|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
22-397 |
5.50e-133 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 389.89 E-value: 5.50e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKP-CVQAVITAPTRELALQIYQRCEKMSEADPkL 100
Cdd:COG0513 22 YTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPrAPQALILAPTRELALQVAEELRKLAKYLG-L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 101 VIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQM 180
Cdd:COG0513 101 RVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDL-IERGALDLSGVETLVLDEADRMLDMGFIEDIERILKLLPKERQT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 181 MSFSATIPQELRLFLKKYMDRPQTVQIEEQSAFHPKIQHILVPVQHKTYAEKVLEILPSFTPYVCLIFANTRSEAANVAS 260
Cdd:COG0513 180 LLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 261 NMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELDYYIHRSGRTGRAGHEG 340
Cdd:COG0513 260 KLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEG 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1589200340 341 ICYALYEKKDDTAIRQLE-VRGIHFDHKTIKngqwcDLEPLHKKKVRKDDPLEKEIAK 397
Cdd:COG0513 340 TAISLVTPDERRLLRAIEkLIGQKIEEEELP-----GFEPVEEKRLERLKPKIKEKLK 392
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
26-358 |
2.72e-78 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 250.49 E-value: 2.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 26 TPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEADPKLVIRLI 105
Cdd:PRK11776 28 TPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAKEIRRLARFIPNIKVLTL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 106 TGGIEKSRMIEQLKVQPHIVVGTPGRIKDlFLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQMMSFSA 185
Cdd:PRK11776 108 CGGVPMGPQIDSLEHGAHIIVGTPGRILD-HLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 186 TIPQELRLFLKKYMDRPQTVQIEEQSAfHPKIQHILVPVQHKTYAEKVLEILPSFTPYVCLIFANTRSEAANVASNMRDA 265
Cdd:PRK11776 187 TYPEGIAAISQRFQRDPVEVKVESTHD-LPAIEQRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQ 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 266 GYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELDYYIHRSGRTGRAGHEGICYAL 345
Cdd:PRK11776 266 GFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSL 345
|
330
....*....|...
gi 1589200340 346 YEKKDDTAIRQLE 358
Cdd:PRK11776 346 VAPEEMQRANAIE 358
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
17-206 |
4.63e-75 |
|
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: 233.49 E-value: 4.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 17 IELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPC----VQAVITAPTRELALQIYQRCEK 92
Cdd:cd00268 5 LKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKkgrgPQALVLAPTRELAMQIAEVARK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 93 MSEAdPKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAG 172
Cdd:cd00268 85 LGKG-TGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDL-IERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKILS 162
|
170 180 190
....*....|....*....|....*....|....
gi 1589200340 173 KMRKDLQMMSFSATIPQELRLFLKKYMDRPQTVQ 206
Cdd:cd00268 163 ALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
22-358 |
6.54e-61 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 209.32 E-value: 6.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEADPKLV 101
Cdd:PRK11634 26 YEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 102 IRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDlFLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQMM 181
Cdd:PRK11634 106 VVALYGGQRYDVQLRALRQGPQIVVGTPGRLLD-HLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 182 SFSATIPQELRLFLKKYMDRPQTVQIEEQSAFHPKIQHILVPVQHKTYAEKVLEILPSFTPYVCLIFANTRSEAANVASN 261
Cdd:PRK11634 185 LFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 262 MRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELDYYIHRSGRTGRAGHEGI 341
Cdd:PRK11634 265 LERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGR 344
|
330
....*....|....*..
gi 1589200340 342 CYALYEKKDDTAIRQLE 358
Cdd:PRK11634 345 ALLFVENRERRLLRNIE 361
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
25-441 |
4.50e-60 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 202.48 E-value: 4.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 25 PTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIME------KVDSSKPCVqaVITAPTRELALQIYQRCEKMSeADP 98
Cdd:PRK11192 24 PTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQhlldfpRRKSGPPRI--LILTPTRELAMQVADQARELA-KHT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 99 KLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDlFLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDL 178
Cdd:PRK11192 101 HLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQ-YIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAAETRWRK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 179 QMMSFSATIPQE-LRLFLKKYMDRPQTVQIEEQSAFHPKIQ---HILVPVQHKTyaeKVLE-ILPSFTPYVCLIFANTRS 253
Cdd:PRK11192 180 QTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHqwyYRADDLEHKT---ALLChLLKQPEVTRSIVFVRTRE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 254 EAANVASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELDYYIHRSGRT 333
Cdd:PRK11192 257 RVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 334 GRAGHEGICYALYEKKDDTAIRQLEvRGIH--FDHKTIKngqwcDLEPLHKKKVRKD--DPLEKEIAKivsrkkkkvkpg 409
Cdd:PRK11192 337 GRAGRKGTAISLVEAHDHLLLGKIE-RYIEepLKARVID-----ELRPKTKAPSEKKtgKPSKKVLAK------------ 398
|
410 420 430
....*....|....*....|....*....|..
gi 1589200340 410 ykkkRQQEVEKLKRKAKRAMIQEDIQRQKKER 441
Cdd:PRK11192 399 ----RAEKKEKEKEKPKVKKRHRDTKNIGKRR 426
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
17-343 |
3.96e-57 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 197.30 E-value: 3.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 17 IELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSK-------PCVqaVITAPTRELALQIYQR 89
Cdd:PTZ00110 145 LKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPllrygdgPIV--LVLAPTRELAEQIREQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 90 CEKMSeADPKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDlFLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDA 169
Cdd:PTZ00110 223 CNKFG-ASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLID-FLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRK 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 170 IAGKMRKDLQMMSFSATIPQELRLfLKKYMDRPQTVQIEEQS----AFHPKIQHILVPVQHKTYAE--KVLEILPSFTPY 243
Cdd:PTZ00110 301 IVSQIRPDRQTLMWSATWPKEVQS-LARDLCKEEPVHVNVGSldltACHNIKQEVFVVEEHEKRGKlkMLLQRIMRDGDK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 244 VcLIFANTRSEAANVASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKEL 323
Cdd:PTZ00110 380 I-LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQI 458
|
330 340
....*....|....*....|
gi 1589200340 324 DYYIHRSGRTGRAGHEGICY 343
Cdd:PTZ00110 459 EDYVHRIGRTGRAGAKGASY 478
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
9-340 |
2.50e-54 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 190.55 E-value: 2.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 9 FQKHTKMFIELEK--FIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVdSSKPCV--------QAVITAP 78
Cdd:PRK04537 14 FDLHPALLAGLESagFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRL-LSRPALadrkpedpRALILAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 79 TRELALQIYQRCEKMSeADPKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLFLNEQVLRVDTADIMVVDEADMT 158
Cdd:PRK04537 93 TRELAIQIHKDAVKFG-ADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDEADRM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 159 LEFGFLEDVDAIAGKM--RKDLQMMSFSATIPQELRLFLKKYMDRPQTVQIEEQSAFHPKI-QHILVPVQHktyaEKV-- 233
Cdd:PRK04537 172 FDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVrQRIYFPADE----EKQtl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 234 -LEILPSFTPYVCLIFANTRSEAANVASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGIS 312
Cdd:PRK04537 248 lLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
330 340
....*....|....*....|....*...
