLRDDImrlDETVHVVIATPGRILD-LIKKGVAKVGQVQMIVLDEADKLLS- 254
Cdd:cd18048 100 LALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGT---DIEAQIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEADVMINv 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 68444623 255 QDFVQMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEINL-MEELT 306
Cdd:cd18048 177 QGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLkKEELT 229
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
108-281 |
5.20e-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: 130.44 E-value: 5.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 108 LLMGIFEMGWEKPSPIQEESIPIALS-GRDILARAKNGTGKSGAYLIPLLERI-DLKKDSI--------QAVVIVPTREL 177
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlSQKSSNGvggkqkplRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 178 ALQVSQICIQVSKHmGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKG---VAKVGQVQMIVLDEADKLLS 254
Cdd:cd17946 81 AVQVKDHLKAIAKY-TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLE 159
|
170 180 190
....*....|....*....|....*....|....
gi 68444623 255 QDFVQMMEEILSSL-------SKQRQILLYSATF 281
Cdd:cd17946 160 KGHFAELEKILELLnkdragkKRKRQTFVFSATL 193
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
97-286 |
5.75e-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: 128.23 E-value: 5.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 97 NEFEDYCLKrELLMGIFEMG-WEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI---------------- 159
Cdd:cd18051 21 ETFSDLDLG-EIIRNNIELArYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgeslpsesgyy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 160 DLKKDSIQAVVIVPTRELAlqvSQICIQVSK--HMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGvaK 237
Cdd:cd18051 100 GRRKQYPLALVLAPTRELA---SQIYDEARKfaYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERG--K 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 68444623 238 VG--QVQMIVLDEADKLLSQDFVQMMEEILSSL----SKQRQILLYSATFPLSVQ 286
Cdd:cd18051 175 IGldYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQ 229
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
114-290 |
8.50e-33 |
|
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: 124.40 E-value: 8.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 114 EMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKK-------DSIQAVVIVPTRELALQVSQICI 186
Cdd:cd17948 7 RQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKllaegpfNAPRGLVITPSRELAEQIGSVAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 187 QVSKHMGgVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEEILS 266
Cdd:cd17948 87 SLTEGLG-LKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLR 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 68444623 267 -------------SLSKQRQILLYSATFPLSVQKFMN 290
Cdd:cd17948 166 rfplasrrsentdGLDPGTQLVLVSATMPSGVGEVLS 202
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
112-301 |
1.35e-32 |
|
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: 125.12 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 112 IFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDL-----KKDSIQAVVIVPTRELALQVSQICI 186
Cdd:cd18050 77 LLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHqpyleRGDGPICLVLAPTRELAQQVQQVAD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 187 QVSKHmGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEEILS 266
Cdd:cd18050 157 DYGKS-SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD 235
|
170 180 190
....*....|....*....|....*....|....*
gi 68444623 267 SLSKQRQILLYSATFPLSVQKFMNSHLQKPYEINL 301
Cdd:cd18050 236 QIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
98-301 |
1.83e-32 |
|
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: 123.58 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 98 EFEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKK-----DSIQAVVIV 172
Cdd:cd18049 25 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflergDGPICLVLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 173 PTRELALQVSQICIQVSKhMGGVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKL 252
Cdd:cd18049 105 PTRELAQQVQQVAAEYGR-ACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 68444623 253 LSQDFVQMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEINL 301
Cdd:cd18049 184 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
321-430 |
5.38e-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: 115.39 E-value: 5.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 321 QKVHCLNTLFSRLQINQSIIFCNSSQRVE--LLAKKIsqlGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRG 398
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEaeLLLEKE---GIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 68444623 399 IDIQAVNVVINFDFPKLGETYLHRIGRSGRFG 430
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
122-298 |
3.56e-28 |
|
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: 111.09 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 122 PIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERI-----DLKKD-SIQAVVIVPTRELALQVSQICIQVSKHMggv 195
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLqedqqPRKRGrAPKVLVLAPTRELANQVTKDFKDITRKL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 196 KVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEEILSSLSKQR--- 272
Cdd:cd17944 92 SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSYKKDsed 171
|
170 180
....*....|....*....|....*...
