|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-412 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 622.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 1 MSFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQntstspaRHQVRG 80
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR-------PRAPQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 81 LILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEA 160
Cdd:COG0513 75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 161 DRMLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIEVARRNATADTVTQVAYPVANDHKRRLLAQ 240
Cdd:COG0513 155 DRMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 241 IIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGLDIDDLPCVV 320
Cdd:COG0513 235 LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 321 NFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYLSDIEKLIKRAIPLEALPGY-GAERLAEAPGKDRYRERTNER 399
Cdd:COG0513 315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFePVEEKRLERLKPKIKEKLKGK 394
|
410
....*....|...
gi 1082644987 400 ArpvVARSVEPEP 412
Cdd:COG0513 395 K---AGRGGRPGP 404
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-378 |
0e+00 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 522.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 1 MSFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQntSTSPARHQVRG 80
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQ--PHAKGRRPVRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 81 LILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEA 160
Cdd:PRK10590 79 LILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 161 DRMLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIEVARRNATADTVTQVAYPVANDHKRRLLAQ 240
Cdd:PRK10590 159 DRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 241 IIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGLDIDDLPCVV 320
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082644987 321 NFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYLSDIEKLIKRAIPLEALPGY 378
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGY 376
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-376 |
1.47e-132 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 390.32 E-value: 1.47e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 1 MSFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLavhqntstSPARHQVRG 80
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--------DVKRFRVQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 81 LILAPTRELAAQVEASVRTYS------KYLSLrstsvYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEF 154
Cdd:PRK11776 76 LVLCPTRELADQVAKEIRRLArfipniKVLTL-----CGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 155 LVLDEADRMLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIEVARRNAtADTVTQVAYPVANDHK 234
Cdd:PRK11776 151 LVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHD-LPAIEQRFYEVSPDER 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 235 RRLLAQIIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGLDID 314
Cdd:PRK11776 230 LPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082644987 315 DLPCVVNFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYLSDIEKLIKRAIPLEALP 376
Cdd:PRK11776 310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLP 371
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-390 |
3.28e-112 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 338.81 E-value: 3.28e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 3 FESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLavhQNTSTSPARH--QVRG 80
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQL---LQTPPPKERYmgEPRA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 81 LILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELR-RGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDE 159
Cdd:PRK01297 166 LIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 160 ADRMLDMGFMPDIRRIFSYLPPR--RQNLLFSATFAEEIKRLASDFMHDPQLIEVARRNATADTVTQVAYPVANDHKRRL 237
Cdd:PRK01297 246 ADRMLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 238 LAQIIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGLDIDDLP 317
Cdd:PRK01297 326 LYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGIS 405
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082644987 318 CVVNFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYLSDIEKLIKRAIPLEALPgygAERLAEAPGKD 390
Cdd:PRK01297 406 HVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPP---AELLKPVPRKH 475
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
2-373 |
2.15e-111 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 339.06 E-value: 2.15e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 2 SFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLhklaVHQNtstspARHQVRG- 80
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAI----VHIN-----AQPLLRYg 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 81 -----LILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFL 155
Cdd:PTZ00110 202 dgpivLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 156 VLDEADRMLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFM-HDPQLIEVARRNATA-DTVTQVAYPVANDH 233
Cdd:PTZ00110 282 VLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDLTAcHNIKQEVFVVEEHE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 234 KR----RLLAQIIKNEDlkQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAAR 309
Cdd:PTZ00110 362 KRgklkMLLQRIMRDGD--KILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASR 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082644987 310 GLDIDDLPCVVNFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYLSDIEKLIKRA---IPLE 373
Cdd:PTZ00110 440 GLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAkqpVPPE 506
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
1-370 |
6.54e-110 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 331.52 E-value: 6.54e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 1 MSFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTSTSPARHqvrg 80
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRI---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 81 LILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEA 160
Cdd:PRK11192 77 LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 161 DRMLDMGFMPDIRRIFSYLPPRRQNLLFSATF-AEEIKRLASDFMHDPQLIEVARRNATADTVTQVAYPVAN-DHKRRLL 238
Cdd:PRK11192 157 DRMLDMGFAQDIETIAAETRWRKQTLLFSATLeGDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDlEHKTALL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 239 AQIIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGLDIDDLPC 318
Cdd:PRK11192 237 CHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSH 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1082644987 319 VVNFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYLSDIEKLIKRAI 370
Cdd:PRK11192 317 VINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPL 368
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-211 |
1.15e-105 |
|
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: 311.68 E-value: 1.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLavhqNTSTSPARHQVRGLILAPTRELAA 91
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKL----LPEPKKKGRGPQALVLAPTRELAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 92 QVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLDMGFMPD 171
Cdd:cd00268 77 QIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEED 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1082644987 172 IRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIE 211
Cdd:cd00268 157 VEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-389 |
2.44e-104 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 323.34 E-value: 2.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 1 MSFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHklavhqNTSTSPARHQVrg 80
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLH------NLDPELKAPQI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 81 LILAPTRELAAQVEASVRTYSKYL-SLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDE 159
Cdd:PRK11634 78 LVLAPTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 160 ADRMLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIEVARRNATADTVTQVAYPVANDHKRRLLA 239
Cdd:PRK11634 158 ADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 240 QIIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGLDIDDLPCV 319
Cdd:PRK11634 238 RFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082644987 320 VNFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYLSDIEKLIKRAIPLEALPG---YGAERLAEAPGK 389
Cdd:PRK11634 318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNaelLGKRRLEKFAAK 390
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
3-402 |
4.80e-101 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 308.44 E-value: 4.80e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 3 FESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQnTSTSPARHQVRGLI 82
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHP-APEDRKVNQPRALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 83 LAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADR 162
Cdd:PRK04837 89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 163 MLDMGFMPDIRRIFSYLPP--RRQNLLFSATFAEEIKRLASDFMHDPQLIEVARRNATADTVTQ-VAYPvANDHKRRLLA 239
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEeLFYP-SNEEKMRLLQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 240 QIIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGLDIDDLPCV 319
Cdd:PRK04837 248 TLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 320 VNFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYLSDIEKLIKRAIPLEAlpgYGAERLAE---APgKDRYRERT 396
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSK---YDSDALLTdlpKP-LRLTRPRT 403
|
....*.
