|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
219-608 |
5.45e-153 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 453.06 E-value: 5.45e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPvtRVLVLVPT 298
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAP--QALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 299 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLD 378
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNregDREAIVAALL 458
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR---DKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 459 TRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF 538
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 539 TMPNTIKHYDHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKMEK 608
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPK 386
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
229-424 |
1.07e-134 |
|
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: 397.40 E-value: 1.07e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRVLVLVPTRELGIQVHSV 308
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 309 TRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKEI 388
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 15422163 389 IRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 424
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
220-590 |
1.12e-93 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 299.94 E-value: 1.12e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAP-VTRVLVLVPT 298
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSgPPRILILTPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 299 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLD 378
Cdd:PRK11192 83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKE-ENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDE-VKDLASVSLKNPVRIfvnsntDVAPFLR-----QEFIRIRPNREgDREA 452
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEV------EAEPSRRerkkiHQWYYRADDLE-HKTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 453 IVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGV 532
Cdd:PRK11192 235 LLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15422163 533 KTVINFTMPNTIKHYDHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARI 590
Cdd:PRK11192 315 SHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARV 372
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
229-423 |
7.72e-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: 286.26 E-value: 7.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPV-TRVLVLVPTRELGIQVHS 307
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRgPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 308 VTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCpSFHLSSIEVLILDEADRMLDEYFEEQMKE 387
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERG-KLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 15422163 388 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
219-593 |
1.20e-87 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 284.77 E-value: 1.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQaPVTRVLVLVPT 298
Cdd:PRK11776 5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--DVKR-FRVQALVLCPT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 299 RELGIQVHSVTRQLAQFC-NI---TTClavGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEAD 374
Cdd:PRK11776 82 RELADQVAKEIRRLARFIpNIkvlTLC---GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRK-GTLDLDALNTLVLDEAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 375 RMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSnTDVAPFLRQEFIRIRPNregDREAIV 454
Cdd:PRK11776 158 RMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES-THDLPAIEQRFYEVSPD---ERLPAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 455 AALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKT 534
Cdd:PRK11776 234 QRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEA 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15422163 535 VINFTMPNTIKHYDHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQ 593
Cdd:PRK11776 314 VINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS 372
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
218-586 |
1.49e-85 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 279.00 E-value: 1.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 218 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQA----PVtRVL 293
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAkgrrPV-RAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 294 VLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEA 373
Cdd:PRK10590 80 ILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQ-NAVKLDQVEILVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 374 DRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREGDreaI 453
Cdd:PRK10590 159 DRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRE---L 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 454 VAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVK 533
Cdd:PRK10590 236 LSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELP 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15422163 534 TVINFTMPNTIKHYDHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPV 586
Cdd:PRK10590 316 HVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
220-596 |
1.13e-78 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 261.39 E-value: 1.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVTRVLVL 295
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPppkeRYMGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 296 VPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAA-PDILIATPGRLIDHLHNcPSFHLSSIEVLILDEAD 374
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQR-GEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 375 RMLDEYFEEQMKEIIRMCSH--HRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQefiRIRPNREGDREA 452
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQ---HVYAVAGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 453 IVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGV 532
Cdd:PRK01297 325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15422163 533 KTVINFTMPNTIKHYDHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQDVI 596
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAELL 468
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
219-586 |
1.40e-74 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 252.39 E-value: 1.40e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALP----VLERLIYKPRQAPVtrVLV 294
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaivhINAQPLLRYGDGPI--VLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 295 LVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLH-NCPSfhLSSIEVLILDEA 373
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLEsNVTN--LRRVTYLVLDEA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 374 DRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKN-PVRIFVNSNTDVAPF-LRQEFIRIRpnrEGDRE 451
Cdd:PTZ00110 287 DRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTACHnIKQEVFVVE---EHEKR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 452 AIVAALLTRTFTD--HVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDI 529
Cdd:PTZ00110 364 GKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDV 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 530 EGVKTVINFTMPNTIKHYDHRVGRTARAGRAGRSVSLVGEDERKMLKEIVK---AAKAPV 586
Cdd:PTZ00110 444 KDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKvlrEAKQPV 503
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
220-570 |
1.93e-74 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 248.35 E-value: 1.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVTRVLVL 295
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPapedRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 296 VPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHL-HNCpsFHLSSIEVLILDEAD 374
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAkQNH--INLGAIQVVVLDEAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 375 RMLDEYFEEQMKEIIRMC--SHHRQTMLFSATMTDEVKDLASVSLKNPVRIfvnsntDVAPfLRQEFIRIR-----PNRE 447
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMppANQRLNMLFSATLSYRVRELAFEHMNNPEYV------EVEP-EQKTGHRIKeelfyPSNE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 448 gDREAIVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGL 527
Cdd:PRK04837 241 -EKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15422163 528 DIEGVKTVINFTMPNTIKHYDHRVGRTARAGRAGRSVSLVGED 570
Cdd:PRK04837 320 HIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 362
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
219-659 |
1.96e-74 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 254.39 E-value: 1.96e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiyKPR-QAPvtRVLVLVP 297
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPElKAP--QILVLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 298 TRELGIQVHSVTRQLAQFCNITTCLAV-GGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRM 376
Cdd:PRK11634 83 TRELAVQVAEAMTDFSKHMRGVNVVALyGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKR-GTLDLSKLSGLVLDEADEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 377 LDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREgdREAIVAA 456
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRK--NEALVRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 457 LLTRTFtDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVI 536
Cdd:PRK11634 240 LEAEDF-DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 537 NFTMPNTIKHYDHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPV------KARILPQDVILKFRDKI----EKM 606
Cdd:PRK11634 319 NYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIpevelpNAELLGKRRLEKFAAKVqqqlESS 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15422163 607 EKDVYAVLqLEAEEKEMQQSEAQINT-AKRLLE--KGKEAVVQEPE-----RSWFQTKEER 659
Cdd:PRK11634 399 DLDQYRAL-LAKIQPTAEGEELDLETlAAALLKmaQGERPLILPPDapmrpKREFRDRDDR 458
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
217-591 |
2.24e-73 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 250.25 E-value: 2.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 217 NLSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVTRV 292
