|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
202-591 |
3.88e-149 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 442.66 E-value: 3.88e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 202 TFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETqvTRVLVLVPT 281
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--PQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 282 RELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNtPSFELSQIEILILDEADRMLD 361
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 362 EYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRIFVNSNTDVAPYLRQEFVRIrpnKEGDREAIVAALL 441
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLV---DKRDKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 442 TRTFQDHVMLFTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVINF 521
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 522 TMPNTVKHYVHRVGRTARAGKVGRSVSLVGETERKMLKEIVKKAKFPVKARVIPQEVILKFRDLIEKLEK 591
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPK 386
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
212-407 |
1.36e-130 |
|
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: 386.23 E-value: 1.36e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQVTRVLVLVPTRELGIQVHTV 291
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 292 ARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTPSFELSQIEILILDEADRMLDEYFEEQMKEI 371
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 49618925 372 IRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRIF 407
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
202-574 |
1.56e-91 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 293.77 E-value: 1.56e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 202 TFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPR-ETQVTRVLVLVP 280
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRrKSGPPRILILTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 281 TRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTpSFELSQIEILILDEADRML 360
Cdd:PRK11192 82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEE-NFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 361 DEYFEEQMKEIIRMCAYQRQTMLFSATM-SEEVKDLASVSLKQPVRIfvnsntDVAPYLR-----QEFVRIRPNKEgDRE 434
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLeGDAVQDFAERLLNDPVEV------EAEPSRRerkkiHQWYYRADDLE-HKT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 435 AIVAALLTrtfQDHV---MLFTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLD 511
Cdd:PRK11192 234 ALLCHLLK---QPEVtrsIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGID 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49618925 512 IEGVKTVINFTMPNTVKHYVHRVGRTARAGKVGRSVSLVGETERKMLKEIVKKAKFPVKARVI 574
Cdd:PRK11192 311 IDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVI 373
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
212-406 |
6.53e-87 |
|
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: 272.78 E-value: 6.53e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRE-TQVTRVLVLVPTRELGIQVHT 290
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKkGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 291 VARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTpSFELSQIEILILDEADRMLDEYFEEQMKE 370
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERG-KLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 49618925 371 IIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
203-554 |
4.05e-85 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 277.45 E-value: 4.05e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 203 FHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQVtrvLVLVPTR 282
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQA---LVLCPTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 283 ELGIQVHTVARQLAQFT-TISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTpSFELSQIEILILDEADRMLD 361
Cdd:PRK11776 83 ELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKG-TLDLDALNTLVLDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 362 EYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRIFVNSnTDVAPYLRQEFVRIRPNkegDREAIVAALL 441
Cdd:PRK11776 162 MGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES-THDLPAIEQRFYEVSPD---ERLPALQRLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 442 tRTFQ-DHVMLFTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVIN 520
Cdd:PRK11776 238 -LHHQpESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVIN 316
|
330 340 350
....*....|....*....|....*....|....
gi 49618925 521 FTMPNTVKHYVHRVGRTARAGKVGRSVSLVGETE 554
Cdd:PRK11776 317 YELARDPEVHVHRIGRTGRAGSKGLALSLVAPEE 350
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
201-575 |
1.27e-84 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 276.30 E-value: 1.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 201 LTFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQ---VTRVLV 277
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrPVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 278 LVPTRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTpSFELSQIEILILDEAD 357
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQN-AVKLDQVEILVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 358 RMLDEYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRIFVNSNTDVAPYLRQ--EFVrirpNKEGDREa 435
Cdd:PRK10590 160 RMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQhvHFV----DKKRKRE- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 436 IVAALLTRTFQDHVMLFTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGV 515
Cdd:PRK10590 235 LLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEEL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 516 KTVINFTMPNTVKHYVHRVGRTARAGKVGRSVSLVGETERKMLKEIVKKAKFPVKARVIP 575
Cdd:PRK10590 315 PHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIP 374
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
200-628 |
3.01e-79 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 265.66 E-value: 3.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 200 NLTFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKP----RETQVTRV 275
Cdd:PRK04537 8 DLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPaladRKPEDPRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 276 LVLVPTRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTPSFELSQIEILILDE 355
Cdd:PRK04537 88 LILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 356 ADRMLDEYFEEQMKEIIRMCAYQ--RQTMLFSATMSEEVKDLASVSLKQPVRIFVNSNTDVAPYLRQefvRIRPNKEGDR 433
Cdd:PRK04537 168 ADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ---RIYFPADEEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 434 EAIVAALLTRTFQDHVMLFTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIE 513
Cdd:PRK04537 245 QTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHID 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 514 GVKTVINFTMPNTVKHYVHRVGRTARAGKVGRSVSLVGETERKMLKEIvkKAKFPVKarvIPQEVILKfrDLIEKLEKDV 593
Cdd:PRK04537 325 GVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDI--EAYIEQK---IPVEPVTA--ELLTPLPRPP 397
|
410 420 430
....*....|....*....|....*....|....*
gi 49618925 594 YAVLCLEKEEKEMAHSEAQISSAQKRLTKSEDEKQ 628
Cdd:PRK04537 398 RVPVEGEEADDEAGDSVGTIFREAREQRAAEEQRR 432
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
203-579 |
1.76e-78 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 260.62 E-value: 1.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 203 FHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKP----RETQVTRVLVL 278
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPppkeRYMGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 279 VPTRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAG-PDVLIATPGRLIDhLHNTPSFELSQIEILILDEAD 357
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLD-FNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 358 RMLDEYFEEQMKEIIRMCAY--QRQTMLFSATMSEEVKDLASVSLKQPVRIFVNSNTDVAPYLRQefvRIRPNKEGDREA 435
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQ---HVYAVAGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 436 IVAALLTRTFQDHVMLFTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGV 515
Cdd:PRK01297 325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49618925 516 KTVINFTMPNTVKHYVHRVGRTARAGKVGRSVSLVGETERKMLKEIVKKAKFPVKARVIPQEVI 579
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAELL 468
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
203-552 |
3.88e-77 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 255.28 E-value: 3.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 203 FHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKP----RETQVTRVLVL 278
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPapedRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 279 VPTRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTpSFELSQIEILILDEADR 358
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQN-HINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 359 MLDEYFEEQMKEIIRMC--AYQRQTMLFSATMSEEVKDLASVSLKQPVRIfvnsntDVAPyLRQEFVRIR-----PNKEg 431
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMppANQRLNMLFSATLSYRVRELAFEHMNNPEYV------EVEP-EQKTGHRIKeelfyPSNE- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 432 DREAIVAALLTRTFQDHVMLFTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLD 511
Cdd:PRK04837 241 EKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLH 320
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 49618925 512 IEGVKTVINFTMPNTVKHYVHRVGRTARAGKVGRSVSLVGE 552
Cdd:PRK04837 321 IPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACE 361
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
202-569 |
3.64e-75 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 253.54 E-value: 3.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 202 TFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKP--RETQVTRVLVLV 279
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPllRYGDGPIVLVLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 280 PTRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTPSfELSQIEILILDEADRM 359
