|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-629 |
0e+00 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 1280.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 1 MAEFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVL 80
Cdd:PRK11634 1 MAEFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 81 APTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
Cdd:PRK11634 81 APTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFL 240
Cdd:PRK11634 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320
Cdd:PRK11634 241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 321 DIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLEKFAAKVQQQLESSDL 400
Cdd:PRK11634 321 DIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLEKFAAKVQQQLESSDL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 401 DQYRALLSKIQPTAEGEELDLETLAAALLKMAQGERTLIVPPDAPMRPKREFRDRDDRGPRDRNDRGPRGDREDRPRRER 480
Cdd:PRK11634 401 DQYRALLAKIQPTAEGEELDLETLAAALLKMAQGERPLILPPDAPMRPKREFRDRDDRGPRDRNDRGPRGDREDRPRRER 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 481 RDVGDMQLYRIEVGRDDGVEVRHIVGAIANEGDISSRYIGNIKLFASHSTIELPKGMPGEVLQHFTRTRILNKPMNMQLL 560
Cdd:PRK11634 481 RDVGDMQLYRIEVGRDDGVEVRHIVGAIANEGDISSRYIGNIKLFASHSTIELPKGMPGEVLQHFTRTRILNKPMNMQLL 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111550 561 GDAQPHTGGERRGGGRGFGGERREGGRNFSGERREGGRGDGRRFSGERREGRAPRRDDSTGRRRFGGDA 629
Cdd:PRK11634 561 GDAQPHTGGERRGGGRGFGGERREGGRNFSGERREGGRGDGRRFSGERREGRAPRRDDSTGRRRFGGDA 629
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
5-399 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 605.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 5 ETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPEL-KAPQILVLAPT 83
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 84 RELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLR 163
Cdd:COG0513 81 RELALQVAEELRKLAKYL-GLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 164 MGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAE 243
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 244 DFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIP 323
Cdd:COG0513 240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111550 324 MDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLEKFAAKVQQQLESSD 399
Cdd:COG0513 320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKK 395
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
6-385 |
3.82e-138 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 410.73 E-value: 3.82e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRE 85
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 86 LAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG 165
Cdd:PRK11776 84 LADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQsSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDF 245
Cdd:PRK11776 164 FQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVE-STHDLPAIEQRFYEVSPDERLPALQRLLLHHQP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
Cdd:PRK11776 243 ESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARD 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 326 SESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLE 385
Cdd:PRK11776 323 PEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLL 382
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
6-365 |
2.92e-113 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 346.16 E-value: 2.92e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLD--PELK--APQILVLA 81
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdfPRRKsgPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 82 PTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
Cdd:PRK11192 81 PTRELAMQVADQARELAKHT-HLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 162 LRMGFIEDVETIMAQIPEGHQTALFSATMP-EAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALVRF 239
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEhKTALLCHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 240 LEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVN 319
Cdd:PRK11192 240 LKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVIN 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 90111550 320 YDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMK 365
Cdd:PRK11192 320 FDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIE 365
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
17-209 |
1.17e-104 |
|
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: 314.77 E-value: 1.17e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPEL----KAPQILVLAPTRELAVQVAE 92
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 93 AMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVET 172
Cdd:cd00268 81 VARKLGKGT-GLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 90111550 173 IMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVR 209
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
7-377 |
4.65e-98 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 307.51 E-value: 4.65e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQ------ILVL 80
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 81 APTRELAVQVAEAMTDFSKHMRGVNVVaLYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLV-VFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFL 240
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 90111550 321 DIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAE 377
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYE 377
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
5-348 |
1.71e-93 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 294.57 E-value: 1.71e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 5 ETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP----LLQNLDPELKA---PQI 77
Cdd:PRK04837 7 EQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKvnqPRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 78 LVLAPTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDE 157
Cdd:PRK04837 87 LIMAPTRELAVQIHADAEPLAQAT-GLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 158 ADEMLRMGFIEDVETIMAQIPEGHQ--TALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEA 235
Cdd:PRK04837 166 ADRMFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 236 LVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERIS 315
Cdd:PRK04837 246 LQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVT 325
|
330 340 350
....*....|....*....|....*....|...
gi 90111550 316 LVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
Cdd:PRK04837 326 HVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
2-379 |
2.25e-86 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 277.56 E-value: 2.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 2 AEFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP----LLQNLDPE---LKA 74
Cdd:PRK01297 83 QEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISiinqLLQTPPPKeryMGE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 75 PQILVLAPTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALR-QGPQIVVGTPGRLLDHLKRGTLDLSKLSGL 153
Cdd:PRK01297 163 PRALIIAPTRELVVQIAKDAAALTKYT-GLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVM 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 154 VLDEADEMLRMGFIEDVETIMAQIP--EGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR 231
Cdd:PRK01297 242 VLDEADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311
Cdd:PRK01297 322 KYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHI 401
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111550 312 ERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIpEVELPNAELL 379
Cdd:PRK01297 402 DGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKI-SCEMPPAELL 468
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
7-379 |
1.36e-85 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 273.24 E-value: 1.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTREL 86
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTREL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 87 AVQ---VAEAMTDFSKhmrgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLR 163
Cdd:PTZ00424 109 AQQiqkVVLALGDYLK----VRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 164 MGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTV----WgmrKNEALVRF 239
Cdd:PTZ00424 185 RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVekeeW---KFDTLCDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 240 LEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVN 319
Cdd:PTZ00424 262 YETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVIN 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 320 YDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
Cdd:PTZ00424 342 YDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
7-379 |
1.43e-80 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 265.28 E-value: 1.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAF---------SLPLLQNLDPElkAPQI 77
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFlvavmnrllSRPALADRKPE--DPRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 78 LVLAPTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKR-GTLDLSKLSGLVLD 156
Cdd:PRK04537 88 LILAPTRELAIQIHKDAVKFGADL-GLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 157 EADEMLRMGFIEDVETIMAQIPE--GHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNE 234
Cdd:PRK04537 167 EADRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 235 ALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERI 314
Cdd:PRK04537 247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111550 315 SLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPeVELPNAELL 379
Cdd:PRK04537 327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIP-VEPVTAELL 390
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
6-365 |
2.77e-79 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 261.25 E-value: 2.77e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQ--NLDPELK---APQILVL 80
Cdd:PTZ00110 130 VSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVhiNAQPLLRygdGPIVLVL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 81 APTRELAVQVAEAMTDFSKHMRGVNVVAlYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
Cdd:PTZ00110 210 APTRELAEQIREQCNKFGASSKIRNTVA-YGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKE-PQEVRIQS-SVTTRPDISQSYWTVWGMRKNEALVR 238
Cdd:PTZ00110 289 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSlDLTACHNIKQEVFVVEEHEKRGKLKM 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 239 FLEA--EDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISL 316
Cdd:PTZ00110 369 LLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKY 448
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 90111550 317 VVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMK 365
Cdd:PTZ00110 449 VINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLR 497
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
8-207 |
1.44e-67 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 219.02 E-value: 1.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELA 87
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 88 VQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLK---RGTLDLSKLSGLVLDEADEMLRM 164
Cdd:cd17955 81 YQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90111550 165 GFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQE 207
Cdd:cd17955 160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFF 202
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
8-208 |
3.48e-66 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 215.24 E-value: 3.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELA 87
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 88 VQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
Cdd:cd17940 81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 90111550 168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEV 208
Cdd:cd17940 160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
7-211 |
4.57e-66 |
|
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: 214.87 E-value: 4.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLdpeLKAPQ---ILVLAPT 83
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL---LENPQrffALVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 84 RELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGT-LDLSKLSGLVLDEADEML 162
Cdd:cd17954 78 RELAQQISEQFEALGSSI-GLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 90111550 163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPqeVRIQ 211
Cdd:cd17954 157 NMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP--VKIE 203
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
10-210 |
6.09e-66 |
|
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: 214.50 E-value: 6.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 10 DLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELAVQ 89
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 90 VAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIED 169
Cdd:cd17939 81 IQKVVKALGDYM-GVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 90111550 170 VETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPqeVRI 210
Cdd:cd17939 160 IYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDP--VRI 198
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
7-203 |
4.88e-63 |
|
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: 207.72 E-value: 4.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNL--DPELKA--------PQ 76
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLleDGPPSVgrgrrkayPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 77 ILVLAPTRELAVQVAEAMTDFSKHmRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLD 156
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYR-SGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90111550 157 EADEMLRMGFIEDVETIMAQ----IPEGHQTALFSATMPEAIRRITRRFMK 203
Cdd:cd17967 160 EADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLK 210
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
30-197 |
8.55e-63 |
|
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: 205.17 E-value: 8.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 30 SPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHMrGVNVVAL 109
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 110 YGGQRYDVQLRALRqGPQIVVGTPGRLLDHLKRgTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTALFSAT 189
Cdd:pfam00270 80 LGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157
|
....*...
