|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-429 |
9.41e-162 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 461.92 E-value: 9.41e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 1 MKKFIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDlnfNNRVLRGLIL 80
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS---RPRAPQALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 81 VPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTM 160
Cdd:COG0513 78 APTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 161 LEMGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQIHDRRDRVDIIKHEAFKVDVKRKKELVAHILK 240
Cdd:COG0513 158 LDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 241 TTKHEQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLVINYT 320
Cdd:COG0513 238 DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 321 LPEATDEFTHRVGRTGRAGNKGTVISMLTVEDYNHFSKIERDLRLNVKREIHEDFPLKDRQPRQKPMKKkmtlseKKGHY 400
Cdd:COG0513 318 LPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPK------IKEKL 391
|
410 420
....*....|....*....|....*....
gi 2570060844 401 KKKQTAREDAPKKSGAKSKKTTKRDAKRS 429
Cdd:COG0513 392 KGKKAGRGGRPGPKGERKARRGKRRRRKR 420
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
13-371 |
2.85e-103 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 314.44 E-value: 2.85e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 13 INKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNF--NNRVLRGLILVPTRELVEQV 90
Cdd:PRK10590 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakGRRPVRALILTPTRELAAQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 91 SKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIE 170
Cdd:PRK10590 92 GENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 171 TIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQIHDRRDRVDIIKHEAFKVDVKRKKELVAHILKTTKHEQVLLF 250
Cdd:PRK10590 172 RVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGKGNWQQVLVF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 251 VNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLVINYTLPEATDEFTH 330
Cdd:PRK10590 252 TRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVH 331
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2570060844 331 RVGRTGRAGNKGTVISMLTVEDYNHFSKIERDLrlnvKREI 371
Cdd:PRK10590 332 RIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL----KKEI 368
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
4-424 |
7.71e-95 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 291.85 E-value: 7.71e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVnndLNFNNRVL---RGLIL 80
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL---LDFPRRKSgppRILIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 81 VPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTM 160
Cdd:PRK11192 80 TPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 161 LEMGFIKEIETIFSLCSPYRQIVMCSATV-SQNIRKLAKEFLRDPVTVQIH-DRRDRVDIIK--HEAfkVDVKRKKELVA 236
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLeGDAVQDFAERLLNDPVEVEAEpSRRERKKIHQwyYRA--DDLEHKTALLC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 237 HILKTTKHEQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLV 316
Cdd:PRK11192 238 HLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 317 INYTLPEATDEFTHRVGRTGRAGNKGTVISMLTVEDYNHFSKIERDLRLNVKREIHEDFPLKDRQPRQKPMKKKMTLSEK 396
Cdd:PRK11192 318 INFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRPKTKAPSEKKTGKPSKKVLA 397
|
410 420
....*....|....*....|....*...
gi 2570060844 397 KGHYKKKQTAREDAPKKSGAKSKKTTKR 424
Cdd:PRK11192 398 KRAEKKEKEKEKPKVKKRHRDTKNIGKR 425
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
21-394 |
3.65e-86 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 270.52 E-value: 3.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 21 GYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKvnndLNFNNRVLRGLILVPTRELVEQVSKSLSEYGKH 100
Cdd:PRK11776 23 GYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK----LDVKRFRVQALVLCPTRELADQVAKEIRRLARF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 101 L-KVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIETIFSLCSPY 179
Cdd:PRK11776 99 IpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 180 RQIVMCSATVSQNIRKLAKEFLRDPVTVQIHDRRDRVDIIKHeAFKVDVKRKKELVAHILKTTKHEQVLLFVNKKDSANA 259
Cdd:PRK11776 179 RQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQR-FYEVSPDERLPALQRLLLHHQPESCVVFCNTKKECQE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 260 AFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLVINYTLPEATDEFTHRVGRTGRAG 339
Cdd:PRK11776 258 VADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAG 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2570060844 340 NKGTVISMLTVEDYNHFSKIERDLRLNVKREIHEDFPLKDRQPRQKPMkkkMTLS 394
Cdd:PRK11776 338 SKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEM---VTLC 389
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
13-208 |
3.78e-84 |
|
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: 255.83 E-value: 3.78e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 13 INKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFNNRVLRGLILVPTRELVEQVSK 92
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 93 SLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIETI 172
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2570060844 173 FSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQ 208
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-378 |
1.10e-76 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 246.36 E-value: 1.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 3 KFIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFNNRVL---RGLI 79
Cdd:PRK01297 88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERYMgepRALI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 80 LVPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGG-IDIVVATAGRLLDLERDELIDLSSVNFIVLDEAD 158
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 159 TMLEMGFIKEIETIFSLCSPY--RQIVMCSATVSQNIRKLAKEFLRDPVTVQIHDRRDRVDIIKHEAFKVDVKRKKELVA 236
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 237 HILKTTKHEQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLV 316
Cdd:PRK01297 328 NLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHV 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2570060844 317 INYTLPEATDEFTHRVGRTGRAGNKGTVISMLTVEDYNHFSKIERDLRLNVKREIHEDFPLK 378
Cdd:PRK01297 408 INFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAELLK 469
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
4-369 |
7.77e-71 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 235.13 E-value: 7.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLnfnnRVLRGLILVPT 83
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPEL----KAPQILVLAPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 84 RELVEQVSKSLSEYGKHLK-VKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLD-LERDELiDLSSVNFIVLDEADTML 161
Cdd:PRK11634 84 RELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDhLKRGTL-DLSKLSGLVLDEADEML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 162 EMGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQIHDRRDRVDIIKHEAFKVDVKRKKELVAHILKT 241
Cdd:PRK11634 163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 242 TKHEQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLVINYTL 321
Cdd:PRK11634 243 EDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDI 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2570060844 322 PEATDEFTHRVGRTGRAGNKGTviSMLTVEDYnhfskiERDLRLNVKR 369
Cdd:PRK11634 323 PMDSESYVHRIGRTGRAGRAGR--ALLFVENR------ERRLLRNIER 362
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
3-376 |
2.64e-69 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 228.89 E-value: 2.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 3 KFIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFNnrvlRG----- 77
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLR----YGdgpiv 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 78 LILVPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEA 157
Cdd:PTZ00110 207 LVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 158 DTMLEMGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRD-PVTVQIhdrrDRVDI-----IKHEAFKVDVKRK 231
Cdd:PTZ00110 287 DRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNV----GSLDLtachnIKQEVFVVEEHEK 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 232 ----KELVAHILKTTkhEQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARG 307
Cdd:PTZ00110 363 rgklKMLLQRIMRDG--DKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRG 440
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570060844 308 LDIKELPLVINYTLPEATDEFTHRVGRTGRAGNKGTVISMLTVEDYnhfsKIERDLrLNVKREIHEDFP 376
Cdd:PTZ00110 441 LDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKY----RLARDL-VKVLREAKQPVP 504
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
2-353 |
1.18e-66 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 218.69 E-value: 1.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 2 KKFIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFNNRVL---RGL 78
Cdd:PRK04837 8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRKVnqpRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 79 ILVPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEAD 158
Cdd:PRK04837 88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 159 TMLEMGFIKEIETIFSLCSP--YRQIVMCSATVSQNIRKLAKEFLRDPVTVQIHDRRDRVDIIKHEAFKVDVKRKKELVA 236
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 237 HILKTTKHEQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLV 316
Cdd:PRK04837 248 TLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350
....*....|....*....|....*....|....*..