Cdd:PRK04537 8 DLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPaladRKPEDPRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 293 LVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDE 372
Cdd:PRK04537 88 LILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 373 ADRMLDEYFEEQMKEIIRMCSHH--RQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQefiRIRPNREGDR 450
Cdd:PRK04537 168 ADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ---RIYFPADEEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 451 EAIVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIE 530
Cdd:PRK04537 245 QTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHID 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15422163 531 GVKTVINFTMPNTIKHYDHRVGRTARAGRAGRSVSLVGEDERKMLKEI-----VKAAKAPVKARIL 591
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 ... |
219-423 |
2.11e-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: 227.20 E-value: 2.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPT 298
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQR---FFALVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 299 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLD 378
Cdd:cd17954 78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15422163 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
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 ... |
220-421 |
2.45e-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: 2.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiykpRQAPV-TRVLVLVPT 298
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL----SEDPYgIFALVLTPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 299 RELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPS--FHLSSIEVLILDEADRM 376
Cdd:cd17955 77 RELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttKVLSRVKFLVLDEADRL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15422163 377 LDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPV 421
Cdd:cd17955 157 LTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
219-423 |
2.72e-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: 2.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQAPV-TRVLVLVP 297
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--KAHSPTVgARALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 298 TRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCpSFHLSSIEVLILDEADRML 377
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEM-NLKLSSVEYVVFDEADRLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15422163 378 DEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
219-425 |
1.15e-62 |
|
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: 1.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTR------- 291
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 292 VLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILD 371
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFI-ERGRISLSSIKFLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15422163 372 EADRMLDEYFEEQMKEIIRMCS----HHRQTMLFSATMTDEVKDLASVSLKNpvRIFV 425
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 ... |
230-426 |
3.83e-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: 207.53 E-value: 3.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 230 LKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiYKPRQAPVTRV--LVLVPTRELGIQVHS 307
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL-YRERWTPEDGLgaLIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 308 VTRQLAQFCNITTCLAVGGLDVKsQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 387
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVK-EEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 15422163 388 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVN 426
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
225-423 |
2.62e-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: 203.20 E-value: 2.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 225 LSRPLlkaITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIykPRQAPVTR-----VLVLVPTR 299
Cdd:cd17949 1 LVSHL---KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLL--SLEPRVDRsdgtlALVLVPTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 300 ELGIQVHSVTRQLAQFC-NITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLD 378
Cdd:cd17949 76 ELALQIYEVLEKLLKPFhWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15422163 379 EYFEEQMKEIIRM-------------CSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17949 156 MGFEKDITKILELlddkrskaggeksKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
218-584 |
1.34e-59 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 210.80 E-value: 1.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 218 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTR----VL 293
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEQrnplAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 294 VLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHL--HNcpsFHLSSIEVLILD 371
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLskHD---IELDNVSVLVLD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 372 EADRMLDEYFEEQMKEIIRMCShHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREgdRE 451
Cdd:PLN00206 278 EVDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQK--KQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 452 AIVAALLTRT-FTDHVMLFTQTKKQAHrmhiLLG-----LMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAAR 525
Cdd:PLN00206 355 KLFDILKSKQhFKPPAVVFVSSRLGAD----LLAnaitvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGR 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15422163 526 GLDIEGVKTVINFTMPNTIKHYDHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKA 584
Cdd:PLN00206 431 GVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKS 489
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
225-421 |
2.37e-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: 197.42 E-value: 2.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 225 LSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLErLIYKPRQA----PVTRVLVLVPTRE 300
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQ-KILKAKAEsgeeQGTRALILVPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 301 LGIQVHSVTRQLAQFC-NITTCLAVGG-LDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLD 378
Cdd:cd17961 80 LAQQVSKVLEQLTAYCrKDVRVVNLSAsSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15422163 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPV 421
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
212-578 |
2.93e-58 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 203.90 E-value: 2.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 212 SQYDENL-SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvT 290
Cdd:PTZ00424 21 SNYDEIVdSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNA---C 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 291 RVLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLIL 370
Cdd:PTZ00424 98 QALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI-DKRHLRVDDLKLFIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 371 DEADRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRpNREGDR 450
Cdd:PTZ00424 177 DEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVE-KEEWKF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 451 EAIVAALLTRTFTdHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIE 530
Cdd:PTZ00424 256 DTLCDLYETLTIT-QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15422163 531 GVKTVINFTMPNTIKHYDHRVGRTARAGRAGRSVSLVGEDERKMLKEI 578
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
229-425 |
4.91e-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: 196.27 E-value: 4.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIyKPRQAPVTRVLVLVPTRELGIQVHSV 308
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLG-KPRKKKGLRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 309 TRQLAQFCNITTCLavggLDvKSQEAALRAAP------DILIATPGRLIDHLHNCPSfHLSSIEVLILDEADRMLDEYFE 382
Cdd:cd17957 80 LLKLSKGTGLRIVL----LS-KSLEAKAKDGPksitkyDILVSTPLRLVFLLKQGPI-DLSSVEYLVLDEADKLFEPGFR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15422163 383 EQMKEIIRMCSHHR-QTMLFSATMTDEVKDLASVSLKNPVRIFV 425
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, ... |
229-423 |
6.69e-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: 195.87 E-value: 6.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRV--LVLVPTRELGIQVH 306
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVgaLIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 307 SVTRQLAQFC--NITTCLAVGGLDVKSQEAALRA-APDILIATPGRLIDHL-HNCPSFHLSSIEVLILDEADRMLDEYFE 382
Cdd:cd17960 81 EVLQSFLEHHlpKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLsRKADKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15422163 383 EQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
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 ... |
230-426 |
3.80e-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: 193.73 E-value: 3.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 230 LKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLErLIYKPRQAPV--TRVLVLVPTRELGIQVHS 307
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIE-LLYKLKFKPRngTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 308 VTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 387
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 15422163 388 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPvRIFVN 426
Cdd:cd17942 161 IIKLLPKRRQTMLFSATQTRKVEDLARISLKKK-PLYVG 198
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
242-412 |
7.47e-57 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 191.69 E-value: 7.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 242 TPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPrqaPVTRVLVLVPTRELGIQVHSVTRQLAQFCNITTC 321
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD---NGPQALVLAPTRELAEQIYEELKKLGKGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 322 LAVGGLDVKSQEAALRAaPDILIATPGRLIDHLHNcpSFHLSSIEVLILDEADRMLDEYFEEQMKEIIRMCSHHRQTMLF 401
Cdd:pfam00270 78 SLLGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQE--RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
|
170
....*....|.
