|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
8-432 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 597.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 8 TTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGRARArmPRTLILEP 87
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--PQALILAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 88 TRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLD 167
Cdd:COG0513 80 TRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 168 MGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIEVAKPASAAETVTQRFVASHGKDyeKRAVLRELVR 247
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD--KLELLRRLLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 248 AQtELKNAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVFNF 327
Cdd:COG0513 238 DE-DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 328 DVPIHSEDYVHRIGRTGRAGRSGAAFTLVTKRDTKFVDAIEKLIGEKVEWLsgDLTSLPPPAEDSRDSERPRRNGRERGA 407
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEE--ELPGFEPVEEKRLERLKPKIKEKLKGK 394
|
410 420
....*....|....*....|....*
gi 502304280 408 RdgAGRDRAPRENGDKDRGRGRGNR 432
Cdd:COG0513 395 K--AGRGGRPGPKGERKARRGKRRR 417
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
8-387 |
5.84e-124 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 370.67 E-value: 5.84e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 8 TTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGRARarmPRTLILEP 87
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFR---VQALVLCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 88 TRELAAQVAENFEKYGKN-HRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRML 166
Cdd:PRK11776 81 TRELADQVAKEIRRLARFiPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 167 DMGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIEVAKpASAAETVTQRF--VASHGKDyekRAVLRE 244
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES-THDLPAIEQRFyeVSPDERL---PALQRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 245 LVRAQTElkNAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHV 324
Cdd:PRK11776 237 LLHHQPE--SCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAV 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502304280 325 FNFDVPIHSEDYVHRIGRTGRAGRSGAAFTLVTKRDTKFVDAIEKLIGEKVEWlsGDLTSLPP 387
Cdd:PRK11776 315 INYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNW--EPLPSLSP 375
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
8-375 |
3.45e-116 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 350.01 E-value: 3.45e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 8 TTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLS-LLEKGRARARMPRTLILE 86
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQhLLDFPRRKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 87 PTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRML 166
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 167 DMGFIPDIERIAKMIPFTRQTLFFSATMPSE-IQKLADRFLQNPERIEVAKPASAAETVTQRFvaSHGKDYE-KRAVLRE 244
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWY--YRADDLEhKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 245 LVRaQTELKNAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHV 324
Cdd:PRK11192 239 LLK-QPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 502304280 325 FNFDVPIHSEDYVHRIGRTGRAGRSGAAFTLVTKRDTKFVDAIEKLIGEKV 375
Cdd:PRK11192 318 INFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPL 368
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
9-484 |
2.23e-113 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 343.33 E-value: 2.23e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 9 TFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKG--RARARMP-RTLIL 85
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqpHAKGRRPvRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 86 EPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRM 165
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 166 LDMGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIEVAKPASAAETVTQRFvasHGKDYEKRAVLREL 245
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHV---HFVDKKRKRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 246 VRAQTELKNAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVF 325
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 326 NFDVPIHSEDYVHRIGRTGRAGRSGAAFTLVTKRDTKFVDAIEKLIGEKVEWLsgdltSLPPPAEDSRDSERPRRNGRER 405
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRI-----AIPGYEPDPSIKAEPIQNGRQQ 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502304280 406 GARDGAGRDRAPRENGDKDRGRGRGNRAAASHKSDNDIQDNGvdvieaapvkadivknERKAEQKPQNNARNSRPYPAN 484
Cdd:PRK10590 394 RGGGGRGQGGGRGQQQGQPRRGEGGAKSASAKPAEKPSRRLG----------------DAKPAGEQQRRRRPRKPAAAQ 456
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
8-369 |
1.04e-104 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 326.81 E-value: 1.04e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 8 TTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEkgrARARMPRTLILEP 87
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD---PELKAPQILVLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 88 TRELAAQVAENFEKYGKN-HRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRML 166
Cdd:PRK11634 83 TRELAVQVAEAMTDFSKHmRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 167 DMGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIEVAKPASAAETVTQRFVASHGkdYEKRAVLRELV 246
Cdd:PRK11634 163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWG--MRKNEALVRFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 247 RAQtELKNAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVFN 326
Cdd:PRK11634 241 EAE-DFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVN 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 502304280 327 FDVPIHSEDYVHRIGRTGRAGRSGAAFTLVTKRDTKFVDAIEK 369
Cdd:PRK11634 320 YDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIER 362
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
8-408 |
3.10e-103 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 316.14 E-value: 3.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 8 TTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLS-LLEKGRARAR---MPRTL 83
Cdd:PRK04837 8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHyLLSHPAPEDRkvnQPRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 84 ILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEAD 163
Cdd:PRK04837 88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 164 RMLDMGFIPDIERIAKMIPFT--RQTLFFSATMPSEIQKLADRFLQNPERIEVAKPASAAETVTQR-FVAShgkDYEKRA 240
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMPPAnqRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEElFYPS---NEEKMR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 241 VLRELVRAQTELKnAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPD 320
Cdd:PRK04837 245 LLQTLIEEEWPDR-AIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 321 VSHVFNFDVPIHSEDYVHRIGRTGRAGRSGAAFTLVTKRDTKFVDAIEKLIGEKVEWLSGD----LTSLPPPA--EDSRD 394
Cdd:PRK04837 324 VTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSKYDsdalLTDLPKPLrlTRPRT 403
|
410
....*....|....
gi 502304280 395 SERPRRNGRERGAR 408
Cdd:PRK04837 404 GNGPRRSGAPRNRR 417
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
19-213 |
6.63e-103 |
|
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: 307.06 E-value: 6.63e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLS-LLEKGRARARMPRTLILEPTRELAAQVAE 97
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEkLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 98 NFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFIPDIERI 177
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 502304280 178 AKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIE 213
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
8-399 |
6.05e-101 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 312.23 E-value: 6.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 8 TTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLL-----EKGRARARmPRT 82
Cdd:PRK01297 87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtppPKERYMGE-PRA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 83 LILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLE-RGADVLICTPGRLLDHFERGKLLMSGVEILVIDE 161
Cdd:PRK01297 166 LIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 162 ADRMLDMGFIPDIERIAKMIPFT--RQTLFFSATMPSEIQKLADRFLQNPERIEVAKPASAAETVTQRFVASHGKDyeKR 239
Cdd:PRK01297 246 ADRMLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSD--KY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 240 AVLRELVRaQTELKNAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIP 319
Cdd:PRK01297 324 KLLYNLVT-QNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHID 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 320 DVSHVFNFDVPIHSEDYVHRIGRTGRAGRSGAAFTLVTKRDTKFVDAIEKLIGEKvewlsgdLTSLPPPAEDSRDSERPR 399
Cdd:PRK01297 403 GISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRK-------ISCEMPPAELLKPVPRKH 475
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
6-503 |
2.25e-97 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 306.11 E-value: 2.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 6 PLT--TFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGRARARM---- 79
Cdd:PRK04537 5 PLTdlTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRkped 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 80 PRTLILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLL-MSGVEILV 158
Cdd:PRK04537 85 PRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVsLHACEICV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 159 IDEADRMLDMGFIPDIERIAKMIP--FTRQTLFFSATMPSEIQKLADRFLQNPERIEVAKPASAAETVTQR--FVAshgk 234
Cdd:PRK04537 165 LDEADRMFDLGFIKDIRFLLRRMPerGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRiyFPA---- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 235 DYEKRAVLRELVrAQTELKNAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAAR 314
Cdd:PRK04537 241 DEEKQTLLLGLL-SRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 315 GLDIPDVSHVFNFDVPIHSEDYVHRIGRTGRAGRSGAAFTLVTKRDTKFVDAIEKLIGEK--VEWLSGD-LTSLPPP--- 388
Cdd:PRK04537 320 GLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKipVEPVTAElLTPLPRPprv 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 389 ---------------------AEDSRDSERPRRNGRERGARDGAGRDRA---PRENGDKDRGRGRGNRAA-ASHKSDNDI 443
Cdd:PRK04537 400 pvegeeaddeagdsvgtifreAREQRAAEEQRRGGGRSGPGGGSRSGSVgggGRRDGAGADGKPRPRRKPrVEGEADAAA 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502304280 444 QDNGVDVIEA-APVKADIVKNERKAEQKPQNNARNSRPYPANDDSRDRRRHRDHDDGPTPV 503
Cdd:PRK04537 480 AGAETPVVAAaAAQAPGVVAADGERAPRKRRRRRNGRPVEGAEPVSTPVPAPAAPRKPTQV 540
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
6-406 |
2.69e-93 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 294.37 E-value: 2.69e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 6 PLTTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPML------SLLEKGRArarm 79
Cdd:PTZ00110 128 PVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIvhinaqPLLRYGDG---- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 80 PRTLILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVI 159
Cdd:PTZ00110 204 PIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 160 DEADRMLDMGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLA-DRFLQNPERIEVAK-PASAAETVTQR-FVAshgKDY 236
Cdd:PTZ00110 284 DEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLArDLCKEEPVHVNVGSlDLTACHNIKQEvFVV---EEH 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 237 EKRAVLRELV-RAQTELKNAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARG 315
Cdd:PTZ00110 361 EKRGKLKMLLqRIMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRG 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 316 LDIPDVSHVFNFDVPIHSEDYVHRIGRTGRAGRSGAAFTLVTKRDTKFVDAIEKLIGEKVEWLSGDLTSLPPpaEDSRDS 395
Cdd:PTZ00110 441 LDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSN--ERSNGT 518
|
410
....*....|.