gi 2570060844 317 INYTLPEATDEFTHRVGRTGRAGNKGTVISmLTVEDY 353
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSIS-LACEEY 363
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
4-361 |
8.90e-64 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 210.45 E-value: 8.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQRKVI-PIINKKiDVIAASKSGTGKTASYVLPMLNKVNNDLNfnnrVLRGLILVP 82
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIkPILDGY-DTIGQAQSGTGKTATFVIAALQLIDYDLN----ACQALILAP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 83 TRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLE 162
Cdd:PTZ00424 105 TRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 163 MGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQIHDRRDRVDIIKHEAFKVDVKRKK-ELVAHILKT 241
Cdd:PTZ00424 185 RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKfDTLCDLYET 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 242 TKHEQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLVINYTL 321
Cdd:PTZ00424 265 LTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDL 344
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2570060844 322 PEATDEFTHRVGRTGRAGNKGTVISMLTVEDYNHFSKIER 361
Cdd:PTZ00424 345 PASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
17-389 |
1.90e-59 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 202.33 E-value: 1.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 17 IEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLN---KVNNDLNFNNRVLRGLILVPTRELVEQVSKS 93
Cdd:PLN00206 136 LETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTIRSGHPSEQRNPLAMVLTPTRELCVQVEDQ 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 94 LSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIETIF 173
Cdd:PLN00206 216 AKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIF 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 174 -SLCSPyrQIVMCSATVSQNIRKLAKEFLRDPVTVQIHDRRDRVDIIKHEAFKVDVKRKKELVAHILKTTKHEQ--VLLF 250
Cdd:PLN00206 296 qALSQP--QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKppAVVF 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 251 VNKKDSANAAFEYFR-SQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLVINYTLPEATDEFT 329
Cdd:PLN00206 374 VSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYI 453
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570060844 330 HRVGRTGRAGNKGTVISMLTVEDYNHFSKIERDLRLN---VKREIHEDFPLKDRQPRQKPMKK 389
Cdd:PLN00206 454 HQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSgaaIPRELANSRYLGSGRKRKKKRRY 516
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
4-346 |
1.84e-56 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 195.55 E-value: 1.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFNNRVL---RGLIL 80
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKPedpRALIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 81 VPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLD-LERDELIDLSSVNFIVLDEADT 159
Cdd:PRK04537 91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDyVKQHKVVSLHACEICVLDEADR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 160 MLEMGFIKEIETIF----SLCSpyRQIVMCSATVSQNIRKLAKEFLRDPV-----TVQIHDRRDRVDIIkheaFKVDvKR 230
Cdd:PRK04537 171 MFDLGFIKDIRFLLrrmpERGT--RQTLLFSATLSHRVLELAYEHMNEPEklvveTETITAARVRQRIY----FPAD-EE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 231 KKELVAHILKTTKHEQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDI 310
Cdd:PRK04537 244 KQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHI 323
|
330 340 350
....*....|....*....|....*....|....*.
gi 2570060844 311 KELPLVINYTLPEATDEFTHRVGRTGRAGNKGTVIS 346
Cdd:PRK04537 324 DGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAIS 359
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
4-208 |
2.03e-52 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 174.42 E-value: 2.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFNNrvLRGLILVPT 83
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVG--ARALILSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 84 RELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEM 163
Cdd:cd17959 81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2570060844 164 GFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQ 208
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
4-203 |
1.30e-50 |
|
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: 170.36 E-value: 1.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFNNRVLRG------ 77
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRRkaypsa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 78 LILVPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEA 157
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2570060844 158 DTMLEMGFIKEIETIFSLCSP----YRQIVMCSATVSQNIRKLAKEFLRD 203
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHPDMppkgERQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
15-207 |
1.96e-50 |
|
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: 169.81 E-value: 1.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 15 KAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNN--DLNFNNRVL--RGLILVPTRELVEQV 90
Cdd:cd17945 3 RVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpPLDEETKDDgpYALILAPTRELAQQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 91 SKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLD-LERdELIDLSSVNFIVLDEADTMLEMGF---- 165
Cdd:cd17945 83 EEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDcLER-RLLVLNQCTYVVLDEADRMIDMGFepqv 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2570060844 166 ----------------IKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:cd17945 162 tkildampvsnkkpdtEEAEKLAASGKHRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
26-196 |
2.02e-49 |
|
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: 165.49 E-value: 2.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 26 TAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKvnndLNFNNRVLRGLILVPTRELVEQVSKSLSEYGKHLKVKH 105
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEA----LDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 106 TKIMGGTSRTKQGETLSGgIDIVVATAGRLLDLERDElIDLSSVNFIVLDEADTMLEMGFIKEIETIFSLCSPYRQIVMC 185
Cdd:pfam00270 77 ASLLGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
|
170
....*....|.
gi 2570060844 186 SATVSQNIRKL 196
Cdd:pfam00270 155 SATLPRNLEDL 165
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
17-209 |
3.41e-49 |
|
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: 165.84 E-value: 3.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 17 IEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNdlNFNNRVLRGLILVPTRELVEQVSKSLSE 96
Cdd:cd17957 5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK--PRKKKGLRALILAPTRELASQIYRELLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 97 YGKHLKVKhTKIMGGTSRTKQ--GETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIETIFS 174
Cdd:cd17957 83 LSKGTGLR-IVLLSKSLEAKAkdGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEILA 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 2570060844 175 LC-SPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQI 209
Cdd:cd17957 162 ACtNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
13-207 |
2.38e-48 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 163.79 E-value: 2.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 13 INKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLnkVNNDLNFNNRVLRG----LILVPTRELVE 88
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF--IHLDLQPIPREQRNgpgvLVLTPTRELAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 89 QVSKSLSEYgKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKE 168
Cdd:cd17958 79 QIEAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQ 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 2570060844 169 IETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:cd17958 158 IRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
15-207 |
2.85e-48 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 163.62 E-value: 2.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 15 KAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDlnfnNRVLRGLILVPTRELVEQVSKSL 94
Cdd:cd17940 12 MGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPK----KDVIQALILVPTRELALQTSQVC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 95 SEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIETIFS 174
Cdd:cd17940 88 KELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILN 167
|
170 180 190
....*....|....*....|....*....|...
