|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
32-391 |
4.24e-143 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 417.63 E-value: 4.24e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 32 SFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNK-IQALIMVPTRE 110
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 111 LALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDF 190
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 191 KTIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEINLM-EELTLKGITQYYAFVEERQKLHCLNTLFSKLQIN 269
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVApENATAETIEQRYYLVDKRDKLELLRRLLRDEDPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 270 QAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTA 349
Cdd:COG0513 243 RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDP 322
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 50289935 350 ETYLHRIGRSGRFGHLGLAINLINWNDRFNLYKIEQELGTEI 391
Cdd:COG0513 323 EDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKI 364
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
33-233 |
1.29e-137 |
|
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: 395.13 E-value: 1.29e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 33 FEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTRELA 112
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 113 LQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKT 192
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 50289935 193 IIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEIN 233
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
31-398 |
2.23e-118 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 353.75 E-value: 2.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 31 NSFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTRE 110
Cdd:PTZ00424 28 DSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 111 LALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDF 190
Cdd:PTZ00424 108 LAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 191 KTIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEINL-MEELTLKGITQYYAFVE-ERQKLHCLNTLFSKLQI 268
Cdd:PTZ00424 188 KGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVkKDELTLEGIRQFYVAVEkEEWKFDTLCDLYETLTI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 269 NQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKT 348
Cdd:PTZ00424 268 TQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPAS 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 50289935 349 AETYLHRIGRSGRFGHLGLAINLINWNDRFNLYKIEQELGTEIAAIPATI 398
Cdd:PTZ00424 348 PENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEV 397
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
31-392 |
4.12e-90 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 283.23 E-value: 4.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 31 NSFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTRE 110
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 111 LALQTSQVIRTLGR--HcGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSR 188
Cdd:PRK11776 84 LADQVAKEIRRLARfiP-NIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 189 DFKTIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEINLMEELTLKGITQYYAFVEERQKLHCLNTLFSKLQI 268
Cdd:PRK11776 163 GFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDERLPALQRLLLHHQP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 269 NQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKT 348
Cdd:PRK11776 243 ESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARD 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 50289935 349 AETYLHRIGRSGRFGHLGLAINLINWNDRFNLYKIEQELGTEIA 392
Cdd:PRK11776 323 PEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
42-232 |
1.12e-83 |
|
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: 257.37 E-value: 1.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 42 LLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKP----KLNKIQALIMVPTRELALQTSQ 117
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 118 VIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTIIEQV 197
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 50289935 198 LTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEI 232
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
32-395 |
3.90e-78 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 252.04 E-value: 3.90e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 32 SFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI-----KPKLNK-IQALIM 105
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitrqpHAKGRRpVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 106 VPTRELALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKM 185
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 186 LSRDFKTIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEINLMEELTL-KGITQYYAFVEERQKLHCLNTLFS 264
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTAsEQVTQHVHFVDKKRKRELLSQMIG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 265 KLQINQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFD 344
Cdd:PRK10590 242 KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 50289935 345 FPKTAETYLHRIGRSGRFGHLGLAINLINWNDRFNLYKIEQELGTEIA--AIP 395
Cdd:PRK10590 322 LPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPriAIP 374
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
33-384 |
9.93e-78 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 250.24 E-value: 9.93e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 33 FEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI------KPKLNKIqaLIMV 106
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfprrKSGPPRI--LILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 107 PTRELALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKML 186
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 187 SRDFKTIIEQVLTFLPKAHQSLLFSATfpL---TVKEFMVKHLHKPYEIN----LMEEltlKGITQYYAFVEERQ-KLHC 258
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSAT--LegdAVQDFAERLLNDPVEVEaepsRRER---KKIHQWYYRADDLEhKTAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 259 LNTLFSKLQINQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVN 338
Cdd:PRK11192 236 LCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 50289935 339 VVINFDFPKTAETYLHRIGRSGRFGHLGLAINLINWNDRFNLYKIE 384
Cdd:PRK11192 316 HVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIE 361
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
32-391 |
1.07e-71 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 239.75 E-value: 1.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 32 SFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTREL 111
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 112 ALQTSQVIRTLGRHC-GVSCMVTTGGTnlRDDI-LR-LNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSR 188
Cdd:PRK11634 87 AVQVAEAMTDFSKHMrGVNVVALYGGQ--RYDVqLRaLRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 189 DFKTIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEINLMEELTLK-GITQYYAFVEERQKLHCLNTLFSKLQ 267
Cdd:PRK11634 165 GFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRpDISQSYWTVWGMRKNEALVRFLEAED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 268 INQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPK 347
Cdd:PRK11634 245 FDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 50289935 348 TAETYLHRIGRSGRFGHLGLAINLINWNDRFNLYKIEQELGTEI 391
Cdd:PRK11634 325 DSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTI 368
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
33-232 |
1.32e-67 |
|
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: 216.16 E-value: 1.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 33 FEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTRELA 112
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 113 LQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKT 192
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 50289935 193 IIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEI 232
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
35-232 |
1.45e-67 |
|
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: 215.65 E-value: 1.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 35 DFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTRELALQ 114
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 115 TSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTII 194
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 50289935 195 EQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEI 232
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
32-368 |
9.48e-65 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 219.26 E-value: 9.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 32 SFEDFYLKrellmGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI--KPKLNKIQA---LIMV 106
Cdd:PTZ00110 136 SFPDYILK-----SLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHInaQPLLRYGDGpivLVLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 107 PTRELALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKML 186
Cdd:PTZ00110 211 PTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRML 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 187 SRDFKTIIEQVLTFLPKAHQSLLFSATFPLTVKEfMVKHL--HKPYEINLmEELTLKG---ITQYYAFVEERQKLHCLNT 261
Cdd:PTZ00110 291 DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQS-LARDLckEEPVHVNV-GSLDLTAchnIKQEVFVVEEHEKRGKLKM 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 262 LFSKL--QINQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNV 339
Cdd:PTZ00110 369 LLQRImrDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKY 448
|
330 340
....*....|....*....|....*....