gi 502304280 396 ERPRRNGRERG 406
Cdd:PTZ00110 519 ERRRWGGYGRF 529
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
9-385 |
1.46e-78 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 251.67 E-value: 1.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 9 TFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEkgrARARMPRTLILEPT 88
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLID---YDLNACQALILAPT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 89 RELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDM 168
Cdd:PTZ00424 106 RELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 169 GFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIEVAKPASAAETVTQRFVASHGKDYeKRAVLRELVRA 248
Cdd:PTZ00424 186 GFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEW-KFDTLCDLYET 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 249 QTeLKNAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVFNFD 328
Cdd:PTZ00424 265 LT-ITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYD 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 502304280 329 VPIHSEDYVHRIGRTGRAGRSGAAFTLVTKRDTKFVDAIEKLIGEKVEWLSGDLTSL 385
Cdd:PTZ00424 344 LPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADY 400
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
9-208 |
5.41e-77 |
|
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: 241.24 E-value: 5.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 9 TFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLS-LLEKG------RARARMPR 81
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISkLLEDGppsvgrGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 82 TLILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDE 161
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502304280 162 ADRMLDMGFIPDIERIAK---MIPFT-RQTLFFSATMPSEIQKLADRFLQN 208
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEhpdMPPKGeRQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
9-213 |
7.59e-73 |
|
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: 229.90 E-value: 7.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 9 TFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPML-SLLEkgrARARMpRTLILEP 87
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILqALLE---NPQRF-FALVLAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 88 TRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGK-LLMSGVEILVIDEADRML 166
Cdd:cd17954 77 TRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502304280 167 DMGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIE 213
Cdd:cd17954 157 NMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
19-212 |
3.11e-67 |
|
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: 215.20 E-value: 3.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGRARARMPRTLILEPTRELAAQVAEN 98
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 99 FEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGK-LLMSGVEILVIDEADRMLDMGFIPDIERI 177
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 502304280 178 AKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
6-206 |
1.30e-65 |
|
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: 213.29 E-value: 1.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 6 PLTTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGRARA------RM 79
Cdd:cd18052 41 AILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTAssfsevQE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 80 PRTLILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVI 159
Cdd:cd18052 121 PQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLIL 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502304280 160 DEADRMLDMGFIPDIERI-------AKMIpftRQTLFFSATMPSEIQKLADRFL 206
Cdd:cd18052 201 DEADRMLDMGFGPEIRKLvsepgmpSKED---RQTLMFSATFPEEIQRLAAEFL 251
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
19-209 |
1.85e-65 |
|
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: 211.41 E-value: 1.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEK-----GRARARMPRTLILEPTRELAA 93
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppldEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 94 QVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFIPD 173
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502304280 174 IERIAKMIPFT--------------------RQTLFFSATMPSEIQKLADRFLQNP 209
Cdd:cd17945 161 VTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRP 216
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
9-212 |
7.95e-65 |
|
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: 209.08 E-value: 7.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 9 TFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLeKGRARARMPRTLILEPT 88
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL-KAHSPTVGARALILSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 89 RELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDM 168
Cdd:cd17959 81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502304280 169 GFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
32-201 |
1.44e-64 |
|
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: 207.09 E-value: 1.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 32 TPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGRARarmPRTLILEPTRELAAQVAENFEKYGKNHRLNVA 111
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG---PQALVLAPTRELAEQIYEELKKLGKGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 112 LLIGGVSFEDQDRKLeRGADVLICTPGRLLDHFERGKLLmSGVEILVIDEADRMLDMGFIPDIERIAKMIPFTRQTLFFS 191
Cdd:pfam00270 78 SLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKLL-KNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLS 155
|
170
....*....|
gi 502304280 192 ATMPSEIQKL 201
Cdd:pfam00270 156 ATLPRNLEDL 165
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
19-212 |
1.40e-63 |
|
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: 205.68 E-value: 1.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPML------SLLEKGRArarmPRTLILEPTRELA 92
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaqPPLERGDG----PIVLVLAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 93 AQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFIP 172
Cdd:cd17966 77 QQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502304280 173 DIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd17966 157 QIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
6-405 |
2.11e-63 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 215.42 E-value: 2.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 6 PLTTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGR----ARARMPR 81
Cdd:PLN00206 119 PILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRsghpSEQRNPL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 82 TLILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDE 161
Cdd:PLN00206 199 AMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 162 ADRMLDMGFIPDIERIAKMIPfTRQTLFFSATMPSEIQKLADRFLQNPERIEVAKPASAAETVTQRFVASHGKdyEKRAV 241
Cdd:PLN00206 279 VDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETK--QKKQK 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 242 LRELVRAQTELK-NAIVFCNRKKDvADLFRSLER--HGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDI 318
Cdd:PLN00206 356 LFDILKSKQHFKpPAVVFVSSRLG-ADLLANAITvvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 319 PDVSHVFNFDVPIHSEDYVHRIGRTGRAGRSGAAFTLVTKRDtkfvdaiEKLIGEKVEWLSGDLTSLPPPAEDSRDSERP 398
Cdd:PLN00206 435 LRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEED-------RNLFPELVALLKSSGAAIPRELANSRYLGSG 507
|
....*..
gi 502304280 399 RRNGRER 405
Cdd:PLN00206 508 RKRKKKR 514
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
6-208 |
4.03e-63 |
|
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: 206.43 E-value: 4.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 6 PLTTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLL-EKG----------- 73
Cdd:cd18051 19 HIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyEQGpgeslpsesgy 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 74 -RARARMPRTLILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMS 152
Cdd:cd18051 99 yGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 153 GVEILVIDEADRMLDMGFIPDIERIAK---MIPF-TRQTLFFSATMPSEIQKLADRFLQN 208
Cdd:cd18051 179 YCKYLVLDEADRMLDMGFEPQIRRIVEqdtMPPTgERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
20-214 |
9.30e-61 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 198.28 E-value: 9.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 20 LSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLekgrARARMPRT-----LILEPTRELAAQ 94
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL----YRERWTPEdglgaLIISPTRELAMQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 95 VAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERgADVLICTPGRLLDHFERGKLL-MSGVEILVIDEADRMLDMGFIPD 173
Cdd:cd17941 78 IFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETPGFdTSNLQMLVLDEADRILDMGFKET 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502304280 174 IERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIEV 214
Cdd:cd17941 157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
23-227 |
1.30e-60 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 198.10 E-value: 1.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 23 VTDAGYTIPTPIQAGAIPFALER-RDICGIAQTGTGKTASFVLPMLSLLEKGRArarmPRTLILEPTRELAAQVAENFEK 101
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKG----GRVLVLVPTRELAEQWAEELKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 102 YGKNHRLNVALLIGGVSFEDQDRKLERG-ADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFIPDIERIAKM 180
Cdd:smart00487 77 LGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502304280 181 IPFTRQTLFFSATMPSEIQKLADRFLQNPERIEVAKPASaaETVTQR 227
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPL--EPIEQF 201
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
10-209 |
2.73e-60 |
|
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: 197.45 E-value: 2.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 10 FADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLekgrarARMPR---TLILE 86
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL------SEDPYgifALVLT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 87 PTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFE---RGKLLMSGVEILVIDEAD 163
Cdd:cd17955 75 PTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEAD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502304280 164 RMLDMGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNP 209
Cdd:cd17955 155 RLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
6-212 |
5.59e-58 |
|
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: 191.82 E-value: 5.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 6 PLTTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGR--ARARMPRTL 83
Cdd:cd17953 10 PIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRpvKPGEGPIGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 84 ILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHF--ERGKLL-MSGVEILVID 160
Cdd:cd17953 90 IMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVTnLRRVTYVVLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502304280 161 EADRMLDMGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd17953 170 EADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
19-212 |
8.01e-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: 190.86 E-value: 8.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGRARARMP--RTLILEPTRELAAQ-- 94
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGqvGALIISPTRELATQiy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 95 -VAENFEKYGKNHrLNVALLIGGVSFEDQDRKLER-GADVLICTPGRLLDHFERGKLL--MSGVEILVIDEADRMLDMGF 170
Cdd:cd17960 81 eVLQSFLEHHLPK-LKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKvkVKSLEVLVLDEADRLLDLGF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502304280 171 IPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd17960 160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
19-212 |
2.44e-57 |
|
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: 189.55 E-value: 2.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLS------LLEKGRArarmPRTLILEPTRELA 92
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVhimdqrELEKGEG----PIAVIVAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 93 AQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFIP 172
Cdd:cd17952 77 QQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502304280 173 DIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd17952 157 QVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
19-214 |
1.90e-56 |
|
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: 187.03 E-value: 1.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKgRARARMPRTLILEPTRELAAQVAEN 98