gi 2570060844 175 LCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:cd17940 168 FLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
4-208 |
1.05e-47 |
|
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: 162.39 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLN--FnnrvlrGLILV 81
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYgiF------ALVLT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 82 PTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLER---DELIDLSSVNFIVLDEAD 158
Cdd:cd17955 75 PTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEAD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2570060844 159 TMLEMGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQ 208
Cdd:cd17955 155 RLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
15-208 |
1.17e-47 |
|
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: 161.77 E-value: 1.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 15 KAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNdlnfNNRVLRG-----LILVPTRELVEQ 89
Cdd:cd17966 3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINA----QPPLERGdgpivLVLAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 90 VSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEI 169
Cdd:cd17966 79 IQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2570060844 170 ETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQ 208
Cdd:cd17966 159 RKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
219-348 |
2.22e-47 |
|
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: 158.82 E-value: 2.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 219 IKHEAFKVDVKRKKE-LVAHILKTTKHEQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKV 297
Cdd:cd18787 1 IKQLYVVVEEEEKKLlLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2570060844 298 LVATDIAARGLDIKELPLVINYTLPEATDEFTHRVGRTGRAGNKGTVISML 348
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
15-208 |
3.81e-47 |
|
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: 160.50 E-value: 3.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 15 KAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDlNFNNRVLRGLILVPTREL---VEQVS 91
Cdd:cd17947 3 RALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYR-PKKKAATRVLVLVPTRELamqCFSVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 92 KSLSEYGKhlkVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDEL-IDLSSVNFIVLDEADTMLEMGFIKEIE 170
Cdd:cd17947 82 QQLAQFTD---ITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADELK 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2570060844 171 TIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQ 208
Cdd:cd17947 159 EILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
15-207 |
6.47e-47 |
|
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: 160.06 E-value: 6.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 15 KAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKV--NNDLNFNNRVLRGLILVPTRELVEQVSK 92
Cdd:cd17961 7 KAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkAKAESGEEQGTRALILVPTRELAQQVSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 93 ---SLSEY-GKHLKVkhTKIMGGTSRTKQGETLSGGIDIVVATAGRLLD-LERDELIDLSSVNFIVLDEADTMLEMGFIK 167
Cdd:cd17961 87 vleQLTAYcRKDVRV--VNLSASSSDSVQRALLAEKPDIVVSTPARLLShLESGSLLLLSTLKYLVIDEADLVLSYGYEE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2570060844 168 EIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:cd17961 165 DLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAIL 204
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
4-202 |
9.39e-46 |
|
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: 158.98 E-value: 9.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNK-VNNDLN---FNNRVL-RGL 78
Cdd:cd18052 45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGmMKEGLTassFSEVQEpQAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 79 ILVPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEAD 158
Cdd:cd18052 125 IVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEAD 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2570060844 159 TMLEMGFIKEIETIFSLCS-PY---RQIVMCSATVSQNIRKLAKEFLR 202
Cdd:cd18052 205 RMLDMGFGPEIRKLVSEPGmPSkedRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
15-207 |
1.06e-45 |
|
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: 156.81 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 15 KAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVnndlnFNNRVLR------GLILVPTRELVE 88
Cdd:cd17952 3 NAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI-----MDQRELEkgegpiAVIVAPTRELAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 89 QVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKE 168
Cdd:cd17952 78 QIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQ 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 2570060844 169 IETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:cd17952 158 VRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
6-205 |
1.43e-45 |
|
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: 156.33 E-value: 1.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 6 EFNFHSSINKAIEDQGYENPTAV-QRKVIPIINKKiDVIAASKSGTGKTASYVLPMLNkvnnDLNFNNRVLRGLILVPTR 84
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIqQRAIVPIIKGR-DVIAQAQSGTGKTATFSIGALQ----RIDTTVRETQALVLAPTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 85 ELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMG 164
Cdd:cd17939 76 ELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2570060844 165 FIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPV 205
Cdd:cd17939 156 FKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPV 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
17-207 |
1.96e-45 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 156.11 E-value: 1.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 17 IEDQGYENPTAVQRKVIPIINKKI-DVIAASKSGTGKTASYVLPMLNKVnndlnFNNRVLRGLILVPTRELVEQVSKSLS 95
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAL-----KRGKGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 96 EYGKHLKVKHTKIMGGTSRTKQGETL-SGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIETIFS 174
Cdd:smart00487 76 KLGPSLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
|
170 180 190
....*....|....*....|....*....|...
