|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-385 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 611.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 1 MKFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFD-NHNIQALVVSPTR 79
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 80 ELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMG 159
Cdd:COG0513 82 ELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 160 FLEDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHVKIKSKEMTADTVDQYYVKAKEFEKFDIMTRLFDVQAP 239
Cdd:COG0513 162 FIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 240 ELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNYDIPQD 319
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489737963 320 PDSYVHRIGRTGRAGHKGVSLTFVTPNEMEYLRVIEKLTKKRMLPLKPPTESEAFAGQLAAAEANV 385
Cdd:COG0513 322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKI 387
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-381 |
2.95e-145 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 425.37 E-value: 2.95e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 1 MKFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRE 80
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 81 LAIQTQEEIFRLGkdeRA----KVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEML 156
Cdd:PRK11776 84 LADQVAKEIRRLA---RFipniKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 157 NMGFLEDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHVKIKSKEmTADTVDQYYVKAKEFEKFDIMTRLFDV 236
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH-DLPAIEQRFYEVSPDERLPALQRLLLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 237 QAPELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNYDI 316
Cdd:PRK11776 240 HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489737963 317 PQDPDSYVHRIGRTGRAGHKGVSLTFVTPNEMEYLRVIEKLTKKRMLPLKPPTESEAFAGQLAAA 381
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPE 384
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-418 |
4.22e-129 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 389.98 E-value: 4.22e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 1 MKFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRE 80
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 81 LAIQTQEEIFRLGKDERaKVQVV--YGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNM 158
Cdd:PRK11634 86 LAVQVAEAMTDFSKHMR-GVNVValYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 159 GFLEDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHVKIKSKEMTADTVDQYYVKAKEFEKFDIMTRLFDVQA 238
Cdd:PRK11634 165 GFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 239 PELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNYDIPQ 318
Cdd:PRK11634 245 FDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 319 DPDSYVHRIGRTGRAGHKGVSLTFVTPNEMEYLRVIEKLTKKRMLPLKPPTESEAFAGQLAAAEANVDSLVAKTSTEKYA 398
Cdd:PRK11634 325 DSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLEKFAAKVQQQLESSDLDQYR 404
|
410 420
....*....|....*....|....*
gi 489737963 399 D-----QAAELLQKYDATDLVAALL 418
Cdd:PRK11634 405 AllakiQPTAEGEELDLETLAAALL 429
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-203 |
2.89e-108 |
|
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: 320.93 E-value: 2.89e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHN----IQALVVSPTRELAIQTQE 87
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKkgrgPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 88 EIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLEDIESI 167
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 489737963 168 IKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHVK 203
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
3-356 |
1.44e-104 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 319.08 E-value: 1.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 3 FTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRELA 82
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 83 IQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLE 162
Cdd:PTZ00424 110 QQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 163 DIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHVKIKSKEMTADTVDQYYVKA-KEFEKFDIMTRLFDVQAPEL 241
Cdd:PTZ00424 190 QIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETLTITQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 242 TIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNYDIPQDPD 321
Cdd:PTZ00424 270 AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPE 349
|
330 340 350
....*....|....*....|....*....|....*
gi 489737963 322 SYVHRIGRTGRAGHKGVSLTFVTPNEMEYLRVIEK 356
Cdd:PTZ00424 350 NYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
1-367 |
1.51e-101 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 312.65 E-value: 1.51e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 1 MKFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRL-DF---DNHNIQALVVS 76
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLlDFprrKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 77 PTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEML 156
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 157 NMGFLEDIESIIKQVPDERQTMLFSATMPPE-IKRIGVQFMKEPHHVKIKSKEMTADTVDQYYVKAKEFE-KFDIMTRLF 234
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEhKTALLCHLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 235 DVQAPELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNY 314
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489737963 315 DIPQDPDSYVHRIGRTGRAGHKGVSLTFVTPNEMEYLRVIEKLTKKrmlPLKP 367
Cdd:PRK11192 321 DMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEE---PLKA 370
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
2-342 |
4.92e-101 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 310.75 E-value: 4.92e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 2 KFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRL----DFDNHNI---QALV 74
Cdd:PRK04837 9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshpAPEDRKVnqpRALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 75 VSPTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADE 154
Cdd:PRK04837 89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 155 MLNMGFLEDIESIIKQVPD--ERQTMLFSATMPPEIKRIGVQFMKEPHHVKIKSKEMTADTVDQYYVKAKEFEKFDIMTR 232
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 233 LFDVQAPELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVY 312
Cdd:PRK04837 249 LIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVF 328
|
330 340 350
....*....|....*....|....*....|
gi 489737963 313 NYDIPQDPDSYVHRIGRTGRAGHKGVSLTF 342
Cdd:PRK04837 329 NYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-360 |
7.95e-100 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 308.66 E-value: 7.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 1 MKFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHN------IQALV 74
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 75 VSPTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADE 154
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 155 MLNMGFLEDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHVKIKSKEMTADTVDQYYVKAKEFEKFDIMTRLF 234
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 235 DVQAPELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNY 314
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489737963 315 DIPQDPDSYVHRIGRTGRAGHKGVSLTFVTPNEMEYLRVIEKLTKK 360
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKK 366
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
2-370 |
2.64e-96 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 300.29 E-value: 2.64e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 2 KFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRL-------DFDNHNIQALV 74
Cdd:PRK01297 88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtpppkERYMGEPRALI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 75 VSPTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQN-PQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEAD 153
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 154 EMLNMGFLEDIESIIKQVP--DERQTMLFSATMPPEIKRIGVQFMKEPHHVKIKSKEMTADTVDQY-YVKAKEfEKFDIM 230
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHvYAVAGS-DKYKLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 231 TRLFDVQAPELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTH 310
Cdd:PRK01297 327 YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 311 VYNYDIPQDPDSYVHRIGRTGRAGHKGVSLTFVTPNEMEYLRVIEKLTKKRMLPLKPPTE 370
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAE 466
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
2-371 |
1.36e-94 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 298.23 E-value: 1.36e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 2 KFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPIL------QRLDFDNHNIqALVV 75
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIvhinaqPLLRYGDGPI-VLVL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 76 SPTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEM 155
Cdd:PTZ00110 210 APTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 156 LNMGFLEDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKE-PHHVKIKSKEMTA-DTVDQYYVKAKEFEKF----DI 229
Cdd:PTZ00110 290 LDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQEVFVVEEHEKRgklkML 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 230 MTRLFdVQAPELtIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVT 309
Cdd:PTZ00110 370 LQRIM-RDGDKI-LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVK 447
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489737963 310 HVYNYDIPQDPDSYVHRIGRTGRAGHKGVSLTFVTPNEMEYLRVIEKLTKKRMLPLKPPTES 371
Cdd:PTZ00110 448 YVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEK 509
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-403 |
3.03e-91 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 290.31 E-value: 3.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 1 MKFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRL-------DFDNHNIQAL 73
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 74 VVSPTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHV-KMLVLDEA 152
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHAcEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 153 DEMLNMGFLEDIESIIKQVPDE--RQTMLFSATMPPEIKRIGVQFMKEPHHVKIKSKEMTADTVDQYYVKAKEFEKFDIM 230
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 231 TRLFDVQAPELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTH 310
Cdd:PRK04537 249 LGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 311 VYNYDIPQDPDSYVHRIGRTGRAGHKGVSLTFVT-------PNEMEYLRV---IEKLTKKRMLPLkPPTESEAFAGQLAA 380
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACeryamslPDIEAYIEQkipVEPVTAELLTPL-PRPPRVPVEGEEAD 407
|
410 420
....*....|....*....|...