gi 68444623 273 --QILLYSATFPLSVQKFMNSHLQKPYE 298
Cdd:cd17944 172 npQTLLFSATCPDWVYNVAKKYMKSQYE 199
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
99-296 |
1.33e-27 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 109.42 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 99 FEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSG--RDILARAKNGTGKSGAYLIPLLERIDLKKDSIQAVVIVPTRE 176
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 177 LALQVSQICIQVSKHMGGVKVMATTGGTNLRDDIMRLDEtvhVVIATPGRILD-LIKKGVAKVGQVQMIVLDEADKLL-S 254
Cdd:cd18047 83 LALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 68444623 255 QDFVQMMEEILSSLSKQRQILLYSATFPLSVQKFMNSHLQKP 296
Cdd:cd18047 160 QGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
114-295 |
2.49e-26 |
|
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: 106.56 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 114 EMGWEKPSPIQEESIPIALSG---------RDILARAKNGTGKSGAYLIPLLERI-DLKKDSIQAVVIVPTRELALQVSQ 183
Cdd:cd17956 7 NNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKELVQQVYK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 184 ICIQVSKHMgGVKVMATTGGTNLRDDIM--------RLDETVHVVIATPGRILDLIKKGVA-KVGQVQMIVLDEADKLLS 254
Cdd:cd17956 87 VFESLCKGT-GLKVVSLSGQKSFKKEQKlllvdtsgRYLSRVDILVATPGRLVDHLNSTPGfTLKHLRFLVIDEADRLLN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 68444623 255 QDFVQMMEEILSSLsKQRQILLYSATFPLSVQKFMNSHLQK 295
Cdd:cd17956 166 QSFQDWLETVMKAL-GRPTAPDLGSFGDANLLERSVRPLQK 205
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
349-430 |
1.09e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 99.98 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 349 ELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLGETYLHRIGRSGR 428
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 68444623 429 FG 430
Cdd:smart00490 81 AG 82
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
119-302 |
3.39e-22 |
|
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: 95.52 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 119 KPSPIQEESIPIALSGRDILAR----------------AKNGTGKSGAYLIPLLEriDLKKDS----------------- 165
Cdd:cd17965 30 KPSPIQTLAIKKLLKTLMRKVTkqtsneepklevfllaAETGSGKTLAYLAPLLD--YLKRQEqepfeeaeeeyesakdt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 166 --IQAVVIVPTRELALQVSQICIQVSKHMG-GVKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQ 242
Cdd:cd17965 108 grPRSVILVPTHELVEQVYSVLKKLSHTVKlGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVT 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 243 MIVLDEADKLLSQDFVQMMEEILSSLSKQRQILLYSATFPLSVQKFMNShlQKPYEINLM 302
Cdd:cd17965 188 HLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRK--LFPDVVRIA 245
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
86-466 |
3.64e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 71.46 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 86 MKTSDVtatKGNEFEDYCLKRellmGIFEMgwekpSPIQEESIP-IALSGRDILARAKNGTGKSgayLI---PLLERIDL 161
Cdd:COG1204 1 MKVAEL---PLEKVIEFLKER----GIEEL-----YPPQAEALEaGLLEGKNLVVSAPTASGKT---LIaelAILKALLN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 162 KKDsiqAVVIVPTRELAlqvSQICIQVSKHMG--GVKVMATTGGTNLRDdimRLDETVHVVIATPGRILDLIKKGVAKVG 239
Cdd:COG1204 66 GGK---ALYIVPLRALA---SEKYREFKRDFEelGIKVGVSTGDYDSDD---EWLGRYDILVATPEKLDSLLRNGPSWLR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 240 QVQMIVLDEADKLLSQDFVQMMEEILSSLSKQR---QILLYSATFPlSVQKF---MNSHL----QKPyeINLMEELTLKG 309
Cdd:COG1204 137 DVDLVVVDEAHLIDDESRGPTLEVLLARLRRLNpeaQIVALSATIG-NAEEIaewLDAELvksdWRP--VPLNEGVLYDG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 310 VTqYYAYVTERQKVHCLNTLFSRLQIN-QSIIFCNSSQRVELLAKKISQ-LGYSCFYI---------------------- 365