gi 1082644987 397 NERARP 402
Cdd:PRK04837 404 GNGPRR 409
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-442 |
6.03e-92 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 289.54 E-value: 6.03e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 1 MSFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKL----AVHQNTSTSParh 76
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpALADRKPEDP--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 77 qvRGLILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQ-KSVNLSQVEFL 155
Cdd:PRK04537 86 --RALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEIC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 156 VLDEADRMLDMGFMPDIRRIFSYLPPR--RQNLLFSATFAEEIKRLASDFMHDPQLIEVARRNATADTVTQVAYPVANDH 233
Cdd:PRK04537 164 VLDEADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 234 KRRLLAQIIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGLDI 313
Cdd:PRK04537 244 KQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 314 DDLPCVVNFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYLSDIEKLIKRAIPLEALPgygAERLAEAPgkdryr 393
Cdd:PRK04537 324 DGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPVT---AELLTPLP------ 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1082644987 394 eRTNERARPVVARSVEPEPSVQYVPEPSVEITEIPEIKRAPIRRPGQKR 442
Cdd:PRK04537 395 -RPPRVPVEGEEADDEAGDSVGTIFREAREQRAAEEQRRGGGRSGPGGG 442
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
2-206 |
2.81e-89 |
|
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: 270.90 E-value: 2.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 2 SFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTSTSPARHQV--R 79
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRRKAypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 80 GLILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDE 159
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1082644987 160 ADRMLDMGFMPDIRRIFSY--LPPR--RQNLLFSATFAEEIKRLASDFMHD 206
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdMPPKgeRQTLMFSATFPREIQRLAADFLKN 211
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
2-383 |
2.71e-81 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 256.68 E-value: 2.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 2 SFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTStsparhQVrgL 81
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNAC------QA--L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 82 ILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEAD 161
Cdd:PTZ00424 101 ILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 162 RMLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIEVARRNATADTVTQVAYPV-ANDHKRRLLAQ 240
Cdd:PTZ00424 181 EMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVeKEEWKFDTLCD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 241 IIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGLDIDDLPCVV 320
Cdd:PTZ00424 261 LYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVI 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082644987 321 NFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYLSDIEKLIKRAIplEALPGYGAERL 383
Cdd:PTZ00424 341 NYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQI--EEMPMEVADYL 401
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-205 |
2.32e-79 |
|
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: 247.19 E-value: 2.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 1 MSFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTSTSPARHQ-VR 79
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQePQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 80 GLILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDE 159
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082644987 160 ADRMLDMGFMPDIRRIFSYL--PP--RRQNLLFSATFAEEIKRLASDFMH 205
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEPgmPSkeDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
12-207 |
2.32e-75 |
|
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: 234.57 E-value: 2.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLhklaVHQNTStsPARHQVRG---LILAPTRE 88
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAI----VHINAQ--PPLERGDGpivLVLAPTRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 89 LAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLDMGF 168
Cdd:cd17966 75 LAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGF 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1082644987 169 MPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDP 207
Cdd:cd17966 155 EPQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDY 193
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
1-373 |
2.96e-74 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 242.00 E-value: 2.96e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 1 MSFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTSTSPARHQVrG 80
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEQRNPL-A 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 81 LILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEA 160
Cdd:PLN00206 200 MVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 161 DRMLDMGFMPDIRRIFSYLpPRRQNLLFSATFAEEIKRLASDFMHDPQLIEVARRNATADTVTQVAYPVANDHKRRLLAQ 240
Cdd:PLN00206 280 DCMLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFD 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 241 IIKNED--LKQVLIFTNTKTGANRLAHQL-MHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGLDIDDLP 317
Cdd:PLN00206 359 ILKSKQhfKPPAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVR 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082644987 318 CVVNFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYLSDIEKLIKR---AIPLE 373
Cdd:PLN00206 439 QVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSsgaAIPRE 497
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
12-207 |
2.06e-73 |
|
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: 229.45 E-value: 2.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAvhqntsTSPARHQV-RGLILAPTRELA 90
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLL------YRPKKKAAtRVLVLVPTRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 91 AQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQ-KSVNLSQVEFLVLDEADRMLDMGFM 169
Cdd:cd17947 75 MQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFA 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1082644987 170 PDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDP 207
Cdd:cd17947 155 DELKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKP 192
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
2-210 |
1.06e-70 |
|
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: 222.57 E-value: 1.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 2 SFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTSTsparhqVRGL 81
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVG------ARAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 82 ILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEAD 161
Cdd:cd17959 76 ILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEAD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1082644987 162 RMLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLI 210
Cdd:cd17959 156 RLFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
6-212 |
3.00e-69 |
|
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: 219.56 E-value: 3.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 6 LGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLaVHQNTSTsPARHQVrGLILAP 85
Cdd:cd17953 17 CGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHI-KDQRPVK-PGEGPI-GLIMAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 86 TRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHL---HQKSVNLSQVEFLVLDEADR 162
Cdd:cd17953 94 TRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082644987 163 MLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPqlIEV 212
Cdd:cd17953 174 MFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP--IEI 221
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
12-207 |
5.53e-69 |
|
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: 218.05 E-value: 5.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLhkLAVHQNTSTSPARHQVrGLILAPTRELAA 91
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPML--VHIMDQRELEKGEGPI-AVIVAPTRELAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 92 QVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLDMGFMPD 171
Cdd:cd17952 78 QIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQ 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1082644987 172 IRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDP 207
Cdd:cd17952 158 VRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDP 193
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
3-211 |
5.75e-69 |
|
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: 218.25 E-value: 5.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 3 FESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLavhqntSTSParHQVRGLI 82
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL------SEDP--YGIFALV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 83 LAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSV---NLSQVEFLVLDE 159
Cdd:cd17955 73 LTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttkVLSRVKFLVLDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1082644987 160 ADRMLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIE 211
Cdd:cd17955 153 ADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
2-214 |
5.92e-68 |
|
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: 217.22 E-value: 5.92e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 2 SFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKL-------AVHQNTSTSPA 74
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgeSLPSESGYYGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 75 RHQV-RGLILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVE 153
Cdd:cd18051 102 RKQYpLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082644987 154 FLVLDEADRMLDMGFMPDIRRIFSY--LPPR--RQNLLFSATFAEEIKRLASDFMHDPQLIEVAR 214
Cdd:cd18051 182 YLVLDEADRMLDMGFEPQIRRIVEQdtMPPTgeRQTLMFSATFPKEIQMLARDFLDNYIFLAVGR 246
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
3-210 |
2.43e-66 |
|
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: 211.39 E-value: 2.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 3 FESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLavhqntstSPARHQVRGLI 82
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI--------DPKKDVIQALI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 83 LAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADR 162
Cdd:cd17940 73 LVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1082644987 163 MLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLI 210
Cdd:cd17940 153 LLSQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
2-211 |
4.99e-65 |
|
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: 207.94 E-value: 4.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 2 SFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAvhqntsTSPARHQVrgL 81
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALL------ENPQRFFA--L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 82 ILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHL-HQKSVNLSQVEFLVLDEA 160
Cdd:cd17954 73 VLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1082644987 161 DRMLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIE 211
Cdd:cd17954 153 DRLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
1-206 |
6.24e-63 |
|
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: 203.70 E-value: 6.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 1 MSFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLhklaVHQNtstsparHQV-- 78
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAI----VHIN-------HQPfl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 79 -RG-----LILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQV 152
Cdd:cd18049 93 eRGdgpicLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRC 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082644987 153 EFLVLDEADRMLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHD 206
Cdd:cd18049 173 TYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
25-199 |
2.37e-62 |
|
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: 199.78 E-value: 2.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 25 TPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNtstsparhQVRGLILAPTRELAAQVEASVRTYSKYL 104
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN--------GPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 105 SLRSTSVYGGVHIDPQIAELRrGVEILVATPGRLLDHLhQKSVNLSQVEFLVLDEADRMLDMGFMPDIRRIFSYLPPRRQ 184
Cdd:pfam00270 73 GLKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLL-QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQ 150
|
170
....*....|....*
gi 1082644987 185 NLLFSATFAEEIKRL 199
Cdd:pfam00270 151 ILLLSATLPRNLEDL 165
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
12-207 |
1.07e-61 |
|
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: 199.85 E-value: 1.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLavhqntSTSPARHQV------RGLILAP 85
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYI------SRLPPLDEEtkddgpYALILAP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 86 TRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLD 165
Cdd:cd17945 75 TRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMID 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082644987 166 MGFMPDIRRIFSYLPP--------------------RRQNLLFSATFAEEIKRLASDFMHDP 207
Cdd:cd17945 155 MGFEPQVTKILDAMPVsnkkpdteeaeklaasgkhrYRQTMMFTATMPPAVEKIAKGYLRRP 216
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
8-211 |
3.53e-60 |
|
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: 195.49 E-value: 3.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 8 LSPDILRAIADAGYTEPTPIQAQAIPVVLS-GKDVMAGAQTGTGKTASFTLPMLHKLAvhqNTSTSPARHQVRGLILAPT 86
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLL---NTKPAGRRSGVSALIISPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 87 RELAAQVEASVRTYSKYL-SLRSTSVYGGVHIDPQIAELRR-GVEILVATPGRLLDHLHQKSV--NLSQVEFLVLDEADR 162
Cdd:cd17964 78 RELALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082644987 163 MLDMGFMPDIRRIFSYLPPR----RQNLLFSATFAEEIKRLASDFM-HDPQLIE 211
Cdd:cd17964 158 LLDMGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTLkKDYKFID 211
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
3-208 |
4.21e-60 |
|
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: 195.23 E-value: 4.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 3 FESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLhklavhqntstsparHQVRGLI 82
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL---------------QIVVALI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 83 LAPTRELAAQVEASVRTYSKYL---SLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDE 159
Cdd:cd17938 66 LEPSRELAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082644987 160 ADRMLDMGFMPDIRRIFSYLPP------RRQNLLFSATF-AEEIKRLASDFMHDPQ 208
Cdd:cd17938 146 ADRLLSQGNLETINRIYNRIPKitsdgkRLQVIVCSATLhSFEVKKLADKIMHFPT 201
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-207 |
3.03e-59 |
|
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: 192.80 E-value: 3.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTstsparHQVRGLILAPTRELAA 91
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKK------KGLRALILAPTRELAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 92 QVEASVRTYSKYLSLRSTSVYGGVH-IDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLDMGFMP 170
Cdd:cd17957 75 QIYRELLKLSKGTGLRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFRE 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1082644987 171 DIRRIFSYLP-PRRQNLLFSATFAEEIKRLASDFMHDP 207
Cdd:cd17957 155 QTDEILAACTnPNLQRSLFSATIPSEVEELARSVMKDP 192
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
12-210 |
3.34e-59 |
|
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: 192.68 E-value: 3.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLhklaVHQNTSTSPaRHQVRG---LILAPTRE 88
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF----IHLDLQPIP-REQRNGpgvLVLTPTRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 89 LAAQVEASVRTYSkYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLDMGF 168
Cdd:cd17958 76 LALQIEAECSKYS-YKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1082644987 169 MPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLI 210
Cdd:cd17958 155 EPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
8-207 |
1.02e-58 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 191.64 E-value: 1.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 8 LSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAvhQNTSTSPARHQVRGLILAPTR 87
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIL--KAKAESGEEQGTRALILVPTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 88 ELAAQVEASVRTYSKYLS--LRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKS-VNLSQVEFLVLDEADRML 164
Cdd:cd17961 79 ELAQQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSlLLLSTLKYLVIDEADLVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1082644987 165 DMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDP 207
Cdd:cd17961 159 SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
12-213 |
3.58e-58 |
|
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: 192.53 E-value: 3.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLhklaVHQNtstsparHQV---RG-----LIL 83
Cdd:cd18050 73 VMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAI----VHIN-------HQPyleRGdgpicLVL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 84 APTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRM 163
Cdd:cd18050 142 APTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRM 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082644987 164 LDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIEVA 213
Cdd:cd18050 222 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
12-207 |
6.39e-58 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 189.32 E-value: 6.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLavhQNTSTSPARHQVRGLILAPTRELAA 91
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEIL---LKRKANLKKGQVGALIISPTRELAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 92 QVEASVRTYSKYLS--LRSTSVYGGVHIDPQIAELRR-GVEILVATPGRLLDHLH--QKSVNLSQVEFLVLDEADRMLDM 166
Cdd:cd17960 78 QIYEVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1082644987 167 GFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDP 207
Cdd:cd17960 158 GFEADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNP 198
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
20-210 |
9.03e-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: 9.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 20 GYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLavhQNTSTSPARHQ-VRGLILAPTRELAAQV-EASV 97
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRL---LSLEPRVDRSDgTLALVLVPTRELALQIyEVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 98 RTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHL-HQKSVNLSQVEFLVLDEADRMLDMGFMPDIRRIF 176
Cdd:cd17949 87 KLLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1082644987 177 SYL-------------PPRRQNLLFSATFAEEIKRLASDFMHDPQLI 210
Cdd:cd17949 167 ELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
222-351 |
1.13e-55 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 181.17 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 222 VTQVAYPVANDHKR-RLLAQIIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRA 300
Cdd:cd18787 1 IKQLYVVVEEEEKKlLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1082644987 301 LVATDIAARGLDIDDLPCVVNFELPHSAEDYVHRVGRTGRAGISGKAISLV 351
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
12-212 |
2.59e-55 |
|
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: 182.49 E-value: 2.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTSTSparhQVRGLILAPTRELAA 91
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPED----GLGALIISPTRELAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 92 QVEASVRTYSKYLSLRSTSVYGGVHIDpqiAELRR--GVEILVATPGRLLDHLHQK-SVNLSQVEFLVLDEADRMLDMGF 168
Cdd:cd17941 77 QIFEVLRKVGKYHSFSAGLIIGGKDVK---EEKERinRMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGF 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1082644987 169 MPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIEV 212
Cdd:cd17941 154 KETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
12-207 |
6.85e-55 |
|
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: 181.77 E-value: 6.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLhKLAVHQNTSTsPARHQ--VRGLILAPTREL 89
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI-MFALEQEKKL-PFIKGegPYGLIVCPSREL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 90 AAQVEASVRTYSKYLS------LRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRM 163
Cdd:cd17951 79 ARQTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1082644987 164 LDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDP 207
Cdd:cd17951 159 IDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKP 202
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
16-225 |
1.81e-54 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 180.38 E-value: 1.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 16 IADAGYTEPTPIQAQAIPVVLSG-KDVMAGAQTGTGKTASFTLPMLHKLAVHQNTSTsparhqvrgLILAPTRELAAQVE 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---------LVLVPTRELAEQWA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 95 ASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGV-EILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLDMGFMPDIR 173
Cdd:smart00487 72 EELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1082644987 174 RIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPqlIEVARRNATADTVTQV 225
Cdd:smart00487 152 KLLKLLPKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
2-212 |
2.52e-52 |
|