gi 489737963 381 AEANvDSlVAKTSTEKYADQAAE 403
Cdd:PRK04537 408 DEAG-DS-VGTIFREAREQRAAE 428
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
3-199 |
2.02e-75 |
|
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: 236.74 E-value: 2.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 3 FTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRELA 82
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 83 IQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIR---RGTVKLDHVKMLVLDEADEMLNMG 159
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489737963 160 FLEDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEP 199
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
3-197 |
2.05e-75 |
|
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: 237.39 E-value: 2.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 3 FTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNI----------QA 72
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 73 LVVSPTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEA 152
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489737963 153 DEMLNMGFLEDIESIIKQ----VPDERQTMLFSATMPPEIKRIGVQFMK 197
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLK 210
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
3-205 |
2.27e-73 |
|
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: 231.44 E-value: 2.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 3 FTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRELA 82
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 83 IQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGT-VKLDHVKMLVLDEADEMLNMGFL 161
Cdd:cd17954 82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLNMDFE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489737963 162 EDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPhhVKIK 205
Cdd:cd17954 162 PEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP--VKIE 203
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
1-343 |
2.85e-72 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 238.92 E-value: 2.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 1 MKFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDF-------DNHNIQAL 73
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTirsghpsEQRNPLAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 74 VVSPTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEAD 153
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 154 EMLNMGFLEDIESIIKQVPdERQTMLFSATMPPEIKRIGVQFMKEPHHVKIKSKEMTADTVDQY--YVKAKEFEK--FDI 229
Cdd:PLN00206 281 CMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLaiWVETKQKKQklFDI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 230 MTRLFDVQAPelTIVFGRTKRRVDELSKGLE-ARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGV 308
Cdd:PLN00206 360 LKSKQHFKPP--AVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRV 437
|
330 340 350
....*....|....*....|....*....|....*
gi 489737963 309 THVYNYDIPQDPDSYVHRIGRTGRAGHKGVSLTFV 343
Cdd:PLN00206 438 RQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
25-191 |
2.02e-71 |
|
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: 225.20 E-value: 2.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 25 TPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRELAIQTQEEIFRLGKDERAKVQVVY 104
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 105 GGADIRRQIRNLKqNPQVIVGTPGRLLDHIRRgTVKLDHVKMLVLDEADEMLNMGFLEDIESIIKQVPDERQTMLFSATM 184
Cdd:pfam00270 81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 489737963 185 PPEIKRI 191
Cdd:pfam00270 159 PRNLEDL 165
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
5-204 |
2.22e-71 |
|
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: 226.44 E-value: 2.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 5 ELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRELAIQ 84
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 85 TQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLEDI 164
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489737963 165 ESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPhhVKI 204
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDP--VRI 198
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
8-200 |
8.34e-69 |
|
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: 220.15 E-value: 8.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 8 LSDSLLKAVNRAGYEEATPIQAETIPMVLE-GKDVIGQAQTGTGKTAAFALPILQRL-----DFDNHNIQALVVSPTREL 81
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 82 AIQTQEEIFRL-GKDERAKVQVVYGGADIRRQIRNL-KQNPQVIVGTPGRLLDHIR--RGTVKLDHVKMLVLDEADEMLN 157
Cdd:cd17964 81 ALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489737963 158 MGFLEDIESIIKQVP----DERQTMLFSATMPPEIKRIGVQFMKEPH 200
Cdd:cd17964 161 MGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLKKDY 207
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
12-203 |
3.15e-68 |
|
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: 217.89 E-value: 3.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRL---DFDNHNIQALVVSPTRELAIQTQEE 88
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 89 IFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRG-TVKLDHVKMLVLDEADEMLNMGFLEDIESI 167
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 489737963 168 IKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHVK 203
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
3-199 |
2.68e-67 |
|
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: 215.62 E-value: 2.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 3 FTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRELA 82
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 83 IQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLE 162
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 489737963 163 DIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEP 199
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-198 |
9.68e-67 |
|
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: 216.37 E-value: 9.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 1 MKFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRL--------DFDN-HNIQ 71
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegltasSFSEvQEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 72 ALVVSPTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDE 151
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489737963 152 ADEMLNMGFLEDIESIIKQ--VPD--ERQTMLFSATMPPEIKRIGVQFMKE 198
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEpgMPSkeDRQTLMFSATFPEEIQRLAAEFLKE 253
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
3-185 |
5.33e-62 |
|
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: 202.15 E-value: 5.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 3 FTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDfdNH----NIQALVVSPT 78
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLK--AHsptvGARALILSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 79 RELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNM 158
Cdd:cd17959 81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
|
170 180
....*....|....*....|....*..
