|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
188-577 |
2.73e-155 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 458.07 E-value: 2.73e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 188 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPvtRVLVLVPT 267
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAP--QALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 268 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLD 347
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 348 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNregDREAIVAALL 427
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR---DKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 428 TRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF 507
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 508 TMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKMEK 577
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPK 386
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
198-393 |
5.20e-135 |
|
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: 397.01 E-value: 5.20e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRVLVLVPTRELGIQVHSV 277
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 278 TRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKEI 357
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1872046761 358 IRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 393
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
189-559 |
7.56e-95 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 302.25 E-value: 7.56e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 189 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAP-VTRVLVLVPT 267
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSgPPRILILTPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 268 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLD 347
Cdd:PRK11192 83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKE-ENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 348 EYFEEQMKEIIRMCSHHRQTMLFSATMTDE-VKDLASVSLKNPVRIfvnsntDVAPFLR-----QEFIRIRPNREgDREA 421
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEV------EAEPSRRerkkiHQWYYRADDLE-HKTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 422 IVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGV 501
Cdd:PRK11192 235 LLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1872046761 502 KTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARI 559
Cdd:PRK11192 315 SHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARV 372
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
198-392 |
7.56e-92 |
|
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: 285.49 E-value: 7.56e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPV-TRVLVLVPTRELGIQVHS 276
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRgPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 277 VTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCpSFHLSSIEVLILDEADRMLDEYFEEQMKE 356
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERG-KLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1872046761 357 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
188-562 |
1.66e-89 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 289.01 E-value: 1.66e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 188 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQaPVTRVLVLVPT 267
Cdd:PRK11776 5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--DVKR-FRVQALVLCPT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 268 RELGIQVHSVTRQLAQFC-NI---TTClavGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEAD 343
Cdd:PRK11776 82 RELADQVAKEIRRLARFIpNIkvlTLC---GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRK-GTLDLDALNTLVLDEAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 344 RMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSnTDVAPFLRQEFIRIRPNregDREAIV 423
Cdd:PRK11776 158 RMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES-THDLPAIEQRFYEVSPD---ERLPAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 424 AALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKT 503
Cdd:PRK11776 234 QRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEA 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1872046761 504 VINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQ 562
Cdd:PRK11776 314 VINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS 372
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
187-555 |
2.44e-87 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 283.24 E-value: 2.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 187 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQA----PVtRVL 262
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAkgrrPV-RAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 263 VLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEA 342
Cdd:PRK10590 80 ILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQ-NAVKLDQVEILVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 343 DRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREGDreaI 422
Cdd:PRK10590 159 DRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRE---L 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 423 VAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVK 502
Cdd:PRK10590 236 LSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELP 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1872046761 503 TVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPV 555
Cdd:PRK10590 316 HVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
189-565 |
5.17e-80 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 264.47 E-value: 5.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 189 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVTRVLVL 264
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPppkeRYMGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 265 VPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAA-PDILIATPGRLIDHLHNcPSFHLSSIEVLILDEAD 343
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQR-GEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 344 RMLDEYFEEQMKEIIRMCSH--HRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQefiRIRPNREGDREA 421
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQ---HVYAVAGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 422 IVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGV 501
Cdd:PRK01297 325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1872046761 502 KTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQDVI 565
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAELL 468
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
189-539 |
3.54e-76 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 252.58 E-value: 3.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 189 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVTRVLVL 264
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPapedRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 265 VPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHL-HNCpsFHLSSIEVLILDEAD 343
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAkQNH--INLGAIQVVVLDEAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 344 RMLDEYFEEQMKEIIRMC--SHHRQTMLFSATMTDEVKDLASVSLKNPVRIfvnsntDVAPfLRQEFIRIR-----PNRE 416
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMppANQRLNMLFSATLSYRVRELAFEHMNNPEYV------EVEP-EQKTGHRIKeelfyPSNE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 417 gDREAIVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGL 496
Cdd:PRK04837 241 -EKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1872046761 497 DIEGVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGED 539
Cdd:PRK04837 320 HIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 362
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
188-628 |
3.76e-76 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 258.62 E-value: 3.76e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 188 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiyKPR-QAPvtRVLVLVP 266
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPElKAP--QILVLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 267 TRELGIQVHSVTRQLAQFCNITTCLAV-GGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRM 345
Cdd:PRK11634 83 TRELAVQVAEAMTDFSKHMRGVNVVALyGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKR-GTLDLSKLSGLVLDEADEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 346 LDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREgdREAIVAA 425
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRK--NEALVRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 426 LLTRTFtDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVI 505
Cdd:PRK11634 240 LEAEDF-DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 506 NFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPV------KARILPQDVILKFRDKI----EKM 575
Cdd:PRK11634 319 NYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIpevelpNAELLGKRRLEKFAAKVqqqlESS 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1872046761 576 EKDVYAVLqLEAEEKEMQQSEAQINT-AKRLLE--KGKEAVVQEPE-----RSWFQTKEER 628
Cdd:PRK11634 399 DLDQYRAL-LAKIQPTAEGEELDLETlAAALLKmaQGERPLILPPDapmrpKREFRDRDDR 458
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
188-555 |
4.41e-76 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 255.85 E-value: 4.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 188 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALP----VLERLIYKPRQAPVtrVLV 263
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaivhINAQPLLRYGDGPI--VLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 264 LVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLH-NCPSfhLSSIEVLILDEA 342
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLEsNVTN--LRRVTYLVLDEA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 343 DRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKN-PVRIFVNSNTDVAPF-LRQEFIRIRpnrEGDRE 420
Cdd:PTZ00110 287 DRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTACHnIKQEVFVVE---EHEKR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 421 AIVAALLTRTFTD--HVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDI 498
Cdd:PTZ00110 364 GKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDV 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 499 EGVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVK---AAKAPV 555
Cdd:PTZ00110 444 KDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKvlrEAKQPV 503
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
186-560 |
4.08e-75 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 254.10 E-value: 4.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 186 NLSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVTRV 261
