|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
1-380 |
0e+00 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 732.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 1 MTFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRILILT 80
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 81 PTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRML 160
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 161 DMGFSTVVNQIAAEARWRKQNLLFSATLEGKGVKTFAHDILNNPEIVEANPSRKEKNKIHQWYHLADDMNHKQALLVNIL 240
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEGDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCHLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 241 KQETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVINF 320
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 321 DMPRKADIYVHRIGRTGRAGAKGTAISLVEAHDFEMVTKAARYMGEPLKARVIDELRPKN 380
Cdd:PRK11192 321 DMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRPKT 380
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-380 |
2.44e-178 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 503.14 E-value: 2.44e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 1 MTFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLdypRKQPGATRILILT 80
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLD---PSRPRAPQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 81 PTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRML 160
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 161 DMGFSTVVNQIAAEARWRKQNLLFSATLEgKGVKTFAHDILNNPEIVEANPSRKEKNKIHQWYHLADDMnHKQALLVNIL 240
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMP-PEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR-DKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 241 KQETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVINF 320
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 321 DMPRKADIYVHRIGRTGRAGAKGTAISLVEAHDFEMVTKAARYMGEPLKARVIDELRPKN 380
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVE 376
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-380 |
2.37e-95 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 293.25 E-value: 2.37e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 1 MTFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPacqfLLDypRKQPGATRI--LI 78
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLG----LLQ--KLDVKRFRVqaLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 79 LTPTRELALQVyeqAVAITKhtqLVCG-----VIT--GGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECL 151
Cdd:PRK11776 78 LCPTRELADQV---AKEIRR---LARFipnikVLTlcGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 152 ILDEADRMLDMGFSTVVNQIAAEARWRKQNLLFSATLeGKGVKTFAHDILNNPEIVEANpSRKEKNKIHQWYHLADDmNH 231
Cdd:PRK11776 152 VLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATY-PEGIAAISQRFQRDPVEVKVE-STHDLPAIEQRFYEVSP-DE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 232 KQALLVNILKQETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDV 311
Cdd:PRK11776 229 RLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDI 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108505179 312 PNVSHVINFDMPRKADIYVHRIGRTGRAGAKGTAISLVEAHDFEMVTKAARYMGEPLKARVIDELRPKN 380
Cdd:PRK11776 309 KALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLS 377
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-353 |
2.29e-90 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 281.03 E-value: 2.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 3 FEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYP---RKQPGATRILIL 79
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPppkERYMGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 80 TPTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETL-SKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADR 158
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 159 MLDMGFSTVVNQIAAEA--RWRKQNLLFSATlegkgvktFAHDILN-------NPEIVEANPSRKEKNKIHQW-YHLADD 228
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTprKEERQTLLFSAT--------FTDDVMNlakqwttDPAIVEIEPENVASDTVEQHvYAVAGS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 229 MNHKqaLLVNILKQETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARG 308
Cdd:PRK01297 321 DKYK--LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRG 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1108505179 309 IDVPNVSHVINFDMPRKADIYVHRIGRTGRAGAKGTAISLVEAHD 353
Cdd:PRK01297 399 IHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
3-348 |
6.05e-90 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 278.01 E-value: 6.05e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 3 FEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYP---RKQPGATRILIL 79
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPapeDRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 80 TPTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRM 159
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 160 LDMGFstvVNQIaaeaRW--RKQ-------NLLFSATLEGKgVKTFAHDILNNPEIVEANPSRKEKNKIHQ--WYhlaDD 228
Cdd:PRK04837 170 FDLGF---IKDI----RWlfRRMppanqrlNMLFSATLSYR-VRELAFEHMNNPEYVEVEPEQKTGHRIKEelFY---PS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 229 MNHKQALLVNILKQETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARG 308
Cdd:PRK04837 239 NEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARG 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1108505179 309 IDVPNVSHVINFDMPRKADIYVHRIGRTGRAGAKGTAISL 348
Cdd:PRK04837 319 LHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-208 |
6.99e-90 |
|
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: 269.70 E-value: 6.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 12 LCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRILILTPTRELALQVYE 91
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 92 QAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVNQI 171
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1108505179 172 AAEARWRKQNLLFSATLEgKGVKTFAHDILNNPEIVE 208
Cdd:cd00268 161 LSALPKDRQTLLFSATLP-EEVKELAKKFLKNPVRIE 196
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-349 |
2.60e-89 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 277.46 E-value: 2.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 1 MTFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPG--ATRILI 78
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGrrPVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 79 LTPTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADR 158
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 159 MLDMGFSTVVNQIAAEARWRKQNLLFSATLEGKgVKTFAHDILNNPEIVEANPSRKEKNKIHQWYHLADDmNHKQALLVN 238
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDD-IKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDK-KRKRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 239 ILKQETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVI 318
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340 350
....*....|....*....|....*....|.
gi 1108505179 319 NFDMPRKADIYVHRIGRTGRAGAKGTAISLV 349
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLV 349
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-348 |
6.26e-79 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 254.10 E-value: 6.26e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 1 MTFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYP---RKQPGATRIL 77
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPalaDRKPEDPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 78 ILTPTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEK-EAADCRDIECLILDEA 156
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 157 DRMLDMGFSTVVNQIAAE--ARWRKQNLLFSATLEGKgVKTFAHDILNNPEIVEANPSRKEKNKIHQ-WYHLADDmnHKQ 233
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRmpERGTRQTLLFSATLSHR-VLELAYEHMNEPEKLVVETETITAARVRQrIYFPADE--EKQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 234 ALLVNILKQETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPN 313
Cdd:PRK04537 246 TLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDG 325
|
330 340 350
....*....|....*....|....*....|....*
gi 1108505179 314 VSHVINFDMPRKADIYVHRIGRTGRAGAKGTAISL 348
Cdd:PRK04537 326 VKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-364 |
7.43e-79 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 255.16 E-value: 7.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 1 MTFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPacqfLLDYPRKQPGATRILILT 80
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP----LLHNLDPELKAPQILVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 81 PTRELALQVYEQAVAITKHTQLVCGV-ITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRM 159
Cdd:PRK11634 82 PTRELAVQVAEAMTDFSKHMRGVNVVaLYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 160 LDMGFSTVVNQIAAEARWRKQNLLFSATLEgKGVKTFAHDILNNPEIVEANPSRKEKNKIHQWYHLADDMNHKQALlVNI 239
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMP-EAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEAL-VRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 240 LKQETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVIN 319
Cdd:PRK11634 240 LEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVN 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1108505179 320 FDMPRKADIYVHRIGRTGRAGAKGTAISLVEAHDFEMVTKAARYM 364
Cdd:PRK11634 320 YDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTM 364
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
2-366 |
1.72e-75 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 244.30 E-value: 1.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 2 TFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRI-LILT 80
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIvLVLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 81 PTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRML 160
Cdd:PTZ00110 211 PTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRML 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 161 DMGFSTVVNQIAAEARWRKQNLLFSATLEgKGVKTFAHDILNNpEIVEANPSR---KEKNKIHQWYHLADDmNHKQALLV 237
Cdd:PTZ00110 291 DMGFEPQIRKIVSQIRPDRQTLMWSATWP-KEVQSLARDLCKE-EPVHVNVGSldlTACHNIKQEVFVVEE-HEKRGKLK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 238 NILKQ--ETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVS 315
Cdd:PTZ00110 368 MLLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVK 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1108505179 316 HVINFDMPRKADIYVHRIGRTGRAGAKGTAISLVEAHDFEMVTKAARYMGE 366
Cdd:PTZ00110 448 YVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLRE 498
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
2-363 |
2.57e-68 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 221.62 E-value: 2.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 2 TFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQfLLDYPRKqpgATRILILTP 81
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQ-LIDYDLN---ACQALILAP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 82 TRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLD 161
Cdd:PTZ00424 105 TRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 162 MGFSTVVNQIAAEARWRKQNLLFSATLEGKgVKTFAHDILNNPEIVEANPSRKEKNKIHQWYHLADDMNHKQALLVNILK 241
Cdd:PTZ00424 185 RGFKGQIYDVFKKLPPDVQVALFSATMPNE-ILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 242 QETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVINFD 321
Cdd:PTZ00424 264 TLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYD 343
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1108505179 322 MPRKADIYVHRIGRTGRAGAKGTAISLVEAHDFEMVTKAARY 363
Cdd:PTZ00424 344 LPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERH 385
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
1-349 |
1.71e-63 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 212.34 E-value: 1.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 1 MTFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLP----ACQFLLDYP--RKQPGAt 74
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrCCTIRSGHPseQRNPLA- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 75 riLILTPTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILD 154
Cdd:PLN00206 200 --MVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 155 EADRMLDMGFSTVVNQIAaEARWRKQNLLFSATLEgKGVKTFAHDILNNPEIVEANPSRKEKNKIHQWYHLADDMNHKQA 234
Cdd:PLN00206 278 EVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVS-PEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 235 LLvNIL--KQETTTSAVVFVKTRDRLQMLKDFLA-SQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDV 311
Cdd:PLN00206 356 LF-DILksKQHFKPPAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
|
330 340 350
....*....|....*....|....*....|....*...