gi 489737963 159 GFLEDIESIIKQVPDERQTMLFSATMP 185
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLP 187
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
3-199 |
1.03e-61 |
|
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: 201.14 E-value: 1.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 3 FTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRELA 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 83 IQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLE 162
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 489737963 163 DIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEP 199
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
214-343 |
1.00e-60 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 195.80 E-value: 1.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 214 VDQYYVKAKEFEKFD-IMTRLFDVQAPELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDI 292
Cdd:cd18787 1 IKQLYVVVEEEEKKLlLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489737963 293 LVATDVAARGLDVSGVTHVYNYDIPQDPDSYVHRIGRTGRAGHKGVSLTFV 343
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
3-199 |
1.54e-59 |
|
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: 195.64 E-value: 1.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 3 FTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRELA 82
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 83 IQTQEEIFRLGKD-ERAKVQVVYGGADIRRQIRNLKQN-PQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEM---LN 157
Cdd:cd17950 84 FQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleqLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489737963 158 MgfLEDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEP 199
Cdd:cd17950 164 M--RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDP 203
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
16-217 |
1.58e-59 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 195.40 E-value: 1.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 16 VNRAGYEEATPIQAETIPMVLEG-KDVIGQAQTGTGKTAAFALPILQRLDfDNHNIQALVVSPTRELAIQTQEEIFRLGK 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 95 DERAKVQVVYGGADIRRQIRNL-KQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLEDIESIIKQVPD 173
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489737963 174 ERQTMLFSATMPPEIKRIGVQFMKEPhhVKIKSKEMTADTVDQY 217
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
12-202 |
5.07e-59 |
|
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: 194.12 E-value: 5.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPIL------QRLDFDNHNIqALVVSPTRELAIQT 85
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaqPPLERGDGPI-VLVLAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 86 QEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLEDIE 165
Cdd:cd17966 80 QQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 489737963 166 SIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHV 202
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
12-203 |
8.09e-58 |
|
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: 190.86 E-value: 8.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRL-----DFDNHNIQALVVSPTRELAIQTQ 86
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 87 EEIFRLGKDERAKV--QVVYGGADIRRQIRNLKQN-PQVIVGTPGRLLDHIRRGT--VKLDHVKMLVLDEADEMLNMGFL 161
Cdd:cd17960 81 EVLQSFLEHHLPKLkcQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489737963 162 EDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHVK 203
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
12-202 |
1.08e-57 |
|
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: 190.70 E-value: 1.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLdFDNHNIQ------ALVVSPTRELAIQT 85
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI-MDQRELEkgegpiAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 86 QEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLEDIE 165
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 489737963 166 SIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHV 202
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
12-202 |
1.49e-57 |
|
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: 190.99 E-value: 1.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLD----FDNHNIQ----ALVVSPTRELAI 83
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlppLDEETKDdgpyALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 84 QTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLED 163
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489737963 164 IESIIKQVPDE--------------------RQTMLFSATMPPEIKRIGVQFMKEPHHV 202
Cdd:cd17945 161 VTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
8-205 |
1.58e-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: 190.09 E-value: 1.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 8 LSDSLLKAVNRAGYEEATPIQAETIPMVLEG--KDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRELAIQT 85
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 86 QEEIFRLGKDERAKVQVVYGGADIRRQiRNLKQnpQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNM-GFLEDI 164
Cdd:cd17963 81 GEVVEKMGKFTGVKVALAVPGNDVPRG-KKITA--QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489737963 165 ESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPhhVKIK 205
Cdd:cd17963 158 IRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNA--NTIK 196
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
2-198 |
1.12e-56 |
|
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: 189.87 E-value: 1.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 2 KFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRL----DFDNHNIQ------ 71
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgPGESLPSEsgyygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 72 ------ALVVSPTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVK 145
Cdd:cd18051 102 rkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489737963 146 MLVLDEADEMLNMGFLEDIESIIKQ----VPDERQTMLFSATMPPEIKRIGVQFMKE 198
Cdd:cd18051 182 YLVLDEADRMLDMGFEPQIRRIVEQdtmpPTGERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
8-199 |
8.21e-56 |
|
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: 185.87 E-value: 8.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 8 LSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRL------DFDNHNIQALVVSPTREL 81
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 82 AIQTQEEIFRLGKDERAKVQVV--YGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKL-DHVKMLVLDEADEMLNM 158
Cdd:cd17961 81 AQQVSKVLEQLTAYCRKDVRVVnlSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489737963 159 GFLEDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEP 199
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
12-203 |
4.17e-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: 183.62 E-value: 4.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRELAIQTQEEIFR 91
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 92 LG-KDERAKVQVVYGGADIRRQIRNLKQnPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLEDIESIIKQ 170
Cdd:cd17943 81 IGkKLEGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|...
gi 489737963 171 VPDERQTMLFSATMPPEIKRIGVQFMKEPHHVK 203
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-204 |
8.80e-55 |
|
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: 182.79 E-value: 8.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRL--DFDNHNIQALVVSPTRELAIQTQEEI 89
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 90 FRLGKDERAKVQVVYGG-ADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLEDIESII 168
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 489737963 169 KQVPDER-QTMLFSATMPPEIKRIGVQFMKEPHHVKI 204
Cdd:cd17957 161 AACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
2-199 |
3.12e-54 |
|
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: 182.19 E-value: 3.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 2 KFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPIL-----QRLDFDNHNIQALVVS 76
Cdd:cd17953 13 KWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhikdQRPVKPGEGPIGLIMA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 77 PTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHI----RRGTvKLDHVKMLVLDEA 152
Cdd:cd17953 93 PTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtannGRVT-NLRRVTYVVLDEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489737963 153 DEMLNMGFLEDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEP 199
Cdd:cd17953 172 DRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
3-199 |
4.73e-54 |
|
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: 181.13 E-value: 4.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 3 FTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRELA 82
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 83 IQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLE 162
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 489737963 163 DIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEP 199
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDP 197
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
3-199 |
1.25e-53 |
|
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: 180.21 E-value: 1.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 3 FTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRldfdnhnIQALVVSPTRELA 82
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------VVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 83 IQTQEEIFRLGK---DERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMG 159
Cdd:cd17938 74 EQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489737963 160 FLEDIESIIKQVP-----DER-QTMLFSATM-PPEIKRIGVQFMKEP 199
Cdd:cd17938 154 NLETINRIYNRIPkitsdGKRlQVIVCSATLhSFEVKKLADKIMHFP 200
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
13-202 |
3.24e-53 |
|
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: 178.64 E-value: 3.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 13 LKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRL------DFDNhnIQALVVSPTRELAIQTQ 86
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyrerwtPEDG--LGALIISPTRELAMQIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 87 EEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNpQVIVGTPGRLLDHIRRgTVKLD--HVKMLVLDEADEMLNMGFLEDI 164
Cdd:cd17941 80 EVLRKVGKYHSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLQHMDE-TPGFDtsNLQMLVLDEADRILDMGFKETL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 489737963 165 ESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHV 202
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
12-199 |
3.80e-53 |
|
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: 178.51 E-value: 3.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRELAIQTQEEIFR 91
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 92 LGKDE-RAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLEDIESIIKQ 170
Cdd:cd17962 81 LMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180
....*....|....*....|....*....
gi 489737963 171 VPDERQTMLFSATMPPEIKRIGVQFMKEP 199
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNP 189
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
12-220 |
1.36e-50 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 173.19 E-value: 1.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPM-VLEGKDVIGQAQTGTGKTAAFALPILQRL-----DFDNHNIQ----ALVVSPTREL 81
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLlsqksSNGVGGKQkplrALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 82 AIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRG---TVKLDHVKMLVLDEADEMLNM 158
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489737963 159 GFLEDIESIIKQVPDE-------RQTMLFSATMppeikrIGVQFMKEPHHVKIKSKEMTADTVDQYYVK 220
Cdd:cd17946 161 GHFAELEKILELLNKDragkkrkRQTFVFSATL------TLDHQLPLKLNSKKKKKKKEKKQKLELLIE 223
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
1-204 |
2.28e-48 |
|
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: 167.11 E-value: 2.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 1 MKFTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLdfdNHN--IQ------A 72
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI---NHQpfLErgdgpiC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 73 LVVSPTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEA 152
Cdd:cd18049 101 LVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489737963 153 DEMLNMGFLEDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHVKI 204
Cdd:cd18049 181 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
12-202 |
4.40e-48 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 165.33 E-value: 4.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFD-NHNIQ-----ALVVSPTRELAIQT 85
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQpIPREQrngpgVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 86 QEEIFRLgKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLEDIE 165
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 489737963 166 SIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHV 202
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
13-202 |
7.73e-46 |
|
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: 159.45 E-value: 7.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 13 LKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALP---ILQRLDFDNHN-IQALVVSPTRELAIQTQEE 88
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKFKPRNgTGVIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 89 IFRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDH-VKMLVLDEADEMLNMGFLEDIESI 167
Cdd:cd17942 82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGFEEEMRQI 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 489737963 168 IKQVPDERQTMLFSATMPPEIKRIG-VQFMKEPHHV 202
Cdd:cd17942 162 IKLLPKRRQTMLFSATQTRKVEDLArISLKKKPLYV 197
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
21-204 |
1.02e-43 |
|
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: 155.94 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 21 YEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQA-----LVVSPTRELAIQTQEEIFRLGKD 95
Cdd:cd18050 82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLVLAPTRELAQQVQQVADDYGKS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 96 ERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLEDIESIIKQVPDER 175
Cdd:cd18050 162 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 241
|
170 180
....*....|....*....|....*....