Cdd:PRK04537 8 DLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPaladRKPEDPRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 262 LVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDE 341
Cdd:PRK04537 88 LILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 342 ADRMLDEYFEEQMKEIIRMCSHH--RQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQefiRIRPNREGDR 419
Cdd:PRK04537 168 ADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ---RIYFPADEEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 420 EAIVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIE 499
Cdd:PRK04537 245 QTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHID 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1872046761 500 GVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEI-----VKAAKAPVKARIL 560
Cdd:PRK04537 325 GVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIeayieQKIPVEPVTAELL 390
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
188-392 |
2.05e-69 |
|
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: 226.81 E-value: 2.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 188 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPT 267
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQR---FFALVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 268 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLD 347
Cdd:cd17954 78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1872046761 348 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd17954 158 MDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
189-390 |
1.61e-68 |
|
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: 224.41 E-value: 1.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 189 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiykpRQAPV-TRVLVLVPT 267
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL----SEDPYgIFALVLTPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 268 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPS--FHLSSIEVLILDEADRM 345
Cdd:cd17955 77 RELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttKVLSRVKFLVLDEADRL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1872046761 346 LDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPV 390
Cdd:cd17955 157 LTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
188-392 |
2.31e-67 |
|
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: 221.41 E-value: 2.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 188 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQAPV-TRVLVLVP 266
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--KAHSPTVgARALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 267 TRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCpSFHLSSIEVLILDEADRML 346
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEM-NLKLSSVEYVVFDEADRLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1872046761 347 DEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
188-394 |
7.60e-63 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350725 [Multi-domain] Cd Length: 221 Bit Score: 209.65 E-value: 7.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 188 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTR------- 260
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 261 VLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILD 340
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFI-ERGRISLSSIKFLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1872046761 341 EADRMLDEYFEEQMKEIIRMCS----HHRQTMLFSATMTDEVKDLASVSLKNpvRIFV 394
Cdd:cd17967 160 EADRMLDMGFEPQIRKIVEHPDmppkGERQTLMFSATFPREIQRLAADFLKN--YIFL 215
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
199-395 |
3.23e-62 |
|
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: 207.14 E-value: 3.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 199 LKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiYKPRQAPVTRV--LVLVPTRELGIQVHS 276
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL-YRERWTPEDGLgaLIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 277 VTRQLAQFCNITTCLAVGGLDVKsQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 356
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVK-EEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1872046761 357 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVN 395
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
187-553 |
1.05e-60 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 213.50 E-value: 1.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 187 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTR----VL 262
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEQrnplAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 263 VLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHL--HNcpsFHLSSIEVLILD 340
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLskHD---IELDNVSVLVLD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 341 EADRMLDEYFEEQMKEIIRMCShHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREgdRE 420
Cdd:PLN00206 278 EVDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQK--KQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 421 AIVAALLTRT-FTDHVMLFTQTKKQAHrmhiLLG-----LMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAAR 494
Cdd:PLN00206 355 KLFDILKSKQhFKPPAVVFVSSRLGAD----LLAnaitvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGR 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1872046761 495 GLDIEGVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKA 553
Cdd:PLN00206 431 GVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKS 489
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
194-392 |
3.00e-60 |
|
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: 202.43 E-value: 3.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 194 LSRPLlkaITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIykPRQAPVTR-----VLVLVPTR 268
Cdd:cd17949 1 LVSHL---KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLL--SLEPRVDRsdgtlALVLVPTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 269 ELGIQVHSVTRQLAQFC-NITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLD 347
Cdd:cd17949 76 ELALQIYEVLEKLLKPFhWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1872046761 348 EYFEEQMKEIIRM-------------CSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd17949 156 MGFEKDITKILELlddkrskaggeksKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
181-547 |
4.56e-59 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 205.83 E-value: 4.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 181 SQYDENL-SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvT 259
Cdd:PTZ00424 21 SNYDEIVdSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNA---C 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 260 RVLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLIL 339
Cdd:PTZ00424 98 QALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI-DKRHLRVDDLKLFIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 340 DEADRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRpNREGDR 419
Cdd:PTZ00424 177 DEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVE-KEEWKF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 420 EAIVAALLTRTFTdHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIE 499
Cdd:PTZ00424 256 DTLCDLYETLTIT-QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1872046761 500 GVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEI 547
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
194-390 |
2.53e-58 |
|
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: 197.04 E-value: 2.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 194 LSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLErLIYKPRQA----PVTRVLVLVPTRE 269
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQ-KILKAKAEsgeeQGTRALILVPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 270 LGIQVHSVTRQLAQFC-NITTCLAVGG-LDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLD 347
Cdd:cd17961 80 LAQQVSKVLEQLTAYCrKDVRVVNLSAsSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1872046761 348 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPV 390
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
198-394 |
5.78e-58 |
|
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: 195.50 E-value: 5.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIyKPRQAPVTRVLVLVPTRELGIQVHSV 277
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLG-KPRKKKGLRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 278 TRQLAQFCNITTCLavggLDvKSQEAALRAAP------DILIATPGRLIDHLHNCPSfHLSSIEVLILDEADRMLDEYFE 351
Cdd:cd17957 80 LLKLSKGTGLRIVL----LS-KSLEAKAKDGPksitkyDILVSTPLRLVFLLKQGPI-DLSSVEYLVLDEADKLFEPGFR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1872046761 352 EQMKEIIRMCSHHR-QTMLFSATMTDEVKDLASVSLKNPVRIFV 394
Cdd:cd17957 154 EQTDEILAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
198-392 |
6.83e-58 |
|
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: 195.49 E-value: 6.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRV--LVLVPTRELGIQVH 275
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVgaLIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 276 SVTRQLAQFC--NITTCLAVGGLDVKSQEAALRA-APDILIATPGRLIDHL-HNCPSFHLSSIEVLILDEADRMLDEYFE 351
Cdd:cd17960 81 EVLQSFLEHHlpKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLsRKADKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1872046761 352 EQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
199-395 |
4.42e-57 |
|
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: 193.35 E-value: 4.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 199 LKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLErLIYKPRQAPV--TRVLVLVPTRELGIQVHS 276
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIE-LLYKLKFKPRngTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 277 VTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 356
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1872046761 357 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPvRIFVN 395
Cdd:cd17942 161 IIKLLPKRRQTMLFSATQTRKVEDLARISLKKK-PLYVG 198
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
211-381 |
1.08e-56 |
|
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: 190.92 E-value: 1.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 211 TPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPrqaPVTRVLVLVPTRELGIQVHSVTRQLAQFCNITTC 290
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD---NGPQALVLAPTRELAEQIYEELKKLGKGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 291 LAVGGLDVKSQEAALRAaPDILIATPGRLIDHLHNcpSFHLSSIEVLILDEADRMLDEYFEEQMKEIIRMCSHHRQTMLF 370
Cdd:pfam00270 78 SLLGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQE--RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
|
170
....*....|.