gi 1589200340 313 HVISMGFPKELDYYIHRSGRTGRAGHEG 340
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEG 355
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
22-358 |
2.73e-53 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 183.49 E-value: 2.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIyQRCEKMSEADPKLV 101
Cdd:PTZ00424 48 FEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQI-QKVVLALGDYLKVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 102 IRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQMM 181
Cdd:PTZ00424 127 CHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDM-IDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 182 SFSATIPQELRLFLKKYMDRPQTVQIEEQSAFHPKIQHILVPVQHKTYA-EKVLEILPSFTPYVCLIFANTRSEAANVAS 260
Cdd:PTZ00424 206 LFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKfDTLCDLYETLTITQAIIYCNTRRKVDYLTK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 261 NMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELDYYIHRSGRTGRAGHEG 340
Cdd:PTZ00424 286 KMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKG 365
|
330
....*....|....*...
gi 1589200340 341 ICYALYEKKDDTAIRQLE 358
Cdd:PTZ00424 366 VAINFVTPDDIEQLKEIE 383
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
2-358 |
7.54e-53 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 184.35 E-value: 7.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 2 SKYSDYMFQKHTKMFIELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQ-------AV 74
Cdd:PRK01297 87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymgeprAL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 75 ITAPTRELALQIYQRCEKMSEADPKLVIRLItGGIEKSRMIEQLKVQ-PHIVVGTPGRIKDlFLNEQVLRVDTADIMVVD 153
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTKYTGLNVMTFV-GGMDFDKQLKQLEARfCDILVATPGRLLD-FNQRGEVHLDMVEVMVLD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 154 EADMTLEFGFLEDVDAIAGK--MRKDLQMMSFSATIPQELRLFLKKYMDRPQTVQIE-EQSAFHPKIQHILVPVQHKTYa 230
Cdd:PRK01297 245 EADRMLDMGFIPQVRQIIRQtpRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEpENVASDTVEQHVYAVAGSDKY- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 231 eKVLEILPSFTPY-VCLIFANTRSEAANVASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIE 309
Cdd:PRK01297 324 -KLLYNLVTQNPWeRVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHID 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1589200340 310 GISHVISMGFPKELDYYIHRSGRTGRAGHEGICYALYEKKDDTAIRQLE 358
Cdd:PRK01297 403 GISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIE 451
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
26-194 |
2.33e-50 |
|
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: 168.19 E-value: 2.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 26 TPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEAdPKLVIRLI 105
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKG-LGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 106 TGGIEKSRMIEQLKvQPHIVVGTPGRIKDLFLNEQVLRvdTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQMMSFSA 185
Cdd:pfam00270 80 LGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKLLK--NLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156
|
....*....
gi 1589200340 186 TIPQELRLF 194
Cdd:pfam00270 157 TLPRNLEDL 165
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
3-345 |
3.29e-49 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 173.23 E-value: 3.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 3 KYSDYMFQKHTKMFIELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLI---------PIMEKVDSSKPcvQA 73
Cdd:PRK04837 9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTatfhyllshPAPEDRKVNQP--RA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 74 VITAPTRELALQIYQRCEKMSEADpKLVIRLITGG--IEKSRmiEQLKVQPHIVVGTPGRIKDlFLNEQVLRVDTADIMV 151
Cdd:PRK04837 87 LIMAPTRELAVQIHADAEPLAQAT-GLKLGLAYGGdgYDKQL--KVLESGVDILIGTTGRLID-YAKQNHINLGAIQVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 152 VDEADMTLEFGFLEDVDAIAGKM---RKDLQMMsFSATIPQELRLFLKKYMDRPQTVQIE-EQSAFHPKIQHILVPVQHk 227
Cdd:PRK04837 163 LDEADRMFDLGFIKDIRWLFRRMppaNQRLNML-FSATLSYRVRELAFEHMNNPEYVEVEpEQKTGHRIKEELFYPSNE- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 228 tyaEKV---LEILPSFTPYVCLIFANTRSEAANVASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAAR 304
Cdd:PRK04837 241 ---EKMrllQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAAR 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1589200340 305 GIDIEGISHVISMGFPKELDYYIHRSGRTGRAGHEGI-----C--YAL 345
Cdd:PRK04837 318 GLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHsislaCeeYAL 365
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
17-340 |
6.22e-49 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 173.46 E-value: 6.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 17 IELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPC------VQAVITAPTRELALQIyqrC 90
Cdd:PRK10590 16 VAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALILTPTRELAAQI---G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 91 EKMSEADPKLVIR--LITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVD 168
Cdd:PRK10590 93 ENVRDYSKYLNIRslVVFGGVSINPQMMKLRGGVDVLVATPGRLLDL-EHQNAVKLDQVEILVLDEADRMLDMGFIHDIR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 169 AIAGKMRKDLQMMSFSATIPQELRLFLKKYMDRPQTVQIEEQSAFHPKIQHILVPVQHKTYAEKVLEILPSFTPYVCLIF 248
Cdd:PRK10590 172 RVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGKGNWQQVLVF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 249 ANTRSEAANVASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELDYYIH 328
Cdd:PRK10590 252 TRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVH 331
|
330
....*....|..
gi 1589200340 329 RSGRTGRAGHEG 340
Cdd:PRK10590 332 RIGRTGRAAATG 343
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
22-205 |
1.80e-47 |
|
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: 162.08 E-value: 1.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEAdPKLV 101
Cdd:cd17940 19 FEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELALQTSQVCKELGKH-MGVK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 102 IRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQMM 181
Cdd:cd17940 98 VMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDL-AKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILNFLPKERQIL 176
|
170 180
....*....|....*....|....
gi 1589200340 182 SFSATIPQELRLFLKKYMDRPQTV 205
Cdd:cd17940 177 LFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
20-206 |
3.83e-45 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 155.50 E-value: 3.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 20 EKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEADPK 99
Cdd:cd17943 8 AGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIGKKLEG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 100 LVIRLITGGIEKSRMIEQLKvQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQ 179
Cdd:cd17943 88 LKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQL-IELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLPKNKQ 165
|
170 180
....*....|....*....|....*..
gi 1589200340 180 MMSFSATIPQELRLFLKKYMDRPQTVQ 206
Cdd:cd17943 166 VIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
22-202 |
9.66e-45 |
|
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: 154.72 E-value: 9.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKV---DSSKPCVQAVITAPTRELALQIYQRCEKMSEADP 98
Cdd:cd17947 10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSVLQQLAQFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 99 kLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLFLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDL 178
Cdd:cd17947 90 -ITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEILRLCPRTR 168
|
170 180
....*....|....*....|....
gi 1589200340 179 QMMSFSATIPQELRLFLKKYMDRP 202
Cdd:cd17947 169 QTMLFSATMTDEVKDLAKLSLNKP 192
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
21-191 |
2.41e-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: 151.19 E-value: 2.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 21 KFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKV-----DSSKPCVQAVITAPTRELALQIYQRCEKMSE 95
Cdd:cd17960 9 GFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIYEVLQSFLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 96 A-DPKLVIRLITGGIEKSRMIEQLKVQ-PHIVVGTPGRIKDLFLNEQVLR-VDTADIMVVDEADMTLEFGFLEDVDAIAG 172
Cdd:cd17960 89 HhLPKLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSRKADKVkVKSLEVLVLDEADRLLDLGFEADLNRILS 168
|
170
....*....|....*....