gi 2570060844 175 LCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI 188
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
21-207 |
4.58e-45 |
|
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: 155.82 E-value: 4.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 21 GYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVnndLNFNNRVLR-----GLILVPTRELVEQVSKSLS 95
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRL---LSLEPRVDRsdgtlALVLVPTRELALQIYEVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 96 eygKHLKVKH----TKIMGGTSRTKQGETLSGGIDIVVATAGRLLD-LERDELIDLSSVNFIVLDEADTMLEMGFIKEIE 170
Cdd:cd17949 87 ---KLLKPFHwivpGYLIGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDIT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2570060844 171 TIFSL-------------CSPYRQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:cd17949 164 KILELlddkrskaggeksKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
4-208 |
2.29e-44 |
|
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: 153.63 E-value: 2.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNdlnfNNRVLRGLILVPT 83
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLE----NPQRFFALVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 84 RELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLD-LERDELIDLSSVNFIVLDEADTMLE 162
Cdd:cd17954 78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADRLLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2570060844 163 MGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQ 208
Cdd:cd17954 158 MDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
1-208 |
4.67e-44 |
|
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: 153.30 E-value: 4.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 1 MKKFIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNdlnfnNRVLR---- 76
Cdd:cd17953 11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKD-----QRPVKpgeg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 77 --GLILVPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDL---ERDELIDLSSVNF 151
Cdd:cd17953 86 piGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDIltaNNGRVTNLRRVTY 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2570060844 152 IVLDEADTMLEMGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQ 208
Cdd:cd17953 166 VVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
13-207 |
1.09e-43 |
|
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: 151.57 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 13 INKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKV-NNDLNFNNRVLRGLILVPTRELVEQVS 91
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlKRKANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 92 KSLSEYGKH--LKVKHTKIMGGTSRTKQGETLS-GGIDIVVATAGRLLDL--ERDELIDLSSVNFIVLDEADTMLEMGFI 166
Cdd:cd17960 81 EVLQSFLEHhlPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELlsRKADKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2570060844 167 KEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
3-209 |
1.11e-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: 152.86 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 3 KFIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFNnrvlRG----- 77
Cdd:cd18049 25 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLE----RGdgpic 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 78 LILVPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEA 157
Cdd:cd18049 101 LVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2570060844 158 DTMLEMGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQI 209
Cdd:cd18049 181 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
4-207 |
5.05e-43 |
|
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: 150.16 E-value: 5.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVnndlnfnnrvlRGLILVPT 83
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-----------VALILEPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 84 RELVEQVSKSLSEYGKHL---KVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTM 160
Cdd:cd17938 70 RELAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2570060844 161 LEMGFIKEIETIFS-----LCSPYR-QIVMCSATV-SQNIRKLAKEFLRDPVTV 207
Cdd:cd17938 150 LSQGNLETINRIYNripkiTSDGKRlQVIVCSATLhSFEVKKLADKIMHFPTWV 203
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
4-209 |
2.14e-42 |
|
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: 148.65 E-value: 2.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFnnrvLRGLILVPT 83
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQ----VSVLVICHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 84 RELVEQVSKSLSEYGKHLK-VKHTKIMGGTSRTKQGETL-SGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTML 161
Cdd:cd17950 80 RELAFQISNEYERFSKYMPnVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKML 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2570060844 162 E-MGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQI 209
Cdd:cd17950 160 EqLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
4-207 |
3.89e-41 |
|
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: 144.90 E-value: 3.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQ-RKVIPIInKKIDVIAASKSGTGKTASYVLPMLNKVNNDLnfnnRVLRGLILVP 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQqRAIMPCI-KGYDVIAQAQSGTGKTATFSISILQQIDTSL----KATQALVLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 83 TRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLE 162
Cdd:cd18046 76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2570060844 163 MGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
9-202 |
4.56e-40 |
|
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: 142.34 E-value: 4.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 9 FHSSINKAIEDQGYENPTAVQRKVI-PIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDL-NFNNRVLRGLILVPTREL 86
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKpAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 87 VEQVS---KSLSEYGKHLKVkHTKImGGTSRTKQGETL-SGGIDIVVATAGRLLDLERDE--LIDLSSVNFIVLDEADTM 160
Cdd:cd17964 81 ALQIAaeaKKLLQGLRKLRV-QSAV-GGTSRRAELNRLrRGRPDILVATPGRLIDHLENPgvAKAFTDLDYLVLDEADRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2570060844 161 LEMGFIKEIETIFSL----CSPYRQIVMCSATVSQNIRKLAKEFLR 202
Cdd:cd17964 159 LDMGFRPDLEQILRHlpekNADPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
15-210 |
6.60e-40 |
|
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: 141.66 E-value: 6.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 15 KAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVnndlnFNNRVLRG-----LILVPTRELVEQ 89
Cdd:cd17941 3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL-----YRERWTPEdglgaLIISPTRELAMQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 90 VSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGgIDIVVATAGRLLD-LERDELIDLSSVNFIVLDEADTMLEMGFIKE 168
Cdd:cd17941 78 IFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGFKET 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2570060844 169 IETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQIH 210
Cdd:cd17941 157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
4-209 |
1.07e-39 |
|
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: 143.23 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFNnrvlRG-----L 78
Cdd:cd18050 64 FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLE----RGdgpicL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 79 ILVPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEAD 158
Cdd:cd18050 140 VLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEAD 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2570060844 159 TMLEMGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQI 209
Cdd:cd18050 220 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
13-190 |
4.13e-38 |
|
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: 138.14 E-value: 4.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 13 INKAIEDQGYENPTAVQRKVIP-IINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFN-----NRVLRGLILVPTREL 86
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNgvggkQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 87 VEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDL--ERDELID-LSSVNFIVLDEADTMLEM 163
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELiqEGNEHLAnLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....
gi 2570060844 164 GFIKEIETIFSL-------CSPYRQIVMCSATVS 190
Cdd:cd17946 161 GHFAELEKILELlnkdragKKRKRQTFVFSATLT 194
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
15-208 |
2.51e-37 |
|
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: 134.31 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 15 KAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKvnndLNFNNRVLRGLILVPTRELVEQVSKSL 94
Cdd:cd17943 3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALES----LDLERRHPQVLILAPTREIAVQIHDVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 95 SEYGKHLKVKHTKI-MGGTSRTKQGETLsGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIETIF 173
Cdd:cd17943 79 KKIGKKLEGLKCEVfIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIF 157
|
170 180 190
....*....|....*....|....*....|....*
gi 2570060844 174 SLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQ 208
Cdd:cd17943 158 SSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
3-203 |
5.12e-37 |
|
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: 135.55 E-value: 5.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 3 KFIEFNFHSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKV------NNDLNFNNRVLR 76
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgESLPSESGYYGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 77 ------GLILVPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLD-LERDElIDLSSV 149
Cdd:cd18051 102 rkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDmLERGK-IGLDYC 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2570060844 150 NFIVLDEADTMLEMGFIKEIETIFSLC----SPYRQIVMCSATVSQNIRKLAKEFLRD 203
Cdd:cd18051 181 KYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
13-207 |
9.07e-36 |
|
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: 130.36 E-value: 9.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 13 INKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNndlnFNNRVLRGLILVPTRELVEQVSK 92
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL----TEHRNPSALILTPTRELAVQIED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 93 SLSEYGKHL-KVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIET 171
Cdd:cd17962 77 QAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 2570060844 172 IFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:cd17962 157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
21-207 |
1.37e-35 |
|
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: 130.28 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 21 GYENPTAVQ-RKVIPIINKKiDVIAASKSGTGKTASYVLPMLNKVnnDLNFnnRVLRGLILVPTRELVEQVSKSLSEYGK 99
Cdd:cd18045 18 GFEKPSAIQqRAIKPIIKGR-DVIAQSQSGTGKTATFSISVLQCL--DIQV--RETQALILSPTRELAVQIQKVLLALGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 100 HLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIETIFSLCSPY 179
Cdd:cd18045 93 YMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYLPPA 172
|
170 180
....*....|....*....|....*...
