|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
2-418 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 589.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 2 TNTFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLsqqsrEETAPKHPRAL 81
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-----DPSRPRAPQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 82 ILAPTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEAD 161
Cdd:COG0513 76 ILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 162 RMLDMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQVAAANSTADTVKQMVYPVDKKRKSELLAYL 241
Cdd:COG0513 156 RMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 242 IGSRNWQQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDIAQLEQVVN 321
Cdd:COG0513 236 LRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVIN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 322 FDMPYKAEDYVHRIGRTGRAGQTGLAVSFMSRDEEYLLQAIENLLDTRLPQEWLAGFEPSEKENyVEDTSSKRTSRSAEK 401
Cdd:COG0513 316 YDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKR-LERLKPKIKEKLKGK 394
|
410
....*....|....*..
gi 516401488 402 RKLKQKLKIHQGRGKKR 418
Cdd:COG0513 395 KAGRGGRPGPKGERKAR 411
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
4-380 |
1.66e-157 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 452.34 E-value: 1.66e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 4 TFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETAPKHPRALIL 83
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 84 APTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRM 163
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 164 LDMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQVAAANSTADTVKQMVYPVDKKRKSELLAYLIG 243
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 244 SRNWQQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDIAQLEQVVNFD 323
Cdd:PRK10590 242 KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 516401488 324 MPYKAEDYVHRIGRTGRAGQTGLAVSFMSRDEEYLLQAIENLLDTRLPQEWLAGFEP 380
Cdd:PRK10590 322 LPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEP 378
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-384 |
3.25e-126 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 372.60 E-value: 3.25e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 1 MTNT-FIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSqqsreetaPKHPR 79
Cdd:PRK11776 1 MSMTaFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD--------VKRFR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 80 --ALILAPTRELAQQVFDNLKQYAQHAD-LAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILV 156
Cdd:PRK11776 73 vqALVLCPTRELADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 157 LDEADRMLDMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQVAAAnSTADTVKQMVYPVDKKRKSE 236
Cdd:PRK11776 153 LDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVEST-HDLPAIEQRFYEVSPDERLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 237 LLAYLIGSRNWQQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDIAQL 316
Cdd:PRK11776 232 ALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516401488 317 EQVVNFDMPYKAEDYVHRIGRTGRAGQTGLAVSFMSRDEEYLLQAIENLLDTRLPQEWLAGFEPSEKE 384
Cdd:PRK11776 312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGV 379
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
4-418 |
1.87e-124 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 367.35 E-value: 1.87e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 4 TFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETAPkhPRALIL 83
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGP--PRILIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 84 APTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRM 163
Cdd:PRK11192 80 TPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 164 LDMGFLPDIQRIMKRMPEERQTLLFSATFETR-VKALAYRLMKEPVEVQVAAANSTADTVKQMVYPVD-KKRKSELLAYL 241
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADdLEHKTALLCHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 242 IGSRNWQQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDIAQLEQVVN 321
Cdd:PRK11192 240 LKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVIN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 322 FDMPYKAEDYVHRIGRTGRAGQTGLAVSFMSRDEEYLLQAIENLLDTRLPQEWLAGFEPSEKENyVEDTSSKRTSRSAEK 401
Cdd:PRK11192 320 FDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRPKTKAP-SEKKTGKPSKKVLAK 398
|
410
....*....|....*..
gi 516401488 402 RKLKQKLKIHQGRGKKR 418
Cdd:PRK11192 399 RAEKKEKEKEKPKVKKR 415
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
1-373 |
3.54e-109 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 329.57 E-value: 3.54e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 1 MTNTFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLI-QMLSQQSREETAPKHPR 79
Cdd:PRK01297 85 GKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIInQLLQTPPPKERYMGEPR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 80 ALILAPTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQL-AKGVDILIATPGRLLDHLFTKKTSLNQLQILVLD 158
Cdd:PRK01297 165 ALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 159 EADRMLDMGFLPDIQRIMKRMP--EERQTLLFSATFETRVKALAYRLMKEPVEVQVAAANSTADTVKQMVYPVDKKRKSE 236
Cdd:PRK01297 245 EADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 237 LLAYLIGSRNWQQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDIAQL 316
Cdd:PRK01297 325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 516401488 317 EQVVNFDMPYKAEDYVHRIGRTGRAGQTGLAVSFMSRDEEYLLQAIENLLDTRLPQE 373
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCE 461
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
5-363 |
4.12e-109 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 327.70 E-value: 4.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 5 FIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQ-MLSQQSREETAPKHPRALIL 83
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHyLLSHPAPEDRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 84 APTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRM 163
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 164 LDMGFLPDIQRIMKRMPE--ERQTLLFSATFETRVKALAYRLMKEPVEVQVAAANSTADTVKQ-MVYPVDKKrKSELLAY 240
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEeLFYPSNEE-KMRLLQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 241 LIgSRNW-QQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDIAQLEQV 319
Cdd:PRK04837 249 LI-EEEWpDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 516401488 320 VNFDMPYKAEDYVHRIGRTGRAGQTGLAVSFMSrdEEYL--LQAIE 363
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISLAC--EEYAlnLPAIE 371
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
4-372 |
1.44e-107 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 330.27 E-value: 1.44e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 4 TFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSreetapKHPRALIL 83
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPEL------KAPQILVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 84 APTRELAQQVFDNLKQYAQHA-DLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADR 162
Cdd:PRK11634 81 APTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 163 MLDMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQVAAANSTADTVKQMVYPVDKKRKSELLAYLI 242
Cdd:PRK11634 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 243 GSRNWQQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDIAQLEQVVNF 322
Cdd:PRK11634 241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 516401488 323 DMPYKAEDYVHRIGRTGRAGQTGLAVSFMSRDEEYLLQAIENLLDTRLPQ 372
Cdd:PRK11634 321 DIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPE 370
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
4-355 |
3.09e-105 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 321.72 E-value: 3.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 4 TFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETApKHPRALIL 83
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYG-DGPIVLVL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 84 APTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRM 163
Cdd:PTZ00110 210 APTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 164 LDMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKE-PVEVQVAAANSTA-DTVKQMVYPVDKKRKSELLAYL 241
Cdd:PTZ00110 290 LDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQEVFVVEEHEKRGKLKML 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 242 IGS--RNWQQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDIAQLEQV 319
Cdd:PTZ00110 370 LQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYV 449
|
330 340 350
....*....|....*....|....*....|....*.
gi 516401488 320 VNFDMPYKAEDYVHRIGRTGRAGQTGLAVSFMSRDE 355
Cdd:PTZ00110 450 INFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK 485
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
14-211 |
2.67e-104 |
|
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: 2.67e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 14 LSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREEtaPKHPRALILAPTRELAQQV 93
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKK--GRGPQALVLAPTRELAMQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 94 FDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFLPDIQ 173
Cdd:cd00268 79 AEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 516401488 174 RIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQ 211
Cdd:cd00268 159 KILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
4-373 |
1.42e-96 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 300.33 E-value: 1.42e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 4 TFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLI-QMLSQQSREETAPKHPRALI 82
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMnRLLSRPALADRKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 83 LAPTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKT-SLNQLQILVLDEAD 161
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 162 RMLDMGFLPDIQRIMKRMPEE--RQTLLFSATFETRVKALAYRLMKEPVEVQVAAANSTADTVKQMVY-PVDKKRKSELL 238
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYfPADEEKQTLLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 239 AYLIGSRNwQQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDIAQLEQ 318
Cdd:PRK04537 250 GLLSRSEG-ARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 516401488 319 VVNFDMPYKAEDYVHRIGRTGRAGQTGLAVSFMSRDEEYLLQAIENLLDTRLPQE 373
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVE 383
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
4-212 |
2.32e-84 |
|
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: 257.03 E-value: 2.32e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 4 TFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQ-MLSQQSREETAPKH---PR 79
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISkLLEDGPPSVGRGRRkayPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 80 ALILAPTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDE 159
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516401488 160 ADRMLDMGFLPDIQRIM--KRMP--EERQTLLFSATFETRVKALAYRLMKEPVEVQV 212
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVehPDMPpkGERQTLMFSATFPREIQRLAADFLKNYIFLTV 217
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
3-370 |
1.84e-74 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 237.80 E-value: 1.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 3 NTFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREetapkhPRALI 82
Cdd:PTZ00424 28 DSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNA------CQALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 83 LAPTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADR 162
Cdd:PTZ00424 102 LAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 163 MLDMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQVAAANSTADTVKQMVYPVDKKR-KSELLAYL 241
Cdd:PTZ00424 182 MLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEwKFDTLCDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 242 IGSRNWQQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDIAQLEQVVN 321
Cdd:PTZ00424 262 YETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVIN 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 516401488 322 FDMPYKAEDYVHRIGRTGRAGQTGLAVSFMSRDEEYLLQAIENLLDTRL 370
Cdd:PTZ00424 342 YDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQI 390
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
4-398 |
3.93e-74 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 240.46 E-value: 3.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 4 TFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQ-QSREETAPKHPRALI 82
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTiRSGHPSEQRNPLAMV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 83 LAPTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADR 162
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 163 MLDMGFLPDIQRIMKRMPEErQTLLFSATFETRVKALAYRLMKEPVEVQVAAANSTADTVKQMVYPVDKKRKSELLAYLI 242
Cdd:PLN00206 282 MLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDIL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 243 GSRNWQQ--VLVFTKTKQGSDALVSEL-KLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDIAQLEQV 319
Cdd:PLN00206 361 KSKQHFKppAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQV 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 320 VNFDMPYKAEDYVHRIGRTGRAGQTGLAVSFMSRDEEYLLQAIENLLDTR---LPQEWLAgfepSEKENYVEDTSSKRTS 396
Cdd:PLN00206 441 IIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSgaaIPRELAN----SRYLGSGRKRKKKRRY 516
|
..
