|
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: 600.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 1 MKFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEA-TIQALVIAPTR 79
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPrAPQALILAPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 80 ELAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMG 159
Cdd:COG0513 82 ELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 160 FLEDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHVKIAAKELTTELVDQYYIRVKEQEKFDTMTRLMDVDQP 239
Cdd:COG0513 162 FIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 240 ELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVYNYDIPQD 319
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343391197 320 PESYVHRIGRTGRAGKSGQSITFVSPNEMGYLQIIENLTKKRMKGLKPASAEEAFQAKKQVALKKI 385
Cdd:COG0513 322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKI 387
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-371 |
7.55e-147 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 429.22 E-value: 7.55e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 1 MKFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRE 80
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 81 LAVQSQEELFRFGRSK-GVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMG 159
Cdd:PRK11776 84 LADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 160 FLEDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHVKIAAKELTTElVDQYYIRVKEQEKFDTMTRLMDVDQP 239
Cdd:PRK11776 164 FQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-IEQRFYEVSPDERLPALQRLLLHHQP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 240 ELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVYNYDIPQD 319
Cdd:PRK11776 243 ESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARD 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 343391197 320 PESYVHRIGRTGRAGKSGQSITFVSPNEMGYLQIIENLTKKR-----MKGLKPASAE 371
Cdd:PRK11776 323 PEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKlnwepLPSLSPLSGV 379
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-423 |
2.15e-118 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 362.24 E-value: 2.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 1 MKFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRE 80
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 81 LAVQSQEELFRFGRS-KGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMG 159
Cdd:PRK11634 86 LAVQVAEAMTDFSKHmRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 160 FLEDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHVKIAAKELTTELVDQYYIRVKEQEKFDTMTRLMDVDQP 239
Cdd:PRK11634 166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 240 ELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVYNYDIPQD 319
Cdd:PRK11634 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 320 PESYVHRIGRTGRAGKSGQSITFVSPNEMGYLQIIENLTKKRMKGLKPASAE-------EAFQAKKQVALKKierdfane 392
Cdd:PRK11634 326 SESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAEllgkrrlEKFAAKVQQQLES-------- 397
|
410 420 430
....*....|....*....|....*....|.
gi 343391197 393 eirSNFEKFGKDARQLASEFSPEELAMYILS 423
Cdd:PRK11634 398 ---SDLDQYRALLAKIQPTAEGEELDLETLA 425
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
2-342 |
4.97e-110 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 333.86 E-value: 4.97e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 2 KFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQ-------ALV 74
Cdd:PRK04837 9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrkvnqprALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 75 IAPTRELAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADE 154
Cdd:PRK04837 89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 155 MLNMGFLEDIEDIISRVPE--NRQTLLFSATMPDAIKRIGVQFMKEPEHVKIAAKELTTElvdqyyiRVKE-------QE 225
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGH-------RIKEelfypsnEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 226 KFDTMTRLMDVDQPELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDI 305
Cdd:PRK04837 242 KMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHI 321
|
330 340 350
....*....|....*....|....*....|....*..
gi 343391197 306 SGVTHVYNYDIPQDPESYVHRIGRTGRAGKSGQSITF 342
Cdd:PRK04837 322 PAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-360 |
5.40e-105 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 322.14 E-value: 5.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 1 MKFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEA------TIQALV 74
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPhakgrrPVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 75 IAPTRELAVQSQEELFRFgrSKGVKVRS--VYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEA 152
Cdd:PRK10590 81 LTPTRELAAQIGENVRDY--SKYLNIRSlvVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 153 DEMLNMGFLEDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHVKIAAKELTTELVDQYYIRVKEQEKFDTMTR 232
Cdd:PRK10590 159 DRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 233 LMDVDQPELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVY 312
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 343391197 313 NYDIPQDPESYVHRIGRTGRAGKSGQSITFVSPNEMGYLQIIENLTKK 360
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKK 366
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-203 |
9.59e-105 |
|
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: 311.68 E-value: 9.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEAT----IQALVIAPTRELAVQSQE 87
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKkgrgPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 88 ELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLEDIEDI 167
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 343391197 168 ISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHVK 203
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
3-356 |
2.38e-102 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 313.30 E-value: 2.38e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRELA 82
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 83 VQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLE 162
Cdd:PTZ00424 110 QQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 163 DIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHVKIAAKELTTELVDQYYIRV-KEQEKFDTMTRLMDVDQPEL 241
Cdd:PTZ00424 190 QIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETLTITQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 242 SIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVYNYDIPQDPE 321
Cdd:PTZ00424 270 AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPE 349
|
330 340 350
....*....|....*....|....*....|....*
gi 343391197 322 SYVHRIGRTGRAGKSGQSITFVSPNEMGYLQIIEN 356
Cdd:PTZ00424 350 NYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
1-387 |
8.28e-98 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 302.63 E-value: 8.28e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 1 MKFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKI----RTEEATIQALVIA 76
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfpRRKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 77 PTRELAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEML 156
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 157 NMGFLEDIEDIISRVPENRQTLLFSATMP-DAIKRIGVQFMKEPehVKIAAKELTTEL--VDQYYIRVKEQE-KFDTMTR 232
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDP--VEVEAEPSRRERkkIHQWYYRADDLEhKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 233 LMDVDQPELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVY 312
Cdd:PRK11192 239 LLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 313 NYDIPQDPESYVHRIGRTGRAGKSGQSITFVSPNEMGYLQIIENLTKKRMK-----GLKPASAEEAFQAKKQVALKKIER 387
Cdd:PRK11192 319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKarvidELRPKTKAPSEKKTGKPSKKVLAK 398
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-371 |
2.41e-95 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 300.71 E-value: 2.41e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 1 MKFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATI-------QAL 73
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALAdrkpedpRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 74 VIAPTRELAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKR-KALKLHDIETLILDEA 152
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 153 DEMLNMGFLEDIEDIISRVPE--NRQTLLFSATMPDAIKRIGVQFMKEPEHVKIAAKELTTELVDQYYIRVKEQEKFDTM 230
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 231 TRLMDVDQPELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTH 310
Cdd:PRK04537 249 LGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343391197 311 VYNYDIPQDPESYVHRIGRTGRAGKSGQSITFVSPNEMGYLQIIENLTKKRMKgLKPASAE 371
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIP-VEPVTAE 388
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
2-347 |
3.14e-95 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 299.77 E-value: 3.14e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 2 KFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTE------EATIqALVI 75
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQpllrygDGPI-VLVL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 76 APTRELAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEM 155
Cdd:PTZ00110 210 APTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 156 LNMGFLEDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKE-PEHVKIAAKELTT-ELVDQYYIRVKEQEKFDTMTRL 233
Cdd:PTZ00110 290 LDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQEVFVVEEHEKRGKLKML 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 234 MD---VDQPELsIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTH 310
Cdd:PTZ00110 370 LQrimRDGDKI-LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKY 448
|
330 340 350
....*....|....*....|....*....|....*..