gi 489737963 176 QTMLFSATMPPEIKRIGVQFMKEPHHVKI 204
Cdd:cd18050 242 QTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
16-192 |
1.92e-43 |
|
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: 153.51 E-value: 1.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 16 VNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQ------ALVVSPTRELAIQTQEEI 89
Cdd:cd17949 6 KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 90 FRLGKDERAKVQ-VVYGG-------ADIRRQIrnlkqnpQVIVGTPGRLLDHIRRgTVKLDH--VKMLVLDEADEMLNMG 159
Cdd:cd17949 86 EKLLKPFHWIVPgYLIGGekrksekARLRKGV-------NILIATPGRLLDHLKN-TQSFDVsnLRWLVLDEADRLLDMG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489737963 160 FLEDIESIIKQVPDE-------------RQTMLFSATMPPEIKRIG 192
Cdd:cd17949 158 FEKDITKILELLDDKrskaggekskpsrRQTVLVSATLTDGVKRLA 203
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
12-189 |
9.64e-43 |
|
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: 151.34 E-value: 9.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPIL-------QRLDF-DNHNIQALVVSPTRELAI 83
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqeKKLPFiKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 84 QTQEEI------FRLGKDERAKVQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLN 157
Cdd:cd17951 81 QTHEVIeyyckaLQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190
....*....|....*....|....*....|..
gi 489737963 158 MGFLEDIESIIKQVPDERQTMLFSATMPPEIK 189
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQ 192
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
26-197 |
1.80e-41 |
|
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: 147.69 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 26 PIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNI------QALVVSPTRELAIQTQEEIFRLGKdeRAK 99
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 100 VQVVYGGADIRRQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLEDIESII-----KQVPDE 174
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsykKDSEDN 172
|
170 180
....*....|....*....|...
gi 489737963 175 RQTMLFSATMPPEIKRIGVQFMK 197
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYMK 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
225-334 |
6.02e-35 |
|
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: 126.94 E-value: 6.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 225 EKFDIMTRLFDVQAPELTIVFGRTKRRVDElSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLD 304
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 489737963 305 VSGVTHVYNYDIPQDPDSYVHRIGRTGRAG 334
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
3-210 |
3.89e-34 |
|
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: 128.60 E-value: 3.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 3 FTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEG--KDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRE 80
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 81 LAIQTQEEIFRLGKdERAKVQVVYGgadIR--RQIRNLKQNPQVIVGTPGRLLDH-IRRGTVKLDHVKMLVLDEADEMLN 157
Cdd:cd18048 100 LALQTGKVVEEMGK-FCVGIQVIYA---IRgnRPGKGTDIEAQIVIGTPGTVLDWcFKLRLIDVTNISVFVLDEADVMIN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489737963 158 M-GFLEDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHVKIKSKEMT 210
Cdd:cd18048 176 VqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
12-184 |
1.75e-33 |
|
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: 126.98 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEG---------KDVIGQAQTGTGKTAAFALPILQRL-DFDNHNIQALVVSPTREL 81
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 82 AIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRNLKQ--------NPQVIVGTPGRLLDHIRRGT-VKLDHVKMLVLDEA 152
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVdtsgrylsRVDILVATPGRLVDHLNSTPgFTLKHLRFLVIDEA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489737963 153 DEMLNMGF---LEDIESIIKQVPDER-----------------QTMLFSATM 184
Cdd:cd17956 161 DRLLNQSFqdwLETVMKALGRPTAPDlgsfgdanllersvrplQKLLFSATL 212
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
12-185 |
5.55e-32 |
|
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: 122.86 E-value: 5.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 12 LLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHN-------IQALVVSPTRELAIQ 84
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLaegpfnaPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 85 TQEEIFRLGKDERAKVQVVYGGaDIRRQIRNLKQ-NPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLED 163
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGG-RTKRQIRNPHFeEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190
....*....|....*....|....*....|....*
gi 489737963 164 IESIIKQVP---------DER----QTMLFSATMP 185
Cdd:cd17948 160 LSHFLRRFPlasrrsentDGLdpgtQLVLVSATMP 194
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
253-334 |
1.05e-29 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 111.53 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 253 DELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNYDIPQDPDSYVHRIGRTGR 332
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 489737963 333 AG 334
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
3-203 |
3.05e-27 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 109.04 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 3 FTELGLSDSLLKAVNRAGYEEATPIQAETIPMVLEG--KDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVVSPTRE 80
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 81 LAIQTQEEIFRLGKdERAKVQVVYGGADIRRQiRNLKQNPQVIVGTPGRLLDH-IRRGTVKLDHVKMLVLDEADEML-NM 158
Cdd:cd18047 83 LALQTGKVIEQMGK-FYPELKLAYAVRGNKLE-RGQKISEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIaTQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489737963 159 GFLEDIESIIKQVPDERQTMLFSATMPPEIKRIGVQFMKEPHHVK 203
Cdd:cd18047 161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
38-183 |
2.07e-21 |
|
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: 90.54 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 38 GKDVIGQAQTGTGKTAAFALPILQRLdfDNHNIQALVVSPTRELAIQTQEEIFRLGkDERAKVQVVYGGADIRRQIRNLK 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLL--LKKGKKVLVLVPTKALALQTAERLRELF-GPGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489737963 118 QNPQVIVGTPGRLLDHIRR-GTVKLDHVKMLVLDEADEML-NM-GFLEDIESIIKQVPDERQTMLFSAT 183
Cdd:cd00046 78 GDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLiDSrGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
11-352 |
5.57e-17 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 83.65 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 11 SLLKAVnrAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALP--ILQRLdfdnhniqALVVSP----------- 77
Cdd:COG0514 7 EVLKRV--FGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLLPGL--------TLVVSPlialmkdqvda 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 78 TRELAI--------QTQEEIfrlgkderakvqvvyggADIRRQIRN--LK---------QNPQVIvgtpgRLLDHIRrgt 138
Cdd:COG0514 77 LRAAGIraaflnssLSAEER-----------------REVLRALRAgeLKllyvaperlLNPRFL-----ELLRRLK--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 139 vkldhVKMLVLDEA--------D---EMLNMGfledieSIIKQVPDeRQTMLFSATMPPE-----IKRIGvqfMKEPHHV 202
Cdd:COG0514 132 -----ISLFAIDEAhcisqwghDfrpDYRRLG------ELRERLPN-VPVLALTATATPRvradiAEQLG---LEDPRVF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 203 KikskemtaDTVD----QYYVKAK-EFEKFDIMTRLFDVQAPELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQR 277
Cdd:COG0514 197 V--------GSFDrpnlRLEVVPKpPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 278 RTQIMRQFKAGKLDILVATdvAARGL-----DVSGVTHvynYDIPQDPDSYVHRIGRTGRAGHKGVSLTFVTPNEMEYLR 352
Cdd:COG0514 269 REANQDRFLRDEVDVIVAT--IAFGMgidkpDVRFVIH---YDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
47-437 |
3.50e-16 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 81.22 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 47 TGTGKTAAFALpILQRLDFDNHniqALVVSPTRELAIQTQEEI---------FRLGKDERAKVQVV-------------- 103
Cdd:COG1061 109 TGTGKTVLALA-LAAELLRGKR---VLVLVPRRELLEQWAEELrrflgdplaGGGKKDSDAPITVAtyqslarrahldel 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 104 -------------YGGADIRRQIRNLKQnPQVIVG---TPGRLlDHIRRGTVKLDHVkmlVLDE-ADEMLNMGFLEDIES 166
Cdd:COG1061 185 gdrfglviideahHAGAPSYRRILEAFP-AAYRLGltaTPFRS-DGREILLFLFDGI---VYEYsLKEAIEDGYLAPPEY 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 167 IIKQVPDERQTMLFSATMPPEIKRIgvqfmkephhvkIKSKEMTADTVDQYYVKAKEFEKfdimtrlfdvqapelTIVFG 246
Cdd:COG1061 260 YGIRVDLTDERAEYDALSERLREAL------------AADAERKDKILRELLREHPDDRK---------------TLVFC 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 247 RTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNYDIPQDPDSYVHR 326
Cdd:COG1061 313 SSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQR 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 327 IGR---TGRAGHKGVSLTFVTpNEMEYLRVIekLTKKRMLPLKPPTESEAFAGQLAAAEANVDSLVAKTSTEKYADQAAE 403
Cdd:COG1061 393 LGRglrPAPGKEDALVYDFVG-NDVPVLEEL--AKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEEL 469
|
410 420 430
....*....|....*....|....*....|....