gi 1589200340 173 KMRKDLQMMSFSATIPQEL 191
Cdd:cd17960 169 KLPKQRRTGLFSATQTDAV 187
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
21-199 |
3.57e-43 |
|
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: 151.20 E-value: 3.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 21 KFIEPTPIQQAVI-PMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPC-----VQAVITAPTRELALQIYQRCEKMS 94
Cdd:cd17964 13 GFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAgrrsgVSALIISPTRELALQIAAEAKKLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 95 EADPKLVIRLITGGIEKSRMIEQL-KVQPHIVVGTPGRIKDLFLNEQVLRV-DTADIMVVDEADMTLEFGFLEDVDAIAG 172
Cdd:cd17964 93 QGLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVAKAfTDLDYLVLDEADRLLDMGFRPDLEQILR 172
|
170 180 190
....*....|....*....|....*....|.
gi 1589200340 173 ----KMRKDLQMMSFSATIPQELRLFLKKYM 199
Cdd:cd17964 173 hlpeKNADPRQTLLFSATVPDEVQQIARLTL 203
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
25-341 |
1.27e-42 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 157.64 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 25 PTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKV---------DSSKPCvqAVITAPTRELALQIYQRCEKMSE 95
Cdd:PLN00206 144 PTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCctirsghpsEQRNPL--AMVLTPTRELCVQVEDQAKVLGK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 96 ADPkLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMR 175
Cdd:PLN00206 222 GLP-FKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDL-LSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 176 KDlQMMSFSATIPQELRLFLKKYMDRPQTVQIEEQSAFHPKIQHILVPVQHKTYAEKVLEILPS---FTPYVcLIFANTR 252
Cdd:PLN00206 300 QP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSkqhFKPPA-VVFVSSR 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 253 ------SEAANVASNMRdagygVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELDYY 326
Cdd:PLN00206 378 lgadllANAITVVTGLK-----ALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEY 452
|
330
....*....|....*
gi 1589200340 327 IHRSGRTGRAGHEGI 341
Cdd:PLN00206 453 IHQIGRASRMGEKGT 467
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
17-209 |
6.29e-42 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 147.64 E-value: 6.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 17 IELEKFIEPTPIQQAVIPMACKG-KDIIGISATGTGKTHAFLIPIMEKVDSSKPCvQAVITAPTRELALQIYQRCEKMSE 95
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG-RVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 96 ADPKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLFLNEQVLRVDTaDIMVVDEADMTLEFGFLEDVDAIAGKMR 175
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNV-DLVILDEAHRLLDGGFGDQLEKLLKLLP 158
|
170 180 190
....*....|....*....|....*....|....
gi 1589200340 176 KDLQMMSFSATIPQELRLFLKKYMDRPQTVQIEE 209
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF 192
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
217-346 |
6.41e-41 |
|
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: 142.26 E-value: 6.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 217 IQHILVPVQHKTYAEKVLEILPSFTPYV-CLIFANTRSEAANVASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSY 295
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGkAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1589200340 296 VVATDIAARGIDIEGISHVISMGFPKELDYYIHRSGRTGRAGHEGICYALY 346
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
25-186 |
7.09e-40 |
|
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: 142.07 E-value: 7.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 25 PTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSeADPKLVIRL 104
Cdd:cd17954 23 PTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELAQQISEQFEALG-SSIGLKSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 105 ITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLFLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQMMSFS 184
Cdd:cd17954 102 LVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLNMDFEPEIDKILKVIPRERTTYLFS 181
|
..
gi 1589200340 185 AT 186
Cdd:cd17954 182 AT 183
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
21-197 |
7.32e-39 |
|
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: 139.64 E-value: 7.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 21 KFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKV------DSSKPCVQAVITAPTRELALQIYQRCEKMS 94
Cdd:cd17961 13 GWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQVSKVLEQLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 95 EA-DPKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLFLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGK 173
Cdd:cd17961 93 AYcRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSYGYEEDLKSLLSY 172
|
170 180
....*....|....*....|....
gi 1589200340 174 MRKDLQMMSFSATIPQELRLfLKK 197
Cdd:cd17961 173 LPKNYQTFLMSATLSEDVEA-LKK 195
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
24-206 |
8.02e-39 |
|
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: 139.28 E-value: 8.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 24 EPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIyqrCEKMSEADPKLVIR 103
Cdd:cd17955 21 EPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELAYQI---AEQFRALGAPLGLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 104 --LITGGIEksrMIEQ---LKVQPHIVVGTPGRIKDLFLNEQVLRVDTADI--MVVDEADMTLEFGFLEDVDAIAGKMRK 176
Cdd:cd17955 98 ccVIVGGMD---MVKQaleLSKRPHIVVATPGRLADHLRSSDDTTKVLSRVkfLVLDEADRLLTGSFEDDLATILSALPP 174
|
170 180 190
....*....|....*....|....*....|
gi 1589200340 177 DLQMMSFSATIPQELRLFLKKYMDRPQTVQ 206
Cdd:cd17955 175 KRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
21-205 |
6.85e-38 |
|
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: 136.65 E-value: 6.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 21 KFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSK----PCVQAVITAPTRELALQIYQRCEK---- 92
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERwtpeDGLGALIISPTRELAMQIFEVLRKvgky 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 93 --MSEAdpklvirLITGGieKSRMIEQLKV-QPHIVVGTPGRIkdLFLNEQVLRVDTAD--IMVVDEADMTLEFGFLEDV 167
Cdd:cd17941 89 hsFSAG-------LIIGG--KDVKEEKERInRMNILVCTPGRL--LQHMDETPGFDTSNlqMLVLDEADRILDMGFKETL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1589200340 168 DAIAGKMRKDLQMMSFSATIPQELRLFLKKYMDRPQTV 205
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
25-206 |
1.40e-37 |
|
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: 135.90 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 25 PTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCV--QAVITAPTRELALQIYQRCEKMSEADpKLVI 102
Cdd:cd17959 24 PTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVgaRALILSPTRELALQTLKVTKELGKFT-DLRT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 103 RLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLFLnEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQMMS 182
Cdd:cd17959 103 ALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLV-EMNLKLSSVEYVVFDEADRLFEMGFAEQLHEILSRLPENRQTLL 181
|
170 180
....*....|....*....|....
gi 1589200340 183 FSATIPQELRLFLKKYMDRPQTVQ 206
Cdd:cd17959 182 FSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
21-202 |
1.46e-37 |
|
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: 135.79 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 21 KFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKV--DSSKPCVQAVITAPTRELALQIYQRCEKMSEADP 98
Cdd:cd17957 9 GYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYRELLKLSKGTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 99 kLVIRLITGGIE-KSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIagkMR-- 175
Cdd:cd17957 89 -LRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFL-LKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI---LAac 163
|
170 180
....*....|....*....|....*....