gi 343391197 311 VYNYDIPQDPESYVHRIGRTGRAGKSGQSITFVSPNE 347
Cdd:PTZ00110 449 VINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK 485
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
2-367 |
2.32e-93 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 292.59 E-value: 2.32e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 2 KFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGL----------PTLEKIRTEEatiQ 71
Cdd:PRK01297 88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLIsiinqllqtpPPKERYMGEP---R 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 72 ALVIAPTRELAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSG-AHIVVGTPGRLLDLIKRKALKLHDIETLILD 150
Cdd:PRK01297 165 ALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 151 EADEMLNMGFLEDIEDIISRVP--ENRQTLLFSATMPDAIKRIGVQFMKEPEHVKIAAKELTTELVDQYYIRVKEQEKFD 228
Cdd:PRK01297 245 EADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 229 TMTRLMDVDQPELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGV 308
Cdd:PRK01297 325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 343391197 309 THVYNYDIPQDPESYVHRIGRTGRAGKSGQSITFVSPNEMGYLQIIENLTKKRMKGLKP 367
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMP 463
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
25-191 |
2.35e-68 |
|
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: 217.11 E-value: 2.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 25 SPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRELAVQSQEELFRFGRSKGVKVRSVY 104
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 105 GGSSIEKQIKALKsGAHIVVGTPGRLLDLIKRKAlKLHDIETLILDEADEMLNMGFLEDIEDIISRVPENRQTLLFSATM 184
Cdd:pfam00270 81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 343391197 185 PDAIKRI 191
Cdd:pfam00270 159 PRNLEDL 165
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
3-197 |
2.93e-66 |
|
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: 213.50 E-value: 2.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKI----------RTEEATIQA 72
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvgrGRRKAYPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 73 LVIAPTRELAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEA 152
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 343391197 153 DEMLNMGFLEDIEDIISR----VPENRQTLLFSATMPDAIKRIGVQFMK 197
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLK 210
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
3-199 |
7.56e-66 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 211.77 E-value: 7.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRELA 82
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 83 VQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLE 162
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 343391197 163 DIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEP 199
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
12-203 |
1.55e-65 |
|
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: 210.96 E-value: 1.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRT---EEATIQALVIAPTRELAVQSQEE 88
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYrpkKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 89 LFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKR-KALKLHDIETLILDEADEMLNMGFLEDIEDI 167
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 343391197 168 ISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHVK 203
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
1-343 |
2.33e-65 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 220.81 E-value: 2.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 1 MKFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLE---KIRTEEATIQ----AL 73
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTIRSGHPSEQrnplAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 74 VIAPTRELAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEAD 153
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 154 EMLNMGFLEDIEDIISRVPENrQTLLFSATMPDAIKRIGVQFMKEPEHVKIAAKELTTELVDQYYIRV----KEQEKFDT 229
Cdd:PLN00206 281 CMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVetkqKKQKLFDI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 230 MTRLMDVDQPelSIVFGRTKRRVDELTRGL-KIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGV 308
Cdd:PLN00206 360 LKSKQHFKPP--AVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRV 437
|
330 340 350
....*....|....*....|....*....|....*
gi 343391197 309 THVYNYDIPQDPESYVHRIGRTGRAGKSGQSITFV 343
Cdd:PLN00206 438 RQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-198 |
2.65e-65 |
|
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: 212.52 E-value: 2.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 1 MKFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATI---------Q 71
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTAssfsevqepQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 72 ALVIAPTRELAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDE 151
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 343391197 152 ADEMLNMGFLEDIEDIISR--VP--ENRQTLLFSATMPDAIKRIGVQFMKE 198
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEpgMPskEDRQTLMFSATFPEEIQRLAAEFLKE 253
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
12-202 |
1.13e-63 |
|
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: 206.79 E-value: 1.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKI-----RTEEATIQ---ALVIAPTRELAV 83
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsrlppLDEETKDDgpyALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 84 QSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLED 163
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 343391197 164 IEDIISRVP--------------------ENRQTLLFSATMPDAIKRIGVQFMKEPEHV 202
Cdd:cd17945 161 VTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
5-204 |
1.26e-63 |
|
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: 206.02 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 5 EFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRELAVQ 84
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 85 SQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLEDI 164
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 343391197 165 EDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPehVKI 204
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDP--VRI 198
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
3-205 |
2.05e-62 |
|
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: 202.93 E-value: 2.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRELA 82
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 83 VQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKR-KALKLHDIETLILDEADEMLNMGFL 161
Cdd:cd17954 82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEADRLLNMDFE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 343391197 162 EDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPehVKIA 205
Cdd:cd17954 162 PEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP--VKIE 203
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
214-343 |
2.58e-62 |
|
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: 200.04 E-value: 2.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 214 VDQYYIRVKEQEKFD-TMTRLMDVDQPELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDV 292
Cdd:cd18787 1 IKQLYVVVEEEEKKLlLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 343391197 293 LVATDVAARGLDISGVTHVYNYDIPQDPESYVHRIGRTGRAGKSGQSITFV 343
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
3-203 |
4.78e-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: 4.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEAT--IQALVIAPTRE 80
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTvgARALILSPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 81 LAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGF 160
Cdd:cd17959 83 LALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 343391197 161 LEDIEDIISRVPENRQTLLFSATMPDAIkrigVQFMK----EPEHVK 203
Cdd:cd17959 163 AEQLHEILSRLPENRQTLLFSATLPKLL----VEFAKaglnEPVLIR 205
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
3-199 |
5.80e-62 |
|
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: 201.68 E-value: 5.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRELA 82
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 83 VQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIK-----RKALKLhdIETLILDEADEMLN 157
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssddtTKVLSR--VKFLVLDEADRLLT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 343391197 158 MGFLEDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEP 199
Cdd:cd17955 159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
3-199 |
1.92e-60 |
|
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: 197.67 E-value: 1.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRELA 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 83 VQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLE 162
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 343391197 163 DIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEP 199
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
12-202 |
2.11e-60 |
|
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: 197.59 E-value: 2.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQ-----ALVIAPTRELAVQSQ 86
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERgdgpiVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 87 EELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLEDIED 166
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 343391197 167 IISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHV 202
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
8-198 |
1.21e-59 |
|
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: 195.88 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 8 LSADLLAEIEKAGFVEASPIQEQTIPLALE-GKDVIGQAQTGTGKTAAFGLPTLE-----KIRTEEATIQALVIAPTREL 81
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQsllntKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 82 AVQSQEElFRF--GRSKGVKVRSVYGGSSIEKQIKAL-KSGAHIVVGTPGRLLDLIK--RKALKLHDIETLILDEADEML 156
Cdd:cd17964 81 ALQIAAE-AKKllQGLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 343391197 157 NMGFLEDIEDIISRVPEN----RQTLLFSATMPDAIKRIGVQFMKE 198
Cdd:cd17964 160 DMGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTLKK 205
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
3-204 |
7.50e-58 |
|
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: 191.40 E-value: 7.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRELA 82
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 83 VQSQEELFRFGRS-KGVKVRSVYGGSSIEKQIKALKSGA-HIVVGTPGRLLDLIKRKALKLHDIETLILDEADEM---LN 157
Cdd:cd17950 84 FQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleqLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 343391197 158 MgfLEDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHVKI 204
Cdd:cd17950 164 M--RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
16-217 |
2.80e-56 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 186.93 E-value: 2.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 16 IEKAGFVEASPIQEQTIPLALEG-KDVIGQAQTGTGKTAAFGLPTLEKIRtEEATIQALVIAPTRELAVQSQEELFRFGR 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 95 SKGVKVRSVYGGSSIEKQIKALKSG-AHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLEDIEDIISRVPE 173
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 343391197 174 NRQTLLFSATMPDAIKRIGVQFMKEPEHVKIaaKELTTELVDQY 217
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
12-202 |
3.93e-56 |
|
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: 186.47 E-value: 3.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTL------EKIRTEEATIqALVIAPTRELAVQS 85
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvhimdqRELEKGEGPI-AVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 86 QEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLEDIE 165
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 343391197 166 DIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHV 202
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
8-199 |
8.25e-56 |
|
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: 186.43 E-value: 8.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 8 LSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKI------RTEEATIqALVIAPTREL 81
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIkdqrpvKPGEGPI-GLIMAPTREL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 82 AVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLI---KRKALKLHDIETLILDEADEMLNM 158
Cdd:cd17953 98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRMFDM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 343391197 159 GFLEDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEP 199
Cdd:cd17953 178 GFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
12-204 |
1.46e-54 |
|
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: 182.39 E-value: 1.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEAT-----IQALVIAPTRELAVQSQ 86
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANlkkgqVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 87 EELFRFGRSKGVKVRS--VYGGSSIEKQIKALK-SGAHIVVGTPGRLLDLIKRKA--LKLHDIETLILDEADEMLNMGFL 161
Cdd:cd17960 81 EVLQSFLEHHLPKLKCqlLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 343391197 162 EDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPehVKI 204
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNP--VRV 201
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
12-203 |
2.49e-54 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 181.31 E-value: 2.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRELAVQSQEELFR 91
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 92 FGRS-KGVKVRSVYGGSSIEKQIKALKsGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLEDIEDIISR 170
Cdd:cd17943 81 IGKKlEGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|...