gi 90111550 190 MPEAIRRI 197
Cdd:pfam00270 158 LPRNLEDL 165
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
6-204 |
2.79e-60 |
|
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: 202.12 E-value: 2.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNL---------DPELKAPQ 76
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegltassFSEVQEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 77 ILVLAPTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLD 156
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGT-CIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILD 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 90111550 157 EADEMLRMGFIEDVETIMAQ--IP--EGHQTALFSATMPEAIRRITRRFMKE 204
Cdd:cd18052 202 EADRMLDMGFGPEIRKLVSEpgMPskEDRQTLMFSATFPEEIQRLAAEFLKE 253
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
7-386 |
1.64e-59 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 207.72 E-value: 1.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNL-------DPELKAPQILV 79
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCctirsghPSEQRNPLAMV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 80 LAPTRELAVQVAEAMTDFSKHM--RGVNVValyGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDE 157
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLpfKTALVV---GGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 158 ADEMLRMGFIEDVETIMAQIPEGhQTALFSATMPEAIRRITRRFMKEPQEVRIQSSvtTRPDISQSYWTVW--GMRKNEA 235
Cdd:PLN00206 279 VDCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNP--NRPNKAVKQLAIWveTKQKKQK 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 236 LVRFLEAEDF--DAAIIFVRTKNATLEVAEALER-NGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVE 312
Cdd:PLN00206 356 LFDILKSKQHfkPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLL 435
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111550 313 RISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRL---LRNIERTMKLTIPEvELPNAELLGKRRLEK 386
Cdd:PLN00206 436 RVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLfpeLVALLKSSGAAIPR-ELANSRYLGSGRKRK 511
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
7-209 |
2.97e-59 |
|
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: 197.14 E-value: 2.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQI--LVLAPTR 84
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGAraLILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 85 ELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRM 164
Cdd:cd17959 82 ELALQTLKVTKELGKFT-DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 90111550 165 GFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVR 209
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
17-205 |
3.08e-59 |
|
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: 197.54 E-value: 3.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLD--PELKA------PQILVLAPTRELAV 88
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlPPLDEetkddgPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 89 QVAEAMTDFSKHmRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIE 168
Cdd:cd17945 81 QIEEETQKFAKP-LGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90111550 169 DVETIMAQIPEGH--------------------QTALFSATMPEAIRRITRRFMKEP 205
Cdd:cd17945 160 QVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRP 216
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
17-211 |
4.65e-59 |
|
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: 196.32 E-value: 4.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNL---DPELKAPQILVLAPTRELAVQVAEA 93
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 94 MTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRG-TLDLSKLSGLVLDEADEMLRMGFIEDVET 172
Cdd:cd17947 81 LQQLAQFT-DITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKE 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 90111550 173 IMAQIPEGHQTALFSATMPEAIRRITRRFMKEPqeVRIQ 211
Cdd:cd17947 160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKP--VRVF 196
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
8-210 |
8.67e-59 |
|
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: 195.74 E-value: 8.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELA 87
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 88 VQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
Cdd:cd18046 81 QQIQKVVMALGDYM-GIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90111550 168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPqeVRI 210
Cdd:cd18046 160 DQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP--IRI 200
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
6-210 |
3.16e-58 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350708 [Multi-domain] Cd Length: 208 Bit Score: 194.49 E-value: 3.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRE 85
Cdd:cd17950 2 SGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 86 LAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALR-QGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLR- 163
Cdd:cd17950 82 LAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEq 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 90111550 164 MGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRI 210
Cdd:cd17950 162 LDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
17-208 |
5.45e-57 |
|
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: 190.66 E-value: 5.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQ--NLDPELK---APQILVLAPTRELAVQVA 91
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVhiNAQPPLErgdGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 92 EAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVE 171
Cdd:cd17966 81 QEANKFG-GSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 90111550 172 TIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEV 208
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
6-208 |
2.73e-56 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 189.90 E-value: 2.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNL--DPELKA---PQILVL 80
Cdd:cd17953 12 QKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIkdQRPVKPgegPIGLIM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 81 APTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHL---KRGTLDLSKLSGLVLDE 157
Cdd:cd17953 92 APTRELALQIYVECKKFSKAL-GLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90111550 158 ADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEV 208
Cdd:cd17953 171 ADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
17-205 |
5.19e-56 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 188.56 E-value: 5.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNL------DPELKAPQILVLAPTRELAVQV 90
Cdd:cd17961 5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 91 AEAMTDFSKHMRG-VNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTL-DLSKLSGLVLDEADEMLRMGFIE 168
Cdd:cd17961 85 SKVLEQLTAYCRKdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGYEE 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 90111550 169 DVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEP 205
Cdd:cd17961 165 DLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
21-222 |
2.23e-55 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 186.54 E-value: 2.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 21 LNDLGYEKPSPIQAECIPHLLNG-RDVLGMAQTGSGKTAAFSLPLLQNLDPElKAPQILVLAPTRELAVQVAEAMTDFSK 99
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 100 HMrGVNVVALYGGQRYDVQLRALRQG-PQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIP 178
Cdd:smart00487 80 SL-GLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 90111550 179 EGHQTALFSATMPEAIRRITRRFMKEPqeVRIQSSVTTRPDISQ 222
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQ 200
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
17-210 |
2.81e-55 |
|
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350710 [Multi-domain] Cd Length: 197 Bit Score: 186.47 E-value: 2.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNL--DPELKA---PQILVLAPTRELAVQVA 91
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImdQRELEKgegPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 92 EAMTDFSKhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVE 171
Cdd:cd17952 81 LEAKKFGK-AYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 90111550 172 TIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPqeVRI 210
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDP--IRV 196
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
220-349 |
1.16e-54 |
|
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: 182.32 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 220 ISQSYWTVWGMRKNEAL-VRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDI 298
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 90111550 299 LIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFV 349
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
13-209 |
1.58e-54 |
|
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: 184.32 E-value: 1.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 13 LKAPILEALNDLGYEKPSPIQAECIPHLLNG--RDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELAVQ- 89
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 90 --VAEAMTDFSkhmrGVNV-VALYGGQRYdvqlRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRM-G 165
Cdd:cd17963 81 geVVEKMGKFT----GVKVaLAVPGNDVP----RGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 90111550 166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVR 209
Cdd:cd17963 153 HGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
17-209 |
1.48e-53 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 181.31 E-value: 1.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELAVQVAEAMTD 96
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 97 FSKHMRGVNVVALYGGQRYDVQLRALRqGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQ 176
Cdd:cd17943 81 IGKKLEGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|...