Cdd:PTZ00110 211 PTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVT-NLRRVTYLVLDEADRM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 360 LDEYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLK-QPVRIFVNSNTDVAPY-LRQEFVRIrpnKEGDREAIV 437
Cdd:PTZ00110 290 LDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKeEPVHVNVGSLDLTACHnIKQEVFVV---EEHEKRGKL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 438 AALLTRTFQD--HVMLFTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGV 515
Cdd:PTZ00110 367 KMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDV 446
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 49618925 516 KTVINFTMPNTVKHYVHRVGRTARAGKVGRSVSLVGETERKMLKEIVK---KAKFPV 569
Cdd:PTZ00110 447 KYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKvlrEAKQPV 503
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
202-662 |
1.05e-74 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 254.77 E-value: 1.05e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 202 TFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLiyKPrETQVTRVLVLVPT 281
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DP-ELKAPQILVLAPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 282 RELGIQVhtvARQLAQFTT----ISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLhNTPSFELSQIEILILDEAD 357
Cdd:PRK11634 84 RELAVQV---AEAMTDFSKhmrgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHL-KRGTLDLSKLSGLVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 358 RMLDEYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRIFVNSNTDVAPYLRQEFVRI---RPNkegdrE 434
Cdd:PRK11634 160 EMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVwgmRKN-----E 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 435 AIVAALLTRTFqDHVMLFTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIEG 514
Cdd:PRK11634 235 ALVRFLEAEDF-DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 515 VKTVINFTMPNTVKHYVHRVGRTARAGKVGRSVSLVGETERKMLKEIVKKAKFPVKARVIPQEVILKFRDL--------- 585
Cdd:PRK11634 314 ISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLekfaakvqq 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 586 -IEKLEKDVYAVLcLEKEEKEMAHSEAQISSAQKRLTK-SEDEKQL---------PRTWFQTNEERKKDRMAKALQDFDL 654
Cdd:PRK11634 394 qLESSDLDQYRAL-LAKIQPTAEGEELDLETLAAALLKmAQGERPLilppdapmrPKREFRDRDDRGPRDRNDRGPRGDR 472
|
....*...
gi 49618925 655 ALRGKKKR 662
Cdd:PRK11634 473 EDRPRRER 480
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
202-406 |
5.77e-67 |
|
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: 220.27 E-value: 5.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 202 TFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPretQVTRVLVLVPT 281
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENP---QRFFALVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 282 RELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTPSFELSQIEILILDEADRMLD 361
Cdd:cd17954 78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 49618925 362 EYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17954 158 MDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
202-406 |
3.79e-66 |
|
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: 218.33 E-value: 3.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 202 TFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLiyKPRETQV-TRVLVLVP 280
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--KAHSPTVgARALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 281 TRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTpSFELSQIEILILDEADRML 360
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEM-NLKLSSVEYVVFDEADRLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 49618925 361 DEYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
202-397 |
1.38e-65 |
|
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: 217.35 E-value: 1.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 202 TFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKP-------RETQVTR 274
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGppsvgrgRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 275 VLVLVPTRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLhNTPSFELSQIEILILD 354
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFI-ERGRISLSSIKFLVLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 49618925 355 EADRMLDEYFEEQMKEIIRMC----AYQRQTMLFSATMSEEVKDLAS 397
Cdd:cd17967 160 EADRMLDMGFEPQIRKIVEHPdmppKGERQTLMFSATFPREIQRLAA 206
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
203-404 |
1.55e-63 |
|
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: 210.93 E-value: 1.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 203 FHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERL------IYkpretqvtrVL 276
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLsedpygIF---------AL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 277 VLVPTRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTPSFE--LSQIEILILD 354
Cdd:cd17955 72 VLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTkvLSRVKFLVLD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 49618925 355 EADRMLDEYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPV 404
Cdd:cd17955 152 EADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
201-579 |
1.58e-63 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 221.59 E-value: 1.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 201 LTFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERL----IYKPRETQVTRVL 276
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCctirSGHPSEQRNPLAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 277 VLVPTRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHL--HNtpsFELSQIEILILD 354
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLskHD---IELDNVSVLVLD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 355 EADRMLDEYFEEQMKEIIRMCAyQRQTMLFSATMSEEVKDLASVSLKQPVRIFVNSNTDVAPYLRQEFVRIRPNKEgdRE 434
Cdd:PLN00206 278 EVDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQK--KQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 435 AIVAALLTRT-FQDHVMLFTQTKKQAHrmhiLLG-----LMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAAR 508
Cdd:PLN00206 355 KLFDILKSKQhFKPPAVVFVSSRLGAD----LLAnaitvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGR 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49618925 509 GLDIEGVKTVINFTMPNTVKHYVHRVGRTARAGKVGRSVSLVGETERKMLKEIVKKAKfpVKARVIPQEVI 579
Cdd:PLN00206 431 GVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLK--SSGAAIPRELA 499
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
213-409 |
4.69e-61 |
|
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: 204.06 E-value: 4.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 213 LKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLiYKPRETQVTRV--LVLVPTRELGIQVHT 290
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL-YRERWTPEDGLgaLIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 291 VARQLAQFTTISTCLAVGGLDLKsQEAALRAGPDVLIATPGRLIDHLHNTPSFELSQIEILILDEADRMLDEYFEEQMKE 370
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVK-EEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 49618925 371 IIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRIFVN 409
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
208-406 |
9.60e-59 |
|
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: 198.58 E-value: 9.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 208 LSRPLlkaISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIykPRETQVTR-----VLVLVPTR 282
Cdd:cd17949 1 LVSHL---KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLL--SLEPRVDRsdgtlALVLVPTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 283 ELGIQVHTVARQLAQ-FTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTPSFELSQIEILILDEADRMLD 361
Cdd:cd17949 76 ELALQIYEVLEKLLKpFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 49618925 362 EYFEEQMKEIIRM-------------CAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17949 156 MGFEKDITKILELlddkrskaggeksKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
213-409 |
6.63e-58 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 195.66 E-value: 6.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 213 LKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLE---RLIYKPRETqvTRVLVLVPTRELGIQVH 289
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyKLKFKPRNG--TGVIIISPTRELALQIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 290 TVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTPSFELSQIEILILDEADRMLDEYFEEQMK 369
Cdd:cd17942 80 GVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 49618925 370 EIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPvRIFVN 409
Cdd:cd17942 160 QIIKLLPKRRQTMLFSATQTRKVEDLARISLKKK-PLYVG 198
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
212-406 |
4.73e-57 |
|
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: 194.08 E-value: 4.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQVTR-----VLVLVPTRELGI 286
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKddgpyALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 287 QVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTpSFELSQIEILILDEADRMLDEYFEE 366
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERR-LLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 367 QMK----------------EIIRMCAYQ----RQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17945 160 QVTkildampvsnkkpdteEAEKLAASGkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
225-395 |
8.64e-57 |
|
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: 191.30 E-value: 8.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 225 TPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQVtrvLVLVPTRELGIQVHTVARQLAQFTTISTC 304
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQA---LVLAPTRELAEQIYEELKKLGKGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 305 LAVGGLDLKSQEAALRaGPDVLIATPGRLIDHLHNTPsfELSQIEILILDEADRMLDEYFEEQMKEIIRMCAYQRQTMLF 384
Cdd:pfam00270 78 SLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
|
170
....*....|.