gi 1872046761 371 SATMTDEVKDL 381
Cdd:pfam00270 155 SATLPRNLEDL 165
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
194-387 |
9.91e-56 |
|
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: 190.10 E-value: 9.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 194 LSRPLLKAITAMGFKQPTPIQKACIPVGL-LGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRV--LVLVPTREL 270
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVsaLIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 271 GIQVHSVTRQLAQFC-NITTCLAVGGLDVKSQEAAL-RAAPDILIATPGRLIDHLHNCPSF-HLSSIEVLILDEADRMLD 347
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVAkAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1872046761 348 EYFEEQMKEIIR----MCSHHRQTMLFSATMTDEVKDLASVSLK 387
Cdd:cd17964 161 MGFRPDLEQILRhlpeKNADPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
198-392 |
1.07e-54 |
|
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: 187.53 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTR-----VLVLVPTRELGI 272
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKddgpyALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 273 QVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcpsfH---LSSIEVLILDEADRMLDEY 349
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLER----RllvLNQCTYVVLDEADRMIDMG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1872046761 350 FEEQMKEII--------------------RMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd17945 157 FEPQVTKILdampvsnkkpdteeaeklaaSGKHRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
191-393 |
2.04e-51 |
|
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: 177.90 E-value: 2.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 191 DMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiykPRQAPVTRVLVLVPTREL 270
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI---DTTVRETQALVLAPTREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 271 GIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYF 350
Cdd:cd17939 78 AQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1872046761 351 EEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 393
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
187-387 |
5.56e-51 |
|
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: 179.01 E-value: 5.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 187 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLI--------YKPRQAPv 258
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkegltassFSEVQEP- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 259 tRVLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLI 338
Cdd:cd18052 122 -QALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFI-GRGKISLSKLKYLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1872046761 339 LDEADRMLDEYFEEQMKEIIRMCS----HHRQTMLFSATMTDEVKDLASVSLK 387
Cdd:cd18052 200 LDEADRMLDMGFGPEIRKLVSEPGmpskEDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
198-394 |
7.66e-51 |
|
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: 177.44 E-value: 7.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIP---------VGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQAPVTRVLVLVPTR 268
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPwllpsskstPPYRPGDLCVSAPTGSGKTLAYVLPIVQAL--SKRVVPRLRALIVVPTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 269 ELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAA--------PDILIATPGRLIDHLHNCPSFHLSSIEVLILD 340
Cdd:cd17956 79 ELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGFTLKHLRFLVID 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1872046761 341 EADRMLDEYFEE------------------QMKEIIRMCSHHR--QTMLFSATMTDEVKDLASVSLKNPvRIFV 394
Cdd:cd17956 159 EADRLLNQSFQDwletvmkalgrptapdlgSFGDANLLERSVRplQKLLFSATLTRDPEKLSSLKLHRP-RLFT 231
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
404-536 |
9.11e-50 |
|
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: 170.77 E-value: 9.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 404 LRQEFIRIRPNREgdREAIVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQI 483
Cdd:cd18787 1 IKQLYVVVEEEEK--KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1872046761 484 DILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLV 536
Cdd:cd18787 79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
198-392 |
2.75e-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: 171.78 E-value: 2.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPV--TRVLVLVPTRELGIQVH 275
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGdgPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 276 SVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDhLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMK 355
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLID-FLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1872046761 356 EIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
189-392 |
8.06e-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: 170.56 E-value: 8.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 189 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKprqAPVTRVLVLVPTR 268
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPK---KDVIQALILVPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 269 ELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDhLHNCPSFHLSSIEVLILDEADRMLDE 348
Cdd:cd17940 78 ELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1872046761 349 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
198-392 |
9.06e-49 |
|
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: 170.29 E-value: 9.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLI----YKPRQAPVtrVLVLVPTRELGIQ 273
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMdqreLEKGEGPI--AVIVAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 274 VHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFEEQ 353
Cdd:cd17952 79 IYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKK-KATNLQRVTYLVLDEADRMFDMGFEYQ 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1872046761 354 MKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd17952 158 VRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
202-392 |
1.05e-47 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 167.67 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 202 ITAMGFKQPTPIQKACIPVGLLG-KDICACAATGTGKTAAFALPVLERLIYKPRqapvTRVLVLVPTRELGIQVHSVTRQ 280
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKG----GRVLVLVPTRELAEQWAEELKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 281 LAQFCNITTCLAVGGLDVKSQEAAL-RAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFEEQMKEIIR 359
Cdd:smart00487 77 LGPSLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
|
170 180 190
....*....|....*....|....*....|...
gi 1872046761 360 MCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI 188
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
198-375 |
4.14e-46 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 164.33 E-value: 4.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLL-GKDICACAATGTGKTAAFALPVLERLIYKPRQAPVT------RVLVLVPTREL 270
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGgkqkplRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 271 GIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSF--HLSSIEVLILDEADRMLDE 348
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1872046761 349 -YFEEqMKEIIRM-------CSHHRQTMLFSATMT 375
Cdd:cd17946 161 gHFAE-LEKILELlnkdragKKRKRQTFVFSATLT 194
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
189-392 |
8.26e-45 |
|
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: 159.53 E-value: 8.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 189 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYkprQAPVTRVLVLVPTR 268
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDT---SLKATQALVLAPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 269 ELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILDEADRMLDE 348
Cdd:cd18046 78 ELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1872046761 349 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd18046 157 GFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
198-392 |
1.26e-44 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350709 [Multi-domain] Cd Length: 206 Bit Score: 159.43 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVL-------ERLIYKPRQAPVTrvLVLVPTREL 270
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqeKKLPFIKGEGPYG--LIVCPSREL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 271 GIQVHSVTRQLAQFCN------ITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILDEADR 344
Cdd:cd17951 79 ARQTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEADR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1872046761 345 MLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd17951 158 MIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
194-392 |
2.91e-43 |
|
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: 156.00 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 194 LSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALP----VLERLIYKPRQAPVTrvLVLVPTRE 269
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPmfrhIKDQRPVKPGEGPIG--LIMAPTRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 270 LGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHL--HNCPSFHLSSIEVLILDEADRMLD 347
Cdd:cd17953 97 LALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVTNLRRVTYVVLDEADRMFD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1872046761 348 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd17953 177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
198-392 |
2.94e-43 |
|
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: 155.01 E-value: 2.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRqAPVTrvLVLVPTRELGIQVHSV 277
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHR-NPSA--LILTPTRELAVQIEDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 278 TRQLAQ-FCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 356
Cdd:cd17962 78 AKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL-KQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1872046761 357 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd17962 157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
198-373 |
5.01e-43 |
|
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: 154.34 E-value: 5.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPTRELGIQVHSV 277
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRH---PQVLILAPTREIAVQIHDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 278 TRQLAQFC-NITTCLAVGGLDVKSQEAALRaAPDILIATPGRlIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 356
Cdd:cd17943 78 FKKIGKKLeGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGR-IKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170
....*....|....*..