gi 1108505179 312 PNVSHVINFDMPRKADIYVHRIGRTGRAGAKGTAISLV 349
Cdd:PLN00206 435 LRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
15-204 |
8.30e-63 |
|
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: 200.56 E-value: 8.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 15 AVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPgATRILILTPTRELALQVYEQAV 94
Cdd:cd17947 4 ALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKA-ATRVLVLVPTRELAMQCFSVLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 95 AITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAA-DCRDIECLILDEADRMLDMGFSTVVNQIAA 173
Cdd:cd17947 83 QLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADELKEILR 162
|
170 180 190
....*....|....*....|....*....|.
gi 1108505179 174 EARWRKQNLLFSATLEGKgVKTFAHDILNNP 204
Cdd:cd17947 163 LCPRTRQTMLFSATMTDE-VKDLAKLSLNKP 192
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
2-208 |
2.00e-62 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 199.85 E-value: 2.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 2 TFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRkqpgATRILILTP 81
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ----RFFALVLAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 82 TRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEK-EAADCRDIECLILDEADRML 160
Cdd:cd17954 77 TRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEADRLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1108505179 161 DMGFSTVVNQIAAEARWRKQNLLFSATLEGKgVKTFAHDILNNPEIVE 208
Cdd:cd17954 157 NMDFEPEIDKILKVIPRERTTYLFSATMTTK-VAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
15-210 |
9.69e-59 |
|
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: 190.19 E-value: 9.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 15 AVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLdypRKQPGATR---ILILTPTRELALQVYE 91
Cdd:cd17941 4 GLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLY---RERWTPEDglgALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 92 QAVAITKHTQLVCGVITGGINYGTDKETLSkNLDILVATPGRLLEHIEKEAA-DCRDIECLILDEADRMLDMGFSTVVNQ 170
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVKEEKERIN-RMNILVCTPGRLLQHMDETPGfDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1108505179 171 IAAEARWRKQNLLFSATLEgKGVKTFAHDILNNPEIVEAN 210
Cdd:cd17941 160 IVENLPKSRQTLLFSATQT-KSVKDLARLSLKNPEYISVH 198
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
2-203 |
1.68e-58 |
|
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: 190.39 E-value: 1.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 2 TFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATR------ 75
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRrkayps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 76 ILILTPTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDE 155
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108505179 156 ADRMLDMGFSTVVNQIA-------AEARwrkQNLLFSATLEgKGVKTFAHDILNN 203
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVehpdmppKGER---QTLMFSATFP-REIQRLAADFLKN 211
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
219-349 |
1.88e-58 |
|
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: 186.94 E-value: 1.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 219 IHQWYHLADDMNHKQALLVNILKQETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPI 298
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1108505179 299 LLATDVAARGIDVPNVSHVINFDMPRKADIYVHRIGRTGRAGAKGTAISLV 349
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
8-202 |
8.49e-54 |
|
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: 177.78 E-value: 8.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 8 LDDALCHAVADMGFEAPTNIQELVIPHAL-DGRDILASAPTGTGKTAAFLLPACQFLL-DYPRKQPGATRILILTPTREL 85
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLnTKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 86 ALQVYEQAVAITKH-TQLVCGVITGGINYGTD-KETLSKNLDILVATPGRLLEHIEKE--AADCRDIECLILDEADRMLD 161
Cdd:cd17964 81 ALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAElNRLRRGRPDILVATPGRLIDHLENPgvAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1108505179 162 MGFSTVVNQI-----AAEARWRkQNLLFSATLEGKgVKTFAHDILN 202
Cdd:cd17964 161 MGFRPDLEQIlrhlpEKNADPR-QTLLFSATVPDE-VQQIARLTLK 204
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
2-207 |
1.12e-52 |
|
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: 174.80 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 2 TFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDypRKQPGATRILILTP 81
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKA--HSPTVGARALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 82 TRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLD 161
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1108505179 162 MGFSTVVNQIAAEARWRKQNLLFSATLEGKGVKtFAHDILNNPEIV 207
Cdd:cd17959 160 MGFAEQLHEILSRLPENRQTLLFSATLPKLLVE-FAKAGLNEPVLI 204
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
15-187 |
2.28e-52 |
|
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: 173.70 E-value: 2.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 15 AVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRILILTPTRELALQVYEQAV 94
Cdd:cd17942 4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYGVAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 95 AITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAA-DCRDIECLILDEADRMLDMGFSTVVNQIAA 173
Cdd:cd17942 84 ELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGfLYKNLQCLIIDEADRILEIGFEEEMRQIIK 163
|
170
....*....|....
gi 1108505179 174 EARWRKQNLLFSAT 187
Cdd:cd17942 164 LLPKRRQTMLFSAT 177
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
14-207 |
2.92e-52 |
|
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: 173.93 E-value: 2.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 14 HAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRK--QPGATRILILTPTRELALQVYE 91
Cdd:cd17949 4 HLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdRSDGTLALVLVPTRELALQIYE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 92 QAVAITK-HTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEK-EAADCRDIECLILDEADRMLDMGFSTVVN 169
Cdd:cd17949 84 VLEKLLKpFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDIT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1108505179 170 QIAAEARW-------------RKQNLLFSATLEgKGVKTFAHDILNNPEIV 207
Cdd:cd17949 164 KILELLDDkrskaggekskpsRRQTVLVSATLT-DGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
12-204 |
7.11e-52 |
|
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: 172.21 E-value: 7.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 12 LCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRI-LILTPTRELALQVY 90
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIaVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 91 EQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVNQ 170
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....
gi 1108505179 171 IAAEARWRKQNLLFSATLEGKgVKTFAHDILNNP 204
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKK-IEQLARDILSDP 193
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
25-188 |
1.47e-51 |
|
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: 170.12 E-value: 1.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 25 TNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLldypRKQPGATRILILTPTRELALQVYEQAVAITKHTQLVC 104
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 105 GVITGGINYGTDKETLsKNLDILVATPGRLLEHIEkEAADCRDIECLILDEADRMLDMGFSTVVNQIAAEARWRKQNLLF 184
Cdd:pfam00270 77 ASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
|
....
gi 1108505179 185 SATL 188
Cdd:pfam00270 155 SATL 158
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
3-189 |
4.11e-50 |
|
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: 167.79 E-value: 4.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 3 FEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLldypRKQPGATRILILTPT 82
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL----SEDPYGIFALVLTPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 83 RELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIE---KEAADCRDIECLILDEADRM 159
Cdd:cd17955 77 RELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRL 156
|
170 180 190
....*....|....*....|....*....|....