gi 90111550 177 IPEGHQTALFSATMPEAIRRITRRFMKEPQEVR 209
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
13-204 |
2.89e-53 |
|
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: 181.24 E-value: 2.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 13 LKAPILEALNDLGYEKPSPIQAECIPHLL-NGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQ-----ILVLAPTREL 86
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRrsgvsALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 87 AVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRAL-RQGPQIVVGTPGRLLDHLK--RGTLDLSKLSGLVLDEADEMLR 163
Cdd:cd17964 81 ALQIAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 90111550 164 MGFIEDVETIMAQIP----EGHQTALFSATMPEAIRRITRRFMKE 204
Cdd:cd17964 161 MGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLKK 205
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
8-210 |
1.68e-52 |
|
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: 179.20 E-value: 1.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELA 87
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 88 VQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
Cdd:cd18045 81 VQIQKVLLALGDYM-NVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90111550 168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPqeVRI 210
Cdd:cd18045 160 EQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDP--IRI 200
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
17-210 |
1.97e-52 |
|
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: 178.92 E-value: 1.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPL---LQNLDPELKAPQI--LVLAPTRELAVQVA 91
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVleiLLKRKANLKKGQVgaLIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 92 EAMTDFSKHMRGVNVVALY-GGQRYDVQLRAL-RQGPQIVVGTPGRLLDHLKRGT--LDLSKLSGLVLDEADEMLRMGFI 167
Cdd:cd17960 81 EVLQSFLEHHLPKLKCQLLiGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90111550 168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPqeVRI 210
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNP--VRV 201
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
17-208 |
1.99e-50 |
|
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: 173.42 E-value: 1.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPEL------KAPQILVLAPTRELAVQV 90
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPipreqrNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 91 AEAMTDFSkhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDV 170
Cdd:cd17958 81 EAECSKYS--YKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 90111550 171 ETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEV 208
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
17-210 |
2.12e-50 |
|
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: 173.16 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQI--LVLAPTRELAVQVAEAM 94
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLraLILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 95 TDFSKHmRGVNVVALYGGQRydVQLRALRQGPQ---IVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVE 171
Cdd:cd17957 81 LKLSKG-TGLRIVLLSKSLE--AKAKDGPKSITkydILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 90111550 172 TIMAQIPEGH-QTALFSATMPEAIRRITRRFMKEPqeVRI 210
Cdd:cd17957 158 EILAACTNPNlQRSLFSATIPSEVEELARSVMKDP--IRI 195
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
8-208 |
3.32e-49 |
|
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: 170.19 E-value: 3.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLdpelkapQILVLAPTRELA 87
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 88 VQVAEAMTDFSKHMRG--VNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG 165
Cdd:cd17938 74 EQTYNCIENFKKYLDNpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90111550 166 FIEDVETIMAQIPEGH------QTALFSATM--PEaIRRITRRFMKEPQEV 208
Cdd:cd17938 154 NLETINRIYNRIPKITsdgkrlQVIVCSATLhsFE-VKKLADKIMHFPTWV 203
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
31-207 |
2.79e-48 |
|
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: 167.72 E-value: 2.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 31 PIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPEL------KAPQILVLAPTRELAVQVAEamtDFSKHMRGV 104
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTK---DFKDITRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 105 NVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIM-----AQIPE 179
Cdd:cd17944 92 SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsykKDSED 171
|
170 180
....*....|....*....|....*...
gi 90111550 180 GHQTALFSATMPEAIRRITRRFMKEPQE 207
Cdd:cd17944 172 NPQTLLFSATCPDWVYNVAKKYMKSQYE 199
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
25-210 |
1.05e-47 |
|
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: 165.80 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGV 104
Cdd:cd17962 9 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGLPPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 105 NVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTA 184
Cdd:cd17962 89 KTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQTI 168
|
170 180
....*....|....*....|....*.
gi 90111550 185 LFSATMPEAIRRITRRFMKEPqeVRI 210
Cdd:cd17962 169 LVSATIPRGIEQLAGQLLQNP--VRI 192
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
22-205 |
3.85e-46 |
|
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: 162.37 E-value: 3.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 22 NDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPL---LQNLDPELK---APQILVLAPTRELAVQVAEAMT 95
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIiqrLLSLEPRVDrsdGTLALVLVPTRELALQIYEVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 96 DFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGT-LDLSKLSGLVLDEADEMLRMGFIEDVETIM 174
Cdd:cd17949 87 KLLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEKDITKIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 90111550 175 ----AQIPEGH---------QTALFSATMPEAIRRITRRFMKEP 205
Cdd:cd17949 167 elldDKRSKAGgekskpsrrQTVLVSATLTDGVKRLAGLSLKDP 210
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
17-237 |
5.77e-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: 162.41 E-value: 5.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPH-LLNGRDVLGMAQTGSGKTAAFSLPLLQNL---------DPELKAPQILVLAPTREL 86
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssngvGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 87 AVQVAEAMTDFSKHMrGVNVVALYGG---QRydvQLRALRQGPQIVVGTPGRLLD-------HLKRgtldLSKLSGLVLD 156
Cdd:cd17946 81 AVQVKDHLKAIAKYT-NIKIASIVGGlavQK---QERLLKKRPEIVVATPGRLWEliqegneHLAN----LKSLRFLVLD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 157 EADEMLRMGFIEDVETIMAQIPEGH-------QTALFSATMPEAIrritrrFMKEPQEVRIQSSVTTRPDISQSYWTVWG 229
Cdd:cd17946 153 EADRMLEKGHFAELEKILELLNKDRagkkrkrQTFVFSATLTLDH------QLPLKLNSKKKKKKKEKKQKLELLIEKVG 226
|
....*...
gi 90111550 230 MRKNEALV 237
Cdd:cd17946 227 FRKKPKVI 234
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
17-208 |
9.94e-46 |
|
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: 160.53 E-value: 9.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQ----ILVLAPTRELAVQVAE 92
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdglgALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 93 AMTDFSKHmRGVNVVALYGGQRYDVQLRALRQgPQIVVGTPGRLLDHLKRG-TLDLSKLSGLVLDEADEMLRMGFIEDVE 171
Cdd:cd17941 81 VLRKVGKY-HSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLD 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 90111550 172 TIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEV 208
Cdd:cd17941 159 AIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
17-208 |
4.03e-45 |
|
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: 159.43 E-value: 4.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPL-LQNLDPELKAPQI-------LVLAPTRELAV 88
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLiMFALEQEKKLPFIkgegpygLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 89 QVAEAMTDFSKHMR-----GVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLR 163
Cdd:cd17951 81 QTHEVIEYYCKALQeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 90111550 164 MGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEV 208
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
6-204 |
5.47e-45 |
|
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: 160.21 E-value: 5.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNL---DPELKAPQ------ 76
Cdd:cd18051 21 ETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqGPGESLPSesgyyg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 77 -------ILVLAPTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSK 149
Cdd:cd18051 101 rrkqyplALVLAPTRELASQIYDEARKFAYRSR-VRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDY 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 90111550 150 LSGLVLDEADEMLRMGFIEDVETIMAQ---IPEG-HQTALFSATMPEAIRRITRRFMKE 204
Cdd:cd18051 180 CKYLVLDEADRMLDMGFEPQIRRIVEQdtmPPTGeRQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
8-210 |
2.09e-43 |
|
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: 155.55 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLD--PELK---APQILVLAP 82
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINhqPFLErgdGPICLVLAP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 83 TRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEML 162
Cdd:cd18049 106 TRELAQQVQQVAAEYGRACR-LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 90111550 163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRI 210
Cdd:cd18049 185 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
17-210 |
2.18e-43 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350808 [Multi-domain] Cd Length: 271 Bit Score: 156.71 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLD--PELK---APQILVLAPTRELAVQVA 91
Cdd:cd18050 73 VMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINhqPYLErgdGPICLVLAPTRELAQQVQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 92 EAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVE 171
Cdd:cd18050 153 QVADDYGKSSR-LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIR 231
|
170 180 190
....*....|....*....|....*....|....*....
gi 90111550 172 TIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRI 210
Cdd:cd18050 232 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
17-205 |
6.39e-39 |
|
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: 142.11 E-value: 6.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQ----ILVLAPTRELAVQVAE 92
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRngtgVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 93 AMTDFSKHmRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSK-LSGLVLDEADEMLRMGFIEDVE 171
Cdd:cd17942 81 VAKELLKY-HSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGFEEEMR 159
|
170 180 190
....*....|....*....|....*....|....*
gi 90111550 172 TIMAQIPEGHQTALFSATMPEAIRRITR-RFMKEP 205
Cdd:cd17942 160 QIIKLLPKRRQTMLFSATQTRKVEDLARiSLKKKP 194
|
|
| RRM_EcCsdA_like |
cd12499 |
RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and ... |
488-560 |
3.74e-37 |
|
RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of E. coli CsdA, also termed ATP-dependent RNA helicase deaD, or translation factor W2, a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. CsdA may be involved in translation initiation, gene regulation after cold-shock, mRNA decay and biogenesis of the large or small ribosomal subunit. It contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.