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: 175.23 E-value: 2.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 2 SFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLavhqntstSPARHQVRGL 81
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL--------EPVDGQVSVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 82 ILAPTRELAAQVEASVRTYSKYL-SLRSTSVYGGVHIDPQIAELRRGV-EILVATPGRLLDHLHQKSVNLSQVEFLVLDE 159
Cdd:cd17950 75 VICHTRELAFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082644987 160 ADRMLDMGFM-PDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIEV 212
Cdd:cd17950 155 CDKMLEQLDMrRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
12-194 |
1.66e-51 |
|
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: 173.96 E-value: 1.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPV-VLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQ--NTSTSPARHqVRGLILAPTRE 88
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKssNGVGGKQKP-LRALILTPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 89 LAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDhLHQKS----VNLSQVEFLVLDEADRML 164
Cdd:cd17946 80 LAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWE-LIQEGnehlANLKSLRFLVLDEADRML 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1082644987 165 DMGFMPDIRRIFSYLP-------PRRQNLLFSATFAE 194
Cdd:cd17946 159 EKGHFAELEKILELLNkdragkkRKRQTFVFSATLTL 195
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
6-210 |
4.77e-51 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 171.35 E-value: 4.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 6 LGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQntstsparHQVRGLILAP 85
Cdd:cd17939 2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTV--------RETQALVLAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 86 TRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLD 165
Cdd:cd17939 74 TRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1082644987 166 MGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLI 210
Cdd:cd17939 154 RGFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
12-200 |
3.93e-49 |
|
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: 166.38 E-value: 3.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLP---MLHKLAVHQNTSTSparhqvrGLILAPTRE 88
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKFKPRNGTG-------VIIISPTRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 89 LAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKS----VNLsqvEFLVLDEADRML 164
Cdd:cd17942 74 LALQIYGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNL---QCLIIDEADRIL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1082644987 165 DMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLA 200
Cdd:cd17942 151 EIGFEEEMRQIIKLLPKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
16-210 |
7.12e-49 |
|
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: 165.80 E-value: 7.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 16 IADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHK-LAVHQNTStsparhqvrGLILAPTRELAAQVE 94
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRcLTEHRNPS---------ALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 95 ASVRTYSK-YLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLDMGFMPDIR 173
Cdd:cd17962 76 DQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1082644987 174 RIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLI 210
Cdd:cd17962 156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
12-211 |
1.23e-48 |
|
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: 164.74 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNtstsparhQVRGLILAPTRELAA 91
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERR--------HPQVLILAPTREIAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 92 QVEASVRTYSKYLSLRSTSVY-GGVHIDPQIAELRRgVEILVATPGRLLdHLHQKSV-NLSQVEFLVLDEADRMLDMGFM 169
Cdd:cd17943 73 QIHDVFKKIGKKLEGLKCEVFiGGTPVKEDKKKLKG-CHIAVGTPGRIK-QLIELGAlNVSHVRLFVLDEADKLMEGSFQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1082644987 170 PDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIE 211
Cdd:cd17943 151 KDVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
3-210 |
2.73e-47 |
|
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: 161.87 E-value: 2.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 3 FESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLhklavhqnTSTSPARHQVRGLI 82
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL--------QCLDIQVRETQALI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 83 LAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADR 162
Cdd:cd18045 73 LSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1082644987 163 MLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLI 210
Cdd:cd18045 153 MLNKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
3-210 |
2.38e-46 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 159.15 E-value: 2.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 3 FESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNtstsparhQVRGLI 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLK--------ATQALV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 83 LAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADR 162
Cdd:cd18046 73 LAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1082644987 163 MLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLI 210
Cdd:cd18046 153 MLSRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
8-210 |
8.92e-46 |
|
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: 157.35 E-value: 8.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 8 LSPDILRAIADAGYTEPTPIQAQAIPVVLSG--KDVMAGAQTGTGKTASFTLPMLHKLavhqntstSPARHQVRGLILAP 85
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV--------DPTLKSPQALCLAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 86 TRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPqiaelRRGVE--ILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRM 163
Cdd:cd17963 73 TRELARQIGEVVEKMGKFTGVKVALAVPGNDVPR-----GKKITaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVM 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1082644987 164 LDM-GFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLI 210
Cdd:cd17963 148 LDTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
20-204 |
2.95e-40 |
|
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: 143.06 E-value: 2.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 20 GYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTSTSPARHQVrgLILAPTRELAAQVEASVRT 99
Cdd:cd17944 9 GVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKV--LVLAPTRELANQVTKDFKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 100 YSKYLSLrsTSVYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLDMGFMPDIRRIFS-- 177
Cdd:cd17944 87 ITRKLSV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvs 164
|
170 180 190
....*....|....*....|....*....|
gi 1082644987 178 YLPPRRQN---LLFSATFAEEIKRLASDFM 204
Cdd:cd17944 165 YKKDSEDNpqtLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
12-210 |
7.73e-35 |
|
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: 129.67 E-value: 7.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSG---------KDVMAGAQTGTGKTASFTLPMLHKLavhqntSTSPARhQVRGLI 82
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQAL------SKRVVP-RLRALI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 83 LAPTRELAAQVEASVRTYSKYLSLRSTSVYGGVHIDPQIAELRRG--------VEILVATPGRLLDHLHQ-KSVNLSQVE 153
Cdd:cd17956 74 VVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNStPGFTLKHLR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082644987 154 FLVLDEADRMLDMGF-------------------MPDIRRIFSYLPPRR-QNLLFSATFAEEIKRLASDFMHDPQLI 210
Cdd:cd17956 154 FLVIDEADRLLNQSFqdwletvmkalgrptapdlGSFGDANLLERSVRPlQKLLFSATLTRDPEKLSSLKLHRPRLF 230
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
12-202 |
1.66e-33 |
|
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: 125.94 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 12 ILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTSTSPARHqVRGLILAPTRELAA 91
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNA-PRGLVITPSRELAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 92 QVEASVRTYSKYLSLRSTSVYGGvHIDPQIAELRRG-VEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLDMGFMP 170
Cdd:cd17948 80 QIGSVAQSLTEGLGLKVKVITGG-RTKRQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1082644987 171 DIRRIFSYLP-------------PRRQNLLFSATFAEEIKRLASD 202
Cdd:cd17948 159 KLSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSK 203
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
234-342 |
9.08e-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: 117.31 E-value: 9.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 234 KRRLLAQIIKNEDLKQVLIFTNTKtgaNRLAHQLMH--EDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGL 311
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTK---KTLEAELLLekEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 1082644987 312 DIDDLPCVVNFELPHSAEDYVHRVGRTGRAG 342
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
2-218 |
1.61e-28 |
|
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: 112.42 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 2 SFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSG--KDVMAGAQTGTGKTASFTLPMLHKLAVHQntsTSParhqvR 79
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALK---LYP-----Q 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 80 GLILAPTRELAAQVEASVRTYSKY-------LSLRSTSVYGGVHIDPQiaelrrgveILVATPGRLLDHLHQ-KSVNLSQ 151
Cdd:cd18048 91 CLCLSPTFELALQTGKVVEEMGKFcvgiqviYAIRGNRPGKGTDIEAQ---------IVIGTPGTVLDWCFKlRLIDVTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082644987 152 VEFLVLDEADRMLDM-GFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIEVARRNAT 218
Cdd:cd18048 162 ISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
3-210 |
5.26e-28 |
|
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: 111.70 E-value: 5.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 3 FESLGLSPDILRAIADA---------GYTEPTPIQAQAIPVVLSG----------------KDVMAGAQTGTGKTASFTL 57
Cdd:cd17965 1 FDQLKLLPSVREAIIKEilkgsnktdEEIKPSPIQTLAIKKLLKTlmrkvtkqtsneepklEVFLLAAETGSGKTLAYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 58 PMLHKL-----AVHQNTSTSPARH----QVRGLILAPTRELAAQVEASVRTYSKYLSLRSTSV---YGGVHIDPQIAeLR 125
Cdd:cd17965 81 PLLDYLkrqeqEPFEEAEEEYESAkdtgRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFssgFGPSYQRLQLA-FK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 126 RGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLDMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMH 205
Cdd:cd17965 160 GRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFP 239
|
....*
gi 1082644987 206 DPQLI 210
Cdd:cd17965 240 DVVRI 244
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
262-342 |
3.22e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 98.44 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 262 RLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGLDIDDLPCVVNFELPHSAEDYVHRVGRTGRA 341
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
|
.