gi 49618925 385 SATMSEEVKDL 395
Cdd:pfam00270 155 SATLPRNLEDL 165
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
201-402 |
2.18e-55 |
|
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: 191.33 E-value: 2.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 201 LTFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIY------KPRETQVTR 274
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKegltasSFSEVQEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 275 VLVLVPTRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLhNTPSFELSQIEILILD 354
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFI-GRGKISLSKLKYLILD 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 49618925 355 EADRMLDEYFEEQMKEIIRMC----AYQRQTMLFSATMSEEVKDLASVSLKQ 402
Cdd:cd18052 202 EADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKE 253
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
212-408 |
2.27e-55 |
|
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: 188.57 E-value: 2.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIyKPRETQVTRVLVLVPTRELGIQVHTV 291
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLG-KPRKKKGLRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 292 ARQLAQFTTISTCLAvggldLKSQEAALRAGP------DVLIATPGRLIDHLHNTPSfELSQIEILILDEADRMLDEYFE 365
Cdd:cd17957 80 LLKLSKGTGLRIVLL-----SKSLEAKAKDGPksitkyDILVSTPLRLVFLLKQGPI-DLSSVEYLVLDEADKLFEPGFR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 49618925 366 EQMKEIIRMCAYQR-QTMLFSATMSEEVKDLASVSLKQPVRIFV 408
Cdd:cd17957 154 EQTDEILAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
208-402 |
8.71e-55 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 187.79 E-value: 8.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 208 LSRPLLKAISTMGFKQPTPIQKACVPVGL-LGKDICACAATGTGKTAAFMLPVLERLIYKPRETQVTRV--LVLVPTREL 284
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVsaLIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 285 GIQVHTVARQLAQFTT-ISTCLAVGGLDLKSQEAAL-RAGPDVLIATPGRLIDHLHNTPSFE-LSQIEILILDEADRMLD 361
Cdd:cd17964 81 ALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVAKaFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 49618925 362 EYFEEQMKEIIR----MCAYQRQTMLFSATMSEEVKDLASVSLKQ 402
Cdd:cd17964 161 MGFRPDLEQILRhlpeKNADPRQTLLFSATVPDEVQQIARLTLKK 205
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
195-561 |
1.17e-54 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 193.89 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 195 SQYDENL-TFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQVt 273
Cdd:PTZ00424 21 SNYDEIVdSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 274 rvLVLVPTRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLhNTPSFELSQIEILIL 353
Cdd:PTZ00424 100 --LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI-DKRHLRVDDLKLFIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 354 DEADRMLDEYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRIFVNSNTDVAPYLRQEFVRIrpNKEGDR 433
Cdd:PTZ00424 177 DEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAV--EKEEWK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 434 EAIVAALLTRTFQDHVMLFTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIE 513
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 49618925 514 GVKTVINFTMPNTVKHYVHRVGRTARAGKVGRSVSLVGETERKMLKEI 561
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
212-406 |
3.48e-54 |
|
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: 185.47 E-value: 3.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQVTRV--LVLVPTRELGIQVH 289
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVgaLIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 290 TVARQLA--QFTTISTCLAVGGLDLKSQEAALRA-GPDVLIATPGRLIDHL-HNTPSFELSQIEILILDEADRMLDEYFE 365
Cdd:cd17960 81 EVLQSFLehHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLsRKADKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 49618925 366 EQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
208-404 |
1.19e-53 |
|
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: 184.32 E-value: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 208 LSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIY---KPRETQVTRVLVLVPTREL 284
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKakaESGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 285 GIQVHTVARQLAQFTT--IStCLAVGG-LDLKSQEAALRAGPDVLIATPGRLIDHLHNTPSFELSQIEILILDEADRMLD 361
Cdd:cd17961 81 AQQVSKVLEQLTAYCRkdVR-VVNLSAsSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 49618925 362 EYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPV 404
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
212-408 |
6.70e-50 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 174.74 E-value: 6.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVP---------VGLLGKDICACAATGTGKTAAFMLPVLERLiyKPRETQVTRVLVLVPTR 282
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPwllpsskstPPYRPGDLCVSAPTGSGKTLAYVLPIVQAL--SKRVVPRLRALIVVPTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 283 ELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAG--------PDVLIATPGRLIDHLHNTPSFELSQIEILILD 354
Cdd:cd17956 79 ELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGFTLKHLRFLVID 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49618925 355 EADRMLDEYFEE----------QMKEIIRMCAYQR----------QTMLFSATMSEEVKDLASVSLKQPvRIFV 408
Cdd:cd17956 159 EADRLLNQSFQDwletvmkalgRPTAPDLGSFGDAnllersvrplQKLLFSATLTRDPEKLSSLKLHRP-RLFT 231
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
203-406 |
1.30e-49 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 172.87 E-value: 1.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 203 FHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQvtrVLVLVPTR 282
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQ---ALILVPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 283 ELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDhLHNTPSFELSQIEILILDEADRMLDE 362
Cdd:cd17940 78 ELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 49618925 363 YFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
205-407 |
6.17e-49 |
|
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: 170.97 E-value: 6.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 205 DMNLSRPLLKAISTMGFKQPTPI-QKACVPVgLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQVtrvLVLVPTRE 283
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIqQRAIVPI-IKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQA---LVLAPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 284 LGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTpSFELSQIEILILDEADRMLDEY 363
Cdd:cd17939 77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRR-SLRTDKIKMFVLDEADEMLSRG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 49618925 364 FEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRIF 407
Cdd:cd17939 156 FKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
212-406 |
6.53e-49 |
|
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: 171.01 E-value: 6.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKP--RETQVTRVLVLVPTRELGIQVH 289
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPplERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 290 TVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDhLHNTPSFELSQIEILILDEADRMLDEYFEEQMK 369
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLID-FLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 49618925 370 EIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
418-550 |
1.09e-48 |
|
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: 167.68 E-value: 1.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 418 LRQEFVRIRPNKEgdREAIVAALLTRTFQDHVMLFTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQI 497
Cdd:cd18787 1 IKQLYVVVEEEEK--KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 49618925 498 DILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGRTARAGKVGRSVSLV 550
Cdd:cd18787 79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
212-406 |
1.83e-47 |
|
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350710 [Multi-domain] Cd Length: 197 Bit Score: 166.82 E-value: 1.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLI----YKPRETQVtrVLVLVPTRELGIQ 287
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMdqreLEKGEGPI--AVIVAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 288 VHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLhNTPSFELSQIEILILDEADRMLDEYFEEQ 367
Cdd:cd17952 79 IYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMV-KKKATNLQRVTYLVLDEADRMFDMGFEYQ 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 49618925 368 MKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17952 158 VRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
216-406 |
2.27e-46 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 164.20 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 216 ISTMGFKQPTPIQKACVPVGLLG-KDICACAATGTGKTAAFMLPVLERLiykpRETQVTRVLVLVPTRELGIQVHTVARQ 294
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL----KRGKGGRVLVLVPTRELAEQWAEELKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 295 LAQFTTISTCLAVGGLDLKSQEAALRAG-PDVLIATPGRLIDHLHNTPsFELSQIEILILDEADRMLDEYFEEQMKEIIR 373
Cdd:smart00487 77 LGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDK-LSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
|
170 180 190
....*....|....*....|....*....|...