gi 516401488 397 RS 398
Cdd:PLN00206 517 GS 518
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
3-206 |
3.96e-73 |
|
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: 229.85 E-value: 3.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 3 NTFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETA---PKHPR 79
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSfseVQEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 80 ALILAPTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDE 159
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 516401488 160 ADRMLDMGFLPDIQRIMKR--MP--EERQTLLFSATFETRVKALAYRLMKE 206
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEpgMPskEDRQTLMFSATFPEEIQRLAAEFLKE 253
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
4-211 |
1.80e-70 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 220.65 E-value: 1.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 4 TFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQsreetaPKHPRALIL 83
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN------PQRFFALVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 84 APTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHL-FTKKTSLNQLQILVLDEADR 162
Cdd:cd17954 75 APTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 516401488 163 MLDMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQ 211
Cdd:cd17954 155 LLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
14-210 |
3.00e-69 |
|
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: 218.34 E-value: 3.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 14 LSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSR--EETAPKHPRALILAPTRELAQ 91
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPldEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 92 QVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFLPD 171
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 516401488 172 IQRIMKRMP--------------------EERQTLLFSATFETRVKALAYRLMKEPVEV 210
Cdd:cd17945 161 VTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
18-211 |
4.14e-69 |
|
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: 217.12 E-value: 4.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 18 LSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQqsreeTAPKHP--RALILAPTRELAQQVFD 95
Cdd:cd17947 5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY-----RPKKKAatRVLVLVPTRELAMQCFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 96 NLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLF-TKKTSLNQLQILVLDEADRMLDMGFLPDIQR 174
Cdd:cd17947 80 VLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRnSPSFDLDSIEILVLDEADRMLEEGFADELKE 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 516401488 175 IMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQ 211
Cdd:cd17947 160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
27-199 |
7.11e-68 |
|
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: 212.87 E-value: 7.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 27 TPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSreetapKHPRALILAPTRELAQQVFDNLKQYAQHADL 106
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD------NGPQALVLAPTRELAEQIYEELKKLGKGLGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 107 AIVTVYGGTSIRVQQEQLaKGVDILIATPGRLLDHLFTKKTsLNQLQILVLDEADRMLDMGFLPDIQRIMKRMPEERQTL 186
Cdd:pfam00270 75 KVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
|
170
....*....|...
gi 516401488 187 LFSATFETRVKAL 199
Cdd:pfam00270 153 LLSATLPRNLEDL 165
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
4-211 |
3.71e-67 |
|
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: 213.01 E-value: 3.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 4 TFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQsREETAPKHPRALIL 83
Cdd:cd17953 13 KWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQ-RPVKPGEGPIGLIM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 84 APTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFT---KKTSLNQLQILVLDEA 160
Cdd:cd17953 92 APTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTAnngRVTNLRRVTYVVLDEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 516401488 161 DRMLDMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQ 211
Cdd:cd17953 172 DRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
4-211 |
2.24e-64 |
|
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: 205.23 E-value: 2.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 4 TFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETApkhpRALIL 83
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGA----RALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 84 APTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRM 163
Cdd:cd17959 78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 516401488 164 LDMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQ 211
Cdd:cd17959 158 FEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
10-206 |
3.57e-63 |
|
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: 202.43 E-value: 3.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 10 LDSSLSDHLSQLGFNTPTPIQQQAIPHLLQ-GRDVLAAAQTGTGKTAAYGLPLIQ-MLSQQSREEtaPKHPRALILAPTR 87
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQsLLNTKPAGR--RSGVSALIISPTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 88 ELAQQVFDNLKQYAQHA-DLAIVTVYGGTSIRVQQEQLAK-GVDILIATPGRLLDHL--FTKKTSLNQLQILVLDEADRM 163
Cdd:cd17964 79 ELALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLenPGVAKAFTDLDYLVLDEADRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516401488 164 LDMGFLPDIQRIMKRMP----EERQTLLFSATFETRVKALAYRLMKE 206
Cdd:cd17964 159 LDMGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLKK 205
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
5-211 |
5.52e-63 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 201.68 E-value: 5.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 5 FIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQsreetaPKHPRALILA 84
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSED------PYGIFALVLT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 85 PTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFT---KKTSLNQLQILVLDEAD 161
Cdd:cd17955 75 PTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSsddTTKVLSRVKFLVLDEAD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 516401488 162 RMLDMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQ 211
Cdd:cd17955 155 RLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
16-211 |
4.38e-62 |
|
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: 199.13 E-value: 4.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 16 DHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETApKHPRALILAPTRELAQQVFD 95
Cdd:cd17966 3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERG-DGPIVLVLAPTRELAQQIQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 96 NLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFLPDIQRI 175
Cdd:cd17966 82 EANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKI 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 516401488 176 MKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQ 211
Cdd:cd17966 162 VDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
18-212 |
1.57e-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: 197.51 E-value: 1.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 18 LSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSqqsREE-TAPKHPRALILAPTRELAQQVFDN 96
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLY---RERwTPEDGLGALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 97 LKQYAQHADLAIVTVYGGTSIRVQQEQLAkGVDILIATPGRLLDHL-FTKKTSLNQLQILVLDEADRMLDMGFLPDIQRI 175
Cdd:cd17941 82 LRKVGKYHSFSAGLIIGGKDVKEEKERIN-RMNILVCTPGRLLQHMdETPGFDTSNLQMLVLDEADRILDMGFKETLDAI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 516401488 176 MKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQV 212
Cdd:cd17941 161 VENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
18-210 |
1.75e-61 |
|
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: 197.25 E-value: 1.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 18 LSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQsREETAPKHPRALILAPTRELAQQVFDNL 97
Cdd:cd17952 5 IRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ-RELEKGEGPIAVIVAPTRELAQQIYLEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 98 KQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFLPDIQRIMK 177
Cdd:cd17952 84 KKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVG 163
|
170 180 190
....*....|....*....|....*....|...