gi 1082644987 342 G 342
Cdd:smart00490 82 G 82
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
2-211 |
1.44e-24 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 100.95 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 2 SFESLGLSPDILRAIADAGYTEPTPIQAQAIPVVLSG--KDVMAGAQTGTGKTASFTLPMLhklavhqnTSTSPARHQVR 79
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAML--------SQVEPANKYPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 80 GLILAPTRELAAQVEASVRTYSKY-------LSLRSTSVYGGVHIDPQiaelrrgveILVATPGRLLDH-LHQKSVNLSQ 151
Cdd:cd18047 74 CLCLSPTYELALQTGKVIEQMGKFypelklaYAVRGNKLERGQKISEQ---------IVIGTPGTVLDWcSKLKFIDPKK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082644987 152 VEFLVLDEADRML-DMGFMPDIRRIFSYLPPRRQNLLFSATFAEEIKRLASDFMHDPQLIE 211
Cdd:cd18047 145 IKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
7-342 |
6.28e-17 |
|
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: 83.35 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 7 GLSPDILRAIADAGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTstsparhqvRGLILAPT 86
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA---------TALYLYPT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 87 RELAAQVEASVRTYSKYLSLR-STSVYGGvhiD-PQIA--ELRRGVEILVATP-----GrLLDHLHQKSVNLSQVEFLVL 157
Cdd:COG1205 111 KALARDQLRRLRELAEALGLGvRVATYDG---DtPPEErrWIREHPDIVLTNPdmlhyG-LLPHHTRWARFFRNLRYVVI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 158 DEA---------------DRMldmgfmpdiRRIFSYLPPRRQNLLFSAT------FAEEI-----------------KRL 199
Cdd:COG1205 187 DEAhtyrgvfgshvanvlRRL---------RRICRHYGSDPQFILASATignpaeHAERLtgrpvtvvdedgsprgeRTF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 200 AsdFMHDPQLIEVARRNATADTvtqvaypvandhkRRLLAQIIKNEdlKQVLIFTNTKTGANRLA---HQLMHEDINAVA 276
Cdd:COG1205 258 V--LWNPPLVDDGIRRSALAEA-------------ARLLADLVREG--LRTLVFTRSRRGAELLAryaRRALREPDLADR 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082644987 277 I---HSDKTQQARMQALAEFKEGKIRALVATDIAARGLDIDDLPCVVNFELPHSAEDYVHRVGRTGRAG 342
Cdd:COG1205 321 VaayRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRG 389
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
41-320 |
1.06e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 79.30 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 41 VMAgaqTGTGKT--ASFtlpMLHKLAVHQNTstsparhqvrgLILAPTRELAAQveasvrTYSKYLSLRSTSVYGGVHID 118
Cdd:COG1061 106 VAP---TGTGKTvlALA---LAAELLRGKRV-----------LVLVPRRELLEQ------WAEELRRFLGDPLAGGGKKD 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 119 pqiaelrRGVEILVATPGRLLDHLHQKSVNlSQVEFLVLDEADRMLDMGFmpdiRRIFSYLPPRRQnLLFSAT------- 191
Cdd:COG1061 163 -------SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAYR-LGLTATpfrsdgr 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 192 -----------FAEEIKRLASD--------FMHDPQLIEVARRNATADTVTQVAYPVANDHKRRLLAQIIKNE-DLKQVL 251
Cdd:COG1061 230 eillflfdgivYEYSLKEAIEDgylappeyYGIRVDLTDERAEYDALSERLREALAADAERKDKILRELLREHpDDRKTL 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082644987 252 IFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIAARGLDIDDLPCVV 320
Cdd:COG1061 310 VFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-368 |
1.35e-15 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 78.78 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 1 MSFESLgLSPDILRAIADAGYTEPTPIQAQAIP-VVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQntstsparhqvR 79
Cdd:COG1204 1 MKVAEL-PLEKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG-----------K 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 80 GLILAPTRELAAQVEASVRTYSKYLSLRSTSVYGGvhIDPQIAELRRgVEILVATPGRLLDHLHQKSVNLSQVEFLVLDE 159
Cdd:COG1204 69 ALYIVPLRALASEKYREFKRDFEELGIKVGVSTGD--YDSDDEWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 160 AdRMLDmgfmpDIRR---------IFSYLPPRRQNLLFSATF--AEEIKRL--ASDFMHD----PQLIEVARRNAT--AD 220
Cdd:COG1204 146 A-HLID-----DESRgptlevllaRLRRLNPEAQIVALSATIgnAEEIAEWldAELVKSDwrpvPLNEGVLYDGVLrfDD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 221 TVTQVAYPVANdhkrrLLAQIIKNEDlkQVLIFTNTKTGANRLAHQLM-----------HEDINAVAI------------ 277
Cdd:COG1204 220 GSRRSKDPTLA-----LALDLLEEGG--QVLVFVSSRRDAESLAKKLAdelkrrltpeeREELEELAEellevseethtn 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 278 --------------HSDKTQQARMQALAEFKEGKIRALVATDIAARGLdidDLP--CVV------NFELPHSAEDYVHRV 335
Cdd:COG1204 293 ekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV---NLParRVIirdtkrGGMVPIPVLEFKQMA 369
|
410 420 430
....*....|....*....|....*....|....*
gi 1082644987 336 GRTGRAGI--SGKAIsLVSPEEKRYLSDIEKLIKR 368
Cdd:COG1204 370 GRAGRPGYdpYGEAI-LVAKSSDEADELFERYILG 403
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
11-374 |
2.06e-15 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 78.26 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 11 DILRAIAdaGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLP--MLHKLAVhqntSTSP--A--RHQVRGLila 84
Cdd:COG0514 7 EVLKRVF--GYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLLPGLTL----VVSPliAlmKDQVDAL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 85 ptreLAAQVEASvrtyskylSLRSTsvyggvhIDPQ-----IAELRRG-VEILVATPGRL-----LDHLHQKSVNLsqve 153
Cdd:COG0514 78 ----RAAGIRAA--------FLNSS-------LSAEerrevLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 154 fLVLDEA--------DrmldmgFMPDIRRIFSYLP--PRRQNLLFSATfA-----EEI-KRLAsdfMHDPQLIE--VARR 215
Cdd:COG0514 135 -FAIDEAhcisqwghD------FRPDYRRLGELRErlPNVPVLALTAT-AtprvrADIaEQLG---LEDPRVFVgsFDRP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 216 NatadtvtqVAY---PVANDHKRRLLAQIIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAE 292
Cdd:COG0514 204 N--------LRLevvPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 293 FKEGKIRALVATdIAArGLDID--DLPCVVNFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYLsdiEKLIKRAI 370
Cdd:COG0514 276 FLRDEVDVIVAT-IAF-GMGIDkpDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQ---RFFIEQSP 350
|
....