Pssm-ID: 409922 [Multi-domain] Cd Length: 73 Bit Score: 132.70 E-value: 3.74e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111550 488 LYRIEVGRDDGVEVRHIVGAIANEGDISSRYIGNIKLFASHSTIELPKGMPGEVLQHFTRTRILNKPMNMQLL 560
Cdd:cd12499 1 RYRIEVGRKDGVKPGNIVGAIANEAGIDSRFIGRIKIFDDHSTVELPKGMPKDVLQHLKKVRVCGQPLNIKLL 73
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
232-340 |
3.25e-34 |
|
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: 125.79 E-value: 3.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 232 KNEALVRFLEAEDFDAAIIFVRTKNaTLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKK-TLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 90111550 312 ERISLVVNYDIPMDSESYVHRIGRTGRAG 340
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
17-190 |
8.11e-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: 128.90 E-value: 8.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNG---------RDVLGMAQTGSGKTAAFSLPLLQNL----DPELKApqiLVLAPT 83
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALskrvVPRLRA---LIVVPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 84 RELAVQVAEAMTDFSKHMrGVNVVALyGGQRYDVQLRALRQ---------GPQIVVGTPGRLLDHLKRGT-LDLSKLSGL 153
Cdd:cd17956 78 KELVQQVYKVFESLCKGT-GLKVVSL-SGQKSFKKEQKLLLvdtsgrylsRVDILVATPGRLVDHLNSTPgFTLKHLRFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90111550 154 VLDEADEMLRMGFIEDVETIMAQI-------------------PEGH-QTALFSATM 190
Cdd:cd17956 156 VIDEADRLLNQSFQDWLETVMKALgrptapdlgsfgdanllerSVRPlQKLLFSATL 212
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
7-216 |
1.05e-31 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 122.82 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNG--RDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTR 84
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 85 ELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDvqlRALRQGPQIVVGTPGRLLDH-LKRGTLDLSKLSGLVLDEADEMLR 163
Cdd:cd18048 99 ELALQTGKVVEEMGKFCVGIQVIYAIRGNRPG---KGTDIEAQIVIGTPGTVLDWcFKLRLIDVTNISVFVLDEADVMIN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 90111550 164 M-GFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTT 216
Cdd:cd18048 176 VqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
7-209 |
4.94e-31 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 120.21 E-value: 4.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNG--RDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTR 84
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 85 ELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDvqlRALRQGPQIVVGTPGRLLDH-LKRGTLDLSKLSGLVLDEADEML- 162
Cdd:cd18047 82 ELALQTGKVIEQMGKFYPELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIa 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 90111550 163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVR 209
Cdd:cd18047 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
17-197 |
6.41e-31 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 120.55 E-value: 6.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNL--DPELK-----APQILVLAPTRELAVQ 89
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrYKLLAegpfnAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 90 VAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIED 169
Cdd:cd17948 81 IGSVAQSLTEGL-GLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 90111550 170 VETIMAQIP-------------EGHQTALFSATMPEAIRRI 197
Cdd:cd17948 160 LSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEV 200
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
260-340 |
1.00e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 100.75 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 260 EVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRA 339
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
|
.
gi 90111550 340 G 340
Cdd:smart00490 82 G 82
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
13-358 |
7.53e-25 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 108.30 E-value: 7.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 13 LKAPILEALNDL-GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP--LLQNLdpelkapqILVLAPTreLAV- 88
Cdd:COG0514 1 LRDDALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLLPGL--------TLVVSPL--IALm 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 89 --QVaEAMTDfskhmRGVNVVALYGGQRYDVQ---LRALRQGpQI----VvgTPGRL-----LDHLKRGtldlsKLSGLV 154
Cdd:COG0514 71 kdQV-DALRA-----AGIRAAFLNSSLSAEERrevLRALRAG-ELkllyV--APERLlnprfLELLRRL-----KISLFA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 155 LDEA--------D---EMLRMGfiedveTIMAQIPeGHQTALFSATMPEAIRR-ITRRF-MKEPQEVRiqSSVTtRPDIS 221
Cdd:COG0514 137 IDEAhcisqwghDfrpDYRRLG------ELRERLP-NVPVLALTATATPRVRAdIAEQLgLEDPRVFV--GSFD-RPNLR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 222 QSYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIA 301
Cdd:COG0514 207 LEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 90111550 302 TdVA-ARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLR 358
Cdd:COG0514 287 T-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
18-212 |
2.00e-24 |
|
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: 102.84 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 18 LEALNDLGYEKPSPIQAECIPHLL---------------NGRDV-LGMAQTGSGKTAAFSLPLLQNL------DPEL--- 72
Cdd:cd17965 20 KGSNKTDEEIKPSPIQTLAIKKLLktlmrkvtkqtsneePKLEVfLLAAETGSGKTLAYLAPLLDYLkrqeqePFEEaee 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 73 --------KAPQILVLAPTRELAVQVAEAMTDFSKHMR-GVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRG 143
Cdd:cd17965 100 eyesakdtGRPRSVILVPTHELVEQVYSVLKKLSHTVKlGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSR 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 144 TLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMP-EAIRRITRRFmkePQEVRIQS 212
Cdd:cd17965 180 PKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPkEFDKTLRKLF---PDVVRIAT 246
|
|
| DbpA |
pfam03880 |
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of ... |
489-559 |
4.08e-21 |
|
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of DEAD helicase proteins. It is sufficient to confer specificity for hairpin 92 of 23S rRNA, which is part of the ribosomal A-site. However, several members of this family lack specificity for 23S rRNA. These can proteins can generally be distinguished by a basic region that extends beyond this domain [Karl Kossen, unpublished data].
Pssm-ID: 461082 [Multi-domain] Cd Length: 72 Bit Score: 87.43 E-value: 4.08e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111550 489 YRIEVGRDDGVEVRHIVGAIANEGDISSRYIGNIKLFASHSTIELPKGMPGEVLQHFTRTRILNKPMNMQL 559
Cdd:pfam03880 2 LFINVGKKDGVRPGDIVGALANEAGLPGDDIGKIDIFDNFSFVEVPAEKAEKVLKALKGTKIKGRKVRVEP 72
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
43-189 |
8.02e-18 |
|
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: 80.53 E-value: 8.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 43 GRDVLGMAQTGSGKTAAFSLPLLQNLDPelKAPQILVLAPTRELAVQVAEAMTDFSKHmrGVNVVALYGGQRYDVQLRAL 122
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLRELFGP--GIRVAVLVGGSSAEEREKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 123 RQGPQIVVGTPGRLLDHLKR-GTLDLSKLSGLVLDEADEML-RMGFI-EDVETIMAQIPEGHQTALFSAT 189
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLiDSRGAlILDLAVRKAGLKNAQVILLSAT 146
|
|
| RRM_DbpA |
cd12252 |
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; ... |
489-557 |
7.43e-16 |
|
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; This subfamily corresponds to the C-terminal RRM homology domain of dbpA proteins implicated in ribosome biogenesis. They bind with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92), which is part of the ribosomal A-site. The majority of dbpA proteins contain two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding. Several members of this family lack specificity for 23S rRNA. These proteins can generally be distinguished by a basic region that extends beyond the C-terminal domain.