gi 15422163 402 SATMTDEVKDL 412
Cdd:pfam00270 155 SATLPRNLEDL 165
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
225-418 |
9.98e-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: 190.49 E-value: 9.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 225 LSRPLLKAITAMGFKQPTPIQKACIPVGL-LGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRV--LVLVPTREL 301
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVsaLIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 302 GIQVHSVTRQLAQFC-NITTCLAVGGLDVKSQEAAL-RAAPDILIATPGRLIDHLHNCPSF-HLSSIEVLILDEADRMLD 378
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVAkAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15422163 379 EYFEEQMKEIIR----MCSHHRQTMLFSATMTDEVKDLASVSLK 418
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 ... |
229-423 |
8.89e-55 |
|
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: 188.30 E-value: 8.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTR-----VLVLVPTRELGI 303
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKddgpyALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 304 QVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcpsfH---LSSIEVLILDEADRMLDEY 380
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLER----RllvLNQCTYVVLDEADRMIDMG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15422163 381 FEEQMKEII--------------------RMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17945 157 FEPQVTKILdampvsnkkpdteeaeklaaSGKHRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
222-424 |
1.90e-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: 178.29 E-value: 1.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 222 DMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLiykPRQAPVTRVLVLVPTREL 301
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI---DTTVRETQALVLAPTREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 302 GIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYF 381
Cdd:cd17939 78 AQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15422163 382 EEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 424
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 ... |
218-418 |
5.72e-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: 179.39 E-value: 5.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 218 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLI--------YKPRQAPv 289
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkegltassFSEVQEP- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 290 tRVLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLI 369
Cdd:cd18052 122 -QALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFI-GRGKISLSKLKYLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15422163 370 LDEADRMLDEYFEEQMKEIIRMCS----HHRQTMLFSATMTDEVKDLASVSLK 418
Cdd:cd18052 200 LDEADRMLDMGFGPEIRKLVSEPGmpskEDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
229-425 |
7.01e-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: 177.82 E-value: 7.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIP---------VGLLGKDICACAATGTGKTAAFALPVLERLiyKPRQAPVTRVLVLVPTR 299
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPwllpsskstPPYRPGDLCVSAPTGSGKTLAYVLPIVQAL--SKRVVPRLRALIVVPTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 300 ELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAA--------PDILIATPGRLIDHLHNCPSFHLSSIEVLILD 371
Cdd:cd17956 79 ELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGFTLKHLRFLVID 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15422163 372 EADRMLDEYFEE------------------QMKEIIRMCSHHR--QTMLFSATMTDEVKDLASVSLKNPvRIFV 425
Cdd:cd17956 159 EADRLLNQSFQDwletvmkalgrptapdlgSFGDANLLERSVRplQKLLFSATLTRDPEKLSSLKLHRP-RLFT 231
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
229-423 |
3.77e-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: 3.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPV--TRVLVLVPTRELGIQVH 306
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGdgPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 307 SVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDhLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMK 386
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLID-FLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 15422163 387 EIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
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 ... |
220-423 |
5.92e-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: 171.33 E-value: 5.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKprqAPVTRVLVLVPTR 299
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPK---KDVIQALILVPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 300 ELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDhLHNCPSFHLSSIEVLILDEADRMLDE 379
Cdd:cd17940 78 ELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15422163 380 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
229-423 |
8.69e-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: 170.67 E-value: 8.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLI----YKPRQAPVtrVLVLVPTRELGIQ 304
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMdqreLEKGEGPI--AVIVAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 305 VHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFEEQ 384
Cdd:cd17952 79 IYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKK-KATNLQRVTYLVLDEADRMFDMGFEYQ 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 15422163 385 MKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17952 158 VRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
233-423 |
5.01e-48 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 168.82 E-value: 5.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 233 ITAMGFKQPTPIQKACIPVGLLG-KDICACAATGTGKTAAFALPVLERLIYKPRqapvTRVLVLVPTRELGIQVHSVTRQ 311
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKG----GRVLVLVPTRELAEQWAEELKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 312 LAQFCNITTCLAVGGLDVKSQEAAL-RAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFEEQMKEIIR 390
Cdd:smart00487 77 LGPSLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
|
170 180 190
....*....|....*....|....*....|...
gi 15422163 391 MCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI 188
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
435-567 |
1.34e-47 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 164.99 E-value: 1.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 435 LRQEFIRIRPnrEGDREAIVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQI 514
Cdd:cd18787 1 IKQLYVVVEE--EEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15422163 515 DILVATDVAARGLDIEGVKTVINFTMPNTIKHYDHRVGRTARAGRAGRSVSLV 567
Cdd:cd18787 79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
229-406 |
3.06e-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: 165.10 E-value: 3.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLL-GKDICACAATGTGKTAAFALPVLERLIYKPRQAPVT------RVLVLVPTREL 301
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGgkqkplRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 302 GIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSF--HLSSIEVLILDEADRMLDE 379
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 15422163 380 -YFEEqMKEIIRM-------CSHHRQTMLFSATMT 406
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 ... |
220-423 |
6.65e-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: 159.92 E-value: 6.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYkprQAPVTRVLVLVPTR 299
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDT---SLKATQALVLAPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 300 ELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILDEADRMLDE 379
Cdd:cd18046 78 ELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15422163 380 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd18046 157 GFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
229-423 |
1.36e-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: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVL-------ERLIYKPRQAPVTrvLVLVPTREL 301
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqeKKLPFIKGEGPYG--LIVCPSREL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 302 GIQVHSVTRQLAQFCN------ITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILDEADR 375
Cdd:cd17951 79 ARQTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEADR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15422163 376 MLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17951 158 MIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
229-423 |
2.32e-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: 155.40 E-value: 2.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRqAPVTrvLVLVPTRELGIQVHSV 308
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHR-NPSA--LILTPTRELAVQIEDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 309 TRQLAQ-FCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLhNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 387
Cdd:cd17962 78 AKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL-KQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 15422163 388 IIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17962 157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
225-423 |
3.07e-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: 3.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 225 LSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALP----VLERLIYKPRQAPVTrvLVLVPTRE 300
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPmfrhIKDQRPVKPGEGPIG--LIMAPTRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 301 LGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHL--HNCPSFHLSSIEVLILDEADRMLD 378
Cdd:cd17953 97 LALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVTNLRRVTYVVLDEADRMFD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15422163 379 EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17953 177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
229-404 |
4.95e-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: 4.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPTRELGIQVHSV 308
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRH---PQVLILAPTREIAVQIHDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 309 TRQLAQFC-NITTCLAVGGLDVKSQEAALRaAPDILIATPGRlIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKE 387
Cdd:cd17943 78 FKKIGKKLeGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGR-IKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170
....*....|....*..