gi 1589200340 176 --KDLQMMSFSATIPQELRLFLKKYMDRP 202
Cdd:cd17957 164 tnPNLQRSLFSATIPSEVEELARSVMKDP 192
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
22-205 |
4.35e-37 |
|
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: 135.14 E-value: 4.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKP-----CVQ---AVITAPTRELALQIYQRCEKM 93
Cdd:cd17945 10 YKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPldeetKDDgpyALILAPTRELAQQIEEETQKF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 94 SEadpKLVIRL--ITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIA 171
Cdd:cd17945 90 AK---PLGIRVvsIVGGHSIEEQAFSLRNGCEILIATPGRLLDC-LERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1589200340 172 GKM--------------------RKDLQMMSFSATIPQELRLFLKKYMDRPQTV 205
Cdd:cd17945 166 DAMpvsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
17-206 |
9.79e-37 |
|
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: 134.43 E-value: 9.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 17 IELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQ-----AVITAPTRELALQIYQRCE 91
Cdd:cd17953 27 IKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPgegpiGLIMAPTRELALQIYVECK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 92 KMSEAdpkLVIRLI--TGGIEKSRMIEQLKVQPHIVVGTPGRIKDLFL--NEQVLRVDTADIMVVDEADMTLEFGFLEDV 167
Cdd:cd17953 107 KFSKA---LGLRVVcvYGGSGISEQIAELKRGAEIVVCTPGRMIDILTanNGRVTNLRRVTYVVLDEADRMFDMGFEPQI 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1589200340 168 DAIAGKMRKDLQMMSFSATIPQELRLFLKKYMDRPQTVQ 206
Cdd:cd17953 184 MKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
20-198 |
5.28e-36 |
|
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: 131.72 E-value: 5.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 20 EKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQ-----AVITAPTRELALQIYQRCEKMS 94
Cdd:cd17966 8 QGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERgdgpiVLVLAPTRELAQQIQQEANKFG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 95 EADpKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDlFLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKM 174
Cdd:cd17966 88 GSS-RLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLID-FLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQI 165
|
170 180
....*....|....*....|....*...
gi 1589200340 175 RKDLQMMSFSATIPQELRL----FLKKY 198
Cdd:cd17966 166 RPDRQTLMWSATWPKEVRRlaedFLKDY 193
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
22-202 |
1.71e-35 |
|
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: 130.14 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEAdPKLV 101
Cdd:cd17939 17 FEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALGDY-MGVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 102 IRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQMM 181
Cdd:cd17939 96 VHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDM-LQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPETQVV 174
|
170 180
....*....|....*....|.
gi 1589200340 182 SFSATIPQELRLFLKKYMDRP 202
Cdd:cd17939 175 LFSATMPHEVLEVTKKFMRDP 195
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
22-202 |
5.24e-35 |
|
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: 129.39 E-value: 5.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEADPKLV 101
Cdd:cd17950 22 FEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISNEYERFSKYMPNVK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 102 IRLITGGIEKSRMIEQLK-VQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMtlefgFLEDVDaiagkMRKDL-- 178
Cdd:cd17950 102 TAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILAL-VREKKLKLSHVKHFVLDECDK-----MLEQLD-----MRRDVqe 170
|
170 180 190
....*....|....*....|....*....|...
gi 1589200340 179 ---------QMMSFSATIPQELRLFLKKYMDRP 202
Cdd:cd17950 171 ifratphdkQVMMFSATLSKEIRPVCKKFMQDP 203
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
22-202 |
1.85e-34 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 127.56 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEAdPKLV 101
Cdd:cd18046 19 FEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELAQQIQKVVMALGDY-MGIK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 102 IRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQMM 181
Cdd:cd18046 98 CHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDM-INRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDTQVV 176
|
170 180
....*....|....*....|.
gi 1589200340 182 SFSATIPQELRLFLKKYMDRP 202
Cdd:cd18046 177 LLSATMPNDVLEVTTKFMRDP 197
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
21-205 |
5.06e-34 |
|
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: 126.68 E-value: 5.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 21 KFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIP-IMEKVDSSK--PCVQ-----AVITAPTRELALQIYQRCEK 92
Cdd:cd17951 9 GIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEKklPFIKgegpyGLIVCPSRELARQTHEVIEY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 93 MSEA-----DPKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDV 167
Cdd:cd17951 89 YCKAlqeggYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDM-LNKKKINLDICRYLCLDEADRMIDMGFEEDI 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1589200340 168 DAIAGKMRKDLQMMSFSATIPQELRLFLKKYMDRPQTV 205
Cdd:cd17951 168 RTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
17-198 |
1.07e-33 |
|
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: 126.06 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 17 IELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKV----------DSSKPCVQAVITAPTRELALQI 86
Cdd:cd17967 15 IKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvgrGRRKAYPSALILAPTRELAIQI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 87 YQRCEKMSEaDPKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDlFLNEQVLRVDTADIMVVDEADMTLEFGFLED 166
Cdd:cd17967 95 YEEARKFSY-RSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVD-FIERGRISLSSIKFLVLDEADRMLDMGFEPQ 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1589200340 167 VDAIAGKM----RKDLQMMSFSATIPQEL-RL---FLKKY 198
Cdd:cd17967 173 IRKIVEHPdmppKGERQTLMFSATFPREIqRLaadFLKNY 212
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
22-202 |
2.57e-33 |
|
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: 124.45 E-value: 2.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIP----IMEKVDSSK---PCvqAVITAPTRELALQIYQRCEKMS 94
Cdd:cd17952 10 YEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPmlvhIMDQRELEKgegPI--AVIVAPTRELAQQIYLEAKKFG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 95 EAdPKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKM 174
Cdd:cd17952 88 KA-YNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDM-VKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVGHV 165
|
170 180
....*....|....*....|....*...
gi 1589200340 175 RKDLQMMSFSATIPQELRLFLKKYMDRP 202
Cdd:cd17952 166 RPDRQTLLFSATFKKKIEQLARDILSDP 193
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
17-205 |
4.89e-33 |
|
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: 123.73 E-value: 4.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 17 IELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDS------SKPCVQAVITAPTRELALQIYQRC 90
Cdd:cd17958 5 IKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLqpipreQRNGPGVLVLTPTRELALQIEAEC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 91 EKMSEADPKLVIrlITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLFLNeQVLRVDTADIMVVDEADMTLEFGFLEDVDAI 170
Cdd:cd17958 85 SKYSYKGLKSVC--VYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMN-NVINLKSITYLVLDEADRMLDMGFEPQIRKI 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1589200340 171 AGKMRKDLQMMSFSATIPQELRLFLKKYMDRPQTV 205
Cdd:cd17958 162 LLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
21-197 |
2.64e-32 |
|
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: 122.73 E-value: 2.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 21 KFIEPTPIQQAVIPMACK-GKDIIGISATGTGKTHAFLIPIMEKV----------DSSKPCvQAVITAPTRELALQIYQR 89
Cdd:cd17946 9 GFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlsqkssngvgGKQKPL-RALILTPTRELAVQVKDH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 90 CEKMSeADPKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLFL--NEQVLRVDTADIMVVDEADMTLEFGFLEDV 167
Cdd:cd17946 88 LKAIA-KYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQegNEHLANLKSLRFLVLDEADRMLEKGHFAEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1589200340 168 DAIAGKM-------RKDLQMMSFSATI----PQELRLFLKK 197
Cdd:cd17946 167 EKILELLnkdragkKRKRQTFVFSATLtldhQLPLKLNSKK 207
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
21-176 |
6.10e-32 |
|
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: 121.15 E-value: 6.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 21 KFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQ------AVITAPTRELALQIYQRCEKMS 94
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 95 EADPKLVIRLITGG----IEKSRmieqLKVQPHIVVGTPGRIKDLFLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAI 170
Cdd:cd17949 90 KPFHWIVPGYLIGGekrkSEKAR----LRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKI 165
|
....*.