gi 1108505179 160 LDMGF----STVVNQIAAEarwrKQNLLFSATLE 189
Cdd:cd17955 157 LTGSFeddlATILSALPPK----RQTLLFSATLT 186
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
16-204 |
8.09e-50 |
|
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: 166.78 E-value: 8.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 16 VADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRI-LILTPTRELALQVYEQAV 94
Cdd:cd17966 5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIvLVLAPTRELAQQIQQEAN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 95 AITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVNQIAAE 174
Cdd:cd17966 85 KFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQ 164
|
170 180 190
....*....|....*....|....*....|
gi 1108505179 175 ARWRKQNLLFSATLEgKGVKTFAHDILNNP 204
Cdd:cd17966 165 IRPDRQTLMWSATWP-KEVRRLAEDFLKDY 193
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
3-206 |
1.50e-49 |
|
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: 166.32 E-value: 1.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 3 FEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLldYPRKqpGATRILILTPT 82
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI--DPKK--DVIQALILVPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 83 RELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDM 162
Cdd:cd17940 77 RELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1108505179 163 GFSTVVNQIAAEARWRKQNLLFSATLEgKGVKTFAHDILNNP-EI 206
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFP-LTVKNFMDRHMHNPyEI 200
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-204 |
1.30e-48 |
|
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: 163.91 E-value: 1.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 12 LCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDyPRKQPGAtRILILTPTRELALQVYE 91
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK-PRKKKGL-RALILAPTRELASQIYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 92 QAVAITKHTQLVCGVITGGINYGT-DKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVNQ 170
Cdd:cd17957 79 ELLKLSKGTGLRIVLLSKSLEAKAkDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDE 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1108505179 171 I-AAEARWRKQNLLFSATLeGKGVKTFAHDILNNP 204
Cdd:cd17957 159 IlAACTNPNLQRSLFSATI-PSEVEELARSVMKDP 192
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-202 |
1.67e-48 |
|
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: 165.53 E-value: 1.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 1 MTFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLL-------DYPRKQPGA 73
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkegltasSFSEVQEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 74 TriLILTPTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLIL 153
Cdd:cd18052 123 A--LIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLIL 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1108505179 154 DEADRMLDMGFSTVVNQIAAEARW----RKQNLLFSATLEGKgVKTFAHDILN 202
Cdd:cd18052 201 DEADRMLDMGFGPEIRKLVSEPGMpskeDRQTLMFSATFPEE-IQRLAAEFLK 252
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
15-188 |
1.62e-47 |
|
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: 161.20 E-value: 1.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 15 AVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDY----PRKQPGAtriLILTPTRELALQVY 90
Cdd:cd17960 4 VVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRkanlKKGQVGA---LIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 91 EQAVAITKH--TQLVCGVITGGINYGTDKETLSKN-LDILVATPGRLLEHIEKEAA--DCRDIECLILDEADRMLDMGFS 165
Cdd:cd17960 81 EVLQSFLEHhlPKLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSRKADkvKVKSLEVLVLDEADRLLDLGFE 160
|
170 180
....*....|....*....|....*
gi 1108505179 166 TVVNQIAaeARWRKQNL--LFSATL 188
Cdd:cd17960 161 ADLNRIL--SKLPKQRRtgLFSATQ 183
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
16-222 |
2.31e-46 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 158.04 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 16 VADMGFEAPTNIQELVIPHALDG-RDILASAPTGTGKTAAFLLPACQFLLDYPRKqpgatRILILTPTRELALQVYEQAV 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG-----RVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 95 AITKHTQLVCGVITGGINYGTDKETL-SKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVNQIAA 173
Cdd:smart00487 76 KLGPSLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1108505179 174 EARWRKQNLLFSATLEGKgVKTFAHDILNNPEIVeaNPSRKEKNKIHQW 222
Cdd:smart00487 156 LLPKNVQLLLLSATPPEE-IENLLELFLNDPVFI--DVGFTPLEPIEQF 201
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
14-220 |
6.55e-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: 157.79 E-value: 6.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 14 HAVADMGFEAPTNIQELVIPHAL-DGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRI-----LILTPTRELAL 87
Cdd:cd17946 3 RALADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQkplraLILTPTRELAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 88 QVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKE---AADCRDIECLILDEADRMLDMG- 163
Cdd:cd17946 83 QVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEKGh 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108505179 164 ---FSTVVNQI----AAEARWRkQNLLFSATLegkgvkTFAHDILNNPEIVEANPSRKEKNKIH 220
Cdd:cd17946 163 faeLEKILELLnkdrAGKKRKR-QTFVFSATL------TLDHQLPLKLNSKKKKKKKEKKQKLE 219
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
8-207 |
1.21e-45 |
|
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: 156.20 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 8 LDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDY--PRKQPGATRILILTPTREL 85
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAkaESGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 86 ALQVYEQAVAITKH-TQLV-CGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEA-ADCRDIECLILDEADRMLDM 162
Cdd:cd17961 81 AQQVSKVLEQLTAYcRKDVrVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSlLLLSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1108505179 163 GFSTVVNQIAAEARWRKQNLLFSATLeGKGVKTFAHDILNNPEIV 207
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATL-SEDVEALKKLVLHNPAIL 204
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
3-208 |
2.61e-45 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 155.56 E-value: 2.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 3 FEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFlldyprkqpgaTRILILTPT 82
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-----------VVALILEPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 83 RELALQVYEQAVAITKHT---QLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRM 159
Cdd:cd17938 70 RELAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108505179 160 LDMGFSTVVNQI------AAEARWRKQNLLFSATLEGKGVKTFAHDILNNPEIVE 208
Cdd:cd17938 150 LSQGNLETINRIynripkITSDGKRLQVIVCSATLHSFEVKKLADKIMHFPTWVD 204
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
15-207 |
8.67e-44 |
|
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: 152.09 E-value: 8.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 15 AVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPrKQPGATRI-----LILTPTRELALQV 89
Cdd:cd17945 4 VIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLP-PLDEETKDdgpyaLILAPTRELAQQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 90 YEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVN 169
Cdd:cd17945 83 EEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108505179 170 QI--------------------AAEARWRKQNLLFSATLEgKGVKTFAHDILNNPEIV 207
Cdd:cd17945 163 KIldampvsnkkpdteeaeklaASGKHRYRQTMMFTATMP-PAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
19-206 |
1.92e-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: 148.29 E-value: 1.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 19 MGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRI-LILTPTRELALQVYEQAVAIT 97
Cdd:cd17953 30 LGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEGPIgLIMAPTRELALQIYVECKKFS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 98 KHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAA---DCRDIECLILDEADRMLDMGFSTVVNQIAAE 174
Cdd:cd17953 110 KALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGrvtNLRRVTYVVLDEADRMFDMGFEPQIMKIVNN 189
|
170 180 190
....*....|....*....|....*....|...
gi 1108505179 175 ARWRKQNLLFSATLEgKGVKTFAHDILNNP-EI 206
Cdd:cd17953 190 IRPDRQTVLFSATFP-RKVEALARKVLHKPiEI 221
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
2-203 |
4.34e-40 |
|
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: 143.26 E-value: 4.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 2 TFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPAC-QFLLDYP------------- 67
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILsQIYEQGPgeslpsesgyygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 68 RKQ-PGAtriLILTPTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCR 146
Cdd:cd18051 102 RKQyPLA---LVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108505179 147 DIECLILDEADRMLDMGFST----VVNQIAAEARWRKQNLLFSATLEgKGVKTFAHDILNN 203
Cdd:cd18051 179 YCKYLVLDEADRMLDMGFEPqirrIVEQDTMPPTGERQTLMFSATFP-KEIQMLARDFLDN 238
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
12-204 |
8.01e-39 |
|
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: 138.07 E-value: 8.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 12 LCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYpRKQPGAtriLILTPTRELALQVYE 91
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTE-HRNPSA---LILTPTRELAVQIED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 92 QAVAITKHT-QLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVNQ 170
Cdd:cd17962 77 QAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
|
170 180 190
....*....|....*....|....*....|....
gi 1108505179 171 IAAEARWRKQNLLFSATLEgKGVKTFAHDILNNP 204
Cdd:cd17962 157 ILENISHDHQTILVSATIP-RGIEQLAGQLLQNP 189
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
15-207 |
4.62e-38 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350709 [Multi-domain] Cd Length: 206 Bit Score: 136.31 E-value: 4.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 15 AVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRI----LILTPTRELALQVY 90
Cdd:cd17951 4 GLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLPFIKGEgpygLIVCPSRELARQTH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 91 EQAVAITKH------TQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGF 164
Cdd:cd17951 84 EVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1108505179 165 STVVNQIAAEARWRKQNLLFSATLEGKgVKTFAHDILNNPEIV 207
Cdd:cd17951 164 EEDIRTIFSYFKGQRQTLLFSATMPKK-IQNFAKSALVKPVTV 205
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
19-207 |
6.78e-38 |
|
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: 135.67 E-value: 6.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 19 MGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPAcqFL-LDY---PRKQPGATRILILTPTRELALQVYEQav 94
Cdd:cd17958 8 QGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPG--FIhLDLqpiPREQRNGPGVLVLTPTRELALQIEAE-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 95 aITKHT----QLVCgvITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVNQ 170
Cdd:cd17958 84 -CSKYSykglKSVC--VYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1108505179 171 IAAEARWRKQNLLFSATLEgKGVKTFAHDILNNPEIV 207
Cdd:cd17958 161 ILLDIRPDRQTIMTSATWP-DGVRRLAQSYLKDPMIV 196
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
5-214 |
2.99e-37 |
|
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: 133.99 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 5 ELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPAcqfLLDYPRKQPgATRILILTPTRE 84
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGA---LQRIDTTVR-ETQALVLAPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 85 LALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGF 164
Cdd:cd17939 77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1108505179 165 STVVNQIAAEARWRKQNLLFSAtlegkgvkTFAHDILNNPEIVEANPSRK 214
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSA--------TMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
18-203 |
4.16e-36 |
|
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: 133.21 E-value: 4.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 18 DMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRI-LILTPTRELALQVYEQAVAI 96
Cdd:cd18050 79 DQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPIcLVLAPTRELAQQVQQVADDY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 97 TKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVNQIAAEAR 176
Cdd:cd18050 159 GKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR 238
|
170 180
....*....|....*....|....*..