gi 489737963 404 LLQKYDATDLVAALLNDLTKDDASAVPVKITPER 437
Cdd:COG1061 470 ELLEDALLLVLAELLLLELLALALELLELAKAEG 503
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-356 |
1.23e-15 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 79.55 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 1 MKFTELgLSDSLLKAVNRAGYEEATPIQAETIPM-VLEGKDVIGQAQTGTGKTAAFALPILQRLdfdNHNIQALVVSPTR 79
Cdd:COG1204 1 MKVAEL-PLEKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKAL---LNGGKALYIVPLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 80 ELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQirnLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEA----DEm 155
Cdd:COG1204 77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE---WLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 156 lNMGF-LEDIESIIKQVPDERQTMLFSATM--PPEI-----------------KRIGV------QFMKEPHHVKIKSKEM 209
Cdd:COG1204 153 -SRGPtLEVLLARLRRLNPEAQIVALSATIgnAEEIaewldaelvksdwrpvpLNEGVlydgvlRFDDGSRRSKDPTLAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 210 TADTVDQ-----YYV-KAKEFEKFdiMTRLFDVQAPELT-IVFGRTKRRVDELSKGLEARGYN-------AAGI---HGD 272
Cdd:COG1204 232 ALDLLEEggqvlVFVsSRRDAESL--AKKLADELKRRLTpEEREELEELAEELLEVSEETHTNekladclEKGVafhHAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 273 LSQQRRTQIMRQFKAGKLDILVATD-------VAARGLDVSGVTHVYNYDIPqdPDSYVHRIGRTGRAGH--KGVSLtFV 343
Cdd:COG1204 310 LPSELRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIP--VLEFKQMAGRAGRPGYdpYGEAI-LV 386
|
410
....*....|...
gi 489737963 344 TPNEMEYLRVIEK 356
Cdd:COG1204 387 AKSSDEADELFER 399
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
20-368 |
2.93e-15 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 78.60 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 20 GYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRldfdnhNIQALVVSPtrelaiqtqeeIFRLGKDERAK 99
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL------DGLTLVVSP-----------LISLMKDQVDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 100 VQVVYGGADIRRQIRNLKQNPQVIVGtpgrlldhIRRGTVKLDHVK-------------------MLVLDEADEMLNMG- 159
Cdd:PRK11057 85 LLANGVAAACLNSTQTREQQLEVMAG--------CRTGQIKLLYIAperlmmdnflehlahwnpaLLAVDEAHCISQWGh 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 160 -FLEDIESI--IKQVPDERQTMLFSATMPPEIKRIGVQF--MKEPHhVKIKSkemtADTVDQYYVKAKEFEKFDIMTRLF 234
Cdd:PRK11057 157 dFRPEYAALgqLRQRFPTLPFMALTATADDTTRQDIVRLlgLNDPL-IQISS----FDRPNIRYTLVEKFKPLDQLMRYV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 235 DVQAPELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNY 314
Cdd:PRK11057 232 QEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHF 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489737963 315 DIPQDPDSYVHRIGRTGRAGHKGVSLTFVTPNEMEYLRviekltkkRMLPLKPP 368
Cdd:PRK11057 312 DIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLR--------RCLEEKPA 357
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
7-339 |
7.24e-15 |
|
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: 77.57 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 7 GLSDSLLKAVNRAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLdFDNHNIQALVVSPTRELAiQTQ 86
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPTKALA-RDQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 87 EEIFR-LGKDERAKVQV-VYGG---ADIRRQIRnlkQNPQVIVGTP-----GRLLDHIR-RGTVK-LDHVkmlVLDEADE 154
Cdd:COG1205 118 LRRLReLAEALGLGVRVaTYDGdtpPEERRWIR---EHPDIVLTNPdmlhyGLLPHHTRwARFFRnLRYV---VIDEAHT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 155 --------MLNMgfLEDIESIIKQVPDERQTMLFSATM--PPEI--KRIGVQFmkepHHVkikskemTADTVDQYyvkAK 222
Cdd:COG1205 192 yrgvfgshVANV--LRRLRRICRHYGSDPQFILASATIgnPAEHaeRLTGRPV----TVV-------DEDGSPRG---ER 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 223 EF------EKFDIMTRLFDVQAPEL----------TIVFGRTKRRVDELSKGLEAR------GYNAAGIHGDLSQQRRTQ 280
Cdd:COG1205 256 TFvlwnppLVDDGIRRSALAEAARLladlvreglrTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERRE 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489737963 281 IMRQFKAGKLDILVAT-------DVAarGLDVsgvthVYNYDIPQDPDSYVHRIGRTGRAGHKGVS 339
Cdd:COG1205 336 IERGLRSGELLGVVSTnalelgiDIG--GLDA-----VVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
45-190 |
2.32e-14 |
|
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: 72.79 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 45 AQTGTGKTAAFALPILQRL----------------DFDNHN-IQALVVSPTRELAIQTQEEIFRLGKDERAKVQVVYGGA 107
Cdd:cd17965 68 AETGSGKTLAYLAPLLDYLkrqeqepfeeaeeeyeSAKDTGrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 108 DIRRQiRNLKQNPQ---VIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNMGFLEDIESIIKQVPDERQTMLFSATM 184
Cdd:cd17965 148 GPSYQ-RLQLAFKGridILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATI 226
|
....*.