gi 1589200340 171 AGKMRK 176
Cdd:cd17949 166 LELLDD 171
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
25-202 |
1.02e-31 |
|
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: 119.96 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 25 PTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEADPKLVIRL 104
Cdd:cd17962 13 PTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGLPPMKTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 105 ITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQMMSFS 184
Cdd:cd17962 93 LVGGLPLPPQLYRLQQGVKVIIATPGRLLDI-LKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQTILVS 171
|
170
....*....|....*...
gi 1589200340 185 ATIPQELRLFLKKYMDRP 202
Cdd:cd17962 172 ATIPRGIEQLAGQLLQNP 189
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
21-207 |
1.34e-31 |
|
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: 119.60 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 21 KFIEPTPIQQAVIPMACKG--KDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEAdP 98
Cdd:cd17963 13 GFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQIGEVVEKMGKF-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 99 KLVIRLITGGIEKSRmieQLKVQPHIVVGTPGRIKDLFlneQVLRVDTADI--MVVDEADMTLEF-GFLEDVDAIAGKMR 175
Cdd:cd17963 92 GVKVALAVPGNDVPR---GKKITAQIVIGTPGTVLDWL---KKRQLDLKKIkiLVLDEADVMLDTqGHGDQSIRIKRMLP 165
|
170 180 190
....*....|....*....|....*....|..
gi 1589200340 176 KDLQMMSFSATIPQELRLFLKKYMdrPQTVQI 207
Cdd:cd17963 166 RNCQILLFSATFPDSVRKFAEKIA--PNANTI 195
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
17-196 |
2.33e-31 |
|
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: 120.84 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 17 IELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEK-----VDSSKPC----VQAVITAPTRELALQIY 87
Cdd:cd18052 58 IRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGmmkegLTASSFSevqePQALIVAPTRELANQIF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 88 QRCEKMSEADpklVIR--LITGGIEKSRMIEQLKVQPHIVVGTPGRIKDlFLNEQVLRVDTADIMVVDEADMTLEFGFLE 165
Cdd:cd18052 138 LEARKFSYGT---CIRpvVVYGGVSVGHQIRQIEKGCHILVATPGRLLD-FIGRGKISLSKLKYLILDEADRMLDMGFGP 213
|
170 180 190
....*....|....*....|....*....|....*....
gi 1589200340 166 DVDAIAGK----MRKDLQMMSFSATIPQEL-RL---FLK 196
Cdd:cd18052 214 EIRKLVSEpgmpSKEDRQTLMFSATFPEEIqRLaaeFLK 252
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
15-205 |
3.40e-31 |
|
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: 118.96 E-value: 3.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 15 MFIELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEkvdsskpCVQAVITAPTRELALQIYQRCEKMS 94
Cdd:cd17938 12 KAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-------IVVALILEPSRELAEQTYNCIENFK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 95 E--ADPKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDlFLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAG 172
Cdd:cd17938 85 KylDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLED-LIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1589200340 173 KM------RKDLQMMSFSATIPQ-ELRLFLKKYMDRPQTV 205
Cdd:cd17938 164 RIpkitsdGKRLQVIVCSATLHSfEVKKLADKIMHFPTWV 203
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
3-199 |
1.44e-29 |
|
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: 115.49 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 3 KYSDYMFQKHTKMFIELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDsSKPCVQ------AVIT 76
Cdd:cd18049 25 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHIN-HQPFLErgdgpiCLVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 77 APTRELALQIYQRCEKMSEAdPKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDlFLNEQVLRVDTADIMVVDEAD 156
Cdd:cd18049 104 APTRELAQQVQQVAAEYGRA-CRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID-FLEAGKTNLRRCTYLVLDEAD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1589200340 157 MTLEFGFLEDVDAIAGKMRKDLQMMSFSATIPQELRL----FLKKYM 199
Cdd:cd18049 182 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQlaedFLKDYI 228
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
13-186 |
9.85e-28 |
|
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: 109.37 E-value: 9.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 13 TKMFIELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSK----PCVQAVITAPTRELALQIYQ 88
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKfkprNGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 89 RCEKMSEADPKLViRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLFLNEQVLRVDTADIMVVDEADMTLEFGFLEDVD 168
Cdd:cd17942 81 VAKELLKYHSQTF-GIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMR 159
|
170
....*....|....*...
gi 1589200340 169 AIAGKMRKDLQMMSFSAT 186
Cdd:cd17942 160 QIIKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
20-199 |
4.72e-27 |
|
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: 109.33 E-value: 4.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 20 EKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDsSKPCVQ------AVITAPTRELALQIYQRCEKM 93
Cdd:cd18050 80 QNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHIN-HQPYLErgdgpiCLVLAPTRELAQQVQQVADDY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 94 SEADpKLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDlFLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGK 173
Cdd:cd18050 159 GKSS-RLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID-FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ 236
|
170 180 190
....*....|....*....|....*....|
gi 1589200340 174 MRKDLQMMSFSATIPQELRL----FLKKYM 199
Cdd:cd18050 237 IRPDRQTLMWSATWPKEVRQlaedFLRDYV 266
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
17-199 |
1.43e-26 |
|
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: 107.43 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 17 IELEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQ----------------AVITAPTR 80
Cdd:cd18051 36 IELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESlpsesgyygrrkqyplALVLAPTR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 81 ELALQIYQRCEKM---SEADPKLVIrlitGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADM 157
Cdd:cd18051 116 ELASQIYDEARKFayrSRVRPCVVY----GGADIGQQMRDLERGCHLLVATPGRLVDM-LERGKIGLDYCKYLVLDEADR 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1589200340 158 TLEFGFLEDVDAIAGK--MRK--DLQMMSFSATIPQEL----RLFLKKYM 199
Cdd:cd18051 191 MLDMGFEPQIRRIVEQdtMPPtgERQTLMFSATFPKEIqmlaRDFLDNYI 240
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
22-202 |
1.60e-25 |
|
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: 103.32 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEAdPKLV 101
Cdd:cd18045 19 FEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELAVQIQKVLLALGDY-MNVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 102 IRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIAGKMRKDLQMM 181
Cdd:cd18045 98 CHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDM-IRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVV 176
|
170 180
....*....|....*....|.
gi 1589200340 182 SFSATIPQELRLFLKKYMDRP 202
Cdd:cd18045 177 LVSATLPQDILEMTNKFMTDP 197
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
27-208 |
3.99e-25 |
|
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: 102.23 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 27 PIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCV------QAVITAPTRELALQIyqrCEKMSEADPKL 100
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQV---TKDFKDITRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 101 VIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLFLNEQvLRVDTADIMVVDEADMTLEFGFLEDV-DAIAGKMRKDL- 178
Cdd:cd17944 92 SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLDMGFAEQVeEILSVSYKKDSe 170
|
170 180 190
....*....|....*....|....*....|...
gi 1589200340 179 ---QMMSFSATIPQELRLFLKKYMdRPQTVQIE 208
Cdd:cd17944 171 dnpQTLLFSATCPDWVYNVAKKYM-KSQYEQVD 202
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
231-337 |
1.19e-23 |
|
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: 94.97 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 231 EKVLEILPSFTPYVCLIFANTRSEAANVASnMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEG 310
Cdd:pfam00271 4 EALLELLKKERGGKVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
|
90 100
....*....|....*....|....*..