gi 343391197 171 VPENRQTLLFSATMPDAIKRIGVQFMKEPEHVK 203
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
3-199 |
4.24e-53 |
|
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: 178.43 E-value: 4.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRELA 82
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 83 VQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLE 162
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 343391197 163 DIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEP 199
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDP 197
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
8-199 |
2.89e-52 |
|
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: 176.23 E-value: 2.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 8 LSADLLAEIEKAGFVEASPIQEQTIPLALEG--KDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRELAVQS 85
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 86 QEELFRFGRSKGVKVRSVYGGSSIEkqiKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNM-GFLEDI 164
Cdd:cd17963 81 GEVVEKMGKFTGVKVALAVPGNDVP---RGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQS 157
|
170 180 190
....*....|....*....|....*....|....*
gi 343391197 165 EDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEP 199
Cdd:cd17963 158 IRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNA 192
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
12-202 |
1.18e-51 |
|
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: 174.57 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLekIRTEEATIQ--------ALVIAPTRELAV 83
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF--IHLDLQPIPreqrngpgVLVLTPTRELAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 84 QSQEELFRFgRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLED 163
Cdd:cd17958 79 QIEAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQ 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 343391197 164 IEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHV 202
Cdd:cd17958 158 IRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-199 |
5.83e-51 |
|
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: 172.77 E-value: 5.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKI--RTEEATIQALVIAPTRELAVQSQEEL 89
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 90 FRFGRSKGVKVRSVYGGSS-IEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLEDIEDII 168
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
|
170 180 190
....*....|....*....|....*....|..
gi 343391197 169 SRVPE-NRQTLLFSATMPDAIKRIGVQFMKEP 199
Cdd:cd17957 161 AACTNpNLQRSLFSATIPSEVEELARSVMKDP 192
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
12-199 |
5.65e-50 |
|
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: 170.04 E-value: 5.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRELAVQSQEELFR 91
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 92 FGRSK-GVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLEDIEDIISR 170
Cdd:cd17962 81 LMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180
....*....|....*....|....*....
gi 343391197 171 VPENRQTLLFSATMPDAIKRIGVQFMKEP 199
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNP 189
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
12-204 |
1.17e-49 |
|
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: 169.69 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEAT------IQALVIAPTRELAVQS 85
Cdd:cd17961 5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAEsgeeqgTRALILVPTRELAQQV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 86 Q---EELFRFGRSKgVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHD-IETLILDEADEMLNMGFL 161
Cdd:cd17961 85 SkvlEQLTAYCRKD-VRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVLSYGYE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 343391197 162 EDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHVKI 204
Cdd:cd17961 164 EDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
18-184 |
1.34e-49 |
|
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: 170.50 E-value: 1.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 18 KAGFVEASPIQEQTIPLAL-EGKDVIGQAQTGTGKTAAFGLPTLEKI-----RTEEATIQ----ALVIAPTRELAVQSQE 87
Cdd:cd17946 7 DLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILERLlsqksSNGVGGKQkplrALILTPTRELAVQVKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 88 ELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRK---ALKLHDIETLILDEADEMLNMGFLEDI 164
Cdd:cd17946 87 HLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEKGHFAEL 166
|
170 180
....*....|....*....|....*..
gi 343391197 165 EDIISRVPEN-------RQTLLFSATM 184
Cdd:cd17946 167 EKILELLNKDragkkrkRQTFVFSATL 193
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
1-206 |
8.03e-49 |
|
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: 168.26 E-value: 8.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 1 MKFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQA-----LVI 75
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGdgpicLVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 76 APTRELAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEM 155
Cdd:cd18049 104 APTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 343391197 156 LNMGFLEDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHVKIAA 206
Cdd:cd18049 184 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
16-202 |
3.13e-48 |
|
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: 165.54 E-value: 3.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 16 IEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIR----TEEATIQALVIAPTRELAVQSQEELFR 91
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwTPEDGLGALIISPTRELAMQIFEVLRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 92 FGRSKGVKVRSVYGGSSIEKQIKALkSGAHIVVGTPGRLLDLIKRKA-LKLHDIETLILDEADEMLNMGFLEDIEDIISR 170
Cdd:cd17941 85 VGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETPgFDTSNLQMLVLDEADRILDMGFKETLDAIVEN 163
|
170 180 190
....*....|....*....|....*....|..
gi 343391197 171 VPENRQTLLFSATMPDAIKRIGVQFMKEPEHV 202
Cdd:cd17941 164 LPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
2-198 |
2.90e-47 |
|
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: 164.83 E-value: 2.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 2 KFNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTE---EATIQ------- 71
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgESLPSesgyygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 72 ------ALVIAPTRELAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIE 145
Cdd:cd18051 102 rkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 343391197 146 TLILDEADEMLNMGFLEDIEDIISR--VPE--NRQTLLFSATMPDAIKRIGVQFMKE 198
Cdd:cd18051 182 YLVLDEADRMLDMGFEPQIRRIVEQdtMPPtgERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
3-202 |
9.38e-45 |
|
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: 156.33 E-value: 9.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEkirteeaTIQALVIAPTRELA 82
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-------IVVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 83 VQSQEELFRFGRS-KGVKVRS--VYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMG 159
Cdd:cd17938 74 EQTYNCIENFKKYlDNPKLRValLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 343391197 160 FLEDIEDIISRVP-----ENR-QTLLFSATM-PDAIKRIGVQFMKEPEHV 202
Cdd:cd17938 154 NLETINRIYNRIPkitsdGKRlQVIVCSATLhSFEVKKLADKIMHFPTWV 203
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
26-197 |
5.62e-43 |
|
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: 151.92 E-value: 5.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 26 PIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATI------QALVIAPTRELAVQSQEELFRFgrSKGVK 99
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQVTKDFKDI--TRKLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 100 VRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLEDIEDIISRV-----PEN 174
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSykkdsEDN 172
|
170 180
....*....|....*....|...