gi 15422163 388 IIRMCSHHRQTMLFSAT 404
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 ... |
229-424 |
1.26e-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: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP---RQAPVTRVLVLVPTRELGIQV 305
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPiprEQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 306 HSVTRQLAqFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDhLHNCPSFHLSSIEVLILDEADRMLDEYFEEQM 385
Cdd:cd17958 81 EAECSKYS-YKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 15422163 386 KEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIF 424
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
225-423 |
2.86e-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: 2.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 225 LSRPLLKAITAMGFKQPTPIQKACIPVgLLG---KDICACAATGTGKTAAFALPVLERLiyKPRQaPVTRVLVLVPTREL 301
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPL-ILSdppENLIAQSQSGTGKTAAFVLAMLSRV--DPTL-KSPQALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 302 GIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEaalRAAPDILIATPGRLIDHL-HNCpsFHLSSIEVLILDEADRMLD-E 379
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVALAVPGNDVPRGK---KITAQIVIGTPGTVLDWLkKRQ--LDLKKIKILVLDEADVMLDtQ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15422163 380 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd17963 152 GHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
219-419 |
5.21e-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: 5.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLI----YKPRQAPVTR--- 291
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYeqgpGESLPSESGYygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 292 ------VLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSI 365
Cdd:cd18051 102 rkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLER-GKIGLDYC 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15422163 366 EVLILDEADRMLDEYFEEQMKEIIRMC----SHHRQTMLFSATMTDEVKDLASVSLKN 419
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 ... |
219-425 |
2.48e-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: 147.49 E-value: 2.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPT 298
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQ---VSVLVICHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 299 RELGIQVHSVTRQLAQFC-NITTCLAVGGLDVKSQEAALR-AAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRM 376
Cdd:cd17950 80 RELAFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVRE-KKLKLSHVKHFVLDECDKM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15422163 377 LDEY-FEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFV 425
Cdd:cd17950 159 LEQLdMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
218-427 |
3.18e-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: 3.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 218 LSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVtrVL 293
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflerGDGPI--CL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 294 VLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHnCPSFHLSSIEVLILDEA 373
Cdd:cd18049 102 VLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLE-AGKTNLRRCTYLVLDEA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15422163 374 DRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNS 427
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 ... |
220-421 |
8.36e-37 |
|
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: 137.07 E-value: 8.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLErliykprqapVTRVLVLVPTR 299
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ----------IVVALILEPSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 300 ELGIQVHSVTRQLAQFCN---ITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRM 376
Cdd:cd17938 71 ELAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKT-GKLDLSSVRFFVLDEADRL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15422163 377 LDEYFEEQMKEIIRMCSHHR------QTMLFSATM-TDEVKDLASVSLKNPV 421
Cdd:cd17938 150 LSQGNLETINRIYNRIPKITsdgkrlQVIVCSATLhSFEVKKLADKIMHFPT 201
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
220-423 |
3.43e-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: 132.59 E-value: 3.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 220 FQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQapvTRVLVLVPTR 299
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRE---TQALILSPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 300 ELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDE 379
Cdd:cd18045 78 ELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEMLNK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15422163 380 YFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
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 ... |
219-423 |
3.83e-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: 3.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPR----QAPVtrVLV 294
Cdd:cd18050 63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYlergDGPI--CLV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 295 LVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSfHLSSIEVLILDEAD 374
Cdd:cd18050 141 LAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEAD 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15422163 375 RMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRI 423
Cdd:cd18050 220 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
229-414 |
1.54e-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: 123.25 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKP----RQAPVTRVLVLVPTRELGIQ 304
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKllaeGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 305 VHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGrLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQ 384
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPG-ALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15422163 385 MKEIIRMCSHHR-------------QTMLFSATMTDEVKDLAS 414
Cdd:cd17948 160 LSHFLRRFPLASrrsentdgldpgtQLVLVSATMPSGVGEVLS 202
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
230-418 |
5.47e-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: 117.64 E-value: 5.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 230 LKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERL---IYKPRQAPVTRVLVLVPTRELGIQV- 305
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLqedQQPRKRGRAPKVLVLAPTRELANQVt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 306 ---HSVTRQLAQFCnittclAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEYFE 382
Cdd:cd17944 82 kdfKDITRKLSVAC------FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQN-GRLDLTKLKHVVLDEVDQMLDMGFA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15422163 383 EQMKEIIRMC-----SHHRQTMLFSATMTDEVKDLASVSLK 418
Cdd:cd17944 155 EQVEEILSVSykkdsEDNPQTLLFSATCPDWVYNVAKKYMK 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
449-558 |
6.43e-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: 114.23 E-value: 6.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 449 DREAIVAALLTRTFTDHVMLFTQTKKQAHrMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLD 528
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 15422163 529 IEGVKTVINFTMPNTIKHYDHRVGRTARAG 558
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
219-420 |
5.60e-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: 107.03 E-value: 5.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLG--KDICACAATGTGKTAAFALPVLERLIYKpRQAPvtRVLVLV 296
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAL-KLYP--QCLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 297 PTRELGIQVHSVTRQLAQFCN-ITTCLAVGGldvKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADR 375
Cdd:cd18048 96 PTFELALQTGKVVEEMGKFCVgIQVIYAIRG---NRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVTNISVFVLDEADV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15422163 376 MLD-EYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNP 420
Cdd:cd18048 173 MINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
478-558 |
3.27e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 96.90 E-value: 3.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 478 RMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYDHRVGRTARA 557
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
|
.