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK-PRKKKGLRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 99 FEKYGKNHRLNVALLIGG-VSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFIPDIERI 177
Cdd:cd17957 80 LLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 502304280 178 AKMIPFTR-QTLFFSATMPSEIQKLADRFLQNPERIEV 214
Cdd:cd17957 160 LAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
10-209 |
3.78e-56 |
|
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: 186.37 E-value: 3.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 10 FADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLekgrararmpRTLILEPTR 89
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV----------VALILEPSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 90 ELAAQVA---ENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRML 166
Cdd:cd17938 71 ELAEQTYnciENFKKYLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502304280 167 DMGFIPDIERIAKMIP------FTRQTLFFSATMPS-EIQKLADRFLQNP 209
Cdd:cd17938 151 SQGNLETINRIYNRIPkitsdgKRLQVIVCSATLHSfEVKKLADKIMHFP 200
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
224-356 |
6.22e-55 |
|
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: 180.78 E-value: 6.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 224 VTQRFVASHGKdyEKRAVLRELVRAQTELKNAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNL 303
Cdd:cd18787 1 IKQLYVVVEEE--EKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 502304280 304 QLLVASDVAARGLDIPDVSHVFNFDVPIHSEDYVHRIGRTGRAGRSGAAFTLV 356
Cdd:cd18787 79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
6-215 |
2.67e-53 |
|
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: 180.21 E-value: 2.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 6 PLTTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPML------SLLEKGRArarm 79
Cdd:cd18049 22 PVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIvhinhqPFLERGDG---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 80 PRTLILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVI 159
Cdd:cd18049 98 PICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502304280 160 DEADRMLDMGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIEVA 215
Cdd:cd18049 178 DEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
6-215 |
3.21e-53 |
|
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: 181.36 E-value: 3.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 6 PLTTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPML------SLLEKGRArarm 79
Cdd:cd18050 60 PVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIvhinhqPYLERGDG---- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 80 PRTLILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVI 159
Cdd:cd18050 136 PICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVL 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502304280 160 DEADRMLDMGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIEVA 215
Cdd:cd18050 216 DEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
15-202 |
3.46e-52 |
|
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: 176.23 E-value: 3.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 15 LSQKVLSAVTDAGYTIPTPIQAGAIPFALE-RRDICGIAQTGTGKTASFVLPML-SLLE-KGRARARMPRTLILEPTREL 91
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIqSLLNtKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 92 AAQVAENFEKYGKNHR-LNVALLIGGVSFEDQDRKLER-GADVLICTPGRLLDHFE--RGKLLMSGVEILVIDEADRMLD 167
Cdd:cd17964 81 ALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 502304280 168 MGFIPDIERIAKMIP----FTRQTLFFSATMPSEIQKLA 202
Cdd:cd17964 161 MGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIA 199
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
10-212 |
1.63e-51 |
|
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: 174.41 E-value: 1.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 10 FADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLsllEKGRARARMPRTLILEPTR 89
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPIL---EKIDPKKDVIQALILVPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 90 ELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMG 169
Cdd:cd17940 78 ELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502304280 170 FIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd17940 158 FQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
15-209 |
8.52e-49 |
|
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: 167.38 E-value: 8.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 15 LSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGRARA---RMPRTLILEPTREL 91
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESgeeQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 92 AAQVAENFEK--YGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKL-LMSGVEILVIDEADRMLDM 168
Cdd:cd17961 81 AQQVSKVLEQltAYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502304280 169 GFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNP 209
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
19-212 |
7.27e-48 |
|
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: 164.26 E-value: 7.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSlleKGRARARMPRTLILEPTRELAAQVAEN 98
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVII---RCLTEHRNPSALILTPTRELAVQIEDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 99 FEKYGKNH-RLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFIPDIERI 177
Cdd:cd17962 78 AKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDI 157
|
170 180 190
....*....|....*....|....*....|....*
gi 502304280 178 AKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd17962 158 LENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
19-209 |
3.46e-47 |
|
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: 162.63 E-value: 3.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLP-MLSLLEKGRARARM--PRTLILEPTRELAAQV 95
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLQPIPREQRngPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 96 AENFEKYGKNHRLNVALLIGGVSFEdQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFIPDIE 175
Cdd:cd17958 81 EAECSKYSYKGLKSVCVYGGGNRNE-QIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....
gi 502304280 176 RIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNP 209
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDP 193
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
12-212 |
2.82e-46 |
|
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: 160.18 E-value: 2.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 12 DLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKgraRARMPRTLILEPTREL 91
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDT---TVRETQALVLAPTREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 92 AAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFI 171
Cdd:cd17939 78 AQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502304280 172 PDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd17939 158 DQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
20-202 |
7.80e-46 |
|
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: 159.06 E-value: 7.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 20 LSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGRArarMPRT----LILEPTRELAAQV 95
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKF---KPRNgtgvIIISPTRELALQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 96 AENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGK-LLMSGVEILVIDEADRMLDMGFIPDI 174
Cdd:cd17942 79 YGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgFLYKNLQCLIIDEADRILEIGFEEEM 158
|
170 180
....*....|....*....|....*...
gi 502304280 175 ERIAKMIPFTRQTLFFSATMPSEIQKLA 202
Cdd:cd17942 159 RQIIKLLPKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
19-218 |
1.82e-45 |
|
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: 159.33 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFAL-ERRDICGIAQTGTGKTASFVLPML-SLLEKGRARA-----RMPRTLILEPTREL 91
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILeRLLSQKSSNGvggkqKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 92 AAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMS---GVEILVIDEADRMLDM 168
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLAnlkSLRFLVLDEADRMLEK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502304280 169 GFIPDIERIAKMIPFT-------RQTLFFSATMpSEIQKLADRFLQNPERIEVAKPA 218
Cdd:cd17946 161 GHFAELEKILELLNKDragkkrkRQTFVFSATL-TLDHQLPLKLNSKKKKKKKEKKQ 216
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
15-212 |
1.17e-44 |
|
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: 155.81 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 15 LSQKVLSAVTDAGYTIPTPIQAGAIPFALE--RRDICGIAQTGTGKTASFVLPMLSLLEkgrARARMPRTLILEPTRELA 92
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSdpPENLIAQSQSGTGKTAAFVLAMLSRVD---PTLKSPQALCLAPTRELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 93 AQVAENFEKYGKNHRLNVALLIGGvsfEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDM-GFI 171
Cdd:cd17963 78 RQIGEVVEKMGKFTGVKVALAVPG---NDVPRGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502304280 172 PDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd17963 155 DQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
19-209 |
3.20e-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: 155.19 E-value: 3.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPML--SLLEKGRA---RARMPRTLILEPTRELAA 93
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfALEQEKKLpfiKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 94 QVAENFEKY------GKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLD 167
Cdd:cd17951 81 QTHEVIEYYckalqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502304280 168 MGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNP 209
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKP 202
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
19-209 |
2.05e-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: 152.42 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLekgRARARMPRTLILEPTRELAAQVAEN 98
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL---DLERRHPQVLILAPTREIAVQIHDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 99 FEKYGKNHR-LNVALLIGGVSFeDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFIPDIERI 177
Cdd:cd17943 78 FKKIGKKLEgLKCEVFIGGTPV-KEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWI 156
|
170 180 190
....*....|....*....|....*....|..
gi 502304280 178 AKMIPFTRQTLFFSATMPSEIQKLADRFLQNP 209
Cdd:cd17943 157 FSSLPKNKQVIAFSATYPKNLDNLLARYMRKP 188
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
27-212 |
2.47e-43 |
|
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: 153.13 E-value: 2.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 27 GYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLekGRARARMPRT-----LILEPTRELAAQVAENFEK 101
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRL--LSLEPRVDRSdgtlaLVLVPTRELALQIYEVLEK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 102 YGKN-HRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGK-LLMSGVEILVIDEADRMLDMGFIPDIERIAK 179
Cdd:cd17949 88 LLKPfHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEKDITKILE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502304280 180 MI-------------PFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd17949 168 LLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
10-212 |
8.58e-41 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 145.67 E-value: 8.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 10 FADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLpmlSLLEKGRARARMPRTLILEPTR 89
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSI---SILQQIDTSLKATQALVLAPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 90 ELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMG 169
Cdd:cd18046 78 ELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502304280 170 FIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd18046 158 FKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
27-207 |
5.02e-39 |
|
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: 141.14 E-value: 5.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 27 GYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKG---RARARMPRTLILEPTRELAAQVAENFEKYG 103
Cdd:cd17944 9 GVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDqqpRKRGRAPKVLVLAPTRELANQVTKDFKDIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 104 KnhRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFIPDIERI-----A 178
Cdd:cd17944 89 R--KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIlsvsyK 166
|
170 180
....*....|....*....|....*....