Cdd:COG1204 214 VL-RFDDGSRRSKDPTLALALDLLEEGgQVLVFVSSRRDAESLAKKLADeLKRRLTPEereeleelaeellevseethtn 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 366 --------------HAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINfDFPKLGET------YLHRIGR 425
Cdd:COG1204 293 ekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-DTKRGGMVpipvleFKQMAGR 371
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 68444623 426 SGRFGH--LGLAInLITYDDRFNLKGIEEQLGTEIKPIPSSID 466
Cdd:COG1204 372 AGRPGYdpYGEAI-LVAKSSDEADELFERYILGEPEPIRSKLA 413
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
134-280 |
4.29e-13 |
|
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: 66.66 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 134 GRDILARAKNGTGKSGAYLIPLLERIDLKKDsiQAVVIVPTRELALQVSQICIQVSKHmgGVKVMATTGGTNLRDDIMRL 213
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGK--KVLVLVPTKALALQTAERLRELFGP--GIRVAVLVGGSSAEEREKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 214 DETVHVVIATPGRILDLIKKGVAKVG-QVQMIVLDEADKLL--SQDFVQMMEEILSSLSKQRQILLYSAT 280
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLREDRLFLkDLKLIIVDEAHALLidSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
339-430 |
6.30e-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: 65.69 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 339 IIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLGET 418
Cdd:cd18794 34 IIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMES 113
|
90
....*....|..
gi 68444623 419 YLHRIGRSGRFG 430
Cdd:cd18794 114 YYQESGRAGRDG 125
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
144-408 |
7.84e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 70.44 E-value: 7.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 144 GTGKS--GAYLIpllERIDLKKdsiQAVVIVPTRELALQVSQiciQVSKHMGGVKVmatTGGtnlrddimRLDETVHVVI 221
Cdd:COG1061 110 GTGKTvlALALA---AELLRGK---RVLVLVPRRELLEQWAE---ELRRFLGDPLA---GGG--------KKDSDAPITV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 222 ATPG--RILDLIKKGVAKVGqvqMIVLDEADKLLSQDFvqmmEEILSSLSKQRQILLySAT------------------F 281
Cdd:COG1061 170 ATYQslARRAHLDELGDRFG---LVIIDEAHHAGAPSY----RRILEAFPAAYRLGL-TATpfrsdgreillflfdgivY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 282 PLSVQKFMNSHLQKPYEI-----------NLMEELTlKGVTQYYAYVTERqKVHCLNTLFSRL-QINQSIIFCNSSQRVE 349
Cdd:COG1061 242 EYSLKEAIEDGYLAPPEYygirvdltderAEYDALS-ERLREALAADAER-KDKILRELLREHpDDRKTLVFCSSVDHAE 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 68444623 350 LLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVI 408
Cdd:COG1061 320 ALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
116-430 |
8.24e-12 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 67.43 E-value: 8.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 116 GWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLkkdsiqAVVIVPTRELAL-QVSQICIQvskhmgG 194
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGL------TLVVSPLISLMKdQVDQLLAN------G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 195 VKVmATTGGTNLRDDI------MRLDETVHVVIAtPGRIL--DLIKKGVAKvgQVQMIVLDEAdKLLSQ---DFvqmmEE 263
Cdd:PRK11057 90 VAA-ACLNSTQTREQQlevmagCRTGQIKLLYIA-PERLMmdNFLEHLAHW--NPALLAVDEA-HCISQwghDF----RP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 264 ILSSLSKQRQ------ILLYSATFPLSVQKFMNS--HLQKPYE-----------INLMEELtlKGVTQYYAYVTErQKVH 324
Cdd:PRK11057 161 EYAALGQLRQrfptlpFMALTATADDTTRQDIVRllGLNDPLIqissfdrpnirYTLVEKF--KPLDQLMRYVQE-QRGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 325 ClntlfsrlqinqSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAV 404
Cdd:PRK11057 238 S------------GIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNV 305
|
330 340
....*....|....*....|....*.