gi 50289935 340 VINFDFPKTAETYLHRIGRSGRFGHLGLA 368
Cdd:PTZ00110 449 VINFDFPNQIEDYVHRIGRTGRAGAKGAS 477
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
33-391 |
1.43e-62 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 211.69 E-value: 1.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 33 FEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIK----PK---LNKIQALIM 105
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLqtppPKeryMGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 106 VPTRELALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNET-VHVLVGTPGRVLDLASRKVADLSECSLFVMDEADK 184
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 185 MLSRDFKTIIEQVLTFLPKA--HQSLLFSATFPLTVKEFMVKHLHKPYEINL-MEELTLKGITQYYAFVEERQKLHCLNT 261
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIePENVASDTVEQHVYAVAGSDKYKLLYN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 262 LFSKLQINQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVI 341
Cdd:PRK01297 329 LVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVI 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 50289935 342 NFDFPKTAETYLHRIGRSGRFGHLGLAINLINWNDRFNLYKIEQELGTEI 391
Cdd:PRK01297 409 NFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKI 458
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
32-418 |
3.72e-60 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 207.50 E-value: 3.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 32 SFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVI---------PTLEKIKPKlnKIQA 102
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVavmnrllsrPALADRKPE--DPRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 103 LIMVPTRELALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLD-LASRKVADLSECSLFVMDE 181
Cdd:PRK04537 88 LILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDyVKQHKVVSLHACEICVLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 182 ADKMLSRDFKTIIEQVLTFLPK--AHQSLLFSATFPLTVKEFMVKHLHKPYEINL-MEELTLKGITQYYAFVEERQKLHC 258
Cdd:PRK04537 168 ADRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVeTETITAARVRQRIYFPADEEKQTL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 259 LNTLFSKLQINQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVN 338
Cdd:PRK04537 248 LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 339 VVINFDFPKTAETYLHRIGRSGRFGHLGLAINLINWNDRFNLYKIEQELGTEIAAIPATidkslyvAEDDTAVPVP--VP 416
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPVT-------AELLTPLPRPprVP 400
|
..
gi 50289935 417 IE 418
Cdd:PRK04537 401 VE 402
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
33-427 |
6.79e-60 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 203.28 E-value: 6.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 33 FEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPT----LEKIKP---KLNKIQALIM 105
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATfhylLSHPAPedrKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 106 VPTRELALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKM 185
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 186 LSRDFKTIIEQVLTFLPKAHQ--SLLFSATFPLTVKEFMVKHLHKPYEINLM-EELTLKGITQ--YYAFVEERQKLhcLN 260
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEpEQKTGHRIKEelFYPSNEEKMRL--LQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 261 TLFSKLQINQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVV 340
Cdd:PRK04837 248 TLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 341 INFDFPKTAETYLHRIGRSGRFGHLGLAINLINWNDRFNLYKIEQELGteiAAIPATIDKSLYVAEDdtaVPVPVPIEDP 420
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIG---HSIPVSKYDSDALLTD---LPKPLRLTRP 401
|
....*..
gi 50289935 421 HIVHQRR 427
Cdd:PRK04837 402 RTGNGPR 408
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
32-405 |
3.15e-58 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 201.17 E-value: 3.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 32 SFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI-------KPKLNKIQALI 104
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCctirsghPSEQRNPLAMV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 105 MVPTRELALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADK 184
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 185 MLSRDFKTIIEQVLTFLPKAhQSLLFSATFPLTV--------KEFMVKHLHKPYEINlmeeltlKGITQYYAFVEERQKL 256
Cdd:PLN00206 282 MLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVekfasslaKDIILISIGNPNRPN-------KAVKQLAIWVETKQKK 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 257 HclnTLFSKLQINQ-----AIIFCNSTNRVELLAKKITDL-GYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTR 330
Cdd:PLN00206 354 Q---KLFDILKSKQhfkppAVVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGR 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50289935 331 GIDIQAVNVVINFDFPKTAETYLHRIGRSGRFGHLGLAINLINWNDRfNLYK-IEQELGTEIAAIPATIDKSLYVA 405
Cdd:PLN00206 431 GVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDR-NLFPeLVALLKSSGAAIPRELANSRYLG 505
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
55-221 |
1.77e-57 |
|
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: 188.22 E-value: 1.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 55 SPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTRELALQTSQVIRTLGRHCGVSCMVTT 134
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 135 GGTNLRDDILRLnETVHVLVGTPGRVLDLASRKVAdLSECSLFVMDEADKMLSRDFKTIIEQVLTFLPKAHQSLLFSATF 214
Cdd:pfam00270 81 GGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 50289935 215 PLTVKEF 221
Cdd:pfam00270 159 PRNLEDL 165
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
38-221 |
3.30e-57 |
|
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: 188.55 E-value: 3.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 38 LKRELLMGIFEAGFEKPSPIQEEAIPVAITG--RDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTRELALQT 115
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 116 SQVIRTLGRHCGVSCMVTtggtnLRDDILRLNETV--HVLVGTPGRVLDLASRKVADLSECSLFVMDEADKML-SRDFKT 192
Cdd:cd17963 81 GEVVEKMGKFTGVKVALA-----VPGNDVPRGKKItaQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLdTQGHGD 155
|
170 180
....*....|....*....|....*....
gi 50289935 193 IIEQVLTFLPKAHQSLLFSATFPLTVKEF 221
Cdd:cd17963 156 QSIRIKRMLPRNCQILLFSATFPDSVRKF 184
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
33-232 |
9.71e-57 |
|
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: 187.67 E-value: 9.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 33 FEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTRELA 112
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 113 LQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKT 192
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 50289935 193 IIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEI 232
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
243-372 |
1.56e-56 |
|
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: 184.63 E-value: 1.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 243 ITQYYAFVEERQKLHCLN-TLFSKLQINQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRT 321
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 50289935 322 LVCSDLLTRGIDIQAVNVVINFDFPKTAETYLHRIGRSGRFGHLGLAINLI 372
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
32-232 |
1.78e-55 |
|
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: 184.44 E-value: 1.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 32 SFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIkpkLNKIQ---ALIMVPT 108
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL---LENPQrffALVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 109 RELALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLD-LASRKVADLSECSLFVMDEADKMLS 187
Cdd:cd17954 78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADRLLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 50289935 188 RDFKTIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEI 232
Cdd:cd17954 158 MDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
42-229 |
3.97e-55 |
|
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: 183.23 E-value: 3.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 42 LLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTRELALQTSQVIRT 121
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 122 LGRHC-GVSCMVTTGGTNLRDDILRLNETvHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTIIEQVLTF 200
Cdd:cd17943 81 IGKKLeGLKCEVFIGGTPVKEDKKKLKGC-HIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180
....*....|....*....|....*....