gi 1872046761 357 IIRMCSHHRQTMLFSAT 373
Cdd:cd17943 156 IFSSLPKNKQVIAFSAT 172
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
198-393 |
1.45e-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: 153.39 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP---RQAPVTRVLVLVPTRELGIQV 274
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPiprEQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 275 HSVTRQLAqFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDhLHNCPSFHLSSIEVLILDEADRMLDEYFEEQM 354
Cdd:cd17958 81 EAECSKYS-YKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1872046761 355 KEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 393
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
194-392 |
3.16e-42 |
|
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: 152.34 E-value: 3.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 194 LSRPLLKAITAMGFKQPTPIQKACIPVgLLG---KDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPTREL 270
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPL-ILSdppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKS---PQALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 271 GIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEaalRAAPDILIATPGRLIDHL-HNCpsFHLSSIEVLILDEADRMLD-E 348
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVALAVPGNDVPRGK---KITAQIVIGTPGTVLDWLkKRQ--LDLKKIKILVLDEADVMLDtQ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1872046761 349 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd17963 152 GHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
188-388 |
4.21e-42 |
|
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: 153.66 E-value: 4.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 188 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLI----YKPRQAPVTR--- 260
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYeqgpGESLPSESGYygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 261 ------VLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSI 334
Cdd:cd18051 102 rkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLER-GKIGLDYC 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1872046761 335 EVLILDEADRMLDEYFEEQMKEIIRMC----SHHRQTMLFSATMTDEVKDLASVSLKN 388
Cdd:cd18051 181 KYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
188-394 |
2.78e-40 |
|
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: 147.11 E-value: 2.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 188 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPT 267
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQ---VSVLVICHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 268 RELGIQVHSVTRQLAQFC-NITTCLAVGGLDVKSQEAALR-AAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRM 345
Cdd:cd17950 80 RELAFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVRE-KKLKLSHVKHFVLDECDKM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1872046761 346 LDEY-FEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFV 394
Cdd:cd17950 159 LEQLdMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
187-396 |
2.93e-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: 145.15 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 187 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVtrVL 262
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflerGDGPI--CL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 263 VLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHnCPSFHLSSIEVLILDEA 342
Cdd:cd18049 102 VLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLE-AGKTNLRRCTYLVLDEA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1872046761 343 DRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNS 396
Cdd:cd18049 181 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
189-390 |
1.10e-36 |
|
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: 136.68 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 189 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLErliykprqapVTRVLVLVPTR 268
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ----------IVVALILEPSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 269 ELGIQVHSVTRQLAQFCN---ITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRM 345
Cdd:cd17938 71 ELAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKT-GKLDLSSVRFFVLDEADRL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1872046761 346 LDEYFEEQMKEIIRMCSHHR------QTMLFSATM-TDEVKDLASVSLKNPV 390
Cdd:cd17938 150 LSQGNLETINRIYNRIPKITsdgkrlQVIVCSATLhSFEVKKLADKIMHFPT 201
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
189-392 |
3.65e-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: 132.21 E-value: 3.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 189 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPTR 268
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRE---TQALILSPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 269 ELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDE 348
Cdd:cd18045 78 ELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEMLNK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1872046761 349 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd18045 157 GFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
188-392 |
3.50e-33 |
|
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: 128.98 E-value: 3.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 188 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPR----QAPVtrVLV 263
Cdd:cd18050 63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYlergDGPI--CLV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 264 LVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSfHLSSIEVLILDEAD 343
Cdd:cd18050 141 LAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEAD 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1872046761 344 RMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 392
Cdd:cd18050 220 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
198-383 |
2.17e-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: 122.48 E-value: 2.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVTRVLVLVPTRELGIQ 273
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKllaeGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 274 VHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGrLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQ 353
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPG-ALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1872046761 354 MKEIIRMCSHHR-------------QTMLFSATMTDEVKDLAS 383
Cdd:cd17948 160 LSHFLRRFPLASrrsentdgldpgtQLVLVSATMPSGVGEVLS 202
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
418-527 |
1.93e-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: 115.39 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 418 DREAIVAALLTRTFTDHVMLFTQTKKQAHrMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLD 497
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 1872046761 498 IEGVKTVINFTMPNTIKHYVHRVGRTARAG 527
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 ... |
199-387 |
7.34e-30 |
|
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: 117.26 E-value: 7.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 199 LKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERL---IYKPRQAPVTRVLVLVPTRELGIQV- 274
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLqedQQPRKRGRAPKVLVLAPTRELANQVt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 275 ---HSVTRQLAQFCnittclAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFE 351
Cdd:cd17944 82 kdfKDITRKLSVAC------FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQN-GRLDLTKLKHVVLDEVDQMLDMGFA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1872046761 352 EQMKEIIRMC-----SHHRQTMLFSATMTDEVKDLASVSLK 387
Cdd:cd17944 155 EQVEEILSVSykkdsEDNPQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
188-389 |
6.51e-26 |
|
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: 106.64 E-value: 6.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 188 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLG--KDICACAATGTGKTAAFALPVLERLIYKpRQAPvtRVLVLV 265
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAL-KLYP--QCLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 266 PTRELGIQVHSVTRQLAQFCN-ITTCLAVGGldvKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADR 344
Cdd:cd18048 96 PTFELALQTGKVVEEMGKFCVgIQVIYAIRG---NRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVTNISVFVLDEADV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1872046761 345 MLD-EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNP 389
Cdd:cd18048 173 MINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
447-527 |
1.06e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 98.05 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 447 RMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGRTARA 526
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
|
.