gi 502304280 179 KMIPFTRQTLFFSATMPSEIQKLADRFLQ 207
Cdd:cd17944 167 KDSEDNPQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
8-214 |
9.86e-39 |
|
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: 140.56 E-value: 9.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 8 TTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEK--GRARArmprtLIL 85
Cdd:cd17950 2 SGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPvdGQVSV-----LVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 86 EPTRELAAQVAENFEKYGKN-HRLNVALLIGGVSF-EDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEAD 163
Cdd:cd17950 77 CHTRELAFQISNEYERFSKYmPNVKTAVFFGGVPIkKDIEVLKNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502304280 164 RM---LDMGfiPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIEV 214
Cdd:cd17950 157 KMleqLDMR--RDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
10-212 |
1.19e-38 |
|
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: 139.91 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 10 FADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEkgrARARMPRTLILEPTR 89
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLD---IQVRETQALILSPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 90 ELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMG 169
Cdd:cd18045 78 ELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502304280 170 FIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd18045 158 FKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
19-209 |
5.86e-38 |
|
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: 138.92 E-value: 5.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALE---------RRDICGIAQTGTGKTASFVLPMLSLLeKGRARARMpRTLILEPTR 89
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPsskstppyrPGDLCVSAPTGSGKTLAYVLPIVQAL-SKRVVPRL-RALIVVPTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 90 ELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERG--------ADVLICTPGRLLDHFERGK-LLMSGVEILVID 160
Cdd:cd17956 79 ELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPgFTLKHLRFLVID 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502304280 161 EADRMLD----------MGFIPDIERIAKMIPFTR----------QTLFFSATMPSEIQKLADRFLQNP 209
Cdd:cd17956 159 EADRLLNqsfqdwletvMKALGRPTAPDLGSFGDAnllersvrplQKLLFSATLTRDPEKLSSLKLHRP 227
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
237-347 |
1.82e-33 |
|
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: 122.70 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 237 EKRAVLRELVRAQTElKNAIVFCNRKKDV-ADLFrsLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARG 315
Cdd:pfam00271 1 EKLEALLELLKKERG-GKVLIFSQTKKTLeAELL--LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 502304280 316 LDIPDVSHVFNFDVPIHSEDYVHRIGRTGRAG 347
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
23-212 |
6.47e-27 |
|
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: 109.00 E-value: 6.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 23 VTDAGYTIPTPIQAGAIPFALE---------------RRDICGI-AQTGTGKTASFVLPMLSLLEK-------------- 72
Cdd:cd17965 23 NKTDEEIKPSPIQTLAIKKLLKtlmrkvtkqtsneepKLEVFLLaAETGSGKTLAYLAPLLDYLKRqeqepfeeaeeeye 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 73 GRARARMPRTLILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKL--ERGADVLICTPGRLLDHFERGKLL 150
Cdd:cd17965 103 SAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLafKGRIDILVTTPGKLASLAKSRPKI 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502304280 151 MSGVEILVIDEADRMLDMGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERI 212
Cdd:cd17965 183 LSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRI 244
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
4-216 |
7.93e-27 |
|
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: 108.18 E-value: 7.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 4 VFPLTTFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALER--RDICGIAQTGTGKTASFVLPMLSLLEkgrARARMPR 81
Cdd:cd18048 14 LFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVD---ALKLYPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 82 TLILEPTRELAAQVAENFEKYGKnhrlnvaLLIG-GVSFEDQDRKLERGAD----VLICTPGRLLDHFERGKLL-MSGVE 155
Cdd:cd18048 91 CLCLSPTFELALQTGKVVEEMGK-------FCVGiQVIYAIRGNRPGKGTDieaqIVIGTPGTVLDWCFKLRLIdVTNIS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502304280 156 ILVIDEADRMLDM-GFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIEVAK 216
Cdd:cd18048 164 VFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKK 225
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
272-347 |
1.14e-26 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 103.06 E-value: 1.14e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502304280 272 LERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVFNFDVPIHSEDYVHRIGRTGRAG 347
Cdd:smart00490 7 LKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
54-469 |
2.28e-25 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 109.73 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 54 TGTGKTASFVLPMLSLLEKGRararmprTLILEPTRELAAQVAENFEKYgknhrLNVALLIGGvsfedqdrKLERGADVL 133
Cdd:COG1061 109 TGTGKTVLALALAAELLRGKR-------VLVLVPRRELLEQWAEELRRF-----LGDPLAGGG--------KKDSDAPIT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 134 ICTPGRLLDHFERgKLLMSGVEILVIDEADRMLDMGFipdiERIAKMIPFTRQ-----TLFFSATMPSEIQK-------- 200
Cdd:COG1061 169 VATYQSLARRAHL-DELGDRFGLVIIDEAHHAGAPSY----RRILEAFPAAYRlgltaTPFRSDGREILLFLfdgivyey 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 201 -----LADRFLQNPERIEV--------AKPASAAETVTQRFVASHGkdyEKRAVLRELVRAQTELKNAIVFCNRKKDVAD 267
Cdd:COG1061 244 slkeaIEDGYLAPPEYYGIrvdltderAEYDALSERLREALAADAE---RKDKILRELLREHPDDRKTLVFCSSVDHAEA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 268 LFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVFNFDvPIHSE-DYVHRIGRTGRA 346
Cdd:COG1061 321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PTGSPrEFIQRLGRGLRP 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 347 GRSgaaftlvtKRDTKFVDaiekLIGEKVEWLSGDLTSLPPPAEDSRDSERPRRNGRERGARDGAGRDRAPRENGDKDRG 426
Cdd:COG1061 400 APG--------KEDALVYD----FVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLE 467
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 502304280 427 RGRGNRAAASHKSDNDIQDNGVDVIEAAPVKADIVKNERKAEQ 469
Cdd:COG1061 468 ELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEE 510
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
9-213 |
1.54e-24 |
|
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: 101.34 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 9 TFADLGLSQKVLSAVTDAGYTIPTPIQAGAIPFALER--RDICGIAQTGTGKTASFVLPMLSLLEKGrarARMPRTLILE 86
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPA---NKYPQCLCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 87 PTRELAAQVAENFEKYGKNH-RLNVALLIGGvsfedqdRKLERGA----DVLICTPGRLLDHFERGKLL-MSGVEILVID 160
Cdd:cd18047 79 PTYELALQTGKVIEQMGKFYpELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKLKFIdPKKIKVFVLD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502304280 161 EADRML-DMGFIPDIERIAKMIPFTRQTLFFSATMPSEIQKLADRFLQNPERIE 213
Cdd:cd18047 152 EADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
19-196 |
2.19e-24 |
|
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: 101.29 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 19 VLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPML------SLLEKGRARArmPRTLILEPTRELA 92
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIqrllryKLLAEGPFNA--PRGLVITPSRELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 93 AQVAENFEKYGKNHRLNVALLIGGVSfEDQDRKLERG-ADVLICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFI 171
Cdd:cd17948 79 EQIGSVAQSLTEGLGLKVKVITGGRT-KRQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 502304280 172 PDIERIAKMIPFTR-------------QTLFFSATMPS 196
Cdd:cd17948 158 EKLSHFLRRFPLASrrsentdgldpgtQLVLVSATMPS 195
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
52-193 |
5.12e-18 |
|
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: 80.91 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 52 AQTGTGKTASFVLPMLSLLEKGRararmPRTLILEPTRELAAQVAENFEKYGKNHrLNVALLIGGVSFEDQDRKLERGAD 131
Cdd:cd00046 8 APTGSGKTLAALLAALLLLLKKG-----KKVLVLVPTKALALQTAERLRELFGPG-IRVAVLVGGSSAEEREKNKLGDAD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502304280 132 VLICTPGRLLDHFERGKLL-MSGVEILVIDEADRMLDMGFIPDIERIA--KMIPFTRQTLFFSAT 193
Cdd:cd00046 82 IIIATPDMLLNLLLREDRLfLKDLKLIIVDEAHALLIDSRGALILDLAvrKAGLKNAQVILLSAT 146
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
32-347 |
1.42e-15 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 79.17 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 32 TPIQAGAIPFALERRD---ICgiAQTGTGKTASFVLPMLSLLEKGrararmPRTLILEPTRELAAQVAENFEKYGKNHRL 108
Cdd:COG1204 24 YPPQAEALEAGLLEGKnlvVS--APTASGKTLIAELAILKALLNG------GKALYIVPLRALASEKYREFKRDFEELGI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 109 NVALLIGGvsFEDQDRKLERgADVLICTPGRLlDHFER-GKLLMSGVEILVIDEA------DR-----MLdmgfipdIER 176
Cdd:COG1204 96 KVGVSTGD--YDSDDEWLGR-YDILVATPEKL-DSLLRnGPSWLRDVDLVVVDEAhliddeSRgptleVL-------LAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 177 IAKMIPFTrQTLFFSATMPSeIQKLAD--------------------------RFLQNPERIEVAKPASAAETVTQR--- 227
Cdd:COG1204 165 LRRLNPEA-QIVALSATIGN-AEEIAEwldaelvksdwrpvplnegvlydgvlRFDDGSRRSKDPTLALALDLLEEGgqv 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 228 --FVAShgkdyeKRAVLRELVRAQTELKNAIVFCNRKK--DVADLFRSLE-------------RHGfsVGALHGDMDQRS 290
Cdd:COG1204 243 lvFVSS------RRDAESLAKKLADELKRRLTPEEREEleELAEELLEVSeethtnekladclEKG--VAFHHAGLPSEL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502304280 291 RTMTLQSFRDGNLQLLVASDVAARGLDIPdVSHVF------NFDVPIHSEDYVHRIGRTGRAG 347
Cdd:COG1204 315 RRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIirdtkrGGMVPIPVLEFKQMAGRAGRPG 376
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
227-459 |
5.86e-15 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 77.85 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 227 RFVASHGKDYEKRAVLRELVRAQTELKN---AIVFCNRKKDVADLFRSLERHGFSVGALHGD--------MDQRSRTMTL 295
Cdd:COG1111 325 RLAEEADIEHPKLSKLREILKEQLGTNPdsrIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEIL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 296 QSFRDGNLQLLVASDVAARGLDIPDVSHVFNFDvPIHSE-DYVHRIGRTGRaGRSGAAFTLVTK--RDTKF--------- 363
Cdd:COG1111 405 ERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PVPSEiRSIQRKGRTGR-KREGRVVVLIAKgtRDEAYywssrrkek 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 364 -----VDAIEKLIGEK-----VEWLSGDLTSLPPPAEDSRDSERPRRNGRERGARDGAGRDRAPRENGDKDRGRGRGNRA 433
Cdd:COG1111 483 kmksiLKKLKKLLDKQekeklKESAQATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVIVSTLAESLE 562
|
250 260
....*....|....*....|....*.