gi 1589200340 311 ISHVISMGFPKELDYYIHRSGRTGRAG 337
Cdd:pfam00271 83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
258-337 |
9.57e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 88.81 E-value: 9.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 258 VASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELDYYIHRSGRTGRAG 337
Cdd:smart00490 3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
23-200 |
2.73e-21 |
|
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: 92.04 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 23 IEPTPIQQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKV--DSSKPCVQ-----AVITAPTRELALQIYQRCEKMSE 95
Cdd:cd17948 11 TKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrYKLLAEGPfnaprGLVITPSRELAEQIGSVAQSLTE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 96 ADPkLVIRLITGGIEKSRMIEQLKVQPHIVVGTPGRIKDLfLNEQVLRVDTADIMVVDEADMTLEFGFLEDVDAIA---- 171
Cdd:cd17948 91 GLG-LKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKL-LTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLrrfp 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1589200340 172 -GKMRKDL--------QMMSFSATIPQELRLFLKKYMD 200
Cdd:cd17948 169 lASRRSENtdgldpgtQLVLVSATMPSGVGEVLSKVID 206
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
22-210 |
3.67e-21 |
|
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: 91.62 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPM--ACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSE--AD 97
Cdd:cd18048 38 FNRPSKIQENALPMmlADPPQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFELALQTGKVVEEMGKfcVG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 98 PKlVIRLITGgiekSRMIEQLKVQPHIVVGTPGRIKDLFLNEQVLRVDTADIMVVDEADMTLEF-GFLEDVDAIAGKMRK 176
Cdd:cd18048 118 IQ-VIYAIRG----NRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVTNISVFVLDEADVMINVqGHSDHSVRVKRSMPK 192
|
170 180 190
....*....|....*....|....*....|....
gi 1589200340 177 DLQMMSFSATIPQELRLFLKKYMDRPQTVQIEEQ 210
Cdd:cd18048 193 ECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKE 226
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
21-194 |
2.22e-19 |
|
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: 86.53 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 21 KFIEPTPIQQAVIPM-----ACKGKDIIG---ISA-TGTGKTHAFLIPIMEKV-DSSKPCVQAVITAPTRELALQIYQRC 90
Cdd:cd17956 9 GITSAFPVQAAVIPWllpssKSTPPYRPGdlcVSApTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKELVQQVYKVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 91 EKMSEADPkLVIRLITGGIEKSRMIEQLKVQPH--------IVVGTPGRIKDlFLNE------QVLRvdtadIMVVDEAD 156
Cdd:cd17956 89 ESLCKGTG-LKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVD-HLNStpgftlKHLR-----FLVIDEAD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1589200340 157 MTLE---FGFLEDVDAIAGKMRKD-----------------LQMMSFSATIPQ------ELRLF 194
Cdd:cd17956 162 RLLNqsfQDWLETVMKALGRPTAPdlgsfgdanllersvrpLQKLLFSATLTRdpeklsSLKLH 225
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
23-227 |
3.22e-18 |
|
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: 83.97 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 23 IEPTPIQQAVIPMACK---------------GKDIIGISA-TGTGKTHAFLIPIMEK-------------------VDSS 67
Cdd:cd17965 29 IKPSPIQTLAIKKLLKtlmrkvtkqtsneepKLEVFLLAAeTGSGKTLAYLAPLLDYlkrqeqepfeeaeeeyesaKDTG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 68 KPcvQAVITAPTRELALQIYQRCEKMSEAdPKLVIRLITGGIEKS--RMIEQLKVQPHIVVGTPGRIKDLF-LNEQVL-R 143
Cdd:cd17965 109 RP--RSVILVPTHELVEQVYSVLKKLSHT-VKLGIKTFSSGFGPSyqRLQLAFKGRIDILVTTPGKLASLAkSRPKILsR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 144 VDTAdimVVDEADMTLEFGFLEDVDAIAGKMRKDLQMMSFSATIPQElrlfLKKYMDRpqtvqieeqsaFHPKIQHILVP 223
Cdd:cd17965 186 VTHL---VVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKE----FDKTLRK-----------LFPDVVRIATP 247
|
....
gi 1589200340 224 VQHK 227
Cdd:cd17965 248 RLHA 251
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
22-206 |
5.51e-18 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 82.08 E-value: 5.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 22 FIEPTPIQQAVIPM--ACKGKDIIGISATGTGKTHAFLIPIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEADPK 99
Cdd:cd18047 21 FNRPSKIQENALPLmlAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 100 LVIRLITGGiekSRMIEQLKVQPHIVVGTPGRIKDLFLNEQVLRVDTADIMVVDEAD-MTLEFGFLEDVDAIAGKMRKDL 178
Cdd:cd18047 101 LKLAYAVRG---NKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMIATQGHQDQSIRIQRMLPRNC 177
|
170 180
....*....|....*....|....*...
gi 1589200340 179 QMMSFSATIPQELRLFLKKYMDRPQTVQ 206
Cdd:cd18047 178 QMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
39-186 |
9.69e-17 |
|
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: 77.06 E-value: 9.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 39 GKDIIGISATGTGKTHAFLIPIMEKVDSSKPcvQAVITAPTRELALQIYQRCekMSEADPKLVIRLITGGI---EKSRMI 115
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGK--KVLVLVPTKALALQTAERL--RELFGPGIRVAVLVGGSsaeEREKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589200340 116 EQLKvqpHIVVGTPGRIKDLFLNEQVLRVDTADIMVVDEADMTL--EFGFLEDVDAIAGKMRKDLQMMSFSAT 186
Cdd:cd00046 77 LGDA---DIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLidSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
29-341 |
1.52e-13 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 72.95 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 29 QQAVIPMACKGKDIIGISATGTGKTHAFLIPIMEKVdSSKPCVQAVITAPTRELALQIYQRCEKMSEA-DPKLVIRLITG 107
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPTKALARDQLRRLRELAEAlGLGVRVATYDG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 108 GI---EKSRMIEQlkvqPHIVVGTPgrikDlFLNEQVLRVDTA--------DIMVVDEADmTLE--FGfledvdA----- 169
Cdd:COG1205 140 DTppeERRWIREH----PDIVLTNP----D-MLHYGLLPHHTRwarffrnlRYVVIDEAH-TYRgvFG------Shvanv 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 170 ------IAGKMRKDLQMMSFSATI--PQEL--RLFlkkymDRPQTVqIEEQSAFHPKIQHILV-------PVQHKTYAEk 232
Cdd:COG1205 204 lrrlrrICRHYGSDPQFILASATIgnPAEHaeRLT-----GRPVTV-VDEDGSPRGERTFVLWnpplvddGIRRSALAE- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 233 VLEILPSFT--PYVCLIFANTRSEAANVASNMRD-----------AGYgvielHGDLTPRERTKAMKDLSNLQKSYVVAT 299
Cdd:COG1205 277 AARLLADLVreGLRTLVFTRSRRGAELLARYARRalrepdladrvAAY-----RAGYLPEERREIERGLRSGELLGVVST 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1589200340 300 DiaA--RGIDIEGISHVISMGFPKELDYYIHRSGRTGRAGHEGI 341
Cdd:COG1205 352 N--AleLGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSL 393
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
20-338 |
1.34e-10 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 63.58 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 20 EKFIEPTPIQQAVIPMACKGKDIIGISATGTGKTHA-FLIPIMEKVDSSKPC-----VQAV-ITaPTRELALQIYQR--- 89