gi 49618925 374 MCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI 188
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
212-406 |
4.07e-46 |
|
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: 163.10 E-value: 4.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQvtrVLVLVPTRELGIQVHTV 291
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPS---ALILTPTRELAVQIEDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 292 ARQLAQ-FTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLhNTPSFELSQIEILILDEADRMLDEYFEEQMKE 370
Cdd:cd17962 78 AKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL-KQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 49618925 371 IIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17962 157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
202-396 |
1.19e-45 |
|
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350809 [Multi-domain] Cd Length: 249 Bit Score: 163.67 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 202 TFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLI-------------YKPR 268
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYeqgpgeslpsesgYYGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 269 ETQVTRVLVLVPTRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTpSFELSQI 348
Cdd:cd18051 102 RKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERG-KIGLDYC 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 49618925 349 EILILDEADRMLDEYFEEQMKEIIRMCAY----QRQTMLFSATMSEEVKDLA 396
Cdd:cd18051 181 KYLVLDEADRMLDMGFEPQIRRIVEQDTMpptgERQTLMFSATFPKEIQMLA 232
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
212-406 |
2.12e-45 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350709 [Multi-domain] Cd Length: 206 Bit Score: 161.35 E-value: 2.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVL-------ERLIYKPRETQVTrvLVLVPTREL 284
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqeKKLPFIKGEGPYG--LIVCPSREL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 285 GIQVHTVARQLAQ------FTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLhNTPSFELSQIEILILDEADR 358
Cdd:cd17951 79 ARQTHEVIEYYCKalqeggYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEADR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 49618925 359 MLDEYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17951 158 MIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
212-390 |
8.87e-44 |
|
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: 158.17 E-value: 8.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLL-GKDICACAATGTGKTAAFMLPVLERLIYKPRETQVT------RVLVLVPTREL 284
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGgkqkplRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 285 GIQV--HTVArqLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTPSF--ELSQIEILILDEADRML 360
Cdd:cd17946 81 AVQVkdHLKA--IAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDEADRML 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 49618925 361 DE-YFEEqMKEIIRM-------CAYQRQTMLFSATMSE 390
Cdd:cd17946 159 EKgHFAE-LEKILELlnkdragKKRKRQTFVFSATLTL 195
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
203-406 |
2.48e-42 |
|
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: 152.60 E-value: 2.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 203 FHDMNLSRPLLKAISTMGFKQPTPIQK-ACVPVgLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQvtrVLVLVPT 281
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQrAIMPC-IKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQ---ALVLAPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 282 RELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLhNTPSFELSQIEILILDEADRMLD 361
Cdd:cd18046 77 RELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 49618925 362 EYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
212-407 |
2.78e-42 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 152.62 E-value: 2.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKP--RETQVT-RVLVLVPTRELGIQV 288
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPipREQRNGpGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 289 HTVARQLAQFTTISTCLaVGGLDLKSQEAALRAGPDVLIATPGRLIDhLHNTPSFELSQIEILILDEADRMLDEYFEEQM 368
Cdd:cd17958 81 EAECSKYSYKGLKSVCV-YGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 49618925 369 KEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRIF 407
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
201-406 |
4.81e-42 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 152.53 E-value: 4.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 201 LTFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLP----VLERLIYKPRETQVTrvL 276
Cdd:cd17953 12 QKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPmfrhIKDQRPVKPGEGPIG--L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 277 VLVPTRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHL--HNTPSFELSQIEILILD 354
Cdd:cd17953 90 IMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVTNLRRVTYVVLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 49618925 355 EADRMLDEYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17953 170 EADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
212-406 |
2.73e-41 |
|
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: 149.34 E-value: 2.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIykpRETQVTRVLVLVPTRELGIQVHTV 291
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD---LERRHPQVLILAPTREIAVQIHDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 292 ARQLAQFTT-ISTCLAVGGLDLKSQEAALRaGPDVLIATPGRlIDHLHNTPSFELSQIEILILDEADRMLDEYFEEQMKE 370
Cdd:cd17943 78 FKKIGKKLEgLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGR-IKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 49618925 371 IIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17943 156 IFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
208-406 |
9.83e-40 |
|
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: 145.03 E-value: 9.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 208 LSRPLLKAISTMGFKQPTPIQKACVPVgLLG---KDICACAATGTGKTAAFMLPVLERLIYKPRETQVtrvLVLVPTREL 284
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPL-ILSdppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQA---LCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 285 GIQVHTVARQLAQFTTISTCLAVGGLDLKSQEaalRAGPDVLIATPGRLIDHLhNTPSFELSQIEILILDEADRMLD-EY 363
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVALAVPGNDVPRGK---KITAQIVIGTPGTVLDWL-KKRQLDLKKIKILVLDEADVMLDtQG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 49618925 364 FEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd17963 153 HGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
201-410 |
1.40e-39 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 146.31 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 201 LTFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKP--RETQVTRVLVL 278
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflERGDGPICLVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 279 VPTRELGIQVHTVARQLAQFTTI-STCLaVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTPSfELSQIEILILDEAD 357
Cdd:cd18049 104 APTRELAQQVQQVAAEYGRACRLkSTCI-YGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEAD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 49618925 358 RMLDEYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRIFVNS 410
Cdd:cd18049 182 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
203-408 |
2.09e-38 |
|
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: 141.71 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 203 FHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLiyKPRETQVTrVLVLVPTR 282