gi 1108505179 177 WRKQNLLFSATLEgKGVKTFAHDILNN 203
Cdd:cd18050 239 PDRQTLMWSATWP-KEVRQLAEDFLRD 264
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
1-203 |
6.05e-36 |
|
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: 131.67 E-value: 6.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 1 MTFEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRI-LIL 79
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPIcLVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 80 TPTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRM 159
Cdd:cd18049 104 APTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1108505179 160 LDMGFSTVVNQIAAEARWRKQNLLFSATLEgKGVKTFAHDILNN 203
Cdd:cd18049 184 LDMGFEPQIRKIVDQIRPDRQTLMWSATWP-KEVRQLAEDFLKD 226
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
15-187 |
1.15e-35 |
|
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: 129.69 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 15 AVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLldypRKQPGATRILILTPTRELALQVYEQAV 94
Cdd:cd17943 4 GLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL----DLERRHPQVLILAPTREIAVQIHDVFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 95 AITKH-TQLVCGVITGGINYGTDKETLsKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVNQIAA 173
Cdd:cd17943 80 KIGKKlEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFS 158
|
170
....*....|....
gi 1108505179 174 EARWRKQNLLFSAT 187
Cdd:cd17943 159 SLPKNKQVIAFSAT 172
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
232-340 |
1.57e-35 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 126.56 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 232 KQALLVNILKQETTTSAVVFVKTRDRLQmLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDV 311
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 1108505179 312 PNVSHVINFDMPRKADIYVHRIGRTGRAG 340
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
12-188 |
3.26e-34 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 126.98 E-value: 3.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 12 LCHAVADMGFEAPTNIQELVIPHALDG---------RDILASAPTGTGKTAAFLLPACQFLLDYPRKQpgaTRILILTPT 82
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPR---LRALIVVPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 83 RELALQVYEQAVAITKHTQLVCGVITGGINygTDKET----------LSKNLDILVATPGRLLEHI-EKEAADCRDIECL 151
Cdd:cd17956 78 KELVQQVYKVFESLCKGTGLKVVSLSGQKS--FKKEQklllvdtsgrYLSRVDILVATPGRLVDHLnSTPGFTLKHLRFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1108505179 152 ILDEADRMLDMGF----STVVNQIAAE--------------ARWRK--QNLLFSATL 188
Cdd:cd17956 156 VIDEADRLLNQSFqdwlETVMKALGRPtapdlgsfgdanllERSVRplQKLLFSATL 212
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
3-188 |
4.45e-34 |
|
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: 125.64 E-value: 4.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 3 FEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQfLLDYPRKqpgATRILILTPT 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQ-QIDTSLK---ATQALVLAPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 83 RELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDM 162
Cdd:cd18046 77 RELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSR 156
|
170 180
....*....|....*....|....*.
gi 1108505179 163 GFSTVVNQIAAEARWRKQNLLFSATL 188
Cdd:cd18046 157 GFKDQIYDIFQKLPPDTQVVLLSATM 182
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
3-208 |
6.61e-34 |
|
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: 125.54 E-value: 6.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 3 FEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLldypRKQPGATRILILTPT 82
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL----EPVDGQVSVLVICHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 83 RELALQVYEQAVAITKH-TQLVCGVITGGINYGTDKETLSKNL-DILVATPGRLLEHIEKEAADCRDIECLILDEADRML 160
Cdd:cd17950 80 RELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKML 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1108505179 161 -DMGFSTVVNQIAAEARWRKQNLLFSATLEgKGVKTFAHDILNNPEIVE 208
Cdd:cd17950 160 eQLDMRRDVQEIFRATPHDKQVMMFSATLS-KEIRPVCKKFMQDPLEIF 207
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
3-213 |
7.69e-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: 124.89 E-value: 7.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 3 FEELELDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKqpgaTRILILTPT 82
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRE----TQALILSPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 83 RELALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDM 162
Cdd:cd18045 77 RELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1108505179 163 GFSTVVNQIAAEARWRKQNLLFSATLegkgvktfAHDILNNPEIVEANPSR 213
Cdd:cd18045 157 GFKEQIYDVYRYLPPATQVVLVSATL--------PQDILEMTNKFMTDPIR 199
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
27-187 |
1.60e-32 |
|
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: 121.49 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 27 IQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLL--DYPRKQPGATRILILTPTRELALQVYEQAVAITKHTQLVC 104
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQedQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITRKLSVAC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 105 gvITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVNQI-----AAEARWRK 179
Cdd:cd17944 96 --FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIlsvsyKKDSEDNP 173
|
....*...
gi 1108505179 180 QNLLFSAT 187
Cdd:cd17944 174 QTLLFSAT 181
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
8-207 |
4.11e-30 |
|
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: 114.98 E-value: 4.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 8 LDDALCHAVADMGFEAPTNIQELVIPHALDG--RDILASAPTGTGKTAAFLLpACQFLLDYPRKQPGAtriLILTPTREL 85
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVL-AMLSRVDPTLKSPQA---LCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 86 ALQVYEQAVAITKHTQLVCGVITGGINYGTDKETLSKnldILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDM-GF 164
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKITAQ---IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1108505179 165 STVVNQIAAEARWRKQNLLFSATLEgKGVKTFAHDILNNPEIV 207
Cdd:cd17963 154 GDQSIRIKRMLPRNCQILLFSATFP-DSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
12-171 |
2.11e-28 |
|
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: 111.30 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 12 LCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGAT---RILILTPTRELALQ 88
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFnapRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 89 VYEQAVAITKHTQLVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVV 168
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
...
gi 1108505179 169 NQI 171
Cdd:cd17948 161 SHF 163
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
259-340 |
1.99e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 103.83 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 259 QMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVINFDMPRKADIYVHRIGRTGR 338
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1108505179 339 AG 340
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
2-216 |
2.51e-24 |
|
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: 100.10 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 2 TFEELELDDALCHAVADMGFEAPTNIQELVIPHALDG--RDILASAPTGTGKTAAFLLpACQFLLDYPRKQPgatRILIL 79
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVL-AMLSRVDALKLYP---QCLCL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 80 TPTRELALQ---VYEQAVAITKHTQLVCGVITGGINYGTDKETlsknlDILVATPGRLLEHIEK-EAADCRDIECLILDE 155
Cdd:cd18048 95 SPTFELALQtgkVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEA-----QIVIGTPGTVLDWCFKlRLIDVTNISVFVLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108505179 156 ADRMLDM-GFSTVVNQIAAEARWRKQNLLFSATLEgKGVKTFAHDILNNPEIVEAnpsRKEK 216
Cdd:cd18048 170 ADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFE-DSVWAFAERIVPDPNIIKL---KKEE 227
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
37-362 |
2.53e-21 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 95.86 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 37 DGRDILASAPTGTGKTAAFLLPACQFLLDYprkqpgatRILILTPTRELALQVYEQAVAITKhtqlvcgvitGGINYGTD 116
Cdd:COG1061 99 GGGRGLVVAPTGTGKTVLALALAAELLRGK--------RVLVLVPRRELLEQWAEELRRFLG----------DPLAGGGK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 117 KETlskNLDILVATPGRLLEHIEKEAADcRDIECLILDEADRMLDMGFSTVVNQIAAEARwrkqnLLFSATLE---GKGV 193
Cdd:COG1061 161 KDS---DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRRILEAFPAAYR-----LGLTATPFrsdGREI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 194 KTFAHD---------------ILNNPEI----VEANPSRKEKNKIHQWY--HLADDMNHKQALLVNILKQETTTSAV-VF 251
Cdd:COG1061 232 LLFLFDgivyeyslkeaiedgYLAPPEYygirVDLTDERAEYDALSERLreALAADAERKDKILRELLREHPDDRKTlVF 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 252 VKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVInFDMPRK-ADIYV 330
Cdd:COG1061 312 CSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPTGsPREFI 390
|
330 340 350
....*....|....*....|....*....|....