gi 68444623 405 NVVINFDFPKLGETYLHRIGRSGRFG 430
Cdd:PRK11057 306 RFVVHFDIPRNIESYYQETGRAGRDG 331
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
114-443 |
1.78e-10 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 63.30 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 114 EMGWEKPSPIQEESIPI-ALSGRDILARAKNGTGKSGAYLIPLLERidLKKDSIQAVVIVPTRELALQVSQICIQVSKHm 192
Cdd:PRK00254 18 ERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNK--LLREGGKAVYLVPLKALAEEKYREFKDWEKL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 193 gGVKVMATTGGTNLRDDIM-RLDetvhVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEEILSSLSKQ 271
Cdd:PRK00254 95 -GLRVAMTTGDYDSTDEWLgKYD----IIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 272 RQILLYSATF--PLSVQKFMNSHL----QKPYEINlmeeltlKGVTqYYAYVT-ERQKVHCLNTLFSRLQIN------QS 338
Cdd:PRK00254 170 AQILGLSATVgnAEELAEWLNAELvvsdWRPVKLR-------KGVF-YQGFLFwEDGKIERFPNSWESLVYDavkkgkGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 339 IIFCNSSQRVE----LLAKKISQL------------------------------GYSCFYiHAKMRQEHRNRVFHDFRNG 384
Cdd:PRK00254 242 LVFVNTRRSAEkealELAKKIKRFltkpelralkeladsleenptneklkkalrGGVAFH-HAGLGRTERVLIEDAFREG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68444623 385 LCRNLVCTDLFTRGIDIQAVNVVI-------NFDFPKLGETYLHR-IGRSGR--FGHLGLAINLITYDD 443
Cdd:PRK00254 321 LIKVITATPTLSAGINLPAFRVIIrdtkrysNFGWEDIPVLEIQQmMGRAGRpkYDEVGEAIIVATTEE 389
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
124-444 |
3.95e-10 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 61.70 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 124 QEESIPIALSGRDILARAKNGTGKSGAYLIP--LLERIdlkkdsiqAVVIVPTreLAL---QVSQICIQvskhmgGVKVM 198
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLLPGL--------TLVVSPL--IALmkdQVDALRAA------GIRAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 199 ATTGGTNL--RDDIMR--LDETVHVVIATP-----GRILDLIKKGvakvgQVQMIVLDEAdKLLSQ---DF---VQMMEE 263
Cdd:COG0514 86 FLNSSLSAeeRREVLRalRAGELKLLYVAPerllnPRFLELLRRL-----KISLFAIDEA-HCISQwghDFrpdYRRLGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 264 ILSSLSkQRQILLYSATFPLSVQKFMNSHL--QKPYEI-------NLmeeltlkgvtqYYAyVTERQKVHCLNTLFSRL- 333
Cdd:COG0514 160 LRERLP-NVPVLALTATATPRVRADIAEQLglEDPRVFvgsfdrpNL-----------RLE-VVPKPPDDKLAQLLDFLk 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 334 -QINQS-IIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFD 411
Cdd:COG0514 227 eHPGGSgIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYD 306
|
330 340 350
....*....|....*....|....*....|...