Pssm-ID: 409698 [Multi-domain] Cd Length: 71 Bit Score: 72.19 E-value: 7.43e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111550 489 YRIEVGRDDGVEVRHIVGAIANEGDISSRYIGNIKLFASHSTIELPKGMPGEVLQHFTRTRILNKPMNM 557
Cdd:cd12252 2 LFINVGRKDGIDPRDLLGAICRAGGISRDDIGAIRIFDNFSFVEVPEAEAERVIEALNGKKIKGKKLRV 70
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
25-348 |
3.01e-15 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 78.99 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLqnldpeLKAPQILVLAPTRELavqvaeaMTDFSKHMR-- 102
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL------VLDGLTLVVSPLISL-------MKDQVDQLLan 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 103 GVNVVALYGGQRYDVQL---RALRQGP-QIVVGTPGRL-----LDHLKRGTLDLsklsgLVLDEADEMLRMGFIEDVE-- 171
Cdd:PRK11057 89 GVAAACLNSTQTREQQLevmAGCRTGQiKLLYIAPERLmmdnfLEHLAHWNPAL-----LAVDEAHCISQWGHDFRPEya 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 172 ---TIMAQIPEGHQTALfSATMPEAIRR-ITRRF-MKEPQevrIQSSVTTRPDISqsYWTVWGMRKNEALVRFLEAEDFD 246
Cdd:PRK11057 164 algQLRQRFPTLPFMAL-TATADDTTRQdIVRLLgLNDPL---IQISSFDRPNIR--YTLVEKFKPLDQLMRYVQEQRGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 247 AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDS 326
Cdd:PRK11057 238 SGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI 317
|
330 340
....*....|....*....|..
gi 90111550 327 ESYVHRIGRTGRAGRAGRALLF 348
Cdd:PRK11057 318 ESYYQETGRAGRDGLPAEAMLF 339
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
42-452 |
5.04e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.14 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 42 NGRDVLGMAqTGSGKTAAFSLpLLQNLdpeLKAPQILVLAPTRELAVQVAEAMTDFSKhmrgvnvVALYGGQRYDVqlra 121
Cdd:COG1061 100 GGRGLVVAP-TGTGKTVLALA-LAAEL---LRGKRVLVLVPRRELLEQWAEELRRFLG-------DPLAGGGKKDS---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 122 lrqGPQIVVGTPGRLLDHLKRGTLDlSKLSGLVLDEA--------DEML-------RMG-----FIEDVETIMAQIPEGH 181
Cdd:COG1061 164 ---DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAhhagapsyRRILeafpaayRLGltatpFRSDGREILLFLFDGI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 182 qtaLFSATMPEAIRR-ITRRFMKEPQEVRIQSSVTTRPDISQSYW---TVWGMRKNEALVRFLEAE-DFDAAIIFVRTKN 256
Cdd:COG1061 240 ---VYEYSLKEAIEDgYLAPPEYYGIRVDLTDERAEYDALSERLRealAADAERKDKILRELLREHpDDRKTLVFCSSVD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 257 ATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDiPMDSES-YVHRIGR 335
Cdd:COG1061 317 HAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PTGSPReFIQRLGR 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 336 TGRAGRAGRALL---FVENRERRLLRNIERTMKLTIPEVELPNAE--LLGKRRLEKFAAKVQQQLESSDLDQYRALLSKI 410
Cdd:COG1061 396 GLRPAPGKEDALvydFVGNDVPVLEELAKDLRDLAGYRVEFLDEEesEELALLIAVKPALEVKGELEEELLEELELLEDA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 90111550 411 QPTAEGEELDLETLAAALLKMAQGERTLIVPPDAPMRPKREF 452
Cdd:COG1061 476 LLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLL 517
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
230-339 |
1.88e-13 |
|
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: 68.00 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 230 MRKNEALVRFLEAEDFDA----AIIFVRTKNATLEVAEALE-----RNGYNSAALNG----------DMNQALREQTLER 290
Cdd:cd18802 6 IPKLQKLIEILREYFPKTpdfrGIIFVERRATAVVLSRLLKehpstLAFIRCGFLIGrgnssqrkrsLMTQRKQKETLDK 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 90111550 291 LKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRtGRA 339
Cdd:cd18802 86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
234-430 |
2.21e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 73.23 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 234 EALVRFLEAEDFDAAIIFVRTKNaTLE-VAEALERNGYNS------AALNGD--MNQALREQTLERLKDGRLDILIATDV 304
Cdd:COG1111 342 EILKEQLGTNPDSRIIVFTQYRD-TAEmIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 305 AARGLDVERISLVVNYDiPMDSE-SYVHRIGRTGRaGRAGRA--LLFVENRE---RRLLRNIERTMKLTIPEVElpnaEL 378
Cdd:COG1111 421 AEEGLDIPEVDLVIFYE-PVPSEiRSIQRKGRTGR-KREGRVvvLIAKGTRDeayYWSSRRKEKKMKSILKKLK----KL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 90111550 379 LGKRRLEKFAAKVQQQLE---SSDLDQYRALLSKIQPTAEGEELDLETLAAALLK 430
Cdd:COG1111 495 LDKQEKEKLKESAQATLDefeSIKELAEDEINEKDLDEIESSENGAHVDWREPVL 549
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
12-347 |
4.67e-13 |
|
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: 72.18 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 12 GLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNL--DPELKApqiLVLAPTRELAVQ 89
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALleDPGATA---LYLYPTKALARD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 90 VAEAMTDFSKHM-RGVNVVALYG----GQRydvqlRALRQGPQIVVGTP-----GRLLDHLKRGTLdLSKLSGLVLDEA- 158
Cdd:COG1205 117 QLRRLRELAEALgLGVRVATYDGdtppEER-----RWIREHPDIVLTNPdmlhyGLLPHHTRWARF-FRNLRYVVIDEAh 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 159 --------------DEMLRmgfiedvetIMAQI---------------PEGHQTALFSATMpEAI-----RRITRRF-MK 203
Cdd:COG1205 191 tyrgvfgshvanvlRRLRR---------ICRHYgsdpqfilasatignPAEHAERLTGRPV-TVVdedgsPRGERTFvLW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 204 EPQEVriqssvttRPDISQSYWTvwgmrknEA--LVRFLEAEDFdAAIIFVRTKNAT----LEVAEALERNGYNS--AAL 275
Cdd:COG1205 261 NPPLV--------DDGIRRSALA-------EAarLLADLVREGL-RTLVFTRSRRGAellaRYARRALREPDLADrvAAY 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111550 276 NGDMNQALREQTLERLKDGRLDILIAT-------DVAarGLDVerislVVNYDIPMDSESYVHRIGRTGRAGRAGRALL 347
Cdd:COG1205 325 RAGYLPEERREIERGLRSGELLGVVSTnalelgiDIG--GLDA-----VVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
246-348 |
3.62e-12 |
|
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: 63.77 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
Cdd:cd18794 31 GSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKS 110
|
90 100
....*....|....*....|...