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL--EPVDGQVS-VLVICHTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 283 ELGIQVHTVARQLAQF-TTISTCLAVGGLDLKSQEAALR-AGPDVLIATPGRLIDhLHNTPSFELSQIEILILDEADRML 360
Cdd:cd17950 81 ELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILA-LVREKKLKLSHVKHFVLDECDKML 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 49618925 361 DEY-FEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRIFV 408
Cdd:cd17950 160 EQLdMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
203-396 |
5.65e-38 |
|
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: 140.53 E-value: 5.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 203 FHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLerliykpretQVTRVLVLVPTR 282
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL----------QIVVALILEPSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 283 ELGIQVHTVARQLAQFT---TISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDhLHNTPSFELSQIEILILDEADRM 359
Cdd:cd17938 71 ELAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLED-LIKTGKLDLSSVRFFVLDEADRL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 49618925 360 LDEYFEEQMKEI------IRMCAYQRQTMLFSATM-SEEVKDLA 396
Cdd:cd17938 150 LSQGNLETINRIynripkITSDGKRLQVIVCSATLhSFEVKKLA 193
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
203-406 |
3.65e-35 |
|
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: 134.75 E-value: 3.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 203 FHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKP--RETQVTRVLVLVP 280
Cdd:cd18050 64 FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPylERGDGPICLVLAP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 281 TRELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTPSfELSQIEILILDEADRML 360
Cdd:cd18050 144 TRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRML 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 49618925 361 DEYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd18050 223 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
203-406 |
5.75e-35 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350803 [Multi-domain] Cd Length: 201 Bit Score: 131.82 E-value: 5.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 203 FHDMNLSRPLLKAISTMGFKQPTPIQK-ACVPVgLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQvtrVLVLVPT 281
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQrAIKPI-IKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQ---ALILSPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 282 RELGIQVHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTpSFELSQIEILILDEADRMLD 361
Cdd:cd18045 77 RELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRR-SLRTRHIKMLVLDEADEMLN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 49618925 362 EYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQPVRI 406
Cdd:cd18045 156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
212-397 |
3.99e-31 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 121.70 E-value: 3.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 212 LLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKP----RETQVTRVLVLVPTRELGIQ 287
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKllaeGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 288 VHTVARQLAQFTTISTCLAVGGLDLKSQEAALRAGPDVLIATPGrLIDHLHNTPSFELSQIEILILDEADRMLDEYFEEQ 367
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPG-ALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 49618925 368 MKEIIRMCAYQR-------------QTMLFSATMSEEVKDLAS 397
Cdd:cd17948 160 LSHFLRRFPLASrrsentdgldpgtQLVLVSATMPSGVGEVLS 202
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
432-541 |
2.98e-30 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 115.00 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 432 DREAIVAALLTRTFQDHVMLFTQTKKQAHrMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLD 511
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 49618925 512 IEGVKTVINFTMPNTVKHYVHRVGRTARAG 541
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
226-401 |
5.20e-29 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 114.94 E-value: 5.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 226 PIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERL---IYKPRETQVTRVLVLVPTRELGIQVHTvarqlaQFTTIS 302
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLqedQQPRKRGRAPKVLVLAPTRELANQVTK------DFKDIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 303 TCLAV----GGLDLKSQEAALRAGPDVLIATPGRLIDHLHNTpSFELSQIEILILDEADRMLDEYFEEQMKEIIRMcAYQ 378
Cdd:cd17944 89 RKLSVacfyGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNG-RLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSV-SYK 166
|
170 180
....*....|....*....|....*....
gi 49618925 379 R------QTMLFSATMSEEVKDLASVSLK 401
Cdd:cd17944 167 KdsednpQTLLFSATCPDWVYNVAKKYMK 195
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
461-541 |
8.17e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 98.44 E-value: 8.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 461 RMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGRTARA 540
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
|
.
gi 49618925 541 G 541
Cdd:smart00490 82 G 82
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
202-403 |
5.82e-22 |
|
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: 95.47 E-value: 5.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 202 TFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLG--KDICACAATGTGKTAAFMLPVLERLIYKPRETQvtrVLVLV 279
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQ---CLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 280 PTRELGIQVHTVARQLAQFTT-ISTCLAV------GGLDLKSQeaalragpdVLIATPGRLIDHLHNTPSFELSQIEILI 352
Cdd:cd18048 96 PTFELALQTGKVVEEMGKFCVgIQVIYAIrgnrpgKGTDIEAQ---------IVIGTPGTVLDWCFKLRLIDVTNISVFV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 49618925 353 LDEADRMLD-EYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQP 403
Cdd:cd18048 167 LDEADVMINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
238-704 |
1.44e-21 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 99.33 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 238 GKDICACAATGTGKTAAFMLpVLERLIYKPRetqvtrVLVLVPTRELGIQVhtvARQLAQFTTIstclAVGGLDLKSQEA 317
Cdd:COG1061 100 GGRGLVVAPTGTGKTVLALA-LAAELLRGKR------VLVLVPRRELLEQW---AEELRRFLGD----PLAGGGKKDSDA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 318 alragpDVLIATPGRLI--DHLHNTPSFelsqIEILILDEADRMLDEYFEEqmkeIIRMCAYQRqTMLFSAT------MS 389
Cdd:COG1061 166 ------PITVATYQSLArrAHLDELGDR----FGLVIIDEAHHAGAPSYRR----ILEAFPAAY-RLGLTATpfrsdgRE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 390 EEVKDLA----SVSLKQ--------PVRIFV------NSNTDVAPYLRQEFVRIRPNKEGDREAIVAALLTRTFQDHVML 451
Cdd:COG1061 231 ILLFLFDgivyEYSLKEaiedgylaPPEYYGirvdltDERAEYDALSERLREALAADAERKDKILRELLREHPDDRKTLV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 452 FTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYV 531
Cdd:COG1061 311 FCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFI 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 532 HRVGRTARAGKVGRSVS---LVGEtERKMLKEIVKKAKFPVKARVIPQEVILKFRDLIEKLEKDVYAVLCLEKEEKEMAH 608
Cdd:COG1061 391 QRLGRGLRPAPGKEDALvydFVGN-DVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEEL 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 609 SEAQISSAQKRLTKSEDEKQLPRTWFQTNEERKKDRMAKALQDFDLALRGKKKRAQFLKQGKRKELTAEERAQLEVLKSQ 688
Cdd:COG1061 470 ELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLE 549
|
490
....*....|....*.