gi 502304280 434 AASHKSDNDIQDNGVDVIEAAPVKAD 459
Cdd:COG1111 563 LRELGEKVDDEVNLILEIDRVDVVDD 588
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
35-374 |
1.50e-13 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 72.87 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 35 QAGAIPFALERRDICGIAQTGTGKTASFVLPmlSLLEKGRararmprTLILEPtreLAA----QVAEnFEKYGknhrLNV 110
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLP--ALLLPGL-------TLVVSP---LIAlmkdQVDA-LRAAG----IRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 111 ALLIGGVSFEDQD---RKLERGA-DVLICTPGRLL-DHFERgklLMSGVEI--LVIDEA--------DrmldmgFIPDIE 175
Cdd:COG0514 85 AFLNSSLSAEERRevlRALRAGElKLLYVAPERLLnPRFLE---LLRRLKIslFAIDEAhcisqwghD------FRPDYR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 176 RIAKMIP-FTR-QTLFFSATMPSEIQK-LADRF-LQNPerievakpasaaetvtQRFVAS-----------HGKDYEKRA 240
Cdd:COG0514 156 RLGELRErLPNvPVLALTATATPRVRAdIAEQLgLEDP----------------RVFVGSfdrpnlrlevvPKPPDDKLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 241 VLRELVRAQTElKNAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASdVA-ARGLDIP 319
Cdd:COG0514 220 QLLDFLKEHPG-GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKP 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 502304280 320 DVSHVFNFDVPIHSEDYVHRIGRTGRAGRSGAAFTLVTKRDtkfVDAIEKLIGEK 374
Cdd:COG0514 298 DVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPED---VAIQRFFIEQS 349
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
247-357 |
2.47e-13 |
|
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: 67.23 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 247 RAQTELKNAIVFCNRKKDVADLFRSLERH---------GFSVGALHG------DMDQRSRTMTLQSFRDGNLQLLVASDV 311
Cdd:cd18802 20 FPKTPDFRGIIFVERRATAVVLSRLLKEHpstlafircGFLIGRGNSsqrkrsLMTQRKQKETLDKFRDGELNLLIATSV 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 502304280 312 AARGLDIPDVSHVFNFDVPIHSEDYVHRigRtGRAGRSGAAFTLVT 357
Cdd:cd18802 100 LEEGIDVPACNLVIRFDLPKTLRSYIQS--R-GRARAPNSKYILMV 142
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
32-195 |
1.02e-12 |
|
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: 66.52 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 32 TPIQAGAIPFALERRD---ICgiAQTGTGKTASFVLPMLSLLEKGRARArmprtLILEPTRELAAQVAENFEKYGKNHRL 108
Cdd:cd17921 3 NPIQREALRALYLSGDsvlVS--APTSSGKTLIAELAILRALATSGGKA-----VYIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 109 NVALLIGGVSFedqDRKLERGADVLICTPGR---LLDHFERgkLLMSGVEILVIDEADrmldmgFIPDIER-------IA 178
Cdd:cd17921 76 NVGLLTGDPSV---NKLLLAEADILVATPEKldlLLRNGGE--RLIQDVRLVVVDEAH------LIGDGERgvvlellLS 144
|
170
....*....|....*....
gi 502304280 179 KMIPFTR--QTLFFSATMP 195
Cdd:cd17921 145 RLLRINKnaRFVGLSATLP 163
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
236-348 |
2.85e-12 |
|
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: 63.77 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 236 YEKRAVLRELVRAQTELKN-----AIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASD 310
Cdd:cd18794 9 RPKDKKDEKLDLLKRIKVEhlggsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATV 88
|
90 100 110
....*....|....*....|....*....|....*...
gi 502304280 311 VAARGLDIPDVSHVFNFDVPIHSEDYVHRIGRTGRAGR 348
Cdd:cd18794 89 AFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGL 126
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
253-350 |
3.53e-12 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 68.97 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 253 KNAIVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVFNFDVPIH 332
Cdd:PRK11057 237 KSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRN 316
|
90
....*....|....*...
gi 502304280 333 SEDYVHrigRTGRAGRSG 350
Cdd:PRK11057 317 IESYYQ---ETGRAGRDG 331
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
210-360 |
3.98e-12 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 68.75 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 210 ERIEVAKPASAAETVTQRFVA------------SHGKDYEKRAVLRELVRAQTELKN---AIVFCNRKKDVADLFRSLER 274
Cdd:PRK13766 308 ERLREEARSSGGSKASKRLVEdprfrkavrkakELDIEHPKLEKLREIVKEQLGKNPdsrIIVFTQYRDTAEKIVDLLEK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 275 HGFSVGALHGD--------MDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVFnFDVPIHSE-DYVHRIGRTGR 345
Cdd:PRK13766 388 EGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPVPSEiRSIQRKGRTGR 466
|
170
....*....|....*..
gi 502304280 346 aGRSGAAFTLVTK--RD 360
Cdd:PRK13766 467 -QEEGRVVVLIAKgtRD 482
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
54-193 |
1.47e-11 |
|
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: 62.32 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 54 TGTGKTasfvLPMLSLLEKgrarARMPRTLILEPTRELAAQVAENFEKYGKNHRLNvalLIGGVSFEDQDrklerGADVL 133
Cdd:cd17926 27 TGSGKT----LTALALIAY----LKELRTLIVVPTDALLDQWKERFEDFLGDSSIG---LIGGGKKKDFD-----DANVV 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 134 ICTPGRLLDHFERGKLLMSGVEILVIDEADRMLDMGFipdiERIAKMIPFTRQtLFFSAT 193
Cdd:cd17926 91 VATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTF----SEILKELNAKYR-LGLTAT 145
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
14-376 |
3.06e-11 |
|
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: 66.01 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 14 GLSQKVLSAVTDAGYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLS-LLEKGRARArmprtLILEPTRELA 92
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEaLLEDPGATA-----LYLYPTKALA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 93 A-QVAEnFEKYGKNH--RLNVALLIGGVSFEDQdRKLERGADVLICTP-----GrLLDHFERGKLLMSGVEILVIDEA-- 162
Cdd:COG1205 115 RdQLRR-LRELAEALglGVRVATYDGDTPPEER-RWIREHPDIVLTNPdmlhyG-LLPHHTRWARFFRNLRYVVIDEAht 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 163 -------------DRMLdmgfipdieRIAKMIPFTRQTLFFSATM--PSEI-QKLADR------------------FLQN 208
Cdd:COG1205 192 yrgvfgshvanvlRRLR---------RICRHYGSDPQFILASATIgnPAEHaERLTGRpvtvvdedgsprgertfvLWNP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 209 PERIEVAKPASAAETvtqrfvashgkdyekRAVLRELVR--AQTelknaIVFCNRKKDVADLFRSLERH------GFSVG 280
Cdd:COG1205 263 PLVDDGIRRSALAEA---------------ARLLADLVRegLRT-----LVFTRSRRGAELLARYARRAlrepdlADRVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 281 ALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVFNFDVP--IHSedYVHRIGRTGRAGRSGAAFtLVTK 358
Cdd:COG1205 323 AYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPgtRAS--FWQQAGRAGRRGQDSLVV-LVAG 399
|
410 420
....*....|....*....|.