gi 15422163 558 G 558
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 ... |
219-420 |
2.75e-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: 92.86 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 219 SFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLG--KDICACAATGTGKTAAFALPVLERLiykPRQAPVTRVLVLV 296
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---EPANKYPQCLCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 297 PTRELGIQVHSVTRQLAQFC-NITTCLAVGGldvKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADR 375
Cdd:cd18047 79 PTYELALQTGKVIEQMGKFYpELKLAYAVRG---NKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15422163 376 ML-DEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNP 420
Cdd:cd18047 156 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
255-713 |
2.26e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 92.78 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 255 GKDICACAATGTGKTAAFALpVLERLIYKPRqapvtrVLVLVPTRELGIQVHsvtrqlAQFCNITTCLAVGGLDVKSQEa 334
Cdd:COG1061 100 GGRGLVVAPTGTGKTVLALA-LAAELLRGKR------VLVLVPRRELLEQWA------EELRRFLGDPLAGGGKKDSDA- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 335 alraapDILIATPGRLIDHLHNcpSFHLSSIEVLILDEADRMLDEYFEEqmkeIIRMCSHHRqTMLFSAT--MTDEvKDL 412
Cdd:COG1061 166 ------PITVATYQSLARRAHL--DELGDRFGLVIIDEAHHAGAPSYRR----ILEAFPAAY-RLGLTATpfRSDG-REI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 413 ASVSLKN-----------------PVRIFV------NSNTDVAPFLRQEFIRIRPNREGDREAIVAALLTRTFTDHVMLF 469
Cdd:COG1061 232 LLFLFDGivyeyslkeaiedgylaPPEYYGirvdltDERAEYDALSERLREALAADAERKDKILRELLREHPDDRKTLVF 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 470 TQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYDH 549
Cdd:COG1061 312 CSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 550 RVGRTARAGRAGRSVS---LVGEDeRKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKMEKDVYAVLQLEAEEKEMQQS 626
Cdd:COG1061 392 RLGRGLRPAPGKEDALvydFVGND-VPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELE 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 627 EAQINTAKRLLEkGKEAVVQEPERSWFQTKEERKKEKIAKALQEFDLALRGKKKRKKFMKDAKKKGEMTAEERSQFEILK 706
Cdd:COG1061 471 LLEDALLLVLAE-LLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLE 549
|
....*..
gi 15422163 707 AQMFAER 713
Cdd:COG1061 550 ELAALLL 556
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
255-404 |
1.47e-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: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 255 GKDICACAATGTGKTAAFALPVLERLIYKPRQapvtrVLVLVPTRELGIQVHSVTRQLAQFcNITTCLAVGGLDVKSQEA 334
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGKK-----VLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREK 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15422163 335 ALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMkEIIRMCSHHR---QTMLFSAT 404
Cdd:cd00046 75 NKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALI-LDLAVRKAGLknaQVILLSAT 146
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
240-408 |
2.14e-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: 76.65 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 240 QPTPIQKACIPVgLLGK----------------DICACAA-TGTGKTAAFALPVLERL-------------IYKPRQAPV 289
Cdd:cd17965 30 KPSPIQTLAIKK-LLKTlmrkvtkqtsneepklEVFLLAAeTGSGKTLAYLAPLLDYLkrqeqepfeeaeeEYESAKDTG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 290 T-RVLVLVPTRELGIQVHSVTRQLAQFC--NITTCLAVGGLDVKSQEAALRAAPDILIATPGrLIDHLHNCPSFHLSSIE 366
Cdd:cd17965 109 RpRSVILVPTHELVEQVYSVLKKLSHTVklGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPG-KLASLAKSRPKILSRVT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15422163 367 VLILDEADRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDE 408
Cdd:cd17965 188 HLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKE 229
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
224-563 |
3.49e-15 |
|
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: 79.88 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 224 NLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRqapvTRVLVLVPTRELGI 303
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPG----ATALYLYPTKALAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 304 -QVHSVtRQLAQFCNITTCLAV--GglDVKSQE-AALRAAPDILIATPgrliD--HLHNCPSFH-----LSSIEVLILDE 372
Cdd:COG1205 116 dQLRRL-RELAEALGLGVRVATydG--DTPPEErRWIREHPDIVLTNP----DmlHYGLLPHHTrwarfFRNLRYVVIDE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 373 A---------------DRMLdeyfeeqmkeiiRMCSHHRQTMLF---SATMtDEVKDLASVSLKNPVRIfVNSNTdvAPF 434
Cdd:COG1205 189 AhtyrgvfgshvanvlRRLR------------RICRHYGSDPQFilaSATI-GNPAEHAERLTGRPVTV-VDEDG--SPR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 435 LRQEFIRIRP---NREGDREAIV-AALLTRTFTDH---VMLFTQTKKQAHRMHILL------GLMGLQVGELHGNLSQTQ 501
Cdd:COG1205 253 GERTFVLWNPplvDDGIRRSALAeAARLLADLVREglrTLVFTRSRRGAELLARYArralrePDLADRVAAYRAGYLPEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15422163 502 RLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIkhydhrvgrtA----RAGRAGRS 563
Cdd:COG1205 333 RREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTR----------AsfwqQAGRAGRR 388
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
497-578 |
5.21e-12 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 69.37 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 497 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF-TMPNTIKhYDHRVGRTARaGRAGRSVSLVGED----- 570
Cdd:COG1111 395 LTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYePVPSEIR-SIQRKGRTGR-KREGRVVVLIAKGtrdea 472
|
90
....*....|....*.
gi 15422163 571 --------ERKMLKEI 578
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 ... |
255-373 |
1.12e-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: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 255 GKDICACAATGTGKTAAFALPVLERLIYKPRqapvTRVLVLVPTRELGI-QVHSVTRQLAQFCNITTCLAVGG-LDVKSQ 332
Cdd:cd17923 15 GRSVVVTTGTASGKSLCYQLPILEALLRDPG----SRALYLYPTKALAQdQLRSLRELLEQLGLGIRVATYDGdTPREER 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15422163 333 EAALRAAPDILIATPGRL---IDHLHNCPSFHLSSIEVLILDEA 373
Cdd:cd17923 91 RAIIRNPPRILLTNPDMLhyaLLPHHDRWARFLRNLRYVVLDEA 134
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
497-645 |
7.55e-10 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 62.58 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 497 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFT-MPNTIKHYdHRVGRTARaGRAGRSVSLVGED----- 570
Cdd:PRK13766 407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRSI-QRKGRTGR-QEEGRVVVLIAKGtrdea 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 571 --------ERKMlKEIVKAAKAPVKARILPQDVILKFRDKIEKMEKDVYAVLQL-EAEEKEMQQSEAQINTAKRLLEKGK 641
Cdd:PRK13766 485 yywssrrkEKKM-KEELKNLKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSkGKEEEEEEEKEEKDKETEEDEPEGP 563
|
....