gi 68444623 412 FPKLGETYLHRIGRSGRFGHLGLAINLITYDDR 444
Cdd:COG0514 307 LPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDV 339
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
348-431 |
1.01e-07 |
|
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: 51.19 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 348 VELLAKKISQL--GYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLGETYLH---- 421
Cdd:cd18810 38 IEKLATQLRQLvpEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYqlrg 117
|
90
....*....|
gi 68444623 422 RIGRSGRFGH 431
Cdd:cd18810 118 RVGRSKERAY 127
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
322-425 |
1.28e-07 |
|
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: 50.67 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 322 KVHCL-NTL---FSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAK-------------MRQEHRN--RVFHDFR 382
Cdd:cd18802 8 KLQKLiEILreyFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrSLMTQRKqkETLDKFR 87
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 68444623 383 NGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLGETYLHRIGR 425
Cdd:cd18802 88 DGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
124-443 |
4.03e-07 |
|
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: 52.53 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 124 QEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIdLKKDSIQAVVIVPTRELAL-QVSQIcIQVSKHMG-GVKVMATT 201
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPTKALARdQLRRL-RELAEALGlGVRVATYD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 202 GGT--NLRDDIMrldETVHVVIATPgrilDLIKKGVAK--------VGQVQMIVLDE----------------------- 248
Cdd:COG1205 139 GDTppEERRWIR---EHPDIVLTNP----DMLHYGLLPhhtrwarfFRNLRYVVIDEahtyrgvfgshvanvlrrlrric 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 249 ----------------------ADKLLSQDFvqmmEEILSSLSKQ--RQILLYSAtfPLSVQKFMNSHLQkpyE-INLME 303
Cdd:COG1205 212 rhygsdpqfilasatignpaehAERLTGRPV----TVVDEDGSPRgeRTFVLWNP--PLVDDGIRRSALA---EaARLLA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 304 ELTLKGVtqyyayvterqkvhclntlfsrlqinQSIIFCNSSQRVELLAKKISQL-----------GYscfyiHAKMRQE 372
Cdd:COG1205 283 DLVREGL--------------------------RTLVFTRSRRGAELLARYARRAlrepdladrvaAY-----RAGYLPE 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68444623 373 HRNRVFHDFRNGLCRNLVCT---DLftrGIDIQAVNVVINFDFPKLGETYLHRIGRSGRFGHLGLAInLITYDD 443
Cdd:COG1205 332 ERREIERGLRSGELLGVVSTnalEL---GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGDD 401
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
337-436 |
4.51e-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: 49.18 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 337 QSIIFCNSSQRVEL--------------LAKKIS--QLGYscfyihakmRQEHRNRVFHDFRNGLCRNLVCTDLFTRGID 400
Cdd:cd18797 37 KTIVFCRSRKLAELllrylkarlveegpLASKVAsyRAGY---------LAEDRREIEAELFNGELLGVVATNALELGID 107
|
90 100 110
....*....|....*....|....*....|....*.
gi 68444623 401 IQAVNVVINFDFPKLGETYLHRIGRSGRFGHLGLAI 436
Cdd:cd18797 108 IGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
389-430 |
5.03e-07 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 47.31 E-value: 5.03e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 68444623 389 LVCTDLFTRGIDIQAVNVVINFDFPKLGETYLHRIGRSGRFG 430
Cdd:cd18785 26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
346-431 |
5.98e-07 |
|
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: 49.19 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 346 QRVELLAKKISQL--GYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLGETYLH-- 421
Cdd:cd18792 45 KSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHql 124
|
90
....*....|..
gi 68444623 422 --RIGRSGRFGH 431
Cdd:cd18792 125 rgRVGRGKHQSY 136
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
329-428 |
8.34e-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: 48.41 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 329 LFSRLQINQSIIFCNSSQRVELLAKKISQLGYSC-----FYIH-AKMRQEHRNRVFHDFRNGLCRNLVCT---DLftrGI 399
Cdd:cd18796 32 IFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRvppdfIALHhGSLSRELREEVEAALKRGDLKVVVATsslEL---GI 108
|
90 100
....*....|....*....|....*....
gi 68444623 400 DIQAVNVVINFDFPKLGETYLHRIGRSGR 428
Cdd:cd18796 109 DIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
339-430 |
1.15e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 51.27 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 339 IIFCNSSQRVELLAKKISQLGYSC--FYIHAK------MRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINF 410
Cdd:COG1111 357 IVFTQYRDTAEMIVEFLSEPGIKAgrFVGQASkegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFY 436
|
90 100
....*....|....*....|...