gi 1108505179 331 HRIGRTGR-AGAKGTA-ISLVEAHDFEMVTKAAR 362
Cdd:COG1061 391 QRLGRGLRpAPGKEDAlVYDFVGNDVPVLEELAK 424
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
2-208 |
2.44e-18 |
|
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: 82.85 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 2 TFEELELDDALCHAVADMGFEAPTNIQELVIPHAL--DGRDILASAPTGTGKTAAFLL-------PACQFlldyprkqpg 72
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLaePPQNLIAQSQSGTGKTAAFVLamlsqvePANKY---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 73 aTRILILTPTRELALQ---VYEQAVAITKHTQLVCGVITGGINYGTDKETlsknlDILVATPGRLLEH-IEKEAADCRDI 148
Cdd:cd18047 72 -PQCLCLSPTYELALQtgkVIEQMGKFYPELKLAYAVRGNKLERGQKISE-----QIVIGTPGTVLDWcSKLKFIDPKKI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108505179 149 ECLILDEADRML-DMGFSTVVNQIAAEARWRKQNLLFSATLEgKGVKTFAHDILNNPEIVE 208
Cdd:cd18047 146 KVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFE-DSVWKFAQKVVPDPNVIK 205
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
3-188 |
4.22e-17 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 80.11 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 3 FEELEL---------DDALCHAVADMGFEAPTNIQELVIPHAL---------------DGRDI-LASAPTGTGKTAAFLL 57
Cdd:cd17965 1 FDQLKLlpsvreaiiKEILKGSNKTDEEIKPSPIQTLAIKKLLktlmrkvtkqtsneePKLEVfLLAAETGSGKTLAYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 58 PacqfLLDY-----------------PRKQPGATRILILTPTRELALQVYEQAVAITKHTQLVCGVITGGIN--YGTDKE 118
Cdd:cd17965 81 P----LLDYlkrqeqepfeeaeeeyeSAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGpsYQRLQL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 119 TLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVNQIAAEARWRKQNLLFSATL 188
Cdd:cd17965 157 AFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATI 226
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
38-187 |
4.56e-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: 74.75 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 38 GRDILASAPTGTGKTAAFLLPACQFLLDYPRKqpgatrILILTPTRELALQVYEQAVAITKHtQLVCGVITGGINYGTDK 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGKK------VLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEERE 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108505179 118 ETLSKNLDILVATPGRLLEHIEKEAADC-RDIECLILDEADRMLDMGFSTVVNQIAAEARWRKQN--LLFSAT 187
Cdd:cd00046 74 KNKLGDADIIIATPDMLLNLLLREDRLFlKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAqvILLSAT 146
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
226-344 |
3.66e-14 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 74.38 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 226 ADDMNHKQALLVNILKQETTTS----AVVFVKTRDRLQMLKDFLASQDIQVCWLQGE--------MPQDKRNTAMARFKS 293
Cdd:COG1111 330 ADIEHPKLSKLREILKEQLGTNpdsrIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRA 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 294 GEVPILLATDVAARGIDVPNVSHVINFDmPRKADI-YVHRIGRTGRAG--------AKGT 344
Cdd:COG1111 410 GEFNVLVATSVAEEGLDIPEVDLVIFYE-PVPSEIrSIQRKGRTGRKRegrvvvliAKGT 468
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
28-366 |
1.68e-13 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 71.71 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 28 QELVIPHALDGRDILASAPTGTGKTAAFLLPAcqfLLdyprkQPGATriLILTPTreLAL---QVyEQAVAItkhtqlvc 104
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPA---LL-----LPGLT--LVVSPL--IALmkdQV-DALRAA-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 105 GV----ITGGINYGTDKETLSK----NLDILVATPGRL-----LEHIEKeaadcRDIECLILDEA--------D-----R 158
Cdd:COG0514 81 GIraafLNSSLSAEERREVLRAlragELKLLYVAPERLlnprfLELLRR-----LKISLFAIDEAhcisqwghDfrpdyR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 159 MLdmgfSTVVNQIAAEARwrkqnLLFSATlegkgvktfA-----HDI-----LNNPEIVEANPSRKekNkIHqwYHLAD- 227
Cdd:COG0514 156 RL----GELRERLPNVPV-----LALTAT---------AtprvrADIaeqlgLEDPRVFVGSFDRP--N-LR--LEVVPk 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 228 DMNHKQALLVNILKQETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATdVA-A 306
Cdd:COG0514 213 PPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfG 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 307 RGIDVPNVSHVINFDMPRKADIYVHRIGRTGRAGAKGTAISLVEAHDFEMvtkaARYMGE 366
Cdd:COG0514 292 MGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAI----QRFFIE 347
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
236-342 |
1.38e-12 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 64.53 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 236 LVNILK----QETTTSAVVFVKTRDRLQMLKDFLA-----SQDIQVCWLQG----------EMPQDKRNTAMARFKSGEV 296
Cdd:cd18802 12 LIEILReyfpKTPDFRGIIFVERRATAVVLSRLLKehpstLAFIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGEL 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1108505179 297 PILLATDVAARGIDVPNVSHVINFDMPRKADIYVHRIGRTGRAGAK 342
Cdd:cd18802 92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSK 137
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
232-334 |
7.24e-12 |
|
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: 62.49 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 232 KQALLVNILKQ--ETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVP--ILLATDVAAR 307
Cdd:cd18793 12 KLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|....*...
gi 1108505179 308 GIDVPNVSHVINFDMP-----------RkadiyVHRIG 334
Cdd:cd18793 92 GLNLTAANRVILYDPWwnpaveeqaidR-----AHRIG 124
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
34-156 |
3.42e-11 |
|
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: 62.28 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 34 HALDgRDILASAPTGTGKT--AAFLLPAcqFLLDYPRKQPGATRILILTPTRELALQvyeQAVAITKHTQLVCGVITG-- 109
Cdd:cd18034 13 AALK-RNTIVVLPTGSGKTliAVMLIKE--MGELNRKEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGem 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1108505179 110 GINYGTD---KETLSKNlDILVATPGRLLEHIEKEAADCRDIECLILDEA 156
Cdd:cd18034 87 GVDKWTKerwKEELEKY-DVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
235-349 |
5.93e-11 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 64.12 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 235 LLVNILKQETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGE--------MPQDKRNTAMARFKSGEVPILLATDVAA 306
Cdd:PRK13766 355 IVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAE 434
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1108505179 307 RGIDVPNVSHVInFDMPRKADI-YVHRIGRTGRaGAKGTAISLV 349
Cdd:PRK13766 435 EGLDIPSVDLVI-FYEPVPSEIrSIQRKGRTGR-QEEGRVVVLI 476
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
25-156 |
2.19e-10 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 59.20 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 25 TNIQELVIPHA-LDGRDILASAPTGTGKTAAFLLpacqFLLDYPRKQPGatRILILTPTRELALQVYEQAVAITKHTQLV 103
Cdd:cd17921 3 NPIQREALRALyLSGDSVLVSAPTSSGKTLIAEL----AILRALATSGG--KAVYIAPTRALVNQKEADLRERFGPLGKN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1108505179 104 CGVITGgiNYGTDKETLSKNlDILVATPGRLLEHIEKEAADC-RDIECLILDEA 156
Cdd:cd17921 77 VGLLTG--DPSVNKLLLAEA-DILVATPEKLDLLLRNGGERLiQDVRLVVVDEA 127
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-156 |
2.28e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 62.22 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 1 MTFEELELDDALcHAVADMGFEAPTNIQELVIPHAL-DGRDILASAPTGTGKTAAFLLPACQFLldyprKQPGatRILIL 79
Cdd:COG1204 1 MKVAELPLEKVI-EFLKERGIEELYPPQAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKAL-----LNGG--KALYI 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108505179 80 TPTRELALQVYEQAVAITKHTQLVCGVITGgiNYGTDKETLSKNlDILVATPGRLLEHIEKEAADCRDIECLILDEA 156