gi 15422163 642 EAVV 645
Cdd:PRK13766 564 KIIV 567
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
253-380 |
1.92e-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: 58.21 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 253 LLGKDICACAATGTGKTAAfALPVLERLIYKPRQAPVTRVLVLVPTrelgiqVHSVTRQLAQFCNITTCLA--VGGL--D 328
Cdd:cd17927 15 LKGKNTIICLPTGSGKTFV-AVLICEHHLKKFPAGRKGKVVFLANK------VPLVEQQKEVFRKHFERPGykVTGLsgD 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15422163 329 VKSQEAALRAAP--DILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEY 380
Cdd:cd17927 88 TSENVSVEQIVEssDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHNTTKNH 141
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
238-564 |
1.30e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 58.58 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 238 FKQPTPIQKACIPVGLLGKDICACAATGTGKT-AAFaLPVLERLIYKPRQAPV---TRVLVLVPTRELGIQVHsvtRQLA 313
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELpdgLRVLYISPLKALANDIE---RNLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 314 QFCNITTCLAVGGL----------DVKSQE--AALRAAPDILIATPgrliDHLH---NCPSF--HLSSIEVLILDE---- 372
Cdd:COG1201 98 APLEEIGEAAGLPLpeirvgvrtgDTPASErqRQRRRPPHILITTP----ESLAlllTSPDAreLLRGVRTVIVDEihal 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 373 ------ADRMLD-EYFEeqmkeiiRMCSHHRQTMLFSATMT--DEVKD-LASVSLKNPVRIfVNSNTDVAPFLR-----Q 437
Cdd:COG1201 174 agskrgVHLALSlERLR-------ALAPRPLQRIGLSATVGplEEVARfLVGYEDPRPVTI-VDAGAGKKPDLEvlvpvE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 438 EFIRIRPNREGDREAIVAALLT-----RTftdhVMLFTQTKKQA----HRMHILLGLMGLQVGELHGNLSQTQRLEALRR 508
Cdd:COG1201 246 DLIERFPWAGHLWPHLYPRVLDlieahRT----TLVFTNTRSQAerlfQRLNELNPEDALPIAAHHGSLSREQRLEVEEA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 509 FKDEQIDILVAT---DVaarGLDIEGVKTVINFTMPntikhydHRVGRTA-RAGRAGRSV 564
Cdd:COG1201 322 LKAGELRAVVATsslEL---GIDIGDVDLVIQVGSP-------KSVARLLqRIGRAGHRV 371
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
512-558 |
2.14e-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: 51.55 E-value: 2.14e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15422163 512 EQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYDHRVGRTARAG 558
Cdd:cd18785 21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
395-562 |
2.08e-07 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 54.38 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 395 HRQTMLFSATMTDEVKD--LASVSLKNPvRIFVnsntdvAPFLRQE-FIRIRPNREGDREAIVAALLTRTFTDHVMLFTQ 471
Cdd:COG0514 166 NVPVLALTATATPRVRAdiAEQLGLEDP-RVFV------GSFDRPNlRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 472 TKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATdVA-ARGLDIEGVKTVINFTMPNTIKHYdhr 550
Cdd:COG0514 239 SRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYyq- 316
|
170
....*....|..
gi 15422163 551 vgrtarAGRAGR 562
Cdd:COG0514 317 -----eIGRAGR 323
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
261-404 |
2.74e-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: 50.77 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 261 CAATGTGKTA-AFALPVLerliykprqAPVTRVLVLVPTRELgiqVHSVTRQLAQFCNITTCLAVGGLDVKSQEAAlraa 339
Cdd:cd17926 24 VLPTGSGKTLtALALIAY---------LKELRTLIVVPTDAL---LDQWKERFEDFLGDSSIGLIGGGKKKDFDDA---- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15422163 340 pDILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRmldeYFEEQMKEIIRMCSHHRQtMLFSAT 404
Cdd:cd17926 88 -NVVVATYQSLSNLAEE-EKDLFDQFGLLIVDEAHH----LPAKTFSEILKELNAKYR-LGLTAT 145
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
229-373 |
3.86e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 53.36 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 229 LLKAITAMGFKQPTPIQKACIPVGLL-GKDICACAATGTGKTAafalpVLERLIYK--PRQApvtRVLVLVPTRELGIQV 305
Cdd:COG1204 11 VIEFLKERGIEELYPPQAEALEAGLLeGKNLVVSAPTASGKTL-----IAELAILKalLNGG---KALYIVPLRALASEK 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15422163 306 HS-VTRQLAQFcNITTCLAVGGLDVKSQEAAlraAPDILIATPGRLIDHLHNCPSFhLSSIEVLILDEA 373
Cdd:COG1204 83 YReFKRDFEEL-GIKVGVSTGDYDSDDEWLG---RYDILVATPEKLDSLLRNGPSW-LRDVDLVVVDEA 146
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
497-557 |
4.10e-07 |
|
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: 49.90 E-value: 4.10e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15422163 497 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYDHRVGRtARA 557
Cdd:cd18802 74 MTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
497-566 |
5.23e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 49.66 E-value: 5.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15422163 497 LSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINF-TMPNTIKHYdHRVGRTARaGRAGRSVSL 566
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYdASPSPIRMI-QRMGRTGR-KRQGRVVVL 142
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
469-562 |
9.35e-07 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 48.74 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 469 FTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYD 548
Cdd:cd18794 36 YCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYY 115
|
90
....*....|....
gi 15422163 549 HRVGrtaRAGRAGR 562
Cdd:cd18794 116 QESG---RAGRDGL 126
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
466-541 |
1.03e-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: 1.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15422163 466 VMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQ--IDILVATDVAARGLDIEGVKTVINFTMP 541
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPW 107
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
256-373 |
1.47e-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: 49.57 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 256 KDICACAATGTGKTaAFALPVLERLIYKPRQ--APVTRVLVLVPTRELGIQVHSVTRQLaqfcnitTCLAVG---GLDVK 330
Cdd:cd18034 17 RNTIVVLPTGSGKT-LIAVMLIKEMGELNRKekNPKKRAVFLVPTVPLVAQQAEAIRSH-------TDLKVGeysGEMGV 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15422163 331 SQEAALR-----AAPDILIATPGRLIDHLHNCpSFHLSSIEVLILDEA 373
Cdd:cd18034 89 DKWTKERwkeelEKYDVLVMTAQILLDALRHG-FLSLSDINLLIFDEC 135
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
468-566 |
5.89e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 46.87 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 468 LFTQTKKQAHRMHILLG------LMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMP 541
Cdd:cd18796 43 VFTNTRSQAERLAQRLRelcpdrVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
|
90 100
....*....|....*....|....*
gi 15422163 542 NTIKHYDHRVGrtaRAGRAGRSVSL 566
Cdd:cd18796 123 KSVARLLQRLG---RSGHRPGAASK 144
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
242-414 |
6.73e-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: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 242 TPIQKACIPVGLL-GKDICACAATGTGKTAAFALPVLERLIYKPRqapvtRVLVLVPTRELGIQVHSVTRQLAQFCNITT 320
Cdd:cd17921 3 NPIQREALRALYLsGDSVLVSAPTSSGKTLIAELAILRALATSGG-----KAVYIAPTRALVNQKEADLRERFGPLGKNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 321 CLAVGGLDVKSQEAAlraAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDE----YFEEQMKEIIRMCSHHR 396
Cdd:cd17921 78 GLLTGDPSVNKLLLA---EADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIGDGergvVLELLLSRLLRINKNAR 154
|
170
....*....|....*...