gi 1082644987 371 PLEA 374
Cdd:COG0514 351 PDEE 354
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
235-351 |
4.79e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 71.30 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 235 RRLLAQIIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAV------AIHSDK--TQQARMQALAEFKEGKIRALVATDI 306
Cdd:COG1111 341 REILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGEFNVLVATSV 420
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1082644987 307 AARGLDIDDLPCVVNFELPHSAEDYVHRVGRTGRAGiSGKAISLV 351
Cdd:COG1111 421 AEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKR-EGRVVVLI 464
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
25-160 |
1.59e-10 |
|
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: 59.97 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 25 TPIQAQAI-PVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTStsparhqvrgLILAPTRELAAQVEASVRTYSKY 103
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKA----------VYIAPTRALVNQKEADLRERFGP 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 104 LSLRSTSVYGGVHIDPQIAELRRgveILVATPGR---LLDHLHQKsvNLSQVEFLVLDEA 160
Cdd:cd17921 73 LGKNVGLLTGDPSVNKLLLAEAD---ILVATPEKldlLLRNGGER--LIQDVRLVVVDEA 127
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
38-191 |
6.42e-10 |
|
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: 57.41 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 38 GKDVMAGAQTGTGKTASFTLPMLHKLAvhqntstsPARHQVrgLILAPTRELAAQVEASVRTYSKyLSLRSTSVYGGVHI 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLL--------KKGKKV--LVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSA 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082644987 118 DPQIAELRRGVEILVATPGRLL-DHLHQKSVNLSQVEFLVLDEADRMLDMGFMPDI--RRIFSYLPPRRQNLLFSAT 191
Cdd:cd00046 70 EEREKNKLGDADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALIldLAVRKAGLKNAQVILLSAT 146
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
219-350 |
6.66e-10 |
|
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: 57.27 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 219 ADTVTQVAYPVANDHKRRLLAQIiknEDLKQVLIFTNTKTGANRLAHQL------MHEDINAVAIHSDKTQQARMQALAE 292
Cdd:cd18796 13 APEIFPWAGESGADAYAEVIFLL---ERHKSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAA 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082644987 293 FKEGKIRALVATDIAARGLDIDDLPCVVNFELPHSAEDYVHRVGRTGRagiSGKAISL 350
Cdd:cd18796 90 LKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH---RPGAASK 144
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
229-342 |
1.50e-09 |
|
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: 56.49 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 229 VANDHKRRLLAQIIKN-EDLKQVLIFTNTKTGANRLAhqlmhEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATDIA 307
Cdd:cd18789 30 AMNPNKLRALEELLKRhEQGDKIIVFTDNVEALYRYA-----KRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVG 104
|
90 100 110
....*....|....*....|....*....|....*.
gi 1082644987 308 ARGLDIDDLPCVVNFE-LPHSAEDYVHRVGRTGRAG 342
Cdd:cd18789 105 DEGIDLPEANVAIQISgHGGSRRQEAQRLGRILRPK 140
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-160 |
9.30e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 54.90 E-value: 9.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 28 QAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAvhqntstspARHQVRGLILAPTRELAAQVEASVRTYSKYLSLR 107
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL---------RDPGSRALYLYPTKALAQDQLRSLRELLEQLGLG 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082644987 108 ST-SVYGG-VHIDPQIAELRRGVEILVATPGRL---LDHLHQKSVN-LSQVEFLVLDEA 160
Cdd:cd17923 76 IRvATYDGdTPREERRAIIRNPPRILLTNPDMLhyaLLPHHDRWARfLRNLRYVVLDEA 134
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
235-430 |
9.32e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.58 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 235 RRLLAQIIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAI------HSDK--TQQARMQALAEFKEGKIRALVATDI 306
Cdd:PRK13766 353 REIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFvgqaskDGDKgmSQKEQIEILDKFRAGEFNVLVSTSV 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 307 AARGLDIDDLPCVVNFELPHSAEDYVHRVGRTGRAGiSGKAISLVSP-------------EEKRYLSDIEKLIKRAIPLE 373
Cdd:PRK13766 433 AEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGRQE-EGRVVVLIAKgtrdeayywssrrKEKKMKEELKNLKGILNKKL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1082644987 374 ALPGYGAERLAEAPGKDryrERTNERARPVVARSVEPEPSVQYVPEPSVEITEIPEI 430
Cdd:PRK13766 512 QELDEEQKGEEEEKDEQ---LSLDDFVKSKGKEEEEEEEKEEKDKETEEDEPEGPKI 565
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
21-339 |
1.96e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 56.65 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 21 YTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKT-ASFtLPMLHKLAvhQNTSTSPARHQVRGLILAPTRELAAQVEASVRT 99
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELA--RRPRPGELPDGLRVLYISPLKALANDIERNLRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 100 yskylSLRSTSVYGGVHIdPQI---------------AELRRGVEILVATPGRLldHL---HQKSV-NLSQVEFLVLDE- 159
Cdd:COG1201 99 -----PLEEIGEAAGLPL-PEIrvgvrtgdtpaserqRQRRRPPHILITTPESL--ALlltSPDAReLLRGVRTVIVDEi 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 160 -AdrmldmgFMPDIR---------RIFSYLP--PRRQNLlfSATFA--EEIKR--LASDFMHDPQLIEV-ARRNATADTV 222
Cdd:COG1201 171 hA-------LAGSKRgvhlalsleRLRALAPrpLQRIGL--SATVGplEEVARflVGYEDPRPVTIVDAgAGKKPDLEVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 223 TQV-----AYPVANDHKRRLLAQIIkneDL----KQVLIFTNTKTGANRLAHQLMH---EDINAVAIH--S-DKTQqaRM 287
Cdd:COG1201 242 VPVedlieRFPWAGHLWPHLYPRVL---DLieahRTTLVFTNTRSQAERLFQRLNElnpEDALPIAAHhgSlSREQ--RL 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1082644987 288 QALAEFKEGKIRALVAT---DIaarGLDIDDLPCVVNFELPHSAEDYVHRVGRTG 339
Cdd:COG1201 317 EVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
47-160 |
4.95e-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: 53.04 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 47 TGTGKTasFTLPMLHKLAVHQNTSTSPARHQVrgLILAPTRELAAQVEASVRTYSKylsLRSTSVYGGVHIDPQIA---- 122
Cdd:cd18034 25 TGSGKT--LIAVMLIKEMGELNRKEKNPKKRA--VFLVPTVPLVAQQAEAIRSHTD---LKVGEYSGEMGVDKWTKerwk 97
|
90 100 110
....*....|....*....|....*....|....*....
gi 1082644987 123 -ELRRgVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEA 160
Cdd:cd18034 98 eELEK-YDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
235-336 |
6.73e-08 |
|
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: 51.32 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 235 RRLLAQIIKNEDlkQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGK--IRALVATDIAARGLD 312
Cdd:cd18793 17 LELLEELREPGE--KVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLN 94
|
90 100 110
....*....|....*....|....*....|
gi 1082644987 313 IDDLPCVVNFELPHS------AEDYVHRVG 336
Cdd:cd18793 95 LTAANRVILYDPWWNpaveeqAIDRAHRIG 124
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
236-344 |
1.08e-07 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 50.67 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 236 RLLAQIIKNEDLKQVLIFTNTKTGANrlahqlmHEDINAVAIHSDKTQQarmQALAEFKEGKIRALVATDIAARGLDIDD 315
Cdd:cd18802 39 VVLSRLLKEHPSTLAFIRCGFLIGRG-------NSSQRKRSLMTQRKQK---ETLDKFRDGELNLLIATSVLEEGIDVPA 108
|
90 100
....*....|....*....|....*....
