|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
185-574 |
3.01e-150 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 444.98 E-value: 3.01e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 185 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAavTRVLVLVPT 264
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--PQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 265 RELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLD 344
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 345 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNregDREAIVAALL 424
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR---DKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 425 MRTFTDHVMLFTQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF 504
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 505 TMPNTVKHYVHRVGRTARAGRAGRSVSLVGEEERKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKLEK 574
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPK 386
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
195-390 |
6.57e-134 |
|
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: 394.31 E-value: 6.57e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAAVTRVLVLVPTRELGIQVHSV 274
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 275 TKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKEI 354
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 124249330 355 IRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 390
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
195-389 |
5.98e-91 |
|
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: 282.79 E-value: 5.98e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAAV-TRVLVLVPTRELGIQVHS 273
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRgPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 274 VTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCpSFHLSSIEVLILDEADRMLDEYFEEQMKE 353
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERG-KLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 124249330 354 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
186-556 |
6.39e-91 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 291.85 E-value: 6.39e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 186 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPR-QAAVTRVLVLVPT 264
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRrKSGPPRILILTPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 265 RELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLD 344
Cdd:PRK11192 83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKE-ENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 345 EYFEEQMKEIIRMCSHHRQTMLFSATMTDE-VKDLASVSLKNPVRIfvnsntDVAPFLR-----QEFIRIRPNREgDREA 418
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEV------EAEPSRRerkkiHQWYYRADDLE-HKTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 419 IVAALLMRTFTDHVMLFTQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGV 498
Cdd:PRK11192 235 LLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 124249330 499 KTVINFTMPNTVKHYVHRVGRTARAGRAGRSVSLVGEEERKMLKEIVKAAKAPVKARI 556
Cdd:PRK11192 315 SHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARV 372
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
183-559 |
4.10e-86 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 279.76 E-value: 4.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 183 SLSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQAAVtRVLVLV 262
Cdd:PRK11776 3 MTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--DVKRFRV-QALVLC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 263 PTRELGIQVHSVTKQLAQFCS----ITTClavGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDE 338
Cdd:PRK11776 80 PTRELADQVAKEIRRLARFIPnikvLTLC---GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRK-GTLDLDALNTLVLDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 339 ADRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSnTDVAPFLRQEFIRIRPNregDREA 418
Cdd:PRK11776 156 ADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES-THDLPAIEQRFYEVSPD---ERLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 419 IVAALLMRTFTDHVMLFTQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGV 498
Cdd:PRK11776 232 ALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124249330 499 KTVINFTMPNTVKHYVHRVGRTARAGRAGRSVSLVGEEERKMLKEIVKAAKAPVKARILPQ 559
Cdd:PRK11776 312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS 372
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
184-552 |
1.91e-82 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 270.14 E-value: 1.91e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 184 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAA---VTRVLV 260
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrPVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 261 LVPTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEAD 340
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQ-NAVKLDQVEILVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 341 RMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREGDreaIV 420
Cdd:PRK10590 160 RMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRE---LL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 421 AALLMRTFTDHVMLFTQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKT 500
Cdd:PRK10590 237 SQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPH 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 124249330 501 VINFTMPNTVKHYVHRVGRTARAGRAGRSVSLVGEEERKMLKEIVKAAKAPV 552
Cdd:PRK10590 317 VVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
186-562 |
7.72e-77 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 255.99 E-value: 7.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 186 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAAVTRVLVL 261
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPppkeRYMGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 262 VPTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAA-PDILIATPGRLIDHLHNcPSFHLSSIEVLILDEAD 340
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQR-GEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 341 RMLDEYFEEQMKEIIRMCSH--HRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQefiRIRPNREGDREA 418
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQ---HVYAVAGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 419 IVAALLMRTFTDHVMLFTQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGV 498
Cdd:PRK01297 325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124249330 499 KTVINFTMPNTVKHYVHRVGRTARAGRAGRSVSLVGEEERKMLKEIVKAAKAPVKARILPQDVI 562
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAELL 468
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
186-536 |
8.45e-75 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 248.73 E-value: 8.45e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 186 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAAVTRVLVL 261
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPapedRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 262 VPTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHL-HNCpsFHLSSIEVLILDEAD 340
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAkQNH--INLGAIQVVVLDEAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 341 RMLDEYFEEQMKEIIRMC--SHHRQTMLFSATMTDEVKDLASVSLKNPVRIfvnsntDVAPfLRQEFIRIR-----PNRE 413
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMppANQRLNMLFSATLSYRVRELAFEHMNNPEYV------EVEP-EQKTGHRIKeelfyPSNE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 414 gDREAIVAALLMRTFTDHVMLFTQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGL 493
Cdd:PRK04837 241 -EKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 124249330 494 DIEGVKTVINFTMPNTVKHYVHRVGRTARAGRAGRSVSLVGEE 536
Cdd:PRK04837 320 HIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 362
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
181-613 |
5.41e-74 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 252.46 E-value: 5.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 181 DKSLSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQAAvTRVLV 260
Cdd:PRK11634 3 EFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPELKA-PQILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 261 LVPTRELGIQVHSVTKQLAQFCSITTCLAV-GGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEA 339
Cdd:PRK11634 80 LAPTRELAVQVAEAMTDFSKHMRGVNVVALyGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKR-GTLDLSKLSGLVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 340 DRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREgdREAI 419
Cdd:PRK11634 159 DEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRK--NEAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 420 VAALLMRTFtDHVMLFTQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVK 499
Cdd:PRK11634 237 VRFLEAEDF-DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERIS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 500 TVINFTMPNTVKHYVHRVGRTARAGRAGRSVSLVGEEERKMLKEIVKAAKAPVKARILPQDVILKFRdkieKLEKDVYAV 579
Cdd:PRK11634 316 LVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKR----RLEKFAAKV 391
|
410 420 430
....*....|....*....|....*....|....