gi 516401488 178 RMPEERQTLLFSATFETRVKALAYRLMKEPVEV 210
Cdd:cd17952 164 HVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
18-210 |
4.11e-61 |
|
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: 196.64 E-value: 4.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 18 LSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETaPKHPRALILAPTRELAQQVFDNL 97
Cdd:cd17960 5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLK-KGQVGALIISPTRELATQIYEVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 98 KQYAQHADLAI--VTVYGGTSIRVQQEQL-AKGVDILIATPGRLLDhLFTKKTSLNQ---LQILVLDEADRMLDMGFLPD 171
Cdd:cd17960 84 QSFLEHHLPKLkcQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEE-LLSRKADKVKvksLEVLVLDEADRLLDLGFEAD 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 516401488 172 IQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEV 210
Cdd:cd17960 163 LNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
3-200 |
9.85e-61 |
|
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: 197.18 E-value: 9.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 3 NTFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETAP------- 75
Cdd:cd18051 21 ETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESLPsesgyyg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 76 ---KHPRALILAPTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQL 152
Cdd:cd18051 101 rrkQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYC 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 516401488 153 QILVLDEADRMLDMGFLPDIQRIMKR--MPE--ERQTLLFSATFETRVKALA 200
Cdd:cd18051 181 KYLVLDEADRMLDMGFEPQIRRIVEQdtMPPtgERQTLMFSATFPKEIQMLA 232
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
18-212 |
4.94e-59 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 191.17 E-value: 4.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 18 LSQLGFNTPTPIQQQAIPHLLQG-RDVLAAAQTGTGKTAAYGLPLIQMLSQQsreetapKHPRALILAPTRELAQQVFDN 96
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-------KGGRVLVLVPTRELAEQWAEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 97 LKQYAQHADLAIVTVYGGTSIRVQQEQLAKGV-DILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFLPDIQRI 175
Cdd:smart00487 74 LKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 516401488 176 MKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQV 212
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV 190
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
18-210 |
1.75e-58 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 189.88 E-value: 1.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 18 LSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQ---QSREETApkhprALILAPTRELAQQVF 94
Cdd:cd17942 5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKlkfKPRNGTG-----VIIISPTRELALQIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 95 DNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHL-FTKKTSLNQLQILVLDEADRMLDMGFLPDIQ 173
Cdd:cd17942 80 GVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLqNTKGFLYKNLQCLIIDEADRILEIGFEEEMR 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 516401488 174 RIMKRMPEERQTLLFSATFETRVKALA-YRLMKEPVEV 210
Cdd:cd17942 160 QIIKLLPKRRQTMLFSATQTRKVEDLArISLKKKPLYV 197
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
18-192 |
1.59e-57 |
|
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: 188.60 E-value: 1.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 18 LSQLGFNTPTPIQQQAIPH-LLQGRDVLAAAQTGTGKTAAYGLPLIQ-MLSQQSREETAP--KHPRALILAPTRELAQQV 93
Cdd:cd17946 5 LADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILErLLSQKSSNGVGGkqKPLRALILTPTRELAVQV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 94 FDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLD-------HLftkkTSLNQLQILVLDEADRMLDM 166
Cdd:cd17946 85 KDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWEliqegneHL----ANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 516401488 167 GFLPDIQRIMKRMPEE-------RQTLLFSATF 192
Cdd:cd17946 161 GHFAELEKILELLNKDragkkrkRQTFVFSATL 193
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
5-210 |
2.00e-57 |
|
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: 187.12 E-value: 2.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 5 FIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLsqqsreETAPKHPRALILA 84
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI------DPKKDVIQALILV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 85 PTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRML 164
Cdd:cd17940 75 PTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 516401488 165 DMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEV 210
Cdd:cd17940 155 SQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
18-210 |
2.32e-57 |
|
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: 186.90 E-value: 2.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 18 LSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLP-LIQMLSQQSREETAPKhPRALILAPTRELAQQVFDN 96
Cdd:cd17958 5 IKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLQPIPREQRNG-PGVLVLTPTRELALQIEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 97 LKQYAqHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFLPDIQRIM 176
Cdd:cd17958 84 CSKYS-YKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKIL 162
|
170 180 190
....*....|....*....|....*....|....
gi 516401488 177 KRMPEERQTLLFSATFETRVKALAYRLMKEPVEV 210
Cdd:cd17958 163 LDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
14-208 |
3.12e-57 |
|
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: 187.02 E-value: 3.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 14 LSDHLSQ-LGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETAPKHPRALILAPTRELAQQ 92
Cdd:cd17949 1 LVSHLKSkMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDGTLALVLVPTRELALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 93 VFDNLKQYAQHAdLAIVT--VYGGTSIRVQQEQLAKGVDILIATPGRLLDHL-FTKKTSLNQLQILVLDEADRMLDMGFL 169
Cdd:cd17949 81 IYEVLEKLLKPF-HWIVPgyLIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 516401488 170 PDIQRIMK-------------RMPEERQTLLFSATFETRVKALAYRLMKEPV 208
Cdd:cd17949 160 KDITKILEllddkrskaggekSKPSRRQTVLVSATLTDGVKRLAGLSLKDPV 211
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
14-212 |
8.53e-57 |
|
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: 185.49 E-value: 8.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 14 LSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREetapKHPRALILAPTRELAQQV 93
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKK----KGLRALILAPTRELASQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 94 FDNLKQYAQHADLAIVTVYGGTS-IRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFLPDI 172
Cdd:cd17957 77 YRELLKLSKGTGLRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516401488 173 QRIMKRMPEER-QTLLFSATFETRVKALAYRLMKEPVEVQV 212
Cdd:cd17957 157 DEILAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
222-350 |
1.36e-56 |
|
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: 182.32 E-value: 1.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 222 VKQMVYPVDKKRKSE-LLAYLIGSRNWQQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRA 300
Cdd:cd18787 1 IKQLYVVVEEEEKKLlLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 516401488 301 LIATDVAARGLDIAQLEQVVNFDMPYKAEDYVHRIGRTGRAGQTGLAVSF 350
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITF 130
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
10-208 |
4.97e-56 |
|
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: 183.55 E-value: 4.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 10 LDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETAPKHPRALILAPTREL 89
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 90 AQQVFDNLKQYAQH--ADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSL-NQLQILVLDEADRMLDM 166
Cdd:cd17961 81 AQQVSKVLEQLTAYcrKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 516401488 167 GFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPV 208
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
5-210 |
1.36e-54 |
|
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: 179.82 E-value: 1.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 5 FIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLsqqsreetapkhpRALILA 84
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------------VALILE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 85 PTRELAQQVFDNLKQYAQHAD---LAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEAD 161
Cdd:cd17938 68 PSRELAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 516401488 162 RMLDMGFLPDIQRIMKRMP-----EER-QTLLFSATFE-TRVKALAYRLMKEPVEV 210
Cdd:cd17938 148 RLLSQGNLETINRIYNRIPkitsdGKRlQVIVCSATLHsFEVKKLADKIMHFPTWV 203
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
5-214 |
6.79e-54 |
|
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: 179.05 E-value: 6.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 5 FIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETApKHPRALILA 84
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERG-DGPICLVLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 85 PTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRML 164
Cdd:cd18049 105 PTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 516401488 165 DMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQVAA 214
Cdd:cd18049 185 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
18-210 |
2.22e-51 |
|
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: 171.75 E-value: 2.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 18 LSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLI-QMLSQQSREETAPKH-PRALILAPTRELAQQVFD 95
Cdd:cd17951 5 LKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImFALEQEKKLPFIKGEgPYGLIVCPSRELARQTHE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 96 NLKQYAQHAD------LAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFL 169
Cdd:cd17951 85 VIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516401488 170 PDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEV 210
Cdd:cd17951 165 EDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
16-213 |
2.12e-50 |
|
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: 171.35 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 16 DHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETApKHPRALILAPTRELAQQVFD 95
Cdd:cd18050 75 DVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERG-DGPICLVLAPTRELAQQVQQ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 96 NLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFLPDIQRI 175
Cdd:cd18050 154 VADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKI 233
|
170 180 190
....*....|....*....|....*....|....*...