gi 1082644987 316 LPCVVNFELPHSAEDYVHRVGRtGRAGIS 344
Cdd:cd18802 109 CNLVIRFDLPKTLRSYIQSRGR-ARAPNS 136
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
230-342 |
1.71e-07 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 49.90 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 230 ANDHKRRLLAQIIKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGKIRALVATdiAAR 309
Cdd:cd18794 13 KKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT--VAF 90
|
90 100 110
....*....|....*....|....*....|....*
gi 1082644987 310 GLDID--DLPCVVNFELPHSAEDYVHRVGRTGRAG 342
Cdd:cd18794 91 GMGIDkpDVRFVIHYSLPKSMESYYQESGRAGRDG 125
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
232-350 |
5.62e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 48.89 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 232 DHKRRLLAQIIKNEDLKQ---VLIFTNTKTGANRLAHQLMHEDINAVAI----HSDK------TQQARMQALAEFKEGKI 298
Cdd:cd18801 12 EKLEEIVKEHFKKKQEGSdtrVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGksskgmSQKEQKEVIEQFRKGGY 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1082644987 299 RALVATDIAARGLDIDDLPCVVNFELPHSAEDYVHRVGRTGRaGISGKAISL 350
Cdd:cd18801 92 NVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVL 142
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
20-359 |
1.68e-06 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 50.48 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 20 GYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHK--LAVHQNTSTSPARHQVRGLilaptreLAAQVEASV 97
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLdgLTLVVSPLISLMKDQVDQL-------LANGVAAAC 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 98 rtyskylsLRST-------SVYGGVhidpqiaelRRG-VEILVATPGRL-----LDHLHQksVNLSqveFLVLDEADRML 164
Cdd:PRK11057 95 --------LNSTqtreqqlEVMAGC---------RTGqIKLLYIAPERLmmdnfLEHLAH--WNPA---LLAVDEAHCIS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 165 DMG--FMPD------IRRIFSYLPPrrqnLLFSATFAE----EIKRLASdfMHDP--QLIEVARRNatadtvtqVAYPVA 230
Cdd:PRK11057 153 QWGhdFRPEyaalgqLRQRFPTLPF----MALTATADDttrqDIVRLLG--LNDPliQISSFDRPN--------IRYTLV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 231 NDHKRrlLAQI---IKNEDLKQVLIFTNTKTGANRLAHQLMHEDINAVAIHS--DKTQQARMQAlaEFKEGKIRALVATD 305
Cdd:PRK11057 219 EKFKP--LDQLmryVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAglDNDVRADVQE--AFQRDDLQIVVATV 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1082644987 306 IAARGLDIDDLPCVVNFELPHSAEDYVHRVGRTGRAGISGKAISLVSPEEKRYL 359
Cdd:PRK11057 295 AFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWL 348
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
300-342 |
1.19e-05 |
|
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: 43.08 E-value: 1.19e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1082644987 300 ALVATDIAARGLDIDDLPCVVNFELPHSAEDYVHRVGRTGRAG 342
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
27-162 |
2.07e-05 |
|
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: 45.20 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 27 IQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLAvhqntstspaRHQVRGLILAPTRELAAQVEASVRTYSKyLSL 106
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLT----------KKGGKVLILAPSRPLVEQHAENLKRVLN-IPD 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082644987 107 RSTSVYGGVHIDPQiAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADR 162
Cdd:cd18035 74 KITSLTGEVKPEER-AERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
291-342 |
2.75e-05 |
|
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: 44.17 E-value: 2.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1082644987 291 AEFKEGKIRALVATDIAARGLDIDDLPCVVNFELPHSAEDYVHRVGRTGRAG 342
Cdd:cd18797 86 AELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRG 137
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
241-348 |
6.01e-05 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 43.31 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 241 IIKNEDLKQVLIFTNTKTGANRLAhqlmhEDINAVAIH------SDKTqqarmqaLAE--FKEGKIRALVATDIAARGLd 312
Cdd:cd18795 37 IETVSEGKPVLVFCSSRKECEKTA-----KDLAGIAFHhagltrEDRE-------LVEelFREGLIKVLVATSTLAAGV- 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1082644987 313 idDLPC--VV---------NFELPHSAEDYVHRVGRTGRAGI--SGKAI 348
Cdd:cd18795 104 --NLPArtVIikgtqrydgKGYRELSPLEYLQMIGRAGRPGFdtRGEAI 150
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
21-339 |
9.40e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 44.88 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 21 YTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKT-ASFT--LPMLHKLAVHQNTS-------TSPAR------HqvRGLI-- 82
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLaiIDELFRLGREGELEdkvyclyVSPLRalnndiH--RNLEep 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 83 LAPTRELAAQ-------VEASVRT-----YSKYLSLRSTSvyggvHI-------------DPQIAELRRGVEILVatpgr 137
Cdd:PRK13767 108 LTEIREIAKErgeelpeIRVAIRTgdtssYEKQKMLKKPP-----HIlittpeslaillnSPKFREKLRTVKWVI----- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 138 lLDHLH-----QKSVNLSqvefLVLDEADRMLDMGFmpdiRRI------------------FSYLPPRRQNLLFSATFAE 194
Cdd:PRK13767 178 -VDEIHslaenKRGVHLS----LSLERLEELAGGEF----VRIglsatiepleevakflvgYEDDGEPRDCEIVDARFVK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 195 EIK-RLAS---DFMHdpqlievarrnATADTVTQVAYpvandhkrRLLAQIIKneDLKQVLIFTNTKTGANRLAHQL--- 267
Cdd:PRK13767 249 PFDiKVISpvdDLIH-----------TPAEEISEALY--------ETLHELIK--EHRTTLIFTNTRSGAERVLYNLrkr 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082644987 268 MHEDINAVAI---HSDKTQQARMQALAEFKEGKIRALVATDIAARGLDIDDLPCVVNFELPHSAEDYVHRVGRTG 339
Cdd:PRK13767 308 FPEEYDEDNIgahHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
27-159 |
9.96e-05 |
|
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: 43.50 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 27 IQAQAIPVVL-SGKDVMAGAQTGTGKTASFTLPMLHKLAvhqnTSTSPARHQVRGLILAPTRELAAQVEASVRTYSKYLS 105
Cdd:cd18023 5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLK----ERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082644987 106 LRSTSVYGgvhiDPQIAELR--RGVEILVATPGR--LLDHLHQKSVNLSQ-VEFLVLDE 159
Cdd:cd18023 81 LSCAELTG----DTEMDDTFeiQDADIILTTPEKwdSMTRRWRDNGNLVQlVALVLIDE 135
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
41-192 |
1.61e-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: 41.91 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 41 VMAgaqTGTGKTAsftlpMLHKLAVHqntstspaRHQVRGLILAPTRELAAQveasvrTYSKYLSLRSTSVYGGVHIDPQ 120
Cdd:cd17926 24 VLP---TGSGKTL-----TALALIAY--------LKELRTLIVVPTDALLDQ------WKERFEDFLGDSSIGLIGGGKK 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082644987 121 IAELRRgvEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLDMGFmpdiRRIFSYLPPRRQnLLFSATF 192
Cdd:cd17926 82 KDFDDA--NVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTF----SEILKELNAKYR-LGLTATP 146
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
21-314 |
1.63e-04 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 43.92 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 21 YTEPTPIQAQAIPVVLSGKDVMAG-----AQTGTGKT-ASFTLpmLHKLAvhqntstspARHQVRGLILA-PTRELAAQv 93
Cdd:COG1203 125 RTPINPLQNEALELALEAAEEEPGlfiltAPTGGGKTeAALLF--ALRLA---------AKHGGRRIIYAlPFTSIINQ- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 94 easvrTYSKYLSLRSTSVyGGVH--IDPQIAELRRGVE----------------ILVATPGRLLDHL-----HQ------ 144
Cdd:COG1203 193 -----TYDRLRDLFGEDV-LLHHslADLDLLEEEEEYEsearwlkllkelwdapVVVTTIDQLFESLfsnrkGQerrlhn 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 145 --KSVnlsqvefLVLDEADrMLDMGFMPDIRRIFSYLppRRQN---LLFSATFAEEIKRLASDfmhdpqlievARRNATA 219
Cdd:COG1203 267 laNSV-------IILDEVQ-AYPPYMLALLLRLLEWL--KNLGgsvILMTATLPPLLREELLE----------AYELIPD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 220 DTVTQVAYPVANDHKR-RLLAQIIKNEDL-----------KQVLIFTNTKTGANRLAHQL--MHEDINAVAIHSDKTQQA 285
Cdd:COG1203 327 EPEELPEYFRAFVRKRvELKEGPLSDEELaelilealhkgKSVLVIVNTVKDAQELYEALkeKLPDEEVYLLHSRFCPAD 406
|
330 340 350
....*....|....*....|....*....|...