gi 90111550 326 SESYVHRIGRTGRAGRAGRALLF 348
Cdd:cd18794 111 MESYYQESGRAGRDGLPSECILF 133
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
25-209 |
3.68e-11 |
|
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: 62.94 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLqnldpeLKAPQILVLAPTRELavqvaeaMTD--FSKHMR 102
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL------LLDGVTLVVSPLISL-------MQDqvDRLQQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 103 GVNVVALYGGQRYD----VQLRALRQGPQIVVGTPGRL--------LDHLKRgtldLSKLSGLVLDEA-----------D 159
Cdd:cd17920 76 GIRAAALNSTLSPEekreVLLRIKNGQYKLLYVTPERLlspdflelLQRLPE----RKRLALIVVDEAhcvsqwghdfrP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 90111550 160 EMLRMGFiedvetIMAQIPeGHQTALFSATMPEAIRR--ITRRFMKEPQEVR 209
Cdd:cd17920 152 DYLRLGR------LRRALP-GVPILALTATATPEVREdiLKRLGLRNPVIFR 196
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
31-158 |
3.35e-10 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 59.58 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 31 PIQAECIPHLLN-GRDVLGMAQTGSGKTAAFSLPLLQNLdpeLKAPQ-ILVLAPTRELAVQVAEamtDFSKHMR--GVNV 106
Cdd:cd17921 4 PIQREALRALYLsGDSVLVSAPTSSGKTLIAELAILRAL---ATSGGkAVYIAPTRALVNQKEA---DLRERFGplGKNV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 90111550 107 VALYGGQRYDvqlRALRQGPQIVVGTPGRLLDHL-KRGTLDLSKLSGLVLDEA 158
Cdd:cd17921 78 GLLTGDPSVN---KLLLAEADILVATPEKLDLLLrNGGERLIQDVRLVVVDEA 127
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
17-193 |
6.73e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 61.83 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 17 ILEALNDLGYEKPSPIQAECIP-HLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKApqiLVLAPTRELAVQVAEamt 95
Cdd:COG1204 11 VIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGKA---LYIVPLRALASEKYR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 96 DFSKHMR--GVNVVALYGGqrYDVQLRALRQgPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEA---DEMLRMGFIEDV 170
Cdd:COG1204 85 EFKRDFEelGIKVGVSTGD--YDSDDEWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliDDESRGPTLEVL 161
|
170 180
....*....|....*....|...
gi 90111550 171 ETIMAQIPEGHQTALFSATMPEA 193
Cdd:COG1204 162 LARLRRLNPEAQIVALSATIGNA 184
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
234-344 |
6.85e-10 |
|
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: 57.75 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 234 EALVRFLEAEDFDA---AIIFVRTKNATLEVAEALERN----------GYNSAALNGDMNQALREQTLERLKDGRLDILI 300
Cdd:cd18801 16 EIVKEHFKKKQEGSdtrVIIFSEFRDSAEEIVNFLSKIrpgiratrfiGQASGKSSKGMSQKEQKEVIEQFRKGGYNVLV 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 90111550 301 ATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRaGRAGR 344
Cdd:cd18801 96 ATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGR 138
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
33-158 |
1.25e-09 |
|
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: 57.98 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 33 QAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNL--DPELKApqiLVLAPTRELAVQVAEAMTDFSKHMRGVNVVALY 110
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALlrDPGSRA---LYLYPTKALAQDQLRSLRELLEQLGLGIRVATY 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 90111550 111 GGQ-RYDVQLRALRQGPQIVVGTPgRLLDH--LKRGTLDLSKLSGL---VLDEA 158
Cdd:cd17923 82 DGDtPREERRAIIRNPPRILLTNP-DMLHYalLPHHDRWARFLRNLryvVLDEA 134
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
284-349 |
4.22e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 53.48 E-value: 4.22e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111550 284 REQTLERLKDgRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAG-RAGRALLFV 349
Cdd:cd18785 12 SIEHAEEIAS-SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
49-356 |
5.76e-09 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 58.94 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 49 MAQTGSGKT-AAFSLpLLQNLDpELKAPQILVLAPTRELAVQVAEAMTDFSK-------HMRGVNVVALYGGQRYDVQLR 120
Cdd:COG1203 153 TAPTGGGKTeAALLF-ALRLAA-KHGGRRIIYALPFTSIINQTYDRLRDLFGedvllhhSLADLDLLEEEEEYESEARWL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 121 ALR----QGPqIVVGTPGRLLDHL----KRGTLDLSKLSG--LVLDEAD----EMLRMgfiedVETIMAQIPEGHQTALF 186
Cdd:COG1203 231 KLLkelwDAP-VVVTTIDQLFESLfsnrKGQERRLHNLANsvIILDEVQayppYMLAL-----LLRLLEWLKNLGGSVIL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 187 -SATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFL--EAEDFDAAIIFVRTKNATLEVAE 263
Cdd:COG1203 305 mTATLPPLLREELLEAYELIPDEPEELPEYFRAFVRKRVELKEGPLSDEELAELIleALHKGKSVLVIVNTVKDAQELYE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 264 ALERNGYNSAA--LNGDMNQALR----EQTLERLKDGRLDILIATDVAARGLDverislvVNYDI------PMDSEsyvh 331
Cdd:COG1203 385 ALKEKLPDEEVylLHSRFCPADRseieKEIKERLERGKPCILVSTQVVEAGVD-------IDFDVvirdlaPLDSL---- 453
|
330 340
....*....|....*....|....*
gi 90111550 332 rigrtgrAGRAGRAllfveNRERRL 356
Cdd:COG1203 454 -------IQRAGRC-----NRHGRK 466
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
234-386 |
2.01e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.58 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 234 EALVRFLEAEDFDAaIIFVrtknatlevaealernGYNSAALNGDMNQalREQ--TLERLKDGRLDILIATDVAARGLDV 311
Cdd:PRK13766 379 EKIVDLLEKEGIKA-VRFV----------------GQASKDGDKGMSQ--KEQieILDKFRAGEFNVLVSTSVAEEGLDI 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 312 ERISLVVNYDiPMDSE-SYVHRIGRTGRaGRAGRALLFV-------------ENRERRLLRNIeRTMKLTIPEVELPNAE 377
Cdd:PRK13766 440 PSVDLVIFYE-PVPSEiRSIQRKGRTGR-QEEGRVVVLIakgtrdeayywssRRKEKKMKEEL-KNLKGILNKKLQELDE 516
|
....*....
gi 90111550 378 LLGKRRLEK 386
Cdd:PRK13766 517 EQKGEEEEK 525
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
52-158 |
2.63e-08 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 54.58 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 52 TGSGKT--AAFSLPLLQNLDPELKAP--QILVLAPTRELAVQVAEAM---TDFS-KHMRGVNVVALYGGQRYDVQLRalr 123
Cdd:cd18034 25 TGSGKTliAVMLIKEMGELNRKEKNPkkRAVFLVPTVPLVAQQAEAIrshTDLKvGEYSGEMGVDKWTKERWKEELE--- 101
|
90 100 110
....*....|....*....|....*....|....*
gi 90111550 124 qGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEA 158
Cdd:cd18034 102 -KYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
26-352 |
1.70e-07 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 54.34 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 26 YEKPSPIQAECIPHLLNGRDVLGMAQTGSGKT-AAFsLPLLQNL----DPELKAPQILVL--APTRELAVQVAEAMTDFs 98
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELarrpRPGELPDGLRVLyiSPLKALANDIERNLRAP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 99 khMRGVNVVALYGGQRYDVQLR-----------ALRQGPQIVVGTP------------GRLLDHL--------------K 141
Cdd:COG1201 100 --LEEIGEAAGLPLPEIRVGVRtgdtpaserqrQRRRPPHILITTPeslallltspdaRELLRGVrtvivdeihalagsK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 142 RGT---LDLSKLSGLVldeADEMLRMGF---IEDVETIMAqipeghqtALFSATMPEAIRRITRRFMKEPqEVRIQSSVT 215
Cdd:COG1201 178 RGVhlaLSLERLRALA---PRPLQRIGLsatVGPLEEVAR--------FLVGYEDPRPVTIVDAGAGKKP-DLEVLVPVE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 216 TRPDISQSYWTVWGmrknEALVRFLEA-EDFDAAIIFVRTKNA----TLEVAEALERNGYNSAALNGDMNQALREQTLER 290
Cdd:COG1201 246 DLIERFPWAGHLWP----HLYPRVLDLiEAHRTTLVFTNTRSQaerlFQRLNELNPEDALPIAAHHGSLSREQRLEVEEA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111550 291 LKDGRLDILIAT---DVaarGLDVERISLVVNYDIPMDSESYVHRIGRTG-RAGRAGRALLFVENR 352
Cdd:COG1201 322 LKAGELRAVVATsslEL---GIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEVSKGRLVPTHR 384
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
28-158 |
2.35e-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: 51.66 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 28 KPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQ--ILVLAPTRELAVQVAEAmtdFSKHMR--G 103
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKgkVVFLANKVPLVEQQKEV---FRKHFErpG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 90111550 104 VNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTL-DLSKLSGLVLDEA 158
Cdd:cd17927 79 YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDEC 134
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
232-334 |
2.46e-07 |
|
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: 50.17 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 232 KNEALVRFLEA--EDFDAAIIFVRTKnATLE-VAEALERNGYNSAALNGDMNQALREQTLERLKDGR--LDILIATDVAA 306
Cdd:cd18793 12 KLEALLELLEElrEPGEKVLIFSQFT-DTLDiLEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGG 90
|
90 100 110
....*....|....*....|....*....|....