gi 489737963 185 PPEIKR 190
Cdd:cd17965 227 PKEFDK 232
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
217-342 |
2.84e-14 |
|
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: 69.54 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 217 YYVKAKEFEKFDIMTRLFDVQAPELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVAT 296
Cdd:cd18794 8 VRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489737963 297 DVAARGLDVSGVTHVYNYDIPQDPDSYVHRIGRTGRAGHKGVSLTF 342
Cdd:cd18794 88 VAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-152 |
2.75e-11 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 62.60 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 28 QAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLdFDNHNIQALVVSPTRELAiQTQEEIFR---LGKDERAKVQVVY 104
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALA-QDQLRSLRellEQLGLGIRVATYD 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489737963 105 GGADIRRQIRNLKQNPQVIVGTPGRL----LDHIRRGTVKLDHVKMLVLDEA 152
Cdd:cd17923 83 GDTPREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
25-185 |
2.67e-10 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 59.58 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 25 TPIQAETI-PMVLEGKDVIGQAQTGTGKTAAFALPILQRLdfDNHNIQALVVSPTRELAIQTQEEIFRLGKDERAKVQVV 103
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRAL--ATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 104 YGGADIRRQirnLKQNPQVIVGTPGRLLDHIRRG-TVKLDHVKMLVLDEAdEMLNMG----FLEDIESIIKQVPDERQTM 178
Cdd:cd17921 81 TGDPSVNKL---LLAEADILVATPEKLDLLLRNGgERLIQDVRLVVVDEA-HLIGDGergvVLELLLSRLLRINKNARFV 156
|
....*..
gi 489737963 179 LFSATMP 185
Cdd:cd17921 157 GLSATLP 163
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
272-333 |
6.01e-10 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 57.60 E-value: 6.01e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489737963 272 DLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNYDIPQDPDSYVHRIGRtGRA 333
Cdd:cd18802 73 LMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
242-334 |
1.44e-09 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 60.51 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 242 TIVFGRTKRRVDELSKGLEARGYNA------AGIHGD--LSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYN 313
Cdd:COG1111 356 IIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIF 435
|
90 100
....*....|....*....|....*
gi 489737963 314 YD-IPqdpdS---YVHRIGRTGRAG 334
Cdd:COG1111 436 YEpVP----SeirSIQRKGRTGRKR 456
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
254-356 |
3.32e-09 |
|
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: 55.81 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 254 ELSKGLEARgYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVynydIPQDPD----SYVHRI-G 328
Cdd:cd18811 53 YLKERFRPE-LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVM----VIEDAErfglSQLHQLrG 127
|
90 100 110
....*....|....*....|....*....|...
gi 489737963 329 RTGRAGHKGVSLtFVTPNEM-----EYLRVIEK 356
Cdd:cd18811 128 RVGRGDHQSYCL-LVYKDPLtetakQRLRVMTE 159
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
243-363 |
4.93e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 59.08 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 243 IVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGK--LDILVATDVAARGLDVSGVTHVYNYDIPQDP 320
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLWWNP 632
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489737963 321 DSY------VHRIGRTgraghKGVSLT-FVTPNEMEyLRVIEKLTKKRML 363
Cdd:COG0553 633 AVEeqaidrAHRIGQT-----RDVQVYkLVAEGTIE-EKILELLEEKRAL 676
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
243-328 |
6.48e-09 |
|
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: 54.40 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 243 IVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGK--LDILVATDVAARGLDVSGVTHVYNYDIPQDP 320
Cdd:cd18793 31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPWWNP 110
|
90
....*....|....*
gi 489737963 321 dSY-------VHRIG 328
Cdd:cd18793 111 -AVeeqaidrAHRIG 124
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
21-336 |
2.70e-08 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 56.82 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 21 YEEATPIQAETIPMVLEGKDVIGQAQTGTGKT-AAFALPI--LQRLDFDN---HNIQALVVSPTRELA-------IQTQE 87
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAIIdeLFRLGREGeleDKVYCLYVSPLRALNndihrnlEEPLT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 88 EIFRLGKDERAKVQvvyggaDIRRQIRN-----------LKQNPQVIVGTPGRL--LDHIRRGTVKLDHVKMLVLDEADE 154
Cdd:PRK13767 110 EIREIAKERGEELP------EIRVAIRTgdtssyekqkmLKKPPHILITTPESLaiLLNSPKFREKLRTVKWVIVDEIHS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 155 MLN-------MGFLEDIESIIKQVPderQTMLFSATMPP--EIKR--IGVQFMKEPHHVKIkskemtadtVDQYYVKake 223
Cdd:PRK13767 184 LAEnkrgvhlSLSLERLEELAGGEF---VRIGLSATIEPleEVAKflVGYEDDGEPRDCEI---------VDARFVK--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 224 feKFDIMT-----------------RLFD-----VQAPELTIVFGRTK----RRVDELSKGLEARgYNAAGI---HGDLS 274
Cdd:PRK13767 249 --PFDIKVispvddlihtpaeeiseALYEtlhelIKEHRTTLIFTNTRsgaeRVLYNLRKRFPEE-YDEDNIgahHSSLS 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489737963 275 QQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNYDIPQDPDSYVHRIgrtGRAGHK 336
Cdd:PRK13767 326 REVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRI---GRAGHR 384
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
38-156 |
1.42e-07 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 51.43 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 38 GKDVIGQAQTGTGKTAAFALPILQRL-DFDNHNIQALVVSPTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRQIRN- 115
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVRHGDTSQSEKAk 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489737963 116 -LKQNPQVIVGTP---GRLLDHiRRGTVKLDHVKMLVLDEADEML 156
Cdd:cd17922 81 qLKNPPGILITTPeslELLLVN-KKLRELFAGLRYVVVDEIHALL 124
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
47-152 |
1.59e-07 |
|
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: 51.88 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 47 TGTGKTAAFALPI-----LQRLDFDNHNIQALVVsPTRELAIQtQEEIFRLGKDerAKVQVVYGGADIRRQIR----NLK 117
Cdd:cd18034 25 TGSGKTLIAVMLIkemgeLNRKEKNPKKRAVFLV-PTVPLVAQ-QAEAIRSHTD--LKVGEYSGEMGVDKWTKerwkEEL 100
|
90 100 110
....*....|....*....|....*....|....*
gi 489737963 118 QNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEA 152
Cdd:cd18034 101 EKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
260-332 |
2.38e-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: 50.05 E-value: 2.38e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489737963 260 EARGYNAAGihgdLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNYDIPQDPDSYVHRIGRTGR 332
Cdd:cd18801 65 QASGKSSKG----MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
264-356 |
2.93e-07 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 50.34 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 264 YNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVynydIPQDPD----SYVHRI-GRTGRAGHKGV 338
Cdd:cd18792 61 ARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTM----IIEDADrfglSQLHQLrGRVGRGKHQSY 136
|
90 100