gi 2570060844 180 RQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:cd18045 173 TQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
15-204 |
4.98e-35 |
|
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: 128.63 E-value: 4.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 15 KAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNdLNFNNRVLRG-LILVPTRELVEQVSKS 93
Cdd:cd17942 3 KAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYK-LKFKPRNGTGvIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 94 LSEYGKHLKVKHTKIMGGTSRTKQGETLSGGIDIVVATAGRLLD-LERDELIDLSSVNFIVLDEADTMLEMGFIKEIETI 172
Cdd:cd17942 82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQI 161
|
170 180 190
....*....|....*....|....*....|..
gi 2570060844 173 FSLCSPYRQIVMCSATVSQNIRKLAKEFLRDP 204
Cdd:cd17942 162 IKLLPKRRQTMLFSATQTRKVEDLARISLKKK 193
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
12-207 |
4.78e-33 |
|
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: 123.07 E-value: 4.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 12 SINKAIEDQGYENPTAVQRKVIPII--NKKIDVIAASKSGTGKTASYVLPMLNKVNNdlnfNNRVLRGLILVPTRELVEQ 89
Cdd:cd17963 4 ELLKGLYAMGFNKPSKIQETALPLIlsDPPENLIAQSQSGTGKTAAFVLAMLSRVDP----TLKSPQALCLAPTRELARQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 90 VSKSLSEYGKHLKVKHTKIMGGTSRtKQGETLSGgiDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEM-GFIKE 168
Cdd:cd17963 80 IGEVVEKMGKFTGVKVALAVPGNDV-PRGKKITA--QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQ 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 2570060844 169 IETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:cd17963 157 SIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
13-207 |
3.72e-32 |
|
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: 121.29 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 13 INKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLN---KVNNDLNF-NNRVLRGLILVPTRELVE 88
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMfalEQEKKLPFiKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 89 QVSKSLSEYGKHL-KVKHTKI-----MGGTSRTKQGETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLE 162
Cdd:cd17951 81 QTHEVIEYYCKALqEGGYPQLrcllcIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2570060844 163 MGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTV 207
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
15-197 |
1.21e-31 |
|
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: 120.43 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 15 KAIEDQGYENPTAVQRKVIPIINKKI---------DVIAASKSGTGKTASYVLPMLNKVnndLNFNNRVLRGLILVPTRE 85
Cdd:cd17956 3 KNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPIVQAL---SKRVVPRLRALIVVPTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 86 LVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGG--------IDIVVATAGRLLD-LERDELIDLSSVNFIVLDE 156
Cdd:cd17956 80 LVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDhLNSTPGFTLKHLRFLVIDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2570060844 157 ADTMLEMGF-------IKEIET------------IFSLCSPYR-QIVMCSATVSQNIRKLA 197
Cdd:cd17956 160 ADRLLNQSFqdwletvMKALGRptapdlgsfgdaNLLERSVRPlQKLLFSATLTRDPEKLS 220
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
231-339 |
4.57e-30 |
|
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: 112.30 E-value: 4.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 231 KKELVAHILKTTKHEQVLLFVNKKDSANAAFeYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDI 310
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 2570060844 311 KELPLVINYTLPEATDEFTHRVGRTGRAG 339
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
4-200 |
6.82e-30 |
|
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: 116.32 E-value: 6.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 4 FIEFNFHSSINKAIEDQ---------GYENPTAVQRKVIPIINK-----------------KIDVIAAsKSGTGKTASYV 57
Cdd:cd17965 1 FDQLKLLPSVREAIIKEilkgsnktdEEIKPSPIQTLAIKKLLKtlmrkvtkqtsneepklEVFLLAA-ETGSGKTLAYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 58 LPMLNKVNNDLNF-------------NNRVLRGLILVPTRELVEQVS---KSLSEYGKhLKVKHTKIMGGTSRTKQGETL 121
Cdd:cd17965 80 APLLDYLKRQEQEpfeeaeeeyesakDTGRPRSVILVPTHELVEQVYsvlKKLSHTVK-LGIKTFSSGFGPSYQRLQLAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 122 SGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIETIFSLCSPYRQIVMCSATVSQNI-RKLAKEF 200
Cdd:cd17965 159 KGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFdKTLRKLF 238
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
41-202 |
5.88e-29 |
|
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: 112.25 E-value: 5.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 41 DVIAASKSGTGKTASYVLPMLNKVNNDLN--FNNRVLRGLILVPTRELVEQVSKSLSEYGKHLKVkhTKIMGGTSRTKQG 118
Cdd:cd17944 29 DLIAQARTGTGKTFSFAIPLIEKLQEDQQprKRGRAPKVLVLAPTRELANQVTKDFKDITRKLSV--ACFYGGTPYQQQI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 119 ETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIETIFSLcsPYR-------QIVMCSATVSQ 191
Cdd:cd17944 107 FAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSV--SYKkdsednpQTLLFSATCPD 184
|
170
....*....|.
gi 2570060844 192 NIRKLAKEFLR 202
Cdd:cd17944 185 WVYNVAKKYMK 195
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
16-196 |
1.63e-26 |
|
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: 106.68 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 16 AIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFNNRVL---RGLILVPTRELVEQVSK 92
Cdd:cd17948 4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFnapRGLVITPSRELAEQIGS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 93 SLSEYGKHLKVKHTKIMGGtsRTKQGETLS--GGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEADTMLEMGFIKEIE 170
Cdd:cd17948 84 VAQSLTEGLGLKVKVITGG--RTKRQIRNPhfEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLS 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 2570060844 171 TIFSLC-------------SPYRQIVMCSATVSQNIRKL 196
Cdd:cd17948 162 HFLRRFplasrrsentdglDPGTQLVLVSATMPSGVGEV 200
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
262-339 |
3.19e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 92.66 E-value: 3.19e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570060844 262 EYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLVINYTLPEATDEFTHRVGRTGRAG 339