gi 90111550 307 RGLDVERISLVVNYDIP------MDSESYVHRIG 334
Cdd:cd18793 91 VGLNLTAANRVILYDPWwnpaveEQAIDRAHRIG 124
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
28-157 |
7.44e-07 |
|
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: 50.17 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 28 KPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQ---ILVLAPTRELAVQVAEAmtdFSKHMRGV 104
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEkgrVVVLVNKVPLVEQQLEK---FFKYFRKG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 90111550 105 -NVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGT----LDLSKLSGLVLDE 157
Cdd:cd18036 79 yKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGReeerVYLSDFSLLIFDE 136
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
249-350 |
1.06e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 48.80 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 249 IIFVRTKNATLEVAEAL-ERNGYNSAALN-----GDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDI 322
Cdd:cd18796 42 LVFTNTRSQAERLAQRLrELCPDRVPPDFialhhGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90 100
....*....|....*....|....*....
gi 90111550 323 PMDSESYVHRIGRTGRA-GRAGRALLFVE 350
Cdd:cd18796 122 PKSVARLLQRLGRSGHRpGAASKGRLVPT 150
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
43-163 |
6.14e-06 |
|
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: 46.81 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 43 GRDVLGMAQTGSGKTAAFSLPLLQNL-DPELKAPQILVLAPTRELAVQVAEAMTDFSKHMR-GVNVVALYGGQRYDVQLR 120
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPLDEIDlEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 90111550 121 ALRQGPQIVVGTP---GRLLDHlKRGTLDLSKLSGLVLDEADEMLR 163
Cdd:cd17922 81 QLKNPPGILITTPeslELLLVN-KKLRELFAGLRYVVVDEIHALLG 125
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
18-348 |
6.91e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 49.51 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 18 LEALNDLGYEKPS--PIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLqnldpeLKAPQILVLAPTRELavqvaeaMT 95
Cdd:PLN03137 448 LEVNNKKVFGNHSfrPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPAL------ICPGITLVISPLVSL-------IQ 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 96 DFSKHMRGVNVVALY--GGQRYDVQLRALRQ------GPQIVVGTPGR------LLDHLK----RGTLdlsklSGLVLDE 157
Cdd:PLN03137 515 DQIMNLLQANIPAASlsAGMEWAEQLEILQElsseysKYKLLYVTPEKvaksdsLLRHLEnlnsRGLL-----ARFVIDE 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 158 ADEMLRMG--FIEDVET--IMAQ----IPEGHQTALFSATMPEAIrritrrfmkePQEVRIQSSVTTRPDISQS---YWT 226
Cdd:PLN03137 590 AHCVSQWGhdFRPDYQGlgILKQkfpnIPVLALTATATASVKEDV----------VQALGLVNCVVFRQSFNRPnlwYSV 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 227 VWGMRKN-EALVRFLEAEDFD-AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDV 304
Cdd:PLN03137 660 VPKTKKClEDIDKFIKENHFDeCGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVA 739
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 90111550 305 AARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
Cdd:PLN03137 740 FGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLY 783
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
28-165 |
2.35e-05 |
|
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: 45.48 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 28 KPSPIQAECIPHLLNG------RDVLGMAQTGSGKTAAFSLPLLQNLDpelKAPQILVLAPTRELAVQVAEAMTDFSKHM 101
Cdd:cd17918 15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAYK---NGKQVAILVPTEILAHQHYEEARKFLPFI 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111550 102 rgvNVVALYGGQRYDVQlralrQGPQIVVGTPGRLldHLKRGTLDLsklsGLVLdeADEMLRMG 165
Cdd:cd17918 92 ---NVELVTGGTKAQIL-----SGISLLVGTHALL--HLDVKFKNL----DLVI--VDEQHRFG 139
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
28-158 |
3.19e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.59 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 28 KPSPIQAECIPHLLNGRD------VLGMAqTGSGKT--AAFslpLLQNLDPELKAPQILVLAPTRELAVQVAEAMTDFSK 99
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKngqkrgLIVMA-TGSGKTltAAK---LIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLP 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111550 100 HMrgVNVVALYGGQRYDVQlralRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVL--DEA 158
Cdd:pfam04851 79 NY--VEIGEIISGDKKDES----VDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEA 133
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
280-360 |
4.26e-05 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350191 [Multi-domain] Cd Length: 238 Bit Score: 45.31 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 280 NQALREQTLERLKDGRLDILIATDVAARGLDVERISLVV--NYDIPMDSESY---------VHRI-GRTGRAGRAGRALL 347
Cdd:cd18804 129 KKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGilNADSGLNSPDFraserafqlLTQVsGRAGRGDKPGKVII 208
|
90
....*....|...
gi 90111550 348 FVENRERRLLRNI 360
Cdd:cd18804 209 QTYNPEHPLIQAA 221
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
232-336 |
1.14e-04 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 45.22 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 232 KNEALVRFLE---AEDfDAAIIFVRTKnATLE-VAEALERNGYNSAALNGDMNQALREQTLERLKDGR--LDILIATDVA 305
Cdd:COG0553 534 KLEALLELLEellAEG-EKVLVFSQFT-DTLDlLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAG 611
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 90111550 306 ARGLDVERISLVVNYDIP---------MDSesyVHRIGRT 336
Cdd:COG0553 612 GEGLNLTAADHVIHYDLWwnpaveeqaIDR---AHRIGQT 648
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
270-349 |
1.58e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 42.33 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 270 YNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRI-GRTGRAGRAGRALLF 348
Cdd:cd18811 62 LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGRGDHQSYCLLV 141
|
.
gi 90111550 349 V 349
Cdd:cd18811 142 Y 142
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
32-157 |
1.95e-04 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 43.11 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 32 IQAECIPHLLNGRDVLGM-AQTGSGKTAAFSLPLLQNL-DPELKAP---QILVLAPTRELavqVAEAMTDFSKHM--RGV 104
Cdd:cd18023 5 IQSEVFPDLLYSDKNFVVsAPTGSGKTVLFELAILRLLkERNPLPWgnrKVVYIAPIKAL---CSEKYDDWKEKFgpLGL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 90111550 105 NVVALYGgqryDVQLRALR--QGPQIVVGTPGRlLDHLKRGTLDLSKLSGLV----LDE 157
Cdd:cd18023 82 SCAELTG----DTEMDDTFeiQDADIILTTPEK-WDSMTRRWRDNGNLVQLValvlIDE 135
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
231-311 |
3.33e-04 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 41.47 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 231 RKNEALVRFLEaeDFDAAIIFVRTKNATLEVAEALerngyNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLD 310
Cdd:cd18789 37 RALEELLKRHE--QGDKIIVFTDNVEALYRYAKRL-----LKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGID 109
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.