gi 343391197 175 RQTLLFSATMPDAIKRIGVQFMK 197
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
17-203 |
8.46e-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: 151.58 E-value: 8.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 17 EKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQ------ALVIAPTRELAVQSQEELF 90
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 91 RFGR-SKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKR-KALKLHDIETLILDEADEMLNMGFLEDIEDII 168
Cdd:cd17949 87 KLLKpFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITKIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 343391197 169 SRV-------------PENRQTLLFSATMPDAIKRIGVQFMKEPEHVK 203
Cdd:cd17949 167 ELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
3-205 |
3.15e-42 |
|
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: 152.09 E-value: 3.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQA-----LVIAP 77
Cdd:cd18050 64 FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLVLAP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 78 TRELAVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLN 157
Cdd:cd18050 144 TRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLD 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 343391197 158 MGFLEDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHVKIA 205
Cdd:cd18050 224 MGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
12-189 |
8.15e-42 |
|
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: 148.64 E-value: 8.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEE---ATIQ-----ALVIAPTRELAV 83
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEkklPFIKgegpyGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 84 QSQE------ELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLN 157
Cdd:cd17951 81 QTHEvieyycKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190
....*....|....*....|....*....|..
gi 343391197 158 MGFLEDIEDIISRVPENRQTLLFSATMPDAIK 189
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQ 192
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
16-183 |
3.41e-40 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 144.04 E-value: 3.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 16 IEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLE-----KIRTEEATiQALVIAPTRELAVQSQ---E 87
Cdd:cd17942 5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyklKFKPRNGT-GVIIISPTRELALQIYgvaK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 88 ELFRFG-RSKGVkvrsVYGGSSIEKQIKALKSGAHIVVGTPGRLLD-LIKRKALKLHDIETLILDEADEMLNMGFLEDIE 165
Cdd:cd17942 84 ELLKYHsQTFGI----VIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMR 159
|
170
....*....|....*...
gi 343391197 166 DIISRVPENRQTLLFSAT 183
Cdd:cd17942 160 QIIKLLPKRRQTMLFSAT 177
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
225-334 |
1.16e-33 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 123.09 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 225 EKFDTMTRLMDVDQPELSIVFGRTKRRVDE--LtrgLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARG 302
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAelL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 343391197 303 LDISGVTHVYNYDIPQDPESYVHRIGRTGRAG 334
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
3-210 |
5.72e-32 |
|
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: 122.82 E-value: 5.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEG--KDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRE 80
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 81 LAVQSQ---EELFRFgrSKGVKV-RSVYG-----GSSIEKQikalksgahIVVGTPGRLLD-LIKRKALKLHDIETLILD 150
Cdd:cd18048 100 LALQTGkvvEEMGKF--CVGIQViYAIRGnrpgkGTDIEAQ---------IVIGTPGTVLDwCFKLRLIDVTNISVFVLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343391197 151 EADEMLNM-GFLEDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKEPEHVKIAAKELT 210
Cdd:cd18048 169 EADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
12-184 |
3.64e-30 |
|
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: 117.73 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEG---------KDVIGQAQTGTGKTAAFGLPTLEKIRTEEAT-IQALVIAPTREL 81
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPrLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 82 AVQSQEELFRFGRSKGVKVRSVYGGSSIEKQIKALK--------SGAHIVVGTPGRLLDLIKR-KALKLHDIETLILDEA 152
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLvdtsgrylSRVDILVATPGRLVDHLNStPGFTLKHLRFLVIDEA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 343391197 153 DEMLNMGFLEDIEDIISRV--------------------PENRQTLLFSATM 184
Cdd:cd17956 161 DRLLNQSFQDWLETVMKALgrptapdlgsfgdanllersVRPLQKLLFSATL 212
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
253-334 |
6.08e-30 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 111.92 E-value: 6.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 253 DELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVYNYDIPQDPESYVHRIGRTGR 332
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 343391197 333 AG 334
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
12-185 |
1.51e-27 |
|
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: 110.53 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 12 LLAEIEKAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKI-------RTEEATIQALVIAPTRELAVQ 84
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 85 SQEELFRFGRSKGVKVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLEDI 164
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190
....*....|....*....|....*....|....
gi 343391197 165 EDIISRVP--ENR-----------QTLLFSATMP 185
Cdd:cd17948 161 SHFLRRFPlaSRRsentdgldpgtQLVLVSATMP 194
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
3-203 |
2.87e-24 |
|
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: 100.56 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 3 FNEFNLSADLLAEIEKAGFVEASPIQEQTIPLALEG--KDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALVIAPTRE 80
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 81 LAVQSQEELFRFGR-SKGVKVRSVYGGSSIEKQIKALKsgaHIVVGTPGRLLD-LIKRKALKLHDIETLILDEADEMLNM 158
Cdd:cd18047 83 LALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIAT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 343391197 159 GFLEDIEDIISR-VPENRQTLLFSATMPDAIKRIGVQFMKEPEHVK 203
Cdd:cd18047 160 QGHQDQSIRIQRmLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
38-183 |
1.43e-20 |
|
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: 88.23 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 38 GKDVIGQAQTGTGKTAAFGLPTLEkiRTEEATIQALVIAPTRELAVQSQEElFRFGRSKGVKVRSVYGGSSIEKQIKALK 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALL--LLLKKGKKVLVLVPTKALALQTAER-LRELFGPGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343391197 118 SGAHIVVGTPGRLLDLIKR-KALKLHDIETLILDEADEML-NM-GFLEDIEDIISRVPENRQTLLFSAT 183
Cdd:cd00046 78 GDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLiDSrGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
219-387 |
7.02e-18 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 86.35 E-value: 7.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 219 IRVKEQEKFDTMTRLMDVDQPELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATdV 298
Cdd:COG0514 210 VPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-I 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 299 A-ARGLDISGVTHVYNYDIPQDPESYVHRIGRTGRAGKSGQSITFVSPNEMgylQIIENLtkkrmkglkpASAEEAFQAK 377
Cdd:COG0514 289 AfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDV---AIQRFF----------IEQSPPDEER 355