Cdd:smart00490 5 ELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
1-209 |
3.61e-20 |
|
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: 88.92 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 1 MKKFIEFNFHSSINKAIEDQGYENPTAVQRKVIPII--NKKIDVIAASKSGTGKTASYVLPMLNKVNNdlnfNNRVLRGL 78
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMlaDPPQNLIAQSQSGTGKTAAFVLAMLSRVDA----LKLYPQCL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 79 ILVPTRELVEQVSKSLSEYGKH-------LKVKHTKIMGGTSRTKQgetlsggidIVVATAGRLLD-LERDELIDLSSVN 150
Cdd:cd18048 93 CLSPTFELALQTGKVVEEMGKFcvgiqviYAIRGNRPGKGTDIEAQ---------IVIGTPGTVLDwCFKLRLIDVTNIS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570060844 151 FIVLDEADTMLEM-GF----IKEIETIFSLCspyrQIVMCSATVSQNIRKLAKEFLRDPVTVQI 209
Cdd:cd18048 164 VFVLDEADVMINVqGHsdhsVRVKRSMPKEC----QMLLFSATFEDSVWAFAERIVPDPNIIKL 223
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
49-380 |
7.27e-18 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 85.85 E-value: 7.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 49 GTGKT--ASYVLpmlnkvnNDLNFNNRVLrglILVPTRELVEQVSKSLSeygkhlKVKHTKIMGGTSRTKQGetlsggiD 126
Cdd:COG1061 110 GTGKTvlALALA-------AELLRGKRVL---VLVPRRELLEQWAEELR------RFLGDPLAGGGKKDSDA-------P 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 127 IVVATAGRLLDLERDELIDlSSVNFIVLDE-----ADTMLEmgFIKEIETIFSLC---SPYRQ------IVMCSATVSQ- 191
Cdd:COG1061 167 ITVATYQSLARRAHLDELG-DRFGLVIIDEahhagAPSYRR--ILEAFPAAYRLGltaTPFRSdgreilLFLFDGIVYEy 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 192 NIRKLAKE-FLRDPVTVQIHD----RRDRVDIIKH---EAFKVDVKRKKELVAHIL-KTTKHEQVLLFVNKKDSANAAFE 262
Cdd:COG1061 244 SLKEAIEDgYLAPPEYYGIRVdltdERAEYDALSErlrEALAADAERKDKILRELLrEHPDDRKTLVFCSSVDHAEALAE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 263 YFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLVINYTLPEATDEFTHRVGRTGRAGNKG 342
Cdd:COG1061 324 LLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGK 403
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2570060844 343 T--VISMLTVEDYNHFSKIERDLRLNVKREIHEDFPLKDR 380
Cdd:COG1061 404 EdaLVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESE 443
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
2-208 |
3.31e-16 |
|
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: 77.07 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 2 KKFIEFNFHSSINKAIEDQGYENPTAVQRKVIPII--NKKIDVIAASKSGTGKTASYVLPMLNKVNNDLNFNnrvlRGLI 79
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMlaEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYP----QCLC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 80 LVPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGETLSGgiDIVVATAGRLLD-LERDELIDLSSVNFIVLDEAD 158
Cdd:cd18047 77 LSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEAD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2570060844 159 TML-EMGFIKEIETIFSLCSPYRQIVMCSATVSQNIRKLAKEFLRDPVTVQ 208
Cdd:cd18047 155 VMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
41-188 |
1.53e-12 |
|
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: 64.73 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 41 DVIAASKSGTGKTASYVLPMLnkvnndLNFNNRVLRGLILVPTRELVEQVSKSLSEYGKHlkVKHTKIMGGTSRTKQGET 120
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAAL------LLLLKKGKKVLVLVPTKALALQTAERLRELFGP--GIRVAVLVGGSSAEEREK 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2570060844 121 LSGG-IDIVVATAGRLL-DLERDELIDLSSVNFIVLDEADTML--EMGFIKEIETIFSLCSPYRQIVMCSAT 188
Cdd:cd00046 75 NKLGdADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLidSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
232-427 |
6.82e-11 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 64.37 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 232 KELVAHILKTTKHEQVLLFVNKKDSANAAFEYFRSQGIKI------AAIHGDVEY--KNRVQAIKDFRSKKVKVLVATDI 303
Cdd:COG1111 341 REILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDKGLtqKEQIEILERFRAGEFNVLVATSV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 304 AARGLDIKELPLVINYTL-PEATdEFTHRVGRTGRaGNKGTVISMLTV----EDYNHFSKI-ERDLRLNVKReIHEDFPL 377
Cdd:COG1111 421 AEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGRVVVLIAKgtrdEAYYWSSRRkEKKMKSILKK-LKKLLDK 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2570060844 378 KDRQPRQKPMKKKMTLSEKKGHYKKKQTAREDAPKKSGAKSKKTTKRDAK 427
Cdd:COG1111 498 QEKEKLKESAQATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREP 547
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
12-339 |
1.41e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 62.99 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 12 SINKAIEDQGYENPTAVQRKVIP--IINKKiDVIAASKSGTGKTASYVLPMLNKVNNDLnfnnrvlRGLILVPTRELVEQ 89
Cdd:COG1204 10 KVIEFLKERGIEELYPPQAEALEagLLEGK-NLVVSAPTASGKTLIAELAILKALLNGG-------KALYIVPLRALASE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 90 VSKSLSEYGKHLKVKHTKIMGGTSRTkqgETLSGGIDIVVATAGRLLDLERDELIDLSSVNFIVLDEA----DTmlEMGF 165
Cdd:COG1204 82 KYREFKRDFEELGIKVGVSTGDYDSD---DEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 166 IKE--IETIFSLCSPyRQIVMCSATVSqNIRKLAKEFLRDPVTvqiHDRRD---RVDIIKHEAFKVDVKRKKE------L 234
Cdd:COG1204 157 TLEvlLARLRRLNPE-AQIVALSATIG-NAEEIAEWLDAELVK---SDWRPvplNEGVLYDGVLRFDDGSRRSkdptlaL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 235 VAHILKTTkhEQVLLFVNKKDSANAAFEYFRSQ--GIKIAAIHGDV-EYKNRVQAIKD---------------------- 289
Cdd:COG1204 232 ALDLLEEG--GQVLVFVSSRRDAESLAKKLADElkRRLTPEEREELeELAEELLEVSEethtnekladclekgvafhhag 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 290 ------------FRSKKVKVLVATDIAARGLDikeLP---LVINYTLPEATDEFTHR-----VGRTGRAG 339
Cdd:COG1204 310 lpselrrlvedaFREGLIKVLVATPTLAAGVN---LParrVIIRDTKRGGMVPIPVLefkqmAGRAGRPG 376
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
195-349 |
1.32e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.19 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 195 KLAKEFLRDPvtvqihdrRDRVDIIKHEAFKVD---VKRKKELVAHILKTTKHEQVLLFVNKKDSANAAFEYFRSQGIKI 271
Cdd:PRK13766 321 KASKRLVEDP--------RFRKAVRKAKELDIEhpkLEKLREIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 272 AAIHG----DVE----YKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLVINYT-LPEATdEFTHRVGRTGRaGNKG 342
Cdd:PRK13766 393 VRFVGqaskDGDkgmsQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEG 470
|
....*..