gi 124249330 580 LQleaeekemQQSEAQIDTAQRLLAKGKETADQE 613
Cdd:PRK11634 392 QQ--------QLESSDLDQYRALLAKIQPTAEGE 417
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
184-557 |
7.32e-73 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 247.94 E-value: 7.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 184 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAAVTRVL 259
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPaladRKPEDPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 260 VLVPTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEA 339
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 340 DRMLDEYFEEQMKEIIRMCSHH--RQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQefiRIRPNREGDRE 417
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ---RIYFPADEEKQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 418 AIVAALLMRTFTDHVMLFTQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEG 497
Cdd:PRK04537 246 TLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDG 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124249330 498 VKTVINFTMPNTVKHYVHRVGRTARAGRAGRSVSLVGEEERKMLKEI-----VKAAKAPVKARIL 557
Cdd:PRK04537 326 VKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIeayieQKIPVEPVTAELL 390
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
185-552 |
4.47e-71 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 242.37 E-value: 4.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 185 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP--RQAAVTRVLVLV 262
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPllRYGDGPIVLVLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 263 PTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLH-NCPSfhLSSIEVLILDEADR 341
Cdd:PTZ00110 211 PTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLEsNVTN--LRRVTYLVLDEADR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 342 MLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKN-PVRIFVNSNTDVAPF-LRQEFIRIRpnrEGDREAI 419
Cdd:PTZ00110 289 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTACHnIKQEVFVVE---EHEKRGK 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 420 VAALLMRTFTD--HVMLFTQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEG 497
Cdd:PTZ00110 366 LKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKD 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 124249330 498 VKTVINFTMPNTVKHYVHRVGRTARAGRAGRSVSLVGEEERKMLKEIVK---AAKAPV 552
Cdd:PTZ00110 446 VKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKvlrEAKQPV 503
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
185-389 |
1.98e-70 |
|
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: 229.13 E-value: 1.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 185 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAAVtrvLVLVPT 264
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFA---LVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 265 RELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLD 344
Cdd:cd17954 78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 124249330 345 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd17954 158 MDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
185-389 |
5.12e-68 |
|
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: 222.95 E-value: 5.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 185 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQAAV-TRVLVLVP 263
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--KAHSPTVgARALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 264 TRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCpSFHLSSIEVLILDEADRML 343
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEM-NLKLSSVEYVVFDEADRLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 124249330 344 DEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
186-387 |
1.61e-67 |
|
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: 221.33 E-value: 1.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 186 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAAvtrVLVLVPTR 265
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIF---ALVLTPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 266 ELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPS--FHLSSIEVLILDEADRML 343
Cdd:cd17955 78 ELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttKVLSRVKFLVLDEADRLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 124249330 344 DEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPV 387
Cdd:cd17955 158 TGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
185-391 |
1.01e-62 |
|
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: 209.27 E-value: 1.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 185 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP-------RQAAVTR 257
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGppsvgrgRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 258 VLVLVPTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILD 337
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFI-ERGRISLSSIKFLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124249330 338 EADRMLDEYFEEQMKEIIRMCS----HHRQTMLFSATMTDEVKDLASVSLKNpvRIFV 391
Cdd:cd17967 160 EADRMLDMGFEPQIRKIVEHPDmppkGERQTLMFSATFPREIQRLAADFLKN--YIFL 215
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
196-392 |
6.35e-62 |
|
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: 206.37 E-value: 6.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 196 LKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiYKPRQAAVTRV--LVLVPTRELGIQVHS 273
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL-YRERWTPEDGLgaLIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 274 VTKQLAQFCSITTCLAVGGLDVKsQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 353
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVK-EEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 124249330 354 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVN 392
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
191-389 |
3.15e-60 |
|
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: 202.43 E-value: 3.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 191 LSRPLlkaITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLI-YKPRqaaVTR-----VLVLVPT 264
Cdd:cd17949 1 LVSHL---KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsLEPR---VDRsdgtlALVLVPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 265 RELGIQVHSVTKQLAQFCS-ITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRML 343
Cdd:cd17949 75 RELALQIYEVLEKLLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124249330 344 DEYFEEQMKEIIRM-------------CSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd17949 155 DMGFEKDITKILELlddkrskaggeksKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
184-550 |
1.70e-58 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 207.33 E-value: 1.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 184 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERL-IYKPRQAAVTR---VL 259
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCcTIRSGHPSEQRnplAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 260 VLVPTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHL--HNcpsFHLSSIEVLILD 337
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLskHD---IELDNVSVLVLD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 338 EADRMLDEYFEEQMKEIIRMCShHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREgdRE 417
Cdd:PLN00206 278 EVDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQK--KQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 418 AIVAALLMRT-FTDHVMLFTQTKKQAHRM-HILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDI 495
Cdd:PLN00206 355 KLFDILKSKQhFKPPAVVFVSSRLGADLLaNAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 124249330 496 EGVKTVINFTMPNTVKHYVHRVGRTARAGRAGRSVSLVGEEERKMLKEIVKAAKA 550
Cdd:PLN00206 435 LRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKS 489
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
191-387 |
2.16e-58 |
|
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: 197.04 E-value: 2.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 191 LSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLErLIYKPRQAA----VTRVLVLVPTRE 266
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQ-KILKAKAESgeeqGTRALILVPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 267 LGIQVHSVTKQLAQFCS-ITTCLAVGG-LDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLD 344
Cdd:cd17961 80 LAQQVSKVLEQLTAYCRkDVRVVNLSAsSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124249330 345 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPV 387
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
195-391 |
4.27e-58 |
|
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: 195.89 E-value: 4.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIyKPRQAAVTRVLVLVPTRELGIQVHSV 274
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLG-KPRKKKGLRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 275 TKQLAQFCSITTCLavggLDvKSQEAALRAAP------DILIATPGRLIDHLHNCPSfHLSSIEVLILDEADRMLDEYFE 348
Cdd:cd17957 80 LLKLSKGTGLRIVL----LS-KSLEAKAKDGPksitkyDILVSTPLRLVFLLKQGPI-DLSSVEYLVLDEADKLFEPGFR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 124249330 349 EQMKEIIRMCSHHR-QTMLFSATMTDEVKDLASVSLKNPVRIFV 391
Cdd:cd17957 154 EQTDEILAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
196-392 |
5.42e-58 |
|
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: 195.66 E-value: 5.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 196 LKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLE---RLIYKPRQAavTRVLVLVPTRELGIQVH 272
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyKLKFKPRNG--TGVIIISPTRELALQIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 273 SVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMK 352
Cdd:cd17942 80 GVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 124249330 353 EIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPvRIFVN 392
Cdd:cd17942 160 QIIKLLPKRRQTMLFSATQTRKVEDLARISLKKK-PLYVG 198
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
178-544 |
6.66e-58 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 202.36 E-value: 6.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 178 SEYDKSL-SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQaavT 256
Cdd:PTZ00424 21 SNYDEIVdSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNA---C 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 257 RVLVLVPTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLIL 336
Cdd:PTZ00424 98 QALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI-DKRHLRVDDLKLFIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 337 DEADRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRpNREGDR 416
Cdd:PTZ00424 177 DEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVE-KEEWKF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 417 EAIVAALLMRTFTdHVMLFTQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIE 496
Cdd:PTZ00424 256 DTLCDLYETLTIT-QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 124249330 497 GVKTVINFTMPNTVKHYVHRVGRTARAGRAGRSVSLVGEEERKMLKEI 544
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
195-389 |
2.34e-57 |
|
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: 193.95 E-value: 2.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAAVTRV--LVLVPTRELGIQVH 272
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVgaLIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 273 SVTKQLAQFCS--ITTCLAVGGLDVKSQEAALRA-APDILIATPGRLIDHL-HNCPSFHLSSIEVLILDEADRMLDEYFE 348
Cdd:cd17960 81 EVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLsRKADKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 124249330 349 EQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
208-378 |
1.57e-56 |
|
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: 190.53 E-value: 1.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 208 TPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQaavTRVLVLVPTRELGIQVHSVTKQLAQFCSITTC 287
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG---PQALVLAPTRELAEQIYEELKKLGKGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 288 LAVGGLDVKSQEAALRAaPDILIATPGRLIDHLHNcpSFHLSSIEVLILDEADRMLDEYFEEQMKEIIRMCSHHRQTMLF 367
Cdd:pfam00270 78 SLLGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQE--RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
|
170
....*....|.