gi 1872046761 527 G 527
Cdd:smart00490 82 G 82
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
188-389 |
3.33e-21 |
|
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: 92.48 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 188 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLG--KDICACAATGTGKTAAFALPVLERLiykPRQAPVTRVLVLV 265
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---EPANKYPQCLCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 266 PTRELGIQVHSVTRQLAQFC-NITTCLAVGGldvKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADR 344
Cdd:cd18047 79 PTYELALQTGKVIEQMGKFYpELKLAYAVRG---NKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1872046761 345 ML-DEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNP 389
Cdd:cd18047 156 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
224-682 |
3.03e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 95.48 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 224 GKDICACAATGTGKTAAFALpVLERLIYKPRqapvtrVLVLVPTRELGIQVHsvtrqlAQFCNITTCLAVGGLDVKSQEa 303
Cdd:COG1061 100 GGRGLVVAPTGTGKTVLALA-LAAELLRGKR------VLVLVPRRELLEQWA------EELRRFLGDPLAGGGKKDSDA- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 304 alraapDILIATPGRLIDHLHNcpSFHLSSIEVLILDEADRMLDEYFEEqmkeIIRMCSHHRqTMLFSAT--MTDEvKDL 381
Cdd:COG1061 166 ------PITVATYQSLARRAHL--DELGDRFGLVIIDEAHHAGAPSYRR----ILEAFPAAY-RLGLTATpfRSDG-REI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 382 ASVSLKN-----------------PVRIFV------NSNTDVAPFLRQEFIRIRPNREGDREAIVAALLTRTFTDHVMLF 438
Cdd:COG1061 232 LLFLFDGivyeyslkeaiedgylaPPEYYGirvdltDERAEYDALSERLREALAADAERKDKILRELLREHPDDRKTLVF 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 439 TQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVH 518
Cdd:COG1061 312 CSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 519 RVGRTARAGRAGRSVS---LVGEDeRKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKMEKDVYAVLQLEAEEKEMQQS 595
Cdd:COG1061 392 RLGRGLRPAPGKEDALvydFVGND-VPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELE 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 596 EAQINTAKRLLEkGKEAVVQEPERSWFQTKEERKKEKIAKALQEFDLALRGKKKRKKFMKDAKKKGEMTAEERSQFEILK 675
Cdd:COG1061 471 LLEDALLLVLAE-LLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLE 549
|
....*..
gi 1872046761 676 AQMFAER 682
Cdd:COG1061 550 ELAALLL 556
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
224-373 |
1.84e-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: 77.06 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 224 GKDICACAATGTGKTAAFALPVLERLIYKPRQapvtrVLVLVPTRELGIQVHSVTRQLAQFcNITTCLAVGGLDVKSQEA 303
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGKK-----VLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREK 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1872046761 304 ALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMkEIIRMCSHHR---QTMLFSAT 373
Cdd:cd00046 75 NKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALI-LDLAVRKAGLknaQVILLSAT 146
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
193-536 |
4.86e-16 |
|
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: 82.58 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 193 NLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRqapvTRVLVLVPTRELGI 272
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPG----ATALYLYPTKALAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 273 -QVHSVtRQLAQFCNITTCLAV--GglDVKSQE-AALRAAPDILIATPgrliD--HLHNCPSFH-----LSSIEVLILDE 341
Cdd:COG1205 116 dQLRRL-RELAEALGLGVRVATydG--DTPPEErRWIREHPDIVLTNP----DmlHYGLLPHHTrwarfFRNLRYVVIDE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 342 A---------------DRMLdeyfeeqmkeiiRMCSHHRQTMLF---SATMtDEVKDLASVSLKNPVRIfVNSNTdvAPF 403
Cdd:COG1205 189 AhtyrgvfgshvanvlRRLR------------RICRHYGSDPQFilaSATI-GNPAEHAERLTGRPVTV-VDEDG--SPR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 404 LRQEFIRIRP---NREGDREAIV-AALLTRTFTDH---VMLFTQTKKQAHRMHILL------GLMGLQVGELHGNLSQTQ 470
Cdd:COG1205 253 GERTFVLWNPplvDDGIRRSALAeAARLLADLVREglrTLVFTRSRRGAELLARYArralrePDLADRVAAYRAGYLPEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1872046761 471 RLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGrtaRAGRAGRSvSLV 536
Cdd:COG1205 333 RREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAG---RAGRRGQD-SLV 394
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
209-377 |
3.89e-15 |
|
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: 75.88 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 209 QPTPIQKACIPVgLLGK----------------DICACAA-TGTGKTAAFALPVLERL-------------IYKPRQAPV 258
Cdd:cd17965 30 KPSPIQTLAIKK-LLKTlmrkvtkqtsneepklEVFLLAAeTGSGKTLAYLAPLLDYLkrqeqepfeeaeeEYESAKDTG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 259 T-RVLVLVPTRELGIQVHSVTRQLAQFC--NITTCLAVGGLDVKSQEAALRAAPDILIATPGrLIDHLHNCPSFHLSSIE 335
Cdd:cd17965 109 RpRSVILVPTHELVEQVYSVLKKLSHTVklGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPG-KLASLAKSRPKILSRVT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1872046761 336 VLILDEADRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDE 377
Cdd:cd17965 188 HLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKE 229
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
466-547 |
1.06e-12 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 71.68 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 466 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF-TMPNTIKhYVHRVGRTARaGRAGRSVSLVGED----- 539
Cdd:COG1111 395 LTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYePVPSEIR-SIQRKGRTGR-KREGRVVVLIAKGtrdea 472
|
90
....*....|....*.
gi 1872046761 540 --------ERKMLKEI 547
Cdd:COG1111 473 yywssrrkEKKMKSIL 488
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
224-342 |
1.07e-10 |
|
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: 61.45 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 224 GKDICACAATGTGKTAAFALPVLERLIYKPRqapvTRVLVLVPTRELGI-QVHSVTRQLAQFCNITTCLAVGG-LDVKSQ 301
Cdd:cd17923 15 GRSVVVTTGTASGKSLCYQLPILEALLRDPG----SRALYLYPTKALAQdQLRSLRELLEQLGLGIRVATYDGdTPREER 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1872046761 302 EAALRAAPDILIATPGRL---IDHLHNCPSFHLSSIEVLILDEA 342
Cdd:cd17923 91 RAIIRNPPRILLTNPDMLhyaLLPHHDRWARFLRNLRYVVLDEA 134
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
466-614 |
2.06e-10 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 64.12 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 466 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFT-MPNTIKhYVHRVGRTARaGRAGRSVSLVGED----- 539
Cdd:PRK13766 407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIR-SIQRKGRTGR-QEEGRVVVLIAKGtrdea 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 540 --------ERKMlKEIVKAAKAPVKARILPQDVILKFRDKIEKMEKDVYAVLQL-EAEEKEMQQSEAQINTAKRLLEKGK 610
Cdd:PRK13766 485 yywssrrkEKKM-KEELKNLKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSkGKEEEEEEEKEEKDKETEEDEPEGP 563
|
....