Cdd:COG1201 20 ARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAaFLPALDELARRPRPGelpdgLRVLyIS-PLKALANDIERNlra 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 90 -CEKMSEAdPKLVIRLITGGI--------EKSRMIEQLkvqPHIVVGTPgriKDLFL------NEQVLRvdTADIMVVDE 154
Cdd:COG1201 99 pLEEIGEA-AGLPLPEIRVGVrtgdtpasERQRQRRRP---PHILITTP---ESLALlltspdARELLR--GVRTVIVDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 155 ----------ADMTLefgFLEDVDAIAGKmrkDLQMMSFSATI--PQELRLFLKKYMDRPQTVQIEEQSAFHPKIQhILV 222
Cdd:COG1201 170 ihalagskrgVHLAL---SLERLRALAPR---PLQRIGLSATVgpLEEVARFLVGYEDPRPVTIVDAGAGKKPDLE-VLV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 223 PVQHKTYA------------EKVLE-ILPSFTpyvCLIFANTRSEAANVASNMRDA---GYGVIEL-HGDLTPRERTKAM 285
Cdd:COG1201 243 PVEDLIERfpwaghlwphlyPRVLDlIEAHRT---TLVFTNTRSQAERLFQRLNELnpeDALPIAAhHGSLSREQRLEVE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1589200340 286 KDLSNLQKSYVVAT---DIaarGIDIEGISHVISMGFPKeldyyihrsG------RTGRAGH 338
Cdd:COG1201 320 EALKAGELRAVVATsslEL---GIDIGDVDLVIQVGSPK---------SvarllqRIGRAGH 369
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
26-157 |
4.93e-09 |
|
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: 55.73 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 26 TPIQQAVIPMACKGKDIIGISA-TGTGKTHAFLIPIMEKVDSSKPCVqaVITAPTRELALQIYQRCEKMSEADPKLVIRL 104
Cdd:cd17921 3 NPIQREALRALYLSGDSVLVSApTSSGKTLIAELAILRALATSGGKA--VYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1589200340 105 ITGGIEKSRMIEqlkvQPHIVVGTPGRIKDLFLNEQVLRVDTADIMVVDEADM 157
Cdd:cd17921 81 TGDPSVNKLLLA----EADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHL 129
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
245-339 |
6.54e-09 |
|
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: 54.58 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 245 CLIFANTRSEAANVASNMRDAGY-----GVIELH-GDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMG 318
Cdd:cd18796 41 TLVFTNTRSQAERLAQRLRELCPdrvppDFIALHhGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
90 100
....*....|....*....|.
gi 1589200340 319 FPKELDYYIHRSGRTGRAGHE 339
Cdd:cd18796 121 SPKSVARLLQRLGRSGHRPGA 141
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
45-450 |
1.13e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 57.34 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 45 ISATGTGKTHAFLIpIMEKVDSSKPcvqAVITAPTRELALQIYQRCEKmseadpKLVIRLITGGIEKSrmieqlkvQPHI 124
Cdd:COG1061 106 VAPTGTGKTVLALA-LAAELLRGKR---VLVLVPRRELLEQWAEELRR------FLGDPLAGGGKKDS--------DAPI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 125 VVGTPgrikDLFLNEQVLR--VDTADIMVVDEA--------DMTLEFG------------FLEDVDAIAGKMRKDLqmmS 182
Cdd:COG1061 168 TVATY----QSLARRAHLDelGDRFGLVIIDEAhhagapsyRRILEAFpaayrlgltatpFRSDGREILLFLFDGI---V 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 183 FSATIPQELRL-FLKKYMDRPQTVQIEEQSAFHPKIQHILVP--VQHKTYAEKVL-EILPSFTPYV-CLIFANTRSEAAN 257
Cdd:COG1061 241 YEYSLKEAIEDgYLAPPEYYGIRVDLTDERAEYDALSERLREalAADAERKDKILrELLREHPDDRkTLVFCSSVDHAEA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 258 VASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELDYYIHRSGR---TG 334
Cdd:COG1061 321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRglrPA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 335 RAGHEGICYALY----EKKDDTAIRQLEVRGIHFDHKTIKNGQWCDLEPLHKKKVRKDDPLEKEIAKIVSRKKKKVKPGY 410
Cdd:COG1061 401 PGKEDALVYDFVgndvPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVL 480
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1589200340 411 KKKRQQEVEKLKRKAKRAMIQEDIQRQKKERAKQKMLEKR 450
Cdd:COG1061 481 AELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLAL 520
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
39-195 |
8.81e-08 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 51.82 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 39 GKDIIGISATGTGKTHAFLIPIMEKV-DSSKPCVQAVITAPTRELALQIYQRCEKM-SEADPKLVIRLITGGIEKSRMIE 116
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPlDEIDLEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 117 QLKVQPHIVVGTPGRIKDLFLNEQvLRVDTADI--MVVDE--ADMTLEFG-----FLEDVDAIAGkmrKDLQMMSFSATI 187
Cdd:cd17922 81 QLKNPPGILITTPESLELLLVNKK-LRELFAGLryVVVDEihALLGSKRGvqlelLLERLRKLTG---RPLRRIGLSATL 156
|
170
....*....|
gi 1589200340 188 --PQELRLFL 195
Cdd:cd17922 157 gnLEEAAAFL 166
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
224-357 |
1.66e-07 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 53.22 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 224 VQHKTYAEK---VLEILPSFTPYVCLIFANTRSEAANVASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATd 300
Cdd:COG0514 209 VVPKPPDDKlaqLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT- 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1589200340 301 IA-ARGIDIEGISHVISMGFPKELDYYIHRSGRTGRAGHEGICYALYEKKDDTAIRQL 357
Cdd:COG0514 288 IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFF 345
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
19-338 |
1.79e-07 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 53.74 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 19 LEKFIEPTPIQQAVIPMACKGKDIIGISATGTGKT-HAFLIPI-----MEKVDSSKPCVQAVITAPTRELA--------- 83
Cdd:PRK13767 27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAIIdelfrLGREGELEDKVYCLYVSPLRALNndihrnlee 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 84 -LQ-IYQRCEKMSEADPKLVIRLITGGI---EKSRMieqLKVQPHIVVGTPGRIKDLfLN----EQVLRvdTADIMVVDE 154
Cdd:PRK13767 107 pLTeIREIAKERGEELPEIRVAIRTGDTssyEKQKM---LKKPPHILITTPESLAIL-LNspkfREKLR--TVKWVIVDE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 155 ----------ADMTLefgFLEDVDAIAGkmrKDLQMMSFSATI--PQELRLFLKKYMD--RPQTVQIEEQSAFHPKIQHI 220
Cdd:PRK13767 181 ihslaenkrgVHLSL---SLERLEELAG---GEFVRIGLSATIepLEEVAKFLVGYEDdgEPRDCEIVDARFVKPFDIKV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 221 LVPV-----------QHKTYAEKVLEILPSFTpyvCLIFANTRSEAANVASNMR---DAGYGV--IEL-HGDLTPRERTK 283
Cdd:PRK13767 255 ISPVddlihtpaeeiSEALYETLHELIKEHRT---TLIFTNTRSGAERVLYNLRkrfPEEYDEdnIGAhHSSLSREVRLE 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1589200340 284 AMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELDYYIHrsgRTGRAGH 338
Cdd:PRK13767 332 VEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQ---RIGRAGH 383
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
269-346 |
4.09e-07 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350178 [Multi-domain] Cd Length: 171 Bit Score: 49.84 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 269 VIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELdYYIHRSG----------------R 332
Cdd:cd18791 77 VLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEK-VYDPRTGlsslvtvwiskasaeqR 155
|
90
....*....|....*.