gi 124249330 368 SATMTDEVKDL 378
Cdd:pfam00270 155 SATLPRNLEDL 165
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
191-384 |
3.09e-55 |
|
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: 188.56 E-value: 3.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 191 LSRPLLKAITAMGFKQPTPIQKACIPVGL-LGKDICACAATGTGKTAAFALPVLERLI--YKPRQAAVTRVLVLVPTREL 267
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLntKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 268 GIQVHSVTKQLAQFC-SITTCLAVGGLDVKSQEAAL-RAAPDILIATPGRLIDHLHNCPSF-HLSSIEVLILDEADRMLD 344
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVAkAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 124249330 345 EYFEEQMKEIIR----MCSHHRQTMLFSATMTDEVKDLASVSLK 384
Cdd:cd17964 161 MGFRPDLEQILRhlpeKNADPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
195-389 |
3.20e-54 |
|
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: 186.37 E-value: 3.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAAVTR-----VLVLVPTRELGI 269
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKddgpyALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 270 QVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcpsfH---LSSIEVLILDEADRMLDEY 346
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLER----RllvLNQCTYVVLDEADRMIDMG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124249330 347 FEEQMKEII--------------------RMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd17945 157 FEPQVTKILdampvsnkkpdteeaeklaaSGKHRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
188-390 |
4.11e-51 |
|
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: 177.13 E-value: 4.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 188 DMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiykPRQAAVTRVLVLVPTREL 267
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI---DTTVRETQALVLAPTREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 268 GIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYF 347
Cdd:cd17939 78 AQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124249330 348 EEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 390
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
195-391 |
1.44e-50 |
|
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: 176.67 E-value: 1.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIP---------VGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQAAVTRVLVLVPTR 265
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPwllpsskstPPYRPGDLCVSAPTGSGKTLAYVLPIVQAL--SKRVVPRLRALIVVPTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 266 ELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAA--------PDILIATPGRLIDHLHNCPSFHLSSIEVLILD 337
Cdd:cd17956 79 ELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGFTLKHLRFLVID 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124249330 338 EADRMLDEYFEE------------------QMKEIIRMCSHHR--QTMLFSATMTDEVKDLASVSLKNPvRIFV 391
Cdd:cd17956 159 EADRLLNQSFQDwletvmkalgrptapdlgSFGDANLLERSVRplQKLLFSATLTRDPEKLSSLKLHRP-RLFT 231
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
184-384 |
1.66e-49 |
|
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: 174.77 E-value: 1.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 184 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLI---YKPRQAAVTR--- 257
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkegLTASSFSEVQepq 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 258 VLVLVPTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILD 337
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFI-GRGKISLSKLKYLILD 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124249330 338 EADRMLDEYFEEQMKEIIRMCS----HHRQTMLFSATMTDEVKDLASVSLK 384
Cdd:cd18052 202 EADRMLDMGFGPEIRKLVSEPGmpskEDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
195-389 |
2.55e-48 |
|
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: 169.09 E-value: 2.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP--RQAAVTRVLVLVPTRELGIQVH 272
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPplERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 273 SVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDhLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMK 352
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLID-FLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 124249330 353 EIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
186-389 |
2.83e-48 |
|
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: 169.02 E-value: 2.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 186 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRqaaVTRVLVLVPTR 265
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKD---VIQALILVPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 266 ELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDhLHNCPSFHLSSIEVLILDEADRMLDE 345
Cdd:cd17940 78 ELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 124249330 346 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
199-389 |
9.74e-48 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 167.67 E-value: 9.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 199 ITAMGFKQPTPIQKACIPVGLLG-KDICACAATGTGKTAAFALPVLERLIYKPRqaavTRVLVLVPTRELGIQVHSVTKQ 277
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKG----GRVLVLVPTRELAEQWAEELKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 278 LAQFCSITTCLAVGGLDVKSQEAAL-RAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFEEQMKEIIR 356
Cdd:smart00487 77 LGPSLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
|
170 180 190
....*....|....*....|....*....|...
gi 124249330 357 MCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI 188
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
195-389 |
2.47e-47 |
|
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: 166.44 E-value: 2.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIykpRQAAVTR-----VLVLVPTRELGI 269
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM---DQRELEKgegpiAVIVAPTRELAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 270 QVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFEE 349
Cdd:cd17952 78 QIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKK-KATNLQRVTYLVLDEADRMFDMGFEY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 124249330 350 QMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd17952 157 QVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
195-372 |
1.19e-46 |
|
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: 165.88 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLL-GKDICACAATGTGKTAAFALPVLERLIYKPRQAAVT------RVLVLVPTREL 267
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGgkqkplRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 268 GIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSF--HLSSIEVLILDEADRMLDE 345
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 124249330 346 -YFEEqMKEIIRM-------CSHHRQTMLFSATMT 372
Cdd:cd17946 161 gHFAE-LEKILELlnkdragKKRKRQTFVFSATLT 194
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
401-533 |
5.94e-46 |
|
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: 159.98 E-value: 5.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 401 LRQEFIRIRPNREgdREAIVAALLMRTFTDHVMLFTQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQI 480
Cdd:cd18787 1 IKQLYVVVEEEEK--KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 124249330 481 DILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGRTARAGRAGRSVSLV 533
Cdd:cd18787 79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
186-389 |
2.41e-44 |
|
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: 158.38 E-value: 2.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 186 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQaavTRVLVLVPTR 265
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKA---TQALVLAPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 266 ELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILDEADRMLDE 345
Cdd:cd18046 78 ELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 124249330 346 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd18046 157 GFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
195-389 |
3.98e-44 |
|
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: 157.89 E-value: 3.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVL-------ERLIYKPRQAAVTrvLVLVPTREL 267
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqeKKLPFIKGEGPYG--LIVCPSREL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 268 GIQVHSVTKQLAQFCS------ITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILDEADR 341
Cdd:cd17951 79 ARQTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEADR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 124249330 342 MLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd17951 158 MIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
195-389 |
9.35e-44 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 156.55 E-value: 9.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAAvtrVLVLVPTRELGIQVHSV 274
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPS---ALILTPTRELAVQIEDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 275 TKQLAQ-FCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 353
Cdd:cd17962 78 AKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL-KQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 124249330 354 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd17962 157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
195-370 |
2.37e-43 |
|
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: 155.11 E-value: 2.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIykpRQAAVTRVLVLVPTRELGIQVHSV 274
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD---LERRHPQVLILAPTREIAVQIHDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 275 TKQLAQFC-SITTCLAVGGLDVKSQEAALRaAPDILIATPGRlIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 353
Cdd:cd17943 78 FKKIGKKLeGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGR-IKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170
....*....|....*..