gi 68444623 411 DfpkLGET---YLHRIGRSGRFG 430
Cdd:COG1111 437 E---PVPSeirSIQRKGRTGRKR 456
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
124-249 |
1.20e-06 |
|
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: 48.74 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 124 QEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIdLKKDSIQAVVIVPTRELAL-QVSQICIQVSKHMGGVKVMATTG 202
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAQdQLRSLRELLEQLGLGIRVATYDG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 68444623 203 GTNLRDDIMRLDETVHVVIATPgRILD--LIKKGVAKVGQVQM---IVLDEA 249
Cdd:cd17923 84 DTPREERRAIIRNPPRILLTNP-DMLHyaLLPHHDRWARFLRNlryVVLDEA 134
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
348-431 |
1.79e-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: 50.82 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 348 VELLAKKISQL--GYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLGETYLH---- 421
Cdd:TIGR00580 673 IEKLATQLRELvpEARIAIAHGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIERADKFGLAQLYqlrg 752
|
90
....*....|
gi 68444623 422 RIGRSGRFGH 431
Cdd:TIGR00580 753 RVGRSKKKAY 762
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
338-413 |
1.96e-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: 1.96e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68444623 338 SIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGL--CRNLVCTDLFTRGIDIQAVNVVINFDFP 413
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPW 107
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
336-428 |
2.99e-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: 47.16 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 336 NQSIIFCNSSQRVELLAKKISQLGyscfYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVI------- 408
Cdd:cd18795 44 KPVLVFCSSRKECEKTAKDLAGIA----FHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIkgtqryd 119
|
90 100
....*....|....*....|.
gi 68444623 409 NFDFPKLGET-YLHRIGRSGR 428
Cdd:cd18795 120 GKGYRELSPLeYLQMIGRAGR 140
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
124-467 |
6.34e-06 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 48.73 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 124 QEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIqavVIVPTRELALQVSQICIQVSKHmgGVKVMATTGG 203
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSI---YIVPLRSLAMEKYEELSRLRSL--GMRVKISIGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 204 TNLRDD-IMRLDetvhVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEEILSS---LSKQRQILLYSA 279
Cdd:PRK01172 102 YDDPPDfIKRYD----VVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSaryVNPDARILALSA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 280 TFP--LSVQKFMNSHLQK------PYEINLM--EELTLKGvtqyyayvTERQKVHCLNTLFSRLQIN-QSIIFCNSSQRV 348
Cdd:PRK01172 178 TVSnaNELAQWLNASLIKsnfrpvPLKLGILyrKRLILDG--------YERSQVDINSLIKETVNDGgQVLVFVSSRKNA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 349 ELLAKKISQ-------------------------LGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQA 403
Cdd:PRK01172 250 EDYAEMLIQhfpefndfkvssennnvyddslnemLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPA 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68444623 404 VNVVIN--FDFPKLGETYL------HRIGRSGRFGHLGLAINLITYDDRFNLKGIEEQLGTEIKPIPSSIDK 467
Cdd:PRK01172 330 RLVIVRdiTRYGNGGIRYLsnmeikQMIGRAGRPGYDQYGIGYIYAASPASYDAAKKYLSGEPEPVISYMGS 401
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
115-249 |
6.51e-06 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 46.76 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 115 MGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIP--LLERIdlkkdsiqAVVIVPTreLAL---QVSQiCIQVs 189
Cdd:cd17920 8 FGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV--------TLVVSPL--ISLmqdQVDR-LQQL- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68444623 190 khmgGVKVMATTGGT----NLRDDIMRLDETVHVVIATP-----GRILDLIKKgVAKVGQVQMIVLDEA 249
Cdd:cd17920 76 ----GIRAAALNSTLspeeKREVLLRIKNGQYKLLYVTPerllsPDFLELLQR-LPERKRLALIVVDEA 139
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
365-431 |
2.33e-05 |
|
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: 44.64 E-value: 2.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68444623 365 IHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLGETYLHRI-GRSGRFGH 431
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGRGDH 134
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
339-408 |
4.33e-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: 42.93 E-value: 4.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68444623 339 IIFCNSSQRVELLAKKISQLGYSCFYIHAK--MRQEHRNRVFHDFRNGLCRN-LVCTDLFTRGIDIQAVNVVI 408
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFFGELKPPiLVTVDLLTTGVDIPEVDNVV 82
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
119-273 |
6.45e-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: 43.79 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 119 KPSPIQEESIPIALSgRDILARAKNGTGKSgayLIPLL------ERIDLKKDSI-QAVVIVPTRELALQ-----VSQICI 186
Cdd:cd18034 2 TPRSYQLELFEAALK-RNTIVVLPTGSGKT---LIAVMlikemgELNRKEKNPKkRAVFLVPTVPLVAQqaeaiRSHTDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 187 QVSKHMGGVKVMATTGGTNLRDDimrldETVHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQD-FVQMMEEIL 265
Cdd:cd18034 78 KVGEYSGEMGVDKWTKERWKEEL-----EKYDVLVMTAQILLDALRHGFLSLSDINLLIFDECHHATGDHpYARIMKEFY 152
|
....*...