gi 2570060844 343 TVISMLT 349
Cdd:PRK13766 471 RVVVLIA 477
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
10-345 |
3.01e-08 |
|
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: 56.00 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 10 HSSINKAIEDQGYENPTAVQRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVnndlnFNNRVLRGLILVPTRELV-E 88
Cdd:COG1205 42 PPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-----LEDPGATALYLYPTKALArD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 89 QVSKsLSEYGKHL--KVKHTKIMGGTSRTKQGETLSGGiDIVVAT-----AGRLLDLER-DELidLSSVNFIVLDEADTm 160
Cdd:COG1205 117 QLRR-LRELAEALglGVRVATYDGDTPPEERRWIREHP-DIVLTNpdmlhYGLLPHHTRwARF--FRNLRYVVIDEAHT- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 161 lemgfikeietifslcspYR-------------------------QIVMCSATVSqNIRKLAKEFLRDPVTVqIHD---- 211
Cdd:COG1205 192 ------------------YRgvfgshvanvlrrlrricrhygsdpQFILASATIG-NPAEHAERLTGRPVTV-VDEdgsp 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 212 --RRDRVdIIKHEAFKVDVKRK-----KELVAHILKttKHEQVLLFVNKKDSANAAFEYFRSQ------GIKIAAIHGDV 278
Cdd:COG1205 252 rgERTFV-LWNPPLVDDGIRRSalaeaARLLADLVR--EGLRTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGY 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570060844 279 EYKNRVQAIKDFRSKKVKVLVAT-------DIAarGLDikelpLVINYTLPEATDEFTHRVGRTGRAGNKGTVI 345
Cdd:COG1205 329 LPEERREIERGLRSGELLGVVSTnalelgiDIG--GLD-----AVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
38-157 |
3.55e-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: 53.42 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 38 KKIDVIAASKSGTGKT--ASYVLPMLNKVNNDLNFNNRvlRGLILVPTRELVEQVSKSLSEYGKHLKVKHTKIMG---GT 112
Cdd:cd18034 15 LKRNTIVVLPTGSGKTliAVMLIKEMGELNRKEKNPKK--RAVFLVPTVPLVAQQAEAIRSHTDLKVGEYSGEMGvdkWT 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2570060844 113 SRTKQGETLSggIDIVVATAGRLLDLERDELIDLSSVNFIVLDEA 157
Cdd:cd18034 93 KERWKEELEK--YDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
232-348 |
1.02e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 50.82 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 232 KELVAHILK---TTKHEQVLLFVNKKDSANAAFEYFRSQGIKIAAI----HGDVEY------KNRVQAIKDFRSKKVKVL 298
Cdd:cd18801 15 EEIVKEHFKkkqEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGKSskgmsqKEQKEVIEQFRKGGYNVL 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2570060844 299 VATDIAARGLDIKELPLVINYTLPEATDEFTHRVGRTGRaGNKGTVISML 348
Cdd:cd18801 95 VATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVLL 143
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
225-316 |
6.01e-07 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 49.17 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 225 KVDVKRKKELVAHILK-----TTKHEQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLV 299
Cdd:cd18790 3 EIEVRPTEGQVDDLLGeirkrVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLV 82
|
90
....*....|....*..
gi 2570060844 300 ATDIAARGLDIKELPLV 316
Cdd:cd18790 83 GINLLREGLDLPEVSLV 99
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
76-188 |
1.22e-06 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 48.86 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 76 RGLILVPTRELVEQVSKSLSEYGKHLKVK-HTKIMGGTSRTKQGETL-----SGGIDIVVATAGRLLDleRDELIDLSSV 149
Cdd:cd17924 62 RSYLIFPTKSLVKQAYERLSKYAEKAGVEvKILVYHSRLKKKEKEELlekieKGDFDILVTTNQFLSK--NFDLLSNKKF 139
|
90 100 110
....*....|....*....|....*....|....*....
gi 2570060844 150 NFIVLDEADTMLEMGfiKEIETIFSLCSpYRQIVMCSAT 188
Cdd:cd17924 140 DFVFVDDVDAVLKSS--KNIDRLLKLLG-FGQLVVSSAT 175
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
242-341 |
1.25e-06 |
|
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: 47.59 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 242 TKHEQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDV---------------EYKNRVQAIKDFRSKKVKVLVATDIAAR 306
Cdd:cd18802 23 TPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGFligrgnssqrkrslmTQRKQKETLDKFRDGELNLLIATSVLEE 102
|
90 100 110
....*....|....*....|....*....|....*
gi 2570060844 307 GLDIKELPLVINYTLPEATDEFTHRVGRTGRAGNK 341
Cdd:cd18802 103 GIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSK 137
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
29-210 |
1.97e-06 |
|
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: 48.03 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 29 QRKVI-PIINKKIDVIAASKSGTGKTASYVLPMLNKVNNdlnFNNRVLrglILVPTRELVEQVSKSLSEYGKHLKVKHTK 107
Cdd:cd17921 6 QREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALAT---SGGKAV---YIAPTRALVNQKEADLRERFGPLGKNVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 108 IMGGTSRTKQgetLSGGIDIVVATAGR---LLDLERDELIDLssVNFIVLDEADtML---EMGFIKE--IETIFSLCSPY 179
Cdd:cd17921 80 LTGDPSVNKL---LLAEADILVATPEKldlLLRNGGERLIQD--VRLVVVDEAH-LIgdgERGVVLEllLSRLLRINKNA 153
|
170 180 190
....*....|....*....|....*....|.
gi 2570060844 180 RQIVMcSATVSqNIRKLAkEFLRDPVTVQIH 210
Cdd:cd17921 154 RFVGL-SATLP-NAEDLA-EWLGVEDLIRFD 181
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
274-342 |
2.65e-06 |
|
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: 45.00 E-value: 2.65e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570060844 274 IHGDVEYKNRVQAIKDFRSKkVKVLVATDIAARGLDIKELPLVINYTLPEATDEFTHRVGRTGRAGNKG 342
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASS-LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
265-345 |
1.08e-05 |
|
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: 44.89 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 265 RSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGLDIKELPLVINYTLPEATDEFTHRVGRTGRAGNKGTV 344
Cdd:cd18794 51 QSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSEC 130
|
.
gi 2570060844 345 I 345
Cdd:cd18794 131 I 131
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
233-335 |
1.96e-05 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 46.76 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 233 ELVAHILKttKHEQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKK--VKVLVATDIAARGLDI 310
Cdd:COG0553 540 ELLEELLA--EGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNL 617
|
90 100 110
....*....|....*....|....*....|..
gi 2570060844 311 KELPLVINYTLP-------EATDEfTHRVGRT 335
Cdd:COG0553 618 TAADHVIHYDLWwnpaveeQAIDR-AHRIGQT 648
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
220-322 |
3.07e-05 |
|
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: 43.62 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 220 KHEafkVDVKRKKELVAHILKTTKH--EQVLLFVNKKDSANAAFEYFRSQGIKIAAIHGDVEYKNRVQAIKDFRS-KKVK 296
Cdd:cd18793 4 KIE---EVVSGKLEALLELLEELREpgEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdPDIR 80
|
90 100
....*....|....*....|....*..