Cdd:COG1204 73 VPLRALASEKYREFKRDFEELGIKVGVSTG--DYDSDDEWLGRY-DILVATPEKLDSLLRNGPSWLRDVDLVVVDEA 146
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
298-354 |
4.12e-10 |
|
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: 55.79 E-value: 4.12e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1108505179 298 ILLATDVAARGIDVPNVSHVINFDMPRKADIYVHRIGRTGRAGAKGtaislVEAHDF 354
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE-----GEVILF 76
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
8-353 |
4.87e-10 |
|
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: 61.39 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 8 LDDALCHAVADMGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRkqpgaTRILILTPTRELAl 87
Cdd:COG1205 41 LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPG-----ATALYLYPTKALA- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 88 qvYEQAVAITKHTQLV-----CGVITGGINyGTDKETLSKNLDILVATP-----GrLLEHIEKEAADCRDIECLILDEA- 156
Cdd:COG1205 115 --RDQLRRLRELAEALglgvrVATYDGDTP-PEERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARFFRNLRYVVIDEAh 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 157 --------------DRMLdmgfstvvnQIAAEARWRKQNLLFSATL----------------------EGKGVKTFAhdi 200
Cdd:COG1205 191 tyrgvfgshvanvlRRLR---------RICRHYGSDPQFILASATIgnpaehaerltgrpvtvvdedgSPRGERTFV--- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 201 LNNPEIVEANPSRkeknkiHQWYHLADdmnhkqaLLVNILKQETTTsaVVFVKTRDR----LQMLKDFLASQDI--QVCW 274
Cdd:COG1205 259 LWNPPLVDDGIRR------SALAEAAR-------LLADLVREGLRT--LVFTRSRRGaellARYARRALREPDLadRVAA 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108505179 275 LQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVINFDMPRKADIYVHRIGRTGRAGAKGTAIsLVEAHD 353
Cdd:COG1205 324 YRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGDD 401
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
230-336 |
5.05e-10 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 61.39 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 230 NHKQALLVNILKQETTTS--AVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVP--ILLATDVA 305
Cdd:COG0553 532 SAKLEALLELLEELLAEGekVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAG 611
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1108505179 306 ARGIDVPNVSHVINFDMP-----------RkadiyVHRIGRT 336
Cdd:COG0553 612 GEGLNLTAADHVIHYDLWwnpaveeqaidR-----AHRIGQT 648
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
21-378 |
1.07e-09 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 60.50 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 21 FEAPTNIQELVIPHALDGRDILASAPTGTGKT-AAFlLPACQFLLDYPRKQPGA--TRILILTPTRELALQVY---EQAV 94
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPdgLRVLYISPLKALANDIErnlRAPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 95 A-ITKHTQLVCGVITGGINYG----TDKETLSKNL-DILVATPGRLleHI----EKEAADCRDIECLILDEA-------- 156
Cdd:COG1201 101 EeIGEAAGLPLPEIRVGVRTGdtpaSERQRQRRRPpHILITTPESL--ALlltsPDARELLRGVRTVIVDEIhalagskr 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 157 -----------DRMLDMGFSTV-----VNQIAAEARW--RKQNLLFSATLEGKGVKTFahDI---LNNPEIVEANPSRKe 215
Cdd:COG1201 179 gvhlalslerlRALAPRPLQRIglsatVGPLEEVARFlvGYEDPRPVTIVDAGAGKKP--DLevlVPVEDLIERFPWAG- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 216 knkiHQWYHLADDmnhkqalLVNILKQETTTsaVVFVKTR---DRL-QMLKDFLASQDIQVCWLQGEMPQDKRNTAMARF 291
Cdd:COG1201 256 ----HLWPHLYPR-------VLDLIEAHRTT--LVFTNTRsqaERLfQRLNELNPEDALPIAAHHGSLSREQRLEVEEAL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 292 KSGEVPILLAT---DVaarGIDVPNVSHVINFDMPRKADIYVHRIGRTG-RAGAKGTAIsLVEAHDFEMV-----TKAAR 362
Cdd:COG1201 323 KAGELRAVVATsslEL---GIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEVSKGR-LVPTHRDELVecaaaLEAAR 398
|
410
....*....|....*.
gi 1108505179 363 ymgeplkARVIDELRP 378
Cdd:COG1201 399 -------AGEIEARRP 407
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
214-338 |
2.31e-09 |
|
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: 55.44 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 214 KEKNKIHQwyhladDMNHKQALLVNILKQE---TTTSAVVFVKTRDRLQMLKDFLASQD--IQVCWLQGE--------MP 280
Cdd:cd18801 2 RKVEKIHP------KLEKLEEIVKEHFKKKqegSDTRVIIFSEFRDSAEEIVNFLSKIRpgIRATRFIGQasgksskgMS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108505179 281 QDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVINFDmPRKADI-YVHRIGRTGR 338
Cdd:cd18801 76 QKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYD-ASPSPIrMIQRMGRTGR 133
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
45-342 |
3.48e-09 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 57.82 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 45 APTGTGKTAAFLLPACQFLldyprKQPGATRILILTPTRELALQVYEQAVAITKHTQLVCGVITG-GINYGTDKETL--- 120
Cdd:cd09639 6 APTGYGKTEAALLWALHSL-----KSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILSsRIKEMGDSEEFehl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 121 ----SKNLDILVATPGRL--LEHIEKEAADC---RDI-------ECLILDEADRMLD--MGFSTVVNQIAAEarWRKQNL 182
Cdd:cd09639 81 fplyIHSNDTLFLDPITVctIDQVLKSVFGEfghYEFtlasianSLLIFDEVHFYDEytLALILAVLEVLKD--NDVPIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 183 LFSATLEgKGVKTFAHDIlnnpEIVEANPSRKEKN-KIHQWYHLADDM----NHKQALLVNILKQettTSAVVFVKTRDR 257
Cdd:cd09639 159 LMSATLP-KFLKEYAEKI----GYVEENEPLDLKPnERAPFIKIESDKvgeiSSLERLLEFIKKG---GSVAIIVNTVDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 258 LQ----MLKDFLASQDIQVcwLQGEMPQ----DKRNTAMARFKSGEVPILLATDVAARGIDvpnvshvINFDM----PRK 325
Cdd:cd09639 231 AQefyqQLKEKGPEEEIML--IHSRFTEkdraKKEAELLLEFKKSEKFVIVATQVIEASLD-------ISVDVmiteLAP 301
|
330
....*....|....*..
gi 1108505179 326 ADIYVHRIGRTGRAGAK 342
Cdd:cd09639 302 IDSLIQRLGRLHRYGEK 318
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
28-378 |
7.01e-09 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 57.95 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 28 QELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRILILTPTRELALQVYEQAVAITKHTQLVC--G 105
Cdd:TIGR04121 18 QLEMWAAALEGRSGLLIAPTGSGKTLAGFLPSLIDLAGPEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGLPIrvE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 106 VITGGINYGTDKETLSKNLDILVATPGRL---LEHieKEAADC-RDIECLILDE-----------------------ADR 158
Cdd:TIGR04121 98 TRTGDTSSSERARQRKKPPDILLTTPESLallLSY--PDAARLfKDLRCVVVDEwhelagskrgdqlelalarlrrlAPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 159 MLDMGFSTVVNQIAAEARW-----RKQNLLFSATLEGKgvktfAHDILNNPEIVEANPsrkeknkihqWY-HLAddmnhK 232
Cdd:TIGR04121 176 LRRWGLSATIGNLEEARRVllgvgGAPAVLVRGKLPKA-----IEVISLLPESEERFP----------WAgHLG-----L 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 233 QAL--LVNILKQETTTsaVVFVKTRDR----LQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAA 306
Cdd:TIGR04121 236 RALpeVYAEIDQARTT--LVFTNTRSQaelwFQALWEANPEFALPIALHHGSLDREQRRWVEAAMAAGRLRAVVCTSSLD 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108505179 307 RGIDVPNVSHVINFDMPRKADIYVHRIGRTG-RAGAKGTAIsLVEAHDFEMV-TKAARymgEPLKARVIDELRP 378
Cdd:TIGR04121 314 LGVDFGPVDLVIQIGSPKGVARLLQRAGRSNhRPGEPSRAL-LVPTNRLELLeCAAAR---EAVAAGAVEGRPP 383
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
260-340 |
3.86e-08 |
|
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: 52.35 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 260 MLKDFLASqDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVINFDMPRKADIYVHRI-GRTGR 338
Cdd:cd18811 53 YLKERFRP-ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGR 131
|
..