gi 50289935 201 LPKAHQSLLFSATFPLTVKEFMVKHLHKP 229
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKP 188
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
42-232 |
6.22e-55 |
|
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: 182.84 E-value: 6.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 42 LLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI---KPKLNKIQALIMVPTRELALQTSQV 118
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 119 IRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLD-LASRKVADLSECSLFVMDEADKMLSRDFKTIIEQV 197
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDhLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 50289935 198 LTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEI 232
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
30-232 |
7.17e-55 |
|
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: 182.93 E-value: 7.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 30 GNSFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTR 109
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 110 ELALQTSQVIRTLGRHC-GVSCMVTTGGTNLRDDILRL-NETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKML- 186
Cdd:cd17950 81 ELAFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLe 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 50289935 187 SRDFKTIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEI 232
Cdd:cd17950 161 QLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
38-214 |
5.24e-51 |
|
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: 172.77 E-value: 5.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 38 LKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI-KPKLNK-----IQALIMVPTREL 111
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlKAKAESgeeqgTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 112 ALQTSQVIRTLGRHCG--VSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRK-VADLSECSLFVMDEADKMLSR 188
Cdd:cd17961 81 AQQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGsLLLLSTLKYLVIDEADLVLSY 160
|
170 180
....*....|....*....|....*.
gi 50289935 189 DFKTIIEQVLTFLPKAHQSLLFSATF 214
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATL 186
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
32-229 |
5.25e-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: 172.87 E-value: 5.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 32 SFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNK--IQALIMVPTR 109
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTvgARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 110 ELALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRD 189
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 50289935 190 FKTIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKP 229
Cdd:cd17959 162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEP 201
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
46-246 |
4.16e-50 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 170.37 E-value: 4.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 46 IFEAGFEKPSPIQEEAIPVAITG-RDILARAKNGTGKTAAFVIPTLEKIKPKlNKIQALIMVPTRELALQTSQVIRTLGR 124
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 125 HCGVSCMVTTGGTNLRDDILRL-NETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTIIEQVLTFLPK 203
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 50289935 204 AHQSLLFSATFPLTVKEFMVKHLHKPYEINLmEELTLKGITQY 246
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV-GFTPLEPIEQF 201
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
32-226 |
6.07e-49 |
|
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: 167.66 E-value: 6.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 32 SFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI---KPKLNKI-------Q 101
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledGPPSVGRgrrkaypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 102 ALIMVPTRELALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDE 181
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 50289935 182 ADKMLSRDFKTIIEQVL---TFLPKA-HQSLLFSATFPLTV----KEFMVKHL 226
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVehpDMPPKGeRQTLMFSATFPREIqrlaADFLKNYI 213
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
33-226 |
1.18e-47 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 164.03 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 33 FEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIkpklnkiQALIMVPTRELA 112
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 113 LQTSQVIRTLGRHCG---VSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRD 189
Cdd:cd17938 74 EQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 50289935 190 FKTIIEQVLTFLPKAH------QSLLFSAtfplTVKEFMVKHL 226
Cdd:cd17938 154 NLETINRIYNRIPKITsdgkrlQVIVCSA----TLHSFEVKKL 192
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
43-234 |
3.14e-47 |
|
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: 162.46 E-value: 3.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 43 LMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPK----LNKIQALIMVPTRELALQTSQV 118
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRErwtpEDGLGALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 119 IRTLGRHCGVSCMVTTGGTNLRDDILRLNeTVHVLVGTPGRVLDLASRKVA-DLSECSLFVMDEADKMLSRDFKTIIEQV 197
Cdd:cd17941 82 LRKVGKYHSFSAGLIIGGKDVKEEKERIN-RMNILVCTPGRLLQHMDETPGfDTSNLQMLVLDEADRILDMGFKETLDAI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 50289935 198 LTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEINL 234
Cdd:cd17941 161 VENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
41-231 |
7.50e-47 |
|
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: 161.98 E-value: 7.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 41 ELLMGIFEAGFEKPSPIQEEAIPVAI-TGRDILARAKNGTGKTAAFVIPTLE-----KIKPKLNKIQALIMVPTRELALQ 114
Cdd:cd17964 4 SLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQsllntKPAGRRSGVSALIISPTRELALQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 115 T-SQVIRTLGRHCGVSCMVTTGGTNLRDDILRL-NETVHVLVGTPGRVLDL--ASRKVADLSECSLFVMDEADKMLSRDF 190
Cdd:cd17964 84 IaAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHleNPGVAKAFTDLDYLVLDEADRLLDMGF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 50289935 191 KTIIEQVLTFLPKAH----QSLLFSATFPLTVKEFMVKHLHKPYE 231
Cdd:cd17964 164 RPDLEQILRHLPEKNadprQTLLFSATVPDEVQQIARLTLKKDYK 208
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
42-229 |
8.28e-47 |
|
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: 162.10 E-value: 8.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 42 LLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI--KPKL---NKIQ---ALIMVPTRELAL 113
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsrLPPLdeeTKDDgpyALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 114 QTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTI 193
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 50289935 194 IEQVLTFLP--------------------KAHQSLLFSATFPLTVKEFMVKHLHKP 229
Cdd:cd17945 161 VTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRP 216
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
33-232 |
1.90e-44 |
|
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: 155.46 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 33 FEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTRELA 112
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 113 LQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDL---ASRKVADLSECSLFVMDEADKMLSRD 189
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHlrsSDDTTKVLSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 50289935 190 FKTIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEI 232
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFW 203
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
38-232 |
2.09e-44 |
|
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: 156.00 E-value: 2.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 38 LKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIK--PKLNKIQ---ALIMVPTRELA 112
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKdqRPVKPGEgpiGLIMAPTRELA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 113 LQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDL---ASRKVADLSECSLFVMDEADKMLSRD 189
Cdd:cd17953 99 LQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDIltaNNGRVTNLRRVTYVVLDEADRMFDMG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 50289935 190 FKTIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEI 232
Cdd:cd17953 179 FEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
42-233 |
1.55e-43 |
|
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: 152.73 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 42 LLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI-----KPKLNKIQALIMVPTRELALQTS 116
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 117 QVIRTLGRHCG--VSCMVTTGGTN-LRDDILRLNETVHVLVGTPGRVLDLASRK--VADLSECSLFVMDEADKMLSRDFK 191
Cdd:cd17960 81 EVLQSFLEHHLpkLKCQLLIGGTNvEEDVKKFKRNGPNILVGTPGRLEELLSRKadKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 50289935 192 TIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEIN 233
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
42-232 |
6.53e-43 |
|
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: 150.78 E-value: 6.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 42 LLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTRELALQTSQVIRT 121
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 122 LGRhcGVSCMVTT---GGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTIIEQVL 198
Cdd:cd17962 81 LMK--GLPPMKTAllvGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
|
170 180 190
....*....|....*....|....*....|....