|
170
....*....|
gi 343391197 378 KQVALKKIER 387
Cdd:COG0514 356 KRVERAKLDA 365
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
45-190 |
3.09e-17 |
|
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: 81.27 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 45 AQTGTGKTAAFGLPTLEKIRTEE-----------------ATIQALVIAPTRELAVQSQEELFRFGRSKGVKVRSVYGGS 107
Cdd:cd17965 68 AETGSGKTLAYLAPLLDYLKRQEqepfeeaeeeyesakdtGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 108 --SIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFLEDIEDIISRVPENRQTLLFSATMP 185
Cdd:cd17965 148 gpSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227
|
....*
gi 343391197 186 DAIKR 190
Cdd:cd17965 228 KEFDK 232
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
243-342 |
5.90e-16 |
|
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: 74.55 E-value: 5.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 243 IVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVYNYDIPQDPES 322
Cdd:cd18794 34 IIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMES 113
|
90 100
....*....|....*....|
gi 343391197 323 YVHRIGRTGRAGKSGQSITF 342
Cdd:cd18794 114 YYQESGRAGRDGLPSECILF 133
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
4-378 |
3.79e-15 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 78.22 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 4 NEFNLSADLLAEIekAGFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKirtEEATiqaLVIAPTRELAV 83
Cdd:PRK11057 8 NLESLAKQVLQET--FGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL---DGLT---LVVSPLISLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 84 QSQEELfrfgRSKGVKVRSVYGGSSIEKQ---IKALKSGA-HIVVGTPGRLL--DLIKRkaLKLHDIETLILDEAD---- 153
Cdd:PRK11057 80 DQVDQL----LANGVAAACLNSTQTREQQlevMAGCRTGQiKLLYIAPERLMmdNFLEH--LAHWNPALLAVDEAHcisq 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 154 -------EMLNMGFLEdiediiSRVPeNRQTLLFSATMPDAIKRIGVQF--MKEPeHVKIAAkelttelVDQYYIRVKEQ 224
Cdd:PRK11057 154 wghdfrpEYAALGQLR------QRFP-TLPFMALTATADDTTRQDIVRLlgLNDP-LIQISS-------FDRPNIRYTLV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 225 EKF---DTMTRLMDVDQPELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAAR 301
Cdd:PRK11057 219 EKFkplDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGM 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343391197 302 GLDISGVTHVYNYDIPQDPESYVHRIGRTGRAGKSGQSITFVSPNEMGYLqiienltkKRMKGLKPASAEEAFQAKK 378
Cdd:PRK11057 299 GINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWL--------RRCLEEKPAGQQQDIERHK 367
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
47-419 |
2.78e-14 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 75.45 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 47 TGTGKT--AAFglpTLEKIRTEEATiqaLVIAPTRELAVQSQEELfrfgrSKGVKVRSVYGGSSiekqikalKSGAHIVV 124
Cdd:COG1061 109 TGTGKTvlALA---LAAELLRGKRV---LVLVPRRELLEQWAEEL-----RRFLGDPLAGGGKK--------DSDAPITV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 125 GTPGRLLDLIKRKALKlHDIETLILDEADEMLNMGFlediEDIISRVPENRqTLLFSAT--------------------- 183
Cdd:COG1061 170 ATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTATpfrsdgreillflfdgivyey 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 184 -MPDAIKR----------IGVQFMKEPEHVKIAAKELTTELVDQyyirvkEQEKFDTMTRLMD-VDQPELSIVFGRTKRR 251
Cdd:COG1061 244 sLKEAIEDgylappeyygIRVDLTDERAEYDALSERLREALAAD------AERKDKILRELLReHPDDRKTLVFCSSVDH 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 252 VDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVYNYDIPQDPESYVHRIGRTG 331
Cdd:COG1061 318 AEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGL 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 332 RAGKSGQS---ITFVSPNEMGYLQIIENLTKKRMKGLKPASAEEAFQAKKQVALKKIERDFANEEIRSNFEKFGKDARQL 408
Cdd:COG1061 398 RPAPGKEDalvYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALL 477
|
410
....*....|.
gi 343391197 409 ASEFSPEELAM 419
Cdd:COG1061 478 LVLAELLLLEL 488
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
26-187 |
5.21e-12 |
|
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: 64.59 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 26 PIQEQTI-PLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIqaLVIAPTRELAVQSQEELFRFGRSKGVKVRSVY 104
Cdd:cd17921 4 PIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKA--VYIAPTRALVNQKEADLRERFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 105 GGSSIEKQikaLKSGAHIVVGTPGRLLDLI-KRKALKLHDIETLILDEAdEMLNMG----FLEDIEDIISRVPENRQTLL 179
Cdd:cd17921 82 GDPSVNKL---LLAEADILVATPEKLDLLLrNGGERLIQDVRLVVVDEA-HLIGDGergvVLELLLSRLLRINKNARFVG 157
|
....*...
gi 343391197 180 FSATMPDA 187
Cdd:cd17921 158 LSATLPNA 165
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
28-341 |
5.97e-12 |
|
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: 68.32 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 28 QEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRtEEATIQALVIAPTRELAvQSQ-EELFRFGRSKGVKVR-SVYG 105
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL-EDPGATALYLYPTKALA-RDQlRRLRELAEALGLGVRvATYD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 106 GSSIEKQIKALKSGAHIVVGTPgrllDLIKRKALKLHD--------IETLILDEADE--------MLNMgfLEDIEDIIS 169
Cdd:COG1205 139 GDTPPEERRWIREHPDIVLTNP----DMLHYGLLPHHTrwarffrnLRYVVIDEAHTyrgvfgshVANV--LRRLRRICR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 170 RVPENRQTLLFSATMPD----AIKRIGVQF----------------MKEPEHVKI--------AAKELTTELVDQyyiRV 221
Cdd:COG1205 213 HYGSDPQFILASATIGNpaehAERLTGRPVtvvdedgsprgertfvLWNPPLVDDgirrsalaEAARLLADLVRE---GL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 222 KeqekfdtmtrlmdvdqpelSIVFGR-----------TKRRVDELTRGLKIRGFRaegihGDLDQNKRLRVLRDFKNGNL 290
Cdd:COG1205 290 R-------------------TLVFTRsrrgaellaryARRALREPDLADRVAAYR-----AGYLPEERREIERGLRSGEL 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 343391197 291 DVLVATDVAARGLDISGVTHVYNYDIPQDPESYVHRIGRTGRAGKSGQSIT 341
Cdd:COG1205 346 LGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-400 |
2.10e-11 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 66.07 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 1 MKFNEFNLsADLLAEIEKAGFVEASPIQEQTIPLAL-EGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEatiQALVIAPTR 79
Cdd:COG1204 1 MKVAELPL-EKVIEFLKERGIEELYPPQAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKALLNGG---KALYIVPLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 80 ELAVQSQEELFRFGRSKGVKVRSVYGGssIEKQIKALKSgAHIVVGTPGRLLDLIKRKALKLHDIETLILDEA----DEm 155
Cdd:COG1204 77 ALASEKYREFKRDFEELGIKVGVSTGD--YDSDDEWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 156 lNMGFLedIEDIISRV---PENRQTLLFSATM--PDAIKRIgvqFMKEPEHVKIAAKELTTELVDQYYIRVKE---QEKF 227
Cdd:COG1204 153 -SRGPT--LEVLLARLrrlNPEAQIVALSATIgnAEEIAEW---LDAELVKSDWRPVPLNEGVLYDGVLRFDDgsrRSKD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 228 DTMTRLMD-VDQPELSIVFGRTKRRV--------DELTRGL-------------KIRGFRAE-------------GI--- 269
Cdd:COG1204 227 PTLALALDlLEEGGQVLVFVSSRRDAeslakklaDELKRRLtpeereeleelaeELLEVSEEthtnekladclekGVafh 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 270 HGDLDQNKRLRVLRDFKNGNLDVLVATD-------VAARGLDISGVTHVYNYDIPqdPESYVHRIGRTGRAGK--SGQSI 340
Cdd:COG1204 307 HAGLPSELRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIP--VLEFKQMAGRAGRPGYdpYGEAI 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343391197 341 tFVSPNEMGYLQIIENLTKKRMKGLKPASAEEAFQAKKQVALkkIERDFAN--EEIRSNFEK 400
Cdd:COG1204 385 -LVAKSSDEADELFERYILGEPEPIRSKLANESALRTHLLAL--IASGFANsrEELLDFLEN 443
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