gi 49618925 689 MFAERAAKRERKQKRA 704
Cdd:COG1061 550 ELAALLLKELLRAALA 565
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
202-403 |
3.35e-20 |
|
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: 89.39 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 202 TFHDMNLSRPLLKAISTMGFKQPTPIQKACVPVGLLG--KDICACAATGTGKTAAFMLPVLERLIYKPRETQvtrVLVLV 279
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ---CLCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 280 PTRELGIQVHTVARQLAQF-TTISTCLAVGGldlKSQEAALRAGPDVLIATPGRLIDHLHNTPSFELSQIEILILDEADR 358
Cdd:cd18047 79 PTYELALQTGKVIEQMGKFyPELKLAYAVRG---NKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 49618925 359 ML-DEYFEEQMKEIIRMCAYQRQTMLFSATMSEEVKDLASVSLKQP 403
Cdd:cd18047 156 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
218-391 |
3.09e-16 |
|
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: 78.96 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 218 TMGFKQPTPIQKACVPVgLLGK----------------DICACAA-TGTGKTAAFMLPVLERLI---YKPRE-------- 269
Cdd:cd17965 25 TDEEIKPSPIQTLAIKK-LLKTlmrkvtkqtsneepklEVFLLAAeTGSGKTLAYLAPLLDYLKrqeQEPFEeaeeeyes 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 270 ---TQVTRVLVLVPTRELGIQVHTVARQLAQFTTIST---CLAVGGLDLKSQEaALRAGPDVLIATPGrLIDHLHNTPSF 343
Cdd:cd17965 104 akdTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIktfSSGFGPSYQRLQL-AFKGRIDILVTTPG-KLASLAKSRPK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 49618925 344 ELSQIEILILDEADRMLDEYFEEQMKEIIRMCAYQRQTMLFSATMSEE 391
Cdd:cd17965 182 ILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKE 229
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
238-387 |
4.38e-16 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 75.90 E-value: 4.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 238 GKDICACAATGTGKTAAFMLPVLERLiykprETQVTRVLVLVPTRELGIQVHTVARQLAQfTTISTCLAVGGLDLKSQEA 317
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLL-----LKKGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREK 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49618925 318 ALRAGPDVLIATPGRLIDHLHNTPSFELSQIEILILDEADRMLDEYFEEQMkEIIRMCAYQR---QTMLFSAT 387
Cdd:cd00046 75 NKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALI-LDLAVRKAGLknaQVILLSAT 146
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
207-542 |
2.90e-14 |
|
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: 76.80 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 207 NLSRPLLKAISTMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRetqvTRVLVLVPTRELgi 286
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPG----ATALYLYPTKAL-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 287 qvhtvAR-QLAqftTISTCLAVGGLDLK--------SQEA--ALRAGPDVLIATPgrliDHLH-----NTPSFE--LSQI 348
Cdd:COG1205 114 -----ARdQLR---RLRELAEALGLGVRvatydgdtPPEErrWIREHPDIVLTNP----DMLHygllpHHTRWArfFRNL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 349 EILILDEA---------------DRMLdeyfeeqmkeiiRMCAYQRQTMLF---SATMS--------------EEVKDla 396
Cdd:COG1205 182 RYVVIDEAhtyrgvfgshvanvlRRLR------------RICRHYGSDPQFilaSATIGnpaehaerltgrpvTVVDE-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 397 SVSLKQPVRI-FVNsntdvaPYLRQEFVRIRPNKEGDReaIVAALLTRTFQdhVMLFTQTKKQAHRMHILL------GLM 469
Cdd:COG1205 248 DGSPRGERTFvLWN------PPLVDDGIRRSALAEAAR--LLADLVREGLR--TLVFTRSRRGAELLARYArralrePDL 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49618925 470 GLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGRTARAGK 542
Cdd:COG1205 318 ADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQ 390
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
449-550 |
7.40e-10 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 62.44 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 449 VMLFTQTKKQAHRMHILLGLMGLKVGELHGN--------LSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVIN 520
Cdd:COG1111 356 IIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIF 435
|
90 100 110
....*....|....*....|....*....|.
gi 49618925 521 F-TMPNTVKhYVHRVGRTARAGKvGRSVSLV 550
Cdd:COG1111 436 YePVPSEIR-SIQRKGRTGRKRE-GRVVVLI 464
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
238-356 |
1.55e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 57.98 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 238 GKDICACAATGTGKTAAFMLPVLERLIYKPRetqvTRVLVLVPTRELGI-QVHTVARQLAQFTTISTCLAVGG-LDLKSQ 315
Cdd:cd17923 15 GRSVVVTTGTASGKSLCYQLPILEALLRDPG----SRALYLYPTKALAQdQLRSLRELLEQLGLGIRVATYDGdTPREER 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 49618925 316 EAALRAGPDVLIATPGRL---IDHLHNTPSFELSQIEILILDEA 356
Cdd:cd17923 91 RAIIRNPPRILLTNPDMLhyaLLPHHDRWARFLRNLRYVVLDEA 134
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
495-544 |
4.07e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 53.86 E-value: 4.07e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 49618925 495 EQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGRTARAGKVG 544
Cdd:cd18785 21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
222-363 |
8.28e-09 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 56.29 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 222 KQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLpVLERLIYKPRETQVTRVLVLVPTrelgiqVHTVARQLAQFTTI 301
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVL-ICEHHLKKFPAGRKGKVVFLANK------VPLVEQQKEVFRKH 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49618925 302 STCLA--VGGL--DLKSQEAALR--AGPDVLIATPGRLIDHLHNTPSFELSQIEILILDEADRMLDEY 363
Cdd:cd17927 74 FERPGykVTGLsgDTSENVSVEQivESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHNTTKNH 141
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
480-540 |
1.98e-08 |
|
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: 53.75 E-value: 1.98e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49618925 480 LSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGRtARA 540
Cdd:cd18802 74 MTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
244-387 |
5.42e-08 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 52.69 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 244 CAATGTGKTAaFMLpvleRLIykpRETQVTRVLVLVPTRELgiqVHTVARQLAQFTTISTCLAVGGLDLKSQEAAlragp 323
Cdd:cd17926 24 VLPTGSGKTL-TAL----ALI---AYLKELRTLIVVPTDAL---LDQWKERFEDFLGDSSIGLIGGGKKKDFDDA----- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49618925 324 DVLIATPgRLIDHLHNTPSFELSQIEILILDEADRMLDEYFEEQMKEIIRMCayqrqTMLFSAT 387
Cdd:cd17926 88 NVVVATY-QSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSEILKELNAKY-----RLGLTAT 145
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
316-552 |
6.04e-08 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 55.92 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 316 EAALRAG-PDVLIATPGRLidhlhNTPSF--ELSQIEI--LILDEA--------D-RmlDEYfeEQMKEIIRMCAyQRQT 381
Cdd:COG0514 100 LRALRAGeLKLLYVAPERL-----LNPRFleLLRRLKIslFAIDEAhcisqwghDfR--PDY--RRLGELRERLP-NVPV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 382 MLFSATMSEEVKD--LASVSLKQPvRIFVNSntdvapylrqeFVR------IRPNKEGDREAIVAALLTRTFQDHVMLFT 453
Cdd:COG0514 170 LALTATATPRVRAdiAEQLGLEDP-RVFVGS-----------FDRpnlrleVVPKPPDDKLAQLLDFLKEHPGGSGIVYC 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 454 QTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATdVA-ARGLDIEGVKTVINFTMPNTVKHYVH 532
Cdd:COG0514 238 LSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQ 316
|
250 260
....*....|....*....|
gi 49618925 533 RVGRTARAGKVGRSVSLVGE 552
Cdd:COG0514 317 EIGRAGRDGLPAEALLLYGP 336
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
225-356 |
2.74e-07 |
|
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: 51.49 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 225 TPIQKACVPVGLL-GKDICACAATGTGKTAAFMLPVLERLIykpreTQVTRVLVLVPTRELGIQVHTVARQLAQFTTIST 303
Cdd:cd17921 3 NPIQREALRALYLsGDSVLVSAPTSSGKTLIAELAILRALA-----TSGGKAVYIAPTRALVNQKEADLRERFGPLGKNV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 49618925 304 CLAVGGLDLKSQEAAlraGPDVLIATPGRLIDHLHNTPSFELSQIEILILDEA 356
Cdd:cd17921 78 GLLTGDPSVNKLLLA---EADILVATPEKLDLLLRNGGERLIQDVRLVVVDEA 127
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
452-542 |
2.89e-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: 50.28 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 452 FTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYV 531
Cdd:cd18794 36 YCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYY 115
|
90
....*....|.