gi 50289935 199 TFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEI 232
Cdd:cd17962 159 ENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
42-229 |
1.17e-42 |
|
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: 150.43 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 42 LLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNK--IQALIMVPTRELALQTSQVI 119
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 120 RTLGRHCGV-SCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTIIEQVL 198
Cdd:cd17957 81 LKLSKGTGLrIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
|
170 180 190
....*....|....*....|....*....|..
gi 50289935 199 TFLPKAH-QSLLFSATFPLTVKEFMVKHLHKP 229
Cdd:cd17957 161 AACTNPNlQRSLFSATIPSEVEELARSVMKDP 192
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
42-232 |
4.19e-41 |
|
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: 146.02 E-value: 4.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 42 LLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI--KPKLNKIQ---ALIMVPTRELALQTS 116
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImdQRELEKGEgpiAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 117 QVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTIIEQ 196
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 50289935 197 VLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEI 232
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
31-230 |
6.34e-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: 147.81 E-value: 6.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 31 NSFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI------KPKLNKIQ--- 101
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegltASSFSEVQepq 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 102 ALIMVPTRELALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDE 181
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 50289935 182 ADKMLSRDFKTIIEQVLTFL---PKA-HQSLLFSATFPLTVKEFMVKHLHKPY 230
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEPgmpSKEdRQTLMFSATFPEEIQRLAAEFLKEDY 255
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
43-213 |
3.50e-40 |
|
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: 143.65 E-value: 3.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 43 LMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLE-----KIKPKlNKIQALIMVPTRELALQTSQ 117
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyklKFKPR-NGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 118 VIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLD-LASRKVADLSECSLFVMDEADKMLSRDFKTIIEQ 196
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
|
170
....*....|....*..
gi 50289935 197 VLTFLPKAHQSLLFSAT 213
Cdd:cd17942 161 IIKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
42-233 |
1.32e-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: 139.78 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 42 LLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIP----TLEKIKpKLNKIQ-----ALIMVPTRELA 112
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlimfALEQEK-KLPFIKgegpyGLIVCPSRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 113 LQTSQVIRTLGRHC------GVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKML 186
Cdd:cd17951 80 RQTHEVIEYYCKALqeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 50289935 187 SRDFKTIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEIN 233
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
32-239 |
3.35e-38 |
|
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: 139.39 E-value: 3.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 32 SFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITG--RDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTR 109
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 110 ELALQTSQVIRTLGRHC-GVSCMVTTGGTNLR--DDIlrlneTVHVLVGTPGRVLDLASR-KVADLSECSLFVMDEADKM 185
Cdd:cd18048 99 ELALQTGKVVEEMGKFCvGIQVIYAIRGNRPGkgTDI-----EAQIVIGTPGTVLDWCFKlRLIDVTNISVFVLDEADVM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 50289935 186 LS-RDFKTIIEQVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKPYEINL-MEELT 239
Cdd:cd18048 174 INvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLkKEELT 229
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
46-233 |
7.40e-38 |
|
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: 137.50 E-value: 7.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 46 IFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIK--PKLNKIQ---ALIMVPTRELALQTSQVIR 120
Cdd:cd17966 5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINaqPPLERGDgpiVLVLAPTRELAQQIQQEAN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 121 TLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTIIEQVLTF 200
Cdd:cd17966 85 KFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQ 164
|
170 180 190
....*....|....*....|....*....|...
gi 50289935 201 LPKAHQSLLFSATFPLTVKEFMVKHLHKPYEIN 233
Cdd:cd17966 165 IRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
31-215 |
1.40e-36 |
|
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: 135.55 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 31 NSFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI---KPKLNKIQ------ 101
Cdd:cd18051 21 ETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqGPGESLPSesgyyg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 102 -------ALIMVPTRELALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSEC 174
Cdd:cd18051 101 rrkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYC 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 50289935 175 SLFVMDEADKMLSRDFKT----IIEQvLTFLPKA-HQSLLFSATFP 215
Cdd:cd18051 181 KYLVLDEADRMLDMGFEPqirrIVEQ-DTMPPTGeRQTLMFSATFP 225
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
50-229 |
1.78e-34 |
|
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: 128.86 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 50 GFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQ------ALIMVPTRELALQTSQVIRTLG 123
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 124 RHCG--VSCMVtTGGTNLRDDILRLNETVHVLVGTPGRVLD-LASRKVADLSECSLFVMDEADKMLSRDFKTIIEQVLTF 200
Cdd:cd17949 90 KPFHwiVPGYL-IGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILEL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 50289935 201 L-------------PKAHQSLLFSATFPLTVKEFMVKHLHKP 229
Cdd:cd17949 169 LddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDP 210
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
254-363 |
1.66e-33 |
|
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: 122.70 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 254 QKLHCLNTLFSKLQINQAIIFCNSTNRVE--LLAKKItdlGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRG 331
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEaeLLLEKE---GIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 50289935 332 IDIQAVNVVINFDFPKTAETYLHRIGRSGRFG 363
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
42-214 |
3.59e-33 |
|
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: 125.81 E-value: 3.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 42 LLMGIFEAGFEKPSPIQEEAIPVAIT-GRDILARAKNGTGKTAAFVIPTLEKI------KPKLNKI---QALIMVPTREL 111
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlsqkssNGVGGKQkplRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 112 ALQTSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRK---VADLSECSLFVMDEADKMLSR 188
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....
gi 50289935 189 -DFKTiIEQVLTFLPKAH-------QSLLFSATF 214
Cdd:cd17946 161 gHFAE-LEKILELLNKDRagkkrkrQTFVFSATL 193
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
32-229 |
1.10e-31 |
|
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: 120.98 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 32 SFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITG--RDILARAKNGTGKTAAFVIPTLEKIKPKLNKIQALIMVPTR 109
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 110 ELALQTSQVIRTLGR-HCGVSCMVTTGGTNLRDDIlRLNEtvHVLVGTPGRVLDLASR-KVADLSECSLFVMDEADKMLS 187
Cdd:cd18047 82 ELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQ-KISE--QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 50289935 188 ----RDFKTIIEQVltfLPKAHQSLLFSATFPLTVKEFMVKHLHKP 229
Cdd:cd18047 159 tqghQDQSIRIQRM---LPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
42-229 |
1.78e-31 |
|
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: 120.26 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 42 LLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIP----TLEKIKPKLNKIQA--LIMVPTRELALQT 115
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgfihLDLQPIPREQRNGPgvLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 116 SQVIRTLgRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTIIE 195
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....
gi 50289935 196 QVLTFLPKAHQSLLFSATFPLTVKEFMVKHLHKP 229
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDP 193
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
51-234 |
6.21e-31 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 119.73 E-value: 6.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 51 FEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI--KPKLNKIQA---LIMVPTRELALQTSQVIRTLGRH 125
Cdd:cd18049 44 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHInhQPFLERGDGpicLVLAPTRELAQQVQQVAAEYGRA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 126 CGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTIIEQVLTFLPKAH 205
Cdd:cd18049 124 CRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 203
|
170 180
....*....|....*....|....*....