gi 68444623 266 SSLSKQRQ 273
Cdd:cd18034 153 HLEGRTSR 160
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
339-428 |
1.17e-04 |
|
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: 42.34 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 339 IIFCNSSQRVELLAKKISQLGY----SCFYIHAK------MRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVI 408
Cdd:cd18801 34 IIFSEFRDSAEEIVNFLSKIRPgiraTRFIGQASgksskgMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLII 113
|
90 100
....*....|....*....|
gi 68444623 409 NFDFPKLGETYLHRIGRSGR 428
Cdd:cd18801 114 CYDASPSPIRMIQRMGRTGR 133
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
121-296 |
1.22e-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: 43.01 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 121 SPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDlKKDSIqAVVIVPTreLAL---QVSqiciQVSKHMGGVKV 197
Cdd:cd18018 14 RPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRR-RGPGL-TLVVSPL--IALmkdQVD----ALPRAIKAAAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 198 MATTGGTNLRDDIMRLDE-TVHVVIATPGRILDL-IKKGVAKVGQVQMIVLDEADKL--LSQDF---VQMMEEILSSLSK 270
Cdd:cd18018 86 NSSLTREERRRILEKLRAgEVKILYVSPERLVNEsFRELLRQTPPISLLVVDEAHCIseWSHNFrpdYLRLCRVLRELLG 165
|
170 180
....*....|....*....|....*.
gi 68444623 271 QRQILLYSATFPLSVQKFMNSHLQKP 296
Cdd:cd18018 166 APPVLALTATATKRVVEDIASHLGIP 191
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
119-299 |
1.30e-04 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain] Cd Length: 204 Bit Score: 43.23 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 119 KPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQ---AVVIVPTRELalqVSQICIQVSKHM-GG 194
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEkgrVVVLVNKVPL---VEQQLEKFFKYFrKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 195 VKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKGVAK----VGQVQMIVLDEADKLLSQD-FVQMM----EEIL 265
Cdd:cd18036 79 YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEervyLSDFSLLIFDECHHTQKEHpYNKIMrmylDKKL 158
|
170 180 190
....*....|....*....|....*....|....
gi 68444623 266 SSLSKQRQILLYSATFPLSVQKFMNSHLQKPYEI 299
Cdd:cd18036 159 SSQGPLPQILGLTASPGVGGARSFEEALEHILKL 192
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
339-413 |
1.43e-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: 1.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68444623 339 IIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRN--LVCTDLFTRGIDIQAVNVVINFDFP 413
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPvfLISLKAGGEGLNLTAADHVIHYDLW 629
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
366-431 |
2.50e-04 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 43.97 E-value: 2.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68444623 366 HAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLGETYLHRI-GRSGRFGH 431
Cdd:PRK10689 842 HGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLrGRVGRSHH 908
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
339-460 |
3.72e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 43.35 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 339 IIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCrNLVC-TDLFTRGIDIQAVNVVINFDFPKLGE 417
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEI-NIICaTVAFGMGINKPDVRFVIHHSLPKSIE 762
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 68444623 418 TYLHRIGRSGRFGHLGLAINLITYDDRFNLKGIEEQLGTEIKP 460
Cdd:PLN03137 763 GYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSP 805
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
338-427 |
6.41e-04 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 42.40 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 338 SIIFCNS-SQrVELLAKKISQLGYSCFYI----HAKMRQEHRNRVFHDFRNGLCRNLVCT---DLftrGIDIQAVNVVIN 409
Cdd:COG1201 275 TLVFTNTrSQ-AERLFQRLNELNPEDALPiaahHGSLSREQRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQ 350
|
90 100
....*....|....*....|..