gi 502304280 359 R---DTKFVDAIEKLIGEKVE 376
Cdd:COG1205 400 DdplDQYYVRHPEELFERPPE 420
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
255-357 |
2.04e-10 |
|
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: 56.94 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 255 AIVFCNRKKDVADLFRSLerhgfsvgalhgdmdqrsrtmtlqsfrdgnlQLLVASDVAARGLDIPDVSHVFNFDVPIHSE 334
Cdd:cd18785 6 IIVFTNSIEHAEEIASSL-------------------------------EILVATNVLGEGIDVPSLDTVIFFDPPSSAA 54
|
90 100
....*....|....*....|...
gi 502304280 335 DYVHRIGRTGRAGRSGAAFTLVT 357
Cdd:cd18785 55 SYIQRVGRAGRGGKDEGEVILFV 77
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
54-162 |
3.07e-10 |
|
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: 59.59 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 54 TGTGKTASFVLPMLSLLEKGRARAR-MPRTLILEPTRELAAQVAENFEKYGKnhrLNVALLIG--GVSFEDQDRKLE--R 128
Cdd:cd18034 25 TGSGKTLIAVMLIKEMGELNRKEKNpKKRAVFLVPTVPLVAQQAEAIRSHTD---LKVGEYSGemGVDKWTKERWKEelE 101
|
90 100 110
....*....|....*....|....*....|....
gi 502304280 129 GADVLICTPGRLLDHFERGKLLMSGVEILVIDEA 162
Cdd:cd18034 102 KYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
239-341 |
9.79e-10 |
|
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: 56.72 E-value: 9.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 239 RAVLRELVRAQTELKNAIVFCNRKkDVADLFRS-LERHGFSVGALHGDMDQRSRTMTLQSFRDGN--LQLLVASDVAARG 315
Cdd:cd18793 14 EALLELLEELREPGEKVLIFSQFT-DTLDILEEaLRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVG 92
|
90 100 110
....*....|....*....|....*....|..
gi 502304280 316 LDIPDVSHVFNFDVP------IHSEDYVHRIG 341
Cdd:cd18793 93 LNLTAANRVILYDPWwnpaveEQAIDRAHRIG 124
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
48-164 |
8.01e-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: 55.52 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 48 ICgiAQTGTGKTASFVLPMLSLLEKGRARaRMPRTLILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLE 127
Cdd:cd17927 22 IC--LPTGSGKTFVAVLICEHHLKKFPAG-RKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENVSVEQIV 98
|
90 100 110
....*....|....*....|....*....|....*...
gi 502304280 128 RGADVLICTPGRLLDHFERGKLL-MSGVEILVIDEADR 164
Cdd:cd17927 99 ESSDVIIVTPQILVNDLKSGTIVsLSDFSLLVFDECHN 136
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
51-329 |
1.95e-08 |
|
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: 56.63 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 51 IAQTGTGKT-ASFvLPMLSLLEKGRARaRMprTLILePTRELAAQvaeNFEKYGKNHRLNVALLIGGVSFEDQDRKLERG 129
Cdd:COG1203 153 TAPTGGGKTeAAL-LFALRLAAKHGGR-RI--IYAL-PFTSIINQ---TYDRLRDLFGEDVLLHHSLADLDLLEEEEEYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 130 --------------ADVLICTPGRLLD-------HFERgKL--LMSGVeiLVIDEADrMLDMGFIPDIERIAKMIPFTRQ 186
Cdd:COG1203 225 searwlkllkelwdAPVVVTTIDQLFEslfsnrkGQER-RLhnLANSV--IILDEVQ-AYPPYMLALLLRLLEWLKNLGG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 187 TLFF-SATMPseiQKLADRFLQNPERI--EVAKPASAAETVTQRFVASHGKDYEKRAVLRELVRAQTELKNAIVFCNRKK 263
Cdd:COG1203 301 SVILmTATLP---PLLREELLEAYELIpdEPEELPEYFRAFVRKRVELKEGPLSDEELAELILEALHKGKSVLVIVNTVK 377
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502304280 264 DVADLFRSLERHGFSVGA--LHGDMDQRSRTMTLQ----SFRDGNLQLLVASDVAARGLDIpdvshvfNFDV 329
Cdd:COG1203 378 DAQELYEALKEKLPDEEVylLHSRFCPADRSEIEKeikeRLERGKPCILVSTQVVEAGVDI-------DFDV 442
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
242-355 |
2.67e-08 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 52.74 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 242 LRELVRAQTELKNA------IVFCNRKKDVADLFRSLERHGFSVGAL----HGD------MDQRSRTMTLQSFRDGNLQL 305
Cdd:cd18801 14 LEEIVKEHFKKKQEgsdtrvIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASgksskgMSQKEQKEVIEQFRKGGYNV 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 502304280 306 LVASDVAARGLDIPDVSHVFNFDV---PIHSedyVHRIGRTGRaGRSGAAFTL 355
Cdd:cd18801 94 LVATSIGEEGLDIGEVDLIICYDAspsPIRM---IQRMGRTGR-KRQGRVVVL 142
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
54-193 |
3.89e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 52.67 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 54 TGTGKTA-SFVLpMLSLLEKGRARarmpRTLILEPTRELAAQVAENFEKYGKNHRlnvalLIGGVSFEDQDRKLERGADV 132
Cdd:pfam04851 32 TGSGKTLtAAKL-IARLFKKGPIK----KVLFLVPRKDLLEQALEEFKKFLPNYV-----EIGEIISGDKKDESVDDNKI 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502304280 133 LICTPGRLLDHFERGKLLMSGVEILVI--DEADRmldmGFIPDIERIAKMIPFTRQtLFFSAT 193
Cdd:pfam04851 102 VVTTIQSLYKALELASLELLPDFFDVIiiDEAHR----SGASSYRNILEYFKPAFL-LGLTAT 159
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
51-193 |
5.17e-08 |
|
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: 53.10 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 51 IAQTGTGKTaSFVLPM-LSLLEKGRararmpRTLILEPTRELAAQVAENFEKYGKNHRLNVALLI--GGVSFEDQDRKLE 127
Cdd:cd17924 38 IAPTGVGKT-TFGLATsLYLASKGK------RSYLIFPTKSLVKQAYERLSKYAEKAGVEVKILVyhSRLKKKEKEELLE 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 128 R----GADVLICTPGRLLDHFERgkLLMSGVEILVIDEADRMLDMGfiPDIERIAKMIPFTrQTLFFSAT 193
Cdd:cd17924 111 KiekgDFDILVTTNQFLSKNFDL--LSNKKFDFVFVDDVDAVLKSS--KNIDRLLKLLGFG-QLVVSSAT 175
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
238-353 |
3.73e-07 |
|
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: 49.56 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 238 KRAVLRELVRAQTELKNAIVFCnrkKDVADLFRSLERhgFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLD 317
Cdd:cd18789 35 KLRALEELLKRHEQGDKIIVFT---DNVEALYRYAKR--LLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGID 109
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 502304280 318 IPDVshvfNFDVPIHS-----EDYVHRIGRTGRAGRSGAAF 353
Cdd:cd18789 110 LPEA----NVAIQISGhggsrRQEAQRLGRILRPKKGGGKN 146
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
31-165 |
8.24e-07 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 49.34 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 31 PTPIQAGAI---------PFALeRRDICGiaQTGTGKTASFVLPMLSLLEKGRararmpRTLILEPTRELAAQVAENFEK 101
Cdd:cd17918 16 LTKDQAQAIkdiekdlhsPEPM-DRLLSG--DVGSGKTLVALGAALLAYKNGK------QVAILVPTEILAHQHYEEARK 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502304280 102 YGKNhrLNVALLIGGvsfedQDRKLERGADVLICTPGRLldHFERGKLlmsGVEILVIDEADRM 165
Cdd:cd17918 87 FLPF--INVELVTGG-----TKAQILSGISLLVGTHALL--HLDVKFK---NLDLVIVDEQHRF 138
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
35-162 |
8.47e-07 |
|
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: 49.12 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 35 QAGAIPFALERRDICGIAQTGTGKTASFVLPML-SLLEKGRARArmprtLILEPTRELAAQVAENFEKYGKNH--RLNVA 111
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeALLRDPGSRA-----LYLYPTKALAQDQLRSLRELLEQLglGIRVA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 502304280 112 LLIGGVSFEDQDRKLERGADVLICTPGRL----LDHFERGKLLMSGVEILVIDEA 162
Cdd:cd17923 80 TYDGDTPREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
42-164 |
1.30e-06 |
|
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: 48.66 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 42 ALERRDICgIAQTGTGKTASFVLPMLSLLEKGRARarmprTLILEPTRELAAQVAENFEkygknHRLNVALLIGGVSFE- 120
Cdd:cd18035 14 ALNGNTLI-VLPTGLGKTIIAILVAADRLTKKGGK-----VLILAPSRPLVEQHAENLK-----RVLNIPDKITSLTGEv 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 502304280 121 --DQDRKLERGADVLICTPGRLLDHFERGKLLMSGVEILVIDEADR 164
Cdd:cd18035 83 kpEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
34-161 |
1.61e-06 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 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: 350781 [Multi-domain] Cd Length: 206 Bit Score: 48.89 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 34 IQAGAIPFALERRDICGI-AQTGTGKTASFVLPMLSLLEKGRARARMPRTLI-LEPTRELAAQVAEN-FEKYGKNHrLNV 110
Cdd:cd18023 5 IQSEVFPDLLYSDKNFVVsAPTGSGKTVLFELAILRLLKERNPLPWGNRKVVyIAPIKALCSEKYDDwKEKFGPLG-LSC 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 502304280 111 ALLIGGVSFEDqDRKLeRGADVLICTPGRlLDHFER----GKLLMSGVEILVIDE 161
Cdd:cd18023 84 AELTGDTEMDD-TFEI-QDADIILTTPEK-WDSMTRrwrdNGNLVQLVALVLIDE 135
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
238-343 |
2.32e-06 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 50.22 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 238 KRAVLRELVRAQTELKN-AIVFCnRKKDVADLFRS-LERHGFSVGALHGDMDQRSRTMTLQSFRDGN--LQLLVASDVAA 313
Cdd:COG0553 534 KLEALLELLEELLAEGEkVLVFS-QFTDTLDLLEErLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGG 612
|
90 100 110
....*....|....*....|....*....|....*.