gi 50289935 206 QSLLFSATFPLTVKEFMVKHLHKPYEINL 234
Cdd:cd18049 204 QTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
56-231 |
2.96e-30 |
|
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: 116.87 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 56 PIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKPKLNKI------QALIMVPTRELALQTSQVIRTLGRHCGVS 129
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQVTKDFKDITRKLSVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 130 CMVttGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTIIEQVLTFLPKAH---- 205
Cdd:cd17944 95 CFY--GGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSYKKDsedn 172
|
170 180
....*....|....*....|....*..
gi 50289935 206 -QSLLFSATFPLTVKEFMVKHLHKPYE 231
Cdd:cd17944 173 pQTLLFSATCPDWVYNVAKKYMKSQYE 199
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
46-234 |
1.73e-29 |
|
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: 117.03 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 46 IFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI--KPKLNKIQA---LIMVPTRELALQTSQVIR 120
Cdd:cd18050 77 LLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHInhQPYLERGDGpicLVLAPTRELAQQVQQVAD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 121 TLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFKTIIEQVLTF 200
Cdd:cd18050 157 DYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ 236
|
170 180 190
....*....|....*....|....*....|....
gi 50289935 201 LPKAHQSLLFSATFPLTVKEFMVKHLHKPYEINL 234
Cdd:cd18050 237 IRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
282-363 |
7.38e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 106.14 E-value: 7.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 282 ELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYLHRIGRSGR 361
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 50289935 362 FG 363
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
42-259 |
1.38e-25 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 104.76 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 42 LLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKI-------KPKLNKIQALIMVPTRELALQ 114
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 115 TSQVIRTLGRHCGVSCMVTTGGTNLRDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEADKMLSRDFktiI 194
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSF---N 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 195 EQVLTFLPKAH----------------QSLLFSATFPLTVKEFmvkhLHKPYEINLMEELTlkgitqyyafveeRQKLHC 258
Cdd:cd17948 158 EKLSHFLRRFPlasrrsentdgldpgtQLVLVSATMPSGVGEV----LSKVIDVDSIETVT-------------SDKLHR 220
|
.
gi 50289935 259 L 259
Cdd:cd17948 221 L 221
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
50-228 |
2.11e-24 |
|
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: 101.55 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 50 GFEKPSPIQEEAIPVAITG---------RDILARAKNGTGKTAAFVIPTLEKIKPK-LNKIQALIMVPTRELALQTSQVI 119
Cdd:cd17956 9 GITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRvVPRLRALIVVPTKELVQQVYKVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 120 RTLGRHCGVSCMVTTGGTNLRDDI--------LRLNETVHVLVGTPGRVLD-LASRKVADLSECSLFVMDEADKMLSRDF 190
Cdd:cd17956 89 ESLCKGTGLKVVSLSGQKSFKKEQklllvdtsGRYLSRVDILVATPGRLVDhLNSTPGFTLKHLRFLVIDEADRLLNQSF 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 50289935 191 KTIIEQVLtFLPKAHQSLLFSATFPLTVKEFMVKHLHK 228
Cdd:cd17956 169 QDWLETVM-KALGRPTAPDLGSFGDANLLERSVRPLQK 205
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
15-358 |
1.83e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 94.71 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 15 KKDTRPQTDDVLNTKGNSFEDFYLKRELL-MGIFEAGFE-KPSPIQEEAI-----PVAITGRDILARAKNGTGKT--AAF 85
Cdd:COG1061 40 LAIKEGTREDGRRLPEEDTERELAEAEALeAGDEASGTSfELRPYQQEALeallaALERGGGRGLVVAPTGTGKTvlALA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 86 VIPTLEKIKPklnkiqALIMVPTRELALQTsqvIRTLGRHCGVScmvttGGTNLRDDILRlnetvHVLVGTpgrVLDLAS 165
Cdd:COG1061 120 LAAELLRGKR------VLVLVPRRELLEQW---AEELRRFLGDP-----LAGGGKKDSDA-----PITVAT---YQSLAR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 166 RKVADL--SECSLFVMDEADKMLSRDFKTIIEQvltfLPKAHQsLLFSAT------FPLTVKEFM--------------- 222
Cdd:COG1061 178 RAHLDElgDRFGLVIIDEAHHAGAPSYRRILEA----FPAAYR-LGLTATpfrsdgREILLFLFDgivyeyslkeaiedg 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 223 --VKHLHKPYEINLMEELTL-----KGITQYYAFVEERqKLHCLNTLFSKL-QINQAIIFCNSTNRVELLAKKITDLGYS 294
Cdd:COG1061 253 ylAPPEYYGIRVDLTDERAEydalsERLREALAADAER-KDKILRELLREHpDDRKTLVFCSSVDHAEALAELLNEAGIR 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50289935 295 CYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYLHRIGR 358
Cdd:COG1061 332 AAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGR 395
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
53-235 |
3.48e-19 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 87.05 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 53 KPSPIQEEAIPvAITGRDILAR-----------------AKNGTGKTAAFVIPTLEKIK-----------------PKLN 98
Cdd:cd17965 30 KPSPIQTLAIK-KLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYLAPLLDYLKrqeqepfeeaeeeyesaKDTG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 99 KIQALIMVPTRELALQTSQVIRTLGRHCGVSC-MVTTGGTNLRDDILRLNET-VHVLVGTPGRVLDLASRKVADLSECSL 176
Cdd:cd17965 109 RPRSVILVPTHELVEQVYSVLKKLSHTVKLGIkTFSSGFGPSYQRLQLAFKGrIDILVTTPGKLASLAKSRPKILSRVTH 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50289935 177 FVMDEADKMLSRDFKTIIEQVLTFLPKAHQSLLFSATFPltvKEFMvKHLHK--PYEINLM 235
Cdd:cd17965 189 LVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP---KEFD-KTLRKlfPDVVRIA 245
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
68-213 |
1.07e-14 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 71.28 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 68 GRDILARAKNGTGKTAAFVIPTLEKIKPKlnKIQALIMVPTRELALQTSQVIRTLGRHcGVSCMVTTGGTNLRDDILRLN 147
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKK--GKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50289935 148 ETVHVLVGTPGRVLDLASRKVAD-LSECSLFVMDEADKMLSRDFKTII--EQVLTFLPKAHQSLLFSAT 213
Cdd:cd00046 78 GDADIIIATPDMLLNLLLREDRLfLKDLKLIIVDEAHALLIDSRGALIldLAVRKAGLKNAQVILLSAT 146
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
271-363 |
1.39e-13 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 67.62 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 271 AIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAE 350
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
90
....*....|...