243-441 |
5.26e-11 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 65.14 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 243 IVFGRTKRRVDELTRGLKIRGFRAE------GIHGD--LDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVYNY 314
Cdd:COG1111 357 IVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 315 DIPQDPESYVHRIGRTGRAGkSGQSITFVSPN--EMGYLQII---ENLTKKRMKGLKPASAEEAFQAKKQVALKKIErDF 389
Cdd:COG1111 437 EPVPSEIRSIQRKGRTGRKR-EGRVVVLIAKGtrDEAYYWSSrrkEKKMKSILKKLKKLLDKQEKEKLKESAQATLD-EF 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 343391197 390 ANEEIRSNFEKFGKDARQLASE---FSPEELAMYILSLTVQDPDSLPEVEIAREK 441
Cdd:COG1111 515 ESIKELAEDEINEKDLDEIESSengAHVDWREPVLLQVIVSTLAESLELRELGEK 569
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-152 |
1.87e-10 |
|
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: 59.91 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 28 QEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATiQALVIAPTRELAvQSQEELFR---FGRSKGVKVRSVY 104
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGS-RALYLYPTKALA-QDQLRSLRellEQLGLGIRVATYD 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 343391197 105 GGSSIEKQIKALKSGAHIVVGTPGRLLDLIKRKALKLHDI----ETLILDEA 152
Cdd:cd17923 83 GDTPREERRAIIRNPPRILLTNPDMLHYALLPHHDRWARFlrnlRYVVLDEA 134
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
36-304 |
7.82e-10 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 61.45 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 36 LEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEATIQALViaPTRELAVQSQEElFRFGRSKGVKVRSVYGGSSIEKQIKA 115
Cdd:COG1202 223 LEGKDQLVVSATATGKTLIGELAGIKNALEGKGKMLFLV--PLVALANQKYED-FKDRYGDGLDVSIRVGASRIRDDGTR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 116 LKSGAHIVVGT-PGrlLDLIKRKALKLHDIETLILDEAdEMLNMgflED----IEDIISR---VPENRQTLLFSATmpda 187
Cdd:COG1202 300 FDPNADIIVGTyEG--IDHALRTGRDLGDIGTVVIDEV-HMLED---PErghrLDGLIARlkyYCPGAQWIYLSAT---- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 188 ikrigvqfMKEPEHVkiaAKELTTELV---------DQYYIRVKEQEKFDTMTRLMDVDQPELS--------IVFGRTKR 250
Cdd:COG1202 370 --------VGNPEEL---AKKLGAKLVeyeerpvplERHLTFADGREKIRIINKLVKREFDTKSskgyrgqtIIFTNSRR 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 343391197 251 RVDELTRGLkirGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLD 304
Cdd:COG1202 439 RCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVD 489
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
262-336 |
3.76e-09 |
|
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: 55.29 E-value: 3.76e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343391197 262 RGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVYNYDIPQDPESYVHRIGRtGRAGKS 336
Cdd:cd18802 63 RGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNS 136
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
242-328 |
1.09e-08 |
|
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: 53.63 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 242 SIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGN--LDVLVATDVAARGLDISGVTHVYNYDIPQD 319
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPWWN 109
|
90
....*....|....*
gi 343391197 320 P------ESYVHRIG 328
Cdd:cd18793 110 PaveeqaIDRAHRIG 124
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
205-415 |
4.41e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 56.04 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 205 AAKELTTEL-VDQYYIRVKEQE----KFDTMTRL----MDVDQPELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGD--- 272
Cdd:PRK13766 322 ASKRLVEDPrFRKAVRKAKELDiehpKLEKLREIvkeqLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQask 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 273 -----LDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVYNYD-IPQDPESyVHRIGRTGRaGKSGQSITFVSPN 346
Cdd:PRK13766 402 dgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEGRVVVLIAKG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 347 -------------EMGYLQIIENLTK---KRMKGLKPASAEEAFQAKKQVALKKIERDFANEEIRSNFEKFGKDARQLAS 410
Cdd:PRK13766 480 trdeayywssrrkEKKMKEELKNLKGilnKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKDKETEEDE 559
|
....*
gi 343391197 411 EFSPE 415
Cdd:PRK13766 560 PEGPK 564
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
290-343 |
7.45e-08 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 49.62 E-value: 7.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 343391197 290 LDVLVATDVAARGLDISGVTHVYNYDIPQDPESYVHRIGRTGRAGK-SGQSITFV 343
Cdd:cd18785 23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKdEGEVILFV 77
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
242-336 |
3.10e-07 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 49.95 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 242 SIVFGRTKRRVDELTRGL------------KIRGFRAegihGDLDQNKRlRVLRDFKNGNLDVLVATDVAARGLDISGVT 309
Cdd:cd18797 38 TIVFCRSRKLAELLLRYLkarlveegplasKVASYRA----GYLAEDRR-EIEAELFNGELLGVVATNALELGIDIGGLD 112
|
90 100
....*....|....*....|....*..
gi 343391197 310 HVYNYDIPQDPESYVHRIGRTGRAGKS 336
Cdd:cd18797 113 AVVLAGYPGSLASLWQQAGRAGRRGKD 139
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
38-156 |
5.94e-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: 49.50 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 38 GKDVIGQAQTGTGKTAAFGLPTLEKIRTE-EATIQALVIAPTRELAVQSQEELFRFGRSKGVKVR-SVYGG--SSIEKQi 113
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEpEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPvAVRHGdtSQSEKA- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 343391197 114 KALKSGAHIVVGTPGRLLDLIKRKAL--KLHDIETLILDEADEML 156
Cdd:cd17922 80 KQLKNPPGILITTPESLELLLVNKKLreLFAGLRYVVVDEIHALL 124
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
265-332 |
8.41e-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: 48.51 E-value: 8.41e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343391197 265 RAEGIHGdLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVYNYDIPQDPESYVHRIGRTGR 332
Cdd:cd18801 67 SGKSSKG-MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
231-344 |
9.02e-07 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 48.41 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 231 TRLMDVDQPELSIVFGRTKRRVDELTRGLK-IRGFRAEGI-----HGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLD 304
Cdd:cd18796 30 EVIFLLERHKSTLVFTNTRSQAERLAQRLReLCPDRVPPDfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGID 109
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 343391197 305 ISGVTHVYNYDIPQDPESYVHRIGRTGRAGKSGQSITFVS 344
Cdd:cd18796 110 IGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLVP 149
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
47-152 |
9.19e-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: 49.57 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 47 TGTGKT--AAFGLPTLEKI--RTEEATIQALVIAPTRELAVQsQEELFRfgRSKGVKVRSVYGGSSIEKQIKALK----S 118
Cdd:cd18034 25 TGSGKTliAVMLIKEMGELnrKEKNPKKRAVFLVPTVPLVAQ-QAEAIR--SHTDLKVGEYSGEMGVDKWTKERWkeelE 101
|
90 100 110
....*....|....*....|....*....|....
gi 343391197 119 GAHIVVGTPGRLLDLIKRKALKLHDIETLILDEA 152
Cdd:cd18034 102 KYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
236-332 |
1.15e-06 |
|
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: 48.78 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 236 VDQPELSIVFGRTKRRVDELTRGLKIRGFRAEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVYNYD 315
Cdd:cd18790 24 VARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
|
90 100
....*....|....*....|..