gi 49618925 532 HRVGRTARAGK 542
Cdd:cd18794 116 QESGRAGRDGL 126
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
239-356 |
4.52e-07 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 51.11 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 239 KDICACAATGTGKT-AAFMLpvLERLIYKPRETQV--TRVLVLVPTRELgiqvhtvARQLAQFTTISTCLAVG------G 309
Cdd:cd18034 17 RNTIVVLPTGSGKTlIAVML--IKEMGELNRKEKNpkKRAVFLVPTVPL-------VAQQAEAIRSHTDLKVGeysgemG 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 49618925 310 LDLKSQEAALR--AGPDVLIATPGRLIDHLHNtpSF-ELSQIEILILDEA 356
Cdd:cd18034 88 VDKWTKERWKEelEKYDVLVMTAQILLDALRH--GFlSLSDINLLIFDEC 135
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
480-627 |
7.02e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 52.95 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 480 LSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVINFT-MPNTVKhYVHRVGRTARaGKVGRSVSLVGE------ 552
Cdd:PRK13766 407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIR-SIQRKGRTGR-QEEGRVVVLIAKgtrdea 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 553 -------TERKMlKEIVKKAKFPVKARVIPQEVILKFRDLIEKLEKDVYAVlclEKEEKEMAHSEAQISSAQKRLTKSED 625
Cdd:PRK13766 485 yywssrrKEKKM-KEELKNLKGILNKKLQELDEEQKGEEEEKDEQLSLDDF---VKSKGKEEEEEEEKEEKDKETEEDEP 560
|
..
gi 49618925 626 EK 627
Cdd:PRK13766 561 EG 562
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
451-542 |
9.65e-07 |
|
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: 49.18 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 451 LFTQTKKQAHRMHILLG------LMGLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMP 524
Cdd:cd18796 43 VFTNTRSQAERLAQRLRelcpdrVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
|
90
....*....|....*...
gi 49618925 525 NTVKHYVHRVGRTARAGK 542
Cdd:cd18796 123 KSVARLLQRLGRSGHRPG 140
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
449-524 |
2.42e-06 |
|
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: 47.47 E-value: 2.42e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49618925 449 VMLFTQTKKQAHRMHILLGLMGLKVGELHGNLSQTQRLESLRRFKDEQ--IDILVATDVAARGLDIEGVKTVINFTMP 524
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPW 107
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
221-536 |
2.60e-06 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 51.26 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 221 FKQPTPIQKACVPVGLLGKDICACAATGTGKT-AAFmLPVLERLIYKPRETQV---TRVLVLVPTRELGIQVHtvaRQLA 296
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELpdgLRVLYISPLKALANDIE---RNLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 297 QFTT-IStclAVGGLDLKSQEAALRAG--------------PDVLIATPgrliDHLH---NTPSFE--LSQIEILILDE- 355
Cdd:COG1201 98 APLEeIG---EAAGLPLPEIRVGVRTGdtpaserqrqrrrpPHILITTP----ESLAlllTSPDARelLRGVRTVIVDEi 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 356 ---AD--R----MLD-EYFEeqmkeiiRMCAYQRQTMLFSATMS--EEVKD-LASVSLKQPVRIfVNSNTDVAPYLR--- 419
Cdd:COG1201 171 halAGskRgvhlALSlERLR-------ALAPRPLQRIGLSATVGplEEVARfLVGYEDPRPVTI-VDAGAGKKPDLEvlv 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 420 --QEFVRIRPNKEGDREAIVAALLTRTfQDH--VMLFTQTKKQAHRMHILLGLMGLKVGEL----HGNLSQTQRLESLRR 491
Cdd:COG1201 243 pvEDLIERFPWAGHLWPHLYPRVLDLI-EAHrtTLVFTNTRSQAERLFQRLNELNPEDALPiaahHGSLSREQRLEVEEA 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 49618925 492 FKDEQIDILVAT---DVaarGLDIEGVKTVINFTMPNTVKHYVHRVGR 536
Cdd:COG1201 322 LKAGELRAVVATsslEL---GIDIGDVDLVIQVGSPKSVARLLQRIGR 366
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
224-355 |
3.25e-06 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 48.63 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 224 PTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQVTRVLVLVPtrelgiQVHTVARQLAQF----- 298
Cdd:cd18036 3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVN------KVPLVEQQLEKFfkyfr 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49618925 299 -----TTIStclavGGLDLKSQEAALRAGPDVLIATPGRLIDHLHN---TPSFELSQIEILILDE 355
Cdd:cd18036 77 kgykvTGLS-----GDSSHKVSFGQIVKASDVIICTPQILINNLLSgreEERVYLSDFSLLIFDE 136
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
480-543 |
8.37e-06 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 46.19 E-value: 8.37e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49618925 480 LSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGRTAR--AGKV 543
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRkrQGRV 139
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
245-355 |
3.11e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 47.61 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 245 AATGTGKTAAFMLPVLERLIYK-------PRETQVTRVLVLVPTRELG--------IQVHTVARQLAQFTTISTCLAVG- 308
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFREggedtreAHKRKTSRILYISPIKALGtdvqrnlqIPLKGIADERRRRGETEVNLRVGi 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 49618925 309 -GLDLKSQEAA--LRAGPDVLIATPGRLIDHLHNTPSFELSQIEILILDE 355
Cdd:PRK09751 83 rTGDTPAQERSklTRNPPDILITTPESLYLMLTSRARETLRGVETVIIDE 132
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
245-361 |
1.70e-04 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to 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: 438711 [Multi-domain] Cd Length: 174 Bit Score: 43.09 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 245 AATGTGKTAAFMLPVLERLIYKPRetqvtRVLVLVPTRelgIQVHTVARQLAQfttiSTCLAVGGLDLKSQEAALRAGPD 324
Cdd:cd17990 24 APPGAGKTTRVPLALLAELWIAGG-----KIIVLEPRR---VAARAAARRLAT----LLGEAPGETVGYRVRGESRVGRR 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 49618925 325 --VLIATPGRLIDHLHNTPsfELSQIEILILDEA-DRMLD 361
Cdd:cd17990 92 trVEVVTEGVLLRRLQRDP--ELSGVGAVILDEFhERSLD 129
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
404-542 |
2.25e-04 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 42.24 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 404 VRIFVN-SNTDVAPYLRQEFVRIR-------PNKEgdreAIVAALLTRTFQ-DHVMLFTQTKKQAHRMHILLGLMGLkvg 474