gi 50289935 351 TYLHRIGRSGRFG 363
Cdd:cd18794 113 SYYQESGRAGRDG 125
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
249-358 |
2.41e-12 |
|
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: 64.53 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 249 FVEERQKLHCLNTLFSKLQINQAIIFCNStnrvellakkITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLL 328
Cdd:cd18802 31 FVERRATAVVLSRLLKEHPSTLAFIRCGF----------LIGRGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVL 100
|
90 100 110
....*....|....*....|....*....|
gi 50289935 329 TRGIDIQAVNVVINFDFPKTAETYLHRIGR 358
Cdd:cd18802 101 EEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
272-361 |
1.45e-11 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 66.32 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 272 IIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCsdllT----RGIDIQAVNVVINFDFPK 347
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVA----TiafgMGIDKPDVRFVIHYDLPK 309
|
90
....*....|....
gi 50289935 348 TAETYLHRIGRSGR 361
Cdd:COG0514 310 SIEAYYQEIGRAGR 323
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
50-363 |
2.89e-10 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 62.81 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 50 GFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKikpklnkiQALIMVPTRELALQTSQVIRTLGRHCGVS 129
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL--------DGLTLVVSPLISLMKDQVDQLLANGVAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 130 CMVTTGGTNLRDDILRLNET--VHVLVGTPGRVL-DLASRKVADLSECSLFVmDEAD--KMLSRDFKT------IIEQVL 198
Cdd:PRK11057 94 CLNSTQTREQQLEVMAGCRTgqIKLLYIAPERLMmDNFLEHLAHWNPALLAV-DEAHciSQWGHDFRPeyaalgQLRQRF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 199 TFLPkahqSLLFSATFPLTVKEFMVK--HLHKPYE-----------INLMEELtlKGITQYYAFVEErQKLHClntlfsk 265
Cdd:PRK11057 173 PTLP----FMALTATADDTTRQDIVRllGLNDPLIqissfdrpnirYTLVEKF--KPLDQLMRYVQE-QRGKS------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 266 lqinqAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDF 345
Cdd:PRK11057 239 -----GIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDI 313
|
330
....*....|....*...
gi 50289935 346 PKTAETYLHRIGRSGRFG 363
Cdd:PRK11057 314 PRNIESYYQETGRAGRDG 331
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
272-361 |
2.76e-09 |
|
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: 55.73 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 272 IIFCNSTNRVELLAKKITDLGYSCYYS------HARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDF 345
Cdd:cd18796 42 LVFTNTRSQAERLAQRLRELCPDRVPPdfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90
....*....|....*.
gi 50289935 346 PKTAETYLHRIGRSGR 361
Cdd:cd18796 122 PKSVARLLQRLGRSGH 137
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
270-363 |
4.78e-09 |
|
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: 53.09 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 270 QAIIFCNSTNRVELLAKKITdlgyscyysharmkqqdrnkvfhdfrqgkvrTLVCSDLLTRGIDIQAVNVVINFDFPKTA 349
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90
....*....|....
gi 50289935 350 ETYLHRIGRSGRFG 363
Cdd:cd18785 54 ASYIQRVGRAGRGG 67
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
53-182 |
1.56e-08 |
|
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: 54.58 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 53 KPSPIQEEAIPVAITgRDILARAKNGTGKT--AAFVIPTLEKI--KPKLNKIQALIMVPTRELALQTSQVIRTlgrHCGV 128
Cdd:cd18034 2 TPRSYQLELFEAALK-RNTIVVLPTGSGKTliAVMLIKEMGELnrKEKNPKKRAVFLVPTVPLVAQQAEAIRS---HTDL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 50289935 129 SCMVTTGGTNL----RDDILRLNETVHVLVGTPGRVLDLASRKVADLSECSLFVMDEA 182
Cdd:cd18034 78 KVGEYSGEMGVdkwtKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
270-369 |
1.98e-08 |
|
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: 53.03 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 270 QAIIFCNSTNRVELLAKKI------TDLGYSCYYSH-ARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVIN 342
Cdd:cd18797 37 KTIVFCRSRKLAELLLRYLkarlveEGPLASKVASYrAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
|
90 100
....*....|....*....|....*..
gi 50289935 343 FDFPKTAETYLHRIGRSGRFGHLGLAI 369
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
268-363 |
3.26e-08 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 56.28 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 268 INQAIIFCNSTNRVELLAKKITDLGYSC--------YYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNV 339
Cdd:COG1111 353 DSRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqasKEGDKGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDL 432
|
90 100
....*....|....*....|....
gi 50289935 340 VINFDFPKTAETYLHRIGRSGRFG 363
Cdd:COG1111 433 VIFYEPVPSEIRSIQRKGRTGRKR 456
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
271-358 |
2.46e-07 |
|
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: 49.09 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 271 AIIFCNSTNRVELLAKKITDLGYSCYYSHAR--MKQQDRNKVFHDF-RQGKVRTLVCSDLLTRGIDIQAVNVVInFDFPK 347
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFfGELKPPILVTVDLLTTGVDIPEVDNVV-FLRPT 87
|
90
....*....|..
gi 50289935 348 TAET-YLHRIGR 358
Cdd:cd18799 88 ESRTlFLQMLGR 99
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
302-361 |
3.78e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 49.28 E-value: 3.78e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 302 MKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYLHRIGRSGR 361
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
48-369 |
4.48e-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: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 48 EAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKIKpKLNKIQALIMVPTRELA---LQT-SQVIRTLG 123
Cdd:COG1205 51 KRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL-EDPGATALYLYPTKALArdqLRRlRELAEALG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 124 RhcGVSCMVTTGGT--NLRDDILrlnETVHVLVGTP-----GrvLDLASRKVAD-LSECSLFVMDEAD----------KM 185
Cdd:COG1205 130 L--GVRVATYDGDTppEERRWIR---EHPDIVLTNPdmlhyG--LLPHHTRWARfFRNLRYVVIDEAHtyrgvfgshvAN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 186 LSRDFKTIIEQV---LTFL--------PKAHQSLLF-----------SATFPLTVkeFMVKhlhkPYEINLMEELtlkgi 243
Cdd:COG1205 203 VLRRLRRICRHYgsdPQFIlasatignPAEHAERLTgrpvtvvdedgSPRGERTF--VLWN----PPLVDDGIRR----- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 244 tqyYAFVEERQklhclntLFSKLQIN--QAIIFCNSTNRVELLAKKITDL-----------GYscyysHARMKQQDRNKV 310
Cdd:COG1205 272 ---SALAEAAR-------LLADLVREglRTLVFTRSRRGAELLARYARRAlrepdladrvaAY-----RAGYLPEERREI 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 50289935 311 FHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYLHRIGRSGRFGHLGLAI 369
Cdd:COG1205 337 ERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
252-341 |
8.47e-07 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 48.78 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 252 ERQKLHCLNTlfSKLQI-----------NQAIIFCNSTNRVELLAKKitdLGYscYYSHARMKQQDRNKVFHDFRQGKVR 320
Cdd:cd18789 24 KRRLLAAMNP--NKLRAleellkrheqgDKIIVFTDNVEALYRYAKR---LLK--PFITGETPQSEREEILQNFREGEYN 96
|
90 100
....*....|....*....|.