....*....|....*....|....*
gi 489737963 339 SLtFVTPNEM-------EYLRVIEK 356
Cdd:cd18792 137 CY-LLYPDPKkltetakKRLRAIAE 160
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
242-305 |
7.63e-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: 7.63e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489737963 242 TIVFGRTKRRVDELSKGLeargyNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDV 305
Cdd:cd18789 52 IIVFTDNVEALYRYAKRL-----LKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDL 110
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
289-344 |
9.45e-07 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 46.54 E-value: 9.45e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 489737963 289 KLDILVATDVAARGLDVSGVTHVYNYDIPQDPDSYVHRIGRTGRAGHKGVSLTFVT 344
Cdd:cd18785 22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1-335 |
2.41e-06 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 50.27 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 1 MKFTELGLSDSLLKAVNRAGYEeATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLdfdNHNIQALVVSPTRE 80
Cdd:PRK01172 1 MKISDLGYDDEFLNLFTGNDFE-LYDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETF---LAGLKSIYIVPLRS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 81 LAIQTQEEIFRLgKDERAKVQVVYGGADirrQIRNLKQNPQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEAdEMLNMGF 160
Cdd:PRK01172 77 LAMEKYEELSRL-RSLGMRVKISIGDYD---DPPDFIKRYDVVILTSEKADSLIHHDPYIINDVGLIVADEI-HIIGDED 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 161 ----LEDIESIIKQVPDERQTMLFSATMP--PEIKR------IGVQFMKEPHHVKIKSKemtadtvDQYYVKAKEFEKFD 228
Cdd:PRK01172 152 rgptLETVLSSARYVNPDARILALSATVSnaNELAQwlnaslIKSNFRPVPLKLGILYR-------KRLILDGYERSQVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 229 IMTRLFD-VQAPELTIVFGRTKRRVDELSKGL---------------EARGYNAA-------GI---HGDLSQQRRTQIM 282
Cdd:PRK01172 225 INSLIKEtVNDGGQVLVFVSSRKNAEDYAEMLiqhfpefndfkvsseNNNVYDDSlnemlphGVafhHAGLSNEQRRFIE 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489737963 283 RQFKAGKLDILVATDVAARGL----------DVS-----GVTHVYNYDIPQdpdsyvhRIGRTGRAGH 335
Cdd:PRK01172 305 EMFRNRYIKVIVATPTLAAGVnlparlvivrDITrygngGIRYLSNMEIKQ-------MIGRAGRPGY 365
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
18-190 |
2.56e-06 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 48.30 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 18 RAGYEEATPIQAETIPMVLEGKDVIGQAQTGTGKTAAFALP--ILQRLdfdnhniqALVVSPTreLAIQtQEEIFRLgkd 95
Cdd:cd17920 7 VFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV--------TLVVSPL--ISLM-QDQVDRL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 96 ERAKVQVVY----GGADIRRQIRNLKQNPQ---VIVgTPGRL-----LDHIRRGTvKLDHVKMLVLDEA--------D-- 153
Cdd:cd17920 73 QQLGIRAAAlnstLSPEEKREVLLRIKNGQyklLYV-TPERLlspdfLELLQRLP-ERKRLALIVVDEAhcvsqwghDfr 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 489737963 154 -EMLNMGFLEDiesIIKQVPderqTMLFSATMPPEIKR 190
Cdd:cd17920 151 pDYLRLGRLRR---ALPGVP----ILALTATATPEVRE 181
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
242-334 |
2.76e-06 |
|
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: 47.25 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 242 TIVFGRTKRRVDELSKGLEAR-------GYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNY 314
Cdd:cd18797 38 TIVFCRSRKLAELLLRYLKARlveegplASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117
|
90 100
....*....|....*....|
gi 489737963 315 DIPQDPDSYVHRIGRTGRAG 334
Cdd:cd18797 118 GYPGSLASLWQQAGRAGRRG 137
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
26-185 |
5.71e-06 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 46.94 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 26 PIQAETI-PMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNhniQALVVSPTRELAIQTQEEiFRlgKDERAKVQVVY 104
Cdd:cd18028 4 PPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG---KALYLVPLRALASEKYEE-FK--KLEEIGLKVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 105 GGADIRRQIRNLKQNPqVIVGTPGRLLDHIRRGTVKLDHVKMLVLDE---ADEMLNMGFLEDIESIIKQVPDERQTMLFS 181
Cdd:cd18028 78 STGDYDEDDEWLGDYD-IIVATYEKFDSLLRHSPSWLRDVGVVVVDEihlISDEERGPTLESIVARLRRLNPNTQIIGLS 156
|
....
gi 489737963 182 ATMP 185
Cdd:cd18028 157 ATIG 160
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
206-337 |
6.34e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 49.10 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 206 SKEMTAD-TVDQYYVKAKEFE----KFDIMTRL----FDVQAPELTIVFGRTKRRVDELSKGLEARGYNA------AGIH 270
Cdd:PRK13766 323 SKRLVEDpRFRKAVRKAKELDiehpKLEKLREIvkeqLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKD 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 271 GD--LSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNYD-IPQDPDSyVHRIGRTGRaGHKG 337
Cdd:PRK13766 403 GDkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEG 470
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
231-345 |
9.19e-06 |
|
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: 45.72 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 231 TRLFDVQAPELTIVFGRTKRRVDELSKGL-EARGYNAAGI-----HGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLD 304
Cdd:cd18796 30 EVIFLLERHKSTLVFTNTRSQAERLAQRLrELCPDRVPPDfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGID 109
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489737963 305 VSGVTHVYNYDIPQDPDSYVHRIGRTGRAGHkGVSLTFVTP 345
Cdd:cd18796 110 IGDVDLVIQIGSPKSVARLLQRLGRSGHRPG-AASKGRLVP 149
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1-184 |
1.30e-05 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 47.89 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 1 MKFTELGLSDSLLKAVNRAGYEEATPIQAETIPM-VLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHniQALVVSPTR 79
Cdd:PRK00254 1 MKVDELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGG--KAVYLVPLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 80 ELAiqtqEEIFRLGKD-ERAKVQVVYGGADIRRQIRNLKQNpQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEADEMLNM 158
Cdd:PRK00254 79 ALA----EEKYREFKDwEKLGLRVAMTTGDYDSTDEWLGKY-DIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSY 153
|
170 180
....*....|....*....|....*.
gi 489737963 159 GFLEDIESIIKQVPDERQTMLFSATM 184
Cdd:PRK00254 154 DRGATLEMILTHMLGRAQILGLSATV 179
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
270-388 |
4.99e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 46.46 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 270 HGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNYDIPQDPDSYVHRIgrtGRAGHK--GVSLTFVTPNE 347
Cdd:PRK09751 308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRI---GRAGHQvgGVSKGLFFPRT 384
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489737963 348 MEYL----RVIEKLTKKRMLPLKPPTESEAFAGQLAAAEANVDSL 388
Cdd:PRK09751 385 RRDLvdsaVIVECMFAGRLENLTPPHNPLDVLAQQTVAAAAMDAL 429
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
47-152 |
1.37e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 42.66 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 47 TGTGKT---AAFALPILQRLDFDNhniqALVVSPTRELAIQTQEEIFRLGKDERAKVQVVYGGADIRRqirnlKQNPQVI 123
Cdd:pfam04851 32 TGSGKTltaAKLIARLFKKGPIKK----VLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDES-----VDDNKIV 102
|
90 100 110
....*....|....*....|....*....|.