gi 1082644987 286 RMQALAE----FKEGKIRALVATDIAARGLDID 314
Cdd:COG1203 407 RSEIEKEikerLERGKPCILVSTQVVEAGVDID 439
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
27-159 |
2.07e-04 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350778 [Multi-domain] Cd Length: 199 Bit Score: 42.42 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 27 IQAQAIPVV-LSGKDVMAGAQTGTGKTASFTLPMLHKLAVHQNTSTSPARHQVRGLILAPTRELAAQVEASVRTYSKYLS 105
Cdd:cd18020 5 IQSLVFPVAyKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQGGVIKKDDFKIVYIAPMKALAAEMVEKFSKRLAPLG 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 106 LRSTSVYGgvhiDPQI--AELRRgVEILVATPGRlLDHLHQKSVN----LSQVEFLVLDE 159
Cdd:cd18020 85 IKVKELTG----DMQLtkKEIAE-TQIIVTTPEK-WDVVTRKSSGdvalSQLVRLLIIDE 138
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
23-199 |
6.97e-04 |
|
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: 40.33 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 23 EPTPIQAQAIPVVLSGKDVMAGAQTGTGKT--ASFTLPMLHKlavhqntstsparHQVRGLILAPTRELAAQveasvrty 100
Cdd:cd18027 8 ELDVFQKQAILHLEAGDSVFVAAHTSAGKTvvAEYAIALAQK-------------HMTRTIYTSPIKALSNQ-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 101 sKYLSLRSTsvYGGVHIDPQIAELRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVLDEADRMLDMGFMPDIRRIFSYLP 180
Cdd:cd18027 67 -KFRDFKNT--FGDVGLITGDVQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLP 143
|
170 180
....*....|....*....|....*
gi 1082644987 181 PRRQNLLFSAT------FAEEIKRL 199
Cdd:cd18027 144 DHVSIILLSATvpntveFADWIGRI 168
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
11-160 |
9.20e-04 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 40.21 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 11 DILRAIAdaGYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLP--MLHKLAVhqntSTSP----ARHQVRGLILA 84
Cdd:cd17920 2 QILKEVF--GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGVTL----VVSPlislMQDQVDRLQQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 85 PTRelAAQVEASVRTYSKYLSLRstsvyggvhidpqiaELRRG-VEILVATPGRLLDHLHQKSVN----LSQVEFLVLDE 159
Cdd:cd17920 76 GIR--AAALNSTLSPEEKREVLL---------------RIKNGqYKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDE 138
|
.
gi 1082644987 160 A 160
Cdd:cd17920 139 A 139
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
251-337 |
9.82e-04 |
|
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: 38.69 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 251 LIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQAR-MQALAEFKEGKI--RALVATDIAARGLDIDDLPCVVNFELPHS 327
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELkpPILVTVDLLTTGVDIPEVDNVVFLRPTES 89
|
90
....*....|
gi 1082644987 328 AEDYVHRVGR 337
Cdd:cd18799 90 RTLFLQMLGR 99
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
23-162 |
1.28e-03 |
|
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: 40.11 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 23 EPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKLavhqntSTSPARHQVRGLILAPTRELAAQVEASVRTYSK 102
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHL------KKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFE 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082644987 103 YLSLRSTSVYGGVHIDPQIAELRRGVEILVATPGRLL-DHLHQKSVNLSQVEFLVLDEADR 162
Cdd:cd17927 76 RPGYKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
20-191 |
1.75e-03 |
|
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: 39.55 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 20 GYTEPTPIQAQAIPVVLSGKDVMAGAQTGTGKTASFTLPMLHKlavhqntstspaRHQVRGLIL--APTRELAA-QVEAS 96
Cdd:cd18018 9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLL------------RRRGPGLTLvvSPLIALMKdQVDAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 97 VRTySKYLSLRSTSVYGGVHIDpqIAELRRG-VEILVATPGRLLDH-----LHQksvnLSQVEFLVLDEADRMLDMG--F 168
Cdd:cd18018 77 PRA-IKAAALNSSLTREERRRI--LEKLRAGeVKILYVSPERLVNEsfrelLRQ----TPPISLLVVDEAHCISEWShnF 149
|
170 180
....*....|....*....|....*.
gi 1082644987 169 MPDIRRIFSYLPPRRQN---LLFSAT 191
Cdd:cd18018 150 RPDYLRLCRVLRELLGAppvLALTAT 175
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
41-192 |
2.48e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.42 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 41 VMAgaqTGTGKT--ASFTLPMLHKLAVHQNTstsparhqvrgLILAPTRELAAQveaSVRTYSKYLS--LRSTSVYGGVH 116
Cdd:pfam04851 29 VMA---TGSGKTltAAKLIARLFKKGPIKKV-----------LFLVPRKDLLEQ---ALEEFKKFLPnyVEIGEIISGDK 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082644987 117 IDPQiaelRRGVEILVATPGRLLDHLHQKSVNLSQVEFLVL--DEADRMLDMGFmpdiRRIFSYLPPRRQnLLFSATF 192
Cdd:pfam04851 92 KDES----VDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHRSGASSY----RNILEYFKPAFL-LGLTATP 160
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
41-198 |
3.85e-03 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 37.93 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 41 VMAgaqTGTGKT--ASFTLPMLHKLAVHQntstsparhqvRGLILAPTRELAAQVEasvRTYSKYLSLRSTSVYGGVHID 118
Cdd:cd18032 26 VMA---TGTGKTytAAFLIKRLLEANRKK-----------RILFLAHREELLEQAE---RSFKEVLPDGSFGNLKGGKKK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 119 PQIAelrrgvEILVATPGRL--LDHLHQKSVNlsQVEFLVLDEADRmldmGFMPDIRRIFSYLPPRRQnLLFSATFAEEI 196
Cdd:cd18032 89 PDDA------RVVFATVQTLnkRKRLEKFPPD--YFDLIIIDEAHH----AIASSYRKILEYFEPAFL-LGLTATPERTD 155
|
..
gi 1082644987 197 KR 198
Cdd:cd18032 156 GL 157
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
230-338 |
9.99e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 38.28 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082644987 230 ANDHKRRLLAQIIKN---EDLKqVLIFTNTKTGANRLAHQLMHEDINAVAIHSDKTQQARMQALAEFKEGK--IRALVAT 304
Cdd:COG0553 530 GRSAKLEALLELLEEllaEGEK-VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISL 608
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1082644987 305 DIAARGLDI---DDlpcVVNFELPHS------AEDYVHRVGRT 338
Cdd:COG0553 609 KAGGEGLNLtaaDH---VIHYDLWWNpaveeqAIDRAHRIGQT 648
|
|
| |