gi 50289935 321 TLVCSDLLTRGIDIQAVNVVI 341
Cdd:cd18789 97 TLVVSKVGDEGIDLPEANVAI 117
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
255-363 |
1.44e-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: 47.47 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 255 KLHCLNTLFSKLQINQ--AIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQG-KVRTLVCSdllTR- 330
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVFLLS---TKa 88
|
90 100 110
....*....|....*....|....*....|....*...
gi 50289935 331 ---GIDIQAVNVVINFDFP--KTAEtyLHRIGRSGRFG 363
Cdd:cd18793 89 ggvGLNLTAANRVILYDPWwnPAVE--EQAIDRAHRIG 124
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
215-361 |
1.89e-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: 47.55 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 215 PLTVKEFMVKHLHkpyeINLMEELTLKGITQYYAFVEERQKLHClntlfsklqiNQAIIFCNSTNRVELLAKKITDLGys 294
Cdd:cd18795 4 PLEEYVLGFNGLG----IKLRVDVMNKFDSDIIVLLKIETVSEG----------KPVLVFCSSRKECEKTAKDLAGIA-- 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50289935 295 cyYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVIN----FDfPKTAE-----TYLHRIGRSGR 361
Cdd:cd18795 68 --FHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKgtqrYD-GKGYRelsplEYLQMIGRAGR 140
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
299-373 |
2.83e-05 |
|
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: 44.57 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 299 HARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDfpktAETY----LHRI-GRSGRFGHLGLAINLIN 373
Cdd:cd18792 67 HGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED----ADRFglsqLHQLrGRVGRGKHQSYCYLLYP 142
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
279-364 |
3.40e-05 |
|
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: 43.87 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 279 NRVE---LLAKKITDL--GYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYL 353
Cdd:cd18810 33 NRIEsieKLATQLRQLvpEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQL 112
|
90
....*....|....*
gi 50289935 354 H----RIGRSGRFGH 364
Cdd:cd18810 113 YqlrgRVGRSKERAY 127
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
271-363 |
3.61e-05 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 46.37 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 271 AIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGK-VRTLVCSdllTR----GIDIQAVNVVINFDF 345
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLIS---LKaggeGLNLTAADHVIHYDL 628
|
90
....*....|....*...
gi 50289935 346 PKTAETYLHRIGRSGRFG 363
Cdd:COG0553 629 WWNPAVEEQAIDRAHRIG 646
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
50-229 |
3.81e-05 |
|
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: 44.55 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 50 GFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTL--EKIKPKLnkiqALIMVPTreLAL---QTSQVIRTLGR 124
Cdd:cd18018 9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALllRRRGPGL----TLVVSPL--IALmkdQVDALPRAIKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 125 HCgVSCMVTTGGTNLRDDILRLNEtVHVLVGTPGRVLDLASRKVADLSEC-SLFVMDEADKM--LSRDFKT---IIEQVL 198
Cdd:cd18018 83 AA-LNSSLTREERRRILEKLRAGE-VKILYVSPERLVNESFRELLRQTPPiSLLVVDEAHCIseWSHNFRPdylRLCRVL 160
|
170 180 190
....*....|....*....|....*....|.
gi 50289935 199 TFLPKAHQSLLFSATFPLTVKEFMVKHLHKP 229
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVEDIASHLGIP 191
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
299-364 |
5.85e-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: 43.49 E-value: 5.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50289935 299 HARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYLHRI-GRSGRFGH 364
Cdd:cd18811 68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGRGDH 134
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
47-360 |
1.61e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 44.49 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 47 FEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKT-AAF--VIPTLEKI--KPKL-NKIQALIMVPTRELA-------L 113
Cdd:PRK13767 26 FKEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFlaIIDELFRLgrEGELeDKVYCLYVSPLRALNndihrnlE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 114 QTSQVIRTLGRHCGVSC-----MVTTGGTNLRDDILRLNETVHVLVGTPGRV-LDLASRKVAD-LSECSLFVMDE----A 182
Cdd:PRK13767 106 EPLTEIREIAKERGEELpeirvAIRTGDTSSYEKQKMLKKPPHILITTPESLaILLNSPKFREkLRTVKWVIVDEihslA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 183 DK------MLSrdfktiIEQVLTFLPKAHQSLLFSATF-PL-TVKEFMV----KHLHKPYEI---NLMEELTLKGITQ-- 245
Cdd:PRK13767 186 ENkrgvhlSLS------LERLEELAGGEFVRIGLSATIePLeEVAKFLVgyedDGEPRDCEIvdaRFVKPFDIKVISPvd 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 246 --YYAFVEERQK-----LHCL-----NTLfsklqinqaiIFCNS---TNRVELLAKKITDLGYS-----CYysHARMKQQ 305
Cdd:PRK13767 260 dlIHTPAEEISEalyetLHELikehrTTL----------IFTNTrsgAERVLYNLRKRFPEEYDednigAH--HSSLSRE 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 50289935 306 DRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYLHRIGRSG 360
Cdd:PRK13767 328 VRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
47-360 |
1.66e-04 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 44.32 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 47 FEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKT-AAFViPTL-----EKIKPKL-NKIQALIMVPTRELA------L 113
Cdd:COG1201 18 FAARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFL-PALdelarRPRPGELpDGLRVLYISPLKALAndiernL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 114 QTsqVIRTLGRHCGVSC-----MVTTGGT--NLRDDILRlnETVHVLVGTPgrvldlasrkvadlsEcSLFVM---DEAD 183
Cdd:COG1201 97 RA--PLEEIGEAAGLPLpeirvGVRTGDTpaSERQRQRR--RPPHILITTP---------------E-SLALLltsPDAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 184 KMLsRDFKTII--------------------EQVLTFLPKAHQSLLFSATF-PL-TVKEFMVKH------------LHKP 229
Cdd:COG1201 157 ELL-RGVRTVIvdeihalagskrgvhlalslERLRALAPRPLQRIGLSATVgPLeEVARFLVGYedprpvtivdagAGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 230 YEI-------NLMEELTLKGITqyYAFVEERqkLHCLntlfsklqINQA---IIFCNSTNRVELLAKKITDLgYSCYYSH 299