gi 15422163 397 qtMLFSATMTDEVKDLAS 414
Cdd:cd17921 155 --FVGLSATLPNAEDLAE 170
|
|
| UTP25 |
pfam06862 |
Utp25, U3 small nucleolar RNA-associated SSU processome protein 25; UTP25 is a family of ... |
341-442 |
8.61e-06 |
|
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: 49.18 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 341 DILIATP-G-RLI----DHLHNCPSFhLSSIEVLILDEADRMLD---EYFEEQMKEI--------------IRM------ 391
Cdd:pfam06862 161 DIIIASPlGlRMIigneDKKKRDFDF-LSSIEVLIVDQADSIEMqnwEHVLTVFKHLnlipkeshgcdfsrVRMwyldgq 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15422163 392 CSHHRQTMLFSATMTDEVKDLASVSLKN---PVRIFVNSNT----DVAPFLRQEFIRI 442
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 ... |
235-427 |
2.16e-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: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 235 AMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERliykprqAPVTrvLVLVPTRELGI-QVHSVTRQLA 313
Cdd:cd17920 7 VFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLL-------DGVT--LVVSPLISLMQdQVDRLQQLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 314 QFCNITtclavGGLDVKSQEAALRAAP----DILIATPGRL-----IDHLHNCPSFHLssIEVLILDEA--------Drm 376
Cdd:cd17920 78 RAAALN-----STLSPEEKREVLLRIKngqyKLLYVTPERLlspdfLELLQRLPERKR--LALIVVDEAhcvsqwghD-- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15422163 377 ldeyFEEQMKEI--IRMCSHHRQTMLFSATMTDEVKDLASVSLK-NPVRIFVNS 427
Cdd:cd17920 149 ----FRPDYLRLgrLRRALPGVPILALTATATPEVREDILKRLGlRNPVIFRAS 198
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
234-377 |
2.39e-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: 45.78 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 234 TAMGFKqPTPIQKACIPVGLLGKDICACAATGTGKT---AAFALpvlerLIYKPRQapvtRVLVLVPTRELGIQVHSVTR 310
Cdd:cd17924 12 KKTGFP-PWGAQRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSL-----YLASKGK----RSYLIFPTKSLVKQAYERLS 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15422163 311 QLAQFCNITTCLAV--GGLDVKSQEAALRAAP----DILIATPGRLIDHLHNCPSFHLSSIevlILDEADRML 377
Cdd:cd17924 82 KYAEKAGVEVKILVyhSRLKKKEKEELLEKIEkgdfDILVTTNQFLSKNFDLLSNKKFDFV---FVDDVDAVL 151
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
262-553 |
3.06e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 48.00 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 262 AATGTGKTAAFALPVLERLIYK-------PRQAPVTRVLVLVPTRELG--------IQVHSVT----RQLAQFCNITTCL 322
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFREggedtreAHKRKTSRILYISPIKALGtdvqrnlqIPLKGIAderrRRGETEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 323 AVGglDVKSQEAA--LRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDE----ADRMLDEYFEEQMKEIIRMCSHHR 396
Cdd:PRK09751 83 RTG--DTPAQERSklTRNPPDILITTPESLYLMLTSRARETLRGVETVIIDEvhavAGSKRGAHLALSLERLDALLHTSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 397 QTMLFSATMTdEVKDLAS-------VSLKNP-------VRIF--VNSNTDVAPFLRQEFIRIRPNREGD-----REAIVA 455
Cdd:PRK09751 161 QRIGLSATVR-SASDVAAflggdrpVTVVNPpamrhpqIRIVvpVANMDDVSSVASGTGEDSHAGREGSiwpyiETGILD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 456 ALLTRTFTdhvMLFTQTKKQAHRMHILL---------------------------------GLMGLQVGELHGNLSQTQR 502
Cdd:PRK09751 240 EVLRHRST---IVFTNSRGLAEKLTARLnelyaarlqrspsiavdaahfestsgatsnrvqSSDVFIARSHHGSVSKEQR 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15422163 503 LEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYDHRVGR 553
Cdd:PRK09751 317 AITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGR 367
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
253-372 |
1.41e-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: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 253 LLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRVLVLVPtrelgiQVHSVTRQLAQFCNIttCLAV-------G 325
Cdd:cd18036 15 LRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVN------KVPLVEQQLEKFFKY--FRKGykvtglsG 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15422163 326 GLDVKSQEAALRAAPDILIATPGRLIDHLHN---CPSFHLSSIEVLILDE 372
Cdd:cd18036 87 DSSHKVSFGQIVKASDVIICTPQILINNLLSgreEERVYLSDFSLLIFDE 136
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
262-529 |
1.43e-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: 45.07 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 262 AATGTGKT---AAFAL-----PVLERLIYkprqapvtrvlVLvPTRelgiqvhSVTRQLAQ-FCNIT-------TCLAV- 324
Cdd:COG1203 154 APTGGGKTeaaLLFALrlaakHGGRRIIY-----------AL-PFT-------SIINQTYDrLRDLFgedvllhHSLADl 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 325 ------GGLDVKSQEAALRA----APdILIATpgrlIDHL---------HNCPSFH--LSSieVLILDEADrMLDEYFEE 383
Cdd:COG1203 215 dlleeeEEYESEARWLKLLKelwdAP-VVVTT----IDQLfeslfsnrkGQERRLHnlANS--VIILDEVQ-AYPPYMLA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 384 QMKEIIRMCSHHRQTMLF-SATMTDEVKDLasvsLKNPVRIfVNSNTDVAPFLRQEFIRIRPN-REG--DREAIVAALLT 459
Cdd:COG1203 287 LLLRLLEWLKNLGGSVILmTATLPPLLREE----LLEAYEL-IPDEPEELPEYFRAFVRKRVElKEGplSDEELAELILE 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15422163 460 RTFTDH-VMLFTQTKKQAHRMHILL--GLMGLQVGELHGNLSQTQRLE----ALRRFKDEQIDILVATDVAARGLDI 529
Cdd:COG1203 362 ALHKGKsVLVIVNTVKDAQELYEALkeKLPDEEVYLLHSRFCPADRSEiekeIKERLERGKPCILVSTQVVEAGVDI 438
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
255-347 |
4.07e-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: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 255 GKDICACAATGTGKTAAFALPVLERLiYKPRQAPVtRVLVLVPTRELGIQVHsvtRQLAQFCN-ITTCLAVG---GlDVK 330
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSL-ADEPEKGV-QVLYISPLKALINDQE---RRLEEPLDeIDLEIPVAvrhG-DTS 74
|
90
....*....|....*....