gi 343391197 316 -----IPQDPESYVHRIGRTGR 332
Cdd:cd18790 104 adkegFLRSETSLIQTIGRAAR 125
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
26-151 |
2.31e-06 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 48.63 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 26 PIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPT---LEKIRTEEATIQALVIAPTRELAVQSQEELFRFGRsKGVKVRS 102
Cdd:cd18036 5 NYQLELVLPALRGKNTIICAPTGSGKTRVAVYICrhhLEKRRSAGEKGRVVVLVNKVPLVEQQLEKFFKYFR-KGYKVTG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 343391197 103 VYGGSSIEKQIKALKSGAHIVVGTPGRLLDLI----KRKALKLHDIETLILDE 151
Cdd:cd18036 84 LSGDSSHKVSFGQIVKASDVIICTPQILINNLlsgrEEERVYLSDFSLLIFDE 136
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
48-330 |
5.86e-06 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 49.07 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 48 GTGKTAAFGLpTLEKIRTEEATIQALVIAPTReLAVQSQEELFRFGRskGVKVRSVYGGSSIEKQIKALKSgAHIVVGTp 127
Cdd:COG0553 270 GLGKTIQALA-LLLELKERGLARPVLIVAPTS-LVGNWQRELAKFAP--GLRVLVLDGTRERAKGANPFED-ADLVITS- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 128 grlLDLIKRKALKLHDIE--TLILDEA----------------------------------DEM------LNMGFL---- 161
Cdd:COG0553 344 ---YGLLRRDIELLAAVDwdLVILDEAqhiknpatkrakavralkarhrlaltgtpvenrlEELwslldfLNPGLLgslk 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 162 ---EDIEDIISRVPENRQTLLFSATMPDAIKRIGVQFMKE-PE-HVKIAAKELTTE------LVDQYYIRVKEQEK---- 226
Cdd:COG0553 421 afrERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDlPEkTEETLYVELTPEqralyeAVLEYLRRELEGAEgirr 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 227 ----FDTMTRL---------MDVDQPELS-----------------------IVFGRTKRRVDELTRGLKIRGFRAEGIH 270
Cdd:COG0553 501 rgliLAALTRLrqicshpalLLEEGAELSgrsakleallelleellaegekvLVFSQFTDTLDLLEERLEERGIEYAYLH 580
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343391197 271 GDLDQNKRLRVLRDFKNGN--LDVLVATDVAARGLDISGVTHVYNYDIPQDPESY------VHRIGRT 330
Cdd:COG0553 581 GGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEeqaidrAHRIGQT 648
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
47-183 |
6.97e-05 |
|
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: 43.06 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 47 TGTGKTA-AFGLP-TLEKIRTeeatiqaLVIAPTRELAVQSQEELFRFGRSKGVKVrsvyggssIEKQIKALKSGAHIVV 124
Cdd:cd17926 27 TGSGKTLtALALIaYLKELRT-------LIVVPTDALLDQWKERFEDFLGDSSIGL--------IGGGKKKDFDDANVVV 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 343391197 125 GTPGRLLDLIKRKALKLHDIETLILDEADEMLNMGFlediEDIISRVPENRQtLLFSAT 183
Cdd:cd17926 92 ATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTF----SEILKELNAKYR-LGLTAT 145
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
21-331 |
1.09e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 44.88 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 21 FVEASPIQEQTIPLALEGKDVIGQAQTGTGKT-AAF-----GLPTLEKIRTEEATIQALVIAPTRELA-------VQSQE 87
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFlaiidELFRLGREGELEDKVYCLYVSPLRALNndihrnlEEPLT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 88 ELFRFGRSKGVKVRSVYGG------SSIEKQiKALKSGAHIVVGTP---GRLLDLIK-RKalKLHDIETLILDEADEMLN 157
Cdd:PRK13767 110 EIREIAKERGEELPEIRVAirtgdtSSYEKQ-KMLKKPPHILITTPeslAILLNSPKfRE--KLRTVKWVIVDEIHSLAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 158 -------MGFLEDIEDIISRVPenrQTLLFSATM--PDAIKR--IGVQFMKEPEHVKIA----AKELTTEL---VDQyYI 219
Cdd:PRK13767 187 nkrgvhlSLSLERLEELAGGEF---VRIGLSATIepLEEVAKflVGYEDDGEPRDCEIVdarfVKPFDIKVispVDD-LI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 220 RVKEQEKFDTMTRLMD--VDQPELSIVFGRTKRRVDELTRGLKIR---GFRAEGI---HGDLDQNKRLRVLRDFKNGNLD 291
Cdd:PRK13767 263 HTPAEEISEALYETLHelIKEHRTTLIFTNTRSGAERVLYNLRKRfpeEYDEDNIgahHSSLSREVRLEVEEKLKRGELK 342
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 343391197 292 VLVATDVAARGLDISGVTHVYNYDIPQDPESYVHRIGRTG 331
Cdd:PRK13767 343 VVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
241-395 |
1.21e-04 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 42.68 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 241 LSIVFGRTKrrVDELTRGLKIRGFRAEGIHgdldqNKRLRVLRDFKNGNLDVLVAT----DVAARGLDISG-VTHVYNYD 315
Cdd:cd18798 31 VSIDYGKEY--AEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLPErIKYAIFYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 316 IPqdPESYVHRIGRTGR--AGK--SGQSITFVSPNEmgylqIIENLtKKRMKGLKPasaEEAFQAKKQVALKKIERDFan 391
Cdd:cd18798 104 VP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPE-----LFEAL-KKRLKLILD---EFIFKELEEVDLEELLSEI-- 170
|
....
gi 343391197 392 EEIR 395
Cdd:cd18798 171 DESR 174
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
269-363 |
1.72e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 42.33 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 269 IHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVynydIPQDPE----SYVHRI-GRTGRAGKsgQSITF- 342
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVM----VIEDAErfglSQLHQLrGRVGRGDH--QSYCLl 140
|
90 100
....*....|....*....|.
gi 343391197 343 VSPNEMGylqiieNLTKKRMK 363
Cdd:cd18811 141 VYKDPLT------ETAKQRLR 155
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
226-305 |
1.89e-04 |
|
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: 41.85 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 226 KFDTMTRLMDV-DQPELSIVFGRTKRRVDELTRGLKIrgfraEGIHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLD 304
Cdd:cd18789 35 KLRALEELLKRhEQGDKIIVFTDNVEALYRYAKRLLK-----PFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGID 109
|
.
gi 343391197 305 I 305
Cdd:cd18789 110 L 110
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
147-335 |
2.24e-04 |
|
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: 43.57 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 147 LILDEAD--EMLNMGFLEDIEDIISRVpeNRQTLLFSATMPDAIKR----IGVQFMKEPehvkiaakeLTTELVDQYYIR 220
Cdd:cd09639 127 LIFDEVHfyDEYTLALILAVLEVLKDN--DVPILLMSATLPKFLKEyaekIGYVEENEP---------LDLKPNERAPFI 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 221 VKEQE---KFDTMTRLMDVDQPELSI-VFGRTKRRVDELTRGLKIRGFRAEG--IHGDLDQNKRLR----VLRDFKNGNL 290
Cdd:cd09639 196 KIESDkvgEISSLERLLEFIKKGGSVaIIVNTVDRAQEFYQQLKEKGPEEEImlIHSRFTEKDRAKkeaeLLLEFKKSEK 275
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 343391197 291 DVLVATDVAARGLDISgvthvynYDI----PQDPESYVHRIGRTGRAGK 335
Cdd:cd09639 276 FVIVATQVIEASLDIS-------VDVmiteLAPIDSLIQRLGRLHRYGE 317
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
27-137 |
2.99e-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: 41.96 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 27 IQEQTIPLALEG-KDVIGQAQTGTGKTAAFGLPTLE--KIRTEEAT--IQALVIAPTRELAVQSQEELF-RFGRSkGVKV 100
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRllKERNPLPWgnRKVVYIAPIKALCSEKYDDWKeKFGPL-GLSC 83
|
90 100 110
....*....|....*....|....*....|....*..