gi 124249330 354 IIRMCSHHRQTMLFSAT 370
Cdd:cd17943 156 IFSSLPKNKQVIAFSAT 172
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
195-390 |
3.53e-42 |
|
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: 152.23 E-value: 3.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP---RQAAVTRVLVLVPTRELGIQV 271
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPiprEQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 272 HSVTKQLAQFCSITTCLaVGGLDVKSQEAALRAAPDILIATPGRLIDhLHNCPSFHLSSIEVLILDEADRMLDEYFEEQM 351
Cdd:cd17958 81 EAECSKYSYKGLKSVCV-YGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 124249330 352 KEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 390
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
191-389 |
4.32e-42 |
|
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: 152.53 E-value: 4.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 191 LSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALP----VLERLIYKPRQAAVTrvLVLVPTRE 266
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPmfrhIKDQRPVKPGEGPIG--LIMAPTRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 267 LGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHL--HNCPSFHLSSIEVLILDEADRMLD 344
Cdd:cd17953 97 LALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVTNLRRVTYVVLDEADRMFD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 124249330 345 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd17953 177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
191-389 |
6.53e-42 |
|
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: 151.19 E-value: 6.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 191 LSRPLLKAITAMGFKQPTPIQKACIPVgLLG---KDICACAATGTGKTAAFALPVLERLiyKPRQAAvTRVLVLVPTREL 267
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPL-ILSdppENLIAQSQSGTGKTAAFVLAMLSRV--DPTLKS-PQALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 268 GIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEaalRAAPDILIATPGRLIDHL-HNCpsFHLSSIEVLILDEADRMLD-E 345
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVALAVPGNDVPRGK---KITAQIVIGTPGTVLDWLkKRQ--LDLKKIKILVLDEADVMLDtQ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 124249330 346 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd17963 152 GHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
185-385 |
2.41e-41 |
|
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: 151.73 E-value: 2.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 185 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLI----YKPRQAAVTR--- 257
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYeqgpGESLPSESGYygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 258 ------VLVLVPTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSI 331
Cdd:cd18051 102 rkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLER-GKIGLDYC 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124249330 332 EVLILDEADRMLDEYFEEQMKEIIRMC----SHHRQTMLFSATMTDEVKDLASVSLKN 385
Cdd:cd18051 181 KYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
183-391 |
1.86e-40 |
|
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: 147.49 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 183 SLSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQaavTRVLVLV 262
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQ---VSVLVIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 263 PTRELGIQVHSVTKQLAQFC-SITTCLAVGGLDVKSQEAALR-AAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEAD 340
Cdd:cd17950 78 HTRELAFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVRE-KKLKLSHVKHFVLDECD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 124249330 341 RMLDEY-FEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFV 391
Cdd:cd17950 157 KMLEQLdMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
184-393 |
6.27e-39 |
|
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: 144.38 E-value: 6.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 184 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP--RQAAVTRVLVL 261
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflERGDGPICLVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 262 VPTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHnCPSFHLSSIEVLILDEADR 341
Cdd:cd18049 104 APTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLE-AGKTNLRRCTYLVLDEADR 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 124249330 342 MLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNS 393
Cdd:cd18049 183 MLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
186-387 |
3.60e-37 |
|
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: 138.22 E-value: 3.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 186 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLErliykprqaaVTRVLVLVPTR 265
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ----------IVVALILEPSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 266 ELGIQVHSVTKQLAQFC---SITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRM 342
Cdd:cd17938 71 ELAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKT-GKLDLSSVRFFVLDEADRL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 124249330 343 LDEYFEEQMKEIIRMCSHHR------QTMLFSATM-TDEVKDLASVSLKNPV 387
Cdd:cd17938 150 LSQGNLETINRIYNRIPKITsdgkrlQVIVCSATLhSFEVKKLADKIMHFPT 201
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
186-389 |
2.61e-34 |
|
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: 129.89 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 186 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQaavTRVLVLVPTR 265
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRE---TQALILSPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 266 ELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDE 345
Cdd:cd18045 78 ELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEMLNK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 124249330 346 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd18045 157 GFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
185-389 |
7.11e-33 |
|
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: 128.20 E-value: 7.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 185 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP--RQAAVTRVLVLV 262
Cdd:cd18050 63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPylERGDGPICLVLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 263 PTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSfHLSSIEVLILDEADRM 342
Cdd:cd18050 143 PTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRM 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 124249330 343 LDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 389