gi 516401488 176 MKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQVA 213
Cdd:cd18050 234 VDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
7-210 |
2.37e-49 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 165.96 E-value: 2.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 7 ELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREetapkhPRALILAPT 86
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRE------TQALVLAPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 87 RELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDM 166
Cdd:cd17939 75 RELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 516401488 167 GFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEV 210
Cdd:cd17939 155 GFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
10-210 |
1.93e-47 |
|
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: 160.82 E-value: 1.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 10 LDSSLSDHLSQLGFNTPTPIQQQAIPHLLQG--RDVLAAAQTGTGKTAAYglpLIQMLSqqsREETAPKHPRALILAPTR 87
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAF---VLAMLS---RVDPTLKSPQALCLAPTR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 88 ELAQQVFDNLKQYAQHADLAI------VTVYGGTSIRVQqeqlakgvdILIATPGRLLDHLFTKKTSLNQLQILVLDEAD 161
Cdd:cd17963 75 ELARQIGEVVEKMGKFTGVKValavpgNDVPRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEAD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 516401488 162 RMLDM-GFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEV 210
Cdd:cd17963 146 VMLDTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
14-210 |
1.63e-46 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 158.48 E-value: 1.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 14 LSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIqmlsqqSREETAPKHPRALILAPTRELAQQV 93
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVI------IRCLTEHRNPSALILTPTRELAVQI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 94 FDNLKQYAQ-HADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFLPDI 172
Cdd:cd17962 75 EDQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQV 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 516401488 173 QRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEV 210
Cdd:cd17962 155 LDILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
5-212 |
2.86e-45 |
|
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: 155.58 E-value: 2.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 5 FIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLsqqsreETAPKHPRALILA 84
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL------EPVDGQVSVLVIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 85 PTRELAQQVFDNLKQYAQH-ADLAIVTVYGGTSIRVQQEQLAKGV-DILIATPGRLLDHLFTKKTSLNQLQILVLDEADR 162
Cdd:cd17950 78 HTRELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 516401488 163 ML-DMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQV 212
Cdd:cd17950 158 MLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
14-191 |
8.61e-45 |
|
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: 155.10 E-value: 8.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 14 LSDHLSQLGFNTPTPIQQQAIPHLLQG---------RDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETapkhpRALILA 84
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRL-----RALIVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 85 PTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKG--------VDILIATPGRLLDHL-FTKKTSLNQLQIL 155
Cdd:cd17956 76 PTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLnSTPGFTLKHLRFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 516401488 156 VLDEADRMLDMGF---LPDIQRIMKRMPEER-----------------QTLLFSAT 191
Cdd:cd17956 156 VIDEADRLLNQSFqdwLETVMKALGRPTAPDlgsfgdanllersvrplQKLLFSAT 211
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
5-210 |
3.49e-44 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 152.60 E-value: 3.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 5 FIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLsqqsreETAPKHPRALILA 84
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI------DTSLKATQALVLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 85 PTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRML 164
Cdd:cd18046 75 PTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEML 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 516401488 165 DMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEV 210
Cdd:cd18046 155 SRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
28-209 |
2.25e-42 |
|
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: 148.07 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 28 PIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETAPKHPRALILAPTRELAQQVFDNLKQYAQhaDLA 107
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 108 IVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFLPDIQRIM----KRMPEER 183
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsyKKDSEDN 172
|
170 180
....*....|....*....|....*..
gi 516401488 184 -QTLLFSATFETRVKALAYRLMKEPVE 209
Cdd:cd17944 173 pQTLLFSATCPDWVYNVAKKYMKSQYE 199
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
18-211 |
1.94e-41 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 145.10 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 18 LSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSReetapkHPRALILAPTRELAQQVFDNL 97
Cdd:cd17943 5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERR------HPQVLILAPTREIAVQIHDVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 98 KQYAQHADLAIVTVY-GGTSIRVQQEQLaKGVDILIATPGRLLdHLFtKKTSLN--QLQILVLDEADRMLDMGFLPDIQR 174
Cdd:cd17943 79 KKIGKKLEGLKCEVFiGGTPVKEDKKKL-KGCHIAVGTPGRIK-QLI-ELGALNvsHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 516401488 175 IMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEVQ 211
Cdd:cd17943 156 IFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
5-210 |
2.90e-40 |
|
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: 142.22 E-value: 2.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 5 FIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREetapkhPRALILA 84
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRE------TQALILS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 85 PTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRML 164
Cdd:cd18045 75 PTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEML 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 516401488 165 DMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEPVEV 210
Cdd:cd18045 155 NKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
14-196 |
2.03e-38 |
|
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: 138.27 E-value: 2.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 14 LSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQ-MLSQQSREETAPKHPRALILAPTRELAQQ 92
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQrLLRYKLLAEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 93 VFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFLPDI 172
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 516401488 173 QRIMKRMP---------EER----QTLLFSATFETRV 196
Cdd:cd17948 161 SHFLRRFPlasrrsentDGLdpgtQLVLVSATMPSGV 197
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
14-191 |
5.29e-33 |
|
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: 124.41 E-value: 5.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 14 LSDHLSQLGFNTPTPIQQQAIPHLLQ---------------GRDV-LAAAQTGTGKTAAYGLPLIQMLSQQSRE------ 71
Cdd:cd17965 19 LKGSNKTDEEIKPSPIQTLAIKKLLKtlmrkvtkqtsneepKLEVfLLAAETGSGKTLAYLAPLLDYLKRQEQEpfeeae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 72 ---ETAPKH--PRALILAPTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLA--KGVDILIATPGRLLDHLFT 144
Cdd:cd17965 99 eeyESAKDTgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLAfkGRIDILVTTPGKLASLAKS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516401488 145 KKTSLNQLQILVLDEADRMLDMGFLPDIQRIMKRMPEERQTLLFSAT 191
Cdd:cd17965 179 RPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSAT 225
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
4-207 |
7.16e-32 |
|
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: 120.90 E-value: 7.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 4 TFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQG--RDVLAAAQTGTGKTAAYGLPLIqmlsqqSREETAPKHPRAL 81
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML------SRVDALKLYPQCL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 82 ILAPTRELAQQVFDNLKQYAQHADlAIVTVYGgtsirVQQEQLAKGVD----ILIATPGRLLDHLFTKK-TSLNQLQILV 156
Cdd:cd18048 93 CLSPTFELALQTGKVVEEMGKFCV-GIQVIYA-----IRGNRPGKGTDieaqIVIGTPGTVLDWCFKLRlIDVTNISVFV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 516401488 157 LDEADRMLDM-GFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEP 207
Cdd:cd18048 167 LDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
234-342 |
7.25e-32 |
|
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: 116.93 E-value: 7.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 234 KSELLAYLIGSRNWQQVLVFTKTKQGSDALVSeLKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDI 313
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 516401488 314 AQLEQVVNFDMPYKAEDYVHRIGRTGRAG 342
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
261-342 |
1.21e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 99.21 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 261 DALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATDVAARGLDIAQLEQVVNFDMPYKAEDYVHRIGRTGR 340
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 516401488 341 AG 342
Cdd:smart00490 81 AG 82
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
9-367 |
1.49e-24 |
|
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: 106.07 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 9 GLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSReetapkhPRALILAPTRE 88
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPG-------ATALYLYPTKA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 89 LAQ-QVfDNLKQYAQHADLAI-VTVYGGTSIRVQQEQLAKGVDILIATP-----GRLLDH-----LFTKktslnqLQILV 156
Cdd:COG1205 113 LARdQL-RRLRELAEALGLGVrVATYDGDTPPEERRWIREHPDIVLTNPdmlhyGLLPHHtrwarFFRN------LRYVV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 157 LDEA---------------DRMldmgflpdiQRIMKRMPEERQTLLFSATfetrV---KALAYRLMKEPVEVqVaaANST 218
Cdd:COG1205 186 IDEAhtyrgvfgshvanvlRRL---------RRICRHYGSDPQFILASAT----IgnpAEHAERLTGRPVTV-V--DEDG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 219 ADTVKQMVY----PVDKK--RKS------ELLAYLIGSRnwQQVLVFTKTKQGSDALVSELK------LDGIKAASINGD 280
Cdd:COG1205 250 SPRGERTFVlwnpPLVDDgiRRSalaeaaRLLADLVREG--LRTLVFTRSRRGAELLARYARralrepDLADRVAAYRAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 281 KSQGARQKALDDFKSGKVRALIATDVAARGLDIAQLEQVVNFDMPYKAEDYVHRIGRTGRAGQTGLAVsFMSRDE---EY 357
Cdd:COG1205 328 YLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGDDpldQY 406
|
410
....*....|
gi 516401488 358 LLQAIENLLD 367
Cdd:COG1205 407 YVRHPEELFE 416
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
4-207 |
7.52e-23 |
|
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: 95.56 E-value: 7.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 4 TFIELGLDSSLSDHLSQLGFNTPTPIQQQAIPHLLQG--RDVLAAAQTGTGKTAAYGLPLIqmlsqqSREETAPKHPRAL 81
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAML------SQVEPANKYPQCL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 82 ILAPTRELAQQ---VFDNLKQYAQHADLAIVtvyggtsirVQQEQLAKGV----DILIATPGRLLDHLFTKK-TSLNQLQ 153
Cdd:cd18047 76 CLSPTYELALQtgkVIEQMGKFYPELKLAYA---------VRGNKLERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516401488 154 ILVLDEADRML-DMGFLPDIQRIMKRMPEERQTLLFSATFETRVKALAYRLMKEP 207
Cdd:cd18047 147 VFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
40-191 |
1.12e-21 |
|
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: 90.54 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 40 GRDVLAAAQTGTGKTAAYGLPLIQmlsqqsreETAPKHPRALILAPTRELAQQVFDNLKQYAQHaDLAIVTVYGGTSIRV 119
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALL--------LLLKKGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516401488 120 QQEQLAKGVDILIATPGRLL-DHLFTKKTSLNQLQILVLDEADRMLDMGF--LPDIQRIMKRMPEERQTLLFSAT 191
Cdd:cd00046 72 REKNKLGDADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRgaLILDLAVRKAGLKNAQVILLSAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
25-385 |
1.70e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 84.31 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 25 TPTPIQQQAI----PHLLQGRD--VLAAAqTGTGKT--AAYglpLIQMLSQQsreetapkhPRALILAPTRELAQQVFDN 96
Cdd:COG1061 80 ELRPYQQEALeallAALERGGGrgLVVAP-TGTGKTvlALA---LAAELLRG---------KRVLVLVPRRELLEQWAEE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 97 LKQYaqhadLAIVTVYGGTSirvqqeqlAKGVDILIATPgrlldHLFTKKTSLNQLQ----ILVLDEADRMLDMGFlpdi 172
Cdd:COG1061 147 LRRF-----LGDPLAGGGKK--------DSDAPITVATY-----QSLARRAHLDELGdrfgLVIIDEAHHAGAPSY---- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 173 QRIMKRMPEERqTLLFSAT------------------FETRVKALA---------YRLMKEPVEVQVAAANSTADTVKQM 225
Cdd:COG1061 205 RRILEAFPAAY-RLGLTATpfrsdgreillflfdgivYEYSLKEAIedgylappeYYGIRVDLTDERAEYDALSERLREA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 226 VYPVDKKRKSELLAYLIGSRNWQQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIATD 305
Cdd:COG1061 284 LAADAERKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVD 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 306 VAARGLDIAQLEQVVnFDMPYKAE-DYVHRIGR---TGRAGQTGLAVSFMSRDEEYLLQAIENLLDTRLPQEWLAGFEPS 381
Cdd:COG1061 364 VLNEGVDVPRLDVAI-LLRPTGSPrEFIQRLGRglrPAPGKEDALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEES 442
|
....