gi 1872046761 611 EAVV 614
Cdd:PRK13766 564 KIIV 567
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
364-530 |
2.06e-09 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 60.54 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 364 HRQTMLFSATMTDEVKD--LASVSLKNPvRIFVnsntdvAPFLRQE-FIRIRPNREGDREAIVAALLTRTFTDHVMLFTQ 440
Cdd:COG0514 166 NVPVLALTATATPRVRAdiAEQLGLEDP-RVFV------GSFDRPNlRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 441 TKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATdVA-ARGLDIEGVKTVINFTMPNTIKHYVHR 519
Cdd:COG0514 239 SRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQE 317
|
170
....*....|.
gi 1872046761 520 VGrtaRAGRAG 530
Cdd:COG0514 318 IG---RAGRDG 325
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
222-349 |
2.41e-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: 57.83 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 222 LLGKDICACAATGTGKTAAfALPVLERLIYKPRQAPVTRVLVLVPTrelgiqVHSVTRQLAQFCNITTCLA--VGGL--D 297
Cdd:cd17927 15 LKGKNTIICLPTGSGKTFV-AVLICEHHLKKFPAGRKGKVVFLANK------VPLVEQQKEVFRKHFERPGykVTGLsgD 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1872046761 298 VKSQEAALRAAP--DILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEY 349
Cdd:cd17927 88 TSENVSVEQIVEssDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHNTTKNH 141
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
481-527 |
1.02e-08 |
|
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: 52.71 E-value: 1.02e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1872046761 481 EQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGRTARAG 527
Cdd:cd18785 21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
207-533 |
1.14e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 58.58 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 207 FKQPTPIQKACIPVGLLGKDICACAATGTGKT-AAFaLPVLERLIYKPRQAPV---TRVLVLVPTRELGIQVHsvtRQLA 282
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELpdgLRVLYISPLKALANDIE---RNLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 283 QFCNITTCLAVGGL----------DVKSQE--AALRAAPDILIATPgrliDHLH---NCPSF--HLSSIEVLILDE---- 341
Cdd:COG1201 98 APLEEIGEAAGLPLpeirvgvrtgDTPASErqRQRRRPPHILITTP----ESLAlllTSPDAreLLRGVRTVIVDEihal 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 342 ------ADRMLD-EYFEeqmkeiiRMCSHHRQTMLFSATMT--DEVKD-LASVSLKNPVRIfVNSNTDVAPFLR-----Q 406
Cdd:COG1201 174 agskrgVHLALSlERLR-------ALAPRPLQRIGLSATVGplEEVARfLVGYEDPRPVTI-VDAGAGKKPDLEvlvpvE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 407 EFIRIRPNREGDREAIVAALLT-----RTftdhVMLFTQTKKQA----HRMHILLGLMGLQVGELHGNLSQTQRLEALRR 477
Cdd:COG1201 246 DLIERFPWAGHLWPHLYPRVLDlieahRT----TLVFTNTRSQAerlfQRLNELNPEDALPIAAHHGSLSREQRLEVEEA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 478 FKDEQIDILVAT---DVaarGLDIEGVKTVINFTMPntikhyvHRVGRTA-RAGRAGRSV 533
Cdd:COG1201 322 LKAGELRAVVATsslEL---GIDIGDVDLVIQVGSP-------KSVARLLqRIGRAGHRV 371
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
466-526 |
1.45e-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: 54.13 E-value: 1.45e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1872046761 466 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGRtARA 526
Cdd:cd18802 74 MTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
438-531 |
6.95e-08 |
|
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: 51.83 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 438 FTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYV 517
Cdd:cd18794 36 YCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYY 115
|
90
....*....|....
gi 1872046761 518 HRVGrtaRAGRAGR 531
Cdd:cd18794 116 QESG---RAGRDGL 126
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
466-535 |
8.29e-08 |
|
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: 51.97 E-value: 8.29e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1872046761 466 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF-TMPNTIKhYVHRVGRTARaGRAGRSVSL 535
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYdASPSPIR-MIQRMGRTGR-KRQGRVVVL 142
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
230-373 |
3.50e-07 |
|
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: 50.38 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 230 CAATGTGKTA-AFALPVLerliykprqAPVTRVLVLVPTRELgiqVHSVTRQLAQFCNITTCLAVGGLDVKSQEAAlraa 308
Cdd:cd17926 24 VLPTGSGKTLtALALIAY---------LKELRTLIVVPTDAL---LDQWKERFEDFLGDSSIGLIGGGKKKDFDDA---- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1872046761 309 pDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFEeqmkEIIRMCSHHRQtMLFSAT 373
Cdd:cd17926 88 -NVVVATYQSLSNLAEE-EKDLFDQFGLLIVDEAHHLPAKTFS----EILKELNAKYR-LGLTAT 145
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
198-342 |
4.38e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 53.36 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 198 LLKAITAMGFKQPTPIQKACIPVGLL-GKDICACAATGTGKTAafalpVLERLIYK--PRQApvtRVLVLVPTRELGIQV 274
Cdd:COG1204 11 VIEFLKERGIEELYPPQAEALEAGLLeGKNLVVSAPTASGKTL-----IAELAILKalLNGG---KALYIVPLRALASEK 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1872046761 275 HS-VTRQLAQFcNITTCLAVGGLDVKSQEAAlraAPDILIATPGRLIDHLHNCPSFhLSSIEVLILDEA 342
Cdd:COG1204 83 YReFKRDFEEL-GIKVGVSTGDYDSDDEWLG---RYDILVATPEKLDSLLRNGPSW-LRDVDLVVVDEA 146
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
437-535 |
7.06e-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: 49.57 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 437 LFTQTKKQAHRMHILLG------LMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMP 510
Cdd:cd18796 43 VFTNTRSQAERLAQRLRelcpdrVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
|
90 100
....*....|....*....|....*
gi 1872046761 511 NTIKHYVHRVGrtaRAGRAGRSVSL 535
Cdd:cd18796 123 KSVARLLQRLG---RSGHRPGAASK 144
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
435-510 |
1.02e-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: 48.63 E-value: 1.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1872046761 435 VMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQ--IDILVATDVAARGLDIEGVKTVINFTMP 510