Cdd:cd18050 222 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
195-380 |
1.38e-30 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 120.16 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAAVT----RVLVLVPTRELGIQ 270
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfnapRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 271 VHSVTKQLAQFCSITTCLAVGGLDVKSQEAALRAAPDILIATPGrLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQ 350
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPG-ALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124249330 351 MKEIIRMCSHHR-------------QTMLFSATMTDEVKDLAS 380
Cdd:cd17948 160 LSHFLRRFPLASrrsentdgldpgtQLVLVSATMPSGVGEVLS 202
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
196-384 |
6.87e-30 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 117.26 E-value: 6.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 196 LKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERL---IYKPRQAAVTRVLVLVPTRELGIQvh 272
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLqedQQPRKRGRAPKVLVLAPTRELANQ-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 273 sVTKqlaQFCSITTCLAV----GGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFE 348
Cdd:cd17944 80 -VTK---DFKDITRKLSVacfyGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQN-GRLDLTKLKHVVLDEVDQMLDMGFA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 124249330 349 EQMKEIIRMC-----SHHRQTMLFSATMTDEVKDLASVSLK 384
Cdd:cd17944 155 EQVEEILSVSykkdsEDNPQTLLFSATCPDWVYNVAKKYMK 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
415-524 |
3.40e-28 |
|
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: 109.22 E-value: 3.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 415 DREAIVAALLMRTFTDHVMLFTQTKKQAHrMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLD 494
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 124249330 495 IEGVKTVINFTMPNTVKHYVHRVGRTARAG 524
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
185-386 |
1.49e-25 |
|
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: 105.87 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 185 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLG--KDICACAATGTGKTAAFALPVLERLIYKPRqaaVTRVLVLV 262
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKL---YPQCLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 263 PTRELGIQVHSVTKQLAQFCS-ITTCLAVGGldvKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADR 341
Cdd:cd18048 96 PTFELALQTGKVVEEMGKFCVgIQVIYAIRG---NRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVTNISVFVLDEADV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 124249330 342 MLD-EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNP 386
Cdd:cd18048 173 MINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
456-524 |
2.92e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 94.20 E-value: 2.92e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124249330 456 VGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGRTARAG 524
Cdd:smart00490 14 VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
185-386 |
2.16e-21 |
|
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: 92.86 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 185 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLG--KDICACAATGTGKTAAFALPVLERLiykPRQAAVTRVLVLV 262
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---EPANKYPQCLCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 263 PTRELGIQVHSVTKQLAQFC-SITTCLAVGGldvKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADR 341
Cdd:cd18047 79 PTYELALQTGKVIEQMGKFYpELKLAYAVRG---NKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 124249330 342 ML-DEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNP 386
Cdd:cd18047 156 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
221-687 |
1.77e-18 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 89.70 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 221 GKDICACAATGTGKTAAFALpVLERLIYKPRqaavtrVLVLVPTRELGIQVHsvtkqlAQFCSITTCLAVGGLDVKSQEa 300
Cdd:COG1061 100 GGRGLVVAPTGTGKTVLALA-LAAELLRGKR------VLVLVPRRELLEQWA------EELRRFLGDPLAGGGKKDSDA- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 301 alraapDILIATPGRLIDHLHNcpSFHLSSIEVLILDEADRMLDEYFEEqmkeIIRMCSHHRqTMLFSAT--MTDEvKDL 378
Cdd:COG1061 166 ------PITVATYQSLARRAHL--DELGDRFGLVIIDEAHHAGAPSYRR----ILEAFPAAY-RLGLTATpfRSDG-REI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 379 ASVSLKN-----------------PVRIFV------NSNTDVAPFLRQEFIRIRPNREGDREAIVAALLMRTFTDHVMLF 435
Cdd:COG1061 232 LLFLFDGivyeyslkeaiedgylaPPEYYGirvdltDERAEYDALSERLREALAADAERKDKILRELLREHPDDRKTLVF 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 436 TQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVH 515
Cdd:COG1061 312 CSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 516 RVGRTARAGRAGRSVSL--VGEEERKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKLEKDVYAVLQLEAEEKEMQQSE 593
Cdd:COG1061 392 RLGRGLRPAPGKEDALVydFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELEL 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 594 AQIDtAQRLLAKGKETADQEPERSWFQTKEERKKEKIAKALQEFDLALRGKKKRKKFMKDAKKKGEMTAEERSQFEILKA 673
Cdd:COG1061 472 LEDA-LLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEE 550
|
490
....*....|....
gi 124249330 674 QMFAERLAKRNRRT 687
Cdd:COG1061 551 LAALLLKELLRAAL 564
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
221-370 |
7.35e-16 |
|
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: 75.13 E-value: 7.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 221 GKDICACAATGTGKTAAFALPVLERLIYKPRQaavtrVLVLVPTRELGIQVHSVTKQLAQFcSITTCLAVGGLDVKSQEA 300
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGKK-----VLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREK 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124249330 301 ALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMkEIIRMCSHHR---QTMLFSAT 370
Cdd:cd00046 75 NKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALI-LDLAVRKAGLknaQVILLSAT 146
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
190-528 |
7.58e-16 |
|
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: 81.81 E-value: 7.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 190 NLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRqaavTRVLVLVPtrelgi 269
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPG----ATALYLYP------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 270 qvhsvTKQLA--QFCSITTCLAVGGLDVK--------SQEA--ALRAAPDILIATPgrliD--HLHNCPSFH-----LSS 330
Cdd:COG1205 110 -----TKALArdQLRRLRELAEALGLGVRvatydgdtPPEErrWIREHPDIVLTNP----DmlHYGLLPHHTrwarfFRN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 331 IEVLILDEA---------------DRMLdeyfeeqmkeiiRMCSHHRQTMLF---SATMtDEVKDLASVSLKNPVRIfVN 392