gi 516401488 382 EKEN 385
Cdd:COG1061 443 EELA 446
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
236-414 |
1.02e-15 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 79.39 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 236 ELLAYLIGSRNWQQVLVFTKTKQGSDALVSELKLDGIKA------ASINGDK--SQGARQKALDDFKSGKVRALIATDVA 307
Cdd:COG1111 342 EILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDKglTQKEQIEILERFRAGEFNVLVATSVA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 308 ARGLDIAQLEQVVNFDMPYKAEDYVHRIGRTGRAGQtGLAVSFM---SRDEEYL-------------LQAIENLLDTR-- 369
Cdd:COG1111 422 EEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKRE-GRVVVLIakgTRDEAYYwssrrkekkmksiLKKLKKLLDKQek 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 516401488 370 -----LPQEWLAGFEPSEKENYVEDTSSKR---TSRSAEKRKLKQKLKIHQGR 414
Cdd:COG1111 501 eklkeSAQATLDEFESIKELAEDEINEKDLdeiESSENGAHVDWREPVLLQVI 553
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
25-191 |
5.17e-13 |
|
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: 66.90 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 25 TPTPIQQQAIPHL-LQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSReetapkhpRALILAPTRELAQQVFDNLKQYAQH 103
Cdd:cd17921 1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSGG--------KAVYIAPTRALVNQKEADLRERFGP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 104 ADLAIVTVYGGTSIRVQQEQLAkgvDILIATPGRLLDHL-FTKKTSLNQLQILVLDEAdRMLDMG----FLPDIQRIMKR 178
Cdd:cd17921 73 LGKNVGLLTGDPSVNKLLLAEA---DILVATPEKLDLLLrNGGERLIQDVRLVVVDEA-HLIGDGergvVLELLLSRLLR 148
|
170
....*....|...
gi 516401488 179 MPEERQTLLFSAT 191
Cdd:cd17921 149 INKNARFVGLSAT 161
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
13-160 |
2.11e-12 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 68.77 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 13 SLSDHLSQLGFNTPTPIQQQAIP-HLLQGRDVLAAAQTGTGKTAayglpLIQMLSQQsreeTAPKHPRALILAPTRELAQ 91
Cdd:COG1204 10 KVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTL-----IAELAILK----ALLNGGKALYIVPLRALAS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 92 QVFDNLKQYAQHADLAIVTVYGGTSIRvqqEQLAKGVDILIATPGRlLDHLFTKKTS-LNQLQILVLDEA 160
Cdd:COG1204 81 EKYREFKRDFEELGIKVGVSTGDYDSD---DEWLGRYDILVATPEK-LDSLLRNGPSwLRDVDLVVVDEA 146
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
23-135 |
2.71e-12 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 68.59 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 23 FNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKT-AAYgLPLIQMLSQQSREETAPKHPRALILAPTRELAQQVFDNLKQ-- 99
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGLRVLYISPLKALANDIERNLRApl 100
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 516401488 100 ----YAQHADLAIVTV---YGGTSIRVQQEQLAKGVDILIATP 135
Cdd:COG1201 101 eeigEAAGLPLPEIRVgvrTGDTPASERQRQRRRPPHILITTP 143
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
30-160 |
4.50e-12 |
|
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: 64.14 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 30 QQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSReetapkhPRALILAPTRELAQQVFDNLKQYAQHADLAI- 108
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPG-------SRALYLYPTKALAQDQLRSLRELLEQLGLGIr 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 516401488 109 VTVYGG-TSIRVQQEQLAKGVDILIATPgRLLDHLFTK-----KTSLNQLQILVLDEA 160
Cdd:cd17923 78 VATYDGdTPREERRAIIRNPPRILLTNP-DMLHYALLPhhdrwARFLRNLRYVVLDEA 134
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
49-410 |
4.03e-11 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 64.89 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 49 TGTGKTAayglplIQMLSQQSREETAPKhpRALILAPTRELAQQVFDNLKQYAQHADLAIVTVYGGTSIRVQQEQLAKGv 128
Cdd:PRK13766 38 TGLGKTA------IALLVIAERLHKKGG--KVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKRAELWEKA- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 129 DILIATPGRLLDHLFTKKTSLNQLQILVLDEADR----------------------MLDMGFLP--DIQRIMK------- 177
Cdd:PRK13766 109 KVIVATPQVIENDLIAGRISLEDVSLLIFDEAHRavgnyayvyiaeryhedaknplVLGLTASPgsDEEKIKEvcenlgi 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 178 ---------------------------RMPEERQTL--LFSATFETRVKALA---------------------------- 200
Cdd:PRK13766 189 ehvevrteddpdvkpyvhkvkiewvrvELPEELKEIrdLLNEALKDRLKKLKelgvivsispdvskkellglqkklqqei 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 201 -------YRLMK------------EPVEVQ------------VAAANSTADT-----------VKQMVYPVDK------- 231
Cdd:PRK13766 269 anddsegYEAISilaeamklrhavELLETQgvealrrylerlREEARSSGGSkaskrlvedprFRKAVRKAKEldiehpk 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 232 -KRKSELLAYLIGSRNWQQVLVFTKTKQGSDALVSELKLDGIKA------ASINGDK--SQGARQKALDDFKSGKVRALI 302
Cdd:PRK13766 349 lEKLREIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 303 ATDVAARGLDIAQLEQVVnFDMPYKAE-DYVHRIGRTGRaGQTGLAVSFMS---RDEEYL-------------LQAIENL 365
Cdd:PRK13766 429 STSVAEEGLDIPSVDLVI-FYEPVPSEiRSIQRKGRTGR-QEEGRVVVLIAkgtRDEAYYwssrrkekkmkeeLKNLKGI 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 516401488 366 LDTRL-PQEWLAGFEPSEKENYVEDTSSKRTSRSAEKRKLKQKLKI 410
Cdd:PRK13766 507 LNKKLqELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKD 552
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
10-373 |
5.09e-11 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 64.39 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 10 LDSSLSDHLSQL-GFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAY--------GL-----PLIqmlsqqsreetap 75
Cdd:COG0514 1 LRDDALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYqlpalllpGLtlvvsPLI------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 76 khprALIlaptrelAQQVfDNLKQYAQHAdlaiVTVYGGTSIRVQQE---QLAKG-VDILIATPGRLLDHLFTKKtsLNQ 151
Cdd:COG0514 68 ----ALM-------KDQV-DALRAAGIRA----AFLNSSLSAEERREvlrALRAGeLKLLYVAPERLLNPRFLEL--LRR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 152 LQI--LVLDEA--------DrmldmgFLPD---IQRIMKRMPEeRQTLLFSATFETRVKA-LAYRL-MKEPVEVQvaaan 216
Cdd:COG0514 130 LKIslFAIDEAhcisqwghD------FRPDyrrLGELRERLPN-VPVLALTATATPRVRAdIAEQLgLEDPRVFV----- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 217 STAD------TVKQMVypvDKKRKSELLAYLIGSRNwQQVLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKAL 290
Cdd:COG0514 198 GSFDrpnlrlEVVPKP---PDDKLAQLLDFLKEHPG-GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 291 DDFKSGKVRALIATdVA-ARGLDIAQLEQVVNFDMPYKAEDYVHRIGRTGRAGQTGLAVSFMSRDEEYLLqaiENLLDTR 369
Cdd:COG0514 274 DRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQ---RFFIEQS 349
|
....