gi 90111550 311 V 311
Cdd:cd18789 110 L 110
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|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
31-142 |
3.77e-04 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 41.86 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 31 PIQAECIPHLLNGRD-VLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVlAPTRELA-VQVAEAMTDFSKHMrGVNVVA 108
Cdd:cd18021 6 PIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYI-APMQELVdARYKDWRAKFGPLL-GKKVVK 83
|
90 100 110
....*....|....*....|....*....|....
gi 90111550 109 LYGGQRYDvqLRALRQGpQIVVGTPGRlLDHLKR 142
Cdd:cd18021 84 LTGETSTD--LKLLAKS-DVILATPEQ-WDVLSR 113
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
248-318 |
4.22e-04 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 40.24 E-value: 4.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111550 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALRE-QTLERLKDG--RLDILIATDVAARGLDVERISLVV 318
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
42-158 |
5.26e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 40.75 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 42 NGRDVLGMAqTGSGKTA-AFSLPLlqnldpELKAPQILVLAPTRELAVQ-VAEAMTDFSKHMRGVNvvalyGGQRYDVQL 119
Cdd:cd17926 18 NRRGILVLP-TGSGKTLtALALIA------YLKELRTLIVVPTDALLDQwKERFEDFLGDSSIGLI-----GGGKKKDFD 85
|
90 100 110
....*....|....*....|....*....|....*....
gi 90111550 120 RAlrqgpQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEA 158
Cdd:cd17926 86 DA-----NVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
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|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
28-157 |
8.59e-04 |
|
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: 40.96 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 28 KPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAfSLPL----LQNLdPELKAPQILVLAPTrelaVQVAEAMTD-FSKHMR 102
Cdd:cd18073 2 KPRNYQLELALPAMKGKNTIICAPTGCGKTFV-SLLIcehhLKKF-PQGQKGKVVFFATK----VPVYEQQKSvFSKYFE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 90111550 103 --GVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTL-DLSKLSGLVLDE 157
Cdd:cd18073 76 rhGYRVTGISGATAENVPVEQIIENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDE 133
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|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
270-353 |
1.01e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 40.33 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 270 YNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRI-GRTGRAGRAGRALLF 348
Cdd:cd18792 61 ARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLrGRVGRGKHQSYCYLL 140
|
....*
gi 90111550 349 VENRE 353
Cdd:cd18792 141 YPDPK 145
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
29-114 |
1.70e-03 |
|
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: 39.47 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 29 PSPIQAECIPHLLNGRD------VLGMAqTGSGKT--AAFslpLLQNLDPELKAPQILVLAPTRELAVQvaeAMTDFSKH 100
Cdd:cd18032 1 PRYYQQEAIEALEEAREkgqrraLLVMA-TGTGKTytAAF---LIKRLLEANRKKRILFLAHREELLEQ---AERSFKEV 73
|
90
....*....|....
gi 90111550 101 MRGVNVVALYGGQR 114
Cdd:cd18032 74 LPDGSFGNLKGGKK 87
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
47-158 |
1.84e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 39.81 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 47 LGMAQTGSGKTAAFSLPLLQNLdpELKAPQILVLAPTRELAVQVAEamtdFSKHMRGVN--VVALYGGQRYDVQLRALRQ 124
Cdd:cd18035 20 LIVLPTGLGKTIIAILVAADRL--TKKGGKVLILAPSRPLVEQHAE----NLKRVLNIPdkITSLTGEVKPEERAERWDA 93
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90 100 110
....*....|....*....|....*....|....
gi 90111550 125 GpQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEA 158
Cdd:cd18035 94 S-KIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
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|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
285-347 |
2.95e-03 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 40.53 E-value: 2.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111550 285 EQTLERLKDGRLDILIATDVAARGLDVERISLV--VNYDIPMDSESYvhR------------IGRTGRAGRAGRALL 347
Cdd:PRK05580 470 EQLLAQFARGEADILIGTQMLAKGHDFPNVTLVgvLDADLGLFSPDF--RasertfqlltqvAGRAGRAEKPGEVLI 544
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|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
25-133 |
6.42e-03 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350777 [Multi-domain] Cd Length: 214 Bit Score: 38.51 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 25 GYEKPSPIQAECIPHLLNGRD-VLGMAQTGSGKTAAFSLPLLQ----NLDPE----LKAPQILVLAPTRELavqVAEAMT 95
Cdd:cd18019 14 GFKSLNRIQSKLFPAAFETDEnLLLCAPTGAGKTNVALLTILReigkHRNPDgtinLDAFKIVYIAPMKAL---VQEMVG 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 90111550 96 DFSKHMR--GVNVVALYGgqryDVQL-RALRQGPQIVVGTP 133
Cdd:cd18019 91 NFSKRLApyGITVAELTG----DQQLtKEQISETQIIVTTP 127
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|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
43-196 |
8.19e-03 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain] Cd Length: 186 Bit Score: 38.04 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 43 GRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLaPTRELAVQVAEAMTDFSKHMRGVNVVAL-YGGQRYDVQLRA 121
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWALKLAARGGKRRIIYAL-PTRATINQMYERIREILGRLDDEDKVLLlHSKAALELLESD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 122 LRQGPQ------------------IVVGTPGRLLD---HLKRGTLDLSKLSG--LVLDEA----DEMLRMgFIEDVETIM 174
Cdd:cd17930 80 EEPDDDpveavdwalllkrswlapIVVTTIDQLLEsllKYKHFERRLHGLANsvVVLDEVqaydPEYMAL-LLKALLELL 158
|
170 180
....*....|....*....|..
gi 90111550 175 AQIpeGHQTALFSATMPEAIRR 196
Cdd:cd17930 159 GEL--GGPVVLMTATLPALLRD 178
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
50-366 |
9.21e-03 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 38.56 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 50 AQTGSGKTAAFSLPLLQNLDPELKAPQILVLaPTRELAvqvaEAMTDFSKHMRGVNVVA----------LYGGQRYDVQL 119
Cdd:cd09639 6 APTGYGKTEAALLWALHSLKSQKADRVIIAL-PTRATI----NAMYRRAKEAFGETGLYhssilssrikEMGDSEEFEHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 120 RALRQGPQ-------IVVGTPGRLLDHLKRG------TLDLSKLSGLVLDEAD--EMLRMGFIEDVetIMAQIPEGHQTA 184
Cdd:cd09639 81 FPLYIHSNdtlfldpITVCTIDQVLKSVFGEfghyefTLASIANSLLIFDEVHfyDEYTLALILAV--LEVLKDNDVPIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 185 LFSATMPEAIRRitrrFMKEPQEVRIQSSVTTRPDISQSYWtvwgMRKNEALV--RFLE-----AEDFDAAIIFVRTKNA 257
Cdd:cd09639 159 LMSATLPKFLKE----YAEKIGYVEENEPLDLKPNERAPFI----KIESDKVGeiSSLErllefIKKGGSVAIIVNTVDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111550 258 TLEVAEALERNGYNSAA--LNGDMNQALRE----QTLERLKDGRLDILIATDVAARGLDVERISLVVNYdIPMDseSYVH 331
Cdd:cd09639 231 AQEFYQQLKEKGPEEEImlIHSRFTEKDRAkkeaELLLEFKKSEKFVIVATQVIEASLDISVDVMITEL-APID--SLIQ 307
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 90111550 332 RIGRTGRAGRAGRALLFV----ENRERRLLRN---IERTMKL 366
Cdd:cd09639 308 RLGRLHRYGEKNGEEVYIitdaPDGKGQKPYPydlVERTIEL 349
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