Cdd:COG1205 181 LRYVVIDEAhtyrgvfgshvanvlRRLR------------RICRHYGSDPQFilaSATI-GNPAEHAERLTGRPVTV-VD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 393 SNTdvAPFLRQEFIRIRP---NREGDREAIV-AALLMRTFTDH---VMLFTQTKKQAHRM------HILLGLLGLQVGEL 459
Cdd:COG1205 247 EDG--SPRGERTFVLWNPplvDDGIRRSALAeAARLLADLVREglrTLVFTRSRRGAELLaryarrALREPDLADRVAAY 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124249330 460 HGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGrtaRAGRAGR 528
Cdd:COG1205 325 RAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAG---RAGRRGQ 390
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
206-374 |
1.25e-15 |
|
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: 77.42 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 206 QPTPIQKACIPVgLLGK----------------DICACAA-TGTGKTAAFALPVLERL-------------IYKP-RQAA 254
Cdd:cd17965 30 KPSPIQTLAIKK-LLKTlmrkvtkqtsneepklEVFLLAAeTGSGKTLAYLAPLLDYLkrqeqepfeeaeeEYESaKDTG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 255 VTRVLVLVPTRELGIQVHSVTKQLAQFCS--ITTCLAVGGLDVKSQEAALRAAPDILIATPGrLIDHLHNCPSFHLSSIE 332
Cdd:cd17965 109 RPRSVILVPTHELVEQVYSVLKKLSHTVKlgIKTFSSGFGPSYQRLQLAFKGRIDILVTTPG-KLASLAKSRPKILSRVT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 124249330 333 VLILDEADRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDE 374
Cdd:cd17965 188 HLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKE 229
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
221-339 |
2.61e-11 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 62.99 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 221 GKDICACAATGTGKTAAFALPVLERLIYKPRqaavTRVLVLVPTRELGI-QVHSVTKQLAQFCSITTCLAVGG-LDVKSQ 298
Cdd:cd17923 15 GRSVVVTTGTASGKSLCYQLPILEALLRDPG----SRALYLYPTKALAQdQLRSLRELLEQLGLGIRVATYDGdTPREER 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 124249330 299 EAALRAAPDILIATPGRL---IDHLHNCPSFHLSSIEVLILDEA 339
Cdd:cd17923 91 RAIIRNPPRILLTNPDMLhyaLLPHHDRWARFLRNLRYVVLDEA 134
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
463-750 |
3.68e-11 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 66.68 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 463 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF-TMPNTVKhYVHRVGRTARaGRAGRSVSLVGE------ 535
Cdd:COG1111 395 LTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYePVPSEIR-SIQRKGRTGR-KREGRVVVLIAKgtrdea 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 536 -------EERKMLKEI--VKAAKAPVKARILPQ--------------DVILKFRDKIEKLEKDVYAVLQLEAEEKEMQQS 592
Cdd:COG1111 473 yywssrrKEKKMKSILkkLKKLLDKQEKEKLKEsaqatldefesikeLAEDEINEKDLDEIESSENGAHVDWREPVLLQV 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 593 EAQIDTAQRLLAKGKETADQEperswfqTKEERKKEKIAKALQEFDLALRGKKKRKKFMKDAKKKGEMTAEERSQFEILK 672
Cdd:COG1111 553 IVSTLAESLELRELGEKVDDE-------VNLILEIDRVDVVDDGSVLRVSRLLVEIGELDGKTRVIIASYGDEYFDAILR 625
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124249330 673 AQMFAERLAKRNRRTKRARAMPEDEPTGPAKKQKQQQKSVFDEELTNTSKKALKQYRAGPSFEERKQSGLPRQRRGNF 750
Cdd:COG1111 626 LTSKIKLPSLVSDISVDIPDLPIVEIVGEAVLCKKEDGSREARFIKKERDLKGIRLAEGETLNDPLIELLRQQLYGEA 703
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
463-523 |
9.58e-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: 54.52 E-value: 9.58e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124249330 463 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGRtARA 523
Cdd:cd18802 74 MTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
478-524 |
1.26e-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: 52.32 E-value: 1.26e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 124249330 478 EQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGRTARAG 524
Cdd:cd18785 21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
463-588 |
1.49e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 58.35 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 463 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFT-MPNTVKhYVHRVGRTARaGRAGRSVSLVGE------ 535
Cdd:PRK13766 407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIR-SIQRKGRTGR-QEEGRVVVLIAKgtrdea 484
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 536 -------EERKMlKEIVKAAKAPVKARILPQDVILKFRDKIEKLEKDVYAVLQLEAEEKE 588
Cdd:PRK13766 485 yywssrrKEKKM-KEELKNLKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEE 543
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
219-346 |
2.07e-08 |
|
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: 55.13 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 219 LLGKDICACAATGTGKTAAfALPVLERLIYKPRQAAVTRVLVLVPTrelgiqVHSVTKQLAQFCSITTCLA--VGGL--D 294
Cdd:cd17927 15 LKGKNTIICLPTGSGKTFV-AVLICEHHLKKFPAGRKGKVVFLANK------VPLVEQQKEVFRKHFERPGykVTGLsgD 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 124249330 295 VKSQEAALRAAP--DILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEY 346
Cdd:cd17927 88 TSENVSVEQIVEssDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHNTTKNH 141
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
463-532 |
2.84e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 50.43 E-value: 2.84e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 463 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGRTARaGRAGRSVSL 532
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVL 142
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
195-528 |
5.03e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 52.98 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 195 LLKAITAMGFKQPTPIQKACIPVGLL-GKDICACAATGTGKTAafalpVLERLIYKprqaAVTR---VLVLVPTRELGIQ 270
Cdd:COG1204 11 VIEFLKERGIEELYPPQAEALEAGLLeGKNLVVSAPTASGKTL-----IAELAILK----ALLNggkALYIVPLRALASE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 271 VHS-VTKQLAQFcSITTCLAVGGLDVKSQEAAlraAPDILIATPGRLIDHLHNCPSFhLSSIEVLILDEAdRMLDEY--- 346
Cdd:COG1204 82 KYReFKRDFEEL-GIKVGVSTGDYDSDDEWLG---RYDILVATPEKLDSLLRNGPSW-LRDVDLVVVDEA-HLIDDEsrg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 347 --FEEQMKEIIRMCShHRQTMLFSATMTDeVKDLASVsLKNPVrifVNSN-TDVApfLRQEFIRIRPNREGDREAI---- 419
Cdd:COG1204 156 ptLEVLLARLRRLNP-EAQIVALSATIGN-AEEIAEW-LDAEL---VKSDwRPVP--LNEGVLYDGVLRFDDGSRRskdp 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 420 VAALLMRTFTD--HVMLFTQTKKQAHRM------HILLGLLGLQVGEL-------------------------------H 460
Cdd:COG1204 228 TLALALDLLEEggQVLVFVSSRRDAESLakkladELKRRLTPEEREELeelaeellevseethtnekladclekgvafhH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 461 GNLSQTQRLEALRRFKDEQIDILVATDVAArgldiEGV----KTVInftmpntvkhyVHRVGRTAR-----------AGR 525
Cdd:COG1204 308 AGLPSELRRLVEDAFREGLIKVLVATPTLA-----AGVnlpaRRVI-----------IRDTKRGGMvpipvlefkqmAGR 371
|
...