gi 516401488 370 LPQE 373
Cdd:COG0514 350 PPDE 353
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
237-336 |
4.42e-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: 57.49 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 237 LLAYLIGSRNWQQ-VLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFK--SGKVRALIATDVAARGLDI 313
Cdd:cd18793 16 LLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGGVGLNL 95
|
90 100
....*....|....*....|....*....
gi 516401488 314 AQLEQVVNFDMPYK------AEDYVHRIG 336
Cdd:cd18793 96 TAANRVILYDPWWNpaveeqAIDRAHRIG 124
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
23-135 |
2.21e-09 |
|
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: 56.98 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 23 FNTptpIQQQAIPHLLQG-RDVLAAAQTGTGKTAAYGLPLIQMLSQqsREETAPKHPRALILAPTRELAQQVFDNLKQYA 101
Cdd:cd18023 2 FNR---IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKE--RNPLPWGNRKVVYIAPIKALCSEKYDDWKEKF 76
|
90 100 110
....*....|....*....|....*....|....
gi 516401488 102 QHADLAIVTVYGGTSIRVQQEqlAKGVDILIATP 135
Cdd:cd18023 77 GPLGLSCAELTGDTEMDDTFE--IQDADIILTTP 108
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
251-341 |
2.62e-09 |
|
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: 55.29 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 251 LVFTKTKQGSDALVS-----ELKLDGIKAASI----NGDKSQGA-----RQK-ALDDFKSGKVRALIATDVAARGLDIAQ 315
Cdd:cd18802 29 IIFVERRATAVVLSRllkehPSTLAFIRCGFLigrgNSSQRKRSlmtqrKQKeTLDKFRDGELNLLIATSVLEEGIDVPA 108
|
90 100
....*....|....*....|....*.
gi 516401488 316 LEQVVNFDMPYKAEDYVHRIGRtGRA 341
Cdd:cd18802 109 CNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
40-159 |
7.44e-09 |
|
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: 54.51 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 40 GRDVLAAAQTGTGKTAAYGLPLIQMLSQQSreetaPKHPRALILAPTRELAQQVFDNLKQYAQHADLAI-VTV-YGGTSI 117
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEP-----EKGVQVLYISPLKALINDQERRLEEPLDEIDLEIpVAVrHGDTSQ 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 516401488 118 RVQQEQLAKGVDILIATPGRL--------LDHLFTkktslnQLQILVLDE 159
Cdd:cd17922 76 SEKAKQLKNPPGILITTPESLelllvnkkLRELFA------GLRYVVVDE 119
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
29-162 |
1.15e-08 |
|
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: 54.44 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 29 IQQQAIPHLLQGRDVLAAAQTGTGKTaayglpLIQMLSQQSREETapKHPRALILAPTRELAQQVFDNLKQYAQHADLaI 108
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKT------IIAILVAADRLTK--KGGKVLILAPSRPLVEQHAENLKRVLNIPDK-I 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 516401488 109 VTVYGGTSIRVQQEQLAKGvDILIATPGRLLDHLFTKKTSLNQLQILVLDEADR 162
Cdd:cd18035 76 TSLTGEVKPEERAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
25-160 |
1.80e-08 |
|
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: 54.19 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 25 TPTPIQQQAIPHLLQgRDVLAAAQTGTGKT--AAYglpLIQMLSQQSREETAPKhPRALILAPTRELAQQVFdnlKQYAQ 102
Cdd:cd18034 2 TPRSYQLELFEAALK-RNTIVVLPTGSGKTliAVM---LIKEMGELNRKEKNPK-KRAVFLVPTVPLVAQQA---EAIRS 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516401488 103 HADLAIVTVYGGTSI-----RVQQEQLAKgVDILIATPGRLLDHLFTKKTSLNQLQILVLDEA 160
Cdd:cd18034 74 HTDLKVGEYSGEMGVdkwtkERWKEELEK-YDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
23-344 |
3.39e-08 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 55.66 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 23 FNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSREETAPKHPRALILAPTRELAQQVFDNLKQ--- 99
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGELEDKVYCLYVSPLRALNNDIHRNLEEplt 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 100 --YAQHADL---------AIVTvyGGTSIRVQQEQLAKGVDILIATPGRLLDHL----FTKKtsLNQLQILVLDEADRML 164
Cdd:PRK13767 110 eiREIAKERgeelpeirvAIRT--GDTSSYEKQKMLKKPPHILITTPESLAILLnspkFREK--LRTVKWVIVDEIHSLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 165 D-------MGFLPDIQRIMKRMPeerQTLLFSAT---FETRVKALA-YRLMKEPVEVQVAAANSTADTVKQMVYPVD--- 230
Cdd:PRK13767 186 EnkrgvhlSLSLERLEELAGGEF---VRIGLSATiepLEEVAKFLVgYEDDGEPRDCEIVDARFVKPFDIKVISPVDdli 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 231 -------KKRKSELLAYLIGS-RNwqqVLVFTKTKQGSDALVSELK--------LDGIKAAsiNGDKSQGARQKALDDFK 294
Cdd:PRK13767 263 htpaeeiSEALYETLHELIKEhRT---TLIFTNTRSGAERVLYNLRkrfpeeydEDNIGAH--HSSLSREVRLEVEEKLK 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 516401488 295 SGKVRALIATDVAARGLDIAQLEQVVNFDMPYKAEDYVHRIGRTG-RAGQT 344
Cdd:PRK13767 338 RGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAGhRLGEV 388
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
18-163 |
3.72e-08 |
|
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: 52.80 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 18 LSQLGFnTPTPIQQQAIPHLLQG------RDVLAAAQTGTGKTAAYGLPLIQMLSqqsreetapKHPRALILAPTRELAQ 91
Cdd:cd17918 9 CKSLPF-SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAYK---------NGKQVAILVPTEILAH 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516401488 92 QVFDNLKQYaqHADLAIVTVYGGTsirvqQEQLAKGVDILIATPGRLldHLFTKKTSLNqlqILVLDEADRM 163
Cdd:cd17918 79 QHYEEARKF--LPFINVELVTGGT-----KAQILSGISLLVGTHALL--HLDVKFKNLD---LVIVDEQHRF 138
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
225-343 |
8.41e-08 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 50.67 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 225 MVYPVDKKRKSELLAYLIGSRNWQQ-VLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGKVRALIA 303
Cdd:cd18794 7 SVRPKDKKDEKLDLLKRIKVEHLGGsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVA 86
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 516401488 304 TdVA-ARGLDIAQLEQVVNFDMPYKAEDYVHRIGRTGRAGQ 343
Cdd:cd18794 87 T-VAfGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGL 126
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
248-340 |
9.44e-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: 50.82 E-value: 9.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 248 QQVLVFTKTKQGSDALVSELK--LDGIKAASI----NGDKSQGARQK----ALDDFKSGKVRALIATDVAARGLDIAQLE 317
Cdd:cd18801 31 TRVIIFSEFRDSAEEIVNFLSkiRPGIRATRFigqaSGKSSKGMSQKeqkeVIEQFRKGGYNVLVATSIGEEGLDIGEVD 110
|
90 100
....*....|....*....|...
gi 516401488 318 QVVNFDMPYKAEDYVHRIGRTGR 340
Cdd:cd18801 111 LIICYDASPSPIRMIQRMGRTGR 133
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
209-340 |
4.88e-07 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 49.18 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 209 EVQVAAANSTADTVKQMVYPVDKKRKSELLAYLIGSRNwqqVLVFTKTKQGSDALVSELK------LDGIKAASINGDKS 282
Cdd:cd18796 3 KLDIKVILPVAPEIFPWAGESGADAYAEVIFLLERHKS---TLVFTNTRSQAERLAQRLRelcpdrVPPDFIALHHGSLS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 516401488 283 QGARQKALDDFKSGKVRALIATDVAARGLDIAQLEQVVNFDMPYKAEDYVHRIGRTGR 340
Cdd:cd18796 80 RELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
247-345 |
8.62e-07 |
|
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: 46.16 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 247 WQQVLVFTKTKQGSDALVSELKLdgikaasingdksqgarqkalddfksgkvraLIATDVAARGLDIAQLEQVVNFDMPY 326
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASSLEI-------------------------------LVATNVLGEGIDVPSLDTVIFFDPPS 51
|
90
....*....|....*....