gi 502304280 314 RGLDIPDVSHVFNFDVPIH------SEDYVHRIGRT 343
Cdd:COG0553 613 EGLNLTAADHVIHYDLWWNpaveeqAIDRAHRIGQT 648
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
51-388 |
7.83e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 48.77 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 51 IAQTGTGKT-ASFVLPMLSLLEKGRARARMP------RTLILEPTRELAAQVAENFE------------KYGKNHRLNVA 111
Cdd:PRK09751 2 IAPTGSGKTlAAFLYALDRLFREGGEDTREAhkrktsRILYISPIKALGTDVQRNLQiplkgiaderrrRGETEVNLRVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 112 LLIGGVSFEDQDRKLERGADVLICTPGRL-LDHFERGKLLMSGVEILVIDE----ADRMLDMGFIPDIERIAKMIPFTRQ 186
Cdd:PRK09751 82 IRTGDTPAQERSKLTRNPPDILITTPESLyLMLTSRARETLRGVETVIIDEvhavAGSKRGAHLALSLERLDALLHTSAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 187 TLFFSATMPSeiqklADR---FLQNPERIEVAKPASAAETVTQRFV------------ASHGKD-----------YEKRA 240
Cdd:PRK09751 162 RIGLSATVRS-----ASDvaaFLGGDRPVTVVNPPAMRHPQIRIVVpvanmddvssvaSGTGEDshagregsiwpYIETG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 241 VLRELVRAqtelKNAIVFCNRK----KDVADL-----------------------------FRSLERHGFSVGALHGDMD 287
Cdd:PRK09751 237 ILDEVLRH----RSTIVFTNSRglaeKLTARLnelyaarlqrspsiavdaahfestsgatsNRVQSSDVFIARSHHGSVS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 288 QRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVFNFDVPIHSEDYVHRIGRTGR--AGRSGAAFTLVTKRDtkFVD 365
Cdd:PRK09751 313 KEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHqvGGVSKGLFFPRTRRD--LVD 390
|
410 420
....*....|....*....|...
gi 502304280 366 AieKLIGEKVewLSGDLTSLPPP 388
Cdd:PRK09751 391 S--AVIVECM--FAGRLENLTPP 409
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
226-370 |
1.19e-05 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 45.41 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 226 QRFVASHGKDYEKRAVLRELVRaqtelkNAIVF--CNRKKDVADLFRSLER--HGFSVGALHGDMDQRSRTMTLQSFRDG 301
Cdd:cd18810 3 RTYVMPYDDELIREAIERELLR------GGQVFyvHNRIESIEKLATQLRQlvPEARIAIAHGQMTENELEEVMLEFAKG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502304280 302 NLQLLVASDVAARGLDIPDVSH--VFNFDVPIHSEDYVHRiGRTGRAGRSGAAFTLVTKRDTKFVDAIEKL 370
Cdd:cd18810 77 EYDILVCTTIIESGIDIPNANTiiIERADKFGLAQLYQLR-GRVGRSKERAYAYFLYPDQKKLTEDALKRL 146
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
33-205 |
1.37e-05 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 46.10 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 33 PIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGRArarmpRTLILEPTRELAA-QVAenfekyGKNHRLNVA 111
Cdd:cd18018 15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPG-----LTLVVSPLIALMKdQVD------ALPRAIKAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 112 LLIGGVSFEDQDRKLER----GADVLICTPGRLLD-HFERGKLLMSGVEILVIDEADRMLDMG--FIPDIERIAKMI--- 181
Cdd:cd18018 84 ALNSSLTREERRRILEKlragEVKILYVSPERLVNeSFRELLRQTPPISLLVVDEAHCISEWShnFRPDYLRLCRVLrel 163
|
170 180
....*....|....*....|....*
gi 502304280 182 PFTRQTLFFSATMPSE-IQKLADRF 205
Cdd:cd18018 164 LGAPPVLALTATATKRvVEDIASHL 188
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
51-161 |
5.54e-05 |
|
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: 43.73 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 51 IAQTGTGKTASFVLPMLSLLEKGRARARmpRTLILEPTRELAAQVAENFEKYGKNHRLN--VALLIGGVSFEDQDRKLER 128
Cdd:cd17922 7 AAPTGSGKTEAAFLPALSSLADEPEKGV--QVLYISPLKALINDQERRLEEPLDEIDLEipVAVRHGDTSQSEKAKQLKN 84
|
90 100 110
....*....|....*....|....*....|....*.
gi 502304280 129 GADVLICTP---GRLLDHfERGKLLMSGVEILVIDE 161
Cdd:cd17922 85 PPGILITTPeslELLLVN-KKLRELFAGLRYVVVDE 119
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
255-342 |
7.42e-05 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 42.16 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 255 AIVFCNRKK---DVADLFRsleRHGFSVGALHGD--MDQRSRTM-TLQSFRDGNLQLLVASDVAARGLDIPDVSHVFnFD 328
Cdd:cd18799 9 TLIFCVSIEhaeFMAEAFN---EAGIDAVALNSDysDRERGDEAlILLFFGELKPPILVTVDLLTTGVDIPEVDNVV-FL 84
|
90
....*....|....*
gi 502304280 329 VPIHSED-YVHRIGR 342
Cdd:cd18799 85 RPTESRTlFLQMLGR 99
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
52-349 |
1.03e-04 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 44.87 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 52 AQTGTGKTAsfvlpML------SLLEKGRARARMPRTlilEPTRELAAQVAENFEKYgknhrlNVALLIGGVsfEDQDRk 125
Cdd:COG4098 136 AVCGAGKTE-----MLfpaiaeALKQGGRVCIATPRV---DVVLELAPRLQQAFPGV------DIAALYGGS--EEKYR- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 126 lerGADVLICTPGRLLdHFERGkllmsgVEILVIDEAD-------RMLDMGfipdIERIAKMipfTRQTLFFSATMPSEI 198
Cdd:COG4098 199 ---YAQLVIATTHQLL-RFYQA------FDLLIIDEVDafpysgdPMLQYA----VKRARKP---DGKLIYLTATPSKAL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 199 QKLADRflqnpERIEVAK-PAsaaetvtqRFvasHG-----------KDYEKRA-------VLRELVRAQTELKN-AIVF 258
Cdd:COG4098 262 QRQVKR-----GKLKVVKlPA--------RY---HGhplpvpkfkwlGNWKKRLrrgklprKLLKWLKKRLKEGRqLLIF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 259 CNRKKDVADLFRSLERH--GFSVGALHGDMDQRSRTmtLQSFRDGNLQLLVASDVAARGLDIPDVS-HVFNFDVPIHSED 335
Cdd:COG4098 326 VPTIELLEQLVALLQKLfpEERIAGVHAEDPERKEK--VQAFRDGEIPILVTTTILERGVTFPNVDvAVLGADHPVFTEA 403
|
330
....*....|....