gi 1108505179 339 AG 340
Cdd:cd18811 132 GD 133
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
27-131 |
1.03e-07 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 51.97 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 27 IQELVIPHALDG-RDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGATRILILTPTRELALQVYEQAVAITKHTQLVCG 105
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCA 84
|
90 100
....*....|....*....|....*.
gi 1108505179 106 VITGGINYGTDKETlsKNLDILVATP 131
Cdd:cd18023 85 ELTGDTEMDDTFEI--QDADIILTTP 108
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
28-353 |
1.10e-07 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 53.95 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 28 QELVIPHALDGRDILASAPTGTGKTAAFLLPAcqfLLdyprkQPGATriLILTPTRELALQVYEQAVAitkhtqlvCGVI 107
Cdd:PRK11057 30 QQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPA---LV-----LDGLT--LVVSPLISLMKDQVDQLLA--------NGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 108 TGGINYGTDKETL--------SKNLDILVATPGRL-----LEHIEKeaadcRDIECLILDEADRMLDMGFS-----TVVN 169
Cdd:PRK11057 92 AACLNSTQTREQQlevmagcrTGQIKLLYIAPERLmmdnfLEHLAH-----WNPALLAVDEAHCISQWGHDfrpeyAALG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 170 QIaaeaRWRKQNLLFSAtLEGKGVKTFAHDI-----LNNPEIveaNPSRKEKNKIHqwYHLADdmNHKQ-ALLVNILKQE 243
Cdd:PRK11057 167 QL----RQRFPTLPFMA-LTATADDTTRQDIvrllgLNDPLI---QISSFDRPNIR--YTLVE--KFKPlDQLMRYVQEQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 244 TTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVINFDMP 323
Cdd:PRK11057 235 RGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIP 314
|
330 340 350
....*....|....*....|....*....|
gi 1108505179 324 RKADIYVHRIGRTGRAGAKGTAISLVEAHD 353
Cdd:PRK11057 315 RNIESYYQETGRAGRDGLPAEAMLFYDPAD 344
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
42-158 |
1.72e-07 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 50.78 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 42 LASAPTGTGKTaaflLPACQFLLDYPRKQPGAtRILILTPTRELALQVYEQAVAITKHTQLVCGVITGGINYGTDKEtLS 121
Cdd:cd18033 20 LVALPTGLGKT----FIAAVVMLNYYRWFPKG-KIVFMAPTKPLVSQQIEACYKITGIPSSQTAELTGSVPPTKRAE-LW 93
|
90 100 110
....*....|....*....|....*....|....*..
gi 1108505179 122 KNLDILVATPGRLLEHIEKEAADCRDIECLILDEADR 158
Cdd:cd18033 94 ASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHR 130
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
275-350 |
1.82e-07 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 50.34 E-value: 1.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108505179 275 LQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVINFDMPR--KADIYVHRiGRTGRAGAKGTAISLVE 350
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRfgLSQLHQLR-GRVGRGKHQSYCYLLYP 142
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
36-210 |
2.36e-07 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 50.41 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 36 LDGRDILASAPTGTGKTAAFLLPACQFLLDyprkqpgATRILILTPTRELALQVYEQaVAITKHTQLVCGVITGgiNYGT 115
Cdd:cd18028 15 LKGENLLISIPTASGKTLIAEMAMVNTLLE-------GGKALYLVPLRALASEKYEE-FKKLEEIGLKVGISTG--DYDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 116 DKETLSKNlDILVATPGRLLEHIEKEAADCRDIECLILDEADRMLDMGFSTVVNQIAAEARWRKQNLLF---SATLegKG 192
Cdd:cd18028 85 DDEWLGDY-DIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRRLNPNTQIiglSATI--GN 161
|
170
....*....|....*...
gi 1108505179 193 VKTFAHDIlnNPEIVEAN 210
Cdd:cd18028 162 PDELAEWL--NAELVESD 177
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
24-158 |
2.50e-07 |
|
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: 50.89 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 24 PTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGatRILILTPTRELALQvyeQAVAITKHTQLV 103
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKG--KVVFLANKVPLVEQ---QKEVFRKHFERP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108505179 104 ---CGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEK-EAADCRDIECLILDEADR 158
Cdd:cd17927 78 gykVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-156 |
5.45e-07 |
|
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: 49.51 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 28 QELVIPHALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRkqpgaTRILILTPTRELAlqvYEQAVAITK-----HTQL 102
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPG-----SRALYLYPTKALA---QDQLRSLRElleqlGLGI 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108505179 103 VCGVITGGINYGTDKETLSKNLDILVATPGRL----LEHIEKEAADCRDIECLILDEA 156
Cdd:cd17923 77 RVATYDGDTPREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
275-352 |
9.10e-07 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 48.11 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 275 LQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVSHVI--NFDMPRKADIYVHRiGRTGRAGAKGTAISLVEAH 352
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQLR-GRVGRSKERAYAYFLYPDQ 135
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
256-315 |
2.51e-06 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 49.66 E-value: 2.51e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 256 DRLQMLKDFLAsqDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVS 315
Cdd:COG1200 492 ETYEELREAFP--GLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNAT 549
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
219-340 |
4.01e-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: 46.05 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 219 IHQWYHLADDMNHKQALLVNILKQETTTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPI 298
Cdd:cd18794 4 LFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQV 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1108505179 299 LLATdVA-ARGIDVPNVSHVINFDMPRKADIYVHRIGRTGRAG 340
Cdd:cd18794 84 IVAT-VAfGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
44-188 |
5.54e-06 |
|
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: 45.76 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 44 SAPTGTGKTA-AFLLPAcqfllDYPRKqpgatRILILTPTRELALQVYEQAVAITKHTQLvcGVITGGINYGTDKEtlsk 122
Cdd:cd17926 24 VLPTGSGKTLtALALIA-----YLKEL-----RTLIVVPTDALLDQWKERFEDFLGDSSI--GLIGGGKKKDFDDA---- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108505179 123 nlDILVATPgRLLEHIEKEAADCRDiEC--LILDEADRMLDMGFSTVVNQIAAEARwrkqnLLFSATL 188
Cdd:cd17926 88 --NVVVATY-QSLSNLAEEEKDLFD-QFglLIVDEAHHLPAKTFSEILKELNAKYR-----LGLTATP 146
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
22-158 |
5.91e-06 |
|
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: 46.35 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 22 EAPTNIQELVIPHALDGrDILASAPTGTGKTAAFLLPACQflldypRKQPGATRILILTPTRELALQVYEQAVAITkHTQ 101
Cdd:cd18035 1 EERRLYQVLIAAVALNG-NTLIVLPTGLGKTIIAILVAAD------RLTKKGGKVLILAPSRPLVEQHAENLKRVL-NIP 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1108505179 102 LVCGVITGGINyGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLILDEADR 158
Cdd:cd18035 73 DKITSLTGEVK-PEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
37-94 |
1.21e-05 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 47.23 E-value: 1.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108505179 37 DGRDILASAPTGTGKTAAFLLPACQFLLDYPRKqpgatrILILTPTRelALQvyEQAV 94
Cdd:COG1199 32 EGRHLLIEAGTGTGKTLAYLVPALLAARETGKK------VVISTATK--ALQ--EQLV 79
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
38-131 |
2.27e-05 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 44.50 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 38 GRDILASAPTGTGKTAAFLLPACQFLLDYPRKqpgATRILILTPTRELALQVYE--QAVAITKHTQLVCGVITGGINYGT 115
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEK---GVQVLYISPLKALINDQERrlEEPLDEIDLEIPVAVRHGDTSQSE 77
|
90
....*....|....*.