gi 124249330 526 AGR 528
Cdd:COG1204 372 AGR 374
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
227-370 |
8.16e-07 |
|
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: 49.23 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 227 CAATGTGKTA-AFALPVLerliykprqAAVTRVLVLVPTRELgiqVHSVTKQLAQFCSITTCLAVGGLDVKSQEAAlraa 305
Cdd:cd17926 24 VLPTGSGKTLtALALIAY---------LKELRTLIVVPTDAL---LDQWKERFEDFLGDSSIGLIGGGKKKDFDDA---- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124249330 306 pDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFEeqmkEIIRMCSHHRQtMLFSAT 370
Cdd:cd17926 88 -NVVVATYQSLSNLAEE-EKDLFDQFGLLIVDEAHHLPAKTFS----EILKELNAKYR-LGLTAT 145
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
434-532 |
1.10e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 48.80 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 434 LFTQTKKQAH------RMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMP 507
Cdd:cd18796 43 VFTNTRSQAErlaqrlRELCPDRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
|
90 100
....*....|....*....|....*
gi 124249330 508 NTVKHYVHRVGrtaRAGRAGRSVSL 532
Cdd:cd18796 123 KSVARLLQRLG---RSGHRPGAASK 144
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
204-519 |
1.88e-06 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 51.64 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 204 FKQPTPIQKACIPVGLLGKDICACAATGTGKT-AAFaLPVLERLIYKPRQAAV---TRVLVLVPTRELGIQVHsvtKQLA 279
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELpdgLRVLYISPLKALANDIE---RNLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 280 QFCSITTCLAVGGL----------DVKSQE--AALRAAPDILIATPgrliDHLH---NCPSF--HLSSIEVLILDE---- 338
Cdd:COG1201 98 APLEEIGEAAGLPLpeirvgvrtgDTPASErqRQRRRPPHILITTP----ESLAlllTSPDAreLLRGVRTVIVDEihal 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 339 ------ADRMLD-EYFEeqmkeiiRMCSHHRQTMLFSATMT--DEVKD-LASVSLKNPVRIfVNSNTDVAPFLR-----Q 403
Cdd:COG1201 174 agskrgVHLALSlERLR-------ALAPRPLQRIGLSATVGplEEVARfLVGYEDPRPVTI-VDAGAGKKPDLEvlvpvE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 404 EFIRIRPNREGDREAIVAALLmrtftDHVM------LFTQTKKQAHRMHILLGLLGLQVGEL----HGNLSQTQRLEALR 473
Cdd:COG1201 246 DLIERFPWAGHLWPHLYPRVL-----DLIEahrttlVFTNTRSQAERLFQRLNELNPEDALPiaahHGSLSREQRLEVEE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 124249330 474 RFKDEQIDILVAT---DVaarGLDIEGVKTVINFTMPNTVKHYVHRVGR 519
Cdd:COG1201 321 ALKAGELRAVVATsslEL---GIDIGDVDLVIQVGSPKSVARLLQRIGR 366
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
460-528 |
2.22e-06 |
|
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: 47.59 E-value: 2.22e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124249330 460 HGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGrtaRAGRAGR 528
Cdd:cd18794 61 HAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESG---RAGRDGL 126
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
228-541 |
2.88e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 51.08 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 228 AATGTGKTAAFALPVLERLIYK-------PRQAAVTRVLVLVPTRELG--------IQVHSVTKQLAQFCSITTCLAVG- 291
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFREggedtreAHKRKTSRILYISPIKALGtdvqrnlqIPLKGIADERRRRGETEVNLRVGi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 292 -GLDVKSQEAA--LRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDE----ADRMLDEYFEEQMKEIIRMCSHHRQT 364
Cdd:PRK09751 83 rTGDTPAQERSklTRNPPDILITTPESLYLMLTSRARETLRGVETVIIDEvhavAGSKRGAHLALSLERLDALLHTSAQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 365 MLFSATMTdEVKDLAS-------VSLKNP-------VRIF--VNSNTDVAPFLRQEFIRIRPNREGD-----REAIVAAL 423
Cdd:PRK09751 163 IGLSATVR-SASDVAAflggdrpVTVVNPpamrhpqIRIVvpVANMDDVSSVASGTGEDSHAGREGSiwpyiETGILDEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 424 LMRTFTdhvMLFTQTKKQAHRM-------HILLGLLGLQVGEL--------------------------HGNLSQTQRLE 470
Cdd:PRK09751 242 LRHRST---IVFTNSRGLAEKLtarlnelYAARLQRSPSIAVDaahfestsgatsnrvqssdvfiarshHGSVSKEQRAI 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124249330 471 ALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGrtaRAGR--AGRSVSLVGEEERKML 541
Cdd:PRK09751 319 TEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIG---RAGHqvGGVSKGLFFPRTRRDL 388
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
222-339 |
2.89e-06 |
|
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: 48.80 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 222 KDICACAATGTGKTaAFALPVLERLIYKPRQAAV--TRVLVLVPTRELGIQvhsvtkqlaQFCSIT--TCLAVG---GLD 294
Cdd:cd18034 17 RNTIVVLPTGSGKT-LIAVMLIKEMGELNRKEKNpkKRAVFLVPTVPLVAQ---------QAEAIRshTDLKVGeysGEM 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 124249330 295 VKSQEAALR-----AAPDILIATPGRLIDHLHNCpSFHLSSIEVLILDEA 339
Cdd:cd18034 87 GVDKWTKERwkeelEKYDVLVMTAQILLDALRHG-FLSLSDINLLIFDEC 135
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
361-542 |
8.49e-06 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 48.98 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 361 HRQTMLFSATMTDEVKD--LASVSLKNPvRIFVnsntdvAPFLRQE-FIRIRPNREGDREAIVAALLMRTFTDHVMLFTQ 437
Cdd:COG0514 166 NVPVLALTATATPRVRAdiAEQLGLEDP-RVFV------GSFDRPNlRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 438 TKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATdVA-ARGLDIEGVKTVINFTMPNTVKHYVHR 516
Cdd:COG0514 239 SRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQE 317
|
170 180
....*....|....*....|....*.
gi 124249330 517 VGRTARAGRAGRSVSLVGEEERKMLK 542
Cdd:COG0514 318 IGRAGRDGLPAEALLLYGPEDVAIQR 343
|
|
| UTP25 |
pfam06862 |
Utp25, U3 small nucleolar RNA-associated SSU processome protein 25; UTP25 is a family of ... |
307-408 |
1.03e-05 |
|
Utp25, U3 small nucleolar RNA-associated SSU processome protein 25; UTP25 is a family of eukaryotic proteins. The family displays limited sequence similarity to DEAD-box RNA helicases, having alternative residues at the Walker A and DEAD-box sites, but conservation of structural and other key residues. The domain is required and sufficient for the interaction of Utp25 with Utp3. UTP25 interacts with nucleolar protein Nop19 in S. cerevisiae, and Nop19p is essential for the incorporation of Utp25p into pre-ribosomes.