Cdd:COG1201 236 PDLevlvpveDLIERFPWAGHL--WPHLYPR--VLDL--------IEAHrttLVFTNTRSQAERLFQRLNEL-NPEDALP 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 300 ARM------KQQdRNKVFHDFRQGKVRTLVCS---DLltrGIDIQAVNVVINFDFPKTAETYLHRIGRSG 360
Cdd:COG1201 303 IAAhhgslsREQ-RLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
282-361 |
2.33e-04 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 41.85 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 282 ELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFD-----FPKTAETYLHRI 356
Cdd:cd18790 41 EDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSETSLIQTI 120
|
....*
gi 50289935 357 GRSGR 361
Cdd:cd18790 121 GRAAR 125
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
56-363 |
2.78e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 43.73 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 56 PIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEK------IKPKLNKIQALIMVptrelALQTSqvirtlgrhcgVS 129
Cdd:PLN03137 463 PNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICpgitlvISPLVSLIQDQIMN-----LLQAN-----------IP 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 130 CMVTTGGT--NLRDDILRLNETVH----VLVGTPGRVL--DLASRKVADLSECSL---FVMDEAD--KMLSRDFKT---- 192
Cdd:PLN03137 527 AASLSAGMewAEQLEILQELSSEYskykLLYVTPEKVAksDSLLRHLENLNSRGLlarFVIDEAHcvSQWGHDFRPdyqg 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 193 --IIEQVLTFLPkahqSLLFSATFPLTVKEFMVKHLHKPYEINLMEELTLKGItqYYAFVEERQKlhCLNTLFSKLQINQ 270
Cdd:PLN03137 607 lgILKQKFPNIP----VLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNL--WYSVVPKTKK--CLEDIDKFIKENH 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 271 ----AIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFP 346
Cdd:PLN03137 679 fdecGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLP 758
|
330
....*....|....*..
gi 50289935 347 KTAETYLHRIGRSGRFG 363
Cdd:PLN03137 759 KSIEGYHQECGRAGRDG 775
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
279-364 |
3.20e-04 |
|
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: 43.50 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 279 NRVE---LLAKKITDL--GYSCYYSHARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYL 353
Cdd:TIGR00580 668 NRIEsieKLATQLRELvpEARIAIAHGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIERADKFGLAQL 747
|
90
....*....|....*
gi 50289935 354 H----RIGRSGRFGH 364
Cdd:TIGR00580 748 YqlrgRVGRSKKKAY 762
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
50-227 |
4.08e-04 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 41.75 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 50 GFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLekIKPKLnkiqALIMVPTreLALQTSQVIRtLGRHcGVS 129
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL--LLDGV----TLVVSPL--ISLMQDQVDR-LQQL-GIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 130 CMVTTGGT-----NLRDDILRLNETVHVLVgTP-----GRVLDLASRKVAdLSECSLFVMDEAdKMLS---RDFK---TI 193
Cdd:cd17920 79 AAALNSTLspeekREVLLRIKNGQYKLLYV-TPerllsPDFLELLQRLPE-RKRLALIVVDEA-HCVSqwgHDFRpdyLR 155
|
170 180 190
....*....|....*....|....*....|....
gi 50289935 194 IEQVLTFLPKaHQSLLFSATFPLTVKEFMVKHLH 227
Cdd:cd17920 156 LGRLRRALPG-VPILALTATATPEVREDILKRLG 188
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
53-185 |
4.63e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 41.25 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 53 KPSPIQEEAI---------PVAitgRDILARAKNGTGKTAAFVIPTLEKIKpklNKIQALIMVPTRELALQTSQVIRTlg 123
Cdd:cd17918 15 SLTKDQAQAIkdiekdlhsPEP---MDRLLSGDVGSGKTLVALGAALLAYK---NGKQVAILVPTEILAHQHYEEARK-- 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50289935 124 RHCGVSCMVTTGGTnlRDDILrlnETVHVLVGTPGRVLDLASRKVADLSecslfVMDEADKM 185
Cdd:cd17918 87 FLPFINVELVTGGT--KAQIL---SGISLLVGTHALLHLDVKFKNLDLV-----IVDEQHRF 138
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
53-182 |
4.81e-04 |
|
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: 41.26 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 53 KPSPIQEEAIPVAITGRDILARAKNGTGKT--AAFVIPTLEKIKPKLNKIQALIMVPTRELALQTSQVIRTLGRHCGVSC 130
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTfvAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 50289935 131 MVTTGGTNLRDDILRLNETVHVLVGTPGRVL-DLASRKVADLSECSLFVMDEA 182
Cdd:cd17927 82 TGLSGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDEC 134
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
299-360 |
1.58e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 41.45 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50289935 299 HARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYLHRIGRSG 360
Cdd:PRK09751 308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
175-387 |
1.76e-03 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 40.49 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 175 SLFVMDEADKMLSrDFKTIIEQVLTFLPKAHQS-LLFSATFPLTVKEFMVKHLhkPYEINlmEELTLKGITQYYAFVEER 253
Cdd:cd09639 125 SLLIFDEVHFYDE-YTLALILAVLEVLKDNDVPiLLMSATLPKFLKEYAEKIG--YVEEN--EPLDLKPNERAPFIKIES 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50289935 254 QKLHCLNTLFSKLQI----NQAIIFCNSTNRVELLAKKITDLGYSCYYS--HARMKQQDRNK----VFHDFRQGKVRTLV 323
Cdd:cd09639 200 DKVGEISSLERLLEFikkgGSVAIIVNTVDRAQEFYQQLKEKGPEEEIMliHSRFTEKDRAKkeaeLLLEFKKSEKFVIV 279
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50289935 324 CSDLLTRGIDIqAVNVVINfdFPKTAETYLHRIGRSGRFGHlglainlinwNDRFNLYKIEQEL 387
Cdd:cd09639 280 ATQVIEASLDI-SVDVMIT--ELAPIDSLIQRLGRLHRYGE----------KNGEEVYIITDAP 330
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
299-368 |
3.78e-03 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 40.11 E-value: 3.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50289935 299 HARMKQQDRNKVFHDFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYLHRI-GRSGRFGHLGLA 368
Cdd:PRK10689 842 HGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLrGRVGRSHHQAYA 912
|
|
| |