gi 68444623 410 FDFPK----LgetyLHRIGRSG 427
Cdd:COG1201 351 VGSPKsvarL----LQRIGRAG 368
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
169-280 |
2.28e-03 |
|
DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 39.23 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 169 VVIVPTRELALQvsQIciQVSKHMGGVKVMAT---TGGTNlRDDIMRLDETVHVVIATPGRILDLIKKGVAKVGQVQMIV 245
Cdd:cd18033 50 VFMAPTKPLVSQ--QI--EACYKITGIPSSQTaelTGSVP-PTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLV 124
|
90 100 110
....*....|....*....|....*....|....*.
gi 68444623 246 LDEADKLLSQ-DFVQMMEEILSSlSKQRQILLYSAT 280
Cdd:cd18033 125 IDEAHRATGNyAYCQVVRELMRY-NSHFRILALTAT 159
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
122-282 |
2.73e-03 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 38.85 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 122 PIQEESIPIAL-SGRDILARAKNGTGKSGAYLIPLLERIDLKKdsiQAVVIVPTRELAlqvSQICIQVSKHMG-GVKVMA 199
Cdd:cd18028 4 PPQAEAVRAGLlKGENLLISIPTASGKTLIAEMAMVNTLLEGG---KALYLVPLRALA---SEKYEEFKKLEEiGLKVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 200 TTGGTNLRDDimRLDETvHVVIATPGRILDLIKKGVAKVGQVQMIVLDEADKLLSQDFVQMMEEILS---SLSKQRQILL 276
Cdd:cd18028 78 STGDYDEDDE--WLGDY-DIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVArlrRLNPNTQIIG 154
|
....*.
gi 68444623 277 YSATFP 282
Cdd:cd18028 155 LSATIG 160
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
123-295 |
4.39e-03 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350778 [Multi-domain] Cd Length: 199 Bit Score: 38.57 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 123 IQEESIPIA-LSGRDILARAKNGTGKSGAYLIPLLERI--------DLKKDSIQAVVIVPTRELAlqvSQICIQVSKHMG 193
Cdd:cd18020 5 IQSLVFPVAyKTNENMLICAPTGAGKTNIAMLTILHEIrqhvnqggVIKKDDFKIVYIAPMKALA---AEMVEKFSKRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 194 --GVKVMATTGGTNLRDDimRLDETvHVVIATPGRILDLIKKG---VAKVGQVQMIVLDEAdKLLSQDFVQMMEEILSSL 268
Cdd:cd18020 82 plGIKVKELTGDMQLTKK--EIAET-QIIVTTPEKWDVVTRKSsgdVALSQLVRLLIIDEV-HLLHDDRGPVIESLVART 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 68444623 269 SKQRQ-------ILLYSATFP--LSVQKFMNSHLQK 295
Cdd:cd18020 158 LRQVEstqsmirIVGLSATLPnyLDVADFLRVNPYK 193
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
119-280 |
5.07e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 38.18 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 119 KPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERIDLKKDSIQA--VVIVPTRELALQVSQICiqvSKHMG--G 194
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGkvVFLANKVPLVEQQKEVF---RKHFErpG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68444623 195 VKVMATTGGTNLRDDIMRLDETVHVVIATPGRILDLIKKG-VAKVGQVQMIVLDEAdKLLSQD--FVQMM----EEILSS 267
Cdd:cd17927 79 YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGtIVSLSDFSLLVFDEC-HNTTKNhpYNEIMfrylDQKLGS 157
|
170
....*....|...
gi 68444623 268 LSKQRQILLYSAT 280
Cdd:cd17927 158 SGPLPQILGLTAS 170
|
|
| |