Pssm-ID: 369113 Cd Length: 471 Bit Score: 48.79 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 307 DILIATP-G-RLI----DHLHNCPSFhLSSIEVLILDEADRMLD---EYFEEQMKEI--------------IRM------ 357
Cdd:pfam06862 161 DIIIASPlGlRMIigneDKKKRDFDF-LSSIEVLIVDQADSIEMqnwEHVLTVFKHLnlipkeshgcdfsrVRMwyldgq 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 124249330 358 CSHHRQTMLFSATMTDEVKDLASVSLKN---PVRIFVNSNT----DVAPFLRQEFIRI 408
Cdd:pfam06862 240 AKYYRQTIVFSSYITPEINSLFNSKCHNiagKVRVKPIYKGgsigQVGLKVRQVFQRF 297
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
208-380 |
2.74e-05 |
|
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: 45.33 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 208 TPIQKACIPVGLL-GKDICACAATGTGKTAafalpVLERLIYKPRQAAVTRVLVLVPTRELGIQVH-SVTKQLAQFCsit 285
Cdd:cd17921 3 NPIQREALRALYLsGDSVLVSAPTSSGKTL-----IAELAILRALATSGGKAVYIAPTRALVNQKEaDLRERFGPLG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 286 tcLAVGGL--DVKSQEAALrAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDE----YFEEQMKEIIRMCS 359
Cdd:cd17921 75 --KNVGLLtgDPSVNKLLL-AEADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIGDGergvVLELLLSRLLRINK 151
|
170 180
....*....|....*....|.
gi 124249330 360 HHRqtMLFSATMTDEVKDLAS 380
Cdd:cd17921 152 NAR--FVGLSATLPNAEDLAE 170
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
200-343 |
4.96e-05 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain] Cd Length: 189 Bit Score: 44.63 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 200 TAMGFKqPTPIQKACIPVGLLGKDICACAATGTGKT---AAFALpvlerLIYKPRQaavtRVLVLVPTRELGIQVHSVTK 276
Cdd:cd17924 12 KKTGFP-PWGAQRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSL-----YLASKGK----RSYLIFPTKSLVKQAYERLS 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124249330 277 QLAQFCSITTCLAV--GGLDVKSQEAALRAAP----DILIATPGRLIDHLHNCPSFHLSSIevlILDEADRML 343
Cdd:cd17924 82 KYAEKAGVEVKILVyhSRLKKKEKEELLEKIEkgdfDILVTTNQFLSKNFDLLSNKKFDFV---FVDDVDAVL 151
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
201-393 |
5.58e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 44.83 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 201 AMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALP--VLERLiykprqaavtrVLVLVPTRELGI-QVHSVTKQ 277
Cdd:cd17920 7 VFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV-----------TLVVSPLISLMQdQVDRLQQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 278 LAQFCSITtclavGGLDVKSQEAALRAAP----DILIATPGRL-----IDHLHNCPSFHLssIEVLILDEA--------D 340
Cdd:cd17920 76 GIRAAALN-----STLSPEEKREVLLRIKngqyKLLYVTPERLlspdfLELLQRLPERKR--LALIVVDEAhcvsqwghD 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124249330 341 rmldeyFEEQMKEI--IRMCSHHRQTMLFSATMTDEVKDLASVSLK-NPVRIFVNS 393
Cdd:cd17920 149 ------FRPDYLRLgrLRRALPGVPILALTATATPEVREDILKRLGlRNPVIFRAS 198
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
432-507 |
1.18e-04 |
|
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: 42.46 E-value: 1.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124249330 432 VMLFTQTKKQAHRMHILLGLLGLQVGELHGNLSQTQRLEALRRFKDEQ--IDILVATDVAARGLDIEGVKTVINFTMP 507
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPW 107
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
219-338 |
3.69e-04 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 42.46 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 219 LLGKDICACAATGTGKTAAFALPVLERLIYKPRQAAVTRVLVLVPtrelgiQVHSVTKQLAQFCSIttCLAV-------G 291
Cdd:cd18036 15 LRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVN------KVPLVEQQLEKFFKY--FRKGykvtglsG 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 124249330 292 GLDVKSQEAALRAAPDILIATPGRLIDHLHN---CPSFHLSSIEVLILDE 338
Cdd:cd18036 87 DSSHKVSFGQIVKASDVIICTPQILINNLLSgreEERVYLSDFSLLIFDE 136
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
228-495 |
6.54e-04 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 43.15 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 228 AATGTGKT---AAFAL-----PVLERLIYK-PRQAAVT---RVLVLVPTRELGIqVHSvtkqLAQFcsiTTCLAVGGLDV 295
Cdd:COG1203 154 APTGGGKTeaaLLFALrlaakHGGRRIIYAlPFTSIINqtyDRLRDLFGEDVLL-HHS----LADL---DLLEEEEEYES 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 296 KSQEAALRA----APdILIATpgrlIDHL---------HNCPSFH--LSSieVLILDEADrMLDEYFEEQMKEIIRMCSH 360
Cdd:COG1203 226 EARWLKLLKelwdAP-VVVTT----IDQLfeslfsnrkGQERRLHnlANS--VIILDEVQ-AYPPYMLALLLRLLEWLKN 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 361 HRQTMLF-SATMTDEVKDLasvsLKNPVRIfVNSNTDVAPFLRQEFI--RIRPNREGDREAIVAALLMRTFTDH--VMLF 435
Cdd:COG1203 298 LGGSVILmTATLPPLLREE----LLEAYEL-IPDEPEELPEYFRAFVrkRVELKEGPLSDEELAELILEALHKGksVLVI 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124249330 436 TQTKKQAHRM--HILLGLLGLQVGELHGNLSQTQRLE----ALRRFKDEQIDILVATDVAARGLDI 495
Cdd:COG1203 373 VNTVKDAQELyeALKEKLPDEEVYLLHSRFCPADRSEiekeIKERLERGKPCILVSTQVVEAGVDI 438
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
210-346 |
4.68e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 38.65 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 210 IQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPrqaavTRVLVLVPTRELGIQVHSVTKQLaqFCSITTCLA 289
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLTKKG-----GKVLILAPSRPLVEQHAENLKRV--LNIPDKITS 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 124249330 290 VGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEY 346
Cdd:cd18035 78 LTGEVKPEERAERWDASKIIVATPQVIENDLLA-GRITLDDVSLLIFDEAHHAVGNY 133
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
456-495 |
4.92e-03 |
|
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: 38.48 E-value: 4.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 124249330 456 VGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDI 495
Cdd:cd18811 64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDV 103
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
455-498 |
5.23e-03 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 40.03 E-value: 5.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124249330 455 QVGELHGNLSQTQRLEALRRFKDEQIDILVATDVaargldIE-GV 498
Cdd:COG1200 505 RVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV------IEvGV 543
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
222-370 |
5.58e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.42 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249330 222 KDICACAATGTGKTA-AFALPvlERLIykpRQAAVTRVLVLVPTRELGIQVHSVTKQLAQFCSITTCLAVGGLDVKSQEA 300
Cdd:pfam04851 24 KRGLIVMATGSGKTLtAAKLI--ARLF---KKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDESVDD 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124249330 301 AlraapDILIATPGRLIDHLHNCP-SFHLSSIEVLILDEADRmldeYFEEQMKEIIRMCSHhrQTML-FSAT 370
Cdd:pfam04851 99 N-----KIVVTTIQSLYKALELASlELLPDFFDVIIIDEAHR----SGASSYRNILEYFKP--AFLLgLTAT 159
|
|
| |