Cdd:cd18789 2 AEIRCPmTPEFYREYLGLGAHRKRrllaamnPNKL----RALEELLKRHEQgDKIIVFTDNVEALYRYAKRLLKPFI--- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 475 elHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDI--EGVKTVINFTMPNTvKHYVHRVGRTARAGK 542
Cdd:cd18789 75 --TGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLpeANVAIQISGHGGSR-RQEAQRLGRILRPKK 141
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
217-410 |
4.39e-04 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 42.14 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 217 STMGFKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLP--VLERLiykpretqvtrVLVLVPTRELGI-QVHTVAR 293
Cdd:cd17920 6 EVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV-----------TLVVSPLISLMQdQVDRLQQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 294 QLAQFTTIStclavGGLDLKSQEAALRA----GPDVLIATPGRLidhlhNTPSF--------ELSQIEILILDEA----- 356
Cdd:cd17920 75 LGIRAAALN-----STLSPEEKREVLLRikngQYKLLYVTPERL-----LSPDFlellqrlpERKRLALIVVDEAhcvsq 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 357 ---DrmldeyFEEQMKEI-IRMCAYQR-QTMLFSATMSEEVKDLASVSLK-QPVRIFVNS 410
Cdd:cd17920 145 wghD------FRPDYLRLgRLRRALPGvPILALTATATPEVREDILKRLGlRNPVIFRAS 198
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
245-363 |
4.76e-04 |
|
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: 41.73 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 245 AATGTGKTAAFMLPVLERLiykprETQVTRVLVLVPTRELGIQVHTVARQLaqFTTISTCLAV-GGLDLKSQEAALRAGp 323
Cdd:cd18035 23 LPTGLGKTIIAILVAADRL-----TKKGGKVLILAPSRPLVEQHAENLKRV--LNIPDKITSLtGEVKPEERAERWDAS- 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 49618925 324 DVLIATPGRLIDHLHNTpSFELSQIEILILDEADRMLDEY 363
Cdd:cd18035 95 KIIVATPQVIENDLLAG-RITLDDVSLLIFDEAHHAVGNY 133
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
221-536 |
2.12e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 41.80 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 221 FKQPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLERLIYKPRETQV-TRVLVLV--PTRELGIQVHtvaRQLAQ 297
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGELeDKVYCLYvsPLRALNNDIH---RNLEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 298 -FTTISTCLAVGGLDLKSQEAALRAG--------------PDVLIATPGRLIDHLhNTPSF--ELSQIEILILDeadrml 360
Cdd:PRK13767 107 pLTEIREIAKERGEELPEIRVAIRTGdtssyekqkmlkkpPHILITTPESLAILL-NSPKFreKLRTVKWVIVD------ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 361 deyfeeqmkEIIRMCAYQRQTMLfSATMsEEVKDLASvslKQPVRI----FVNSNTDVAPYL---------RQ-EFVRIR 426
Cdd:PRK13767 180 ---------EIHSLAENKRGVHL-SLSL-ERLEELAG---GEFVRIglsaTIEPLEEVAKFLvgyeddgepRDcEIVDAR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 427 PNKEGD--------------REAIVAAL---LTRTFQDH--VMLFTQTKKQAHR-MHILLGLMGLKVGEL-----HGNLS 481
Cdd:PRK13767 246 FVKPFDikvispvddlihtpAEEISEALyetLHELIKEHrtTLIFTNTRSGAERvLYNLRKRFPEEYDEDnigahHSSLS 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 49618925 482 QTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGR 536
Cdd:PRK13767 326 REVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGR 380
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
220-360 |
2.35e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 40.00 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 220 GFKqPTPIQKACVPVGLLGKDICACAATGTGKTAAFMLPVLerLIYKPREtqvtRVLVLVPTRELGIQVHTVARQLAQFT 299
Cdd:cd17924 15 GFP-PWGAQRTWAKRLLRGKSFAIIAPTGVGKTTFGLATSL--YLASKGK----RSYLIFPTKSLVKQAYERLSKYAEKA 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49618925 300 TISTCLAV--GGLDLKSQEAALRA----GPDVLIATPGRLIDHLHNTPSFELSqieILILDEADRML 360
Cdd:cd17924 88 GVEVKILVyhSRLKKKEKEELLEKiekgDFDILVTTNQFLSKNFDLLSNKKFD---FVFVDDVDAVL 151
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
470-515 |
4.37e-03 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 40.42 E-value: 4.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 49618925 470 GLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVaargldIE-GV 515
Cdd:COG1200 503 GLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV------IEvGV 543
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
471-512 |
5.04e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 38.48 E-value: 5.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 49618925 471 LKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDI 512
Cdd:cd18811 62 LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDV 103
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
238-355 |
8.46e-03 |
|
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: 37.95 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 238 GKDICACAATGTGKTAAFMLPVLERLIYKPRETqvTRVLVLVPTRELGIQVHtvaRQLaqfTTISTCLAVG-------Gl 310
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKG--VQVLYISPLKALINDQE---RRL---EEPLDEIDLEipvavrhG- 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 49618925 311 DLKSQE--AALRAGPDVLIATPGRLIDHLHNTPSFE-LSQIEILILDE 355
Cdd:cd17922 72 DTSQSEkaKQLKNPPGILITTPESLELLLVNKKLRElFAGLRYVVVDE 119
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
245-365 |
8.52e-03 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 37.93 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49618925 245 AATGTGKT--AAFMLPvleRLIykpRETQVTRVLVLVPTRELGIQvhtVARQLAQFTTISTCLAVGGLDLKSQEAalrag 322
Cdd:cd18032 27 MATGTGKTytAAFLIK---RLL---EANRKKRILFLAHREELLEQ---AERSFKEVLPDGSFGNLKGGKKKPDDA----- 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 49618925 323 pDVLIATPGRL--IDHLHNTPS--FELsqieiLILDEADR-------MLDEYFE 365
Cdd:cd18032 93 -RVVFATVQTLnkRKRLEKFPPdyFDL-----IIIDEAHHaiassyrKILEYFE 140
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
470-541 |
8.95e-03 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 39.31 E-value: 8.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49618925 470 GLKVGELHGNLSQTQRLESLRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTVKHYVHRVGRTARAG 541
Cdd:PRK11057 260 GISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
|
|
| |