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPW 107
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
225-342 |
1.76e-06 |
|
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: 49.19 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 225 KDICACAATGTGKTaAFALPVLERLIYKPRQ--APVTRVLVLVPTRELGIQVHSVTRQLaqfcnitTCLAVG---GLDVK 299
Cdd:cd18034 17 RNTIVVLPTGSGKT-LIAVMLIKEMGELNRKekNPKKRAVFLVPTVPLVAQQAEAIRSH-------TDLKVGeysGEMGV 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1872046761 300 SQEAALR-----AAPDILIATPGRLIDHLHNCpSFHLSSIEVLILDEA 342
Cdd:cd18034 89 DKWTKERwkeelEKYDVLVMTAQILLDALRHG-FLSLSDINLLIFDEC 135
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
231-522 |
6.35e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 49.92 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 231 AATGTGKTAAFALPVLERLIYK-------PRQAPVTRVLVLVPTRELG--------IQVHSVT----RQLAQFCNITTCL 291
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFREggedtreAHKRKTSRILYISPIKALGtdvqrnlqIPLKGIAderrRRGETEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 292 AVGglDVKSQEAA--LRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDE----ADRMLDEYFEEQMKEIIRMCSHHR 365
Cdd:PRK09751 83 RTG--DTPAQERSklTRNPPDILITTPESLYLMLTSRARETLRGVETVIIDEvhavAGSKRGAHLALSLERLDALLHTSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 366 QTMLFSATMTdEVKDLAS-------VSLKNP-------VRIF--VNSNTDVAPFLRQEFIRIRPNREGD-----REAIVA 424
Cdd:PRK09751 161 QRIGLSATVR-SASDVAAflggdrpVTVVNPpamrhpqIRIVvpVANMDDVSSVASGTGEDSHAGREGSiwpyiETGILD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 425 ALLTRTFTdhvMLFTQTKKQAHRMHILL---------------------------------GLMGLQVGELHGNLSQTQR 471
Cdd:PRK09751 240 EVLRHRST---IVFTNSRGLAEKLTARLnelyaarlqrspsiavdaahfestsgatsnrvqSSDVFIARSHHGSVSKEQR 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1872046761 472 LEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGR 522
Cdd:PRK09751 317 AITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGR 367
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
211-383 |
7.06e-06 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 47.26 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 211 TPIQKACIPVGLL-GKDICACAATGTGKTAAFALPVLERLIYKPRqapvtRVLVLVPTRELGIQVHSVTRQLAQFCNITT 289
Cdd:cd17921 3 NPIQREALRALYLsGDSVLVSAPTSSGKTLIAELAILRALATSGG-----KAVYIAPTRALVNQKEADLRERFGPLGKNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 290 CLAVGGLDVKSQEAAlraAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDE----YFEEQMKEIIRMCSHHR 365
Cdd:cd17921 78 GLLTGDPSVNKLLLA---EADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIGDGergvVLELLLSRLLRINKNAR 154
|
170
....*....|....*...
gi 1872046761 366 qtMLFSATMTDEVKDLAS 383
Cdd:cd17921 155 --FVGLSATLPNAEDLAE 170
|
|
| UTP25 |
pfam06862 |
Utp25, U3 small nucleolar RNA-associated SSU processome protein 25; UTP25 is a family of ... |
310-411 |
1.04e-05 |
|
Utp25, U3 small nucleolar RNA-associated SSU processome protein 25; UTP25 is a family of eukaryotic proteins. The family displays limited sequence similarity to DEAD-box RNA helicases, having alternative residues at the Walker A and DEAD-box sites, but conservation of structural and other key residues. The domain is required and sufficient for the interaction of Utp25 with Utp3. UTP25 interacts with nucleolar protein Nop19 in S. cerevisiae, and Nop19p is essential for the incorporation of Utp25p into pre-ribosomes.
Pssm-ID: 369113 Cd Length: 471 Bit Score: 48.79 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 310 DILIATP-G-RLI----DHLHNCPSFhLSSIEVLILDEADRMLD---EYFEEQMKEI--------------IRM------ 360
Cdd:pfam06862 161 DIIIASPlGlRMIigneDKKKRDFDF-LSSIEVLIVDQADSIEMqnwEHVLTVFKHLnlipkeshgcdfsrVRMwyldgq 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1872046761 361 CSHHRQTMLFSATMTDEVKDLASVSLKN---PVRIFVNSNT----DVAPFLRQEFIRI 411
Cdd:pfam06862 240 AKYYRQTIVFSSYITPEINSLFNSKCHNiagKVRVKPIYKGgsigQVGLKVRQVFQRF 297
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
204-396 |
2.06e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 45.99 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 204 AMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERliykprqAPVTrvLVLVPTRELGI-QVHSVTRQLA 282
Cdd:cd17920 7 VFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLL-------DGVT--LVVSPLISLMQdQVDRLQQLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 283 QFCNITtclavGGLDVKSQEAALRAAP----DILIATPGRL-----IDHLHNCPSFHLssIEVLILDEA--------Drm 345
Cdd:cd17920 78 RAAALN-----STLSPEEKREVLLRIKngqyKLLYVTPERLlspdfLELLQRLPERKR--LALIVVDEAhcvsqwghD-- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1872046761 346 ldeyFEEQMKEI--IRMCSHHRQTMLFSATMTDEVKDLASVSLK-NPVRIFVNS 396
Cdd:cd17920 149 ----FRPDYLRLgrLRRALPGVPILALTATATPEVREDILKRLGlRNPVIFRAS 198
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
203-346 |
2.96e-05 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 45.40 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 203 TAMGFKqPTPIQKACIPVGLLGKDICACAATGTGKT---AAFALpvlerLIYKPRQapvtRVLVLVPTRELGIQVHSVTR 279
Cdd:cd17924 12 KKTGFP-PWGAQRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSL-----YLASKGK----RSYLIFPTKSLVKQAYERLS 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1872046761 280 QLAQFCNITTCLAV--GGLDVKSQEAALRAAP----DILIATPGRLIDHLHNCPSFHLSSIevlILDEADRML 346
Cdd:cd17924 82 KYAEKAGVEVKILVyhSRLKKKEKEELLEKIEkgdfDILVTTNQFLSKNFDLLSNKKFDFV---FVDDVDAVL 151
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
222-341 |
1.55e-04 |
|
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: 43.62 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 222 LLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRVLVLVPtrelgiQVHSVTRQLAQFCNIttCLAV-------G 294
Cdd:cd18036 15 LRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVN------KVPLVEQQLEKFFKY--FRKGykvtglsG 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1872046761 295 GLDVKSQEAALRAAPDILIATPGRLIDHLHN---CPSFHLSSIEVLILDE 341
Cdd:cd18036 87 DSSHKVSFGQIVKASDVIICTPQILINNLLSgreEERVYLSDFSLLIFDE 136
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