gi 502304280 336 YVHRIGrtGRAGRS 349
Cdd:COG4098 404 ALVQIA--GRVGRS 415
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
51-109 |
1.25e-04 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 44.59 E-value: 1.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 51 IAQTGTGKTASFVLPMLSLLEKGRArarmprTLILEPTRELAAQVAENFEKYGKN-HRLN 109
Cdd:COG3505 5 IGPTGSGKTVGLVIPNLTQLARGES------VVVTDPKGDLAELTAGFRRRAGYDvYVFD 58
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
28-98 |
5.11e-04 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 42.78 E-value: 5.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502304280 28 YTIPTPIQAGAIPFALERRDICGIAQTGTGKT-ASFVLPMLSLLEKGRARARMPRTLIL--EPTRELAAQVAEN 98
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDELARRPRPGELPDGLRVLyiSPLKALANDIERN 95
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
31-161 |
8.48e-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: 40.92 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 31 PTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPMLSLLEKGRARARMPRTLILEPTRELAAQVAENFEKYgKNHRLNV 110
Cdd:cd18036 3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQQLEKFFKY-FRKGYKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 502304280 111 ALLIGGVSFEDQDRKLERGADVLICTPGRLLDHFERG----KLLMSGVEILVIDE 161
Cdd:cd18036 82 TGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGreeeRVYLSDFSLLIFDE 136
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
263-393 |
1.49e-03 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain] Cd Length: 174 Bit Score: 39.60 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 263 KDVAD-LFRSLERHGFSVGALHgdmdqRSRTMTLQSFRDGNLQLLVAS----DVAARGLDIPDVSH--VFnFDVPIHSed 335
Cdd:cd18798 37 KEYAEeLKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLPERIKyaIF-YGVPVTT-- 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502304280 336 YVHRIGRTGR--AGR--SGAAFTLVTkrDTKFVDAIEK---LIGEKVEWLSG---DLTSLPPPAEDSR 393
Cdd:cd18798 109 YIQASGRTSRlyAGGltKGLSVVLVD--DPELFEALKKrlkLILDEFIFKELeevDLEELLSEIDESR 174
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
244-345 |
1.51e-03 |
|
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: 39.17 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 244 ELVRAQTELKNAIVFCNRKKDVADLFRSL------ERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLD 317
Cdd:cd18796 30 EVIFLLERHKSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGID 109
|
90 100
....*....|....*....|....*...
gi 502304280 318 IPDVSHVFNFDVPIHSEDYVHRIGRTGR 345
Cdd:cd18796 110 IGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
250-356 |
1.89e-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: 39.25 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 250 TELKNAIVFCNRKKDVadlFRSlerhGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVfnfdV 329
Cdd:cd18811 42 LDLKAAVAMYEYLKER---FRP----ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVM----V 110
|
90 100 110
....*....|....*....|....*....|..
gi 502304280 330 PIHSEDY----VHRI-GRTGRAGRSGAAFTLV 356
Cdd:cd18811 111 IEDAERFglsqLHQLrGRVGRGDHQSYCLLVY 142
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
256-349 |
3.16e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 40.26 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 256 IVFCNRKKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVFNFDVPIHSED 335
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|....*
gi 502304280 336 YVHRIGRTGRAG-RS 349
Cdd:PLN03137 764 YHQECGRAGRDGqRS 778
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
52-137 |
3.50e-03 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 38.78 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 52 AQTGTGKT--ASF-VLPMLSLLEKGRArarmprtLILEPTRELAAQVAENFE-KYGKNHRLNVALLIGGVSfedQDRKLE 127
Cdd:cd18021 26 APTGSGKTvcAELaLLRHWRQNPKGRA-------VYIAPMQELVDARYKDWRaKFGPLLGKKVVKLTGETS---TDLKLL 95
|
90
....*....|
gi 502304280 128 RGADVLICTP 137
Cdd:cd18021 96 AKSDVILATP 105
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
238-370 |
3.63e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain] Cd Length: 160 Bit Score: 38.40 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 238 KRAVLRELVRAqtelKNAIVFCNR--------KKDVADLFRSLERH--GFSVGALHGDMDQRSRTMTLQSFRDGNLQLLV 307
Cdd:cd18792 16 YEAIERELARG----GQVYYVYPRieesekldLKSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILV 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502304280 308 ASDVAARGLDIPDVshvfNFDVPIHSEDY----VHRI-GRTGRAGRSGAAFtLVTKRDTKFV-DAIEKL 370
Cdd:cd18792 92 STTVIEVGIDVPNA----NTMIIEDADRFglsqLHQLrGRVGRGKHQSYCY-LLYPDPKKLTeTAKKRL 155
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
262-328 |
3.94e-03 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 38.38 E-value: 3.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502304280 262 KKDVADLFRSLERHGFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVASDVAARGLDIPDVSHVFNFD 328
Cdd:cd18790 37 KRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
263-308 |
5.25e-03 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 39.65 E-value: 5.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 502304280 263 KDVADLFRSLERH--GFSVGALHGDMDQRSRTMTLQSFRDGNLQLLVA 308
Cdd:COG1200 488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVA 535
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
55-193 |
5.52e-03 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350750 [Multi-domain] Cd Length: 225 Bit Score: 38.28 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 55 GTGKTASFVLPMLSLLEKGRARARMPrtlilePTRELAAQVAENFEKYGKNHRLNVALLIGGVSFEDQDRKLERGA---- 130
Cdd:cd17992 76 GSGKTVVAALAMLAAVENGYQVALMA------PTEILAEQHYDSLKKLLEPLGIRVALLTGSTKAKEKREILEKIAsgei 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502304280 131 DVLICTpgrlldHfergKLLMSGVE-----ILVIDEADR--------MLDMGFIPDIeriakmipftrqtLFFSAT 193
Cdd:cd17992 150 DIVIGT------H----ALIQEDVEfhnlgLVIIDEQHRfgveqrlkLREKGETPHV-------------LVMTAT 202
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
30-161 |
6.30e-03 |
|
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an important role in the assembly of the mitochondrial large ribosomal subunit. DHX30 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350734 [Multi-domain] Cd Length: 178 Bit Score: 37.85 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 30 IPTPIQAGAIPFALERRDICGIA-QTGTGKTASfvLPMLsLLEKGRARARMPR--TLILEPTRELAAQVAENF-EKYGKN 105
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISgDTGCGKTTR--IPQF-ILEDYVLRGRGARcnVVITQPRRISAVSVAQRVaHELGPN 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 502304280 106 HRLNValligGVSFEDQDRKLERGADVLICTPGRLLDHFErGKLLMSGVEILVIDE 161
Cdd:cd17976 78 LRRNV-----GYQVRLESRPPPRGGALLFCTVGVLLKKLQ-SNPRLEGVSHVIVDE 127
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
51-201 |
7.72e-03 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain] Cd Length: 186 Bit Score: 37.66 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 51 IAQTGTGKT-ASfvlpmLSLLEKGRARARMPRTLILEPTRELAAQVAENFEKY--GKNHRLNVALLIGGVSFEDQDRKLE 127
Cdd:cd17930 7 EAPTGSGKTeAA-----LLWALKLAARGGKRRIIYALPTRATINQMYERIREIlgRLDDEDKVLLLHSKAALELLESDEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 128 RG------------------ADVLICTPGRLLD------HFE-RGKLLMSGVeiLVIDEAdRMLD---MGFIpdIERIAK 179
Cdd:cd17930 82 PDddpveavdwalllkrswlAPIVVTTIDQLLEsllkykHFErRLHGLANSV--VVLDEV-QAYDpeyMALL--LKALLE 156
|
170 180
....*....|....*....|....*..
gi 502304280 180 M-----IPFtrqtLFFSATMPSEIQKL 201
Cdd:cd17930 157 LlgelgGPV----VLMTATLPALLRDE 179
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
27-200 |
8.44e-03 |
|
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: 37.51 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 27 GYTIPTPIQAGAIPFALERRDICGIAQTGTGKTASFVLPmlSLLEKGrararmpRTLILEPTRELAA-QVAENfekygKN 105
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLP--ALLLDG-------VTLVVSPLISLMQdQVDRL-----QQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 106 HRLNVALLIGGVSFEDQ---DRKLERG-ADVLICTPGRLL--DHFE--RGKLLMSGVEILVIDEADRMLDMG--FIPDIE 175
Cdd:cd17920 75 LGIRAAALNSTLSPEEKrevLLRIKNGqYKLLYVTPERLLspDFLEllQRLPERKRLALIVVDEAHCVSQWGhdFRPDYL 154
|
170 180
....*....|....*....|....*..
gi 502304280 176 RIAKMIPFTR--QTLFFSATMPSEIQK 200
Cdd:cd17920 155 RLGRLRRALPgvPILALTATATPEVRE 181
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
54-164 |
8.91e-03 |
|
DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 37.30 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304280 54 TGTGKT--ASFVlpMLSLLE---KGRArarmprtLILEPTRELAAQVAENFEKYGKNHRLNVALLIGGVSfEDQDRKLER 128
Cdd:cd18033 25 TGLGKTfiAAVV--MLNYYRwfpKGKI-------VFMAPTKPLVSQQIEACYKITGIPSSQTAELTGSVP-PTKRAELWA 94
|
90 100 110
....*....|....*....|....*....|....*.
gi 502304280 129 GADVLICTPGRLLDHFERGKLLMSGVEILVIDEADR 164
Cdd:cd18033 95 SKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHR 130
|
|
| |