gi 1589200340 333 TGRAGH--EGICYALY 346
Cdd:cd18791 156 AGRAGRtrPGKCYRLY 171
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
246-346 |
4.13e-07 |
|
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: 49.13 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 246 LIFANTRSEAANVASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELDY 325
Cdd:cd18794 34 IIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMES 113
|
90 100
....*....|....*....|.
gi 1589200340 326 YIHRSGRTGRAGHEGICYALY 346
Cdd:cd18794 114 YYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
49-200 |
6.96e-07 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 49.34 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 49 GTGKTHAFLIPIMEKVDSSKpcvQAVITAPTRELALQIYQRCEKMSeadPKLVIRLITGGIEksrmiEQLKVQPHIVVGT 128
Cdd:cd17918 46 GSGKTLVALGAALLAYKNGK---QVAILVPTEILAHQHYEEARKFL---PFINVELVTGGTK-----AQILSGISLLVGT 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589200340 129 PGRI--KDLFLNeqvlrvdtADIMVVDEADmtlEFGfLEDVDAIAGKMRKDLQMMsfSAT-IPQELRLFLKKYMD 200
Cdd:cd17918 115 HALLhlDVKFKN--------LDLVIVDEQH---RFG-VAQREALYNLGATHFLEA--TATpIPRTLALALSGLLD 175
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
36-155 |
4.02e-06 |
|
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: 47.19 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 36 ACKGKDIIGISATGTGKTHAFLIPIMEKVdSSKPCVQAVITAPTRELALQIYQRCEK-MSEADPKLVIRLITGGIEKSRM 114
Cdd:cd17923 12 ARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAQDQLRSLRElLEQLGLGIRVATYDGDTPREER 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1589200340 115 IEQLKVQPHIVVGTPgrikDLfLNEQVLRVDTADI--------MVVDEA 155
Cdd:cd17923 91 RAIIRNPPRILLTNP----DM-LHYALLPHHDRWArflrnlryVVLDEA 134
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
245-337 |
1.66e-05 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 44.56 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 245 CLIFANTRSEAANVASNMRDAGYGVIEL-------HGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISM 317
Cdd:cd18797 38 TIVFCRSRKLAELLLRYLKARLVEEGPLaskvasyRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117
|
90 100
....*....|....*....|
gi 1589200340 318 GFPKELDYYIHRSGRTGRAG 337
Cdd:cd18797 118 GYPGSLASLWQQAGRAGRRG 137
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
296-343 |
1.76e-05 |
|
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: 42.69 E-value: 1.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1589200340 296 VVATDIAARGIDIEGISHVISMGFPKELDYYIHRSGRTGRAG-HEGICY 343
Cdd:cd18785 26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVI 74
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
246-361 |
2.26e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 43.73 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 246 LIFANTRSEAANVASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVISMGFPKELDY 325
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90 100 110
....*....|....*....|....*....|....*.
gi 1589200340 326 YIHRSGRTGRAGHEGICYALYEKKDDTAIRQLEVRG 361
Cdd:PLN03137 764 YHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQG 799
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
45-155 |
1.03e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 39.58 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 45 ISATGTGKTHAFLIpIMEKVDSSKPCVQAVITAPTRELALQIYQRCEKMSEADPKLVIrlITGGIEKSRMIEQLKvqphI 124
Cdd:pfam04851 29 VMATGSGKTLTAAK-LIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGE--IISGDKKDESVDDNK----I 101
|
90 100 110
....*....|....*....|....*....|..
gi 1589200340 125 VVGTPGRI-KDLFLNEQVLRVDTADIMVVDEA 155
Cdd:pfam04851 102 VVTTIQSLyKALELASLELLPDFFDVIIIDEA 133
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
150-337 |
1.35e-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: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 150 MVVDEADMTLEF--GFLEDVDAIAgkMRKDLQMMSFSATIPQELRLFLKKyMDRPQTVQIEEQSAF--HPKIQHILVPVQ 225
Cdd:cd09639 127 LIFDEVHFYDEYtlALILAVLEVL--KDNDVPILLMSATLPKFLKEYAEK-IGYVEENEPLDLKPNerAPFIKIESDKVG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 226 HKTYAEKVLEILPSFTPyvCLIFANTRSEAANVASNMRDAGYG--VIELHGDLTPRERTKA----MKDLSNLQKSYVVAT 299
Cdd:cd09639 204 EISSLERLLEFIKKGGS--VAIIVNTVDRAQEFYQQLKEKGPEeeIMLIHSRFTEKDRAKKeaelLLEFKKSEKFVIVAT 281
|
170 180 190
....*....|....*....|....*....|....*...
gi 1589200340 300 DIAARGIDIEgISHVISMGFPkeLDYYIHRSGRTGRAG 337
Cdd:cd09639 282 QVIEASLDIS-VDVMITELAP--IDSLIQRLGRLHRYG 316
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
245-308 |
1.78e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 37.92 E-value: 1.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589200340 245 CLIFANTRSEAANVASNMRDAGYGVIELHGDLTPRERTKAMKDLSN---LQKSYVVATDIAARGIDI 308
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEALILLFfgeLKPPILVTVDLLTTGVDI 75
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
245-315 |
1.81e-03 |
|
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: 38.61 E-value: 1.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589200340 245 CLIFANTRSEAANVASNMRDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYV--VATDIAARGIDIEGISHVI 315
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVflLSTKAGGVGLNLTAANRVI 102
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
28-155 |
2.50e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 39.03 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 28 IQQAVIPMACKGKDIIGISATGTGKThafLIPIMEKVDS-SKPCVQAVITAPTRELALQIYQRCEKMSEADPKLVIrlIT 106
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKT---IIAILVAADRlTKKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITS--LT 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1589200340 107 GGIE-KSRmiEQLKVQPHIVVGTPGRIKDLFLNEQVlRVDTADIMVVDEA 155
Cdd:cd18035 80 GEVKpEER--AERWDASKIIVATPQVIENDLLAGRI-TLDDVSLLIFDEA 126
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
272-359 |
3.13e-03 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 38.09 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 272 LHGDLTPRERTKAMKDLSNLQKSYVVATDIAARGIDIEGISHVI-----SMGFPkelDYYIHRsGRTGRAGHEGICYALY 346
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGLA---QLYQLR-GRVGRSKERAYAYFLY 132
|
90
....*....|....*.
gi 1589200340 347 ---EKKDDTAIRQLEV 359
Cdd:cd18810 133 pdqKKLTEDALKRLEA 148
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
231-332 |
3.70e-03 |
|
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: 37.57 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589200340 231 EKVLEILPSFTPYV----CLIFANTRSEAanvasnmrDAGYGVIELHGDLTPRERTKAMKDLSNLQKSYV---------- 296
Cdd:cd18802 10 QKLIEILREYFPKTpdfrGIIFVERRATA--------VVLSRLLKEHPSTLAFIRCGFLIGRGNSSQRKRslmtqrkqke 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1589200340 297 -------------VATDIAARGIDIEGISHVISMGFPKELDYYIHRSGR 332
Cdd:cd18802 82 tldkfrdgelnllIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
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