gi 1108505179 116 DKETLSKNLDILVATP 131
Cdd:cd17922 78 KAKQLKNPPGILITTP 93
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
22-158 |
3.62e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 43.81 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 22 EAPTNIQELVIPHAldgRDILASAPTGTGKTAAFLlpacqFLLDYPRKQPGATRILILTPTRELALQVYEqavAITKHtq 101
Cdd:pfam04851 10 EAIENLLESIKNGQ---KRGLIVMATGSGKTLTAA-----KLIARLFKKGPIKKVLFLVPRKDLLEQALE---EFKKF-- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108505179 102 LVCGVITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRD--IECLILDEADR 158
Cdd:pfam04851 77 LPNYVEIGEIISGDKKDESVDDNKIVVTTIQSLYKALELASLELLPdfFDVIIIDEAHR 135
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
20-194 |
3.80e-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: 44.24 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 20 GFEaPTNIQELVIPHALDGRDILASAPTGTGKTAaFLLPACQFLldYPRKQpgatRILILTPTRELALQVYEQavaITKH 99
Cdd:cd17924 15 GFP-PWGAQRTWAKRLLRGKSFAIIAPTGVGKTT-FGLATSLYL--ASKGK----RSYLIFPTKSLVKQAYER---LSKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 100 TQLVCG-----VITGGINyGTDKETLSKNL-----DILVATPGRLLEHIEKEAAdcRDIECLILDEAD----------RM 159
Cdd:cd17924 84 AEKAGVevkilVYHSRLK-KKEKEELLEKIekgdfDILVTTNQFLSKNFDLLSN--KKFDFVFVDDVDavlkssknidRL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1108505179 160 LDM-GFSTVVnqIAaearwrkqnllfSATLEGKGVK 194
Cdd:cd17924 161 LKLlGFGQLV--VS------------SATGRPRGIR 182
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
19-60 |
4.50e-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: 44.06 E-value: 4.50e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1108505179 19 MGFEAPTNIQELVIPHALDGRDILASAPTGTGKTAAFLLPAC 60
Cdd:cd17920 8 FGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL 49
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
229-343 |
5.98e-05 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 43.01 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 229 MN-HKQALLVNILKQ-ETTTSAVVFVktrDRLQMLKDflASQDIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAA 306
Cdd:cd18789 31 MNpNKLRALEELLKRhEQGDKIIVFT---DNVEALYR--YAKRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGD 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1108505179 307 RGIDVP--NVSHVI--NFDMPRKadiYVHRIGRTGRAGAKG 343
Cdd:cd18789 106 EGIDLPeaNVAIQIsgHGGSRRQ---EAQRLGRILRPKKGG 143
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
269-315 |
1.02e-04 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 44.37 E-value: 1.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1108505179 269 DIQVCWLQGEMPQDKRNTAMARFKSGEVPILLATDVAARGIDVPNVS 315
Cdd:PRK10917 505 ELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNAT 551
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
39-187 |
1.45e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 42.40 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 39 RDILASAPTGTGKTAAFLLPAcqfLLDYPRKQpgatRILILTPTRELALQVYEQAVaiTKHTQLVCGVITGGInygtdKE 118
Cdd:cd17918 37 MDRLLSGDVGSGKTLVALGAA---LLAYKNGK----QVAILVPTEILAHQHYEEAR--KFLPFINVELVTGGT-----KA 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 119 TLSKNLDILVATPGRLLEHIEKEAADcrdieCLILDEADRMldmgfstVVNQIAAEARWRKQNLL-FSAT 187
Cdd:cd17918 103 QILSGISLLVGTHALLHLDVKFKNLD-----LVIVDEQHRF-------GVAQREALYNLGATHFLeATAT 160
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
18-158 |
2.10e-04 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain] Cd Length: 163 Bit Score: 41.39 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 18 DMGFEAPTNIQELVIphalDGRD-ILASAPTGTGKT--AAFLlpaCQFLLDYPRKQpgatRILILTPTRELAlqvyEQAv 94
Cdd:cd18032 3 YYQQEAIEALEEARE----KGQRrALLVMATGTGKTytAAFL---IKRLLEANRKK----RILFLAHREELL----EQA- 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108505179 95 aiTKHTQLVCGVITGGINYGTDKETLSKnlDILVATPGRLLEHIEKEAADCRDIECLILDEADR 158
Cdd:cd18032 67 --ERSFKEVLPDGSFGNLKGGKKKPDDA--RVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHH 126
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
21-56 |
2.27e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 43.34 E-value: 2.27e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1108505179 21 FEAPTNIQELVIPHALDGRDILASAPTGTGKT-AAFL 56
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL 66
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
28-156 |
3.16e-04 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 41.47 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 28 QELVIPHALDGRDILASAPTGTGKTAAFLLPAcqflLDYPRKQPGATriLILTPTREL------ALQVYEQAVAITkHTQ 101
Cdd:cd18018 17 QEEAIARLLSGRSTLVVLPTGAGKSLCYQLPA----LLLRRRGPGLT--LVVSPLIALmkdqvdALPRAIKAAALN-SSL 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1108505179 102 lvcgviTGGINYGTDKETLSKNLDILVATPGRLL-EHIEKEAADCRDIECLILDEA 156
Cdd:cd18018 90 ------TREERRRILEKLRAGEVKILYVSPERLVnESFRELLRQTPPISLLVVDEA 139
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
45-155 |
8.94e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 41.83 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 45 APTGTGKTAAFLLPACQFLL-----DYPRKQPGA-TRILILTPTRELA------LQVYEQAVAITKH------TQLVCGV 106
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFreggeDTREAHKRKtSRILYISPIKALGtdvqrnLQIPLKGIADERRrrgeteVNLRVGI 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1108505179 107 ITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADC-RDIECLILDE 155
Cdd:PRK09751 83 RTGDTPAQERSKLTRNPPDILITTPESLYLMLTSRARETlRGVETVIIDE 132
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
215-338 |
1.18e-03 |
|
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: 39.17 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 215 EKNKIHQW-YHLADDMnHKQaLLVNILKQETTtsaVVFVKTR-------DRLQMLKDFLASQDIQVCWlQGEMPQDKRNT 286
Cdd:cd18796 12 VAPEIFPWaGESGADA-YAE-VIFLLERHKST---LVFTNTRsqaerlaQRLRELCPDRVPPDFIALH-HGSLSRELREE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1108505179 287 AMARFKSGEVPILLATDVAARGIDVPNVSHVINFDMPRKADIYVHRIGRTGR 338
Cdd:cd18796 86 VEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
29-155 |
1.30e-03 |
|
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: 39.77 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 29 ELVIPhALDGRDILASAPTGTGKTAAFLLpACQFLLDYPRKQPGATRILILTPTRELalqVYEQAVAITKHTQLVCGV-- 106
Cdd:cd18036 9 ELVLP-ALRGKNTIICAPTGSGKTRVAVY-ICRHHLEKRRSAGEKGRVVVLVNKVPL---VEQQLEKFFKYFRKGYKVtg 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1108505179 107 ITGGINYGTDKETLSKNLDILVATP----GRLLEHIEKEAADCRDIECLILDE 155
Cdd:cd18036 84 LSGDSSHKVSFGQIVKASDVIICTPqiliNNLLSGREEERVYLSDFSLLIFDE 136
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
211-340 |
2.12e-03 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members 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: 350178 [Multi-domain] Cd Length: 171 Bit Score: 38.67 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 211 PSRKEKNKIHQWYHLADDMNHKQALLVNILKQETTTSAVVFV-------KTRDRLQMLKDFLASQDIQVCWLQGEMPQDK 283
Cdd:cd18791 9 EDILELLGISSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLpgqeeieRLCELLREELLSPDLGKLLVLPLHSSLPPEE 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108505179 284 RNTAMARFKSGEVPILLATDVAARGIDVPNVSHVINFDMpRKADIYVHRIG----------------RTGRAG 340
Cdd:cd18791 89 QQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGL-VKEKVYDPRTGlsslvtvwiskasaeqRAGRAG 160
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
245-335 |
3.20e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 37.15 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 245 TTSAVVFVKTRDRLQMLKDFLASQDIQVCWLQGEMPQDKRNTAMA-RFKSGE--VPILLATDVAARGIDVPNVSHVInFD 321
Cdd:cd18799 6 EIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEALiLLFFGElkPPILVTVDLLTTGVDIPEVDNVV-FL 84
|
90
....*....|....*
gi 1108505179 322 MP-RKADIYVHRIGR 335
Cdd:cd18799 85 RPtESRTLFLQMLGR 99
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
24-155 |
3.83e-03 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain] Cd Length: 202 Bit Score: 38.26 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108505179 24 PTNIQ-ELVIPhALDGRDILASAPTGTGKTAAFLLPACQFLLDYPRKQPGatRILILTPTrelaLQVYEQAVAITKH--- 99
Cdd:cd18073 3 PRNYQlELALP-AMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKG--KVVFFATK----VPVYEQQKSVFSKyfe 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108505179 100 --TQLVCGvITGGINYGTDKETLSKNLDILVATPGRLLEHIEKEAADCRDIECLIL-DE 155
Cdd:cd18073 76 rhGYRVTG-ISGATAENVPVEQIIENNDIIILTPQILVNNLKKGTIPSLSIFTLMIfDE 133
|
|
| |