gi 516401488 327 KAEDYVHRIGRTGRAGQTG 345
Cdd:cd18785 52 SAASYIQRVGRAGRGGKDE 70
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
235-348 |
1.30e-06 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 47.64 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 235 SELLAYLIgsRNWQQVLVFTKTKQGSDALVSELKLDGIKA-------ASINGDKSQGARQKALDDFKSGKVRALIATDVA 307
Cdd:cd18797 25 ARLFADLV--RAGVKTIVFCRSRKLAELLLRYLKARLVEEgplaskvASYRAGYLAEDRREIEAELFNGELLGVVATNAL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 516401488 308 ARGLDIAQLEQVVNFDMPYKAEDYVHRIGRTGRAGQTGLAV 348
Cdd:cd18797 103 ELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
25-162 |
1.65e-06 |
|
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: 48.58 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 25 TPTPIQQQAIPHLLQGRDVLAAAQTGTGKTaayglpLIQMLSQQSREETAPKHP--RALILAPTRELAQQVFDNLKQYAQ 102
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKT------FVAVLICEHHLKKFPAGRkgKVVFLANKVPLVEQQKEVFRKHFE 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516401488 103 HADLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFT-KKTSLNQLQILVLDEADR 162
Cdd:cd17927 76 RPGYKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
26-191 |
1.88e-06 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L 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: 350785 [Multi-domain] Cd Length: 179 Bit Score: 48.03 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 26 PTPIQQQAIPHLLQGRDVLAAAQTGTGKT--AAYGLPLIQmlsqqsreetapKH-PRALILAPTRELAQQVFDNLKQyaq 102
Cdd:cd18027 9 LDVFQKQAILHLEAGDSVFVAAHTSAGKTvvAEYAIALAQ------------KHmTRTIYTSPIKALSNQKFRDFKN--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 103 hadlaivtVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRMLDMGFLPDIQRIMKRMPEE 182
Cdd:cd18027 74 --------TFGDVGLITGDVQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDH 145
|
....*....
gi 516401488 183 RQTLLFSAT 191
Cdd:cd18027 146 VSIILLSAT 154
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
250-338 |
3.11e-06 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 49.45 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 250 VLVFTKTKQGSDALVSELKLDGIKAASINGDKSQGARQKALDDFKSGK--VRALIATDVAARGLDIAQLEQVVNFDMPY- 326
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLWWn 631
|
90
....*....|....*..
gi 516401488 327 -----KAEDYVHRIGRT 338
Cdd:COG0553 632 paveeQAIDRAHRIGQT 648
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
21-203 |
4.06e-06 |
|
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: 46.94 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 21 LGFNtPTPIQQQAIPHLLQGRDVLAAAQTGTGKT---AAYGLPLiqmlsqqsreetAPKHPRALILAPTRELAQQVFDNL 97
Cdd:cd17924 14 TGFP-PWGAQRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSLYL------------ASKGKRSYLIFPTKSLVKQAYERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 98 KQYAQHADLA--IVTVYGGTSIRVQQEQL----AKGVDILIATPGRLLDHLftKKTSLNQLQILVLDEADRMLDMGflPD 171
Cdd:cd17924 81 SKYAEKAGVEvkILVYHSRLKKKEKEELLekieKGDFDILVTTNQFLSKNF--DLLSNKKFDFVFVDDVDAVLKSS--KN 156
|
170 180 190
....*....|....*....|....*....|...
gi 516401488 172 IQRIMKrMPEERQTLLFSATFETR-VKALAYRL 203
Cdd:cd17924 157 IDRLLK-LLGFGQLVVSSATGRPRgIRPLLFRE 188
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
21-196 |
4.17e-06 |
|
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: 47.25 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 21 LGFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPlIQMLSQQSREETapkhpraLILAPTRELAQ-QVfDNL-- 97
Cdd:cd18018 8 FGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLP-ALLLRRRGPGLT-------LVVSPLIALMKdQV-DALpr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 98 --KQYAQHADLAivtvygGTSIRVQQEQLAKG-VDILIATPGRLLDHLFTKKT-SLNQLQILVLDEADRMLDMG--FLPD 171
Cdd:cd18018 79 aiKAAALNSSLT------REERRRILEKLRAGeVKILYVSPERLVNESFRELLrQTPPISLLVVDEAHCISEWShnFRPD 152
|
170 180
....*....|....*....|....*...
gi 516401488 172 ---IQRIMKRMPEERQTLLFSATFETRV 196
Cdd:cd18018 153 ylrLCRVLRELLGAPPVLALTATATKRV 180
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
22-211 |
5.81e-06 |
|
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: 46.76 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 22 GFNTPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLP-LIqmlsqqsreetapKHPRALILAPTRELAQ-QVfDNLKQ 99
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPaLL-------------LDGVTLVVSPLISLMQdQV-DRLQQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 100 YAQHAdlaiVTVYGGTSIRVQQEQLAK----GVDILIATPGRLL-DHLFT---KKTSLNQLQILVLDEADRMLDMG--FL 169
Cdd:cd17920 75 LGIRA----AALNSTLSPEEKREVLLRikngQYKLLYVTPERLLsPDFLEllqRLPERKRLALIVVDEAHCVSQWGhdFR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 516401488 170 PDIQRI--MKRMPEERQTLLFSATFETRVKALAYRL--MKEPVEVQ 211
Cdd:cd17920 151 PDYLRLgrLRRALPGVPILALTATATPEVREDILKRlgLRNPVIFR 196
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
23-135 |
1.12e-05 |
|
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: 45.71 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 23 FNtptPIQQQAIPHLLQGRD-VLAAAQTGTGKTAAYGLPLIQMLSQQsreetaPKHpRALILAPTRELAQQVFDNL-KQY 100
Cdd:cd18021 4 FN---PIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAELALLRHWRQN------PKG-RAVYIAPMQELVDARYKDWrAKF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 516401488 101 AQHADLAIVTVYGGTSirVQQEQLAKGvDILIATP 135
Cdd:cd18021 74 GPLLGKKVVKLTGETS--TDLKLLAKS-DVILATP 105
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
25-193 |
1.20e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 45.36 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 25 TPTPIQQQAIPHLLQGRD-----VLAAAQTGTGKTAAYgLPLIQMLSQQSREEtapkhpRALILAPTRELAQQVFDNLKQ 99
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKngqkrGLIVMATGSGKTLTA-AKLIARLFKKGPIK------KVLFLVPRKDLLEQALEEFKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 100 YAqHADLAIVTVYGGTSIRVQQEQlakgVDILIATPGRL--LDHLFTKKTSLNQLQILVLDEADRMLDMGFlpdiQRIMK 177
Cdd:pfam04851 76 FL-PNYVEIGEIISGDKKDESVDD----NKIVVTTIQSLykALELASLELLPDFFDVIIIDEAHRSGASSY----RNILE 146
|
170
....*....|....*.
gi 516401488 178 RMPEERQtLLFSATFE 193
Cdd:pfam04851 147 YFKPAFL-LGLTATPE 161
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
28-209 |
4.35e-05 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain] Cd Length: 177 Bit Score: 43.86 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 28 PIQQQAIPH-LLQGRDVLAAAQTGTGKTAaygLPLIQMLSqqsreeTAPKHPRALILAPTRELAQQVFDNLKQYAQHA-D 105
Cdd:cd18028 4 PPQAEAVRAgLLKGENLLISIPTASGKTL---IAEMAMVN------TLLEGGKALYLVPLRALASEKYEEFKKLEEIGlK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 106 LAIVTvyggTSIRVQQEQLAKgVDILIATPGRlLDHLFTKKTS-LNQLQILVLDEADRMLDMGFLPDIQRI---MKRMPE 181
Cdd:cd18028 75 VGIST----GDYDEDDEWLGD-YDIIVATYEK-FDSLLRHSPSwLRDVGVVVVDEIHLISDEERGPTLESIvarLRRLNP 148
|
170 180
....*....|....*....|....*...