gi 15422163 331 SQE--AALRAAPDILIATP 347
Cdd:cd17922 75 QSEkaKQLKNPPGILITTP 93
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
487-532 |
8.03e-04 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 43.11 E-value: 8.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15422163 487 GLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVaargldIE-GV 532
Cdd:COG1200 503 GLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV------IEvGV 543
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
256-404 |
2.57e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 39.19 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 256 KDICACAATGTGKTA-AFALPvlERLIykpRQAPVTRVLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEA 334
Cdd:pfam04851 24 KRGLIVMATGSGKTLtAAKLI--ARLF---KKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDESVDD 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15422163 335 AlraapDILIATPGRLIDHLHNCP-SFHLSSIEVLILDEADRmldeYFEEQMKEIIRMCSHhrQTML-FSAT 404
Cdd:pfam04851 99 N-----KIVVTTIQSLYKALELASlELLPDFFDVIIIDEAHR----SGASSYRNILEYFKP--AFLLgLTAT 159
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
493-562 |
2.66e-03 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350178 [Multi-domain] Cd Length: 171 Bit Score: 39.44 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 493 LHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNtIKHYDHRVGRTA-------------RAGR 559
Cdd:cd18791 80 LHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVK-EKVYDPRTGLSSlvtvwiskasaeqRAGR 158
|
...
gi 15422163 560 AGR 562
Cdd:cd18791 159 AGR 161
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
488-529 |
3.20e-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: 3.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 15422163 488 LQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDI 529
Cdd:cd18811 62 LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDV 103
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
487-561 |
3.28e-03 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 40.85 E-value: 3.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15422163 487 GLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYDHrvgRTARAGRAG 561
Cdd:PRK11057 260 GISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQ---ETGRAGRDG 331
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
494-567 |
3.72e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 41.03 E-value: 3.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15422163 494 HGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYDHRVGrtaRAGRAGRSVSLV 567
Cdd:PLN03137 711 HGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECG---RAGRDGQRSSCV 781
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
258-383 |
4.15e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 258 ICACAATGTGKTAafalpVLERLIYKPRQAPVTRVLVLVPtrelgiqvHSVTRQ--LAQFCNITTCLAVGGLDVKsqeaA 335
Cdd:pfam13401 8 LVLTGESGTGKTT-----LLRRLLEQLPEVRDSVVFVDLP--------SGTSPKdlLRALLRALGLPLSGRLSKE----E 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15422163 336 LRAapdiliatpgRLIDHLHncpsfHLSSIEVLILDEADRMLDEYFEE 383
Cdd:pfam13401 71 LLA----------ALQQLLL-----ALAVAVVLIIDEAQHLSLEALEE 103
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
487-532 |
4.62e-03 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 40.52 E-value: 4.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15422163 487 GLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVaargldIE-GV 532
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 ... |
262-382 |
4.99e-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: 38.70 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 262 AATGTGKT--AAFalpvlerLIYK-PRQAPVTRVLVLVPTRELGIQVHSvtrqlaQFCNITTCLAVGGLDVKSQEAALRa 338
Cdd:cd18032 27 MATGTGKTytAAF-------LIKRlLEANRKKRILFLAHREELLEQAER------SFKEVLPDGSFGNLKGGKKKPDDA- 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15422163 339 apDILIATPGRL--IDHLHNCPSFHLSSIevlILDEADR-------MLDEYFE 382
Cdd:cd18032 93 --RVVFATVQTLnkRKRLEKFPPDYFDLI---IIDEAHHaiassyrKILEYFE 140
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
466-558 |
5.42e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 40.21 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 466 VMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQ--IDILVATDVAARGLDIEGVKTVINFTMPNT 543
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLWWN 631
|
90
....*....|....*
gi 15422163 544 IKHYDHRVGRTARAG 558
Cdd:COG0553 632 PAVEEQAIDRAHRIG 646
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
451-559 |
8.41e-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: 37.61 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 451 EAIVAALLTRTF-TDHVMLFTQTKKQAHRMHILLGLMGLqvgelHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDI 529
Cdd:cd18789 36 LRALEELLKRHEqGDKIIVFTDNVEALYRYAKRLLKPFI-----TGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDL 110
|
90 100 110
....*....|....*....|....*....|..
gi 15422163 530 --EGVKTVINFTMPNTiKHYDHRVGRTARAGR 559
Cdd:cd18789 111 peANVAIQISGHGGSR-RQEAQRLGRILRPKK 141
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
262-380 |
8.60e-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: 38.26 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15422163 262 AATGTGKTAAFALPVLERLIYKPrqapvTRVLVLVPTRELGIQvHSvtRQLAQFCNIT-TCLAVGGLDVKSQEAALRAAP 340
Cdd:cd18035 23 LPTGLGKTIIAILVAADRLTKKG-----GKVLILAPSRPLVEQ-HA--ENLKRVLNIPdKITSLTGEVKPEERAERWDAS 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15422163 341 DILIATPGRLIDHLHNcPSFHLSSIEVLILDEADRMLDEY 380
Cdd:cd18035 95 KIIVATPQVIENDLLA-GRITLDDVSLLIFDEAHHAVGNY 133
|
|
| |