gi 2570060844 297 V-LVATDIAARGLDIKELPLVINYTLP 322
Cdd:cd18793 81 VfLLSTKAGGVGLNLTAANRVILYDPW 107
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
236-347 |
5.40e-05 |
|
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: 43.02 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 236 AHILKTTKHEQVLLFVNKKDSA-------NAAFEYfRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAARGL 308
Cdd:cd18796 30 EVIFLLERHKSTLVFTNTRSQAerlaqrlRELCPD-RVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGI 108
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2570060844 309 DIKELPLVINYTLPEATDEFTHRVGRTGRAGN---KGTVISM 347
Cdd:cd18796 109 DIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGaasKGRLVPT 150
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
29-199 |
6.59e-05 |
|
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: 43.34 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 29 QRKVIPIINKKIDVIAASKSGTGKTASYVLPMLNKVNNDlnfnNRVlRGLILVPTRELVEQVSKSLSEY--GKHLKVKHT 106
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD----PGS-RALYLYPTKALAQDQLRSLRELleQLGLGIRVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 107 KIMGGTSRTKQGETLSGGIDIVVATAGRL--LDLERDELID--LSSVNFIVLDEADTM-----LEMGFIkeIETIFSLCS 177
Cdd:cd17923 80 TYDGDTPREERRAIIRNPPRILLTNPDMLhyALLPHHDRWArfLRNLRYVVLDEAHTYrgvfgSHVALL--LRRLRRLCR 157
|
170 180
....*....|....*....|....*
gi 2570060844 178 PYR---QIVMCSATVSqNIRKLAKE 199
Cdd:cd17923 158 RYGadpQFILTSATIG-NPAEHART 181
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
230-342 |
8.87e-05 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 42.62 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 230 RKKELVAHILKttKHEQ---VLLFVNKKDSANAAfeyfrSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATDIAAR 306
Cdd:cd18789 34 NKLRALEELLK--RHEQgdkIIVFTDNVEALYRY-----AKRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDE 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2570060844 307 GLDikelplvinytLPEAT------------DEFTHRVGRTGRAGNKG 342
Cdd:cd18789 107 GID-----------LPEANvaiqisghggsrRQEAQRLGRILRPKKGG 143
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
41-189 |
1.45e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 42.80 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 41 DVIAASKSGTGKTASYVLPMLNKVNNDLNFNNRvlRGLILVPTRELVEQVSKSLSEYGKHLKVKHTKIMGGTSRTKQGET 120
Cdd:cd17927 19 NTIICLPTGSGKTFVAVLICEHHLKKFPAGRKG--KVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENVSVEQ 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570060844 121 LSGGIDIVVATAGRLL-DLERDELIDLSSVNFIVLDEADTMLEMGFIKEIETIFSLC-----SPYRQIVMCSATV 189
Cdd:cd17927 97 IVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHNTTKNHPYNEIMFRYLDQklgssGPLPQILGLTASP 171
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
37-157 |
1.77e-04 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 41.78 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 37 NKKIDVIAASksGTGKT--ASYVLPMLNKvnndlnfNNRVLRGLILVPTRELVEQVSKSLSEYGKHLKVkhTKIMGGTSR 114
Cdd:cd18032 20 QRRALLVMAT--GTGKTytAAFLIKRLLE-------ANRKKRILFLAHREELLEQAERSFKEVLPDGSF--GNLKGGKKK 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2570060844 115 TKQGetlsggiDIVVATAGRLLDLERDELIDLSSVNFIVLDEA 157
Cdd:cd18032 89 PDDA-------RVVFATVQTLNKRKRLEKFPPDYFDLIIIDEA 124
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
125-341 |
1.84e-04 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 43.21 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 125 IDIVVATagRLLDLERDELIDLSSVN-FIVLDEADTMLEmgFIKE-IETIFSLCSPYRQ-IVMCSATVSQNIRKLAK--- 198
Cdd:TIGR01587 102 IDQVLKS--VFGEFGHYEFTLASIANsLLIFDEVHFYDE--YTLAlILAVLEVLKDNDVpILLMSATLPKFLKEYAEkig 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 199 --EFLRDPVTVQIhDRRDRVDIIKHEAFKV-DVKRKKELVAHILKTTKheqVLLFVNKKDSANAAFEYFRSQG--IKIAA 273
Cdd:TIGR01587 178 yvEFNEPLDLKEE-RRFENHRFILIESDKVgEISSLERLLEFIKKGGS---IAIIVNTVDRAQEFYQQLKEKApeEEIIL 253
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570060844 274 IHGDVEYKNRV----QAIKDFRSKKVK-VLVATDIAARGLDIKelpLVINYTLPEATDEFTHRVGRTGRAGNK 341
Cdd:TIGR01587 254 YHSRFTEKDRAkkeaELLREMKKSNEKfVIVATQVIEASLDIS---ADVMITELAPIDSLIQRLGRLHRYGRK 323
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
152-341 |
1.09e-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: 40.88 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 152 IVLDEADTMLEmgFIKE-IETIFSLCSPYRQ-IVMCSATVSQNIRKLAK--EFLRDPVTVQIHDRRDRVDIIKHEAFKVD 227
Cdd:cd09639 127 LIFDEVHFYDE--YTLAlILAVLEVLKDNDVpILLMSATLPKFLKEYAEkiGYVEENEPLDLKPNERAPFIKIESDKVGE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 228 VKRKKELVAHILKTTKheqVLLFVNKKDSANAAFEYFRSQG--IKIAAIHGDVEYKNRV----QAIKDFRSKKVKVLVAT 301
Cdd:cd09639 205 ISSLERLLEFIKKGGS---VAIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSRFTEKDRAkkeaELLLEFKKSEKFVIVAT 281
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2570060844 302 DIAARGLDIKelpLVINYTLPEATDEFTHRVGRTGRAGNK 341
Cdd:cd09639 282 QVIEASLDIS---VDVMITELAPIDSLIQRLGRLHRYGEK 318
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
262-345 |
2.99e-03 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 39.74 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570060844 262 EYFRSQGIKIAAIHGDVEYKNRVQAIKDFRSKKVKVLVATdIA-ARGLDIKELPLVINYTLPEATDEFTHRVGRTGRAGN 340
Cdd:COG0514 248 EWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGL 326
|
....*
gi 2570060844 341 KGTVI 345
Cdd:COG0514 327 PAEAL 331
|
|
| |