gi 516401488 182 ERQTLLFSATFeTRVKALAYRLMKEPVE 209
Cdd:cd18028 149 NTQIIGLSATI-GNPDELAEWLNAELVE 175
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
226-375 |
9.52e-05 |
|
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: 42.68 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 226 VYPVDKKRKSELLAYL--IGSrnwqQVLVFTKT---KQGSDALVSELKLDGIKAASINGDksqgaRQKALDDFKSGKVRA 300
Cdd:cd18798 5 VYIEDSDSLEKLLELVkkLGD----GGLIFVSIdygKEYAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEIDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 301 LIAT----DVAARGLDIAQ-LEQVVNFDMPYKAedYVHRIGRTGR--AGQTGLAVSFMSRDEEYLLQAIENLLDTRLPQE 373
Cdd:cd18798 76 LIGVasyyGVLVRGIDLPErIKYAIFYGVPVTT--YIQASGRTSRlyAGGLTKGLSVVLVDDPELFEALKKRLKLILDEF 153
|
..
gi 516401488 374 WL 375
Cdd:cd18798 154 IF 155
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
233-343 |
1.13e-04 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 42.24 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 233 RKSELLAYLIGS-RNWQQVLVFTKTKQGSDALVSELKLDGIkaasiNGDKSQGARQKALDDFKSGKVRALIATDVAARGL 311
Cdd:cd18789 34 NKLRALEELLKRhEQGDKIIVFTDNVEALYRYAKRLLKPFI-----TGETPQSEREEILQNFREGEYNTLVVSKVGDEGI 108
|
90 100 110
....*....|....*....|....*....|...
gi 516401488 312 DIAQLEQVVNFDMPYKAE-DYVHRIGRTGRAGQ 343
Cdd:cd18789 109 DLPEANVAIQISGHGGSRrQEAQRLGRILRPKK 141
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1-54 |
1.74e-04 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 43.77 E-value: 1.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 516401488 1 MTNT-FIELGLDSSLSDHLSQLGFnTPTPIQQQAIPHLLQGRDVLAAAQTGTGKT 54
Cdd:COG4581 1 MTLSpARADARLEALADFAEERGF-ELDPFQEEAILALEAGRSVLVAAPTGSGKT 54
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
28-192 |
2.14e-04 |
|
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: 41.14 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 28 PIQQQAIPHLLQ----GRDVLAAAqTGTGKTAAyGLPLIQMLSQqsreetapkhPRALILAPTRELAQQVFDNLKQYAQH 103
Cdd:cd17926 3 PYQEEALEAWLAhknnRRGILVLP-TGSGKTLT-ALALIAYLKE----------LRTLIVVPTDALLDQWKERFEDFLGD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 104 ADLAIVtvyGGTSIRVQqeqlaKGVDILIATPGRLLDHLFTKKTSLNQLQILVLDEADRmldmgfLPDIQ--RIMKRMPE 181
Cdd:cd17926 71 SSIGLI---GGGKKKDF-----DDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH------LPAKTfsEILKELNA 136
|
170
....*....|.
gi 516401488 182 ERQtLLFSATF 192
Cdd:cd17926 137 KYR-LGLTATP 146
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
47-376 |
4.59e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 42.60 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 47 AQTGTGKTAAYGLPLIQMLSQQSREETAPKHPRA----LILAPTRELAQQVFDNLK--------QYAQHADLAIVTVYG- 113
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFREGGEDTREAHKRKtsriLYISPIKALGTDVQRNLQiplkgiadERRRRGETEVNLRVGi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 114 --GTSIRVQQEQLAKG-VDILIATPGRLLDHLFTK-KTSLNQLQILVLDE----ADRMLDMGFLPDIQRIMKRMPEERQT 185
Cdd:PRK09751 83 rtGDTPAQERSKLTRNpPDILITTPESLYLMLTSRaRETLRGVETVIIDEvhavAGSKRGAHLALSLERLDALLHTSAQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 186 LLFSATFETRVKALAYRLMKEPVEVqVAAANSTADTVKqMVYPVDKKRKSELLAYLIGSRN--------WQQV------- 250
Cdd:PRK09751 163 IGLSATVRSASDVAAFLGGDRPVTV-VNPPAMRHPQIR-IVVPVANMDDVSSVASGTGEDShagregsiWPYIetgilde 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 251 -------LVFTKTKQGSDALVSELK--------------LDGIKAASING---DKSQGA----------------RQKAL 290
Cdd:PRK09751 241 vlrhrstIVFTNSRGLAEKLTARLNelyaarlqrspsiaVDAAHFESTSGatsNRVQSSdvfiarshhgsvskeqRAITE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 291 DDFKSGKVRALIATDVAARGLDIAQLEQVVNFDMPYKAEDYVHRIGRTGR---AGQTGLAVSFMSRD--------EEYLL 359
Cdd:PRK09751 321 QALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHqvgGVSKGLFFPRTRRDlvdsavivECMFA 400
|
410
....*....|....*..
gi 516401488 360 QAIENLLDTRLPQEWLA 376
Cdd:PRK09751 401 GRLENLTPPHNPLDVLA 417
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
25-159 |
1.21e-03 |
|
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: 39.77 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 25 TPTPIQQQAIPHLLQGRDVLAAAQTGTGKTAAYGLPLIQMLSQQSReetAPKHPRALILAPTRELAQQVFDNLKQYAQHA 104
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRS---AGEKGRVVVLVNKVPLVEQQLEKFFKYFRKG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 516401488 105 dLAIVTVYGGTSIRVQQEQLAKGVDILIATPGRLLDHLFT----KKTSLNQLQILVLDE 159
Cdd:cd18036 79 -YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSgreeERVYLSDFSLLIFDE 136
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
37-172 |
2.44e-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: 39.05 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 37 LLQGrDVlaaaqtGTGKTAAYGLPLIQMLSQ--QsreetapkhprALILAPTRELAQQVFDNLKQYAQHADLAIVTVYGG 114
Cdd:cd17992 70 LLQG-DV------GSGKTVVAALAMLAAVENgyQ-----------VALMAPTEILAEQHYDSLKKLLEPLGIRVALLTGS 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516401488 115 TSI---RVQQEQLAKG-VDILIATpgrlldH-LFTKKTSLNQLQILVLDEADR--------MLDMGFLPDI 172
Cdd:cd17992 132 TKAkekREILEKIASGeIDIVIGT------HaLIQEDVEFHNLGLVIIDEQHRfgveqrlkLREKGETPHV 196
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
18-159 |
3.12e-03 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 39.75 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 18 LSQLGFnTPTPIQQQAI---------PH----LLQGrDVlaaaqtGTGKTA-AyglpLIQMLSqqsreeTAPKHPRALIL 83
Cdd:PRK10917 255 LASLPF-ELTGAQKRVVaeiladlasPKpmnrLLQG-DV------GSGKTVvA----ALAALA------AIEAGYQAALM 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 84 APTRELAQQVFDNLKQYAQHADLAIVTVYGGTSI---RVQQEQLAKG-VDILIATpgrlldH-LFTKKTSLNQLQILVLD 158
Cdd:PRK10917 317 APTEILAEQHYENLKKLLEPLGIRVALLTGSLKGkerREILEAIASGeADIVIGT------HaLIQDDVEFHNLGLVIID 390
|
.
gi 516401488 159 E 159
Cdd:PRK10917 391 E 391
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
7-191 |
3.73e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 39.56 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 7 ELGLDSSLSDHLSQLGFNTPTPIQQQAIPH-LLQGRDVLAAAQTGTGKTaayglpLI---QMLSQQSREETapkhprALI 82
Cdd:PRK02362 5 ELPLPEGVIEFYEAEGIEELYPPQAEAVEAgLLDGKNLLAAIPTASGKT------LIaelAMLKAIARGGK------ALY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516401488 83 LAPTRELAQQVFDNLKQYAQHA-DLAIVTvyGGTSIRvqQEQLAKGvDILIATPGRlLDHLFTKKTS-LNQLQILVLDE- 159
Cdd:PRK02362 73 IVPLRALASEKFEEFERFEELGvRVGIST--GDYDSR--DEWLGDN-DIIVATSEK-VDSLLRNGAPwLDDITCVVVDEv 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 516401488 160 -----ADR--MLDMgflpDIQRIMKRMPeERQTLLFSAT 191
Cdd:PRK02362 147 hlidsANRgpTLEV----TLAKLRRLNP-DLQVVALSAT 180
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
251-320 |
5.49e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 36.38 E-value: 5.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516401488 251 LVFTKTKQGSDALVSELKLDGIKAASINGDKSQGAR-QKALDDFKSG--KVRALIATDVAARGLDIAQLEQVV 320
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| |