310-498 |
2.07e-04 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 44.69 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 310 DILIATpgrlIDHL---------HNCPSFH--LSSieVLILDEADrMLDEYFEEQMKEIIRMCSHHRQTMLF-SATMTDE 377
Cdd:COG1203 240 PVVVTT----IDQLfeslfsnrkGQERRLHnlANS--VIILDEVQ-AYPPYMLALLLRLLEWLKNLGGSVILmTATLPPL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 378 VKDLasvsLKNPVRIfVNSNTDVAPFLRQEFIRIRPN-REG--DREAIVAALLTRTFTDH-VMLFTQTKKQAHRMHILL- 452
Cdd:COG1203 313 LREE----LLEAYEL-IPDEPEELPEYFRAFVRKRVElKEGplSDEELAELILEALHKGKsVLVIVNTVKDAQELYEALk 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1872046761 453 -GLMGLQVGELHGNLSQTQRLE----ALRRFKDEQIDILVATDVAARGLDI 498
Cdd:COG1203 388 eKLPDEEVYLLHSRFCPADRSEiekeIKERLERGKPCILVSTQVVEAGVDI 438
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
224-316 |
4.12e-04 |
|
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: 41.80 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 224 GKDICACAATGTGKTAAFALPVLERLiYKPRQAPVtRVLVLVPTRELGIQVHsvtRQLAQFCN-ITTCLAVG---GlDVK 299
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSL-ADEPEKGV-QVLYISPLKALINDQE---RRLEEPLDeIDLEIPVAvrhG-DTS 74
|
90
....*....|....*....
gi 1872046761 300 SQE--AALRAAPDILIATP 316
Cdd:cd17922 75 QSEkaKQLKNPPGILITTP 93
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
456-501 |
8.04e-04 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 42.73 E-value: 8.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1872046761 456 GLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVaargldIE-GV 501
Cdd:COG1200 503 GLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV------IEvGV 543
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
420-528 |
1.16e-03 |
|
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: 40.31 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 420 EAIVAALLTRTF-TDHVMLFTQTKKQAHRMHILLGLMGLqvgelHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDI 498
Cdd:cd18789 36 LRALEELLKRHEqGDKIIVFTDNVEALYRYAKRLLKPFI-----TGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDL 110
|
90 100 110
....*....|....*....|....*....|..
gi 1872046761 499 --EGVKTVINFTMPNTiKHYVHRVGRTARAGR 528
Cdd:cd18789 111 peANVAIQISGHGGSR-RQEAQRLGRILRPKK 141
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
456-530 |
1.79e-03 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 41.62 E-value: 1.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1872046761 456 GLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHrvgRTARAGRAG 530
Cdd:PRK11057 260 GISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQ---ETGRAGRDG 331
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
457-498 |
3.40e-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: 38.86 E-value: 3.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1872046761 457 LQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDI 498
Cdd:cd18811 62 LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDV 103
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
225-373 |
3.82e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.81 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 225 KDICACAATGTGKTA-AFALPvlERLIykpRQAPVTRVLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEA 303
Cdd:pfam04851 24 KRGLIVMATGSGKTLtAAKLI--ARLF---KKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDESVDD 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1872046761 304 AlraapDILIATPGRLIDHLHNCP-SFHLSSIEVLILDEADRmldeYFEEQMKEIIRMCSHhrQTML-FSAT 373
Cdd:pfam04851 99 N-----KIVVTTIQSLYKALELASlELLPDFFDVIIIDEAHR----SGASSYRNILEYFKP--AFLLgLTAT 159
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
227-352 |
4.46e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 227 ICACAATGTGKTAafalpVLERLIYKPRQAPVTRVLVLVPtrelgiqvHSVTRQ--LAQFCNITTCLAVGGLDVKsqeaA 304
Cdd:pfam13401 8 LVLTGESGTGKTT-----LLRRLLEQLPEVRDSVVFVDLP--------SGTSPKdlLRALLRALGLPLSGRLSKE----E 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1872046761 305 LRAapdiliatpgRLIDHLHncpsfHLSSIEVLILDEADRMLDEYFEE 352
Cdd:pfam13401 71 LLA----------ALQQLLL-----ALAVAVVLIIDEAQHLSLEALEE 103
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
456-501 |
4.71e-03 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 40.52 E-value: 4.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1872046761 456 GLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVaargldIE-GV 501
Cdd:PRK10917 505 ELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTV------IEvGV 545
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
231-351 |
6.27e-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: 38.31 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 231 AATGTGKT--AAFalpvlerLIYK-PRQAPVTRVLVLVPTRELGIQVHSvtrqlaQFCNITTCLAVGGLDVKSQEAALRa 307
Cdd:cd18032 27 MATGTGKTytAAF-------LIKRlLEANRKKRILFLAHREELLEQAER------SFKEVLPDGSFGNLKGGKKKPDDA- 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1872046761 308 apDILIATPGRL--IDHLHNCPSFHLSSIevlILDEADR-------MLDEYFE 351
Cdd:cd18032 93 --RVVFATVQTLnkRKRLEKFPPDYFDLI---IIDEAHHaiassyrKILEYFE 140
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
463-536 |
6.47e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 40.26 E-value: 6.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1872046761 463 HGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGrtaRAGRAGRSVSLV 536
Cdd:PLN03137 711 HGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECG---RAGRDGQRSSCV 781
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
213-349 |
8.77e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 37.88 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872046761 213 IQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPrqapvTRVLVLVPTRELGIQvHSvtRQLAQFCNIT-TCL 291
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLTKKG-----GKVLILAPSRPLVEQ-HA--ENLKRVLNIPdKIT 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1872046761 292 AVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEY 349
Cdd:cd18035 77 SLTGEVKPEERAERWDASKIIVATPQVIENDLLA-GRITLDDVSLLIFDEAHHAVGNY 133
|
|
| |