gi 343391197 101 RSVYGGSSIEKQIKAlkSGAHIVVGTPGRlLDLIKRK 137
Cdd:cd18023 84 AELTGDTEMDDTFEI--QDADIILTTPEK-WDSMTRR 117
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
22-152 |
3.99e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 41.65 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 22 VEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPT---LEKIRTEEaTIQALVIAPTRELAVQSQEELFRFGRSKGV 98
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICehhLKKFPAGR-KGKVVFLANKVPLVEQQKEVFRKHFERPGY 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 343391197 99 KVRSVYGGSSIEKQIKALKSGAHIVVGTPGRLL-DLIKRKALKLHDIETLILDEA 152
Cdd:cd17927 80 KVTGLSGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDEC 134
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
269-337 |
7.73e-04 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 40.33 E-value: 7.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343391197 269 IHGDLDQNKRLRVLRDFKNGNLDVLVATDVAARGLDISGVTHVynydIPQDPE----SYVHRI-GRTGRAGKSG 337
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTM----IIEDADrfglSQLHQLrGRVGRGKHQS 135
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
44-151 |
1.80e-03 |
|
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: 39.32 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 44 QAQTGTGKTAAFGLPTLEKIrteEATIQALVIAPTRELAVQSQEELFRFgrSKGVKVRSVYGGssieKQIKALkSGAHIV 123
Cdd:cd17918 42 SGDVGSGKTLVALGAALLAY---KNGKQVAILVPTEILAHQHYEEARKF--LPFINVELVTGG----TKAQIL-SGISLL 111
|
90 100
....*....|....*....|....*...
gi 343391197 124 VGTPGrlldLIKRKALKlHDIETLILDE 151
Cdd:cd17918 112 VGTHA----LLHLDVKF-KNLDLVIVDE 134
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
48-151 |
2.66e-03 |
|
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350771 [Multi-domain] Cd Length: 218 Bit Score: 39.26 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 48 GTGKTAAfGLPTLEKIRTEEATIQALVIAPTRELAVQSQEELFRFGRSKGVKVRSVYGGSSieKQIKALKSGAHIVVGTP 127
Cdd:cd18013 25 GLGKTVT-TLTALSDLQLDDFTRRVLVIAPLRVARSTWPDEVEKWNHLRNLTVSVAVGTER--QRSKAANTPADLYVINR 101
|
90 100
....*....|....*....|....
gi 343391197 128 GRLLDLIKRKaLKLHDIETLILDE 151
Cdd:cd18013 102 ENLKWLVNKS-GDPWPFDMVVIDE 124
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
36-187 |
3.78e-03 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 38.47 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 36 LEGKDVIGQAQTGTGKTAafgLPTLEKIRTEEATIQALVIAPTRELAVQSQEElFRFGRSKGVKVRSVYGgsSIEKQIKA 115
Cdd:cd18028 15 LKGENLLISIPTASGKTL---IAEMAMVNTLLEGGKALYLVPLRALASEKYEE-FKKLEEIGLKVGISTG--DYDEDDEW 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343391197 116 LKSgAHIVVGTPGRLLDLIKRKALKLHDIETLILDE---ADEMLNMGFLEDIEDIISRVPENRQTLLFSATMPDA 187
Cdd:cd18028 89 LGD-YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEihlISDEERGPTLESIVARLRRLNPNTQIIGLSATIGNP 162
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1-187 |
4.92e-03 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 39.80 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 1 MKFNEFNLSADLLAEIEKAGFVEASPIQEQTIPL-ALEGKDVIGQAQTGTGKTAAFGLPTLEKIRTEEAtiQALVIAPTR 79
Cdd:PRK00254 1 MKVDELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGG--KAVYLVPLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 80 ELAVQSQEElFRFGRSKGVKVRSVYGG-SSIEKQIkalkSGAHIVVGTPGRLLDLIKRKALKLHDIETLILDEADEMLNM 158
Cdd:PRK00254 79 ALAEEKYRE-FKDWEKLGLRVAMTTGDyDSTDEWL----GKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSY 153
|
170 180
....*....|....*....|....*....
gi 343391197 159 GFLEDIEDIISRVPENRQTLLFSATMPDA 187
Cdd:PRK00254 154 DRGATLEMILTHMLGRAQILGLSATVGNA 182
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
147-335 |
5.10e-03 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 39.36 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 147 LILDEAD--EMLNMGFLEDIEDIISRVpeNRQTLLFSATMPDAIKRIGVQFMKEPEHVKIAAKELTTELVDQYYIRVKEQ 224
Cdd:TIGR01587 128 LIFDEVHfyDEYTLALILAVLEVLKDN--DVPILLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 225 -EKFDTMTRLMDVDQPELSI-VFGRTKRRVDELTRGLKIRGFRAEGI--HGDLDQN----KRLRVLRDFKNGNLD-VLVA 295
Cdd:TIGR01587 206 vGEISSLERLLEFIKKGGSIaIIVNTVDRAQEFYQQLKEKAPEEEIIlyHSRFTEKdrakKEAELLREMKKSNEKfVIVA 285
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 343391197 296 TDVAARGLDISgvthvynYDI----PQDPESYVHRIGRTGRAGK 335
Cdd:TIGR01587 286 TQVIEASLDIS-------ADVmiteLAPIDSLIQRLGRLHRYGR 322
|
|
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
37-102 |
5.72e-03 |
|
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate. In humans, a defect in the ASS gene causes citrullinemia, a genetic disease characterized by severe vomiting spells and mental retardation. ASS is a homotetrameric enzyme of about 400 amino-acid residues. An arginine residue seems to be important for the enzyme's catalytic mechanism. The sequences of ASS from various prokaryotes, archaeabacteria and eukaryotes show significant similarity.
Pssm-ID: 467503 Cd Length: 386 Bit Score: 39.06 E-value: 5.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343391197 37 EGKDVIGQAQTGTGKtaafglptlEKIRtEEATIQAL-----VIAPTRELAVQSQEELFRFGRSKGVKVRS 102
Cdd:cd01999 106 EGATAVAHGCTGKGN---------DQVR-FELAIKALapdlkVIAPWRDWNFLTRAEEIAYAKKHGIPVPV 166
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
20-152 |
6.00e-03 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 38.01 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343391197 20 GFVEASPIQEQTIPLALEGKDVIGQAQTGTGKTAAFGLPTLekIRTEEATIQALVIAPTRELaVQSQEE-LFRFgrSKGV 98
Cdd:cd18018 9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL--LLRRRGPGLTLVVSPLIAL-MKDQVDaLPRA--IKAA 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 343391197 99 KVRSVYGGSSIEKQIKALKSG-AHIVVGTPGRLLDLIKRKALKLHD-IETLILDEA 152
Cdd:cd18018 84 ALNSSLTREERRRILEKLRAGeVKILYVSPERLVNESFRELLRQTPpISLLVVDEA 139
|
|
| |