gi 489737963 124 VGTPGRLLDHIRRGTVKL--DHVKMLVLDEA 152
Cdd:pfam04851 103 VTTIQSLYKALELASLELlpDFFDVIIIDEA 133
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
44-126 |
1.48e-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: 42.79 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 44 QAQTGTGKTAAFALPILqrLDFDNHNiQALVVSPTRELAIQTQEEIFRLGKDerAKVQVVYGGAdiRRQIrnlKQNPQVI 123
Cdd:cd17918 42 SGDVGSGKTLVALGAAL--LAYKNGK-QVAILVPTEILAHQHYEEARKFLPF--INVELVTGGT--KAQI---LSGISLL 111
|
...
gi 489737963 124 VGT 126
Cdd:cd17918 112 VGT 114
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
47-152 |
1.99e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are 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: 350684 [Multi-domain] Cd Length: 146 Bit Score: 41.52 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 47 TGTGKTA-AFALPilqrldFDNHNIQALVVSPTRELAIQTQEEIFRLGKDERakVQVVYGGADIRRQIRNlkqnpqVIVG 125
Cdd:cd17926 27 TGSGKTLtALALI------AYLKELRTLIVVPTDALLDQWKERFEDFLGDSS--IGLIGGGKKKDFDDAN------VVVA 92
|
90 100
....*....|....*....|....*..
gi 489737963 126 TPGRLLDHIRRGTVKLDHVKMLVLDEA 152
Cdd:cd17926 93 TYQSLSNLAEEEKDLFDQFGLLIVDEA 119
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
236-332 |
2.74e-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: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 236 VQAPELTIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDVAARGLDVSGVTHVYNYD 315
Cdd:cd18790 24 VARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
|
90 100
....*....|....*....|..
gi 489737963 316 -----IPQDPDSYVHRIGRTGR 332
Cdd:cd18790 104 adkegFLRSETSLIQTIGRAAR 125
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
251-298 |
3.37e-04 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 43.50 E-value: 3.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 489737963 251 RVDELSKGLeaRGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDV 298
Cdd:COG1200 493 TYEELREAF--PGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV 538
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
45-329 |
4.70e-04 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 42.76 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 45 AQTGTGKT---AAFALPILQRldfdnHNIQALVVS-PTRELAIQTQEEIFRLGKDErakVQVVYGGADI----------- 109
Cdd:COG1203 154 APTGGGKTeaaLLFALRLAAK-----HGGRRIIYAlPFTSIINQTYDRLRDLFGED---VLLHHSLADLdlleeeeeyes 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 110 -RRQIRNLKQN---PqVIVGTPGRLLDHI----RRGTVKLdHV---KMLVLDEAD----EMLNM--GFLEDIE----SII 168
Cdd:COG1203 226 eARWLKLLKELwdaP-VVVTTIDQLFESLfsnrKGQERRL-HNlanSVIILDEVQayppYMLALllRLLEWLKnlggSVI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 169 kqvpderqtmLFSATMPPEIKRIGVQFMK----EPHHVKIKSKEMTADTVDqyyVKAKEFEKFDIMTRLFDVQAPE---L 241
Cdd:COG1203 304 ----------LMTATLPPLLREELLEAYElipdEPEELPEYFRAFVRKRVE---LKEGPLSDEELAELILEALHKGksvL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 242 TIVfgRTKRRVDELSKGLEARGyNAAGI---HGDLSQQRRT----QIMRQFKAGKLDILVATDVAARGLDVSgvthvynY 314
Cdd:COG1203 371 VIV--NTVKDAQELYEALKEKL-PDEEVyllHSRFCPADRSeiekEIKERLERGKPCILVSTQVVEAGVDID-------F 440
|
330
....*....|....*....
gi 489737963 315 DI----PQDPDSYVHRIGR 329
Cdd:COG1203 441 DVvirdLAPLDSLIQRAGR 459
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
27-85 |
5.49e-04 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 41.19 E-value: 5.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489737963 27 IQAETIPMVLEG-KDVIGQAQTGTGKTAAFALPILQ----RLDFDNHNIQALVVSPTRELAIQT 85
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRllkeRNPLPWGNRKVVYIAPIKALCSEK 68
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
242-305 |
7.76e-04 |
|
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: 39.46 E-value: 7.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489737963 242 TIVFGRTKRRVDELSKGLEARGYNAAGIHGDLSQQRRT--QIMRQFKA-GKLDILVATDVAARGLDV 305
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdeALILLFFGeLKPPILVTVDLLTTGVDI 75
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
253-298 |
1.73e-03 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 41.29 E-value: 1.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489737963 253 DELSKGLEarGYNAAGIHGDLSQQRRTQIMRQFKAGKLDILVATDV 298
Cdd:PRK10917 497 EELQEAFP--ELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTV 540
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
27-152 |
3.22e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 38.65 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 27 IQAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIqaLVVSPTRELAIQtQEEIFRLGKDERAKVQVVYGG 106
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLTKKGGKV--LILAPSRPLVEQ-HAENLKRVLNIPDKITSLTGE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489737963 107 ADIRRQIRNLKQNpQVIVGTPGRLLDHIRRGTVKLDHVKMLVLDEA 152
Cdd:cd18035 82 VKPEERAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
28-152 |
3.54e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 38.95 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 28 QAETIPMVLEGKDVIGQAQTGTGKTAAFALPILQRLDFDNHNIQALVV--SPTRELAIQTQEEIFRLGKDERAKVQVVYG 105
Cdd:cd17927 7 QLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGKVVflANKVPLVEQQKEVFRKHFERPGYKVTGLSG 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489737963 106 gaDIRRQIRNLK--QNPQVIVGTPGRLLDHIRRGT-VKLDHVKMLVLDEA 152
Cdd:cd17927 87 --DTSENVSVEQivESSDVIIVTPQILVNDLKSGTiVSLSDFSLLVFDEC 134
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
147-336 |
4.30e-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: 39.34 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 147 LVLDEAD--EMLNMGFLEDIESIIKQVpdERQTMLFSATMPPEIKrigvQFMKEPHHVKIKSKEMTADTVDQYYVK--AK 222
Cdd:cd09639 127 LIFDEVHfyDEYTLALILAVLEVLKDN--DVPILLMSATLPKFLK----EYAEKIGYVEENEPLDLKPNERAPFIKieSD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737963 223 EFEKFDIMTRLFD-VQAPELTIVFGRTKRRVDELSKGLEARG--YNAAGIHGDLSQQRR----TQIMRQFKAGKLDILVA 295
Cdd:cd09639 201 KVGEISSLERLLEfIKKGGSVAIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVA 280
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489737963 296 TDVAARGLDVSgvthvynYDI----PQDPDSYVHRIGRTGRAGHK 336
Cdd:cd09639 281 TQVIEASLDIS-------VDVmiteLAPIDSLIQRLGRLHRYGEK 318
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
468-521 |
6.04e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 39.50 E-value: 6.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 489737963 468 GRGGYSHNGRNRDRDRNGGRGDRKSNGYKGRSRDDNRSSNRNHDEGRKQSSKRS 521
Cdd:PRK12678 183 AEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRR 236
|
|
| |
